data_9GBR
# 
_entry.id   9GBR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9GBR         pdb_00009gbr 10.2210/pdb9gbr/pdb 
WWPDB D_1292140642 ?            ?                   
# 
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 2025-03-19 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
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.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GBR 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-31 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              bsskra@bath.ac.uk 
_pdbx_contact_author.name_first         'K. Ravi' 
_pdbx_contact_author.name_last          Acharya 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3009-4058 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Gregory, K.S.' 1 ? 
'Cozier, G.E.'  2 ? 
'Acharya, K.R.' 3 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Febs J.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1742-464X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            292 
_citation.language                  ? 
_citation.page_first                1141 
_citation.page_last                 1158 
_citation.title                     
'Molecular basis of human angiotensin-1 converting enzyme inhibition by a series of diprolyl-derived compounds.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1111/febs.17384 
_citation.pdbx_database_id_PubMed   39763019 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gregory, K.S.'  1 ? 
primary 'Cozier, G.E.'   2 ? 
primary 'Fienberg, S.'   3 ? 
primary 'Chibale, K.'    4 ? 
primary 'Sturrock, E.D.' 5 ? 
primary 'Acharya, K.R.'  6 ? 
# 
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 'Angiotensin-converting enzyme, soluble form' 72493.352 2   ? ? ? ? 
2  branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   1   ? ? ? ? 
3  branched    syn 'alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose' 367.349   1   ? ? ? ? 
4  branched    syn 
;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose
;
732.682   1   ? ? ? ? 
5  non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   2   ? ? ? ? 
6  non-polymer syn 'ZINC ION' 65.409    2   ? ? ? ? 
7  non-polymer syn 'CHLORIDE ION' 35.453    2   ? ? ? ? 
8  non-polymer syn 
;(2S)-1-[(2S)-2-[[(1S)-1-[(2S)-1-[(2S)-2-azanyl-5-oxidanyl-5-oxidanylidene-pentanoyl]pyrrolidin-2-yl]-2-oxidanyl-2-oxidanylidene-ethyl]amino]propanoyl]pyrrolidine-2-carboxylic acid
;
442.464   2   ? ? ? ? 
9  non-polymer syn 'TRIETHYLENE GLYCOL' 150.173   1   ? ? ? ? 
10 non-polymer syn 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL 326.383   1   ? ? ? ? 
11 non-polymer syn 'TETRAETHYLENE GLYCOL' 194.226   1   ? ? ? ? 
12 water       nat water 18.015    591 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;LDPGLQPGQFSADEAGAQLFAQSYQSSAEQVLFQSVAASWAHDTNITAENARRQEEAALLSQEFAEAWGQKAKELYEPIW
QQFTDPQLRRIIGAVRTLGSANLPLAKRQQYNALLSQMSRIYSTAKVCLPQKTATCWSLDPDLTNILASSRSYAMLLFAW
EGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDR
YINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWQATHMFRVAEEFFTSLELSPMPPEFWEGSMLE
KPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVHHEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVS
TPEHLHKIGLLDRVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDWWYLRTKYQGICPPVTRN
ETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLRAGSSRPWQEVLKDMV
GLDALDAQPLLKYFQLVTQWLQEQNQQNGEVLGWPEYQWHPPLPDNYPEGIDLVTDEAEASKFVEEYD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;LDPGLQPGQFSADEAGAQLFAQSYQSSAEQVLFQSVAASWAHDTNITAENARRQEEAALLSQEFAEAWGQKAKELYEPIW
QQFTDPQLRRIIGAVRTLGSANLPLAKRQQYNALLSQMSRIYSTAKVCLPQKTATCWSLDPDLTNILASSRSYAMLLFAW
EGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDR
YINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWQATHMFRVAEEFFTSLELSPMPPEFWEGSMLE
KPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVHHEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVS
TPEHLHKIGLLDRVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDWWYLRTKYQGICPPVTRN
ETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLRAGSSRPWQEVLKDMV
GLDALDAQPLLKYFQLVTQWLQEQNQQNGEVLGWPEYQWHPPLPDNYPEGIDLVTDEAEASKFVEEYD
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
5  2-acetamido-2-deoxy-beta-D-glucopyranose NAG   
6  'ZINC ION' ZN    
7  'CHLORIDE ION' CL    
8  
;(2S)-1-[(2S)-2-[[(1S)-1-[(2S)-1-[(2S)-2-azanyl-5-oxidanyl-5-oxidanylidene-pentanoyl]pyrrolidin-2-yl]-2-oxidanyl-2-oxidanylidene-ethyl]amino]propanoyl]pyrrolidine-2-carboxylic acid
;
A1IJX 
9  'TRIETHYLENE GLYCOL' PGE   
10 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL P33   
11 'TETRAETHYLENE GLYCOL' PG4   
12 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   LEU n 
1 2   ASP n 
1 3   PRO n 
1 4   GLY n 
1 5   LEU n 
1 6   GLN n 
1 7   PRO n 
1 8   GLY n 
1 9   GLN n 
1 10  PHE n 
1 11  SER n 
1 12  ALA n 
1 13  ASP n 
1 14  GLU n 
1 15  ALA n 
1 16  GLY n 
1 17  ALA n 
1 18  GLN n 
1 19  LEU n 
1 20  PHE n 
1 21  ALA n 
1 22  GLN n 
1 23  SER n 
1 24  TYR n 
1 25  GLN n 
1 26  SER n 
1 27  SER n 
1 28  ALA n 
1 29  GLU n 
1 30  GLN n 
1 31  VAL n 
1 32  LEU n 
1 33  PHE n 
1 34  GLN n 
1 35  SER n 
1 36  VAL n 
1 37  ALA n 
1 38  ALA n 
1 39  SER n 
1 40  TRP n 
1 41  ALA n 
1 42  HIS n 
1 43  ASP n 
1 44  THR n 
1 45  ASN n 
1 46  ILE n 
1 47  THR n 
1 48  ALA n 
1 49  GLU n 
1 50  ASN n 
1 51  ALA n 
1 52  ARG n 
1 53  ARG n 
1 54  GLN n 
1 55  GLU n 
1 56  GLU n 
1 57  ALA n 
1 58  ALA n 
1 59  LEU n 
1 60  LEU n 
1 61  SER n 
1 62  GLN n 
1 63  GLU n 
1 64  PHE n 
1 65  ALA n 
1 66  GLU n 
1 67  ALA n 
1 68  TRP n 
1 69  GLY n 
1 70  GLN n 
1 71  LYS n 
1 72  ALA n 
1 73  LYS n 
1 74  GLU n 
1 75  LEU n 
1 76  TYR n 
1 77  GLU n 
1 78  PRO n 
1 79  ILE n 
1 80  TRP n 
1 81  GLN n 
1 82  GLN n 
1 83  PHE n 
1 84  THR n 
1 85  ASP n 
1 86  PRO n 
1 87  GLN n 
1 88  LEU n 
1 89  ARG n 
1 90  ARG n 
1 91  ILE n 
1 92  ILE n 
1 93  GLY n 
1 94  ALA n 
1 95  VAL n 
1 96  ARG n 
1 97  THR n 
1 98  LEU n 
1 99  GLY n 
1 100 SER n 
1 101 ALA n 
1 102 ASN n 
1 103 LEU n 
1 104 PRO n 
1 105 LEU n 
1 106 ALA n 
1 107 LYS n 
1 108 ARG n 
1 109 GLN n 
1 110 GLN n 
1 111 TYR n 
1 112 ASN n 
1 113 ALA n 
1 114 LEU n 
1 115 LEU n 
1 116 SER n 
1 117 GLN n 
1 118 MET n 
1 119 SER n 
1 120 ARG n 
1 121 ILE n 
1 122 TYR n 
1 123 SER n 
1 124 THR n 
1 125 ALA n 
1 126 LYS n 
1 127 VAL n 
1 128 CYS n 
1 129 LEU n 
1 130 PRO n 
1 131 GLN n 
1 132 LYS n 
1 133 THR n 
1 134 ALA n 
1 135 THR n 
1 136 CYS n 
1 137 TRP n 
1 138 SER n 
1 139 LEU n 
1 140 ASP n 
1 141 PRO n 
1 142 ASP n 
1 143 LEU n 
1 144 THR n 
1 145 ASN n 
1 146 ILE n 
1 147 LEU n 
1 148 ALA n 
1 149 SER n 
1 150 SER n 
1 151 ARG n 
1 152 SER n 
1 153 TYR n 
1 154 ALA n 
1 155 MET n 
1 156 LEU n 
1 157 LEU n 
1 158 PHE n 
1 159 ALA n 
1 160 TRP n 
1 161 GLU n 
1 162 GLY n 
1 163 TRP n 
1 164 HIS n 
1 165 ASN n 
1 166 ALA n 
1 167 ALA n 
1 168 GLY n 
1 169 ILE n 
1 170 PRO n 
1 171 LEU n 
1 172 LYS n 
1 173 PRO n 
1 174 LEU n 
1 175 TYR n 
1 176 GLU n 
1 177 ASP n 
1 178 PHE n 
1 179 THR n 
1 180 ALA n 
1 181 LEU n 
1 182 SER n 
1 183 ASN n 
1 184 GLU n 
1 185 ALA n 
1 186 TYR n 
1 187 LYS n 
1 188 GLN n 
1 189 ASP n 
1 190 GLY n 
1 191 PHE n 
1 192 THR n 
1 193 ASP n 
1 194 THR n 
1 195 GLY n 
1 196 ALA n 
1 197 TYR n 
1 198 TRP n 
1 199 ARG n 
1 200 SER n 
1 201 TRP n 
1 202 TYR n 
1 203 ASN n 
1 204 SER n 
1 205 PRO n 
1 206 THR n 
1 207 PHE n 
1 208 GLU n 
1 209 ASP n 
1 210 ASP n 
1 211 LEU n 
1 212 GLU n 
1 213 HIS n 
1 214 LEU n 
1 215 TYR n 
1 216 GLN n 
1 217 GLN n 
1 218 LEU n 
1 219 GLU n 
1 220 PRO n 
1 221 LEU n 
1 222 TYR n 
1 223 LEU n 
1 224 ASN n 
1 225 LEU n 
1 226 HIS n 
1 227 ALA n 
1 228 PHE n 
1 229 VAL n 
1 230 ARG n 
1 231 ARG n 
1 232 ALA n 
1 233 LEU n 
1 234 HIS n 
1 235 ARG n 
1 236 ARG n 
1 237 TYR n 
1 238 GLY n 
1 239 ASP n 
1 240 ARG n 
1 241 TYR n 
1 242 ILE n 
1 243 ASN n 
1 244 LEU n 
1 245 ARG n 
1 246 GLY n 
1 247 PRO n 
1 248 ILE n 
1 249 PRO n 
1 250 ALA n 
1 251 HIS n 
1 252 LEU n 
1 253 LEU n 
1 254 GLY n 
1 255 ASP n 
1 256 MET n 
1 257 TRP n 
1 258 ALA n 
1 259 GLN n 
1 260 SER n 
1 261 TRP n 
1 262 GLU n 
1 263 ASN n 
1 264 ILE n 
1 265 TYR n 
1 266 ASP n 
1 267 MET n 
1 268 VAL n 
1 269 VAL n 
1 270 PRO n 
1 271 PHE n 
1 272 PRO n 
1 273 ASP n 
1 274 LYS n 
1 275 PRO n 
1 276 ASN n 
1 277 LEU n 
1 278 ASP n 
1 279 VAL n 
1 280 THR n 
1 281 SER n 
1 282 THR n 
1 283 MET n 
1 284 LEU n 
1 285 GLN n 
1 286 GLN n 
1 287 GLY n 
1 288 TRP n 
1 289 GLN n 
1 290 ALA n 
1 291 THR n 
1 292 HIS n 
1 293 MET n 
1 294 PHE n 
1 295 ARG n 
1 296 VAL n 
1 297 ALA n 
1 298 GLU n 
1 299 GLU n 
1 300 PHE n 
1 301 PHE n 
1 302 THR n 
1 303 SER n 
1 304 LEU n 
1 305 GLU n 
1 306 LEU n 
1 307 SER n 
1 308 PRO n 
1 309 MET n 
1 310 PRO n 
1 311 PRO n 
1 312 GLU n 
1 313 PHE n 
1 314 TRP n 
1 315 GLU n 
1 316 GLY n 
1 317 SER n 
1 318 MET n 
1 319 LEU n 
1 320 GLU n 
1 321 LYS n 
1 322 PRO n 
1 323 ALA n 
1 324 ASP n 
1 325 GLY n 
1 326 ARG n 
1 327 GLU n 
1 328 VAL n 
1 329 VAL n 
1 330 CYS n 
1 331 HIS n 
1 332 ALA n 
1 333 SER n 
1 334 ALA n 
1 335 TRP n 
1 336 ASP n 
1 337 PHE n 
1 338 TYR n 
1 339 ASN n 
1 340 ARG n 
1 341 LYS n 
1 342 ASP n 
1 343 PHE n 
1 344 ARG n 
1 345 ILE n 
1 346 LYS n 
1 347 GLN n 
1 348 CYS n 
1 349 THR n 
1 350 ARG n 
1 351 VAL n 
1 352 THR n 
1 353 MET n 
1 354 ASP n 
1 355 GLN n 
1 356 LEU n 
1 357 SER n 
1 358 THR n 
1 359 VAL n 
1 360 HIS n 
1 361 HIS n 
1 362 GLU n 
1 363 MET n 
1 364 GLY n 
1 365 HIS n 
1 366 ILE n 
1 367 GLN n 
1 368 TYR n 
1 369 TYR n 
1 370 LEU n 
1 371 GLN n 
1 372 TYR n 
1 373 LYS n 
1 374 ASP n 
1 375 LEU n 
1 376 PRO n 
1 377 VAL n 
1 378 SER n 
1 379 LEU n 
1 380 ARG n 
1 381 ARG n 
1 382 GLY n 
1 383 ALA n 
1 384 ASN n 
1 385 PRO n 
1 386 GLY n 
1 387 PHE n 
1 388 HIS n 
1 389 GLU n 
1 390 ALA n 
1 391 ILE n 
1 392 GLY n 
1 393 ASP n 
1 394 VAL n 
1 395 LEU n 
1 396 ALA n 
1 397 LEU n 
1 398 SER n 
1 399 VAL n 
1 400 SER n 
1 401 THR n 
1 402 PRO n 
1 403 GLU n 
1 404 HIS n 
1 405 LEU n 
1 406 HIS n 
1 407 LYS n 
1 408 ILE n 
1 409 GLY n 
1 410 LEU n 
1 411 LEU n 
1 412 ASP n 
1 413 ARG n 
1 414 VAL n 
1 415 THR n 
1 416 ASN n 
1 417 ASP n 
1 418 THR n 
1 419 GLU n 
1 420 SER n 
1 421 ASP n 
1 422 ILE n 
1 423 ASN n 
1 424 TYR n 
1 425 LEU n 
1 426 LEU n 
1 427 LYS n 
1 428 MET n 
1 429 ALA n 
1 430 LEU n 
1 431 GLU n 
1 432 LYS n 
1 433 ILE n 
1 434 ALA n 
1 435 PHE n 
1 436 LEU n 
1 437 PRO n 
1 438 PHE n 
1 439 GLY n 
1 440 TYR n 
1 441 LEU n 
1 442 VAL n 
1 443 ASP n 
1 444 GLN n 
1 445 TRP n 
1 446 ARG n 
1 447 TRP n 
1 448 GLY n 
1 449 VAL n 
1 450 PHE n 
1 451 SER n 
1 452 GLY n 
1 453 ARG n 
1 454 THR n 
1 455 PRO n 
1 456 PRO n 
1 457 SER n 
1 458 ARG n 
1 459 TYR n 
1 460 ASN n 
1 461 PHE n 
1 462 ASP n 
1 463 TRP n 
1 464 TRP n 
1 465 TYR n 
1 466 LEU n 
1 467 ARG n 
1 468 THR n 
1 469 LYS n 
1 470 TYR n 
1 471 GLN n 
1 472 GLY n 
1 473 ILE n 
1 474 CYS n 
1 475 PRO n 
1 476 PRO n 
1 477 VAL n 
1 478 THR n 
1 479 ARG n 
1 480 ASN n 
1 481 GLU n 
1 482 THR n 
1 483 HIS n 
1 484 PHE n 
1 485 ASP n 
1 486 ALA n 
1 487 GLY n 
1 488 ALA n 
1 489 LYS n 
1 490 PHE n 
1 491 HIS n 
1 492 VAL n 
1 493 PRO n 
1 494 ASN n 
1 495 VAL n 
1 496 THR n 
1 497 PRO n 
1 498 TYR n 
1 499 ILE n 
1 500 ARG n 
1 501 TYR n 
1 502 PHE n 
1 503 VAL n 
1 504 SER n 
1 505 PHE n 
1 506 VAL n 
1 507 LEU n 
1 508 GLN n 
1 509 PHE n 
1 510 GLN n 
1 511 PHE n 
1 512 HIS n 
1 513 GLU n 
1 514 ALA n 
1 515 LEU n 
1 516 CYS n 
1 517 LYS n 
1 518 GLU n 
1 519 ALA n 
1 520 GLY n 
1 521 TYR n 
1 522 GLU n 
1 523 GLY n 
1 524 PRO n 
1 525 LEU n 
1 526 HIS n 
1 527 GLN n 
1 528 CYS n 
1 529 ASP n 
1 530 ILE n 
1 531 TYR n 
1 532 ARG n 
1 533 SER n 
1 534 THR n 
1 535 LYS n 
1 536 ALA n 
1 537 GLY n 
1 538 ALA n 
1 539 LYS n 
1 540 LEU n 
1 541 ARG n 
1 542 LYS n 
1 543 VAL n 
1 544 LEU n 
1 545 ARG n 
1 546 ALA n 
1 547 GLY n 
1 548 SER n 
1 549 SER n 
1 550 ARG n 
1 551 PRO n 
1 552 TRP n 
1 553 GLN n 
1 554 GLU n 
1 555 VAL n 
1 556 LEU n 
1 557 LYS n 
1 558 ASP n 
1 559 MET n 
1 560 VAL n 
1 561 GLY n 
1 562 LEU n 
1 563 ASP n 
1 564 ALA n 
1 565 LEU n 
1 566 ASP n 
1 567 ALA n 
1 568 GLN n 
1 569 PRO n 
1 570 LEU n 
1 571 LEU n 
1 572 LYS n 
1 573 TYR n 
1 574 PHE n 
1 575 GLN n 
1 576 LEU n 
1 577 VAL n 
1 578 THR n 
1 579 GLN n 
1 580 TRP n 
1 581 LEU n 
1 582 GLN n 
1 583 GLU n 
1 584 GLN n 
1 585 ASN n 
1 586 GLN n 
1 587 GLN n 
1 588 ASN n 
1 589 GLY n 
1 590 GLU n 
1 591 VAL n 
1 592 LEU n 
1 593 GLY n 
1 594 TRP n 
1 595 PRO n 
1 596 GLU n 
1 597 TYR n 
1 598 GLN n 
1 599 TRP n 
1 600 HIS n 
1 601 PRO n 
1 602 PRO n 
1 603 LEU n 
1 604 PRO n 
1 605 ASP n 
1 606 ASN n 
1 607 TYR n 
1 608 PRO n 
1 609 GLU n 
1 610 GLY n 
1 611 ILE n 
1 612 ASP n 
1 613 LEU n 
1 614 VAL n 
1 615 THR n 
1 616 ASP n 
1 617 GLU n 
1 618 ALA n 
1 619 GLU n 
1 620 ALA n 
1 621 SER n 
1 622 LYS n 
1 623 PHE n 
1 624 VAL n 
1 625 GLU n 
1 626 GLU n 
1 627 TYR n 
1 628 ASP n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   628 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'ACE, DCP, DCP1' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Cricetulus griseus' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     10029 
_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                   ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
2 oligosaccharide 
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 2 DGlcpNAcb1-4DGlcpNAcb1-ROH                                                                          
'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1'                                               WURCS PDB2Glycan 1.1.0 
3 2 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}'                                                     LINUCS PDB-CARE   ?     
4 3 LFucpa1-6DGlcpNAcb1-ROH                                                                             
'Glycam Condensed Sequence' GMML       1.0   
5 3 'WURCS=2.0/2,2,1/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-2/a6-b1'                                WURCS PDB2Glycan 1.1.0 
6 3 '[][D-1-deoxy-GlcpNAc]{[(6+1)][a-L-Fucp]{}}'                                                        LINUCS PDB-CARE   ?     
7 4 'DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-ROH'                                                    
'Glycam Condensed Sequence' GMML       1.0   
8 4 'WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1221m-1a_1-5]/1-1-2-3/a4-b1_a6-d1_b4-c1' WURCS PDB2Glycan 1.1.0 
9 4 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}[(6+1)][a-L-Fucp]{}}'               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 2 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 3 2 FUC C1 O1 1 NAG O6 HO6 sing ? 
3 4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
4 4 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
5 4 4 FUC C1 O1 1 NAG O6 HO6 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 
A1IJX non-polymer                   . 
;(2S)-1-[(2S)-2-[[(1S)-1-[(2S)-1-[(2S)-2-azanyl-5-oxidanyl-5-oxidanylidene-pentanoyl]pyrrolidin-2-yl]-2-oxidanyl-2-oxidanylidene-ethyl]amino]propanoyl]pyrrolidine-2-carboxylic acid
;
'3,4-di-O-acetyl-6-O-sulfamoyl-alpha-D-mannose; 3,4-di-O-acetyl-6-O-sulfamoyl-D-mannose; 3,4-di-O-acetyl-6-O-sulfamoyl-mannose' 
'C19 H30 N4 O8'  442.464 
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 
CL    non-polymer                   . 'CHLORIDE ION' ? 'Cl -1'          35.453  
CYS   'L-peptide linking'           y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
FUC   'L-saccharide, alpha linking' . alpha-L-fucopyranose 'alpha-L-fucose; 6-deoxy-alpha-L-galactopyranose; L-fucose; fucose' 
'C6 H12 O5'      164.156 
GLN   'L-peptide linking'           y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking'           y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'             y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking'           y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer                   . WATER ? 'H2 O'           18.015  
ILE   'L-peptide linking'           y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking'           y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking'           y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking'           y METHIONINE ? 'C5 H11 N O2 S'  149.211 
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 
P33   non-polymer                   . 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL 'HEPTAETHYLENE GLYCOL; PEG330' 'C14 H30 O8'     
326.383 
PG4   non-polymer                   . 'TETRAETHYLENE GLYCOL' ? 'C8 H18 O5'      194.226 
PGE   non-polymer                   . 'TRIETHYLENE GLYCOL' ? 'C6 H14 O4'      150.173 
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 
ZN    non-polymer                   . 'ZINC ION' ? 'Zn 2'           65.409  
# 
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                            
FUC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 LFucpa                         
FUC 'COMMON NAME'                         GMML     1.0 a-L-fucopyranose               
FUC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-L-Fucp                       
FUC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Fuc                            
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   LEU 1   1   1   LEU LEU A . n 
A 1 2   ASP 2   2   2   ASP ASP A . n 
A 1 3   PRO 3   3   3   PRO PRO A . n 
A 1 4   GLY 4   4   4   GLY GLY A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   GLN 6   6   6   GLN GLN A . n 
A 1 7   PRO 7   7   7   PRO PRO A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   GLN 9   9   9   GLN GLN A . n 
A 1 10  PHE 10  10  10  PHE PHE A . n 
A 1 11  SER 11  11  11  SER SER A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  ASP 13  13  13  ASP ASP A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  GLN 18  18  18  GLN GLN A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  SER 27  27  27  SER SER A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  GLN 30  30  30  GLN GLN A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  GLN 34  34  34  GLN GLN A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ALA 37  37  37  ALA ALA A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  SER 39  39  39  SER SER A . n 
A 1 40  TRP 40  40  40  TRP TRP A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  HIS 42  42  42  HIS HIS A . n 
A 1 43  ASP 43  43  43  ASP ASP A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  ASN 45  45  45  ASN ASN A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  ARG 52  52  52  ARG ARG A . n 
A 1 53  ARG 53  53  53  ARG ARG A . n 
A 1 54  GLN 54  54  54  GLN GLN A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  GLU 56  56  56  GLU GLU A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  SER 61  61  61  SER SER A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  TRP 68  68  68  TRP TRP A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  GLN 70  70  70  GLN GLN A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  LYS 73  73  73  LYS LYS A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  TYR 76  76  76  TYR TYR A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  PRO 78  78  78  PRO PRO A . n 
A 1 79  ILE 79  79  79  ILE ILE A . n 
A 1 80  TRP 80  80  80  TRP TRP A . n 
A 1 81  GLN 81  81  81  GLN GLN A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  PHE 83  83  83  PHE PHE A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  PRO 86  86  86  PRO PRO A . n 
A 1 87  GLN 87  87  87  GLN GLN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  ILE 92  92  92  ILE ILE A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 PRO 104 104 104 PRO PRO A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 GLN 109 109 109 GLN GLN A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 TYR 111 111 111 TYR TYR A . n 
A 1 112 ASN 112 112 112 ASN ASN A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 SER 116 116 116 SER SER A . n 
A 1 117 GLN 117 117 117 GLN GLN A . n 
A 1 118 MET 118 118 118 MET MET A . n 
A 1 119 SER 119 119 119 SER SER A . n 
A 1 120 ARG 120 120 120 ARG ARG A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 TYR 122 122 122 TYR TYR A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 THR 124 124 124 THR THR A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 LYS 126 126 126 LYS LYS A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 PRO 130 130 ?   ?   ?   A . n 
A 1 131 GLN 131 131 ?   ?   ?   A . n 
A 1 132 LYS 132 132 ?   ?   ?   A . n 
A 1 133 THR 133 133 ?   ?   ?   A . n 
A 1 134 ALA 134 134 ?   ?   ?   A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 CYS 136 136 136 CYS CYS A . n 
A 1 137 TRP 137 137 137 TRP TRP A . n 
A 1 138 SER 138 138 138 SER SER A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 ASP 140 140 140 ASP ASP A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 ASP 142 142 142 ASP ASP A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 THR 144 144 144 THR THR A . n 
A 1 145 ASN 145 145 145 ASN ASN A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 SER 149 149 149 SER SER A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 ARG 151 151 151 ARG ARG A . n 
A 1 152 SER 152 152 152 SER SER A . n 
A 1 153 TYR 153 153 153 TYR TYR A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 MET 155 155 155 MET MET A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 PHE 158 158 158 PHE PHE A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 TRP 160 160 160 TRP TRP A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 GLY 162 162 162 GLY GLY A . n 
A 1 163 TRP 163 163 163 TRP TRP A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 ASN 165 165 165 ASN ASN A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 ALA 167 167 167 ALA ALA A . n 
A 1 168 GLY 168 168 168 GLY GLY A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 LYS 172 172 172 LYS LYS A . n 
A 1 173 PRO 173 173 173 PRO PRO A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 TYR 175 175 175 TYR TYR A . n 
A 1 176 GLU 176 176 176 GLU GLU A . n 
A 1 177 ASP 177 177 177 ASP ASP A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 ASN 183 183 183 ASN ASN A . n 
A 1 184 GLU 184 184 184 GLU GLU A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 TYR 186 186 186 TYR TYR A . n 
A 1 187 LYS 187 187 187 LYS LYS A . n 
A 1 188 GLN 188 188 188 GLN GLN A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 GLY 190 190 190 GLY GLY A . n 
A 1 191 PHE 191 191 191 PHE PHE A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 ASP 193 193 193 ASP ASP A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 TYR 197 197 197 TYR TYR A . n 
A 1 198 TRP 198 198 198 TRP TRP A . n 
A 1 199 ARG 199 199 199 ARG ARG A . n 
A 1 200 SER 200 200 200 SER SER A . n 
A 1 201 TRP 201 201 201 TRP TRP A . n 
A 1 202 TYR 202 202 202 TYR TYR A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 PRO 205 205 205 PRO PRO A . n 
A 1 206 THR 206 206 206 THR THR A . n 
A 1 207 PHE 207 207 207 PHE PHE A . n 
A 1 208 GLU 208 208 208 GLU GLU A . n 
A 1 209 ASP 209 209 209 ASP ASP A . n 
A 1 210 ASP 210 210 210 ASP ASP A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 HIS 213 213 213 HIS HIS A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 TYR 215 215 215 TYR TYR A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 GLN 217 217 217 GLN GLN A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 PRO 220 220 220 PRO PRO A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 TYR 222 222 222 TYR TYR A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ASN 224 224 224 ASN ASN A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 HIS 226 226 226 HIS HIS A . n 
A 1 227 ALA 227 227 227 ALA ALA A . n 
A 1 228 PHE 228 228 228 PHE PHE A . n 
A 1 229 VAL 229 229 229 VAL VAL A . n 
A 1 230 ARG 230 230 230 ARG ARG A . n 
A 1 231 ARG 231 231 231 ARG ARG A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 LEU 233 233 233 LEU LEU A . n 
A 1 234 HIS 234 234 234 HIS HIS A . n 
A 1 235 ARG 235 235 235 ARG ARG A . n 
A 1 236 ARG 236 236 236 ARG ARG A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 GLY 238 238 238 GLY GLY A . n 
A 1 239 ASP 239 239 239 ASP ASP A . n 
A 1 240 ARG 240 240 240 ARG ARG A . n 
A 1 241 TYR 241 241 241 TYR TYR A . n 
A 1 242 ILE 242 242 242 ILE ILE A . n 
A 1 243 ASN 243 243 243 ASN ASN A . n 
A 1 244 LEU 244 244 244 LEU LEU A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 PRO 247 247 247 PRO PRO A . n 
A 1 248 ILE 248 248 248 ILE ILE A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 HIS 251 251 251 HIS HIS A . n 
A 1 252 LEU 252 252 252 LEU LEU A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 GLY 254 254 254 GLY GLY A . n 
A 1 255 ASP 255 255 255 ASP ASP A . n 
A 1 256 MET 256 256 256 MET MET A . n 
A 1 257 TRP 257 257 257 TRP TRP A . n 
A 1 258 ALA 258 258 258 ALA ALA A . n 
A 1 259 GLN 259 259 259 GLN GLN A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 TRP 261 261 261 TRP TRP A . n 
A 1 262 GLU 262 262 262 GLU GLU A . n 
A 1 263 ASN 263 263 263 ASN ASN A . n 
A 1 264 ILE 264 264 264 ILE ILE A . n 
A 1 265 TYR 265 265 265 TYR TYR A . n 
A 1 266 ASP 266 266 266 ASP ASP A . n 
A 1 267 MET 267 267 267 MET MET A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 PRO 270 270 270 PRO PRO A . n 
A 1 271 PHE 271 271 271 PHE PHE A . n 
A 1 272 PRO 272 272 272 PRO PRO A . n 
A 1 273 ASP 273 273 273 ASP ASP A . n 
A 1 274 LYS 274 274 274 LYS LYS A . n 
A 1 275 PRO 275 275 275 PRO PRO A . n 
A 1 276 ASN 276 276 276 ASN ASN A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 ASP 278 278 278 ASP ASP A . n 
A 1 279 VAL 279 279 279 VAL VAL A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 SER 281 281 281 SER SER A . n 
A 1 282 THR 282 282 282 THR THR A . n 
A 1 283 MET 283 283 283 MET MET A . n 
A 1 284 LEU 284 284 284 LEU LEU A . n 
A 1 285 GLN 285 285 285 GLN GLN A . n 
A 1 286 GLN 286 286 286 GLN GLN A . n 
A 1 287 GLY 287 287 287 GLY GLY A . n 
A 1 288 TRP 288 288 288 TRP TRP A . n 
A 1 289 GLN 289 289 289 GLN GLN A . n 
A 1 290 ALA 290 290 290 ALA ALA A . n 
A 1 291 THR 291 291 291 THR THR A . n 
A 1 292 HIS 292 292 292 HIS HIS A . n 
A 1 293 MET 293 293 293 MET MET A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ARG 295 295 295 ARG ARG A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 GLU 298 298 298 GLU GLU A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 PHE 300 300 300 PHE PHE A . n 
A 1 301 PHE 301 301 301 PHE PHE A . n 
A 1 302 THR 302 302 302 THR THR A . n 
A 1 303 SER 303 303 303 SER SER A . n 
A 1 304 LEU 304 304 304 LEU LEU A . n 
A 1 305 GLU 305 305 305 GLU GLU A . n 
A 1 306 LEU 306 306 306 LEU LEU A . n 
A 1 307 SER 307 307 307 SER SER A . n 
A 1 308 PRO 308 308 308 PRO PRO A . n 
A 1 309 MET 309 309 309 MET MET A . n 
A 1 310 PRO 310 310 310 PRO PRO A . n 
A 1 311 PRO 311 311 311 PRO PRO A . n 
A 1 312 GLU 312 312 312 GLU GLU A . n 
A 1 313 PHE 313 313 313 PHE PHE A . n 
A 1 314 TRP 314 314 314 TRP TRP A . n 
A 1 315 GLU 315 315 315 GLU GLU A . n 
A 1 316 GLY 316 316 316 GLY GLY A . n 
A 1 317 SER 317 317 317 SER SER A . n 
A 1 318 MET 318 318 318 MET MET A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 LYS 321 321 321 LYS LYS A . n 
A 1 322 PRO 322 322 322 PRO PRO A . n 
A 1 323 ALA 323 323 323 ALA ALA A . n 
A 1 324 ASP 324 324 324 ASP ASP A . n 
A 1 325 GLY 325 325 325 GLY GLY A . n 
A 1 326 ARG 326 326 326 ARG ARG A . n 
A 1 327 GLU 327 327 327 GLU GLU A . n 
A 1 328 VAL 328 328 328 VAL VAL A . n 
A 1 329 VAL 329 329 329 VAL VAL A . n 
A 1 330 CYS 330 330 330 CYS CYS A . n 
A 1 331 HIS 331 331 331 HIS HIS A . n 
A 1 332 ALA 332 332 332 ALA ALA A . n 
A 1 333 SER 333 333 333 SER SER A . n 
A 1 334 ALA 334 334 334 ALA ALA A . n 
A 1 335 TRP 335 335 335 TRP TRP A . n 
A 1 336 ASP 336 336 336 ASP ASP A . n 
A 1 337 PHE 337 337 337 PHE PHE A . n 
A 1 338 TYR 338 338 338 TYR TYR A . n 
A 1 339 ASN 339 339 339 ASN ASN A . n 
A 1 340 ARG 340 340 340 ARG ARG A . n 
A 1 341 LYS 341 341 341 LYS LYS A . n 
A 1 342 ASP 342 342 342 ASP ASP A . n 
A 1 343 PHE 343 343 343 PHE PHE A . n 
A 1 344 ARG 344 344 344 ARG ARG A . n 
A 1 345 ILE 345 345 345 ILE ILE A . n 
A 1 346 LYS 346 346 346 LYS LYS A . n 
A 1 347 GLN 347 347 347 GLN GLN A . n 
A 1 348 CYS 348 348 348 CYS CYS A . n 
A 1 349 THR 349 349 349 THR THR A . n 
A 1 350 ARG 350 350 350 ARG ARG A . n 
A 1 351 VAL 351 351 351 VAL VAL A . n 
A 1 352 THR 352 352 352 THR THR A . n 
A 1 353 MET 353 353 353 MET MET A . n 
A 1 354 ASP 354 354 354 ASP ASP A . n 
A 1 355 GLN 355 355 355 GLN GLN A . n 
A 1 356 LEU 356 356 356 LEU LEU A . n 
A 1 357 SER 357 357 357 SER SER A . n 
A 1 358 THR 358 358 358 THR THR A . n 
A 1 359 VAL 359 359 359 VAL VAL A . n 
A 1 360 HIS 360 360 360 HIS HIS A . n 
A 1 361 HIS 361 361 361 HIS HIS A . n 
A 1 362 GLU 362 362 362 GLU GLU A . n 
A 1 363 MET 363 363 363 MET MET A . n 
A 1 364 GLY 364 364 364 GLY GLY A . n 
A 1 365 HIS 365 365 365 HIS HIS A . n 
A 1 366 ILE 366 366 366 ILE ILE A . n 
A 1 367 GLN 367 367 367 GLN GLN A . n 
A 1 368 TYR 368 368 368 TYR TYR A . n 
A 1 369 TYR 369 369 369 TYR TYR A . n 
A 1 370 LEU 370 370 370 LEU LEU A . n 
A 1 371 GLN 371 371 371 GLN GLN A . n 
A 1 372 TYR 372 372 372 TYR TYR A . n 
A 1 373 LYS 373 373 373 LYS LYS A . n 
A 1 374 ASP 374 374 374 ASP ASP A . n 
A 1 375 LEU 375 375 375 LEU LEU A . n 
A 1 376 PRO 376 376 376 PRO PRO A . n 
A 1 377 VAL 377 377 377 VAL VAL A . n 
A 1 378 SER 378 378 378 SER SER A . n 
A 1 379 LEU 379 379 379 LEU LEU A . n 
A 1 380 ARG 380 380 380 ARG ARG A . n 
A 1 381 ARG 381 381 381 ARG ARG A . n 
A 1 382 GLY 382 382 382 GLY GLY A . n 
A 1 383 ALA 383 383 383 ALA ALA A . n 
A 1 384 ASN 384 384 384 ASN ASN A . n 
A 1 385 PRO 385 385 385 PRO PRO A . n 
A 1 386 GLY 386 386 386 GLY GLY A . n 
A 1 387 PHE 387 387 387 PHE PHE A . n 
A 1 388 HIS 388 388 388 HIS HIS A . n 
A 1 389 GLU 389 389 389 GLU GLU A . n 
A 1 390 ALA 390 390 390 ALA ALA A . n 
A 1 391 ILE 391 391 391 ILE ILE A . n 
A 1 392 GLY 392 392 392 GLY GLY A . n 
A 1 393 ASP 393 393 393 ASP ASP A . n 
A 1 394 VAL 394 394 394 VAL VAL A . n 
A 1 395 LEU 395 395 395 LEU LEU A . n 
A 1 396 ALA 396 396 396 ALA ALA A . n 
A 1 397 LEU 397 397 397 LEU LEU A . n 
A 1 398 SER 398 398 398 SER SER A . n 
A 1 399 VAL 399 399 399 VAL VAL A . n 
A 1 400 SER 400 400 400 SER SER A . n 
A 1 401 THR 401 401 401 THR THR A . n 
A 1 402 PRO 402 402 402 PRO PRO A . n 
A 1 403 GLU 403 403 403 GLU GLU A . n 
A 1 404 HIS 404 404 404 HIS HIS A . n 
A 1 405 LEU 405 405 405 LEU LEU A . n 
A 1 406 HIS 406 406 406 HIS HIS A . n 
A 1 407 LYS 407 407 407 LYS LYS A . n 
A 1 408 ILE 408 408 408 ILE ILE A . n 
A 1 409 GLY 409 409 409 GLY GLY A . n 
A 1 410 LEU 410 410 410 LEU LEU A . n 
A 1 411 LEU 411 411 411 LEU LEU A . n 
A 1 412 ASP 412 412 412 ASP ASP A . n 
A 1 413 ARG 413 413 413 ARG ARG A . n 
A 1 414 VAL 414 414 414 VAL VAL A . n 
A 1 415 THR 415 415 415 THR THR A . n 
A 1 416 ASN 416 416 416 ASN ASN A . n 
A 1 417 ASP 417 417 417 ASP ASP A . n 
A 1 418 THR 418 418 418 THR THR A . n 
A 1 419 GLU 419 419 419 GLU GLU A . n 
A 1 420 SER 420 420 420 SER SER A . n 
A 1 421 ASP 421 421 421 ASP ASP A . n 
A 1 422 ILE 422 422 422 ILE ILE A . n 
A 1 423 ASN 423 423 423 ASN ASN A . n 
A 1 424 TYR 424 424 424 TYR TYR A . n 
A 1 425 LEU 425 425 425 LEU LEU A . n 
A 1 426 LEU 426 426 426 LEU LEU A . n 
A 1 427 LYS 427 427 427 LYS LYS A . n 
A 1 428 MET 428 428 428 MET MET A . n 
A 1 429 ALA 429 429 429 ALA ALA A . n 
A 1 430 LEU 430 430 430 LEU LEU A . n 
A 1 431 GLU 431 431 431 GLU GLU A . n 
A 1 432 LYS 432 432 432 LYS LYS A . n 
A 1 433 ILE 433 433 433 ILE ILE A . n 
A 1 434 ALA 434 434 434 ALA ALA A . n 
A 1 435 PHE 435 435 435 PHE PHE A . n 
A 1 436 LEU 436 436 436 LEU LEU A . n 
A 1 437 PRO 437 437 437 PRO PRO A . n 
A 1 438 PHE 438 438 438 PHE PHE A . n 
A 1 439 GLY 439 439 439 GLY GLY A . n 
A 1 440 TYR 440 440 440 TYR TYR A . n 
A 1 441 LEU 441 441 441 LEU LEU A . n 
A 1 442 VAL 442 442 442 VAL VAL A . n 
A 1 443 ASP 443 443 443 ASP ASP A . n 
A 1 444 GLN 444 444 444 GLN GLN A . n 
A 1 445 TRP 445 445 445 TRP TRP A . n 
A 1 446 ARG 446 446 446 ARG ARG A . n 
A 1 447 TRP 447 447 447 TRP TRP A . n 
A 1 448 GLY 448 448 448 GLY GLY A . n 
A 1 449 VAL 449 449 449 VAL VAL A . n 
A 1 450 PHE 450 450 450 PHE PHE A . n 
A 1 451 SER 451 451 451 SER SER A . n 
A 1 452 GLY 452 452 452 GLY GLY A . n 
A 1 453 ARG 453 453 453 ARG ARG A . n 
A 1 454 THR 454 454 454 THR THR A . n 
A 1 455 PRO 455 455 455 PRO PRO A . n 
A 1 456 PRO 456 456 456 PRO PRO A . n 
A 1 457 SER 457 457 457 SER SER A . n 
A 1 458 ARG 458 458 458 ARG ARG A . n 
A 1 459 TYR 459 459 459 TYR TYR A . n 
A 1 460 ASN 460 460 460 ASN ASN A . n 
A 1 461 PHE 461 461 461 PHE PHE A . n 
A 1 462 ASP 462 462 462 ASP ASP A . n 
A 1 463 TRP 463 463 463 TRP TRP A . n 
A 1 464 TRP 464 464 464 TRP TRP A . n 
A 1 465 TYR 465 465 465 TYR TYR A . n 
A 1 466 LEU 466 466 466 LEU LEU A . n 
A 1 467 ARG 467 467 467 ARG ARG A . n 
A 1 468 THR 468 468 468 THR THR A . n 
A 1 469 LYS 469 469 469 LYS LYS A . n 
A 1 470 TYR 470 470 470 TYR TYR A . n 
A 1 471 GLN 471 471 471 GLN GLN A . n 
A 1 472 GLY 472 472 472 GLY GLY A . n 
A 1 473 ILE 473 473 473 ILE ILE A . n 
A 1 474 CYS 474 474 474 CYS CYS A . n 
A 1 475 PRO 475 475 475 PRO PRO A . n 
A 1 476 PRO 476 476 476 PRO PRO A . n 
A 1 477 VAL 477 477 477 VAL VAL A . n 
A 1 478 THR 478 478 478 THR THR A . n 
A 1 479 ARG 479 479 479 ARG ARG A . n 
A 1 480 ASN 480 480 480 ASN ASN A . n 
A 1 481 GLU 481 481 481 GLU GLU A . n 
A 1 482 THR 482 482 482 THR THR A . n 
A 1 483 HIS 483 483 483 HIS HIS A . n 
A 1 484 PHE 484 484 484 PHE PHE A . n 
A 1 485 ASP 485 485 485 ASP ASP A . n 
A 1 486 ALA 486 486 486 ALA ALA A . n 
A 1 487 GLY 487 487 487 GLY GLY A . n 
A 1 488 ALA 488 488 488 ALA ALA A . n 
A 1 489 LYS 489 489 489 LYS LYS A . n 
A 1 490 PHE 490 490 490 PHE PHE A . n 
A 1 491 HIS 491 491 491 HIS HIS A . n 
A 1 492 VAL 492 492 492 VAL VAL A . n 
A 1 493 PRO 493 493 493 PRO PRO A . n 
A 1 494 ASN 494 494 494 ASN ASN A . n 
A 1 495 VAL 495 495 495 VAL VAL A . n 
A 1 496 THR 496 496 496 THR THR A . n 
A 1 497 PRO 497 497 497 PRO PRO A . n 
A 1 498 TYR 498 498 498 TYR TYR A . n 
A 1 499 ILE 499 499 499 ILE ILE A . n 
A 1 500 ARG 500 500 500 ARG ARG A . n 
A 1 501 TYR 501 501 501 TYR TYR A . n 
A 1 502 PHE 502 502 502 PHE PHE A . n 
A 1 503 VAL 503 503 503 VAL VAL A . n 
A 1 504 SER 504 504 504 SER SER A . n 
A 1 505 PHE 505 505 505 PHE PHE A . n 
A 1 506 VAL 506 506 506 VAL VAL A . n 
A 1 507 LEU 507 507 507 LEU LEU A . n 
A 1 508 GLN 508 508 508 GLN GLN A . n 
A 1 509 PHE 509 509 509 PHE PHE A . n 
A 1 510 GLN 510 510 510 GLN GLN A . n 
A 1 511 PHE 511 511 511 PHE PHE A . n 
A 1 512 HIS 512 512 512 HIS HIS A . n 
A 1 513 GLU 513 513 513 GLU GLU A . n 
A 1 514 ALA 514 514 514 ALA ALA A . n 
A 1 515 LEU 515 515 515 LEU LEU A . n 
A 1 516 CYS 516 516 516 CYS CYS A . n 
A 1 517 LYS 517 517 517 LYS LYS A . n 
A 1 518 GLU 518 518 518 GLU GLU A . n 
A 1 519 ALA 519 519 519 ALA ALA A . n 
A 1 520 GLY 520 520 520 GLY GLY A . n 
A 1 521 TYR 521 521 521 TYR TYR A . n 
A 1 522 GLU 522 522 522 GLU GLU A . n 
A 1 523 GLY 523 523 523 GLY GLY A . n 
A 1 524 PRO 524 524 524 PRO PRO A . n 
A 1 525 LEU 525 525 525 LEU LEU A . n 
A 1 526 HIS 526 526 526 HIS HIS A . n 
A 1 527 GLN 527 527 527 GLN GLN A . n 
A 1 528 CYS 528 528 528 CYS CYS A . n 
A 1 529 ASP 529 529 529 ASP ASP A . n 
A 1 530 ILE 530 530 530 ILE ILE A . n 
A 1 531 TYR 531 531 531 TYR TYR A . n 
A 1 532 ARG 532 532 532 ARG ARG A . n 
A 1 533 SER 533 533 533 SER SER A . n 
A 1 534 THR 534 534 534 THR THR A . n 
A 1 535 LYS 535 535 535 LYS LYS A . n 
A 1 536 ALA 536 536 536 ALA ALA A . n 
A 1 537 GLY 537 537 537 GLY GLY A . n 
A 1 538 ALA 538 538 538 ALA ALA A . n 
A 1 539 LYS 539 539 539 LYS LYS A . n 
A 1 540 LEU 540 540 540 LEU LEU A . n 
A 1 541 ARG 541 541 541 ARG ARG A . n 
A 1 542 LYS 542 542 542 LYS LYS A . n 
A 1 543 VAL 543 543 543 VAL VAL A . n 
A 1 544 LEU 544 544 544 LEU LEU A . n 
A 1 545 ARG 545 545 545 ARG ARG A . n 
A 1 546 ALA 546 546 546 ALA ALA A . n 
A 1 547 GLY 547 547 547 GLY GLY A . n 
A 1 548 SER 548 548 548 SER SER A . n 
A 1 549 SER 549 549 549 SER SER A . n 
A 1 550 ARG 550 550 550 ARG ARG A . n 
A 1 551 PRO 551 551 551 PRO PRO A . n 
A 1 552 TRP 552 552 552 TRP TRP A . n 
A 1 553 GLN 553 553 553 GLN GLN A . n 
A 1 554 GLU 554 554 554 GLU GLU A . n 
A 1 555 VAL 555 555 555 VAL VAL A . n 
A 1 556 LEU 556 556 556 LEU LEU A . n 
A 1 557 LYS 557 557 557 LYS LYS A . n 
A 1 558 ASP 558 558 558 ASP ASP A . n 
A 1 559 MET 559 559 559 MET MET A . n 
A 1 560 VAL 560 560 560 VAL VAL A . n 
A 1 561 GLY 561 561 561 GLY GLY A . n 
A 1 562 LEU 562 562 562 LEU LEU A . n 
A 1 563 ASP 563 563 563 ASP ASP A . n 
A 1 564 ALA 564 564 564 ALA ALA A . n 
A 1 565 LEU 565 565 565 LEU LEU A . n 
A 1 566 ASP 566 566 566 ASP ASP A . n 
A 1 567 ALA 567 567 567 ALA ALA A . n 
A 1 568 GLN 568 568 568 GLN GLN A . n 
A 1 569 PRO 569 569 569 PRO PRO A . n 
A 1 570 LEU 570 570 570 LEU LEU A . n 
A 1 571 LEU 571 571 571 LEU LEU A . n 
A 1 572 LYS 572 572 572 LYS LYS A . n 
A 1 573 TYR 573 573 573 TYR TYR A . n 
A 1 574 PHE 574 574 574 PHE PHE A . n 
A 1 575 GLN 575 575 575 GLN GLN A . n 
A 1 576 LEU 576 576 576 LEU LEU A . n 
A 1 577 VAL 577 577 577 VAL VAL A . n 
A 1 578 THR 578 578 578 THR THR A . n 
A 1 579 GLN 579 579 579 GLN GLN A . n 
A 1 580 TRP 580 580 580 TRP TRP A . n 
A 1 581 LEU 581 581 581 LEU LEU A . n 
A 1 582 GLN 582 582 582 GLN GLN A . n 
A 1 583 GLU 583 583 583 GLU GLU A . n 
A 1 584 GLN 584 584 584 GLN GLN A . n 
A 1 585 ASN 585 585 585 ASN ASN A . n 
A 1 586 GLN 586 586 586 GLN GLN A . n 
A 1 587 GLN 587 587 587 GLN GLN A . n 
A 1 588 ASN 588 588 588 ASN ASN A . n 
A 1 589 GLY 589 589 589 GLY GLY A . n 
A 1 590 GLU 590 590 590 GLU GLU A . n 
A 1 591 VAL 591 591 591 VAL VAL A . n 
A 1 592 LEU 592 592 592 LEU LEU A . n 
A 1 593 GLY 593 593 593 GLY GLY A . n 
A 1 594 TRP 594 594 594 TRP TRP A . n 
A 1 595 PRO 595 595 595 PRO PRO A . n 
A 1 596 GLU 596 596 596 GLU GLU A . n 
A 1 597 TYR 597 597 597 TYR TYR A . n 
A 1 598 GLN 598 598 598 GLN GLN A . n 
A 1 599 TRP 599 599 599 TRP TRP A . n 
A 1 600 HIS 600 600 600 HIS HIS A . n 
A 1 601 PRO 601 601 601 PRO PRO A . n 
A 1 602 PRO 602 602 602 PRO PRO A . n 
A 1 603 LEU 603 603 603 LEU LEU A . n 
A 1 604 PRO 604 604 604 PRO PRO A . n 
A 1 605 ASP 605 605 605 ASP ASP A . n 
A 1 606 ASN 606 606 606 ASN ASN A . n 
A 1 607 TYR 607 607 607 TYR TYR A . n 
A 1 608 PRO 608 608 608 PRO PRO A . n 
A 1 609 GLU 609 609 609 GLU GLU A . n 
A 1 610 GLY 610 610 ?   ?   ?   A . n 
A 1 611 ILE 611 611 ?   ?   ?   A . n 
A 1 612 ASP 612 612 ?   ?   ?   A . n 
A 1 613 LEU 613 613 ?   ?   ?   A . n 
A 1 614 VAL 614 614 ?   ?   ?   A . n 
A 1 615 THR 615 615 ?   ?   ?   A . n 
A 1 616 ASP 616 616 ?   ?   ?   A . n 
A 1 617 GLU 617 617 ?   ?   ?   A . n 
A 1 618 ALA 618 618 ?   ?   ?   A . n 
A 1 619 GLU 619 619 ?   ?   ?   A . n 
A 1 620 ALA 620 620 ?   ?   ?   A . n 
A 1 621 SER 621 621 ?   ?   ?   A . n 
A 1 622 LYS 622 622 ?   ?   ?   A . n 
A 1 623 PHE 623 623 ?   ?   ?   A . n 
A 1 624 VAL 624 624 ?   ?   ?   A . n 
A 1 625 GLU 625 625 ?   ?   ?   A . n 
A 1 626 GLU 626 626 ?   ?   ?   A . n 
A 1 627 TYR 627 627 ?   ?   ?   A . n 
A 1 628 ASP 628 628 ?   ?   ?   A . n 
B 1 1   LEU 1   1   ?   ?   ?   B . n 
B 1 2   ASP 2   2   2   ASP ASP B . n 
B 1 3   PRO 3   3   3   PRO PRO B . n 
B 1 4   GLY 4   4   4   GLY GLY B . n 
B 1 5   LEU 5   5   5   LEU LEU B . n 
B 1 6   GLN 6   6   6   GLN GLN B . n 
B 1 7   PRO 7   7   7   PRO PRO B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   GLN 9   9   9   GLN GLN B . n 
B 1 10  PHE 10  10  10  PHE PHE B . n 
B 1 11  SER 11  11  11  SER SER B . n 
B 1 12  ALA 12  12  12  ALA ALA B . n 
B 1 13  ASP 13  13  13  ASP ASP B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  ALA 15  15  15  ALA ALA B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  ALA 17  17  17  ALA ALA B . n 
B 1 18  GLN 18  18  18  GLN GLN B . n 
B 1 19  LEU 19  19  19  LEU LEU B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  GLN 22  22  22  GLN GLN B . n 
B 1 23  SER 23  23  23  SER SER B . n 
B 1 24  TYR 24  24  24  TYR TYR B . n 
B 1 25  GLN 25  25  25  GLN GLN B . n 
B 1 26  SER 26  26  26  SER SER B . n 
B 1 27  SER 27  27  27  SER SER B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  GLU 29  29  29  GLU GLU B . n 
B 1 30  GLN 30  30  30  GLN GLN B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  PHE 33  33  33  PHE PHE B . n 
B 1 34  GLN 34  34  34  GLN GLN B . n 
B 1 35  SER 35  35  35  SER SER B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ALA 37  37  37  ALA ALA B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  SER 39  39  39  SER SER B . n 
B 1 40  TRP 40  40  40  TRP TRP B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  HIS 42  42  42  HIS HIS B . n 
B 1 43  ASP 43  43  43  ASP ASP B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  ASN 45  45  45  ASN ASN B . n 
B 1 46  ILE 46  46  46  ILE ILE B . n 
B 1 47  THR 47  47  47  THR THR B . n 
B 1 48  ALA 48  48  48  ALA ALA B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  ASN 50  50  50  ASN ASN B . n 
B 1 51  ALA 51  51  51  ALA ALA B . n 
B 1 52  ARG 52  52  52  ARG ARG B . n 
B 1 53  ARG 53  53  53  ARG ARG B . n 
B 1 54  GLN 54  54  54  GLN GLN B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  GLU 56  56  56  GLU GLU B . n 
B 1 57  ALA 57  57  57  ALA ALA B . n 
B 1 58  ALA 58  58  58  ALA ALA B . n 
B 1 59  LEU 59  59  59  LEU LEU B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  SER 61  61  61  SER SER B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  GLU 63  63  63  GLU GLU B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  ALA 65  65  65  ALA ALA B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  ALA 67  67  67  ALA ALA B . n 
B 1 68  TRP 68  68  68  TRP TRP B . n 
B 1 69  GLY 69  69  69  GLY GLY B . n 
B 1 70  GLN 70  70  70  GLN GLN B . n 
B 1 71  LYS 71  71  71  LYS LYS B . n 
B 1 72  ALA 72  72  72  ALA ALA B . n 
B 1 73  LYS 73  73  73  LYS LYS B . n 
B 1 74  GLU 74  74  74  GLU GLU B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  TYR 76  76  76  TYR TYR B . n 
B 1 77  GLU 77  77  77  GLU GLU B . n 
B 1 78  PRO 78  78  78  PRO PRO B . n 
B 1 79  ILE 79  79  79  ILE ILE B . n 
B 1 80  TRP 80  80  80  TRP TRP B . n 
B 1 81  GLN 81  81  81  GLN GLN B . n 
B 1 82  GLN 82  82  82  GLN GLN B . n 
B 1 83  PHE 83  83  83  PHE PHE B . n 
B 1 84  THR 84  84  84  THR THR B . n 
B 1 85  ASP 85  85  85  ASP ASP B . n 
B 1 86  PRO 86  86  86  PRO PRO B . n 
B 1 87  GLN 87  87  87  GLN GLN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ARG 89  89  89  ARG ARG B . n 
B 1 90  ARG 90  90  90  ARG ARG B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  ILE 92  92  92  ILE ILE B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  ARG 96  96  96  ARG ARG B . n 
B 1 97  THR 97  97  97  THR THR B . n 
B 1 98  LEU 98  98  98  LEU LEU B . n 
B 1 99  GLY 99  99  99  GLY GLY B . n 
B 1 100 SER 100 100 100 SER SER B . n 
B 1 101 ALA 101 101 101 ALA ALA B . n 
B 1 102 ASN 102 102 102 ASN ASN B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 PRO 104 104 104 PRO PRO B . n 
B 1 105 LEU 105 105 105 LEU LEU B . n 
B 1 106 ALA 106 106 106 ALA ALA B . n 
B 1 107 LYS 107 107 107 LYS LYS B . n 
B 1 108 ARG 108 108 108 ARG ARG B . n 
B 1 109 GLN 109 109 109 GLN GLN B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 TYR 111 111 111 TYR TYR B . n 
B 1 112 ASN 112 112 112 ASN ASN B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 LEU 114 114 114 LEU LEU B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 SER 116 116 116 SER SER B . n 
B 1 117 GLN 117 117 117 GLN GLN B . n 
B 1 118 MET 118 118 118 MET MET B . n 
B 1 119 SER 119 119 119 SER SER B . n 
B 1 120 ARG 120 120 120 ARG ARG B . n 
B 1 121 ILE 121 121 121 ILE ILE B . n 
B 1 122 TYR 122 122 122 TYR TYR B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 THR 124 124 124 THR THR B . n 
B 1 125 ALA 125 125 125 ALA ALA B . n 
B 1 126 LYS 126 126 126 LYS LYS B . n 
B 1 127 VAL 127 127 127 VAL VAL B . n 
B 1 128 CYS 128 128 128 CYS CYS B . n 
B 1 129 LEU 129 129 129 LEU LEU B . n 
B 1 130 PRO 130 130 ?   ?   ?   B . n 
B 1 131 GLN 131 131 ?   ?   ?   B . n 
B 1 132 LYS 132 132 ?   ?   ?   B . n 
B 1 133 THR 133 133 ?   ?   ?   B . n 
B 1 134 ALA 134 134 ?   ?   ?   B . n 
B 1 135 THR 135 135 ?   ?   ?   B . n 
B 1 136 CYS 136 136 136 CYS CYS B . n 
B 1 137 TRP 137 137 137 TRP TRP B . n 
B 1 138 SER 138 138 138 SER SER B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 ASP 140 140 140 ASP ASP B . n 
B 1 141 PRO 141 141 141 PRO PRO B . n 
B 1 142 ASP 142 142 142 ASP ASP B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 THR 144 144 144 THR THR B . n 
B 1 145 ASN 145 145 145 ASN ASN B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 ALA 148 148 148 ALA ALA B . n 
B 1 149 SER 149 149 149 SER SER B . n 
B 1 150 SER 150 150 150 SER SER B . n 
B 1 151 ARG 151 151 151 ARG ARG B . n 
B 1 152 SER 152 152 152 SER SER B . n 
B 1 153 TYR 153 153 153 TYR TYR B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 MET 155 155 155 MET MET B . n 
B 1 156 LEU 156 156 156 LEU LEU B . n 
B 1 157 LEU 157 157 157 LEU LEU B . n 
B 1 158 PHE 158 158 158 PHE PHE B . n 
B 1 159 ALA 159 159 159 ALA ALA B . n 
B 1 160 TRP 160 160 160 TRP TRP B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 GLY 162 162 162 GLY GLY B . n 
B 1 163 TRP 163 163 163 TRP TRP B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 ASN 165 165 165 ASN ASN B . n 
B 1 166 ALA 166 166 166 ALA ALA B . n 
B 1 167 ALA 167 167 167 ALA ALA B . n 
B 1 168 GLY 168 168 168 GLY GLY B . n 
B 1 169 ILE 169 169 169 ILE ILE B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 LEU 171 171 171 LEU LEU B . n 
B 1 172 LYS 172 172 172 LYS LYS B . n 
B 1 173 PRO 173 173 173 PRO PRO B . n 
B 1 174 LEU 174 174 174 LEU LEU B . n 
B 1 175 TYR 175 175 175 TYR TYR B . n 
B 1 176 GLU 176 176 176 GLU GLU B . n 
B 1 177 ASP 177 177 177 ASP ASP B . n 
B 1 178 PHE 178 178 178 PHE PHE B . n 
B 1 179 THR 179 179 179 THR THR B . n 
B 1 180 ALA 180 180 180 ALA ALA B . n 
B 1 181 LEU 181 181 181 LEU LEU B . n 
B 1 182 SER 182 182 182 SER SER B . n 
B 1 183 ASN 183 183 183 ASN ASN B . n 
B 1 184 GLU 184 184 184 GLU GLU B . n 
B 1 185 ALA 185 185 185 ALA ALA B . n 
B 1 186 TYR 186 186 186 TYR TYR B . n 
B 1 187 LYS 187 187 187 LYS LYS B . n 
B 1 188 GLN 188 188 188 GLN GLN B . n 
B 1 189 ASP 189 189 189 ASP ASP B . n 
B 1 190 GLY 190 190 190 GLY GLY B . n 
B 1 191 PHE 191 191 191 PHE PHE B . n 
B 1 192 THR 192 192 192 THR THR B . n 
B 1 193 ASP 193 193 193 ASP ASP B . n 
B 1 194 THR 194 194 194 THR THR B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 ALA 196 196 196 ALA ALA B . n 
B 1 197 TYR 197 197 197 TYR TYR B . n 
B 1 198 TRP 198 198 198 TRP TRP B . n 
B 1 199 ARG 199 199 199 ARG ARG B . n 
B 1 200 SER 200 200 200 SER SER B . n 
B 1 201 TRP 201 201 201 TRP TRP B . n 
B 1 202 TYR 202 202 202 TYR TYR B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 SER 204 204 204 SER SER B . n 
B 1 205 PRO 205 205 205 PRO PRO B . n 
B 1 206 THR 206 206 206 THR THR B . n 
B 1 207 PHE 207 207 207 PHE PHE B . n 
B 1 208 GLU 208 208 208 GLU GLU B . n 
B 1 209 ASP 209 209 209 ASP ASP B . n 
B 1 210 ASP 210 210 210 ASP ASP B . n 
B 1 211 LEU 211 211 211 LEU LEU B . n 
B 1 212 GLU 212 212 212 GLU GLU B . n 
B 1 213 HIS 213 213 213 HIS HIS B . n 
B 1 214 LEU 214 214 214 LEU LEU B . n 
B 1 215 TYR 215 215 215 TYR TYR B . n 
B 1 216 GLN 216 216 216 GLN GLN B . n 
B 1 217 GLN 217 217 217 GLN GLN B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 GLU 219 219 219 GLU GLU B . n 
B 1 220 PRO 220 220 220 PRO PRO B . n 
B 1 221 LEU 221 221 221 LEU LEU B . n 
B 1 222 TYR 222 222 222 TYR TYR B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 ASN 224 224 224 ASN ASN B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 HIS 226 226 226 HIS HIS B . n 
B 1 227 ALA 227 227 227 ALA ALA B . n 
B 1 228 PHE 228 228 228 PHE PHE B . n 
B 1 229 VAL 229 229 229 VAL VAL B . n 
B 1 230 ARG 230 230 230 ARG ARG B . n 
B 1 231 ARG 231 231 231 ARG ARG B . n 
B 1 232 ALA 232 232 232 ALA ALA B . n 
B 1 233 LEU 233 233 233 LEU LEU B . n 
B 1 234 HIS 234 234 234 HIS HIS B . n 
B 1 235 ARG 235 235 235 ARG ARG B . n 
B 1 236 ARG 236 236 236 ARG ARG B . n 
B 1 237 TYR 237 237 237 TYR TYR B . n 
B 1 238 GLY 238 238 238 GLY GLY B . n 
B 1 239 ASP 239 239 239 ASP ASP B . n 
B 1 240 ARG 240 240 240 ARG ARG B . n 
B 1 241 TYR 241 241 241 TYR TYR B . n 
B 1 242 ILE 242 242 242 ILE ILE B . n 
B 1 243 ASN 243 243 243 ASN ASN B . n 
B 1 244 LEU 244 244 244 LEU LEU B . n 
B 1 245 ARG 245 245 245 ARG ARG B . n 
B 1 246 GLY 246 246 246 GLY GLY B . n 
B 1 247 PRO 247 247 247 PRO PRO B . n 
B 1 248 ILE 248 248 248 ILE ILE B . n 
B 1 249 PRO 249 249 249 PRO PRO B . n 
B 1 250 ALA 250 250 250 ALA ALA B . n 
B 1 251 HIS 251 251 251 HIS HIS B . n 
B 1 252 LEU 252 252 252 LEU LEU B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 GLY 254 254 254 GLY GLY B . n 
B 1 255 ASP 255 255 255 ASP ASP B . n 
B 1 256 MET 256 256 256 MET MET B . n 
B 1 257 TRP 257 257 257 TRP TRP B . n 
B 1 258 ALA 258 258 258 ALA ALA B . n 
B 1 259 GLN 259 259 259 GLN GLN B . n 
B 1 260 SER 260 260 260 SER SER B . n 
B 1 261 TRP 261 261 261 TRP TRP B . n 
B 1 262 GLU 262 262 262 GLU GLU B . n 
B 1 263 ASN 263 263 263 ASN ASN B . n 
B 1 264 ILE 264 264 264 ILE ILE B . n 
B 1 265 TYR 265 265 265 TYR TYR B . n 
B 1 266 ASP 266 266 266 ASP ASP B . n 
B 1 267 MET 267 267 267 MET MET B . n 
B 1 268 VAL 268 268 268 VAL VAL B . n 
B 1 269 VAL 269 269 269 VAL VAL B . n 
B 1 270 PRO 270 270 270 PRO PRO B . n 
B 1 271 PHE 271 271 271 PHE PHE B . n 
B 1 272 PRO 272 272 272 PRO PRO B . n 
B 1 273 ASP 273 273 273 ASP ASP B . n 
B 1 274 LYS 274 274 274 LYS LYS B . n 
B 1 275 PRO 275 275 275 PRO PRO B . n 
B 1 276 ASN 276 276 276 ASN ASN B . n 
B 1 277 LEU 277 277 277 LEU LEU B . n 
B 1 278 ASP 278 278 278 ASP ASP B . n 
B 1 279 VAL 279 279 279 VAL VAL B . n 
B 1 280 THR 280 280 280 THR THR B . n 
B 1 281 SER 281 281 281 SER SER B . n 
B 1 282 THR 282 282 282 THR THR B . n 
B 1 283 MET 283 283 283 MET MET B . n 
B 1 284 LEU 284 284 284 LEU LEU B . n 
B 1 285 GLN 285 285 285 GLN GLN B . n 
B 1 286 GLN 286 286 286 GLN GLN B . n 
B 1 287 GLY 287 287 287 GLY GLY B . n 
B 1 288 TRP 288 288 288 TRP TRP B . n 
B 1 289 GLN 289 289 289 GLN GLN B . n 
B 1 290 ALA 290 290 290 ALA ALA B . n 
B 1 291 THR 291 291 291 THR THR B . n 
B 1 292 HIS 292 292 292 HIS HIS B . n 
B 1 293 MET 293 293 293 MET MET B . n 
B 1 294 PHE 294 294 294 PHE PHE B . n 
B 1 295 ARG 295 295 295 ARG ARG B . n 
B 1 296 VAL 296 296 296 VAL VAL B . n 
B 1 297 ALA 297 297 297 ALA ALA B . n 
B 1 298 GLU 298 298 298 GLU GLU B . n 
B 1 299 GLU 299 299 299 GLU GLU B . n 
B 1 300 PHE 300 300 300 PHE PHE B . n 
B 1 301 PHE 301 301 301 PHE PHE B . n 
B 1 302 THR 302 302 302 THR THR B . n 
B 1 303 SER 303 303 303 SER SER B . n 
B 1 304 LEU 304 304 304 LEU LEU B . n 
B 1 305 GLU 305 305 305 GLU GLU B . n 
B 1 306 LEU 306 306 306 LEU LEU B . n 
B 1 307 SER 307 307 307 SER SER B . n 
B 1 308 PRO 308 308 308 PRO PRO B . n 
B 1 309 MET 309 309 309 MET MET B . n 
B 1 310 PRO 310 310 310 PRO PRO B . n 
B 1 311 PRO 311 311 311 PRO PRO B . n 
B 1 312 GLU 312 312 312 GLU GLU B . n 
B 1 313 PHE 313 313 313 PHE PHE B . n 
B 1 314 TRP 314 314 314 TRP TRP B . n 
B 1 315 GLU 315 315 315 GLU GLU B . n 
B 1 316 GLY 316 316 316 GLY GLY B . n 
B 1 317 SER 317 317 317 SER SER B . n 
B 1 318 MET 318 318 318 MET MET B . n 
B 1 319 LEU 319 319 319 LEU LEU B . n 
B 1 320 GLU 320 320 320 GLU GLU B . n 
B 1 321 LYS 321 321 321 LYS LYS B . n 
B 1 322 PRO 322 322 322 PRO PRO B . n 
B 1 323 ALA 323 323 323 ALA ALA B . n 
B 1 324 ASP 324 324 324 ASP ASP B . n 
B 1 325 GLY 325 325 325 GLY GLY B . n 
B 1 326 ARG 326 326 326 ARG ARG B . n 
B 1 327 GLU 327 327 327 GLU GLU B . n 
B 1 328 VAL 328 328 328 VAL VAL B . n 
B 1 329 VAL 329 329 329 VAL VAL B . n 
B 1 330 CYS 330 330 330 CYS CYS B . n 
B 1 331 HIS 331 331 331 HIS HIS B . n 
B 1 332 ALA 332 332 332 ALA ALA B . n 
B 1 333 SER 333 333 333 SER SER B . n 
B 1 334 ALA 334 334 334 ALA ALA B . n 
B 1 335 TRP 335 335 335 TRP TRP B . n 
B 1 336 ASP 336 336 336 ASP ASP B . n 
B 1 337 PHE 337 337 337 PHE PHE B . n 
B 1 338 TYR 338 338 338 TYR TYR B . n 
B 1 339 ASN 339 339 339 ASN ASN B . n 
B 1 340 ARG 340 340 340 ARG ARG B . n 
B 1 341 LYS 341 341 341 LYS LYS B . n 
B 1 342 ASP 342 342 342 ASP ASP B . n 
B 1 343 PHE 343 343 343 PHE PHE B . n 
B 1 344 ARG 344 344 344 ARG ARG B . n 
B 1 345 ILE 345 345 345 ILE ILE B . n 
B 1 346 LYS 346 346 346 LYS LYS B . n 
B 1 347 GLN 347 347 347 GLN GLN B . n 
B 1 348 CYS 348 348 348 CYS CYS B . n 
B 1 349 THR 349 349 349 THR THR B . n 
B 1 350 ARG 350 350 350 ARG ARG B . n 
B 1 351 VAL 351 351 351 VAL VAL B . n 
B 1 352 THR 352 352 352 THR THR B . n 
B 1 353 MET 353 353 353 MET MET B . n 
B 1 354 ASP 354 354 354 ASP ASP B . n 
B 1 355 GLN 355 355 355 GLN GLN B . n 
B 1 356 LEU 356 356 356 LEU LEU B . n 
B 1 357 SER 357 357 357 SER SER B . n 
B 1 358 THR 358 358 358 THR THR B . n 
B 1 359 VAL 359 359 359 VAL VAL B . n 
B 1 360 HIS 360 360 360 HIS HIS B . n 
B 1 361 HIS 361 361 361 HIS HIS B . n 
B 1 362 GLU 362 362 362 GLU GLU B . n 
B 1 363 MET 363 363 363 MET MET B . n 
B 1 364 GLY 364 364 364 GLY GLY B . n 
B 1 365 HIS 365 365 365 HIS HIS B . n 
B 1 366 ILE 366 366 366 ILE ILE B . n 
B 1 367 GLN 367 367 367 GLN GLN B . n 
B 1 368 TYR 368 368 368 TYR TYR B . n 
B 1 369 TYR 369 369 369 TYR TYR B . n 
B 1 370 LEU 370 370 370 LEU LEU B . n 
B 1 371 GLN 371 371 371 GLN GLN B . n 
B 1 372 TYR 372 372 372 TYR TYR B . n 
B 1 373 LYS 373 373 373 LYS LYS B . n 
B 1 374 ASP 374 374 374 ASP ASP B . n 
B 1 375 LEU 375 375 375 LEU LEU B . n 
B 1 376 PRO 376 376 376 PRO PRO B . n 
B 1 377 VAL 377 377 377 VAL VAL B . n 
B 1 378 SER 378 378 378 SER SER B . n 
B 1 379 LEU 379 379 379 LEU LEU B . n 
B 1 380 ARG 380 380 380 ARG ARG B . n 
B 1 381 ARG 381 381 381 ARG ARG B . n 
B 1 382 GLY 382 382 382 GLY GLY B . n 
B 1 383 ALA 383 383 383 ALA ALA B . n 
B 1 384 ASN 384 384 384 ASN ASN B . n 
B 1 385 PRO 385 385 385 PRO PRO B . n 
B 1 386 GLY 386 386 386 GLY GLY B . n 
B 1 387 PHE 387 387 387 PHE PHE B . n 
B 1 388 HIS 388 388 388 HIS HIS B . n 
B 1 389 GLU 389 389 389 GLU GLU B . n 
B 1 390 ALA 390 390 390 ALA ALA B . n 
B 1 391 ILE 391 391 391 ILE ILE B . n 
B 1 392 GLY 392 392 392 GLY GLY B . n 
B 1 393 ASP 393 393 393 ASP ASP B . n 
B 1 394 VAL 394 394 394 VAL VAL B . n 
B 1 395 LEU 395 395 395 LEU LEU B . n 
B 1 396 ALA 396 396 396 ALA ALA B . n 
B 1 397 LEU 397 397 397 LEU LEU B . n 
B 1 398 SER 398 398 398 SER SER B . n 
B 1 399 VAL 399 399 399 VAL VAL B . n 
B 1 400 SER 400 400 400 SER SER B . n 
B 1 401 THR 401 401 401 THR THR B . n 
B 1 402 PRO 402 402 402 PRO PRO B . n 
B 1 403 GLU 403 403 403 GLU GLU B . n 
B 1 404 HIS 404 404 404 HIS HIS B . n 
B 1 405 LEU 405 405 405 LEU LEU B . n 
B 1 406 HIS 406 406 406 HIS HIS B . n 
B 1 407 LYS 407 407 407 LYS LYS B . n 
B 1 408 ILE 408 408 408 ILE ILE B . n 
B 1 409 GLY 409 409 409 GLY GLY B . n 
B 1 410 LEU 410 410 410 LEU LEU B . n 
B 1 411 LEU 411 411 411 LEU LEU B . n 
B 1 412 ASP 412 412 412 ASP ASP B . n 
B 1 413 ARG 413 413 413 ARG ARG B . n 
B 1 414 VAL 414 414 414 VAL VAL B . n 
B 1 415 THR 415 415 415 THR THR B . n 
B 1 416 ASN 416 416 416 ASN ASN B . n 
B 1 417 ASP 417 417 417 ASP ASP B . n 
B 1 418 THR 418 418 418 THR THR B . n 
B 1 419 GLU 419 419 419 GLU GLU B . n 
B 1 420 SER 420 420 420 SER SER B . n 
B 1 421 ASP 421 421 421 ASP ASP B . n 
B 1 422 ILE 422 422 422 ILE ILE B . n 
B 1 423 ASN 423 423 423 ASN ASN B . n 
B 1 424 TYR 424 424 424 TYR TYR B . n 
B 1 425 LEU 425 425 425 LEU LEU B . n 
B 1 426 LEU 426 426 426 LEU LEU B . n 
B 1 427 LYS 427 427 427 LYS LYS B . n 
B 1 428 MET 428 428 428 MET MET B . n 
B 1 429 ALA 429 429 429 ALA ALA B . n 
B 1 430 LEU 430 430 430 LEU LEU B . n 
B 1 431 GLU 431 431 431 GLU GLU B . n 
B 1 432 LYS 432 432 432 LYS LYS B . n 
B 1 433 ILE 433 433 433 ILE ILE B . n 
B 1 434 ALA 434 434 434 ALA ALA B . n 
B 1 435 PHE 435 435 435 PHE PHE B . n 
B 1 436 LEU 436 436 436 LEU LEU B . n 
B 1 437 PRO 437 437 437 PRO PRO B . n 
B 1 438 PHE 438 438 438 PHE PHE B . n 
B 1 439 GLY 439 439 439 GLY GLY B . n 
B 1 440 TYR 440 440 440 TYR TYR B . n 
B 1 441 LEU 441 441 441 LEU LEU B . n 
B 1 442 VAL 442 442 442 VAL VAL B . n 
B 1 443 ASP 443 443 443 ASP ASP B . n 
B 1 444 GLN 444 444 444 GLN GLN B . n 
B 1 445 TRP 445 445 445 TRP TRP B . n 
B 1 446 ARG 446 446 446 ARG ARG B . n 
B 1 447 TRP 447 447 447 TRP TRP B . n 
B 1 448 GLY 448 448 448 GLY GLY B . n 
B 1 449 VAL 449 449 449 VAL VAL B . n 
B 1 450 PHE 450 450 450 PHE PHE B . n 
B 1 451 SER 451 451 451 SER SER B . n 
B 1 452 GLY 452 452 452 GLY GLY B . n 
B 1 453 ARG 453 453 453 ARG ARG B . n 
B 1 454 THR 454 454 454 THR THR B . n 
B 1 455 PRO 455 455 455 PRO PRO B . n 
B 1 456 PRO 456 456 456 PRO PRO B . n 
B 1 457 SER 457 457 457 SER SER B . n 
B 1 458 ARG 458 458 458 ARG ARG B . n 
B 1 459 TYR 459 459 459 TYR TYR B . n 
B 1 460 ASN 460 460 460 ASN ASN B . n 
B 1 461 PHE 461 461 461 PHE PHE B . n 
B 1 462 ASP 462 462 462 ASP ASP B . n 
B 1 463 TRP 463 463 463 TRP TRP B . n 
B 1 464 TRP 464 464 464 TRP TRP B . n 
B 1 465 TYR 465 465 465 TYR TYR B . n 
B 1 466 LEU 466 466 466 LEU LEU B . n 
B 1 467 ARG 467 467 467 ARG ARG B . n 
B 1 468 THR 468 468 468 THR THR B . n 
B 1 469 LYS 469 469 469 LYS LYS B . n 
B 1 470 TYR 470 470 470 TYR TYR B . n 
B 1 471 GLN 471 471 471 GLN GLN B . n 
B 1 472 GLY 472 472 472 GLY GLY B . n 
B 1 473 ILE 473 473 473 ILE ILE B . n 
B 1 474 CYS 474 474 474 CYS CYS B . n 
B 1 475 PRO 475 475 475 PRO PRO B . n 
B 1 476 PRO 476 476 476 PRO PRO B . n 
B 1 477 VAL 477 477 477 VAL VAL B . n 
B 1 478 THR 478 478 478 THR THR B . n 
B 1 479 ARG 479 479 479 ARG ARG B . n 
B 1 480 ASN 480 480 480 ASN ASN B . n 
B 1 481 GLU 481 481 481 GLU GLU B . n 
B 1 482 THR 482 482 482 THR THR B . n 
B 1 483 HIS 483 483 483 HIS HIS B . n 
B 1 484 PHE 484 484 484 PHE PHE B . n 
B 1 485 ASP 485 485 485 ASP ASP B . n 
B 1 486 ALA 486 486 486 ALA ALA B . n 
B 1 487 GLY 487 487 487 GLY GLY B . n 
B 1 488 ALA 488 488 488 ALA ALA B . n 
B 1 489 LYS 489 489 489 LYS LYS B . n 
B 1 490 PHE 490 490 490 PHE PHE B . n 
B 1 491 HIS 491 491 491 HIS HIS B . n 
B 1 492 VAL 492 492 492 VAL VAL B . n 
B 1 493 PRO 493 493 493 PRO PRO B . n 
B 1 494 ASN 494 494 494 ASN ASN B . n 
B 1 495 VAL 495 495 495 VAL VAL B . n 
B 1 496 THR 496 496 496 THR THR B . n 
B 1 497 PRO 497 497 497 PRO PRO B . n 
B 1 498 TYR 498 498 498 TYR TYR B . n 
B 1 499 ILE 499 499 499 ILE ILE B . n 
B 1 500 ARG 500 500 500 ARG ARG B . n 
B 1 501 TYR 501 501 501 TYR TYR B . n 
B 1 502 PHE 502 502 502 PHE PHE B . n 
B 1 503 VAL 503 503 503 VAL VAL B . n 
B 1 504 SER 504 504 504 SER SER B . n 
B 1 505 PHE 505 505 505 PHE PHE B . n 
B 1 506 VAL 506 506 506 VAL VAL B . n 
B 1 507 LEU 507 507 507 LEU LEU B . n 
B 1 508 GLN 508 508 508 GLN GLN B . n 
B 1 509 PHE 509 509 509 PHE PHE B . n 
B 1 510 GLN 510 510 510 GLN GLN B . n 
B 1 511 PHE 511 511 511 PHE PHE B . n 
B 1 512 HIS 512 512 512 HIS HIS B . n 
B 1 513 GLU 513 513 513 GLU GLU B . n 
B 1 514 ALA 514 514 514 ALA ALA B . n 
B 1 515 LEU 515 515 515 LEU LEU B . n 
B 1 516 CYS 516 516 516 CYS CYS B . n 
B 1 517 LYS 517 517 517 LYS LYS B . n 
B 1 518 GLU 518 518 518 GLU GLU B . n 
B 1 519 ALA 519 519 519 ALA ALA B . n 
B 1 520 GLY 520 520 520 GLY GLY B . n 
B 1 521 TYR 521 521 521 TYR TYR B . n 
B 1 522 GLU 522 522 522 GLU GLU B . n 
B 1 523 GLY 523 523 523 GLY GLY B . n 
B 1 524 PRO 524 524 524 PRO PRO B . n 
B 1 525 LEU 525 525 525 LEU LEU B . n 
B 1 526 HIS 526 526 526 HIS HIS B . n 
B 1 527 GLN 527 527 527 GLN GLN B . n 
B 1 528 CYS 528 528 528 CYS CYS B . n 
B 1 529 ASP 529 529 529 ASP ASP B . n 
B 1 530 ILE 530 530 530 ILE ILE B . n 
B 1 531 TYR 531 531 531 TYR TYR B . n 
B 1 532 ARG 532 532 532 ARG ARG B . n 
B 1 533 SER 533 533 533 SER SER B . n 
B 1 534 THR 534 534 534 THR THR B . n 
B 1 535 LYS 535 535 535 LYS LYS B . n 
B 1 536 ALA 536 536 536 ALA ALA B . n 
B 1 537 GLY 537 537 537 GLY GLY B . n 
B 1 538 ALA 538 538 538 ALA ALA B . n 
B 1 539 LYS 539 539 539 LYS LYS B . n 
B 1 540 LEU 540 540 540 LEU LEU B . n 
B 1 541 ARG 541 541 541 ARG ARG B . n 
B 1 542 LYS 542 542 542 LYS LYS B . n 
B 1 543 VAL 543 543 543 VAL VAL B . n 
B 1 544 LEU 544 544 544 LEU LEU B . n 
B 1 545 ARG 545 545 545 ARG ARG B . n 
B 1 546 ALA 546 546 546 ALA ALA B . n 
B 1 547 GLY 547 547 547 GLY GLY B . n 
B 1 548 SER 548 548 548 SER SER B . n 
B 1 549 SER 549 549 549 SER SER B . n 
B 1 550 ARG 550 550 550 ARG ARG B . n 
B 1 551 PRO 551 551 551 PRO PRO B . n 
B 1 552 TRP 552 552 552 TRP TRP B . n 
B 1 553 GLN 553 553 553 GLN GLN B . n 
B 1 554 GLU 554 554 554 GLU GLU B . n 
B 1 555 VAL 555 555 555 VAL VAL B . n 
B 1 556 LEU 556 556 556 LEU LEU B . n 
B 1 557 LYS 557 557 557 LYS LYS B . n 
B 1 558 ASP 558 558 558 ASP ASP B . n 
B 1 559 MET 559 559 559 MET MET B . n 
B 1 560 VAL 560 560 560 VAL VAL B . n 
B 1 561 GLY 561 561 561 GLY GLY B . n 
B 1 562 LEU 562 562 562 LEU LEU B . n 
B 1 563 ASP 563 563 563 ASP ASP B . n 
B 1 564 ALA 564 564 564 ALA ALA B . n 
B 1 565 LEU 565 565 565 LEU LEU B . n 
B 1 566 ASP 566 566 566 ASP ASP B . n 
B 1 567 ALA 567 567 567 ALA ALA B . n 
B 1 568 GLN 568 568 568 GLN GLN B . n 
B 1 569 PRO 569 569 569 PRO PRO B . n 
B 1 570 LEU 570 570 570 LEU LEU B . n 
B 1 571 LEU 571 571 571 LEU LEU B . n 
B 1 572 LYS 572 572 572 LYS LYS B . n 
B 1 573 TYR 573 573 573 TYR TYR B . n 
B 1 574 PHE 574 574 574 PHE PHE B . n 
B 1 575 GLN 575 575 575 GLN GLN B . n 
B 1 576 LEU 576 576 576 LEU LEU B . n 
B 1 577 VAL 577 577 577 VAL VAL B . n 
B 1 578 THR 578 578 578 THR THR B . n 
B 1 579 GLN 579 579 579 GLN GLN B . n 
B 1 580 TRP 580 580 580 TRP TRP B . n 
B 1 581 LEU 581 581 581 LEU LEU B . n 
B 1 582 GLN 582 582 582 GLN GLN B . n 
B 1 583 GLU 583 583 583 GLU GLU B . n 
B 1 584 GLN 584 584 584 GLN GLN B . n 
B 1 585 ASN 585 585 585 ASN ASN B . n 
B 1 586 GLN 586 586 586 GLN GLN B . n 
B 1 587 GLN 587 587 587 GLN GLN B . n 
B 1 588 ASN 588 588 588 ASN ASN B . n 
B 1 589 GLY 589 589 589 GLY GLY B . n 
B 1 590 GLU 590 590 590 GLU GLU B . n 
B 1 591 VAL 591 591 591 VAL VAL B . n 
B 1 592 LEU 592 592 592 LEU LEU B . n 
B 1 593 GLY 593 593 593 GLY GLY B . n 
B 1 594 TRP 594 594 594 TRP TRP B . n 
B 1 595 PRO 595 595 595 PRO PRO B . n 
B 1 596 GLU 596 596 596 GLU GLU B . n 
B 1 597 TYR 597 597 597 TYR TYR B . n 
B 1 598 GLN 598 598 598 GLN GLN B . n 
B 1 599 TRP 599 599 599 TRP TRP B . n 
B 1 600 HIS 600 600 600 HIS HIS B . n 
B 1 601 PRO 601 601 601 PRO PRO B . n 
B 1 602 PRO 602 602 602 PRO PRO B . n 
B 1 603 LEU 603 603 603 LEU LEU B . n 
B 1 604 PRO 604 604 604 PRO PRO B . n 
B 1 605 ASP 605 605 605 ASP ASP B . n 
B 1 606 ASN 606 606 606 ASN ASN B . n 
B 1 607 TYR 607 607 607 TYR TYR B . n 
B 1 608 PRO 608 608 608 PRO PRO B . n 
B 1 609 GLU 609 609 609 GLU GLU B . n 
B 1 610 GLY 610 610 ?   ?   ?   B . n 
B 1 611 ILE 611 611 ?   ?   ?   B . n 
B 1 612 ASP 612 612 ?   ?   ?   B . n 
B 1 613 LEU 613 613 ?   ?   ?   B . n 
B 1 614 VAL 614 614 ?   ?   ?   B . n 
B 1 615 THR 615 615 ?   ?   ?   B . n 
B 1 616 ASP 616 616 ?   ?   ?   B . n 
B 1 617 GLU 617 617 ?   ?   ?   B . n 
B 1 618 ALA 618 618 ?   ?   ?   B . n 
B 1 619 GLU 619 619 ?   ?   ?   B . n 
B 1 620 ALA 620 620 ?   ?   ?   B . n 
B 1 621 SER 621 621 ?   ?   ?   B . n 
B 1 622 LYS 622 622 ?   ?   ?   B . n 
B 1 623 PHE 623 623 ?   ?   ?   B . n 
B 1 624 VAL 624 624 ?   ?   ?   B . n 
B 1 625 GLU 625 625 ?   ?   ?   B . n 
B 1 626 GLU 626 626 ?   ?   ?   B . n 
B 1 627 TYR 627 627 ?   ?   ?   B . n 
B 1 628 ASP 628 628 ?   ?   ?   B . 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 
C 2 NAG 1 C NAG 1 B NAG 701 n 
C 2 NAG 2 C NAG 2 B NAG 702 n 
D 3 NAG 1 D NAG 1 B NAG 708 n 
D 3 FUC 2 D FUC 2 B FUC 709 n 
E 4 NAG 1 E NAG 1 C NAG 1   n 
E 4 NAG 2 E NAG 2 C NAG 2   n 
E 4 BMA 3 E BMA 3 C BMA 3   n 
E 4 FUC 4 E FUC 4 C FUC 4   n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IJX 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IJX 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
F 5  NAG   1   701  701  NAG   NAG A . 
G 5  NAG   1   702  704  NAG   NAG A . 
H 6  ZN    1   703  707  ZN    ZN  A . 
I 7  CL    1   704  708  CL    CL  A . 
J 8  A1IJX 1   705  707  A1IJX SG7 A . 
K 9  PGE   1   701  703  PGE   PGE B . 
L 10 P33   1   702  704  P33   P33 B . 
M 11 PG4   1   703  706  PG4   PG4 B . 
N 6  ZN    1   704  707  ZN    ZN  B . 
O 7  CL    1   705  710  CL    CL  B . 
P 8  A1IJX 1   706  1106 A1IJX SG7 B . 
Q 12 HOH   1   801  801  HOH   HOH A . 
Q 12 HOH   2   802  802  HOH   HOH A . 
Q 12 HOH   3   803  803  HOH   HOH A . 
Q 12 HOH   4   804  807  HOH   HOH A . 
Q 12 HOH   5   805  806  HOH   HOH A . 
Q 12 HOH   6   806  804  HOH   HOH A . 
Q 12 HOH   7   807  818  HOH   HOH A . 
Q 12 HOH   8   808  808  HOH   HOH A . 
Q 12 HOH   9   809  805  HOH   HOH A . 
Q 12 HOH   10  810  810  HOH   HOH A . 
Q 12 HOH   11  811  811  HOH   HOH A . 
Q 12 HOH   12  812  828  HOH   HOH A . 
Q 12 HOH   13  813  823  HOH   HOH A . 
Q 12 HOH   14  814  819  HOH   HOH A . 
Q 12 HOH   15  815  809  HOH   HOH A . 
Q 12 HOH   16  816  815  HOH   HOH A . 
Q 12 HOH   17  817  812  HOH   HOH A . 
Q 12 HOH   18  818  814  HOH   HOH A . 
Q 12 HOH   19  819  816  HOH   HOH A . 
Q 12 HOH   20  820  813  HOH   HOH A . 
Q 12 HOH   21  821  817  HOH   HOH A . 
Q 12 HOH   22  822  826  HOH   HOH A . 
Q 12 HOH   23  823  827  HOH   HOH A . 
Q 12 HOH   24  824  822  HOH   HOH A . 
Q 12 HOH   25  825  829  HOH   HOH A . 
Q 12 HOH   26  826  830  HOH   HOH A . 
Q 12 HOH   27  827  842  HOH   HOH A . 
Q 12 HOH   28  828  820  HOH   HOH A . 
Q 12 HOH   29  829  824  HOH   HOH A . 
Q 12 HOH   30  830  831  HOH   HOH A . 
Q 12 HOH   31  831  825  HOH   HOH A . 
Q 12 HOH   32  832  851  HOH   HOH A . 
Q 12 HOH   33  833  840  HOH   HOH A . 
Q 12 HOH   34  834  850  HOH   HOH A . 
Q 12 HOH   35  835  847  HOH   HOH A . 
Q 12 HOH   36  836  833  HOH   HOH A . 
Q 12 HOH   37  837  848  HOH   HOH A . 
Q 12 HOH   38  838  837  HOH   HOH A . 
Q 12 HOH   39  839  841  HOH   HOH A . 
Q 12 HOH   40  840  843  HOH   HOH A . 
Q 12 HOH   41  841  832  HOH   HOH A . 
Q 12 HOH   42  842  839  HOH   HOH A . 
Q 12 HOH   43  843  845  HOH   HOH A . 
Q 12 HOH   44  844  835  HOH   HOH A . 
Q 12 HOH   45  845  854  HOH   HOH A . 
Q 12 HOH   46  846  834  HOH   HOH A . 
Q 12 HOH   47  847  846  HOH   HOH A . 
Q 12 HOH   48  848  838  HOH   HOH A . 
Q 12 HOH   49  849  867  HOH   HOH A . 
Q 12 HOH   50  850  858  HOH   HOH A . 
Q 12 HOH   51  851  844  HOH   HOH A . 
Q 12 HOH   52  852  861  HOH   HOH A . 
Q 12 HOH   53  853  863  HOH   HOH A . 
Q 12 HOH   54  854  886  HOH   HOH A . 
Q 12 HOH   55  855  872  HOH   HOH A . 
Q 12 HOH   56  856  868  HOH   HOH A . 
Q 12 HOH   57  857  865  HOH   HOH A . 
Q 12 HOH   58  858  857  HOH   HOH A . 
Q 12 HOH   59  859  882  HOH   HOH A . 
Q 12 HOH   60  860  870  HOH   HOH A . 
Q 12 HOH   61  861  875  HOH   HOH A . 
Q 12 HOH   62  862  864  HOH   HOH A . 
Q 12 HOH   63  863  836  HOH   HOH A . 
Q 12 HOH   64  864  855  HOH   HOH A . 
Q 12 HOH   65  865  862  HOH   HOH A . 
Q 12 HOH   66  866  849  HOH   HOH A . 
Q 12 HOH   67  867  885  HOH   HOH A . 
Q 12 HOH   68  868  866  HOH   HOH A . 
Q 12 HOH   69  869  853  HOH   HOH A . 
Q 12 HOH   70  870  892  HOH   HOH A . 
Q 12 HOH   71  871  821  HOH   HOH A . 
Q 12 HOH   72  872  887  HOH   HOH A . 
Q 12 HOH   73  873  881  HOH   HOH A . 
Q 12 HOH   74  874  852  HOH   HOH A . 
Q 12 HOH   75  875  869  HOH   HOH A . 
Q 12 HOH   76  876  873  HOH   HOH A . 
Q 12 HOH   77  877  860  HOH   HOH A . 
Q 12 HOH   78  878  894  HOH   HOH A . 
Q 12 HOH   79  879  871  HOH   HOH A . 
Q 12 HOH   80  880  889  HOH   HOH A . 
Q 12 HOH   81  881  901  HOH   HOH A . 
Q 12 HOH   82  882  859  HOH   HOH A . 
Q 12 HOH   83  883  895  HOH   HOH A . 
Q 12 HOH   84  884  899  HOH   HOH A . 
Q 12 HOH   85  885  879  HOH   HOH A . 
Q 12 HOH   86  886  893  HOH   HOH A . 
Q 12 HOH   87  887  878  HOH   HOH A . 
Q 12 HOH   88  888  880  HOH   HOH A . 
Q 12 HOH   89  889  923  HOH   HOH A . 
Q 12 HOH   90  890  856  HOH   HOH A . 
Q 12 HOH   91  891  883  HOH   HOH A . 
Q 12 HOH   92  892  890  HOH   HOH A . 
Q 12 HOH   93  893  905  HOH   HOH A . 
Q 12 HOH   94  894  948  HOH   HOH A . 
Q 12 HOH   95  895  903  HOH   HOH A . 
Q 12 HOH   96  896  904  HOH   HOH A . 
Q 12 HOH   97  897  918  HOH   HOH A . 
Q 12 HOH   98  898  877  HOH   HOH A . 
Q 12 HOH   99  899  874  HOH   HOH A . 
Q 12 HOH   100 900  913  HOH   HOH A . 
Q 12 HOH   101 901  915  HOH   HOH A . 
Q 12 HOH   102 902  924  HOH   HOH A . 
Q 12 HOH   103 903  916  HOH   HOH A . 
Q 12 HOH   104 904  909  HOH   HOH A . 
Q 12 HOH   105 905  911  HOH   HOH A . 
Q 12 HOH   106 906  876  HOH   HOH A . 
Q 12 HOH   107 907  908  HOH   HOH A . 
Q 12 HOH   108 908  931  HOH   HOH A . 
Q 12 HOH   109 909  898  HOH   HOH A . 
Q 12 HOH   110 910  902  HOH   HOH A . 
Q 12 HOH   111 911  896  HOH   HOH A . 
Q 12 HOH   112 912  891  HOH   HOH A . 
Q 12 HOH   113 913  910  HOH   HOH A . 
Q 12 HOH   114 914  934  HOH   HOH A . 
Q 12 HOH   115 915  919  HOH   HOH A . 
Q 12 HOH   116 916  900  HOH   HOH A . 
Q 12 HOH   117 917  935  HOH   HOH A . 
Q 12 HOH   118 918  912  HOH   HOH A . 
Q 12 HOH   119 919  921  HOH   HOH A . 
Q 12 HOH   120 920  926  HOH   HOH A . 
Q 12 HOH   121 921  951  HOH   HOH A . 
Q 12 HOH   122 922  927  HOH   HOH A . 
Q 12 HOH   123 923  942  HOH   HOH A . 
Q 12 HOH   124 924  897  HOH   HOH A . 
Q 12 HOH   125 925  954  HOH   HOH A . 
Q 12 HOH   126 926  917  HOH   HOH A . 
Q 12 HOH   127 927  884  HOH   HOH A . 
Q 12 HOH   128 928  936  HOH   HOH A . 
Q 12 HOH   129 929  956  HOH   HOH A . 
Q 12 HOH   130 930  922  HOH   HOH A . 
Q 12 HOH   131 931  907  HOH   HOH A . 
Q 12 HOH   132 932  957  HOH   HOH A . 
Q 12 HOH   133 933  928  HOH   HOH A . 
Q 12 HOH   134 934  947  HOH   HOH A . 
Q 12 HOH   135 935  943  HOH   HOH A . 
Q 12 HOH   136 936  929  HOH   HOH A . 
Q 12 HOH   137 937  973  HOH   HOH A . 
Q 12 HOH   138 938  930  HOH   HOH A . 
Q 12 HOH   139 939  963  HOH   HOH A . 
Q 12 HOH   140 940  888  HOH   HOH A . 
Q 12 HOH   141 941  914  HOH   HOH A . 
Q 12 HOH   142 942  939  HOH   HOH A . 
Q 12 HOH   143 943  937  HOH   HOH A . 
Q 12 HOH   144 944  925  HOH   HOH A . 
Q 12 HOH   145 945  933  HOH   HOH A . 
Q 12 HOH   146 946  946  HOH   HOH A . 
Q 12 HOH   147 947  952  HOH   HOH A . 
Q 12 HOH   148 948  953  HOH   HOH A . 
Q 12 HOH   149 949  962  HOH   HOH A . 
Q 12 HOH   150 950  969  HOH   HOH A . 
Q 12 HOH   151 951  950  HOH   HOH A . 
Q 12 HOH   152 952  958  HOH   HOH A . 
Q 12 HOH   153 953  960  HOH   HOH A . 
Q 12 HOH   154 954  959  HOH   HOH A . 
Q 12 HOH   155 955  979  HOH   HOH A . 
Q 12 HOH   156 956  966  HOH   HOH A . 
Q 12 HOH   157 957  941  HOH   HOH A . 
Q 12 HOH   158 958  944  HOH   HOH A . 
Q 12 HOH   159 959  932  HOH   HOH A . 
Q 12 HOH   160 960  967  HOH   HOH A . 
Q 12 HOH   161 961  970  HOH   HOH A . 
Q 12 HOH   162 962  984  HOH   HOH A . 
Q 12 HOH   163 963  971  HOH   HOH A . 
Q 12 HOH   164 964  949  HOH   HOH A . 
Q 12 HOH   165 965  945  HOH   HOH A . 
Q 12 HOH   166 966  940  HOH   HOH A . 
Q 12 HOH   167 967  955  HOH   HOH A . 
Q 12 HOH   168 968  976  HOH   HOH A . 
Q 12 HOH   169 969  972  HOH   HOH A . 
Q 12 HOH   170 970  964  HOH   HOH A . 
Q 12 HOH   171 971  961  HOH   HOH A . 
Q 12 HOH   172 972  968  HOH   HOH A . 
Q 12 HOH   173 973  974  HOH   HOH A . 
Q 12 HOH   174 974  995  HOH   HOH A . 
Q 12 HOH   175 975  994  HOH   HOH A . 
Q 12 HOH   176 976  991  HOH   HOH A . 
Q 12 HOH   177 977  1005 HOH   HOH A . 
Q 12 HOH   178 978  906  HOH   HOH A . 
Q 12 HOH   179 979  975  HOH   HOH A . 
Q 12 HOH   180 980  920  HOH   HOH A . 
Q 12 HOH   181 981  938  HOH   HOH A . 
Q 12 HOH   182 982  980  HOH   HOH A . 
Q 12 HOH   183 983  977  HOH   HOH A . 
Q 12 HOH   184 984  1002 HOH   HOH A . 
Q 12 HOH   185 985  992  HOH   HOH A . 
Q 12 HOH   186 986  1003 HOH   HOH A . 
Q 12 HOH   187 987  986  HOH   HOH A . 
Q 12 HOH   188 988  989  HOH   HOH A . 
Q 12 HOH   189 989  1001 HOH   HOH A . 
Q 12 HOH   190 990  965  HOH   HOH A . 
Q 12 HOH   191 991  982  HOH   HOH A . 
Q 12 HOH   192 992  998  HOH   HOH A . 
Q 12 HOH   193 993  1000 HOH   HOH A . 
Q 12 HOH   194 994  978  HOH   HOH A . 
Q 12 HOH   195 995  996  HOH   HOH A . 
Q 12 HOH   196 996  988  HOH   HOH A . 
Q 12 HOH   197 997  987  HOH   HOH A . 
Q 12 HOH   198 998  999  HOH   HOH A . 
Q 12 HOH   199 999  1009 HOH   HOH A . 
Q 12 HOH   200 1000 990  HOH   HOH A . 
Q 12 HOH   201 1001 1023 HOH   HOH A . 
Q 12 HOH   202 1002 997  HOH   HOH A . 
Q 12 HOH   203 1003 1010 HOH   HOH A . 
Q 12 HOH   204 1004 985  HOH   HOH A . 
Q 12 HOH   205 1005 1012 HOH   HOH A . 
Q 12 HOH   206 1006 1014 HOH   HOH A . 
Q 12 HOH   207 1007 1007 HOH   HOH A . 
Q 12 HOH   208 1008 1004 HOH   HOH A . 
Q 12 HOH   209 1009 1016 HOH   HOH A . 
Q 12 HOH   210 1010 1049 HOH   HOH A . 
Q 12 HOH   211 1011 1027 HOH   HOH A . 
Q 12 HOH   212 1012 1019 HOH   HOH A . 
Q 12 HOH   213 1013 1022 HOH   HOH A . 
Q 12 HOH   214 1014 1017 HOH   HOH A . 
Q 12 HOH   215 1015 981  HOH   HOH A . 
Q 12 HOH   216 1016 1013 HOH   HOH A . 
Q 12 HOH   217 1017 1043 HOH   HOH A . 
Q 12 HOH   218 1018 1030 HOH   HOH A . 
Q 12 HOH   219 1019 1008 HOH   HOH A . 
Q 12 HOH   220 1020 993  HOH   HOH A . 
Q 12 HOH   221 1021 1039 HOH   HOH A . 
Q 12 HOH   222 1022 1018 HOH   HOH A . 
Q 12 HOH   223 1023 1021 HOH   HOH A . 
Q 12 HOH   224 1024 1011 HOH   HOH A . 
Q 12 HOH   225 1025 1020 HOH   HOH A . 
Q 12 HOH   226 1026 1044 HOH   HOH A . 
Q 12 HOH   227 1027 983  HOH   HOH A . 
Q 12 HOH   228 1028 1031 HOH   HOH A . 
Q 12 HOH   229 1029 1033 HOH   HOH A . 
Q 12 HOH   230 1030 1041 HOH   HOH A . 
Q 12 HOH   231 1031 1024 HOH   HOH A . 
Q 12 HOH   232 1032 1028 HOH   HOH A . 
Q 12 HOH   233 1033 1048 HOH   HOH A . 
Q 12 HOH   234 1034 1032 HOH   HOH A . 
Q 12 HOH   235 1035 1025 HOH   HOH A . 
Q 12 HOH   236 1036 1015 HOH   HOH A . 
Q 12 HOH   237 1037 1006 HOH   HOH A . 
Q 12 HOH   238 1038 1035 HOH   HOH A . 
Q 12 HOH   239 1039 1029 HOH   HOH A . 
Q 12 HOH   240 1040 1053 HOH   HOH A . 
Q 12 HOH   241 1041 1026 HOH   HOH A . 
Q 12 HOH   242 1042 1034 HOH   HOH A . 
Q 12 HOH   243 1043 1056 HOH   HOH A . 
Q 12 HOH   244 1044 1050 HOH   HOH A . 
Q 12 HOH   245 1045 1038 HOH   HOH A . 
Q 12 HOH   246 1046 1036 HOH   HOH A . 
Q 12 HOH   247 1047 1067 HOH   HOH A . 
Q 12 HOH   248 1048 1054 HOH   HOH A . 
Q 12 HOH   249 1049 1047 HOH   HOH A . 
Q 12 HOH   250 1050 1037 HOH   HOH A . 
Q 12 HOH   251 1051 1060 HOH   HOH A . 
Q 12 HOH   252 1052 1042 HOH   HOH A . 
Q 12 HOH   253 1053 1057 HOH   HOH A . 
Q 12 HOH   254 1054 1059 HOH   HOH A . 
Q 12 HOH   255 1055 1070 HOH   HOH A . 
Q 12 HOH   256 1056 1058 HOH   HOH A . 
Q 12 HOH   257 1057 1055 HOH   HOH A . 
Q 12 HOH   258 1058 1051 HOH   HOH A . 
Q 12 HOH   259 1059 1069 HOH   HOH A . 
Q 12 HOH   260 1060 1046 HOH   HOH A . 
Q 12 HOH   261 1061 1079 HOH   HOH A . 
Q 12 HOH   262 1062 1040 HOH   HOH A . 
Q 12 HOH   263 1063 1073 HOH   HOH A . 
Q 12 HOH   264 1064 1052 HOH   HOH A . 
Q 12 HOH   265 1065 1061 HOH   HOH A . 
Q 12 HOH   266 1066 1085 HOH   HOH A . 
Q 12 HOH   267 1067 1063 HOH   HOH A . 
Q 12 HOH   268 1068 1064 HOH   HOH A . 
Q 12 HOH   269 1069 1075 HOH   HOH A . 
Q 12 HOH   270 1070 1074 HOH   HOH A . 
Q 12 HOH   271 1071 1045 HOH   HOH A . 
Q 12 HOH   272 1072 1066 HOH   HOH A . 
Q 12 HOH   273 1073 1062 HOH   HOH A . 
Q 12 HOH   274 1074 1086 HOH   HOH A . 
Q 12 HOH   275 1075 1072 HOH   HOH A . 
Q 12 HOH   276 1076 1078 HOH   HOH A . 
Q 12 HOH   277 1077 1077 HOH   HOH A . 
Q 12 HOH   278 1078 1065 HOH   HOH A . 
Q 12 HOH   279 1079 1068 HOH   HOH A . 
Q 12 HOH   280 1080 1084 HOH   HOH A . 
Q 12 HOH   281 1081 1076 HOH   HOH A . 
Q 12 HOH   282 1082 1071 HOH   HOH A . 
Q 12 HOH   283 1083 1082 HOH   HOH A . 
Q 12 HOH   284 1084 1083 HOH   HOH A . 
Q 12 HOH   285 1085 1087 HOH   HOH A . 
Q 12 HOH   286 1086 1091 HOH   HOH A . 
Q 12 HOH   287 1087 1080 HOH   HOH A . 
Q 12 HOH   288 1088 1089 HOH   HOH A . 
Q 12 HOH   289 1089 1088 HOH   HOH A . 
Q 12 HOH   290 1090 1090 HOH   HOH A . 
Q 12 HOH   291 1091 1099 HOH   HOH A . 
Q 12 HOH   292 1092 1097 HOH   HOH A . 
Q 12 HOH   293 1093 1093 HOH   HOH A . 
Q 12 HOH   294 1094 1092 HOH   HOH A . 
Q 12 HOH   295 1095 1095 HOH   HOH A . 
Q 12 HOH   296 1096 1096 HOH   HOH A . 
Q 12 HOH   297 1097 1098 HOH   HOH A . 
Q 12 HOH   298 1098 1101 HOH   HOH A . 
Q 12 HOH   299 1099 1102 HOH   HOH A . 
Q 12 HOH   300 1100 1094 HOH   HOH A . 
Q 12 HOH   301 1101 1081 HOH   HOH A . 
Q 12 HOH   302 1102 1100 HOH   HOH A . 
Q 12 HOH   303 1103 1104 HOH   HOH A . 
Q 12 HOH   304 1104 1106 HOH   HOH A . 
Q 12 HOH   305 1105 1105 HOH   HOH A . 
Q 12 HOH   306 1106 1107 HOH   HOH A . 
Q 12 HOH   307 1107 1108 HOH   HOH A . 
Q 12 HOH   308 1108 1109 HOH   HOH A . 
Q 12 HOH   309 1109 1114 HOH   HOH A . 
Q 12 HOH   310 1110 1111 HOH   HOH A . 
Q 12 HOH   311 1111 1120 HOH   HOH A . 
Q 12 HOH   312 1112 1116 HOH   HOH A . 
Q 12 HOH   313 1113 1117 HOH   HOH A . 
Q 12 HOH   314 1114 1110 HOH   HOH A . 
Q 12 HOH   315 1115 1115 HOH   HOH A . 
Q 12 HOH   316 1116 1113 HOH   HOH A . 
Q 12 HOH   317 1117 1112 HOH   HOH A . 
Q 12 HOH   318 1118 1119 HOH   HOH A . 
Q 12 HOH   319 1119 1118 HOH   HOH A . 
Q 12 HOH   320 1120 1123 HOH   HOH A . 
Q 12 HOH   321 1121 1122 HOH   HOH A . 
Q 12 HOH   322 1122 1121 HOH   HOH A . 
Q 12 HOH   323 1123 1127 HOH   HOH A . 
Q 12 HOH   324 1124 1128 HOH   HOH A . 
Q 12 HOH   325 1125 1125 HOH   HOH A . 
Q 12 HOH   326 1126 1126 HOH   HOH A . 
Q 12 HOH   327 1127 1129 HOH   HOH A . 
Q 12 HOH   328 1128 1133 HOH   HOH A . 
Q 12 HOH   329 1129 1124 HOH   HOH A . 
Q 12 HOH   330 1130 1135 HOH   HOH A . 
Q 12 HOH   331 1131 1130 HOH   HOH A . 
Q 12 HOH   332 1132 1134 HOH   HOH A . 
Q 12 HOH   333 1133 1132 HOH   HOH A . 
Q 12 HOH   334 1134 1131 HOH   HOH A . 
Q 12 HOH   335 1135 1136 HOH   HOH A . 
Q 12 HOH   336 1136 1137 HOH   HOH A . 
Q 12 HOH   337 1137 1140 HOH   HOH A . 
Q 12 HOH   338 1138 1138 HOH   HOH A . 
Q 12 HOH   339 1139 1144 HOH   HOH A . 
Q 12 HOH   340 1140 1141 HOH   HOH A . 
Q 12 HOH   341 1141 1143 HOH   HOH A . 
Q 12 HOH   342 1142 1142 HOH   HOH A . 
Q 12 HOH   343 1143 1139 HOH   HOH A . 
Q 12 HOH   344 1144 1146 HOH   HOH A . 
Q 12 HOH   345 1145 1147 HOH   HOH A . 
Q 12 HOH   346 1146 1148 HOH   HOH A . 
Q 12 HOH   347 1147 1151 HOH   HOH A . 
Q 12 HOH   348 1148 1145 HOH   HOH A . 
Q 12 HOH   349 1149 1150 HOH   HOH A . 
Q 12 HOH   350 1150 1156 HOH   HOH A . 
Q 12 HOH   351 1151 1149 HOH   HOH A . 
Q 12 HOH   352 1152 1153 HOH   HOH A . 
Q 12 HOH   353 1153 1152 HOH   HOH A . 
Q 12 HOH   354 1154 1155 HOH   HOH A . 
Q 12 HOH   355 1155 1154 HOH   HOH A . 
Q 12 HOH   356 1156 1157 HOH   HOH A . 
Q 12 HOH   357 1157 1159 HOH   HOH A . 
Q 12 HOH   358 1158 1158 HOH   HOH A . 
Q 12 HOH   359 1159 1160 HOH   HOH A . 
Q 12 HOH   360 1160 1161 HOH   HOH A . 
R 12 HOH   1   801  851  HOH   HOH B . 
R 12 HOH   2   802  802  HOH   HOH B . 
R 12 HOH   3   803  804  HOH   HOH B . 
R 12 HOH   4   804  808  HOH   HOH B . 
R 12 HOH   5   805  909  HOH   HOH B . 
R 12 HOH   6   806  801  HOH   HOH B . 
R 12 HOH   7   807  806  HOH   HOH B . 
R 12 HOH   8   808  807  HOH   HOH B . 
R 12 HOH   9   809  805  HOH   HOH B . 
R 12 HOH   10  810  809  HOH   HOH B . 
R 12 HOH   11  811  803  HOH   HOH B . 
R 12 HOH   12  812  816  HOH   HOH B . 
R 12 HOH   13  813  828  HOH   HOH B . 
R 12 HOH   14  814  810  HOH   HOH B . 
R 12 HOH   15  815  821  HOH   HOH B . 
R 12 HOH   16  816  811  HOH   HOH B . 
R 12 HOH   17  817  817  HOH   HOH B . 
R 12 HOH   18  818  822  HOH   HOH B . 
R 12 HOH   19  819  818  HOH   HOH B . 
R 12 HOH   20  820  823  HOH   HOH B . 
R 12 HOH   21  821  833  HOH   HOH B . 
R 12 HOH   22  822  844  HOH   HOH B . 
R 12 HOH   23  823  819  HOH   HOH B . 
R 12 HOH   24  824  829  HOH   HOH B . 
R 12 HOH   25  825  820  HOH   HOH B . 
R 12 HOH   26  826  835  HOH   HOH B . 
R 12 HOH   27  827  850  HOH   HOH B . 
R 12 HOH   28  828  825  HOH   HOH B . 
R 12 HOH   29  829  827  HOH   HOH B . 
R 12 HOH   30  830  837  HOH   HOH B . 
R 12 HOH   31  831  830  HOH   HOH B . 
R 12 HOH   32  832  831  HOH   HOH B . 
R 12 HOH   33  833  843  HOH   HOH B . 
R 12 HOH   34  834  836  HOH   HOH B . 
R 12 HOH   35  835  812  HOH   HOH B . 
R 12 HOH   36  836  867  HOH   HOH B . 
R 12 HOH   37  837  862  HOH   HOH B . 
R 12 HOH   38  838  841  HOH   HOH B . 
R 12 HOH   39  839  813  HOH   HOH B . 
R 12 HOH   40  840  899  HOH   HOH B . 
R 12 HOH   41  841  839  HOH   HOH B . 
R 12 HOH   42  842  824  HOH   HOH B . 
R 12 HOH   43  843  842  HOH   HOH B . 
R 12 HOH   44  844  859  HOH   HOH B . 
R 12 HOH   45  845  840  HOH   HOH B . 
R 12 HOH   46  846  838  HOH   HOH B . 
R 12 HOH   47  847  814  HOH   HOH B . 
R 12 HOH   48  848  826  HOH   HOH B . 
R 12 HOH   49  849  852  HOH   HOH B . 
R 12 HOH   50  850  815  HOH   HOH B . 
R 12 HOH   51  851  834  HOH   HOH B . 
R 12 HOH   52  852  854  HOH   HOH B . 
R 12 HOH   53  853  873  HOH   HOH B . 
R 12 HOH   54  854  853  HOH   HOH B . 
R 12 HOH   55  855  846  HOH   HOH B . 
R 12 HOH   56  856  861  HOH   HOH B . 
R 12 HOH   57  857  847  HOH   HOH B . 
R 12 HOH   58  858  860  HOH   HOH B . 
R 12 HOH   59  859  832  HOH   HOH B . 
R 12 HOH   60  860  876  HOH   HOH B . 
R 12 HOH   61  861  858  HOH   HOH B . 
R 12 HOH   62  862  871  HOH   HOH B . 
R 12 HOH   63  863  848  HOH   HOH B . 
R 12 HOH   64  864  863  HOH   HOH B . 
R 12 HOH   65  865  845  HOH   HOH B . 
R 12 HOH   66  866  856  HOH   HOH B . 
R 12 HOH   67  867  868  HOH   HOH B . 
R 12 HOH   68  868  874  HOH   HOH B . 
R 12 HOH   69  869  866  HOH   HOH B . 
R 12 HOH   70  870  913  HOH   HOH B . 
R 12 HOH   71  871  865  HOH   HOH B . 
R 12 HOH   72  872  869  HOH   HOH B . 
R 12 HOH   73  873  898  HOH   HOH B . 
R 12 HOH   74  874  870  HOH   HOH B . 
R 12 HOH   75  875  883  HOH   HOH B . 
R 12 HOH   76  876  880  HOH   HOH B . 
R 12 HOH   77  877  878  HOH   HOH B . 
R 12 HOH   78  878  872  HOH   HOH B . 
R 12 HOH   79  879  882  HOH   HOH B . 
R 12 HOH   80  880  857  HOH   HOH B . 
R 12 HOH   81  881  864  HOH   HOH B . 
R 12 HOH   82  882  919  HOH   HOH B . 
R 12 HOH   83  883  879  HOH   HOH B . 
R 12 HOH   84  884  887  HOH   HOH B . 
R 12 HOH   85  885  894  HOH   HOH B . 
R 12 HOH   86  886  906  HOH   HOH B . 
R 12 HOH   87  887  961  HOH   HOH B . 
R 12 HOH   88  888  881  HOH   HOH B . 
R 12 HOH   89  889  888  HOH   HOH B . 
R 12 HOH   90  890  855  HOH   HOH B . 
R 12 HOH   91  891  893  HOH   HOH B . 
R 12 HOH   92  892  896  HOH   HOH B . 
R 12 HOH   93  893  891  HOH   HOH B . 
R 12 HOH   94  894  905  HOH   HOH B . 
R 12 HOH   95  895  929  HOH   HOH B . 
R 12 HOH   96  896  925  HOH   HOH B . 
R 12 HOH   97  897  980  HOH   HOH B . 
R 12 HOH   98  898  912  HOH   HOH B . 
R 12 HOH   99  899  849  HOH   HOH B . 
R 12 HOH   100 900  900  HOH   HOH B . 
R 12 HOH   101 901  922  HOH   HOH B . 
R 12 HOH   102 902  902  HOH   HOH B . 
R 12 HOH   103 903  892  HOH   HOH B . 
R 12 HOH   104 904  884  HOH   HOH B . 
R 12 HOH   105 905  901  HOH   HOH B . 
R 12 HOH   106 906  897  HOH   HOH B . 
R 12 HOH   107 907  895  HOH   HOH B . 
R 12 HOH   108 908  886  HOH   HOH B . 
R 12 HOH   109 909  903  HOH   HOH B . 
R 12 HOH   110 910  908  HOH   HOH B . 
R 12 HOH   111 911  910  HOH   HOH B . 
R 12 HOH   112 912  890  HOH   HOH B . 
R 12 HOH   113 913  933  HOH   HOH B . 
R 12 HOH   114 914  920  HOH   HOH B . 
R 12 HOH   115 915  916  HOH   HOH B . 
R 12 HOH   116 916  914  HOH   HOH B . 
R 12 HOH   117 917  928  HOH   HOH B . 
R 12 HOH   118 918  950  HOH   HOH B . 
R 12 HOH   119 919  877  HOH   HOH B . 
R 12 HOH   120 920  924  HOH   HOH B . 
R 12 HOH   121 921  911  HOH   HOH B . 
R 12 HOH   122 922  932  HOH   HOH B . 
R 12 HOH   123 923  926  HOH   HOH B . 
R 12 HOH   124 924  904  HOH   HOH B . 
R 12 HOH   125 925  907  HOH   HOH B . 
R 12 HOH   126 926  934  HOH   HOH B . 
R 12 HOH   127 927  918  HOH   HOH B . 
R 12 HOH   128 928  921  HOH   HOH B . 
R 12 HOH   129 929  923  HOH   HOH B . 
R 12 HOH   130 930  964  HOH   HOH B . 
R 12 HOH   131 931  930  HOH   HOH B . 
R 12 HOH   132 932  935  HOH   HOH B . 
R 12 HOH   133 933  955  HOH   HOH B . 
R 12 HOH   134 934  927  HOH   HOH B . 
R 12 HOH   135 935  940  HOH   HOH B . 
R 12 HOH   136 936  947  HOH   HOH B . 
R 12 HOH   137 937  889  HOH   HOH B . 
R 12 HOH   138 938  937  HOH   HOH B . 
R 12 HOH   139 939  956  HOH   HOH B . 
R 12 HOH   140 940  946  HOH   HOH B . 
R 12 HOH   141 941  936  HOH   HOH B . 
R 12 HOH   142 942  945  HOH   HOH B . 
R 12 HOH   143 943  953  HOH   HOH B . 
R 12 HOH   144 944  917  HOH   HOH B . 
R 12 HOH   145 945  959  HOH   HOH B . 
R 12 HOH   146 946  938  HOH   HOH B . 
R 12 HOH   147 947  943  HOH   HOH B . 
R 12 HOH   148 948  949  HOH   HOH B . 
R 12 HOH   149 949  941  HOH   HOH B . 
R 12 HOH   150 950  948  HOH   HOH B . 
R 12 HOH   151 951  944  HOH   HOH B . 
R 12 HOH   152 952  954  HOH   HOH B . 
R 12 HOH   153 953  931  HOH   HOH B . 
R 12 HOH   154 954  960  HOH   HOH B . 
R 12 HOH   155 955  963  HOH   HOH B . 
R 12 HOH   156 956  957  HOH   HOH B . 
R 12 HOH   157 957  973  HOH   HOH B . 
R 12 HOH   158 958  958  HOH   HOH B . 
R 12 HOH   159 959  915  HOH   HOH B . 
R 12 HOH   160 960  968  HOH   HOH B . 
R 12 HOH   161 961  965  HOH   HOH B . 
R 12 HOH   162 962  939  HOH   HOH B . 
R 12 HOH   163 963  974  HOH   HOH B . 
R 12 HOH   164 964  962  HOH   HOH B . 
R 12 HOH   165 965  952  HOH   HOH B . 
R 12 HOH   166 966  969  HOH   HOH B . 
R 12 HOH   167 967  966  HOH   HOH B . 
R 12 HOH   168 968  976  HOH   HOH B . 
R 12 HOH   169 969  972  HOH   HOH B . 
R 12 HOH   170 970  982  HOH   HOH B . 
R 12 HOH   171 971  970  HOH   HOH B . 
R 12 HOH   172 972  988  HOH   HOH B . 
R 12 HOH   173 973  971  HOH   HOH B . 
R 12 HOH   174 974  975  HOH   HOH B . 
R 12 HOH   175 975  875  HOH   HOH B . 
R 12 HOH   176 976  951  HOH   HOH B . 
R 12 HOH   177 977  977  HOH   HOH B . 
R 12 HOH   178 978  978  HOH   HOH B . 
R 12 HOH   179 979  981  HOH   HOH B . 
R 12 HOH   180 980  979  HOH   HOH B . 
R 12 HOH   181 981  967  HOH   HOH B . 
R 12 HOH   182 982  983  HOH   HOH B . 
R 12 HOH   183 983  984  HOH   HOH B . 
R 12 HOH   184 984  1000 HOH   HOH B . 
R 12 HOH   185 985  991  HOH   HOH B . 
R 12 HOH   186 986  985  HOH   HOH B . 
R 12 HOH   187 987  989  HOH   HOH B . 
R 12 HOH   188 988  998  HOH   HOH B . 
R 12 HOH   189 989  990  HOH   HOH B . 
R 12 HOH   190 990  987  HOH   HOH B . 
R 12 HOH   191 991  992  HOH   HOH B . 
R 12 HOH   192 992  993  HOH   HOH B . 
R 12 HOH   193 993  986  HOH   HOH B . 
R 12 HOH   194 994  997  HOH   HOH B . 
R 12 HOH   195 995  994  HOH   HOH B . 
R 12 HOH   196 996  995  HOH   HOH B . 
R 12 HOH   197 997  999  HOH   HOH B . 
R 12 HOH   198 998  996  HOH   HOH B . 
R 12 HOH   199 999  1003 HOH   HOH B . 
R 12 HOH   200 1000 1002 HOH   HOH B . 
R 12 HOH   201 1001 1001 HOH   HOH B . 
R 12 HOH   202 1002 1005 HOH   HOH B . 
R 12 HOH   203 1003 1103 HOH   HOH B . 
R 12 HOH   204 1004 1006 HOH   HOH B . 
R 12 HOH   205 1005 1004 HOH   HOH B . 
R 12 HOH   206 1006 1007 HOH   HOH B . 
R 12 HOH   207 1007 1008 HOH   HOH B . 
R 12 HOH   208 1008 1009 HOH   HOH B . 
R 12 HOH   209 1009 1011 HOH   HOH B . 
R 12 HOH   210 1010 1010 HOH   HOH B . 
R 12 HOH   211 1011 1012 HOH   HOH B . 
R 12 HOH   212 1012 1013 HOH   HOH B . 
R 12 HOH   213 1013 1014 HOH   HOH B . 
R 12 HOH   214 1014 1015 HOH   HOH B . 
R 12 HOH   215 1015 1020 HOH   HOH B . 
R 12 HOH   216 1016 1018 HOH   HOH B . 
R 12 HOH   217 1017 1019 HOH   HOH B . 
R 12 HOH   218 1018 1017 HOH   HOH B . 
R 12 HOH   219 1019 1022 HOH   HOH B . 
R 12 HOH   220 1020 1016 HOH   HOH B . 
R 12 HOH   221 1021 1021 HOH   HOH B . 
R 12 HOH   222 1022 1023 HOH   HOH B . 
R 12 HOH   223 1023 1025 HOH   HOH B . 
R 12 HOH   224 1024 1024 HOH   HOH B . 
R 12 HOH   225 1025 1026 HOH   HOH B . 
R 12 HOH   226 1026 1028 HOH   HOH B . 
R 12 HOH   227 1027 1027 HOH   HOH B . 
R 12 HOH   228 1028 1029 HOH   HOH B . 
R 12 HOH   229 1029 1030 HOH   HOH B . 
R 12 HOH   230 1030 885  HOH   HOH B . 
R 12 HOH   231 1031 942  HOH   HOH B . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS   ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  88.38 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   64.31 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  74.92 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GBR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     73.053 
_cell.length_a_esd                 ? 
_cell.length_b                     77.377 
_cell.length_b_esd                 ? 
_cell.length_c                     82.914 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         9GBR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 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                   9GBR 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.91 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.73 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_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    
;1 M Tris/Bicine pH8.5
60 mM divalent cations (MgCl2 and CaCl2)
30% PEG550 MME/PEG20K
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.15 
# 
_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 EIGER2 XE 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         2018-10-23 
_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   0.976 
_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                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GBR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.90 
_reflns.d_resolution_low                               74.365 
_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                                     1157631 
_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                           97.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.054 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_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                                    1.90 
_reflns_shell.d_res_low                                     1.93 
_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                             5928 
_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                               1.071 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.329 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.5 
_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]                            -0.147 
_refine.aniso_B[1][2]                            0.882 
_refine.aniso_B[1][3]                            0.253 
_refine.aniso_B[2][2]                            0.393 
_refine.aniso_B[2][3]                            -0.079 
_refine.aniso_B[3][3]                            0.310 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               32.980 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.958 
_refine.correlation_coeff_Fo_to_Fc_free          0.932 
_refine.details                                  'Hydrogens have not been used' 
_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                                 9GBR 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.900 
_refine.ls_d_res_low                             74.365 
_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                     121230 
_refine.ls_number_reflns_R_free                  5952 
_refine.ls_number_reflns_R_work                  115278 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.821 
_refine.ls_percent_reflns_R_free                 4.910 
_refine.ls_R_factor_all                          0.189 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2253 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1875 
_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                    'MASK BULK SOLVENT' 
_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                          ? 
_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       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.141 
_refine.pdbx_overall_ESU_R_Free                  0.134 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_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                 ? 
_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                             7.994 
_refine.overall_SU_ML                            0.104 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.900 
_refine_hist.d_res_low                        74.365 
_refine_hist.number_atoms_solvent             591 
_refine_hist.number_atoms_total               10694 
_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        9863 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         240 
_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' ? 0.012  0.012  10524 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 2.263  1.831  14349 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.600  5.000  1224  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 8.211  5.000  67    ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 15.115 10.000 1619  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 14.751 10.000 534   ? r_dihedral_angle_6_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.149  0.200  1495  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.020  8423  ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.222  0.200  4978  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.318  0.200  7264  ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.166  0.200  669   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.231  0.200  37    ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.167  0.200  6     ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 1.776  1.494  4875  ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 2.648  2.676  6106  ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 3.045  1.866  5649  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 4.612  3.268  8243  ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 5.927  16.795 16522 ? r_lrange_it                    ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.900 1.949  9166 . 427 8414 96.4543 . 0.275 . . 0.273 . . . . . 0.267 . 20 . 0.956 0.942 0.308 
'X-RAY DIFFRACTION' 1.949 2.003  8889 . 424 8168 96.6588 . 0.247 . . 0.246 . . . . . 0.237 . 20 . 0.962 0.949 0.275 
'X-RAY DIFFRACTION' 2.003 2.061  8709 . 405 8026 96.8079 . 0.233 . . 0.231 . . . . . 0.220 . 20 . 0.966 0.955 0.266 
'X-RAY DIFFRACTION' 2.061 2.124  8474 . 395 7823 96.9790 . 0.226 . . 0.224 . . . . . 0.213 . 20 . 0.967 0.956 0.264 
'X-RAY DIFFRACTION' 2.124 2.194  8181 . 396 7551 97.1397 . 0.213 . . 0.211 . . . . . 0.199 . 20 . 0.971 0.958 0.255 
'X-RAY DIFFRACTION' 2.194 2.271  7878 . 379 7293 97.3851 . 0.214 . . 0.212 . . . . . 0.200 . 20 . 0.972 0.958 0.255 
'X-RAY DIFFRACTION' 2.271 2.356  7665 . 363 7114 97.5473 . 0.202 . . 0.199 . . . . . 0.189 . 20 . 0.975 0.959 0.255 
'X-RAY DIFFRACTION' 2.356 2.452  7332 . 322 6844 97.7360 . 0.197 . . 0.195 . . . . . 0.188 . 20 . 0.976 0.963 0.235 
'X-RAY DIFFRACTION' 2.452 2.561  7034 . 359 6537 98.0381 . 0.196 . . 0.193 . . . . . 0.187 . 20 . 0.977 0.964 0.248 
'X-RAY DIFFRACTION' 2.561 2.686  6764 . 314 6327 98.1815 . 0.192 . . 0.190 . . . . . 0.187 . 20 . 0.978 0.965 0.240 
'X-RAY DIFFRACTION' 2.686 2.831  6372 . 305 5959 98.3051 . 0.191 . . 0.189 . . . . . 0.186 . 20 . 0.979 0.969 0.235 
'X-RAY DIFFRACTION' 2.831 3.003  6060 . 303 5661 98.4158 . 0.196 . . 0.192 . . . . . 0.194 . 20 . 0.977 0.956 0.268 
'X-RAY DIFFRACTION' 3.003 3.210  5723 . 294 5350 98.6196 . 0.186 . . 0.185 . . . . . 0.190 . 20 . 0.980 0.974 0.202 
'X-RAY DIFFRACTION' 3.210 3.466  5290 . 249 4979 98.8280 . 0.185 . . 0.183 . . . . . 0.191 . 20 . 0.981 0.969 0.221 
'X-RAY DIFFRACTION' 3.466 3.796  4861 . 239 4574 99.0126 . 0.166 . . 0.165 . . . . . 0.177 . 20 . 0.986 0.980 0.188 
'X-RAY DIFFRACTION' 3.796 4.243  4390 . 223 4129 99.1344 . 0.146 . . 0.145 . . . . . 0.161 . 20 . 0.988 0.980 0.182 
'X-RAY DIFFRACTION' 4.243 4.897  3917 . 198 3692 99.3107 . 0.152 . . 0.150 . . . . . 0.169 . 20 . 0.987 0.981 0.181 
'X-RAY DIFFRACTION' 4.897 5.991  3286 . 160 3109 99.4827 . 0.164 . . 0.162 . . . . . 0.180 . 20 . 0.986 0.981 0.198 
'X-RAY DIFFRACTION' 5.991 8.445  2527 . 119 2396 99.5251 . 0.200 . . 0.198 . . . . . 0.219 . 20 . 0.984 0.979 0.222 
'X-RAY DIFFRACTION' 8.445 74.365 1413 . 78  1333 99.8585 . 0.209 . . 0.208 . . . . . 0.237 . 20 . 0.967 0.903 0.230 
# 
_struct.entry_id                     9GBR 
_struct.title                        'Human Angiotensin-1 converting enzyme N-domain in complex with a diprolyl inhibitor- SG17' 
_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        9GBR 
_struct_keywords.text            'Inhibitor, complex, protease, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1  ? 
B N N 1  ? 
C N N 2  ? 
D N N 3  ? 
E N N 4  ? 
F N N 5  ? 
G N N 5  ? 
H N N 6  ? 
I N N 7  ? 
J N N 8  ? 
K N N 9  ? 
L N N 10 ? 
M N N 11 ? 
N N N 6  ? 
O N N 7  ? 
P N N 8  ? 
Q N N 12 ? 
R N N 12 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ACE_HUMAN 
_struct_ref.pdbx_db_accession          P12821 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;LDPGLQPGNFSADEAGAQLFAQSYNSSAEQVLFQSVAASWAHDTNITAENARRQEEAALLSQEFAEAWGQKAKELYEPIW
QNFTDPQLRRIIGAVRTLGSANLPLAKRQQYNALLSNMSRIYSTAKVCLPNKTATCWSLDPDLTNILASSRSYAMLLFAW
EGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDR
YINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWNATHMFRVAEEFFTSLELSPMPPEFWEGSMLE
KPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVHHEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVS
TPEHLHKIGLLDRVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDWWYLRTKYQGICPPVTRN
ETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLQAGSSRPWQEVLKDMV
GLDALDAQPLLKYFQPVTQWLQEQNQQNGEVLGWPEYQWHPPLPDNYPEGIDLVTDEAEASKFVEEYD
;
_struct_ref.pdbx_align_begin           30 
# 
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 9GBR A 1 ? 628 ? P12821 30 ? 657 ? 1 628 
2 1 9GBR B 1 ? 628 ? P12821 30 ? 657 ? 1 628 
# 
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 9GBR GLN A 9   ? UNP P12821 ASN 38  'engineered mutation' 9   1  
1 9GBR GLN A 25  ? UNP P12821 ASN 54  'engineered mutation' 25  2  
1 9GBR GLN A 82  ? UNP P12821 ASN 111 'engineered mutation' 82  3  
1 9GBR GLN A 117 ? UNP P12821 ASN 146 'engineered mutation' 117 4  
1 9GBR GLN A 131 ? UNP P12821 ASN 160 'engineered mutation' 131 5  
1 9GBR GLN A 289 ? UNP P12821 ASN 318 'engineered mutation' 289 6  
1 9GBR ARG A 545 ? UNP P12821 GLN 574 'engineered mutation' 545 7  
1 9GBR LEU A 576 ? UNP P12821 PRO 605 'engineered mutation' 576 8  
2 9GBR GLN B 9   ? UNP P12821 ASN 38  'engineered mutation' 9   9  
2 9GBR GLN B 25  ? UNP P12821 ASN 54  'engineered mutation' 25  10 
2 9GBR GLN B 82  ? UNP P12821 ASN 111 'engineered mutation' 82  11 
2 9GBR GLN B 117 ? UNP P12821 ASN 146 'engineered mutation' 117 12 
2 9GBR GLN B 131 ? UNP P12821 ASN 160 'engineered mutation' 131 13 
2 9GBR GLN B 289 ? UNP P12821 ASN 318 'engineered mutation' 289 14 
2 9GBR ARG B 545 ? UNP P12821 GLN 574 'engineered mutation' 545 15 
2 9GBR LEU B 576 ? UNP P12821 PRO 605 'engineered mutation' 576 16 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6520  ? 
1 MORE         10    ? 
1 'SSA (A^2)'  46240 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 ASP A 2   ? GLN A 6   ? ASP A 2   GLN A 6   5 ? 5  
HELX_P HELX_P2  AA2 ASP A 13  ? THR A 44  ? ASP A 13  THR A 44  1 ? 32 
HELX_P HELX_P3  AA3 THR A 47  ? GLU A 77  ? THR A 47  GLU A 77  1 ? 31 
HELX_P HELX_P4  AA4 PRO A 78  ? PHE A 83  ? PRO A 78  PHE A 83  5 ? 6  
HELX_P HELX_P5  AA5 ASP A 85  ? ARG A 96  ? ASP A 85  ARG A 96  1 ? 12 
HELX_P HELX_P6  AA6 LEU A 98  ? LEU A 103 ? LEU A 98  LEU A 103 5 ? 6  
HELX_P HELX_P7  AA7 PRO A 104 ? ALA A 125 ? PRO A 104 ALA A 125 1 ? 22 
HELX_P HELX_P8  AA8 PRO A 141 ? SER A 150 ? PRO A 141 SER A 150 1 ? 10 
HELX_P HELX_P9  AA9 SER A 152 ? GLN A 188 ? SER A 152 GLN A 188 1 ? 37 
HELX_P HELX_P10 AB1 ASP A 193 ? TRP A 201 ? ASP A 193 TRP A 201 1 ? 9  
HELX_P HELX_P11 AB2 THR A 206 ? GLY A 238 ? THR A 206 GLY A 238 1 ? 33 
HELX_P HELX_P12 AB3 TRP A 261 ? ASN A 263 ? TRP A 261 ASN A 263 5 ? 3  
HELX_P HELX_P13 AB4 ILE A 264 ? VAL A 269 ? ILE A 264 VAL A 269 1 ? 6  
HELX_P HELX_P14 AB5 VAL A 279 ? GLY A 287 ? VAL A 279 GLY A 287 1 ? 9  
HELX_P HELX_P15 AB6 GLN A 289 ? LEU A 304 ? GLN A 289 LEU A 304 1 ? 16 
HELX_P HELX_P16 AB7 PRO A 310 ? SER A 317 ? PRO A 310 SER A 317 1 ? 8  
HELX_P HELX_P17 AB8 THR A 352 ? TYR A 372 ? THR A 352 TYR A 372 1 ? 21 
HELX_P HELX_P18 AB9 PRO A 376 ? ARG A 380 ? PRO A 376 ARG A 380 5 ? 5  
HELX_P HELX_P19 AC1 ASN A 384 ? SER A 400 ? ASN A 384 SER A 400 1 ? 17 
HELX_P HELX_P20 AC2 THR A 401 ? ILE A 408 ? THR A 401 ILE A 408 1 ? 8  
HELX_P HELX_P21 AC3 ASP A 417 ? ILE A 433 ? ASP A 417 ILE A 433 1 ? 17 
HELX_P HELX_P22 AC4 ALA A 434 ? SER A 451 ? ALA A 434 SER A 451 1 ? 18 
HELX_P HELX_P23 AC5 PRO A 455 ? SER A 457 ? PRO A 455 SER A 457 5 ? 3  
HELX_P HELX_P24 AC6 ARG A 458 ? GLY A 472 ? ARG A 458 GLY A 472 1 ? 15 
HELX_P HELX_P25 AC7 PHE A 484 ? LYS A 489 ? PHE A 484 LYS A 489 5 ? 6  
HELX_P HELX_P26 AC8 TYR A 498 ? ALA A 519 ? TYR A 498 ALA A 519 1 ? 22 
HELX_P HELX_P27 AC9 PRO A 524 ? CYS A 528 ? PRO A 524 CYS A 528 5 ? 5  
HELX_P HELX_P28 AD1 SER A 533 ? GLY A 547 ? SER A 533 GLY A 547 1 ? 15 
HELX_P HELX_P29 AD2 PRO A 551 ? GLY A 561 ? PRO A 551 GLY A 561 1 ? 11 
HELX_P HELX_P30 AD3 ALA A 567 ? ASN A 588 ? ALA A 567 ASN A 588 1 ? 22 
HELX_P HELX_P31 AD4 ASP B 2   ? GLN B 6   ? ASP B 2   GLN B 6   5 ? 5  
HELX_P HELX_P32 AD5 ASP B 13  ? THR B 44  ? ASP B 13  THR B 44  1 ? 32 
HELX_P HELX_P33 AD6 THR B 47  ? GLU B 77  ? THR B 47  GLU B 77  1 ? 31 
HELX_P HELX_P34 AD7 ILE B 79  ? PHE B 83  ? ILE B 79  PHE B 83  5 ? 5  
HELX_P HELX_P35 AD8 ASP B 85  ? ARG B 96  ? ASP B 85  ARG B 96  1 ? 12 
HELX_P HELX_P36 AD9 LEU B 98  ? LEU B 103 ? LEU B 98  LEU B 103 5 ? 6  
HELX_P HELX_P37 AE1 PRO B 104 ? ALA B 125 ? PRO B 104 ALA B 125 1 ? 22 
HELX_P HELX_P38 AE2 PRO B 141 ? SER B 150 ? PRO B 141 SER B 150 1 ? 10 
HELX_P HELX_P39 AE3 SER B 152 ? GLN B 188 ? SER B 152 GLN B 188 1 ? 37 
HELX_P HELX_P40 AE4 ASP B 193 ? TRP B 201 ? ASP B 193 TRP B 201 1 ? 9  
HELX_P HELX_P41 AE5 THR B 206 ? GLY B 238 ? THR B 206 GLY B 238 1 ? 33 
HELX_P HELX_P42 AE6 TRP B 261 ? ASN B 263 ? TRP B 261 ASN B 263 5 ? 3  
HELX_P HELX_P43 AE7 ILE B 264 ? VAL B 269 ? ILE B 264 VAL B 269 1 ? 6  
HELX_P HELX_P44 AE8 VAL B 279 ? GLY B 287 ? VAL B 279 GLY B 287 1 ? 9  
HELX_P HELX_P45 AE9 GLN B 289 ? LEU B 304 ? GLN B 289 LEU B 304 1 ? 16 
HELX_P HELX_P46 AF1 PRO B 310 ? SER B 317 ? PRO B 310 SER B 317 1 ? 8  
HELX_P HELX_P47 AF2 THR B 352 ? TYR B 372 ? THR B 352 TYR B 372 1 ? 21 
HELX_P HELX_P48 AF3 PRO B 376 ? ARG B 380 ? PRO B 376 ARG B 380 5 ? 5  
HELX_P HELX_P49 AF4 ASN B 384 ? SER B 400 ? ASN B 384 SER B 400 1 ? 17 
HELX_P HELX_P50 AF5 THR B 401 ? ILE B 408 ? THR B 401 ILE B 408 1 ? 8  
HELX_P HELX_P51 AF6 ASP B 417 ? ILE B 433 ? ASP B 417 ILE B 433 1 ? 17 
HELX_P HELX_P52 AF7 PHE B 435 ? SER B 451 ? PHE B 435 SER B 451 1 ? 17 
HELX_P HELX_P53 AF8 PRO B 455 ? SER B 457 ? PRO B 455 SER B 457 5 ? 3  
HELX_P HELX_P54 AF9 ARG B 458 ? GLY B 472 ? ARG B 458 GLY B 472 1 ? 15 
HELX_P HELX_P55 AG1 PHE B 484 ? LYS B 489 ? PHE B 484 LYS B 489 5 ? 6  
HELX_P HELX_P56 AG2 TYR B 498 ? ALA B 519 ? TYR B 498 ALA B 519 1 ? 22 
HELX_P HELX_P57 AG3 PRO B 524 ? CYS B 528 ? PRO B 524 CYS B 528 5 ? 5  
HELX_P HELX_P58 AG4 SER B 533 ? ALA B 546 ? SER B 533 ALA B 546 1 ? 14 
HELX_P HELX_P59 AG5 PRO B 551 ? GLY B 561 ? PRO B 551 GLY B 561 1 ? 11 
HELX_P HELX_P60 AG6 ALA B 567 ? ASN B 588 ? ALA B 567 ASN B 588 1 ? 22 
# 
_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 330 SG  ? ? ? 1_555 A CYS   348 SG  ? ? A CYS 330 A CYS   348 1_555 ? ? ? ? ? ? ? 2.190 ? ? 
disulf2  disulf ?    ? A CYS 516 SG  ? ? ? 1_555 A CYS   528 SG  ? ? A CYS 516 A CYS   528 1_555 ? ? ? ? ? ? ? 2.101 ? ? 
disulf3  disulf ?    ? B CYS 128 SG  ? ? ? 1_555 B CYS   136 SG  ? ? B CYS 128 B CYS   136 1_555 ? ? ? ? ? ? ? 2.906 ? ? 
disulf4  disulf ?    ? B CYS 330 SG  ? ? ? 1_555 B CYS   348 SG  ? ? B CYS 330 B CYS   348 1_555 ? ? ? ? ? ? ? 2.766 ? ? 
disulf5  disulf ?    ? B CYS 516 SG  ? ? ? 1_555 B CYS   528 SG  ? ? B CYS 516 B CYS   528 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
covale1  covale one  ? A ASN 45  ND2 ? ? ? 1_555 F NAG   .   C1  ? ? A ASN 45  A NAG   701 1_555 ? ? ? ? ? ? ? 1.471 ? 
N-Glycosylation 
covale2  covale one  ? A ASN 416 ND2 ? ? ? 1_555 E NAG   .   C1  ? ? A ASN 416 E NAG   1   1_555 ? ? ? ? ? ? ? 1.411 ? 
N-Glycosylation 
covale3  covale one  ? A ASN 480 ND2 ? ? ? 1_555 G NAG   .   C1  ? ? A ASN 480 A NAG   702 1_555 ? ? ? ? ? ? ? 1.454 ? 
N-Glycosylation 
covale4  covale one  ? B ASN 416 ND2 ? ? ? 1_555 C NAG   .   C1  ? ? B ASN 416 C NAG   1   1_555 ? ? ? ? ? ? ? 1.454 ? 
N-Glycosylation 
covale5  covale one  ? B ASN 480 ND2 ? ? ? 1_555 D NAG   .   C1  ? ? B ASN 480 D NAG   1   1_555 ? ? ? ? ? ? ? 1.426 ? 
N-Glycosylation 
covale6  covale both ? C NAG .   O4  ? ? ? 1_555 C NAG   .   C1  ? ? C NAG 1   C NAG   2   1_555 ? ? ? ? ? ? ? 1.397 ? ? 
covale7  covale both ? D NAG .   O6  ? ? ? 1_555 D FUC   .   C1  ? ? D NAG 1   D FUC   2   1_555 ? ? ? ? ? ? ? 1.404 ? ? 
covale8  covale both ? E NAG .   O4  ? ? ? 1_555 E NAG   .   C1  ? ? E NAG 1   E NAG   2   1_555 ? ? ? ? ? ? ? 1.389 ? ? 
covale9  covale both ? E NAG .   O6  ? ? ? 1_555 E FUC   .   C1  ? ? E NAG 1   E FUC   4   1_555 ? ? ? ? ? ? ? 1.415 ? ? 
covale10 covale both ? E NAG .   O4  ? ? ? 1_555 E BMA   .   C1  ? ? E NAG 2   E BMA   3   1_555 ? ? ? ? ? ? ? 1.398 ? ? 
metalc1  metalc ?    ? A HIS 361 NE2 ? ? ? 1_555 H ZN    .   ZN  ? ? A HIS 361 A ZN    703 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
metalc2  metalc ?    ? A HIS 365 NE2 ? ? ? 1_555 H ZN    .   ZN  ? ? A HIS 365 A ZN    703 1_555 ? ? ? ? ? ? ? 1.876 ? ? 
metalc3  metalc ?    ? A GLU 389 OE2 ? ? ? 1_555 H ZN    .   ZN  ? ? A GLU 389 A ZN    703 1_555 ? ? ? ? ? ? ? 2.013 ? ? 
metalc4  metalc ?    ? H ZN  .   ZN  ? ? ? 1_555 J A1IJX .   O21 ? ? A ZN  703 A A1IJX 705 1_555 ? ? ? ? ? ? ? 2.569 ? ? 
metalc5  metalc ?    ? H ZN  .   ZN  ? ? ? 1_555 J A1IJX .   O22 ? ? A ZN  703 A A1IJX 705 1_555 ? ? ? ? ? ? ? 1.985 ? ? 
metalc6  metalc ?    ? B HIS 361 NE2 ? ? ? 1_555 N ZN    .   ZN  ? ? B HIS 361 B ZN    704 1_555 ? ? ? ? ? ? ? 1.968 ? ? 
metalc7  metalc ?    ? B HIS 365 NE2 ? ? ? 1_555 N ZN    .   ZN  ? ? B HIS 365 B ZN    704 1_555 ? ? ? ? ? ? ? 2.003 ? ? 
metalc8  metalc ?    ? B GLU 389 OE2 ? ? ? 1_555 N ZN    .   ZN  ? ? B GLU 389 B ZN    704 1_555 ? ? ? ? ? ? ? 1.987 ? ? 
metalc9  metalc ?    ? N ZN  .   ZN  ? ? ? 1_555 P A1IJX .   O21 ? ? B ZN  704 B A1IJX 706 1_555 ? ? ? ? ? ? ? 2.287 ? ? 
metalc10 metalc ?    ? N ZN  .   ZN  ? ? ? 1_555 P A1IJX .   O22 ? ? B ZN  704 B A1IJX 706 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS   361 ? A HIS   361 ? 1_555 ZN ? H ZN . ? A ZN 703 ? 1_555 NE2 ? A HIS   365 ? A HIS   365 ? 1_555 107.0 ? 
2  NE2 ? A HIS   361 ? A HIS   361 ? 1_555 ZN ? H ZN . ? A ZN 703 ? 1_555 OE2 ? A GLU   389 ? A GLU   389 ? 1_555 94.0  ? 
3  NE2 ? A HIS   365 ? A HIS   365 ? 1_555 ZN ? H ZN . ? A ZN 703 ? 1_555 OE2 ? A GLU   389 ? A GLU   389 ? 1_555 103.4 ? 
4  NE2 ? A HIS   361 ? A HIS   361 ? 1_555 ZN ? H ZN . ? A ZN 703 ? 1_555 O21 ? J A1IJX .   ? A A1IJX 705 ? 1_555 98.0  ? 
5  NE2 ? A HIS   365 ? A HIS   365 ? 1_555 ZN ? H ZN . ? A ZN 703 ? 1_555 O21 ? J A1IJX .   ? A A1IJX 705 ? 1_555 90.4  ? 
6  OE2 ? A GLU   389 ? A GLU   389 ? 1_555 ZN ? H ZN . ? A ZN 703 ? 1_555 O21 ? J A1IJX .   ? A A1IJX 705 ? 1_555 158.3 ? 
7  NE2 ? A HIS   361 ? A HIS   361 ? 1_555 ZN ? H ZN . ? A ZN 703 ? 1_555 O22 ? J A1IJX .   ? A A1IJX 705 ? 1_555 115.7 ? 
8  NE2 ? A HIS   365 ? A HIS   365 ? 1_555 ZN ? H ZN . ? A ZN 703 ? 1_555 O22 ? J A1IJX .   ? A A1IJX 705 ? 1_555 129.8 ? 
9  OE2 ? A GLU   389 ? A GLU   389 ? 1_555 ZN ? H ZN . ? A ZN 703 ? 1_555 O22 ? J A1IJX .   ? A A1IJX 705 ? 1_555 98.9  ? 
10 O21 ? J A1IJX .   ? A A1IJX 705 ? 1_555 ZN ? H ZN . ? A ZN 703 ? 1_555 O22 ? J A1IJX .   ? A A1IJX 705 ? 1_555 59.6  ? 
11 NE2 ? B HIS   361 ? B HIS   361 ? 1_555 ZN ? N ZN . ? B ZN 704 ? 1_555 NE2 ? B HIS   365 ? B HIS   365 ? 1_555 107.1 ? 
12 NE2 ? B HIS   361 ? B HIS   361 ? 1_555 ZN ? N ZN . ? B ZN 704 ? 1_555 OE2 ? B GLU   389 ? B GLU   389 ? 1_555 93.1  ? 
13 NE2 ? B HIS   365 ? B HIS   365 ? 1_555 ZN ? N ZN . ? B ZN 704 ? 1_555 OE2 ? B GLU   389 ? B GLU   389 ? 1_555 103.1 ? 
14 NE2 ? B HIS   361 ? B HIS   361 ? 1_555 ZN ? N ZN . ? B ZN 704 ? 1_555 O21 ? P A1IJX .   ? B A1IJX 706 ? 1_555 97.2  ? 
15 NE2 ? B HIS   365 ? B HIS   365 ? 1_555 ZN ? N ZN . ? B ZN 704 ? 1_555 O21 ? P A1IJX .   ? B A1IJX 706 ? 1_555 93.1  ? 
16 OE2 ? B GLU   389 ? B GLU   389 ? 1_555 ZN ? N ZN . ? B ZN 704 ? 1_555 O21 ? P A1IJX .   ? B A1IJX 706 ? 1_555 157.3 ? 
17 NE2 ? B HIS   361 ? B HIS   361 ? 1_555 ZN ? N ZN . ? B ZN 704 ? 1_555 O22 ? P A1IJX .   ? B A1IJX 706 ? 1_555 117.6 ? 
18 NE2 ? B HIS   365 ? B HIS   365 ? 1_555 ZN ? N ZN . ? B ZN 704 ? 1_555 O22 ? P A1IJX .   ? B A1IJX 706 ? 1_555 130.5 ? 
19 OE2 ? B GLU   389 ? B GLU   389 ? 1_555 ZN ? N ZN . ? B ZN 704 ? 1_555 O22 ? P A1IJX .   ? B A1IJX 706 ? 1_555 94.9  ? 
20 O21 ? P A1IJX .   ? B A1IJX 706 ? 1_555 ZN ? N ZN . ? B ZN 704 ? 1_555 O22 ? P A1IJX .   ? B A1IJX 706 ? 1_555 62.4  ? 
# 
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 C .   ? ASN B 416 ? NAG C 1   ? 1_555 ASN B 416 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG D .   ? ASN B 480 ? NAG D 1   ? 1_555 ASN B 480 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG E .   ? ASN A 416 ? NAG E 1   ? 1_555 ASN A 416 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG F .   ? ASN A 45  ? NAG A 701 ? 1_555 ASN A 45  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG G .   ? ASN A 480 ? NAG A 702 ? 1_555 ASN A 480 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  CYS A 330 ? CYS A 348 ? CYS A 330 ? 1_555 CYS A 348 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
7  CYS A 516 ? CYS A 528 ? CYS A 516 ? 1_555 CYS A 528 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8  CYS B 128 ? CYS B 136 ? CYS B 128 ? 1_555 CYS B 136 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9  CYS B 330 ? CYS B 348 ? CYS B 330 ? 1_555 CYS B 348 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
10 CYS B 516 ? CYS B 528 ? CYS B 516 ? 1_555 CYS B 528 ? 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 ASP 140 A . ? ASP 140 A PRO 141 A ? PRO 141 A 1 2.91  
2 TYR 607 A . ? TYR 607 A PRO 608 A ? PRO 608 A 1 -8.32 
3 ASP 140 B . ? ASP 140 B PRO 141 B ? PRO 141 B 1 4.53  
4 TYR 607 B . ? TYR 607 B PRO 608 B ? PRO 608 B 1 1.92  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA5 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 248 ? PRO A 249 ? ILE A 248 PRO A 249 
AA1 2 ILE A 473 ? CYS A 474 ? ILE A 473 CYS A 474 
AA2 1 SER A 333 ? ASP A 336 ? SER A 333 ASP A 336 
AA2 2 PHE A 343 ? LYS A 346 ? PHE A 343 LYS A 346 
AA3 1 LYS B 126 ? VAL B 127 ? LYS B 126 VAL B 127 
AA3 2 TRP B 137 ? SER B 138 ? TRP B 137 SER B 138 
AA4 1 ILE B 248 ? PRO B 249 ? ILE B 248 PRO B 249 
AA4 2 ILE B 473 ? CYS B 474 ? ILE B 473 CYS B 474 
AA5 1 SER B 333 ? ASP B 336 ? SER B 333 ASP B 336 
AA5 2 PHE B 343 ? LYS B 346 ? PHE B 343 LYS B 346 
# 
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 ILE A 248 ? N ILE A 248 O CYS A 474 ? O CYS A 474 
AA2 1 2 N TRP A 335 ? N TRP A 335 O ARG A 344 ? O ARG A 344 
AA3 1 2 N VAL B 127 ? N VAL B 127 O TRP B 137 ? O TRP B 137 
AA4 1 2 N ILE B 248 ? N ILE B 248 O CYS B 474 ? O CYS B 474 
AA5 1 2 N TRP B 335 ? N TRP B 335 O ARG B 344 ? O ARG B 344 
# 
_pdbx_entry_details.entry_id                   9GBR 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   B PRO 7   ? ? O   B HOH 801 ? ? 1.85 
2 1 ND2 B ASN 102 ? ? OD1 B ASP 189 ? ? 2.04 
3 1 OG  A SER 260 ? ? OE1 A GLU 262 ? ? 2.13 
4 1 OD1 B ASP 140 ? ? O   B HOH 802 ? ? 2.19 
# 
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 C  B ALA 12  ? ? O   B ALA 12  ? ? 1.429 1.229 0.200 0.019 N 
2 1 C  B ALA 15  ? ? O   B ALA 15  ? ? 1.387 1.229 0.158 0.019 N 
3 1 CD B GLU 262 ? ? OE1 B GLU 262 ? ? 1.327 1.252 0.075 0.011 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CB A GLN 18  ? ? CA A GLN 18  ? ? C   A GLN 18  ? ? 95.57  110.40 -14.83 2.00 N 
2  1 CB A LEU 59  ? ? CG A LEU 59  ? ? CD2 A LEU 59  ? ? 124.17 111.00 13.17  1.70 N 
3  1 NE A ARG 89  ? ? CZ A ARG 89  ? ? NH1 A ARG 89  ? ? 117.06 120.30 -3.24  0.50 N 
4  1 CA A THR 97  ? ? CB A THR 97  ? ? OG1 A THR 97  ? ? 96.37  109.00 -12.63 2.10 N 
5  1 CD A LYS 107 ? ? CE A LYS 107 ? ? NZ  A LYS 107 ? ? 95.30  111.70 -16.40 2.30 N 
6  1 NE A ARG 151 ? ? CZ A ARG 151 ? ? NH2 A ARG 151 ? ? 124.75 120.30 4.45   0.50 N 
7  1 CA A ARG 236 ? ? CB A ARG 236 ? ? CG  A ARG 236 ? ? 97.89  113.40 -15.51 2.20 N 
8  1 CD A ARG 236 ? ? NE A ARG 236 ? ? CZ  A ARG 236 ? ? 132.18 123.60 8.58   1.40 N 
9  1 NE A ARG 236 ? ? CZ A ARG 236 ? ? NH2 A ARG 236 ? ? 116.98 120.30 -3.32  0.50 N 
10 1 CG A MET 267 ? ? SD A MET 267 ? ? CE  A MET 267 ? ? 85.77  100.20 -14.43 1.60 N 
11 1 CG A ARG 340 ? ? CD A ARG 340 ? ? NE  A ARG 340 ? ? 98.37  111.80 -13.43 2.10 N 
12 1 CD A LYS 373 ? ? CE A LYS 373 ? ? NZ  A LYS 373 ? ? 97.68  111.70 -14.02 2.30 N 
13 1 CA A ARG 453 ? ? CB A ARG 453 ? ? CG  A ARG 453 ? ? 99.75  113.40 -13.65 2.20 N 
14 1 CD A ARG 550 ? ? NE A ARG 550 ? ? CZ  A ARG 550 ? ? 132.74 123.60 9.14   1.40 N 
15 1 NE A ARG 550 ? ? CZ A ARG 550 ? ? NH2 A ARG 550 ? ? 116.42 120.30 -3.88  0.50 N 
16 1 CB B GLN 9   ? ? CA B GLN 9   ? ? C   B GLN 9   ? ? 123.89 110.40 13.49  2.00 N 
17 1 CB B ASN 50  ? ? CA B ASN 50  ? ? C   B ASN 50  ? ? 123.29 110.40 12.89  2.00 N 
18 1 CB B GLN 54  ? ? CA B GLN 54  ? ? C   B GLN 54  ? ? 126.80 110.40 16.40  2.00 N 
19 1 CB B CYS 128 ? ? CA B CYS 128 ? ? C   B CYS 128 ? ? 97.69  110.40 -12.71 2.00 N 
20 1 CB B ASN 203 ? ? CA B ASN 203 ? ? C   B ASN 203 ? ? 94.50  110.40 -15.90 2.00 N 
21 1 N  B PRO 272 ? ? CA B PRO 272 ? ? C   B PRO 272 ? ? 131.78 112.10 19.68  2.60 N 
22 1 NE B ARG 295 ? ? CZ B ARG 295 ? ? NH2 B ARG 295 ? ? 116.58 120.30 -3.72  0.50 N 
23 1 CB B ASN 339 ? ? CA B ASN 339 ? ? C   B ASN 339 ? ? 89.00  110.40 -21.40 2.00 N 
24 1 NE B ARG 344 ? ? CZ B ARG 344 ? ? NH1 B ARG 344 ? ? 116.94 120.30 -3.36  0.50 N 
25 1 CB B ASP 412 ? ? CA B ASP 412 ? ? C   B ASP 412 ? ? 123.96 110.40 13.56  2.00 N 
26 1 CG B MET 559 ? ? SD B MET 559 ? ? CE  B MET 559 ? ? 110.42 100.20 10.22  1.60 N 
27 1 N  B PRO 608 ? ? CA B PRO 608 ? ? CB  B PRO 608 ? ? 93.46  102.60 -9.14  1.10 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 45  ? ? -171.89 79.00  
2  1 PRO A 78  ? ? -69.84  -73.21 
3  1 ILE A 79  ? ? -49.81  -12.03 
4  1 ASN A 203 ? ? 39.73   57.07  
5  1 LYS A 341 ? ? -131.36 -48.72 
6  1 TYR A 531 ? ? -39.73  131.15 
7  1 PRO A 608 ? ? -97.19  35.22  
8  1 PHE B 10  ? ? -170.18 147.21 
9  1 ASP B 13  ? ? 171.61  172.76 
10 1 ASN B 45  ? ? -177.05 74.64  
11 1 ASN B 203 ? ? 27.69   69.63  
12 1 THR B 206 ? ? -98.11  30.27  
13 1 LYS B 341 ? ? -124.56 -50.19 
14 1 VAL B 377 ? ? -28.78  -54.74 
15 1 ASN B 416 ? ? -68.36  70.10  
16 1 PRO B 608 ? ? -108.78 76.83  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   PRO 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    78 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   ILE 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    79 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -149.02 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 381 ? ? 0.075 'SIDE CHAIN' 
2 1 ARG A 453 ? ? 0.100 'SIDE CHAIN' 
3 1 ARG B 120 ? ? 0.084 'SIDE CHAIN' 
4 1 ARG B 236 ? ? 0.098 'SIDE CHAIN' 
5 1 ARG B 467 ? ? 0.074 '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 1.8980  -14.8504 -18.6243 0.0154 ? 0.0319 ? -0.0048 ? 0.1131 ? -0.0011 ? 0.0086 ? 1.0209 ? -0.1645 
? 0.0601  ? 1.1594 ? 0.2556 ? 0.5367 ? 0.0614  ? 0.0947  ? -0.0731 ? -0.0898 ? -0.0323 ? 0.0424 ? -0.0183 ? 0.0062  ? -0.0292 ? 
2 'X-RAY DIFFRACTION' ? refined -1.5732 14.9662  18.4896  0.0773 ? 0.0094 ? -0.0006 ? 0.0874 ? -0.0079 ? 0.0561 ? 0.9597 ? -0.3477 
? -0.3068 ? 1.3280 ? 0.6861 ? 1.8827 ? -0.0406 ? -0.1101 ? -0.0275 ? 0.2047  ? 0.0224  ? 0.0616 ? 0.1154  ? -0.0548 ? 0.0182  ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    Ap 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_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    Ap 
_pdbx_refine_tls_group.end_auth_seq_id     1161 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ALL 
_pdbx_refine_tls_group.selection_details   ? 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       1160 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.60 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A PRO 130 ? A PRO 130 
2  1 Y 1 A GLN 131 ? A GLN 131 
3  1 Y 1 A LYS 132 ? A LYS 132 
4  1 Y 1 A THR 133 ? A THR 133 
5  1 Y 1 A ALA 134 ? A ALA 134 
6  1 Y 1 A GLY 610 ? A GLY 610 
7  1 Y 1 A ILE 611 ? A ILE 611 
8  1 Y 1 A ASP 612 ? A ASP 612 
9  1 Y 1 A LEU 613 ? A LEU 613 
10 1 Y 1 A VAL 614 ? A VAL 614 
11 1 Y 1 A THR 615 ? A THR 615 
12 1 Y 1 A ASP 616 ? A ASP 616 
13 1 Y 1 A GLU 617 ? A GLU 617 
14 1 Y 1 A ALA 618 ? A ALA 618 
15 1 Y 1 A GLU 619 ? A GLU 619 
16 1 Y 1 A ALA 620 ? A ALA 620 
17 1 Y 1 A SER 621 ? A SER 621 
18 1 Y 1 A LYS 622 ? A LYS 622 
19 1 Y 1 A PHE 623 ? A PHE 623 
20 1 Y 1 A VAL 624 ? A VAL 624 
21 1 Y 1 A GLU 625 ? A GLU 625 
22 1 Y 1 A GLU 626 ? A GLU 626 
23 1 Y 1 A TYR 627 ? A TYR 627 
24 1 Y 1 A ASP 628 ? A ASP 628 
25 1 Y 1 B LEU 1   ? B LEU 1   
26 1 Y 1 B PRO 130 ? B PRO 130 
27 1 Y 1 B GLN 131 ? B GLN 131 
28 1 Y 1 B LYS 132 ? B LYS 132 
29 1 Y 1 B THR 133 ? B THR 133 
30 1 Y 1 B ALA 134 ? B ALA 134 
31 1 Y 1 B THR 135 ? B THR 135 
32 1 Y 1 B GLY 610 ? B GLY 610 
33 1 Y 1 B ILE 611 ? B ILE 611 
34 1 Y 1 B ASP 612 ? B ASP 612 
35 1 Y 1 B LEU 613 ? B LEU 613 
36 1 Y 1 B VAL 614 ? B VAL 614 
37 1 Y 1 B THR 615 ? B THR 615 
38 1 Y 1 B ASP 616 ? B ASP 616 
39 1 Y 1 B GLU 617 ? B GLU 617 
40 1 Y 1 B ALA 618 ? B ALA 618 
41 1 Y 1 B GLU 619 ? B GLU 619 
42 1 Y 1 B ALA 620 ? B ALA 620 
43 1 Y 1 B SER 621 ? B SER 621 
44 1 Y 1 B LYS 622 ? B LYS 622 
45 1 Y 1 B PHE 623 ? B PHE 623 
46 1 Y 1 B VAL 624 ? B VAL 624 
47 1 Y 1 B GLU 625 ? B GLU 625 
48 1 Y 1 B GLU 626 ? B GLU 626 
49 1 Y 1 B TYR 627 ? B TYR 627 
50 1 Y 1 B ASP 628 ? B ASP 628 
# 
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 
A1IJX O01  O  N N 1   
A1IJX C02  C  N N 2   
A1IJX C03  C  N S 3   
A1IJX N04  N  N N 4   
A1IJX C05  C  N S 5   
A1IJX C06  C  N S 6   
A1IJX C07  C  N N 7   
A1IJX C08  C  N N 8   
A1IJX C09  C  N N 9   
A1IJX N10  N  N N 10  
A1IJX C11  C  N N 11  
A1IJX C12  C  N S 12  
A1IJX N13  N  N N 13  
A1IJX C14  C  N N 14  
A1IJX C15  C  N N 15  
A1IJX C16  C  N N 16  
A1IJX O17  O  N N 17  
A1IJX O18  O  N N 18  
A1IJX O19  O  N N 19  
A1IJX C20  C  N N 20  
A1IJX O21  O  N N 21  
A1IJX O22  O  N N 22  
A1IJX C23  C  N N 23  
A1IJX N24  N  N N 24  
A1IJX C25  C  N N 25  
A1IJX C26  C  N N 26  
A1IJX C27  C  N N 27  
A1IJX C28  C  N S 28  
A1IJX C29  C  N N 29  
A1IJX O30  O  N N 30  
A1IJX O31  O  N N 31  
A1IJX H1   H  N N 32  
A1IJX H2   H  N N 33  
A1IJX H4   H  N N 34  
A1IJX H5   H  N N 35  
A1IJX H6   H  N N 36  
A1IJX H7   H  N N 37  
A1IJX H8   H  N N 38  
A1IJX H9   H  N N 39  
A1IJX H10  H  N N 40  
A1IJX H11  H  N N 41  
A1IJX H12  H  N N 42  
A1IJX H13  H  N N 43  
A1IJX H14  H  N N 44  
A1IJX H16  H  N N 45  
A1IJX H17  H  N N 46  
A1IJX H18  H  N N 47  
A1IJX H19  H  N N 48  
A1IJX H20  H  N N 49  
A1IJX H21  H  N N 50  
A1IJX H22  H  N N 51  
A1IJX H23  H  N N 52  
A1IJX H24  H  N N 53  
A1IJX H25  H  N N 54  
A1IJX H26  H  N N 55  
A1IJX H27  H  N N 56  
A1IJX H28  H  N N 57  
A1IJX H29  H  N N 58  
A1IJX H30  H  N N 59  
A1IJX H31  H  N N 60  
A1IJX H32  H  N N 61  
ALA   N    N  N N 62  
ALA   CA   C  N S 63  
ALA   C    C  N N 64  
ALA   O    O  N N 65  
ALA   CB   C  N N 66  
ALA   OXT  O  N N 67  
ALA   H    H  N N 68  
ALA   H2   H  N N 69  
ALA   HA   H  N N 70  
ALA   HB1  H  N N 71  
ALA   HB2  H  N N 72  
ALA   HB3  H  N N 73  
ALA   HXT  H  N N 74  
ARG   N    N  N N 75  
ARG   CA   C  N S 76  
ARG   C    C  N N 77  
ARG   O    O  N N 78  
ARG   CB   C  N N 79  
ARG   CG   C  N N 80  
ARG   CD   C  N N 81  
ARG   NE   N  N N 82  
ARG   CZ   C  N N 83  
ARG   NH1  N  N N 84  
ARG   NH2  N  N N 85  
ARG   OXT  O  N N 86  
ARG   H    H  N N 87  
ARG   H2   H  N N 88  
ARG   HA   H  N N 89  
ARG   HB2  H  N N 90  
ARG   HB3  H  N N 91  
ARG   HG2  H  N N 92  
ARG   HG3  H  N N 93  
ARG   HD2  H  N N 94  
ARG   HD3  H  N N 95  
ARG   HE   H  N N 96  
ARG   HH11 H  N N 97  
ARG   HH12 H  N N 98  
ARG   HH21 H  N N 99  
ARG   HH22 H  N N 100 
ARG   HXT  H  N N 101 
ASN   N    N  N N 102 
ASN   CA   C  N S 103 
ASN   C    C  N N 104 
ASN   O    O  N N 105 
ASN   CB   C  N N 106 
ASN   CG   C  N N 107 
ASN   OD1  O  N N 108 
ASN   ND2  N  N N 109 
ASN   OXT  O  N N 110 
ASN   H    H  N N 111 
ASN   H2   H  N N 112 
ASN   HA   H  N N 113 
ASN   HB2  H  N N 114 
ASN   HB3  H  N N 115 
ASN   HD21 H  N N 116 
ASN   HD22 H  N N 117 
ASN   HXT  H  N N 118 
ASP   N    N  N N 119 
ASP   CA   C  N S 120 
ASP   C    C  N N 121 
ASP   O    O  N N 122 
ASP   CB   C  N N 123 
ASP   CG   C  N N 124 
ASP   OD1  O  N N 125 
ASP   OD2  O  N N 126 
ASP   OXT  O  N N 127 
ASP   H    H  N N 128 
ASP   H2   H  N N 129 
ASP   HA   H  N N 130 
ASP   HB2  H  N N 131 
ASP   HB3  H  N N 132 
ASP   HD2  H  N N 133 
ASP   HXT  H  N N 134 
BMA   C1   C  N R 135 
BMA   C2   C  N S 136 
BMA   C3   C  N S 137 
BMA   C4   C  N S 138 
BMA   C5   C  N R 139 
BMA   C6   C  N N 140 
BMA   O1   O  N N 141 
BMA   O2   O  N N 142 
BMA   O3   O  N N 143 
BMA   O4   O  N N 144 
BMA   O5   O  N N 145 
BMA   O6   O  N N 146 
BMA   H1   H  N N 147 
BMA   H2   H  N N 148 
BMA   H3   H  N N 149 
BMA   H4   H  N N 150 
BMA   H5   H  N N 151 
BMA   H61  H  N N 152 
BMA   H62  H  N N 153 
BMA   HO1  H  N N 154 
BMA   HO2  H  N N 155 
BMA   HO3  H  N N 156 
BMA   HO4  H  N N 157 
BMA   HO6  H  N N 158 
CL    CL   CL N N 159 
CYS   N    N  N N 160 
CYS   CA   C  N R 161 
CYS   C    C  N N 162 
CYS   O    O  N N 163 
CYS   CB   C  N N 164 
CYS   SG   S  N N 165 
CYS   OXT  O  N N 166 
CYS   H    H  N N 167 
CYS   H2   H  N N 168 
CYS   HA   H  N N 169 
CYS   HB2  H  N N 170 
CYS   HB3  H  N N 171 
CYS   HG   H  N N 172 
CYS   HXT  H  N N 173 
FUC   C1   C  N R 174 
FUC   C2   C  N S 175 
FUC   C3   C  N R 176 
FUC   C4   C  N S 177 
FUC   C5   C  N S 178 
FUC   C6   C  N N 179 
FUC   O1   O  N N 180 
FUC   O2   O  N N 181 
FUC   O3   O  N N 182 
FUC   O4   O  N N 183 
FUC   O5   O  N N 184 
FUC   H1   H  N N 185 
FUC   H2   H  N N 186 
FUC   H3   H  N N 187 
FUC   H4   H  N N 188 
FUC   H5   H  N N 189 
FUC   H61  H  N N 190 
FUC   H62  H  N N 191 
FUC   H63  H  N N 192 
FUC   HO1  H  N N 193 
FUC   HO2  H  N N 194 
FUC   HO3  H  N N 195 
FUC   HO4  H  N N 196 
GLN   N    N  N N 197 
GLN   CA   C  N S 198 
GLN   C    C  N N 199 
GLN   O    O  N N 200 
GLN   CB   C  N N 201 
GLN   CG   C  N N 202 
GLN   CD   C  N N 203 
GLN   OE1  O  N N 204 
GLN   NE2  N  N N 205 
GLN   OXT  O  N N 206 
GLN   H    H  N N 207 
GLN   H2   H  N N 208 
GLN   HA   H  N N 209 
GLN   HB2  H  N N 210 
GLN   HB3  H  N N 211 
GLN   HG2  H  N N 212 
GLN   HG3  H  N N 213 
GLN   HE21 H  N N 214 
GLN   HE22 H  N N 215 
GLN   HXT  H  N N 216 
GLU   N    N  N N 217 
GLU   CA   C  N S 218 
GLU   C    C  N N 219 
GLU   O    O  N N 220 
GLU   CB   C  N N 221 
GLU   CG   C  N N 222 
GLU   CD   C  N N 223 
GLU   OE1  O  N N 224 
GLU   OE2  O  N N 225 
GLU   OXT  O  N N 226 
GLU   H    H  N N 227 
GLU   H2   H  N N 228 
GLU   HA   H  N N 229 
GLU   HB2  H  N N 230 
GLU   HB3  H  N N 231 
GLU   HG2  H  N N 232 
GLU   HG3  H  N N 233 
GLU   HE2  H  N N 234 
GLU   HXT  H  N N 235 
GLY   N    N  N N 236 
GLY   CA   C  N N 237 
GLY   C    C  N N 238 
GLY   O    O  N N 239 
GLY   OXT  O  N N 240 
GLY   H    H  N N 241 
GLY   H2   H  N N 242 
GLY   HA2  H  N N 243 
GLY   HA3  H  N N 244 
GLY   HXT  H  N N 245 
HIS   N    N  N N 246 
HIS   CA   C  N S 247 
HIS   C    C  N N 248 
HIS   O    O  N N 249 
HIS   CB   C  N N 250 
HIS   CG   C  Y N 251 
HIS   ND1  N  Y N 252 
HIS   CD2  C  Y N 253 
HIS   CE1  C  Y N 254 
HIS   NE2  N  Y N 255 
HIS   OXT  O  N N 256 
HIS   H    H  N N 257 
HIS   H2   H  N N 258 
HIS   HA   H  N N 259 
HIS   HB2  H  N N 260 
HIS   HB3  H  N N 261 
HIS   HD1  H  N N 262 
HIS   HD2  H  N N 263 
HIS   HE1  H  N N 264 
HIS   HE2  H  N N 265 
HIS   HXT  H  N N 266 
HOH   O    O  N N 267 
HOH   H1   H  N N 268 
HOH   H2   H  N N 269 
ILE   N    N  N N 270 
ILE   CA   C  N S 271 
ILE   C    C  N N 272 
ILE   O    O  N N 273 
ILE   CB   C  N S 274 
ILE   CG1  C  N N 275 
ILE   CG2  C  N N 276 
ILE   CD1  C  N N 277 
ILE   OXT  O  N N 278 
ILE   H    H  N N 279 
ILE   H2   H  N N 280 
ILE   HA   H  N N 281 
ILE   HB   H  N N 282 
ILE   HG12 H  N N 283 
ILE   HG13 H  N N 284 
ILE   HG21 H  N N 285 
ILE   HG22 H  N N 286 
ILE   HG23 H  N N 287 
ILE   HD11 H  N N 288 
ILE   HD12 H  N N 289 
ILE   HD13 H  N N 290 
ILE   HXT  H  N N 291 
LEU   N    N  N N 292 
LEU   CA   C  N S 293 
LEU   C    C  N N 294 
LEU   O    O  N N 295 
LEU   CB   C  N N 296 
LEU   CG   C  N N 297 
LEU   CD1  C  N N 298 
LEU   CD2  C  N N 299 
LEU   OXT  O  N N 300 
LEU   H    H  N N 301 
LEU   H2   H  N N 302 
LEU   HA   H  N N 303 
LEU   HB2  H  N N 304 
LEU   HB3  H  N N 305 
LEU   HG   H  N N 306 
LEU   HD11 H  N N 307 
LEU   HD12 H  N N 308 
LEU   HD13 H  N N 309 
LEU   HD21 H  N N 310 
LEU   HD22 H  N N 311 
LEU   HD23 H  N N 312 
LEU   HXT  H  N N 313 
LYS   N    N  N N 314 
LYS   CA   C  N S 315 
LYS   C    C  N N 316 
LYS   O    O  N N 317 
LYS   CB   C  N N 318 
LYS   CG   C  N N 319 
LYS   CD   C  N N 320 
LYS   CE   C  N N 321 
LYS   NZ   N  N N 322 
LYS   OXT  O  N N 323 
LYS   H    H  N N 324 
LYS   H2   H  N N 325 
LYS   HA   H  N N 326 
LYS   HB2  H  N N 327 
LYS   HB3  H  N N 328 
LYS   HG2  H  N N 329 
LYS   HG3  H  N N 330 
LYS   HD2  H  N N 331 
LYS   HD3  H  N N 332 
LYS   HE2  H  N N 333 
LYS   HE3  H  N N 334 
LYS   HZ1  H  N N 335 
LYS   HZ2  H  N N 336 
LYS   HZ3  H  N N 337 
LYS   HXT  H  N N 338 
MET   N    N  N N 339 
MET   CA   C  N S 340 
MET   C    C  N N 341 
MET   O    O  N N 342 
MET   CB   C  N N 343 
MET   CG   C  N N 344 
MET   SD   S  N N 345 
MET   CE   C  N N 346 
MET   OXT  O  N N 347 
MET   H    H  N N 348 
MET   H2   H  N N 349 
MET   HA   H  N N 350 
MET   HB2  H  N N 351 
MET   HB3  H  N N 352 
MET   HG2  H  N N 353 
MET   HG3  H  N N 354 
MET   HE1  H  N N 355 
MET   HE2  H  N N 356 
MET   HE3  H  N N 357 
MET   HXT  H  N N 358 
NAG   C1   C  N R 359 
NAG   C2   C  N R 360 
NAG   C3   C  N R 361 
NAG   C4   C  N S 362 
NAG   C5   C  N R 363 
NAG   C6   C  N N 364 
NAG   C7   C  N N 365 
NAG   C8   C  N N 366 
NAG   N2   N  N N 367 
NAG   O1   O  N N 368 
NAG   O3   O  N N 369 
NAG   O4   O  N N 370 
NAG   O5   O  N N 371 
NAG   O6   O  N N 372 
NAG   O7   O  N N 373 
NAG   H1   H  N N 374 
NAG   H2   H  N N 375 
NAG   H3   H  N N 376 
NAG   H4   H  N N 377 
NAG   H5   H  N N 378 
NAG   H61  H  N N 379 
NAG   H62  H  N N 380 
NAG   H81  H  N N 381 
NAG   H82  H  N N 382 
NAG   H83  H  N N 383 
NAG   HN2  H  N N 384 
NAG   HO1  H  N N 385 
NAG   HO3  H  N N 386 
NAG   HO4  H  N N 387 
NAG   HO6  H  N N 388 
P33   O22  O  N N 389 
P33   C21  C  N N 390 
P33   C20  C  N N 391 
P33   O19  O  N N 392 
P33   C18  C  N N 393 
P33   C17  C  N N 394 
P33   O16  O  N N 395 
P33   C15  C  N N 396 
P33   C14  C  N N 397 
P33   O13  O  N N 398 
P33   C12  C  N N 399 
P33   C11  C  N N 400 
P33   O10  O  N N 401 
P33   C9   C  N N 402 
P33   C8   C  N N 403 
P33   O7   O  N N 404 
P33   C6   C  N N 405 
P33   C5   C  N N 406 
P33   O4   O  N N 407 
P33   C3   C  N N 408 
P33   C2   C  N N 409 
P33   O1   O  N N 410 
P33   H22  H  N N 411 
P33   H211 H  N N 412 
P33   H212 H  N N 413 
P33   H201 H  N N 414 
P33   H202 H  N N 415 
P33   H181 H  N N 416 
P33   H182 H  N N 417 
P33   H171 H  N N 418 
P33   H172 H  N N 419 
P33   H151 H  N N 420 
P33   H152 H  N N 421 
P33   H141 H  N N 422 
P33   H142 H  N N 423 
P33   H121 H  N N 424 
P33   H122 H  N N 425 
P33   H111 H  N N 426 
P33   H112 H  N N 427 
P33   H91  H  N N 428 
P33   H92  H  N N 429 
P33   H81  H  N N 430 
P33   H82  H  N N 431 
P33   H61  H  N N 432 
P33   H62  H  N N 433 
P33   H51  H  N N 434 
P33   H52  H  N N 435 
P33   H31  H  N N 436 
P33   H32  H  N N 437 
P33   H21  H  N N 438 
P33   H22A H  N N 439 
P33   HO1  H  N N 440 
PG4   O1   O  N N 441 
PG4   C1   C  N N 442 
PG4   C2   C  N N 443 
PG4   O2   O  N N 444 
PG4   C3   C  N N 445 
PG4   C4   C  N N 446 
PG4   O3   O  N N 447 
PG4   C5   C  N N 448 
PG4   C6   C  N N 449 
PG4   O4   O  N N 450 
PG4   C7   C  N N 451 
PG4   C8   C  N N 452 
PG4   O5   O  N N 453 
PG4   HO1  H  N N 454 
PG4   H11  H  N N 455 
PG4   H12  H  N N 456 
PG4   H21  H  N N 457 
PG4   H22  H  N N 458 
PG4   H31  H  N N 459 
PG4   H32  H  N N 460 
PG4   H41  H  N N 461 
PG4   H42  H  N N 462 
PG4   H51  H  N N 463 
PG4   H52  H  N N 464 
PG4   H61  H  N N 465 
PG4   H62  H  N N 466 
PG4   H71  H  N N 467 
PG4   H72  H  N N 468 
PG4   H81  H  N N 469 
PG4   H82  H  N N 470 
PG4   HO5  H  N N 471 
PGE   C1   C  N N 472 
PGE   O1   O  N N 473 
PGE   C2   C  N N 474 
PGE   O2   O  N N 475 
PGE   C3   C  N N 476 
PGE   C4   C  N N 477 
PGE   O4   O  N N 478 
PGE   C6   C  N N 479 
PGE   C5   C  N N 480 
PGE   O3   O  N N 481 
PGE   H1   H  N N 482 
PGE   H12  H  N N 483 
PGE   HO1  H  N N 484 
PGE   H2   H  N N 485 
PGE   H22  H  N N 486 
PGE   H3   H  N N 487 
PGE   H32  H  N N 488 
PGE   H4   H  N N 489 
PGE   H42  H  N N 490 
PGE   HO4  H  N N 491 
PGE   H6   H  N N 492 
PGE   H62  H  N N 493 
PGE   H5   H  N N 494 
PGE   H52  H  N N 495 
PHE   N    N  N N 496 
PHE   CA   C  N S 497 
PHE   C    C  N N 498 
PHE   O    O  N N 499 
PHE   CB   C  N N 500 
PHE   CG   C  Y N 501 
PHE   CD1  C  Y N 502 
PHE   CD2  C  Y N 503 
PHE   CE1  C  Y N 504 
PHE   CE2  C  Y N 505 
PHE   CZ   C  Y N 506 
PHE   OXT  O  N N 507 
PHE   H    H  N N 508 
PHE   H2   H  N N 509 
PHE   HA   H  N N 510 
PHE   HB2  H  N N 511 
PHE   HB3  H  N N 512 
PHE   HD1  H  N N 513 
PHE   HD2  H  N N 514 
PHE   HE1  H  N N 515 
PHE   HE2  H  N N 516 
PHE   HZ   H  N N 517 
PHE   HXT  H  N N 518 
PRO   N    N  N N 519 
PRO   CA   C  N S 520 
PRO   C    C  N N 521 
PRO   O    O  N N 522 
PRO   CB   C  N N 523 
PRO   CG   C  N N 524 
PRO   CD   C  N N 525 
PRO   OXT  O  N N 526 
PRO   H    H  N N 527 
PRO   HA   H  N N 528 
PRO   HB2  H  N N 529 
PRO   HB3  H  N N 530 
PRO   HG2  H  N N 531 
PRO   HG3  H  N N 532 
PRO   HD2  H  N N 533 
PRO   HD3  H  N N 534 
PRO   HXT  H  N N 535 
SER   N    N  N N 536 
SER   CA   C  N S 537 
SER   C    C  N N 538 
SER   O    O  N N 539 
SER   CB   C  N N 540 
SER   OG   O  N N 541 
SER   OXT  O  N N 542 
SER   H    H  N N 543 
SER   H2   H  N N 544 
SER   HA   H  N N 545 
SER   HB2  H  N N 546 
SER   HB3  H  N N 547 
SER   HG   H  N N 548 
SER   HXT  H  N N 549 
THR   N    N  N N 550 
THR   CA   C  N S 551 
THR   C    C  N N 552 
THR   O    O  N N 553 
THR   CB   C  N R 554 
THR   OG1  O  N N 555 
THR   CG2  C  N N 556 
THR   OXT  O  N N 557 
THR   H    H  N N 558 
THR   H2   H  N N 559 
THR   HA   H  N N 560 
THR   HB   H  N N 561 
THR   HG1  H  N N 562 
THR   HG21 H  N N 563 
THR   HG22 H  N N 564 
THR   HG23 H  N N 565 
THR   HXT  H  N N 566 
TRP   N    N  N N 567 
TRP   CA   C  N S 568 
TRP   C    C  N N 569 
TRP   O    O  N N 570 
TRP   CB   C  N N 571 
TRP   CG   C  Y N 572 
TRP   CD1  C  Y N 573 
TRP   CD2  C  Y N 574 
TRP   NE1  N  Y N 575 
TRP   CE2  C  Y N 576 
TRP   CE3  C  Y N 577 
TRP   CZ2  C  Y N 578 
TRP   CZ3  C  Y N 579 
TRP   CH2  C  Y N 580 
TRP   OXT  O  N N 581 
TRP   H    H  N N 582 
TRP   H2   H  N N 583 
TRP   HA   H  N N 584 
TRP   HB2  H  N N 585 
TRP   HB3  H  N N 586 
TRP   HD1  H  N N 587 
TRP   HE1  H  N N 588 
TRP   HE3  H  N N 589 
TRP   HZ2  H  N N 590 
TRP   HZ3  H  N N 591 
TRP   HH2  H  N N 592 
TRP   HXT  H  N N 593 
TYR   N    N  N N 594 
TYR   CA   C  N S 595 
TYR   C    C  N N 596 
TYR   O    O  N N 597 
TYR   CB   C  N N 598 
TYR   CG   C  Y N 599 
TYR   CD1  C  Y N 600 
TYR   CD2  C  Y N 601 
TYR   CE1  C  Y N 602 
TYR   CE2  C  Y N 603 
TYR   CZ   C  Y N 604 
TYR   OH   O  N N 605 
TYR   OXT  O  N N 606 
TYR   H    H  N N 607 
TYR   H2   H  N N 608 
TYR   HA   H  N N 609 
TYR   HB2  H  N N 610 
TYR   HB3  H  N N 611 
TYR   HD1  H  N N 612 
TYR   HD2  H  N N 613 
TYR   HE1  H  N N 614 
TYR   HE2  H  N N 615 
TYR   HH   H  N N 616 
TYR   HXT  H  N N 617 
VAL   N    N  N N 618 
VAL   CA   C  N S 619 
VAL   C    C  N N 620 
VAL   O    O  N N 621 
VAL   CB   C  N N 622 
VAL   CG1  C  N N 623 
VAL   CG2  C  N N 624 
VAL   OXT  O  N N 625 
VAL   H    H  N N 626 
VAL   H2   H  N N 627 
VAL   HA   H  N N 628 
VAL   HB   H  N N 629 
VAL   HG11 H  N N 630 
VAL   HG12 H  N N 631 
VAL   HG13 H  N N 632 
VAL   HG21 H  N N 633 
VAL   HG22 H  N N 634 
VAL   HG23 H  N N 635 
VAL   HXT  H  N N 636 
ZN    ZN   ZN N N 637 
# 
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 
A1IJX O19 C11  doub N N 1   
A1IJX C23 C03  sing N N 2   
A1IJX N04 C03  sing N N 3   
A1IJX N04 C05  sing N N 4   
A1IJX C07 C06  sing N N 5   
A1IJX C07 C08  sing N N 6   
A1IJX C06 N10  sing N N 7   
A1IJX C06 C05  sing N N 8   
A1IJX N13 C12  sing N N 9   
A1IJX C11 N10  sing N N 10  
A1IJX C11 C12  sing N N 11  
A1IJX O21 C20  doub N N 12  
A1IJX C03 C02  sing N N 13  
A1IJX N10 C09  sing N N 14  
A1IJX C05 C20  sing N N 15  
A1IJX C12 C14  sing N N 16  
A1IJX C20 O22  sing N N 17  
A1IJX C08 C09  sing N N 18  
A1IJX O18 C16  doub N N 19  
A1IJX C02 O01  doub N N 20  
A1IJX C02 N24  sing N N 21  
A1IJX C14 C15  sing N N 22  
A1IJX O31 C29  doub N N 23  
A1IJX N24 C25  sing N N 24  
A1IJX N24 C28  sing N N 25  
A1IJX C25 C26  sing N N 26  
A1IJX C16 C15  sing N N 27  
A1IJX C16 O17  sing N N 28  
A1IJX C29 C28  sing N N 29  
A1IJX C29 O30  sing N N 30  
A1IJX C28 C27  sing N N 31  
A1IJX C26 C27  sing N N 32  
A1IJX C03 H1   sing N N 33  
A1IJX N04 H2   sing N N 34  
A1IJX C05 H4   sing N N 35  
A1IJX C06 H5   sing N N 36  
A1IJX C07 H6   sing N N 37  
A1IJX C07 H7   sing N N 38  
A1IJX C08 H8   sing N N 39  
A1IJX C08 H9   sing N N 40  
A1IJX C09 H10  sing N N 41  
A1IJX C09 H11  sing N N 42  
A1IJX C12 H12  sing N N 43  
A1IJX N13 H13  sing N N 44  
A1IJX N13 H14  sing N N 45  
A1IJX C14 H16  sing N N 46  
A1IJX C14 H17  sing N N 47  
A1IJX C15 H18  sing N N 48  
A1IJX C15 H19  sing N N 49  
A1IJX O17 H20  sing N N 50  
A1IJX O22 H21  sing N N 51  
A1IJX C23 H22  sing N N 52  
A1IJX C23 H23  sing N N 53  
A1IJX C23 H24  sing N N 54  
A1IJX C25 H25  sing N N 55  
A1IJX C25 H26  sing N N 56  
A1IJX C26 H27  sing N N 57  
A1IJX C26 H28  sing N N 58  
A1IJX C27 H29  sing N N 59  
A1IJX C27 H30  sing N N 60  
A1IJX C28 H31  sing N N 61  
A1IJX O30 H32  sing N N 62  
ALA   N   CA   sing N N 63  
ALA   N   H    sing N N 64  
ALA   N   H2   sing N N 65  
ALA   CA  C    sing N N 66  
ALA   CA  CB   sing N N 67  
ALA   CA  HA   sing N N 68  
ALA   C   O    doub N N 69  
ALA   C   OXT  sing N N 70  
ALA   CB  HB1  sing N N 71  
ALA   CB  HB2  sing N N 72  
ALA   CB  HB3  sing N N 73  
ALA   OXT HXT  sing N N 74  
ARG   N   CA   sing N N 75  
ARG   N   H    sing N N 76  
ARG   N   H2   sing N N 77  
ARG   CA  C    sing N N 78  
ARG   CA  CB   sing N N 79  
ARG   CA  HA   sing N N 80  
ARG   C   O    doub N N 81  
ARG   C   OXT  sing N N 82  
ARG   CB  CG   sing N N 83  
ARG   CB  HB2  sing N N 84  
ARG   CB  HB3  sing N N 85  
ARG   CG  CD   sing N N 86  
ARG   CG  HG2  sing N N 87  
ARG   CG  HG3  sing N N 88  
ARG   CD  NE   sing N N 89  
ARG   CD  HD2  sing N N 90  
ARG   CD  HD3  sing N N 91  
ARG   NE  CZ   sing N N 92  
ARG   NE  HE   sing N N 93  
ARG   CZ  NH1  sing N N 94  
ARG   CZ  NH2  doub N N 95  
ARG   NH1 HH11 sing N N 96  
ARG   NH1 HH12 sing N N 97  
ARG   NH2 HH21 sing N N 98  
ARG   NH2 HH22 sing N N 99  
ARG   OXT HXT  sing N N 100 
ASN   N   CA   sing N N 101 
ASN   N   H    sing N N 102 
ASN   N   H2   sing N N 103 
ASN   CA  C    sing N N 104 
ASN   CA  CB   sing N N 105 
ASN   CA  HA   sing N N 106 
ASN   C   O    doub N N 107 
ASN   C   OXT  sing N N 108 
ASN   CB  CG   sing N N 109 
ASN   CB  HB2  sing N N 110 
ASN   CB  HB3  sing N N 111 
ASN   CG  OD1  doub N N 112 
ASN   CG  ND2  sing N N 113 
ASN   ND2 HD21 sing N N 114 
ASN   ND2 HD22 sing N N 115 
ASN   OXT HXT  sing N N 116 
ASP   N   CA   sing N N 117 
ASP   N   H    sing N N 118 
ASP   N   H2   sing N N 119 
ASP   CA  C    sing N N 120 
ASP   CA  CB   sing N N 121 
ASP   CA  HA   sing N N 122 
ASP   C   O    doub N N 123 
ASP   C   OXT  sing N N 124 
ASP   CB  CG   sing N N 125 
ASP   CB  HB2  sing N N 126 
ASP   CB  HB3  sing N N 127 
ASP   CG  OD1  doub N N 128 
ASP   CG  OD2  sing N N 129 
ASP   OD2 HD2  sing N N 130 
ASP   OXT HXT  sing N N 131 
BMA   C1  C2   sing N N 132 
BMA   C1  O1   sing N N 133 
BMA   C1  O5   sing N N 134 
BMA   C1  H1   sing N N 135 
BMA   C2  C3   sing N N 136 
BMA   C2  O2   sing N N 137 
BMA   C2  H2   sing N N 138 
BMA   C3  C4   sing N N 139 
BMA   C3  O3   sing N N 140 
BMA   C3  H3   sing N N 141 
BMA   C4  C5   sing N N 142 
BMA   C4  O4   sing N N 143 
BMA   C4  H4   sing N N 144 
BMA   C5  C6   sing N N 145 
BMA   C5  O5   sing N N 146 
BMA   C5  H5   sing N N 147 
BMA   C6  O6   sing N N 148 
BMA   C6  H61  sing N N 149 
BMA   C6  H62  sing N N 150 
BMA   O1  HO1  sing N N 151 
BMA   O2  HO2  sing N N 152 
BMA   O3  HO3  sing N N 153 
BMA   O4  HO4  sing N N 154 
BMA   O6  HO6  sing N N 155 
CYS   N   CA   sing N N 156 
CYS   N   H    sing N N 157 
CYS   N   H2   sing N N 158 
CYS   CA  C    sing N N 159 
CYS   CA  CB   sing N N 160 
CYS   CA  HA   sing N N 161 
CYS   C   O    doub N N 162 
CYS   C   OXT  sing N N 163 
CYS   CB  SG   sing N N 164 
CYS   CB  HB2  sing N N 165 
CYS   CB  HB3  sing N N 166 
CYS   SG  HG   sing N N 167 
CYS   OXT HXT  sing N N 168 
FUC   C1  C2   sing N N 169 
FUC   C1  O1   sing N N 170 
FUC   C1  O5   sing N N 171 
FUC   C1  H1   sing N N 172 
FUC   C2  C3   sing N N 173 
FUC   C2  O2   sing N N 174 
FUC   C2  H2   sing N N 175 
FUC   C3  C4   sing N N 176 
FUC   C3  O3   sing N N 177 
FUC   C3  H3   sing N N 178 
FUC   C4  C5   sing N N 179 
FUC   C4  O4   sing N N 180 
FUC   C4  H4   sing N N 181 
FUC   C5  C6   sing N N 182 
FUC   C5  O5   sing N N 183 
FUC   C5  H5   sing N N 184 
FUC   C6  H61  sing N N 185 
FUC   C6  H62  sing N N 186 
FUC   C6  H63  sing N N 187 
FUC   O1  HO1  sing N N 188 
FUC   O2  HO2  sing N N 189 
FUC   O3  HO3  sing N N 190 
FUC   O4  HO4  sing N N 191 
GLN   N   CA   sing N N 192 
GLN   N   H    sing N N 193 
GLN   N   H2   sing N N 194 
GLN   CA  C    sing N N 195 
GLN   CA  CB   sing N N 196 
GLN   CA  HA   sing N N 197 
GLN   C   O    doub N N 198 
GLN   C   OXT  sing N N 199 
GLN   CB  CG   sing N N 200 
GLN   CB  HB2  sing N N 201 
GLN   CB  HB3  sing N N 202 
GLN   CG  CD   sing N N 203 
GLN   CG  HG2  sing N N 204 
GLN   CG  HG3  sing N N 205 
GLN   CD  OE1  doub N N 206 
GLN   CD  NE2  sing N N 207 
GLN   NE2 HE21 sing N N 208 
GLN   NE2 HE22 sing N N 209 
GLN   OXT HXT  sing N N 210 
GLU   N   CA   sing N N 211 
GLU   N   H    sing N N 212 
GLU   N   H2   sing N N 213 
GLU   CA  C    sing N N 214 
GLU   CA  CB   sing N N 215 
GLU   CA  HA   sing N N 216 
GLU   C   O    doub N N 217 
GLU   C   OXT  sing N N 218 
GLU   CB  CG   sing N N 219 
GLU   CB  HB2  sing N N 220 
GLU   CB  HB3  sing N N 221 
GLU   CG  CD   sing N N 222 
GLU   CG  HG2  sing N N 223 
GLU   CG  HG3  sing N N 224 
GLU   CD  OE1  doub N N 225 
GLU   CD  OE2  sing N N 226 
GLU   OE2 HE2  sing N N 227 
GLU   OXT HXT  sing N N 228 
GLY   N   CA   sing N N 229 
GLY   N   H    sing N N 230 
GLY   N   H2   sing N N 231 
GLY   CA  C    sing N N 232 
GLY   CA  HA2  sing N N 233 
GLY   CA  HA3  sing N N 234 
GLY   C   O    doub N N 235 
GLY   C   OXT  sing N N 236 
GLY   OXT HXT  sing N N 237 
HIS   N   CA   sing N N 238 
HIS   N   H    sing N N 239 
HIS   N   H2   sing N N 240 
HIS   CA  C    sing N N 241 
HIS   CA  CB   sing N N 242 
HIS   CA  HA   sing N N 243 
HIS   C   O    doub N N 244 
HIS   C   OXT  sing N N 245 
HIS   CB  CG   sing N N 246 
HIS   CB  HB2  sing N N 247 
HIS   CB  HB3  sing N N 248 
HIS   CG  ND1  sing Y N 249 
HIS   CG  CD2  doub Y N 250 
HIS   ND1 CE1  doub Y N 251 
HIS   ND1 HD1  sing N N 252 
HIS   CD2 NE2  sing Y N 253 
HIS   CD2 HD2  sing N N 254 
HIS   CE1 NE2  sing Y N 255 
HIS   CE1 HE1  sing N N 256 
HIS   NE2 HE2  sing N N 257 
HIS   OXT HXT  sing N N 258 
HOH   O   H1   sing N N 259 
HOH   O   H2   sing N N 260 
ILE   N   CA   sing N N 261 
ILE   N   H    sing N N 262 
ILE   N   H2   sing N N 263 
ILE   CA  C    sing N N 264 
ILE   CA  CB   sing N N 265 
ILE   CA  HA   sing N N 266 
ILE   C   O    doub N N 267 
ILE   C   OXT  sing N N 268 
ILE   CB  CG1  sing N N 269 
ILE   CB  CG2  sing N N 270 
ILE   CB  HB   sing N N 271 
ILE   CG1 CD1  sing N N 272 
ILE   CG1 HG12 sing N N 273 
ILE   CG1 HG13 sing N N 274 
ILE   CG2 HG21 sing N N 275 
ILE   CG2 HG22 sing N N 276 
ILE   CG2 HG23 sing N N 277 
ILE   CD1 HD11 sing N N 278 
ILE   CD1 HD12 sing N N 279 
ILE   CD1 HD13 sing N N 280 
ILE   OXT HXT  sing N N 281 
LEU   N   CA   sing N N 282 
LEU   N   H    sing N N 283 
LEU   N   H2   sing N N 284 
LEU   CA  C    sing N N 285 
LEU   CA  CB   sing N N 286 
LEU   CA  HA   sing N N 287 
LEU   C   O    doub N N 288 
LEU   C   OXT  sing N N 289 
LEU   CB  CG   sing N N 290 
LEU   CB  HB2  sing N N 291 
LEU   CB  HB3  sing N N 292 
LEU   CG  CD1  sing N N 293 
LEU   CG  CD2  sing N N 294 
LEU   CG  HG   sing N N 295 
LEU   CD1 HD11 sing N N 296 
LEU   CD1 HD12 sing N N 297 
LEU   CD1 HD13 sing N N 298 
LEU   CD2 HD21 sing N N 299 
LEU   CD2 HD22 sing N N 300 
LEU   CD2 HD23 sing N N 301 
LEU   OXT HXT  sing N N 302 
LYS   N   CA   sing N N 303 
LYS   N   H    sing N N 304 
LYS   N   H2   sing N N 305 
LYS   CA  C    sing N N 306 
LYS   CA  CB   sing N N 307 
LYS   CA  HA   sing N N 308 
LYS   C   O    doub N N 309 
LYS   C   OXT  sing N N 310 
LYS   CB  CG   sing N N 311 
LYS   CB  HB2  sing N N 312 
LYS   CB  HB3  sing N N 313 
LYS   CG  CD   sing N N 314 
LYS   CG  HG2  sing N N 315 
LYS   CG  HG3  sing N N 316 
LYS   CD  CE   sing N N 317 
LYS   CD  HD2  sing N N 318 
LYS   CD  HD3  sing N N 319 
LYS   CE  NZ   sing N N 320 
LYS   CE  HE2  sing N N 321 
LYS   CE  HE3  sing N N 322 
LYS   NZ  HZ1  sing N N 323 
LYS   NZ  HZ2  sing N N 324 
LYS   NZ  HZ3  sing N N 325 
LYS   OXT HXT  sing N N 326 
MET   N   CA   sing N N 327 
MET   N   H    sing N N 328 
MET   N   H2   sing N N 329 
MET   CA  C    sing N N 330 
MET   CA  CB   sing N N 331 
MET   CA  HA   sing N N 332 
MET   C   O    doub N N 333 
MET   C   OXT  sing N N 334 
MET   CB  CG   sing N N 335 
MET   CB  HB2  sing N N 336 
MET   CB  HB3  sing N N 337 
MET   CG  SD   sing N N 338 
MET   CG  HG2  sing N N 339 
MET   CG  HG3  sing N N 340 
MET   SD  CE   sing N N 341 
MET   CE  HE1  sing N N 342 
MET   CE  HE2  sing N N 343 
MET   CE  HE3  sing N N 344 
MET   OXT HXT  sing N N 345 
NAG   C1  C2   sing N N 346 
NAG   C1  O1   sing N N 347 
NAG   C1  O5   sing N N 348 
NAG   C1  H1   sing N N 349 
NAG   C2  C3   sing N N 350 
NAG   C2  N2   sing N N 351 
NAG   C2  H2   sing N N 352 
NAG   C3  C4   sing N N 353 
NAG   C3  O3   sing N N 354 
NAG   C3  H3   sing N N 355 
NAG   C4  C5   sing N N 356 
NAG   C4  O4   sing N N 357 
NAG   C4  H4   sing N N 358 
NAG   C5  C6   sing N N 359 
NAG   C5  O5   sing N N 360 
NAG   C5  H5   sing N N 361 
NAG   C6  O6   sing N N 362 
NAG   C6  H61  sing N N 363 
NAG   C6  H62  sing N N 364 
NAG   C7  C8   sing N N 365 
NAG   C7  N2   sing N N 366 
NAG   C7  O7   doub N N 367 
NAG   C8  H81  sing N N 368 
NAG   C8  H82  sing N N 369 
NAG   C8  H83  sing N N 370 
NAG   N2  HN2  sing N N 371 
NAG   O1  HO1  sing N N 372 
NAG   O3  HO3  sing N N 373 
NAG   O4  HO4  sing N N 374 
NAG   O6  HO6  sing N N 375 
P33   O22 C21  sing N N 376 
P33   O22 H22  sing N N 377 
P33   C21 C20  sing N N 378 
P33   C21 H211 sing N N 379 
P33   C21 H212 sing N N 380 
P33   C20 O19  sing N N 381 
P33   C20 H201 sing N N 382 
P33   C20 H202 sing N N 383 
P33   O19 C18  sing N N 384 
P33   C18 C17  sing N N 385 
P33   C18 H181 sing N N 386 
P33   C18 H182 sing N N 387 
P33   C17 O16  sing N N 388 
P33   C17 H171 sing N N 389 
P33   C17 H172 sing N N 390 
P33   O16 C15  sing N N 391 
P33   C15 C14  sing N N 392 
P33   C15 H151 sing N N 393 
P33   C15 H152 sing N N 394 
P33   C14 O13  sing N N 395 
P33   C14 H141 sing N N 396 
P33   C14 H142 sing N N 397 
P33   O13 C12  sing N N 398 
P33   C12 C11  sing N N 399 
P33   C12 H121 sing N N 400 
P33   C12 H122 sing N N 401 
P33   C11 O10  sing N N 402 
P33   C11 H111 sing N N 403 
P33   C11 H112 sing N N 404 
P33   O10 C9   sing N N 405 
P33   C9  C8   sing N N 406 
P33   C9  H91  sing N N 407 
P33   C9  H92  sing N N 408 
P33   C8  O7   sing N N 409 
P33   C8  H81  sing N N 410 
P33   C8  H82  sing N N 411 
P33   O7  C6   sing N N 412 
P33   C6  C5   sing N N 413 
P33   C6  H61  sing N N 414 
P33   C6  H62  sing N N 415 
P33   C5  O4   sing N N 416 
P33   C5  H51  sing N N 417 
P33   C5  H52  sing N N 418 
P33   O4  C3   sing N N 419 
P33   C3  C2   sing N N 420 
P33   C3  H31  sing N N 421 
P33   C3  H32  sing N N 422 
P33   C2  O1   sing N N 423 
P33   C2  H21  sing N N 424 
P33   C2  H22A sing N N 425 
P33   O1  HO1  sing N N 426 
PG4   O1  C1   sing N N 427 
PG4   O1  HO1  sing N N 428 
PG4   C1  C2   sing N N 429 
PG4   C1  H11  sing N N 430 
PG4   C1  H12  sing N N 431 
PG4   C2  O2   sing N N 432 
PG4   C2  H21  sing N N 433 
PG4   C2  H22  sing N N 434 
PG4   O2  C3   sing N N 435 
PG4   C3  C4   sing N N 436 
PG4   C3  H31  sing N N 437 
PG4   C3  H32  sing N N 438 
PG4   C4  O3   sing N N 439 
PG4   C4  H41  sing N N 440 
PG4   C4  H42  sing N N 441 
PG4   O3  C5   sing N N 442 
PG4   C5  C6   sing N N 443 
PG4   C5  H51  sing N N 444 
PG4   C5  H52  sing N N 445 
PG4   C6  O4   sing N N 446 
PG4   C6  H61  sing N N 447 
PG4   C6  H62  sing N N 448 
PG4   O4  C7   sing N N 449 
PG4   C7  C8   sing N N 450 
PG4   C7  H71  sing N N 451 
PG4   C7  H72  sing N N 452 
PG4   C8  O5   sing N N 453 
PG4   C8  H81  sing N N 454 
PG4   C8  H82  sing N N 455 
PG4   O5  HO5  sing N N 456 
PGE   C1  O1   sing N N 457 
PGE   C1  C2   sing N N 458 
PGE   C1  H1   sing N N 459 
PGE   C1  H12  sing N N 460 
PGE   O1  HO1  sing N N 461 
PGE   C2  O2   sing N N 462 
PGE   C2  H2   sing N N 463 
PGE   C2  H22  sing N N 464 
PGE   O2  C3   sing N N 465 
PGE   C3  C4   sing N N 466 
PGE   C3  H3   sing N N 467 
PGE   C3  H32  sing N N 468 
PGE   C4  O3   sing N N 469 
PGE   C4  H4   sing N N 470 
PGE   C4  H42  sing N N 471 
PGE   O4  C6   sing N N 472 
PGE   O4  HO4  sing N N 473 
PGE   C6  C5   sing N N 474 
PGE   C6  H6   sing N N 475 
PGE   C6  H62  sing N N 476 
PGE   C5  O3   sing N N 477 
PGE   C5  H5   sing N N 478 
PGE   C5  H52  sing N N 479 
PHE   N   CA   sing N N 480 
PHE   N   H    sing N N 481 
PHE   N   H2   sing N N 482 
PHE   CA  C    sing N N 483 
PHE   CA  CB   sing N N 484 
PHE   CA  HA   sing N N 485 
PHE   C   O    doub N N 486 
PHE   C   OXT  sing N N 487 
PHE   CB  CG   sing N N 488 
PHE   CB  HB2  sing N N 489 
PHE   CB  HB3  sing N N 490 
PHE   CG  CD1  doub Y N 491 
PHE   CG  CD2  sing Y N 492 
PHE   CD1 CE1  sing Y N 493 
PHE   CD1 HD1  sing N N 494 
PHE   CD2 CE2  doub Y N 495 
PHE   CD2 HD2  sing N N 496 
PHE   CE1 CZ   doub Y N 497 
PHE   CE1 HE1  sing N N 498 
PHE   CE2 CZ   sing Y N 499 
PHE   CE2 HE2  sing N N 500 
PHE   CZ  HZ   sing N N 501 
PHE   OXT HXT  sing N N 502 
PRO   N   CA   sing N N 503 
PRO   N   CD   sing N N 504 
PRO   N   H    sing N N 505 
PRO   CA  C    sing N N 506 
PRO   CA  CB   sing N N 507 
PRO   CA  HA   sing N N 508 
PRO   C   O    doub N N 509 
PRO   C   OXT  sing N N 510 
PRO   CB  CG   sing N N 511 
PRO   CB  HB2  sing N N 512 
PRO   CB  HB3  sing N N 513 
PRO   CG  CD   sing N N 514 
PRO   CG  HG2  sing N N 515 
PRO   CG  HG3  sing N N 516 
PRO   CD  HD2  sing N N 517 
PRO   CD  HD3  sing N N 518 
PRO   OXT HXT  sing N N 519 
SER   N   CA   sing N N 520 
SER   N   H    sing N N 521 
SER   N   H2   sing N N 522 
SER   CA  C    sing N N 523 
SER   CA  CB   sing N N 524 
SER   CA  HA   sing N N 525 
SER   C   O    doub N N 526 
SER   C   OXT  sing N N 527 
SER   CB  OG   sing N N 528 
SER   CB  HB2  sing N N 529 
SER   CB  HB3  sing N N 530 
SER   OG  HG   sing N N 531 
SER   OXT HXT  sing N N 532 
THR   N   CA   sing N N 533 
THR   N   H    sing N N 534 
THR   N   H2   sing N N 535 
THR   CA  C    sing N N 536 
THR   CA  CB   sing N N 537 
THR   CA  HA   sing N N 538 
THR   C   O    doub N N 539 
THR   C   OXT  sing N N 540 
THR   CB  OG1  sing N N 541 
THR   CB  CG2  sing N N 542 
THR   CB  HB   sing N N 543 
THR   OG1 HG1  sing N N 544 
THR   CG2 HG21 sing N N 545 
THR   CG2 HG22 sing N N 546 
THR   CG2 HG23 sing N N 547 
THR   OXT HXT  sing N N 548 
TRP   N   CA   sing N N 549 
TRP   N   H    sing N N 550 
TRP   N   H2   sing N N 551 
TRP   CA  C    sing N N 552 
TRP   CA  CB   sing N N 553 
TRP   CA  HA   sing N N 554 
TRP   C   O    doub N N 555 
TRP   C   OXT  sing N N 556 
TRP   CB  CG   sing N N 557 
TRP   CB  HB2  sing N N 558 
TRP   CB  HB3  sing N N 559 
TRP   CG  CD1  doub Y N 560 
TRP   CG  CD2  sing Y N 561 
TRP   CD1 NE1  sing Y N 562 
TRP   CD1 HD1  sing N N 563 
TRP   CD2 CE2  doub Y N 564 
TRP   CD2 CE3  sing Y N 565 
TRP   NE1 CE2  sing Y N 566 
TRP   NE1 HE1  sing N N 567 
TRP   CE2 CZ2  sing Y N 568 
TRP   CE3 CZ3  doub Y N 569 
TRP   CE3 HE3  sing N N 570 
TRP   CZ2 CH2  doub Y N 571 
TRP   CZ2 HZ2  sing N N 572 
TRP   CZ3 CH2  sing Y N 573 
TRP   CZ3 HZ3  sing N N 574 
TRP   CH2 HH2  sing N N 575 
TRP   OXT HXT  sing N N 576 
TYR   N   CA   sing N N 577 
TYR   N   H    sing N N 578 
TYR   N   H2   sing N N 579 
TYR   CA  C    sing N N 580 
TYR   CA  CB   sing N N 581 
TYR   CA  HA   sing N N 582 
TYR   C   O    doub N N 583 
TYR   C   OXT  sing N N 584 
TYR   CB  CG   sing N N 585 
TYR   CB  HB2  sing N N 586 
TYR   CB  HB3  sing N N 587 
TYR   CG  CD1  doub Y N 588 
TYR   CG  CD2  sing Y N 589 
TYR   CD1 CE1  sing Y N 590 
TYR   CD1 HD1  sing N N 591 
TYR   CD2 CE2  doub Y N 592 
TYR   CD2 HD2  sing N N 593 
TYR   CE1 CZ   doub Y N 594 
TYR   CE1 HE1  sing N N 595 
TYR   CE2 CZ   sing Y N 596 
TYR   CE2 HE2  sing N N 597 
TYR   CZ  OH   sing N N 598 
TYR   OH  HH   sing N N 599 
TYR   OXT HXT  sing N N 600 
VAL   N   CA   sing N N 601 
VAL   N   H    sing N N 602 
VAL   N   H2   sing N N 603 
VAL   CA  C    sing N N 604 
VAL   CA  CB   sing N N 605 
VAL   CA  HA   sing N N 606 
VAL   C   O    doub N N 607 
VAL   C   OXT  sing N N 608 
VAL   CB  CG1  sing N N 609 
VAL   CB  CG2  sing N N 610 
VAL   CB  HB   sing N N 611 
VAL   CG1 HG11 sing N N 612 
VAL   CG1 HG12 sing N N 613 
VAL   CG1 HG13 sing N N 614 
VAL   CG2 HG21 sing N N 615 
VAL   CG2 HG22 sing N N 616 
VAL   CG2 HG23 sing N N 617 
VAL   OXT HXT  sing N N 618 
# 
_pdbx_audit_support.funding_organization   'Biotechnology and Biological Sciences Research Council (BBSRC)' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           BB/X001032/1 
_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 
2 NAG 1 n 
2 NAG 2 n 
3 NAG 1 n 
3 FUC 2 n 
4 NAG 1 n 
4 NAG 2 n 
4 BMA 3 n 
4 FUC 4 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   6F9V 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GBR 
_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]   0.013689 
_atom_sites.fract_transf_matrix[1][2]   -0.003688 
_atom_sites.fract_transf_matrix[1][3]   -0.006976 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013385 
_atom_sites.fract_transf_matrix[2][3]   0.001306 
_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]   0.013447 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.pdbx_scat_Z 
_atom_type.pdbx_N_electrons 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
C  6  6  2.3103  20.8439 1.0201 10.2075 1.5888 0.5687  0.8651 51.6512 0.2156   
CL 17 17 11.4601 0.0104  7.1962 1.1662  6.2554 18.5194 1.6455 47.7784 -9.3453  
N  7  7  12.2220 0.0057  3.1346 9.8933  2.0141 28.9975 1.1672 0.5826  -11.5379 
O  8  8  3.0487  13.2771 2.2870 5.7011  1.5464 0.3239  0.8671 32.9089 0.2508   
S  16 16 6.9054  1.4679  5.2035 22.2151 1.4379 0.2536  1.5863 56.1720 1.0486   
ZN 30 30 14.0812 3.2655  7.0352 0.2333  5.1677 10.3163 2.4112 58.7097 1.0042   
# 
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_site.pdbx_tls_group_id 
ATOM   1     N  N   . LEU   A 1  1   ? -32.235 -17.069 -26.222 1    41.191  ? 1    LEU   A N   1 1 
ATOM   2     C  CA  . LEU   A 1  1   ? -31.427 -18.31  -26.219 1    38.081  ? 1    LEU   A CA  1 1 
ATOM   3     C  C   . LEU   A 1  1   ? -32.211 -19.381 -26.956 1    39.495  ? 1    LEU   A C   1 1 
ATOM   4     O  O   . LEU   A 1  1   ? -33.431 -19.501 -26.791 1    38.928  ? 1    LEU   A O   1 1 
ATOM   5     C  CB  . LEU   A 1  1   ? -31.186 -18.616 -24.741 1    38.092  ? 1    LEU   A CB  1 1 
ATOM   6     C  CG  . LEU   A 1  1   ? -30.245 -19.769 -24.412 1    36.607  ? 1    LEU   A CG  1 1 
ATOM   7     C  CD1 . LEU   A 1  1   ? -28.9   -19.556 -25.079 1    34.473  ? 1    LEU   A CD1 1 1 
ATOM   8     C  CD2 . LEU   A 1  1   ? -30.135 -19.933 -22.891 1    35.076  ? 1    LEU   A CD2 1 1 
ATOM   9     N  N   . ASP   A 1  2   ? -31.529 -20.06  -27.884 1    39.393  ? 2    ASP   A N   1 1 
ATOM   10    C  CA  . ASP   A 1  2   ? -32.191 -21.071 -28.698 1    43.096  ? 2    ASP   A CA  1 1 
ATOM   11    C  C   . ASP   A 1  2   ? -32.862 -22.099 -27.787 1    40.87   ? 2    ASP   A C   1 1 
ATOM   12    O  O   . ASP   A 1  2   ? -32.269 -22.49  -26.785 1    37.594  ? 2    ASP   A O   1 1 
ATOM   13    C  CB  . ASP   A 1  2   ? -31.213 -21.759 -29.638 1    50.197  ? 2    ASP   A CB  1 1 
ATOM   14    C  CG  . ASP   A 1  2   ? -31.896 -22.68  -30.632 1    59.214  ? 2    ASP   A CG  1 1 
ATOM   15    O  OD1 . ASP   A 1  2   ? -32.605 -22.145 -31.522 1    68.75   ? 2    ASP   A OD1 1 1 
ATOM   16    O  OD2 . ASP   A 1  2   ? -31.795 -23.917 -30.452 1    64.73   ? 2    ASP   A OD2 1 1 
ATOM   17    N  N   . PRO   A 1  3   ? -34.098 -22.577 -28.075 1    41.308  ? 3    PRO   A N   1 1 
ATOM   18    C  CA  . PRO   A 1  3   ? -34.748 -23.575 -27.213 1    42.398  ? 3    PRO   A CA  1 1 
ATOM   19    C  C   . PRO   A 1  3   ? -33.897 -24.789 -26.828 1    42.294  ? 3    PRO   A C   1 1 
ATOM   20    O  O   . PRO   A 1  3   ? -33.844 -25.157 -25.651 1    41.156  ? 3    PRO   A O   1 1 
ATOM   21    C  CB  . PRO   A 1  3   ? -36.024 -23.964 -27.977 1    43.117  ? 3    PRO   A CB  1 1 
ATOM   22    C  CG  . PRO   A 1  3   ? -36.314 -22.764 -28.857 1    43.307  ? 3    PRO   A CG  1 1 
ATOM   23    C  CD  . PRO   A 1  3   ? -34.92  -22.273 -29.267 1    43.455  ? 3    PRO   A CD  1 1 
ATOM   24    N  N   . GLY   A 1  4   ? -33.205 -25.384 -27.818 1    41.798  ? 4    GLY   A N   1 1 
ATOM   25    C  CA  . GLY   A 1  4   ? -32.288 -26.482 -27.559 1    41.59   ? 4    GLY   A CA  1 1 
ATOM   26    C  C   . GLY   A 1  4   ? -31.111 -26.089 -26.673 1    41.092  ? 4    GLY   A C   1 1 
ATOM   27    O  O   . GLY   A 1  4   ? -30.333 -26.951 -26.269 1    42.14   ? 4    GLY   A O   1 1 
ATOM   28    N  N   . LEU   A 1  5   ? -30.943 -24.792 -26.359 1    38.166  ? 5    LEU   A N   1 1 
ATOM   29    C  CA  . LEU   A 1  5   ? -29.799 -24.421 -25.534 1    36.257  ? 5    LEU   A CA  1 1 
ATOM   30    C  C   . LEU   A 1  5   ? -30.229 -24.121 -24.099 1    33.691  ? 5    LEU   A C   1 1 
ATOM   31    O  O   . LEU   A 1  5   ? -29.39  -23.852 -23.235 1    31.632  ? 5    LEU   A O   1 1 
ATOM   32    C  CB  . LEU   A 1  5   ? -28.993 -23.246 -26.111 1    37.554  ? 5    LEU   A CB  1 1 
ATOM   33    C  CG  . LEU   A 1  5   ? -28.229 -23.519 -27.417 1    39.427  ? 5    LEU   A CG  1 1 
ATOM   34    C  CD1 . LEU   A 1  5   ? -27.608 -22.269 -28.049 1    39.43   ? 5    LEU   A CD1 1 1 
ATOM   35    C  CD2 . LEU   A 1  5   ? -27.144 -24.557 -27.239 1    37.126  ? 5    LEU   A CD2 1 1 
ATOM   36    N  N   . GLN   A 1  6   ? -31.543 -24.122 -23.866 1    34.334  ? 6    GLN   A N   1 1 
ATOM   37    C  CA  . GLN   A 1  6   ? -32.077 -23.656 -22.597 1    33.239  ? 6    GLN   A CA  1 1 
ATOM   38    C  C   . GLN   A 1  6   ? -32.172 -24.821 -21.632 1    32.262  ? 6    GLN   A C   1 1 
ATOM   39    O  O   . GLN   A 1  6   ? -32.502 -25.902 -22.089 1    32.985  ? 6    GLN   A O   1 1 
ATOM   40    C  CB  . GLN   A 1  6   ? -33.524 -23.18  -22.788 1    34.218  ? 6    GLN   A CB  1 1 
ATOM   41    C  CG  . GLN   A 1  6   ? -33.625 -21.937 -23.66  1    34.692  ? 6    GLN   A CG  1 1 
ATOM   42    C  CD  . GLN   A 1  6   ? -35.045 -21.441 -23.806 1    37.595  ? 6    GLN   A CD  1 1 
ATOM   43    O  OE1 . GLN   A 1  6   ? -35.977 -21.925 -23.158 1    39.633  ? 6    GLN   A OE1 1 1 
ATOM   44    N  NE2 . GLN   A 1  6   ? -35.257 -20.52  -24.732 1    38.837  ? 6    GLN   A NE2 1 1 
ATOM   45    N  N   . PRO   A 1  7   ? -32.086 -24.601 -20.294 1    30.929  ? 7    PRO   A N   1 1 
ATOM   46    C  CA  . PRO   A 1  7   ? -32.335 -25.664 -19.315 1    31.474  ? 7    PRO   A CA  1 1 
ATOM   47    C  C   . PRO   A 1  7   ? -33.771 -26.146 -19.166 1    33.782  ? 7    PRO   A C   1 1 
ATOM   48    O  O   . PRO   A 1  7   ? -34.684 -25.326 -19.076 1    34.135  ? 7    PRO   A O   1 1 
ATOM   49    C  CB  . PRO   A 1  7   ? -31.865 -25.04  -17.982 1    30.419  ? 7    PRO   A CB  1 1 
ATOM   50    C  CG  . PRO   A 1  7   ? -32.012 -23.552 -18.162 1    29.775  ? 7    PRO   A CG  1 1 
ATOM   51    C  CD  . PRO   A 1  7   ? -31.849 -23.295 -19.65  1    29.923  ? 7    PRO   A CD  1 1 
ATOM   52    N  N   . GLY   A 1  8   ? -33.926 -27.474 -19.029 1    35.409  ? 8    GLY   A N   1 1 
ATOM   53    C  CA  . GLY   A 1  8   ? -35.18  -28.127 -18.688 1    38.103  ? 8    GLY   A CA  1 1 
ATOM   54    C  C   . GLY   A 1  8   ? -35.377 -28.158 -17.176 1    39.233  ? 8    GLY   A C   1 1 
ATOM   55    O  O   . GLY   A 1  8   ? -34.882 -27.306 -16.444 1    41.401  ? 8    GLY   A O   1 1 
ATOM   56    N  N   . GLN   A 1  9   ? -36.082 -29.171 -16.709 1    40.672  ? 9    GLN   A N   1 1 
ATOM   57    C  CA  . GLN   A 1  9   ? -36.336 -29.362 -15.297 1    41.818  ? 9    GLN   A CA  1 1 
ATOM   58    C  C   . GLN   A 1  9   ? -35.502 -30.545 -14.812 1    41.671  ? 9    GLN   A C   1 1 
ATOM   59    O  O   . GLN   A 1  9   ? -35.241 -31.499 -15.538 1    39.584  ? 9    GLN   A O   1 1 
ATOM   60    C  CB  . GLN   A 1  9   ? -37.836 -29.567 -15.023 1    44.791  ? 9    GLN   A CB  1 1 
ATOM   61    C  CG  . GLN   A 1  9   ? -38.341 -29.028 -13.679 1    47.068  ? 9    GLN   A CG  1 1 
ATOM   62    C  CD  . GLN   A 1  9   ? -37.755 -27.713 -13.158 1    48.767  ? 9    GLN   A CD  1 1 
ATOM   63    O  OE1 . GLN   A 1  9   ? -37.481 -26.703 -13.857 1    45.583  ? 9    GLN   A OE1 1 1 
ATOM   64    N  NE2 . GLN   A 1  9   ? -37.563 -27.736 -11.844 1    50.04   ? 9    GLN   A NE2 1 1 
ATOM   65    N  N   . PHE   A 1  10  ? -35.07  -30.401 -13.56  1    42.865  ? 10   PHE   A N   1 1 
ATOM   66    C  CA  . PHE   A 1  10  ? -34.236 -31.342 -12.835 1    42.726  ? 10   PHE   A CA  1 1 
ATOM   67    C  C   . PHE   A 1  10  ? -34.749 -31.292 -11.4   1    43.015  ? 10   PHE   A C   1 1 
ATOM   68    O  O   . PHE   A 1  10  ? -35.272 -30.281 -10.968 1    44.832  ? 10   PHE   A O   1 1 
ATOM   69    C  CB  . PHE   A 1  10  ? -32.745 -30.98  -13.001 1    39.02   ? 10   PHE   A CB  1 1 
ATOM   70    C  CG  . PHE   A 1  10  ? -32.328 -30.777 -14.451 1    38.003  ? 10   PHE   A CG  1 1 
ATOM   71    C  CD1 . PHE   A 1  10  ? -32.063 -31.863 -15.28  1    39.069  ? 10   PHE   A CD1 1 1 
ATOM   72    C  CD2 . PHE   A 1  10  ? -32.267 -29.5   -14.999 1    37.544  ? 10   PHE   A CD2 1 1 
ATOM   73    C  CE1 . PHE   A 1  10  ? -31.731 -31.676 -16.618 1    38.222  ? 10   PHE   A CE1 1 1 
ATOM   74    C  CE2 . PHE   A 1  10  ? -31.881 -29.316 -16.329 1    36.338  ? 10   PHE   A CE2 1 1 
ATOM   75    C  CZ  . PHE   A 1  10  ? -31.652 -30.395 -17.134 1    36.627  ? 10   PHE   A CZ  1 1 
ATOM   76    N  N   . SER   A 1  11  ? -34.669 -32.406 -10.689 1    44.667  ? 11   SER   A N   1 1 
ATOM   77    C  CA  . SER   A 1  11  ? -35.087 -32.437 -9.303  1    45.824  ? 11   SER   A CA  1 1 
ATOM   78    C  C   . SER   A 1  11  ? -34.07  -31.679 -8.462  1    47.246  ? 11   SER   A C   1 1 
ATOM   79    O  O   . SER   A 1  11  ? -32.931 -31.437 -8.898  1    47.81   ? 11   SER   A O   1 1 
ATOM   80    C  CB  . SER   A 1  11  ? -35.185 -33.866 -8.886  1    48.677  ? 11   SER   A CB  1 1 
ATOM   81    O  OG  . SER   A 1  11  ? -34.274 -34.579 -9.719  1    47.55   ? 11   SER   A OG  1 1 
ATOM   82    N  N   . ALA   A 1  12  ? -34.503 -31.319 -7.258  1    49.443  ? 12   ALA   A N   1 1 
ATOM   83    C  CA  . ALA   A 1  12  ? -33.786 -30.452 -6.34   1    49.964  ? 12   ALA   A CA  1 1 
ATOM   84    C  C   . ALA   A 1  12  ? -32.843 -31.272 -5.444  1    50.23   ? 12   ALA   A C   1 1 
ATOM   85    O  O   . ALA   A 1  12  ? -32.937 -31.191 -4.224  1    50.546  ? 12   ALA   A O   1 1 
ATOM   86    C  CB  . ALA   A 1  12  ? -34.828 -29.725 -5.512  1    50.159  ? 12   ALA   A CB  1 1 
ATOM   87    N  N   . ASP   A 1  13  ? -31.892 -32.009 -6.044  1    51.762  ? 13   ASP   A N   1 1 
ATOM   88    C  CA  . ASP   A 1  13  ? -31.1   -33.009 -5.337  1    50.834  ? 13   ASP   A CA  1 1 
ATOM   89    C  C   . ASP   A 1  13  ? -29.899 -33.425 -6.192  1    49.173  ? 13   ASP   A C   1 1 
ATOM   90    O  O   . ASP   A 1  13  ? -29.799 -33.036 -7.369  1    44.242  ? 13   ASP   A O   1 1 
ATOM   91    C  CB  . ASP   A 1  13  ? -31.968 -34.22  -4.996  1    56.89   ? 13   ASP   A CB  1 1 
ATOM   92    C  CG  . ASP   A 1  13  ? -32.62  -34.899 -6.197  1    61.908  ? 13   ASP   A CG  1 1 
ATOM   93    O  OD1 . ASP   A 1  13  ? -31.972 -34.953 -7.271  1    61.381  ? 13   ASP   A OD1 1 1 
ATOM   94    O  OD2 . ASP   A 1  13  ? -33.772 -35.368 -6.068  1    67.8    ? 13   ASP   A OD2 1 1 
ATOM   95    N  N   . GLU   A 1  14  ? -29.004 -34.228 -5.59   1    45.418  ? 14   GLU   A N   1 1 
ATOM   96    C  CA  . GLU   A 1  14  ? -27.754 -34.547 -6.245  1    43.771  ? 14   GLU   A CA  1 1 
ATOM   97    C  C   . GLU   A 1  14  ? -27.988 -35.386 -7.514  1    47.921  ? 14   GLU   A C   1 1 
ATOM   98    O  O   . GLU   A 1  14  ? -27.142 -35.382 -8.429  1    46.019  ? 14   GLU   A O   1 1 
ATOM   99    C  CB  . GLU   A 1  14  ? -26.803 -35.345 -5.351  1    46.03   ? 14   GLU   A CB  1 1 
ATOM   100   C  CG  . GLU   A 1  14  ? -25.449 -35.577 -6.046  1    44.194  ? 14   GLU   A CG  1 1 
ATOM   101   C  CD  . GLU   A 1  14  ? -24.151 -35.973 -5.321  1    45.999  ? 14   GLU   A CD  1 1 
ATOM   102   O  OE1 . GLU   A 1  14  ? -24.205 -36.2   -4.084  1    43.458  ? 14   GLU   A OE1 1 1 
ATOM   103   O  OE2 . GLU   A 1  14  ? -23.079 -36.013 -6.032  1    43.892  ? 14   GLU   A OE2 1 1 
ATOM   104   N  N   . ALA   A 1  15  ? -29.12  -36.129 -7.584  1    49.336  ? 15   ALA   A N   1 1 
ATOM   105   C  CA  . ALA   A 1  15  ? -29.274 -36.953 -8.78   1    50.335  ? 15   ALA   A CA  1 1 
ATOM   106   C  C   . ALA   A 1  15  ? -29.732 -36.079 -9.958  1    48.173  ? 15   ALA   A C   1 1 
ATOM   107   O  O   . ALA   A 1  15  ? -29.299 -36.288 -11.093 1    50.148  ? 15   ALA   A O   1 1 
ATOM   108   C  CB  . ALA   A 1  15  ? -30.111 -38.206 -8.554  1    49.861  ? 15   ALA   A CB  1 1 
ATOM   109   N  N   . GLY   A 1  16  ? -30.56  -35.076 -9.664  1    47.67   ? 16   GLY   A N   1 1 
ATOM   110   C  CA  . GLY   A 1  16  ? -30.924 -34.011 -10.595 1    47.452  ? 16   GLY   A CA  1 1 
ATOM   111   C  C   . GLY   A 1  16  ? -29.733 -33.164 -11.062 1    42.94   ? 16   GLY   A C   1 1 
ATOM   112   O  O   . GLY   A 1  16  ? -29.521 -32.982 -12.263 1    44.62   ? 16   GLY   A O   1 1 
ATOM   113   N  N   . ALA   A 1  17  ? -28.905 -32.693 -10.123 1    40.258  ? 17   ALA   A N   1 1 
ATOM   114   C  CA  . ALA   A 1  17  ? -27.599 -32.091 -10.437 1    35.115  ? 17   ALA   A CA  1 1 
ATOM   115   C  C   . ALA   A 1  17  ? -26.751 -32.789 -11.538 1    34.177  ? 17   ALA   A C   1 1 
ATOM   116   O  O   . ALA   A 1  17  ? -26.241 -32.074 -12.424 1    29.923  ? 17   ALA   A O   1 1 
ATOM   117   C  CB  . ALA   A 1  17  ? -26.803 -31.868 -9.178  1    32.817  ? 17   ALA   A CB  1 1 
ATOM   118   N  N   . GLN   A 1  18  ? -26.557 -34.126 -11.45  1    33.215  ? 18   GLN   A N   1 1 
ATOM   119   C  CA  . GLN   A 1  18  ? -25.789 -34.919 -12.404 1    35.852  ? 18   GLN   A CA  1 1 
ATOM   120   C  C   . GLN   A 1  18  ? -26.382 -34.864 -13.821 1    35.028  ? 18   GLN   A C   1 1 
ATOM   121   O  O   . GLN   A 1  18  ? -25.622 -34.704 -14.799 1    32.085  ? 18   GLN   A O   1 1 
ATOM   122   C  CB  . GLN   A 1  18  ? -25.868 -36.453 -12.268 1    41.389  ? 18   GLN   A CB  1 1 
ATOM   123   C  CG  . GLN   A 1  18  ? -24.835 -37.176 -11.41  1    48.797  ? 18   GLN   A CG  1 1 
ATOM   124   C  CD  . GLN   A 1  18  ? -23.383 -36.768 -11.597 1    57.323  ? 18   GLN   A CD  1 1 
ATOM   125   O  OE1 . GLN   A 1  18  ? -22.999 -36.156 -12.605 1    55.512  ? 18   GLN   A OE1 1 1 
ATOM   126   N  NE2 . GLN   A 1  18  ? -22.559 -37.118 -10.605 1    55.997  ? 18   GLN   A NE2 1 1 
ATOM   127   N  N   . LEU   A 1  19  ? -27.722 -35.072 -13.913 1    34.481  ? 19   LEU   A N   1 1 
ATOM   128   C  CA  . LEU   A 1  19  ? -28.443 -34.903 -15.172 1    35.886  ? 19   LEU   A CA  1 1 
ATOM   129   C  C   . LEU   A 1  19  ? -28.319 -33.455 -15.637 1    33.899  ? 19   LEU   A C   1 1 
ATOM   130   O  O   . LEU   A 1  19  ? -28.083 -33.199 -16.813 1    35.39   ? 19   LEU   A O   1 1 
ATOM   131   C  CB  . LEU   A 1  19  ? -29.904 -35.314 -15.015 1    38.477  ? 19   LEU   A CB  1 1 
ATOM   132   C  CG  . LEU   A 1  19  ? -30.117 -36.746 -14.512 1    41.657  ? 19   LEU   A CG  1 1 
ATOM   133   C  CD1 . LEU   A 1  19  ? -31.522 -36.919 -13.953 1    43.626  ? 19   LEU   A CD1 1 1 
ATOM   134   C  CD2 . LEU   A 1  19  ? -29.824 -37.755 -15.611 1    43.955  ? 19   LEU   A CD2 1 1 
ATOM   135   N  N   . PHE   A 1  20  ? -28.417 -32.515 -14.709 1    31.838  ? 20   PHE   A N   1 1 
ATOM   136   C  CA  . PHE   A 1  20  ? -28.252 -31.099 -15.071 1    32.511  ? 20   PHE   A CA  1 1 
ATOM   137   C  C   . PHE   A 1  20  ? -26.864 -30.802 -15.689 1    31.024  ? 20   PHE   A C   1 1 
ATOM   138   O  O   . PHE   A 1  20  ? -26.701 -30.102 -16.718 1    29.326  ? 20   PHE   A O   1 1 
ATOM   139   C  CB  . PHE   A 1  20  ? -28.384 -30.302 -13.773 1    31.71   ? 20   PHE   A CB  1 1 
ATOM   140   C  CG  . PHE   A 1  20  ? -28.189 -28.798 -13.943 1    32.495  ? 20   PHE   A CG  1 1 
ATOM   141   C  CD1 . PHE   A 1  20  ? -26.939 -28.212 -13.773 1    29.386  ? 20   PHE   A CD1 1 1 
ATOM   142   C  CD2 . PHE   A 1  20  ? -29.269 -27.959 -14.194 1    32.198  ? 20   PHE   A CD2 1 1 
ATOM   143   C  CE1 . PHE   A 1  20  ? -26.758 -26.844 -13.92  1    29.145  ? 20   PHE   A CE1 1 1 
ATOM   144   C  CE2 . PHE   A 1  20  ? -29.08  -26.583 -14.298 1    31.478  ? 20   PHE   A CE2 1 1 
ATOM   145   C  CZ  . PHE   A 1  20  ? -27.838 -26.022 -14.196 1    29.675  ? 20   PHE   A CZ  1 1 
ATOM   146   N  N   . ALA   A 1  21  ? -25.819 -31.335 -15.054 1    31.425  ? 21   ALA   A N   1 1 
ATOM   147   C  CA  . ALA   A 1  21  ? -24.482 -31.064 -15.537 1    30.246  ? 21   ALA   A CA  1 1 
ATOM   148   C  C   . ALA   A 1  21  ? -24.316 -31.726 -16.921 1    33.446  ? 21   ALA   A C   1 1 
ATOM   149   O  O   . ALA   A 1  21  ? -23.671 -31.156 -17.804 1    35.751  ? 21   ALA   A O   1 1 
ATOM   150   C  CB  . ALA   A 1  21  ? -23.544 -31.621 -14.542 1    30.184  ? 21   ALA   A CB  1 1 
ATOM   151   N  N   . GLN   A 1  22  ? -24.898 -32.907 -17.113 1    31.735  ? 22   GLN   A N   1 1 
ATOM   152   C  CA  . GLN   A 1  22  ? -24.745 -33.618 -18.372 1    36.08   ? 22   GLN   A CA  1 1 
ATOM   153   C  C   . GLN   A 1  22  ? -25.474 -32.861 -19.495 1    36.555  ? 22   GLN   A C   1 1 
ATOM   154   O  O   . GLN   A 1  22  ? -24.963 -32.736 -20.616 1    35.006  ? 22   GLN   A O   1 1 
ATOM   155   C  CB  . GLN   A 1  22  ? -25.263 -35.065 -18.291 1    41.77   ? 22   GLN   A CB  1 1 
ATOM   156   C  CG  . GLN   A 1  22  ? -24.495 -35.992 -17.343 1    45.71   ? 22   GLN   A CG  1 1 
ATOM   157   C  CD  . GLN   A 1  22  ? -25.17  -37.335 -17.11  1    53.543  ? 22   GLN   A CD  1 1 
ATOM   158   O  OE1 . GLN   A 1  22  ? -26.397 -37.458 -16.993 1    61.641  ? 22   GLN   A OE1 1 1 
ATOM   159   N  NE2 . GLN   A 1  22  ? -24.372 -38.387 -17.068 1    55.761  ? 22   GLN   A NE2 1 1 
ATOM   160   N  N   . SER   A 1  23  ? -26.701 -32.394 -19.195 1    35.153  ? 23   SER   A N   1 1 
ATOM   161   C  CA  . SER   A 1  23  ? -27.45  -31.589 -20.134 1    36.561  ? 23   SER   A CA  1 1 
ATOM   162   C  C   . SER   A 1  23  ? -26.726 -30.266 -20.432 1    34.218  ? 23   SER   A C   1 1 
ATOM   163   O  O   . SER   A 1  23  ? -26.664 -29.842 -21.591 1    35.213  ? 23   SER   A O   1 1 
ATOM   164   C  CB  . SER   A 1  23  ? -28.856 -31.386 -19.632 1    39.118  ? 23   SER   A CB  1 1 
ATOM   165   O  OG  . SER   A 1  23  ? -29.461 -30.437 -20.486 1    42.218  ? 23   SER   A OG  1 1 
ATOM   166   N  N   . TYR   A 1  24  ? -26.173 -29.611 -19.409 1    29.633  ? 24   TYR   A N   1 1 
ATOM   167   C  CA  . TYR   A 1  24  ? -25.408 -28.392 -19.62  1    30.401  ? 24   TYR   A CA  1 1 
ATOM   168   C  C   . TYR   A 1  24  ? -24.231 -28.593 -20.584 1    31.766  ? 24   TYR   A C   1 1 
ATOM   169   O  O   . TYR   A 1  24  ? -23.896 -27.69  -21.4   1    28.954  ? 24   TYR   A O   1 1 
ATOM   170   C  CB  . TYR   A 1  24  ? -24.756 -28.019 -18.283 1    27.791  ? 24   TYR   A CB  1 1 
ATOM   171   C  CG  . TYR   A 1  24  ? -23.825 -26.838 -18.34  1    28.05   ? 24   TYR   A CG  1 1 
ATOM   172   C  CD1 . TYR   A 1  24  ? -24.314 -25.542 -18.393 1    28.196  ? 24   TYR   A CD1 1 1 
ATOM   173   C  CD2 . TYR   A 1  24  ? -22.43  -27.006 -18.277 1    27.827  ? 24   TYR   A CD2 1 1 
ATOM   174   C  CE1 . TYR   A 1  24  ? -23.471 -24.44  -18.426 1    28.436  ? 24   TYR   A CE1 1 1 
ATOM   175   C  CE2 . TYR   A 1  24  ? -21.571 -25.913 -18.311 1    28.815  ? 24   TYR   A CE2 1 1 
ATOM   176   C  CZ  . TYR   A 1  24  ? -22.087 -24.629 -18.378 1    28.176  ? 24   TYR   A CZ  1 1 
ATOM   177   O  OH  . TYR   A 1  24  ? -21.268 -23.553 -18.356 1    27.452  ? 24   TYR   A OH  1 1 
ATOM   178   N  N   . GLN   A 1  25  ? -23.527 -29.742 -20.402 1    32.904  ? 25   GLN   A N   1 1 
ATOM   179   C  CA  . GLN   A 1  25  ? -22.266 -29.976 -21.097 1    36.536  ? 25   GLN   A CA  1 1 
ATOM   180   C  C   . GLN   A 1  25  ? -22.562 -30.075 -22.597 1    39.789  ? 25   GLN   A C   1 1 
ATOM   181   O  O   . GLN   A 1  25  ? -21.796 -29.633 -23.448 1    40.372  ? 25   GLN   A O   1 1 
ATOM   182   C  CB  . GLN   A 1  25  ? -21.755 -31.345 -20.623 1    39.229  ? 25   GLN   A CB  1 1 
ATOM   183   C  CG  . GLN   A 1  25  ? -21.105 -32.202 -21.709 1    44.193  ? 25   GLN   A CG  1 1 
ATOM   184   C  CD  . GLN   A 1  25  ? -19.628 -31.911 -21.866 1    49.002  ? 25   GLN   A CD  1 1 
ATOM   185   O  OE1 . GLN   A 1  25  ? -19.008 -31.309 -20.98  1    48      ? 25   GLN   A OE1 1 1 
ATOM   186   N  NE2 . GLN   A 1  25  ? -19.063 -32.334 -22.99  1    49.84   ? 25   GLN   A NE2 1 1 
ATOM   187   N  N   . SER   A 1  26  ? -23.703 -30.654 -22.913 1    39.18   ? 26   SER   A N   1 1 
ATOM   188   C  CA  . SER   A 1  26  ? -24.095 -30.793 -24.302 1    47.183  ? 26   SER   A CA  1 1 
ATOM   189   C  C   . SER   A 1  26  ? -24.296 -29.418 -24.936 1    49.022  ? 26   SER   A C   1 1 
ATOM   190   O  O   . SER   A 1  26  ? -23.929 -29.182 -26.095 1    52.943  ? 26   SER   A O   1 1 
ATOM   191   C  CB  . SER   A 1  26  ? -25.363 -31.601 -24.381 1    51.228  ? 26   SER   A CB  1 1 
ATOM   192   O  OG  . SER   A 1  26  ? -25.362 -32.553 -23.327 1    50.541  ? 26   SER   A OG  1 1 
ATOM   193   N  N   . SER   A 1  27  ? -24.927 -28.507 -24.183 1    43.182  ? 27   SER   A N   1 1 
ATOM   194   C  CA  . SER   A 1  27  ? -25.17  -27.199 -24.761 1    39.689  ? 27   SER   A CA  1 1 
ATOM   195   C  C   . SER   A 1  27  ? -23.989 -26.234 -24.57  1    35.412  ? 27   SER   A C   1 1 
ATOM   196   O  O   . SER   A 1  27  ? -23.737 -25.443 -25.475 1    36.834  ? 27   SER   A O   1 1 
ATOM   197   C  CB  . SER   A 1  27  ? -26.52  -26.645 -24.362 1    38.808  ? 27   SER   A CB  1 1 
ATOM   198   O  OG  . SER   A 1  27  ? -27.544 -27.427 -24.986 1    39.401  ? 27   SER   A OG  1 1 
ATOM   199   N  N   . ALA   A 1  28  ? -23.282 -26.29  -23.432 1    31.423  ? 28   ALA   A N   1 1 
ATOM   200   C  CA  . ALA   A 1  28  ? -22.101 -25.436 -23.231 1    32.819  ? 28   ALA   A CA  1 1 
ATOM   201   C  C   . ALA   A 1  28  ? -21.072 -25.531 -24.367 1    33.541  ? 28   ALA   A C   1 1 
ATOM   202   O  O   . ALA   A 1  28  ? -20.437 -24.524 -24.665 1    32.967  ? 28   ALA   A O   1 1 
ATOM   203   C  CB  . ALA   A 1  28  ? -21.414 -25.681 -21.916 1    28.764  ? 28   ALA   A CB  1 1 
ATOM   204   N  N   . GLU   A 1  29  ? -20.835 -26.718 -24.962 1    32.243  ? 29   GLU   A N   1 1 
ATOM   205   C  CA  . GLU   A 1  29  ? -19.718 -26.797 -25.892 1    31.703  ? 29   GLU   A CA  1 1 
ATOM   206   C  C   . GLU   A 1  29  ? -20.127 -26.064 -27.17  1    33.323  ? 29   GLU   A C   1 1 
ATOM   207   O  O   . GLU   A 1  29  ? -19.3   -25.466 -27.873 1    32.222  ? 29   GLU   A O   1 1 
ATOM   208   C  CB  . GLU   A 1  29  ? -19.324 -28.205 -26.377 1    34.211  ? 29   GLU   A CB  1 1 
ATOM   209   C  CG  . GLU   A 1  29  ? -18.697 -29.129 -25.335 1    32.286  ? 29   GLU   A CG  1 1 
ATOM   210   C  CD  . GLU   A 1  29  ? -18.212 -30.479 -25.913 1    34.857  ? 29   GLU   A CD  1 1 
ATOM   211   O  OE1 . GLU   A 1  29  ? -18.947 -30.987 -26.8   1    36.962  ? 29   GLU   A OE1 1 1 
ATOM   212   O  OE2 . GLU   A 1  29  ? -17.141 -31.067 -25.522 1    30.301  ? 29   GLU   A OE2 1 1 
ATOM   213   N  N   . GLN   A 1  30  ? -21.429 -26.079 -27.47  1    31.538  ? 30   GLN   A N   1 1 
ATOM   214   C  CA  . GLN   A 1  30  ? -21.798 -25.379 -28.679 1    31.962  ? 30   GLN   A CA  1 1 
ATOM   215   C  C   . GLN   A 1  30  ? -21.664 -23.9   -28.397 1    28.459  ? 30   GLN   A C   1 1 
ATOM   216   O  O   . GLN   A 1  30  ? -21.273 -23.158 -29.288 1    29.052  ? 30   GLN   A O   1 1 
ATOM   217   C  CB  . GLN   A 1  30  ? -23.174 -25.561 -29.303 1    33.926  ? 30   GLN   A CB  1 1 
ATOM   218   C  CG  . GLN   A 1  30  ? -23.478 -27.007 -29.659 1    39.694  ? 30   GLN   A CG  1 1 
ATOM   219   C  CD  . GLN   A 1  30  ? -24.98  -27.192 -29.64  1    45.708  ? 30   GLN   A CD  1 1 
ATOM   220   O  OE1 . GLN   A 1  30  ? -25.494 -28.08  -28.945 1    47.816  ? 30   GLN   A OE1 1 1 
ATOM   221   N  NE2 . GLN   A 1  30  ? -25.668 -26.286 -30.335 1    42.977  ? 30   GLN   A NE2 1 1 
ATOM   222   N  N   . VAL   A 1  31  ? -21.944 -23.497 -27.166 1    28.302  ? 31   VAL   A N   1 1 
ATOM   223   C  CA  . VAL   A 1  31  ? -21.923 -22.059 -26.904 1    28.632  ? 31   VAL   A CA  1 1 
ATOM   224   C  C   . VAL   A 1  31  ? -20.464 -21.543 -26.765 1    27.163  ? 31   VAL   A C   1 1 
ATOM   225   O  O   . VAL   A 1  31  ? -20.105 -20.47  -27.273 1    27.894  ? 31   VAL   A O   1 1 
ATOM   226   C  CB  . VAL   A 1  31  ? -22.847 -21.622 -25.752 1    28.478  ? 31   VAL   A CB  1 1 
ATOM   227   C  CG1 . VAL   A 1  31  ? -22.718 -20.123 -25.471 1    27.305  ? 31   VAL   A CG1 1 1 
ATOM   228   C  CG2 . VAL   A 1  31  ? -24.331 -21.895 -26.09  1    28.516  ? 31   VAL   A CG2 1 1 
ATOM   229   N  N   . LEU   A 1  32  ? -19.637 -22.276 -26.043 1    27.873  ? 32   LEU   A N   1 1 
ATOM   230   C  CA  . LEU   A 1  32  ? -18.188 -22.015 -25.998 1    26.998  ? 32   LEU   A CA  1 1 
ATOM   231   C  C   . LEU   A 1  32  ? -17.542 -21.934 -27.38  1    25.913  ? 32   LEU   A C   1 1 
ATOM   232   O  O   . LEU   A 1  32  ? -16.844 -20.964 -27.681 1    26.105  ? 32   LEU   A O   1 1 
ATOM   233   C  CB  . LEU   A 1  32  ? -17.575 -23.071 -25.1   1    28.433  ? 32   LEU   A CB  1 1 
ATOM   234   C  CG  . LEU   A 1  32  ? -17.884 -22.845 -23.617 1    33.887  ? 32   LEU   A CG  1 1 
ATOM   235   C  CD1 . LEU   A 1  32  ? -17.441 -23.917 -22.623 1    31.465  ? 32   LEU   A CD1 1 1 
ATOM   236   C  CD2 . LEU   A 1  32  ? -17.235 -21.512 -23.239 1    34.874  ? 32   LEU   A CD2 1 1 
ATOM   237   N  N   . PHE   A 1  33  ? -17.838 -22.903 -28.264 1    25.166  ? 33   PHE   A N   1 1 
ATOM   238   C  CA  . PHE   A 1  33  ? -17.271 -22.923 -29.607 1    25.676  ? 33   PHE   A CA  1 1 
ATOM   239   C  C   . PHE   A 1  33  ? -17.611 -21.629 -30.344 1    26.993  ? 33   PHE   A C   1 1 
ATOM   240   O  O   . PHE   A 1  33  ? -16.701 -20.934 -30.825 1    27.677  ? 33   PHE   A O   1 1 
ATOM   241   C  CB  . PHE   A 1  33  ? -17.648 -24.24  -30.327 1    29.832  ? 33   PHE   A CB  1 1 
ATOM   242   C  CG  . PHE   A 1  33  ? -17.295 -24.219 -31.807 1    32.688  ? 33   PHE   A CG  1 1 
ATOM   243   C  CD1 . PHE   A 1  33  ? -16.014 -24.593 -32.222 1    30.655  ? 33   PHE   A CD1 1 1 
ATOM   244   C  CD2 . PHE   A 1  33  ? -18.21  -23.739 -32.747 1    32.574  ? 33   PHE   A CD2 1 1 
ATOM   245   C  CE1 . PHE   A 1  33  ? -15.659 -24.487 -33.56  1    33.137  ? 33   PHE   A CE1 1 1 
ATOM   246   C  CE2 . PHE   A 1  33  ? -17.853 -23.628 -34.08  1    34.278  ? 33   PHE   A CE2 1 1 
ATOM   247   C  CZ  . PHE   A 1  33  ? -16.586 -24.021 -34.485 1    34.974  ? 33   PHE   A CZ  1 1 
ATOM   248   N  N   . GLN   A 1  34  ? -18.927 -21.278 -30.441 1    25.946  ? 34   GLN   A N   1 1 
ATOM   249   C  CA  . GLN   A 1  34  ? -19.306 -20.099 -31.21  1    26.953  ? 34   GLN   A CA  1 1 
ATOM   250   C  C   . GLN   A 1  34  ? -18.549 -18.87  -30.685 1    24.429  ? 34   GLN   A C   1 1 
ATOM   251   O  O   . GLN   A 1  34  ? -18.151 -17.974 -31.442 1    24.966  ? 34   GLN   A O   1 1 
ATOM   252   C  CB  . GLN   A 1  34  ? -20.835 -19.867 -31.301 1    29.336  ? 34   GLN   A CB  1 1 
ATOM   253   C  CG  . GLN   A 1  34  ? -21.519 -19.64  -29.953 1    30.373  ? 34   GLN   A CG  1 1 
ATOM   254   C  CD  . GLN   A 1  34  ? -21.703 -18.177 -29.552 1    30.663  ? 34   GLN   A CD  1 1 
ATOM   255   O  OE1 . GLN   A 1  34  ? -22.014 -17.314 -30.39  1    33.102  ? 34   GLN   A OE1 1 1 
ATOM   256   N  NE2 . GLN   A 1  34  ? -21.531 -17.861 -28.268 1    28.232  ? 34   GLN   A NE2 1 1 
ATOM   257   N  N   . SER   A 1  35  ? -18.411 -18.807 -29.386 1    23.471  ? 35   SER   A N   1 1 
ATOM   258   C  CA  . SER   A 1  35  ? -17.75  -17.689 -28.745 1    25.764  ? 35   SER   A CA  1 1 
ATOM   259   C  C   . SER   A 1  35  ? -16.237 -17.661 -29.045 1    24.252  ? 35   SER   A C   1 1 
ATOM   260   O  O   . SER   A 1  35  ? -15.682 -16.633 -29.473 1    23.507  ? 35   SER   A O   1 1 
ATOM   261   C  CB  . SER   A 1  35  ? -17.922 -17.857 -27.273 1    29.112  ? 35   SER   A CB  1 1 
ATOM   262   O  OG  . SER   A 1  35  ? -17.416 -16.682 -26.681 1    33.848  ? 35   SER   A OG  1 1 
ATOM   263   N  N   . VAL   A 1  36  ? -15.577 -18.802 -28.812 1    22.985  ? 36   VAL   A N   1 1 
ATOM   264   C  CA  . VAL   A 1  36  ? -14.166 -18.943 -29.169 1    21.37   ? 36   VAL   A CA  1 1 
ATOM   265   C  C   . VAL   A 1  36  ? -13.939 -18.678 -30.653 1    21.418  ? 36   VAL   A C   1 1 
ATOM   266   O  O   . VAL   A 1  36  ? -13.032 -17.912 -31.003 1    21.063  ? 36   VAL   A O   1 1 
ATOM   267   C  CB  . VAL   A 1  36  ? -13.57  -20.268 -28.67  1    21.421  ? 36   VAL   A CB  1 1 
ATOM   268   C  CG1 . VAL   A 1  36  ? -12.09  -20.396 -29.087 1    19.67   ? 36   VAL   A CG1 1 1 
ATOM   269   C  CG2 . VAL   A 1  36  ? -13.627 -20.318 -27.131 1    21.048  ? 36   VAL   A CG2 1 1 
ATOM   270   N  N   . ALA   A 1  37  ? -14.814 -19.224 -31.531 1    23.329  ? 37   ALA   A N   1 1 
ATOM   271   C  CA  . ALA   A 1  37  ? -14.649 -19.053 -32.976 1    24.637  ? 37   ALA   A CA  1 1 
ATOM   272   C  C   . ALA   A 1  37  ? -14.721 -17.583 -33.375 1    25.318  ? 37   ALA   A C   1 1 
ATOM   273   O  O   . ALA   A 1  37  ? -13.942 -17.094 -34.212 1    24.688  ? 37   ALA   A O   1 1 
ATOM   274   C  CB  . ALA   A 1  37  ? -15.625 -19.904 -33.777 1    25.039  ? 37   ALA   A CB  1 1 
ATOM   275   N  N   . ALA   A 1  38  ? -15.683 -16.88  -32.765 1    25.176  ? 38   ALA   A N   1 1 
ATOM   276   C  CA  . ALA   A 1  38  ? -15.877 -15.478 -33.078 1    25.086  ? 38   ALA   A CA  1 1 
ATOM   277   C  C   . ALA   A 1  38  ? -14.684 -14.663 -32.577 1    23.568  ? 38   ALA   A C   1 1 
ATOM   278   O  O   . ALA   A 1  38  ? -14.295 -13.716 -33.258 1    25.323  ? 38   ALA   A O   1 1 
ATOM   279   C  CB  . ALA   A 1  38  ? -17.191 -14.964 -32.462 1    25.921  ? 38   ALA   A CB  1 1 
ATOM   280   N  N   . SER   A 1  39  ? -14.106 -15.037 -31.437 1    23.794  ? 39   SER   A N   1 1 
ATOM   281   C  CA  . SER   A 1  39  ? -12.885 -14.387 -30.928 1    23.204  ? 39   SER   A CA  1 1 
ATOM   282   C  C   . SER   A 1  39  ? -11.681 -14.598 -31.855 1    22.191  ? 39   SER   A C   1 1 
ATOM   283   O  O   . SER   A 1  39  ? -10.875 -13.694 -32.07  1    20.582  ? 39   SER   A O   1 1 
ATOM   284   C  CB  . SER   A 1  39  ? -12.549 -14.854 -29.533 1    24.68   ? 39   SER   A CB  1 1 
ATOM   285   O  OG  . SER   A 1  39  ? -13.475 -14.325 -28.599 1    26.154  ? 39   SER   A OG  1 1 
ATOM   286   N  N   . TRP   A 1  40  ? -11.572 -15.816 -32.394 1    22.627  ? 40   TRP   A N   1 1 
ATOM   287   C  CA  . TRP   A 1  40  ? -10.508 -16.195 -33.315 1    22.718  ? 40   TRP   A CA  1 1 
ATOM   288   C  C   . TRP   A 1  40  ? -10.625 -15.355 -34.571 1    24.315  ? 40   TRP   A C   1 1 
ATOM   289   O  O   . TRP   A 1  40  ? -9.622  -14.776 -35.003 1    25.412  ? 40   TRP   A O   1 1 
ATOM   290   C  CB  . TRP   A 1  40  ? -10.55  -17.708 -33.615 1    22.796  ? 40   TRP   A CB  1 1 
ATOM   291   C  CG  . TRP   A 1  40  ? -9.523  -18.138 -34.617 1    23.629  ? 40   TRP   A CG  1 1 
ATOM   292   C  CD1 . TRP   A 1  40  ? -9.631  -18.142 -35.979 1    25.325  ? 40   TRP   A CD1 1 1 
ATOM   293   C  CD2 . TRP   A 1  40  ? -8.18   -18.562 -34.306 1    22.913  ? 40   TRP   A CD2 1 1 
ATOM   294   N  NE1 . TRP   A 1  40  ? -8.44   -18.53  -36.529 1    24.081  ? 40   TRP   A NE1 1 1 
ATOM   295   C  CE2 . TRP   A 1  40  ? -7.538  -18.794 -35.538 1    23.884  ? 40   TRP   A CE2 1 1 
ATOM   296   C  CE3 . TRP   A 1  40  ? -7.461  -18.706 -33.099 1    22.335  ? 40   TRP   A CE3 1 1 
ATOM   297   C  CZ2 . TRP   A 1  40  ? -6.208  -19.204 -35.627 1    23.036  ? 40   TRP   A CZ2 1 1 
ATOM   298   C  CZ3 . TRP   A 1  40  ? -6.15   -19.128 -33.202 1    20.829  ? 40   TRP   A CZ3 1 1 
ATOM   299   C  CH2 . TRP   A 1  40  ? -5.544  -19.349 -34.434 1    21.695  ? 40   TRP   A CH2 1 1 
ATOM   300   N  N   . ALA   A 1  41  ? -11.857 -15.218 -35.098 1    24.217  ? 41   ALA   A N   1 1 
ATOM   301   C  CA  . ALA   A 1  41  ? -12.043 -14.545 -36.363 1    26.353  ? 41   ALA   A CA  1 1 
ATOM   302   C  C   . ALA   A 1  41  ? -11.633 -13.101 -36.165 1    27.314  ? 41   ALA   A C   1 1 
ATOM   303   O  O   . ALA   A 1  41  ? -11.142 -12.458 -37.082 1    33.431  ? 41   ALA   A O   1 1 
ATOM   304   C  CB  . ALA   A 1  41  ? -13.485 -14.65  -36.889 1    28.568  ? 41   ALA   A CB  1 1 
ATOM   305   N  N   . HIS   A 1  42  ? -11.869 -12.596 -34.965 1    27.718  ? 42   HIS   A N   1 1 
ATOM   306   C  CA  . HIS   A 1  42  ? -11.603 -11.199 -34.678 1    29.014  ? 42   HIS   A CA  1 1 
ATOM   307   C  C   . HIS   A 1  42  ? -10.101 -11.02  -34.462 1    26.488  ? 42   HIS   A C   1 1 
ATOM   308   O  O   . HIS   A 1  42  ? -9.474  -10.188 -35.094 1    27.566  ? 42   HIS   A O   1 1 
ATOM   309   C  CB  . HIS   A 1  42  ? -12.388 -10.7   -33.458 1    28.594  ? 42   HIS   A CB  1 1 
ATOM   310   C  CG  . HIS   A 1  42  ? -11.933 -9.355  -33.029 1    33.577  ? 42   HIS   A CG  1 1 
ATOM   311   N  ND1 . HIS   A 1  42  ? -10.997 -9.159  -32.013 1    36.742  ? 42   HIS   A ND1 1 1 
ATOM   312   C  CD2 . HIS   A 1  42  ? -12.216 -8.138  -33.533 1    35.869  ? 42   HIS   A CD2 1 1 
ATOM   313   C  CE1 . HIS   A 1  42  ? -10.792 -7.845  -31.87  1    36.273  ? 42   HIS   A CE1 1 1 
ATOM   314   N  NE2 . HIS   A 1  42  ? -11.519 -7.208  -32.774 1    34.183  ? 42   HIS   A NE2 1 1 
ATOM   315   N  N   . ASP   A 1  43  ? -9.524  -11.878 -33.646 1    26.385  ? 43   ASP   A N   1 1 
ATOM   316   C  CA  . ASP   A 1  43  ? -8.116  -11.729 -33.26  1    26.681  ? 43   ASP   A CA  1 1 
ATOM   317   C  C   . ASP   A 1  43  ? -7.138  -11.999 -34.414 1    27.654  ? 43   ASP   A C   1 1 
ATOM   318   O  O   . ASP   A 1  43  ? -6.035  -11.47  -34.365 1    29.745  ? 43   ASP   A O   1 1 
ATOM   319   C  CB  . ASP   A 1  43  ? -7.791  -12.555 -32.023 1    26.913  ? 43   ASP   A CB  1 1 
ATOM   320   C  CG  . ASP   A 1  43  ? -8.38   -12.03  -30.721 1    30.528  ? 43   ASP   A CG  1 1 
ATOM   321   O  OD1 . ASP   A 1  43  ? -9.18   -11.08  -30.777 1    28.703  ? 43   ASP   A OD1 1 1 
ATOM   322   O  OD2 . ASP   A 1  43  ? -8.06   -12.595 -29.665 1    30.484  ? 43   ASP   A OD2 1 1 
ATOM   323   N  N   . THR   A 1  44  ? -7.528  -12.795 -35.431 1    26.233  ? 44   THR   A N   1 1 
ATOM   324   C  CA  . THR   A 1  44  ? -6.682  -13.053 -36.578 1    28.252  ? 44   THR   A CA  1 1 
ATOM   325   C  C   . THR   A 1  44  ? -7.036  -12.122 -37.721 1    32.308  ? 44   THR   A C   1 1 
ATOM   326   O  O   . THR   A 1  44  ? -6.554  -12.343 -38.844 1    35.409  ? 44   THR   A O   1 1 
ATOM   327   C  CB  . THR   A 1  44  ? -6.766  -14.519 -37.026 1    30.257  ? 44   THR   A CB  1 1 
ATOM   328   O  OG1 . THR   A 1  44  ? -8.127  -14.735 -37.407 1    27.65   ? 44   THR   A OG1 1 1 
ATOM   329   C  CG2 . THR   A 1  44  ? -6.275  -15.456 -35.926 1    26.872  ? 44   THR   A CG2 1 1 
ATOM   330   N  N   . ASN   A 1  45  ? -7.943  -11.15  -37.476 1    32.068  ? 45   ASN   A N   1 1 
ATOM   331   C  CA  . ASN   A 1  45  ? -8.41   -10.33  -38.585 1    31.496  ? 45   ASN   A CA  1 1 
ATOM   332   C  C   . ASN   A 1  45  ? -9.256  -9.198  -38.008 1    32.232  ? 45   ASN   A C   1 1 
ATOM   333   O  O   . ASN   A 1  45  ? -10.493 -9.303  -37.976 1    34.04   ? 45   ASN   A O   1 1 
ATOM   334   C  CB  . ASN   A 1  45  ? -9.209  -11.221 -39.535 1    34.49   ? 45   ASN   A CB  1 1 
ATOM   335   C  CG  . ASN   A 1  45  ? -9.814  -10.5   -40.714 1    38.009  ? 45   ASN   A CG  1 1 
ATOM   336   O  OD1 . ASN   A 1  45  ? -9.423  -9.373  -41.024 1    39.952  ? 45   ASN   A OD1 1 1 
ATOM   337   N  ND2 . ASN   A 1  45  ? -10.732 -11.161 -41.397 1    40.642  ? 45   ASN   A ND2 1 1 
ATOM   338   N  N   . ILE   A 1  46  ? -8.587  -8.165  -37.48  1    31.278  ? 46   ILE   A N   1 1 
ATOM   339   C  CA  . ILE   A 1  46  ? -9.273  -7.209  -36.62  1    32.888  ? 46   ILE   A CA  1 1 
ATOM   340   C  C   . ILE   A 1  46  ? -10.066 -6.273  -37.542 1    34.603  ? 46   ILE   A C   1 1 
ATOM   341   O  O   . ILE   A 1  46  ? -9.487  -5.65   -38.422 1    38.499  ? 46   ILE   A O   1 1 
ATOM   342   C  CB  . ILE   A 1  46  ? -8.321  -6.454  -35.685 1    30.121  ? 46   ILE   A CB  1 1 
ATOM   343   C  CG1 . ILE   A 1  46  ? -7.511  -7.428  -34.828 1    30.218  ? 46   ILE   A CG1 1 1 
ATOM   344   C  CG2 . ILE   A 1  46  ? -9.073  -5.472  -34.764 1    30.157  ? 46   ILE   A CG2 1 1 
ATOM   345   C  CD1 . ILE   A 1  46  ? -6.676  -6.737  -33.792 1    29.354  ? 46   ILE   A CD1 1 1 
ATOM   346   N  N   . THR   A 1  47  ? -11.392 -6.358  -37.492 1    38.619  ? 47   THR   A N   1 1 
ATOM   347   C  CA  . THR   A 1  47  ? -12.26  -5.524  -38.341 1    37.939  ? 47   THR   A CA  1 1 
ATOM   348   C  C   . THR   A 1  47  ? -13.474 -5.142  -37.51  1    36.279  ? 47   THR   A C   1 1 
ATOM   349   O  O   . THR   A 1  47  ? -13.777 -5.804  -36.527 1    34.629  ? 47   THR   A O   1 1 
ATOM   350   C  CB  . THR   A 1  47  ? -12.693 -6.17   -39.662 1    41.012  ? 47   THR   A CB  1 1 
ATOM   351   O  OG1 . THR   A 1  47  ? -13.693 -7.16   -39.42  1    41.634  ? 47   THR   A OG1 1 1 
ATOM   352   C  CG2 . THR   A 1  47  ? -11.557 -6.708  -40.522 1    41.466  ? 47   THR   A CG2 1 1 
ATOM   353   N  N   . ALA   A 1  48  ? -14.149 -4.049  -37.885 1    39.336  ? 48   ALA   A N   1 1 
ATOM   354   C  CA  . ALA   A 1  48  ? -15.341 -3.597  -37.165 1    38.516  ? 48   ALA   A CA  1 1 
ATOM   355   C  C   . ALA   A 1  48  ? -16.409 -4.698  -37.2   1    36.888  ? 48   ALA   A C   1 1 
ATOM   356   O  O   . ALA   A 1  48  ? -17.087 -4.965  -36.209 1    35.75   ? 48   ALA   A O   1 1 
ATOM   357   C  CB  . ALA   A 1  48  ? -15.867 -2.284  -37.774 1    37.802  ? 48   ALA   A CB  1 1 
ATOM   358   N  N   . GLU   A 1  49  ? -16.514 -5.357  -38.345 1    36.317  ? 49   GLU   A N   1 1 
ATOM   359   C  CA  . GLU   A 1  49  ? -17.511 -6.386  -38.545 1    40.768  ? 49   GLU   A CA  1 1 
ATOM   360   C  C   . GLU   A 1  49  ? -17.199 -7.61   -37.69  1    38.66   ? 49   GLU   A C   1 1 
ATOM   361   O  O   . GLU   A 1  49  ? -18.1   -8.22   -37.112 1    37.497  ? 49   GLU   A O   1 1 
ATOM   362   C  CB  . GLU   A 1  49  ? -17.647 -6.649  -40.043 1    45.65   ? 49   GLU   A CB  1 1 
ATOM   363   C  CG  . GLU   A 1  49  ? -18.611 -7.775  -40.391 1    55.469  ? 49   GLU   A CG  1 1 
ATOM   364   C  CD  . GLU   A 1  49  ? -20.011 -7.821  -39.773 1    63.529  ? 49   GLU   A CD  1 1 
ATOM   365   O  OE1 . GLU   A 1  49  ? -20.872 -8.555  -40.318 1    71.737  ? 49   GLU   A OE1 1 1 
ATOM   366   O  OE2 . GLU   A 1  49  ? -20.258 -7.184  -38.728 1    65.607  ? 49   GLU   A OE2 1 1 
ATOM   367   N  N   . ASN   A 1  50  ? -15.923 -8.009  -37.641 1    35.043  ? 50   ASN   A N   1 1 
ATOM   368   C  CA  . ASN   A 1  50  ? -15.55  -9.068  -36.705 1    31.735  ? 50   ASN   A CA  1 1 
ATOM   369   C  C   . ASN   A 1  50  ? -15.8   -8.654  -35.252 1    29.027  ? 50   ASN   A C   1 1 
ATOM   370   O  O   . ASN   A 1  50  ? -16.137 -9.497  -34.419 1    27.205  ? 50   ASN   A O   1 1 
ATOM   371   C  CB  . ASN   A 1  50  ? -14.147 -9.627  -36.995 1    29.658  ? 50   ASN   A CB  1 1 
ATOM   372   C  CG  . ASN   A 1  50  ? -14.1   -10.249 -38.378 1    33.905  ? 50   ASN   A CG  1 1 
ATOM   373   O  OD1 . ASN   A 1  50  ? -15.144 -10.706 -38.874 1    35.083  ? 50   ASN   A OD1 1 1 
ATOM   374   N  ND2 . ASN   A 1  50  ? -12.938 -10.292 -39.036 1    32.184  ? 50   ASN   A ND2 1 1 
ATOM   375   N  N   . ALA   A 1  51  ? -15.531 -7.392  -34.865 1    28.664  ? 51   ALA   A N   1 1 
ATOM   376   C  CA  . ALA   A 1  51  ? -15.766 -7.122  -33.449 1    27.846  ? 51   ALA   A CA  1 1 
ATOM   377   C  C   . ALA   A 1  51  ? -17.276 -7.183  -33.147 1    31.206  ? 51   ALA   A C   1 1 
ATOM   378   O  O   . ALA   A 1  51  ? -17.673 -7.639  -32.067 1    30.287  ? 51   ALA   A O   1 1 
ATOM   379   C  CB  . ALA   A 1  51  ? -15.134 -5.808  -33.041 1    28.479  ? 51   ALA   A CB  1 1 
ATOM   380   N  N   . ARG   A 1  52  ? -18.105 -6.789  -34.139 1    30.256  ? 52   ARG   A N   1 1 
ATOM   381   C  CA  . ARG   A 1  52  ? -19.553 -6.83   -33.938 1    34.461  ? 52   ARG   A CA  1 1 
ATOM   382   C  C   . ARG   A 1  52  ? -20.003 -8.268  -33.69  1    31.768  ? 52   ARG   A C   1 1 
ATOM   383   O  O   . ARG   A 1  52  ? -20.763 -8.569  -32.761 1    29.785  ? 52   ARG   A O   1 1 
ATOM   384   C  CB  . ARG   A 1  52  ? -20.264 -6.145  -35.108 1    38.931  ? 52   ARG   A CB  1 1 
ATOM   385   C  CG  . ARG   A 1  52  ? -21.712 -5.777  -34.802 1    48.503  ? 52   ARG   A CG  1 1 
ATOM   386   C  CD  . ARG   A 1  52  ? -22.578 -5.364  -36.015 1    53.331  ? 52   ARG   A CD  1 1 
ATOM   387   N  NE  . ARG   A 1  52  ? -22.769 -6.394  -37.055 1    60.001  ? 52   ARG   A NE  1 1 
ATOM   388   C  CZ  . ARG   A 1  52  ? -23.07  -7.709  -36.952 1    63.209  ? 52   ARG   A CZ  1 1 
ATOM   389   N  NH1 . ARG   A 1  52  ? -23.38  -8.277  -35.79  1    64.711  ? 52   ARG   A NH1 1 1 
ATOM   390   N  NH2 . ARG   A 1  52  ? -23.057 -8.472  -38.038 1    65.168  ? 52   ARG   A NH2 1 1 
ATOM   391   N  N   . ARG   A 1  53  ? -19.469 -9.185  -34.499 1    32.751  ? 53   ARG   A N   1 1 
ATOM   392   C  CA  . ARG   A 1  53  ? -19.832 -10.584 -34.372 1    32.049  ? 53   ARG   A CA  1 1 
ATOM   393   C  C   . ARG   A 1  53  ? -19.364 -11.127 -33.04  1    29.419  ? 53   ARG   A C   1 1 
ATOM   394   O  O   . ARG   A 1  53  ? -20.05  -11.951 -32.455 1    29.03   ? 53   ARG   A O   1 1 
ATOM   395   C  CB  . ARG   A 1  53  ? -19.282 -11.454 -35.504 1    35.784  ? 53   ARG   A CB  1 1 
ATOM   396   C  CG  . ARG   A 1  53  ? -19.972 -11.205 -36.833 1    41.877  ? 53   ARG   A CG  1 1 
ATOM   397   C  CD  . ARG   A 1  53  ? -19.417 -12.218 -37.826 1    46.691  ? 53   ARG   A CD  1 1 
ATOM   398   N  NE  . ARG   A 1  53  ? -19.874 -11.882 -39.179 1    61.626  ? 53   ARG   A NE  1 1 
ATOM   399   C  CZ  . ARG   A 1  53  ? -19.104 -11.434 -40.169 1    65.86   ? 53   ARG   A CZ  1 1 
ATOM   400   N  NH1 . ARG   A 1  53  ? -19.687 -11.051 -41.282 1    67.355  ? 53   ARG   A NH1 1 1 
ATOM   401   N  NH2 . ARG   A 1  53  ? -17.784 -11.316 -40.037 1    63.968  ? 53   ARG   A NH2 1 1 
ATOM   402   N  N   . GLN   A 1  54  ? -18.18  -10.696 -32.551 1    27.361  ? 54   GLN   A N   1 1 
ATOM   403   C  CA  . GLN   A 1  54  ? -17.679 -11.263 -31.314 1    25.705  ? 54   GLN   A CA  1 1 
ATOM   404   C  C   . GLN   A 1  54  ? -18.557 -10.753 -30.177 1    24.548  ? 54   GLN   A C   1 1 
ATOM   405   O  O   . GLN   A 1  54  ? -18.788 -11.458 -29.2   1    23.196  ? 54   GLN   A O   1 1 
ATOM   406   C  CB  . GLN   A 1  54  ? -16.209 -10.837 -31.198 1    24.707  ? 54   GLN   A CB  1 1 
ATOM   407   C  CG  . GLN   A 1  54  ? -15.454 -11.479 -30.043 1    26.689  ? 54   GLN   A CG  1 1 
ATOM   408   C  CD  . GLN   A 1  54  ? -15.795 -10.826 -28.721 1    27.531  ? 54   GLN   A CD  1 1 
ATOM   409   O  OE1 . GLN   A 1  54  ? -16.055 -11.523 -27.733 1    29.752  ? 54   GLN   A OE1 1 1 
ATOM   410   N  NE2 . GLN   A 1  54  ? -15.851 -9.493  -28.705 1    25.926  ? 54   GLN   A NE2 1 1 
ATOM   411   N  N   . GLU   A 1  55  ? -18.984 -9.485  -30.29  1    26.486  ? 55   GLU   A N   1 1 
ATOM   412   C  CA  . GLU   A 1  55  ? -19.846 -8.923  -29.271 1    27.927  ? 55   GLU   A CA  1 1 
ATOM   413   C  C   . GLU   A 1  55  ? -21.144 -9.715  -29.233 1    27.753  ? 55   GLU   A C   1 1 
ATOM   414   O  O   . GLU   A 1  55  ? -21.597 -10.053 -28.153 1    27.553  ? 55   GLU   A O   1 1 
ATOM   415   C  CB  . GLU   A 1  55  ? -20.085 -7.424  -29.407 1    32.059  ? 55   GLU   A CB  1 1 
ATOM   416   C  CG  . GLU   A 1  55  ? -18.812 -6.662  -29.018 1    36.423  ? 55   GLU   A CG  1 1 
ATOM   417   C  CD  . GLU   A 1  55  ? -18.947 -5.19   -29.382 1    42.898  ? 55   GLU   A CD  1 1 
ATOM   418   O  OE1 . GLU   A 1  55  ? -20.1   -4.706  -29.228 1    42.094  ? 55   GLU   A OE1 1 1 
ATOM   419   O  OE2 . GLU   A 1  55  ? -17.963 -4.532  -29.82  1    43.256  ? 55   GLU   A OE2 1 1 
ATOM   420   N  N   . GLU   A 1  56  ? -21.733 -10.03  -30.39  1    27.666  ? 56   GLU   A N   1 1 
ATOM   421   C  CA  . GLU   A 1  56  ? -22.966 -10.797 -30.377 1    29.673  ? 56   GLU   A CA  1 1 
ATOM   422   C  C   . GLU   A 1  56  ? -22.747 -12.187 -29.779 1    27.064  ? 56   GLU   A C   1 1 
ATOM   423   O  O   . GLU   A 1  56  ? -23.613 -12.732 -29.109 1    26.465  ? 56   GLU   A O   1 1 
ATOM   424   C  CB  . GLU   A 1  56  ? -23.676 -10.863 -31.739 1    35.214  ? 56   GLU   A CB  1 1 
ATOM   425   C  CG  . GLU   A 1  56  ? -24.273 -9.525  -32.16  1    48.992  ? 56   GLU   A CG  1 1 
ATOM   426   C  CD  . GLU   A 1  56  ? -25.533 -8.905  -31.502 1    62.223  ? 56   GLU   A CD  1 1 
ATOM   427   O  OE1 . GLU   A 1  56  ? -26.273 -9.56   -30.704 1    64.871  ? 56   GLU   A OE1 1 1 
ATOM   428   O  OE2 . GLU   A 1  56  ? -25.786 -7.702  -31.791 1    61.243  ? 56   GLU   A OE2 1 1 
ATOM   429   N  N   . ALA   A 1  57  ? -21.58  -12.799 -30.021 1    26.274  ? 57   ALA   A N   1 1 
ATOM   430   C  CA  . ALA   A 1  57  ? -21.34  -14.123 -29.475 1    25.953  ? 57   ALA   A CA  1 1 
ATOM   431   C  C   . ALA   A 1  57  ? -21.197 -14.042 -27.956 1    26.112  ? 57   ALA   A C   1 1 
ATOM   432   O  O   . ALA   A 1  57  ? -21.591 -14.961 -27.225 1    26.279  ? 57   ALA   A O   1 1 
ATOM   433   C  CB  . ALA   A 1  57  ? -20.099 -14.762 -30.132 1    25.358  ? 57   ALA   A CB  1 1 
ATOM   434   N  N   . ALA   A 1  58  ? -20.618 -12.942 -27.478 1    25.27   ? 58   ALA   A N   1 1 
ATOM   435   C  CA  . ALA   A 1  58  ? -20.401 -12.831 -26.043 1    26.008  ? 58   ALA   A CA  1 1 
ATOM   436   C  C   . ALA   A 1  58  ? -21.752 -12.653 -25.371 1    25.022  ? 58   ALA   A C   1 1 
ATOM   437   O  O   . ALA   A 1  58  ? -21.943 -13.146 -24.281 1    26.297  ? 58   ALA   A O   1 1 
ATOM   438   C  CB  . ALA   A 1  58  ? -19.432 -11.713 -25.696 1    26.847  ? 58   ALA   A CB  1 1 
ATOM   439   N  N   . LEU   A 1  59  ? -22.715 -11.995 -26.037 1    25.293  ? 59   LEU   A N   1 1 
ATOM   440   C  CA  . LEU   A 1  59  ? -24.034 -11.772 -25.457 1    25.608  ? 59   LEU   A CA  1 1 
ATOM   441   C  C   . LEU   A 1  59  ? -24.769 -13.109 -25.362 1    25.883  ? 59   LEU   A C   1 1 
ATOM   442   O  O   . LEU   A 1  59  ? -25.499 -13.383 -24.413 1    25.979  ? 59   LEU   A O   1 1 
ATOM   443   C  CB  . LEU   A 1  59  ? -24.761 -10.846 -26.442 1    27.271  ? 59   LEU   A CB  1 1 
ATOM   444   C  CG  . LEU   A 1  59  ? -25.354 -9.526  -25.914 1    29.688  ? 59   LEU   A CG  1 1 
ATOM   445   C  CD1 . LEU   A 1  59  ? -26.572 -9.077  -26.736 1    30.559  ? 59   LEU   A CD1 1 1 
ATOM   446   C  CD2 . LEU   A 1  59  ? -25.485 -9.172  -24.418 1    27.448  ? 59   LEU   A CD2 1 1 
ATOM   447   N  N   . LEU   A 1  60  ? -24.641 -13.927 -26.414 1    26.897  ? 60   LEU   A N   1 1 
ATOM   448   C  CA  . LEU   A 1  60  ? -25.236 -15.255 -26.374 1    28.738  ? 60   LEU   A CA  1 1 
ATOM   449   C  C   . LEU   A 1  60  ? -24.693 -16.049 -25.183 1    27.85   ? 60   LEU   A C   1 1 
ATOM   450   O  O   . LEU   A 1  60  ? -25.476 -16.697 -24.494 1    27.195  ? 60   LEU   A O   1 1 
ATOM   451   C  CB  . LEU   A 1  60  ? -25.045 -16.009 -27.681 1    31.464  ? 60   LEU   A CB  1 1 
ATOM   452   C  CG  . LEU   A 1  60  ? -25.743 -17.375 -27.789 1    37      ? 60   LEU   A CG  1 1 
ATOM   453   C  CD1 . LEU   A 1  60  ? -27.22  -17.218 -27.499 1    39.129  ? 60   LEU   A CD1 1 1 
ATOM   454   C  CD2 . LEU   A 1  60  ? -25.566 -17.836 -29.238 1    38.668  ? 60   LEU   A CD2 1 1 
ATOM   455   N  N   A SER   A 1  61  ? -23.353 -16.034 -24.992 0.71 26.056  ? 61   SER   A N   1 1 
ATOM   456   N  N   B SER   A 1  61  ? -23.378 -15.977 -24.947 0.29 26.183  ? 61   SER   A N   1 1 
ATOM   457   C  CA  A SER   A 1  61  ? -22.704 -16.674 -23.857 0.71 26.196  ? 61   SER   A CA  1 1 
ATOM   458   C  CA  B SER   A 1  61  ? -22.799 -16.744 -23.862 0.29 25.649  ? 61   SER   A CA  1 1 
ATOM   459   C  C   A SER   A 1  61  ? -23.313 -16.226 -22.548 0.71 26.132  ? 61   SER   A C   1 1 
ATOM   460   C  C   B SER   A 1  61  ? -23.255 -16.22  -22.506 0.29 25.554  ? 61   SER   A C   1 1 
ATOM   461   O  O   A SER   A 1  61  ? -23.544 -17.048 -21.662 0.71 26.459  ? 61   SER   A O   1 1 
ATOM   462   O  O   B SER   A 1  61  ? -23.396 -16.993 -21.561 0.29 25.517  ? 61   SER   A O   1 1 
ATOM   463   C  CB  A SER   A 1  61  ? -21.2   -16.424 -23.801 0.71 25.138  ? 61   SER   A CB  1 1 
ATOM   464   C  CB  B SER   A 1  61  ? -21.301 -16.811 -23.952 0.29 24.548  ? 61   SER   A CB  1 1 
ATOM   465   O  OG  A SER   A 1  61  ? -20.621 -16.936 -24.986 0.71 26.31   ? 61   SER   A OG  1 1 
ATOM   466   O  OG  B SER   A 1  61  ? -20.912 -18.09  -23.484 0.29 24.235  ? 61   SER   A OG  1 1 
ATOM   467   N  N   . GLN   A 1  62  ? -23.479 -14.903 -22.408 1    25.201  ? 62   GLN   A N   1 1 
ATOM   468   C  CA  . GLN   A 1  62  ? -24.092 -14.364 -21.204 1    26.228  ? 62   GLN   A CA  1 1 
ATOM   469   C  C   . GLN   A 1  62  ? -25.537 -14.854 -21.046 1    25.391  ? 62   GLN   A C   1 1 
ATOM   470   O  O   . GLN   A 1  62  ? -25.989 -15.091 -19.939 1    24.698  ? 62   GLN   A O   1 1 
ATOM   471   C  CB  . GLN   A 1  62  ? -24.031 -12.825 -21.126 1    26.637  ? 62   GLN   A CB  1 1 
ATOM   472   C  CG  . GLN   A 1  62  ? -22.627 -12.352 -20.772 1    27.941  ? 62   GLN   A CG  1 1 
ATOM   473   C  CD  . GLN   A 1  62  ? -22.288 -11.001 -21.384 1    27.587  ? 62   GLN   A CD  1 1 
ATOM   474   O  OE1 . GLN   A 1  62  ? -22.823 -10.642 -22.432 1    24.955  ? 62   GLN   A OE1 1 1 
ATOM   475   N  NE2 . GLN   A 1  62  ? -21.285 -10.349 -20.801 1    24.193  ? 62   GLN   A NE2 1 1 
ATOM   476   N  N   . GLU   A 1  63  ? -26.296 -14.935 -22.133 1    27.239  ? 63   GLU   A N   1 1 
ATOM   477   C  CA  . GLU   A 1  63  ? -27.674 -15.382 -21.985 1    29.959  ? 63   GLU   A CA  1 1 
ATOM   478   C  C   . GLU   A 1  63  ? -27.727 -16.828 -21.477 1    28.774  ? 63   GLU   A C   1 1 
ATOM   479   O  O   . GLU   A 1  63  ? -28.515 -17.159 -20.597 1    26.827  ? 63   GLU   A O   1 1 
ATOM   480   C  CB  . GLU   A 1  63  ? -28.406 -15.477 -23.319 1    35.78   ? 63   GLU   A CB  1 1 
ATOM   481   C  CG  . GLU   A 1  63  ? -29.015 -14.16  -23.766 1    42.797  ? 63   GLU   A CG  1 1 
ATOM   482   C  CD  . GLU   A 1  63  ? -29.871 -14.406 -25.006 1    49.852  ? 63   GLU   A CD  1 1 
ATOM   483   O  OE1 . GLU   A 1  63  ? -31.064 -14.753 -24.878 1    53.765  ? 63   GLU   A OE1 1 1 
ATOM   484   O  OE2 . GLU   A 1  63  ? -29.305 -14.314 -26.113 1    55.775  ? 63   GLU   A OE2 1 1 
ATOM   485   N  N   . PHE   A 1  64  ? -26.82  -17.643 -22.035 1    28.472  ? 64   PHE   A N   1 1 
ATOM   486   C  CA  . PHE   A 1  64  ? -26.632 -19.042 -21.666 1    28.488  ? 64   PHE   A CA  1 1 
ATOM   487   C  C   . PHE   A 1  64  ? -26.259 -19.119 -20.185 1    26.354  ? 64   PHE   A C   1 1 
ATOM   488   O  O   . PHE   A 1  64  ? -26.936 -19.78  -19.414 1    26.017  ? 64   PHE   A O   1 1 
ATOM   489   C  CB  . PHE   A 1  64  ? -25.599 -19.638 -22.628 1    28.055  ? 64   PHE   A CB  1 1 
ATOM   490   C  CG  . PHE   A 1  64  ? -25.374 -21.113 -22.341 1    29.732  ? 64   PHE   A CG  1 1 
ATOM   491   C  CD1 . PHE   A 1  64  ? -26.238 -22.069 -22.895 1    29.897  ? 64   PHE   A CD1 1 1 
ATOM   492   C  CD2 . PHE   A 1  64  ? -24.302 -21.522 -21.534 1    31.14   ? 64   PHE   A CD2 1 1 
ATOM   493   C  CE1 . PHE   A 1  64  ? -26.063 -23.418 -22.615 1    31.708  ? 64   PHE   A CE1 1 1 
ATOM   494   C  CE2 . PHE   A 1  64  ? -24.102 -22.894 -21.29  1    33.123  ? 64   PHE   A CE2 1 1 
ATOM   495   C  CZ  . PHE   A 1  64  ? -25.002 -23.829 -21.81  1    30.515  ? 64   PHE   A CZ  1 1 
ATOM   496   N  N   . ALA   A 1  65  ? -25.227 -18.372 -19.787 1    26.427  ? 65   ALA   A N   1 1 
ATOM   497   C  CA  . ALA   A 1  65  ? -24.722 -18.416 -18.43  1    25.525  ? 65   ALA   A CA  1 1 
ATOM   498   C  C   . ALA   A 1  65  ? -25.815 -18.007 -17.47  1    27.09   ? 65   ALA   A C   1 1 
ATOM   499   O  O   . ALA   A 1  65  ? -25.962 -18.602 -16.427 1    26.835  ? 65   ALA   A O   1 1 
ATOM   500   C  CB  . ALA   A 1  65  ? -23.488 -17.558 -18.267 1    26.416  ? 65   ALA   A CB  1 1 
ATOM   501   N  N   . GLU   A 1  66  ? -26.6   -16.971 -17.83  1    26.307  ? 66   GLU   A N   1 1 
ATOM   502   C  CA  . GLU   A 1  66  ? -27.622 -16.509 -16.935 1    27.545  ? 66   GLU   A CA  1 1 
ATOM   503   C  C   . GLU   A 1  66  ? -28.716 -17.583 -16.819 1    27.851  ? 66   GLU   A C   1 1 
ATOM   504   O  O   . GLU   A 1  66  ? -29.262 -17.789 -15.722 1    27.824  ? 66   GLU   A O   1 1 
ATOM   505   C  CB  . GLU   A 1  66  ? -28.143 -15.184 -17.529 1    31.824  ? 66   GLU   A CB  1 1 
ATOM   506   C  CG  . GLU   A 1  66  ? -29.479 -14.741 -16.967 1    35.798  ? 66   GLU   A CG  1 1 
ATOM   507   C  CD  . GLU   A 1  66  ? -30.194 -13.63  -17.777 1    44.489  ? 66   GLU   A CD  1 1 
ATOM   508   O  OE1 . GLU   A 1  66  ? -30.732 -12.792 -17.018 1    43.148  ? 66   GLU   A OE1 1 1 
ATOM   509   O  OE2 . GLU   A 1  66  ? -30.238 -13.545 -19.061 1    44.104  ? 66   GLU   A OE2 1 1 
ATOM   510   N  N   . ALA   A 1  67  ? -29.141 -18.202 -17.939 1    28.074  ? 67   ALA   A N   1 1 
ATOM   511   C  CA  . ALA   A 1  67  ? -30.242 -19.166 -17.794 1    31.021  ? 67   ALA   A CA  1 1 
ATOM   512   C  C   . ALA   A 1  67  ? -29.806 -20.398 -16.965 1    30.86   ? 67   ALA   A C   1 1 
ATOM   513   O  O   . ALA   A 1  67  ? -30.531 -20.838 -16.075 1    31.01   ? 67   ALA   A O   1 1 
ATOM   514   C  CB  . ALA   A 1  67  ? -30.859 -19.567 -19.127 1    31.885  ? 67   ALA   A CB  1 1 
ATOM   515   N  N   . TRP   A 1  68  ? -28.606 -20.932 -17.244 1    29.302  ? 68   TRP   A N   1 1 
ATOM   516   C  CA  . TRP   A 1  68  ? -28.18  -22.171 -16.595 1    29.97   ? 68   TRP   A CA  1 1 
ATOM   517   C  C   . TRP   A 1  68  ? -27.721 -21.876 -15.171 1    30.403  ? 68   TRP   A C   1 1 
ATOM   518   O  O   . TRP   A 1  68  ? -28.065 -22.62  -14.259 1    31.765  ? 68   TRP   A O   1 1 
ATOM   519   C  CB  . TRP   A 1  68  ? -27.062 -22.827 -17.407 1    27.575  ? 68   TRP   A CB  1 1 
ATOM   520   C  CG  . TRP   A 1  68  ? -27.693 -23.54  -18.57  1    28.344  ? 68   TRP   A CG  1 1 
ATOM   521   C  CD1 . TRP   A 1  68  ? -27.91  -23.069 -19.831 1    28.048  ? 68   TRP   A CD1 1 1 
ATOM   522   C  CD2 . TRP   A 1  68  ? -28.123 -24.913 -18.569 1    28.439  ? 68   TRP   A CD2 1 1 
ATOM   523   N  NE1 . TRP   A 1  68  ? -28.447 -24.055 -20.61  1    29.265  ? 68   TRP   A NE1 1 1 
ATOM   524   C  CE2 . TRP   A 1  68  ? -28.557 -25.205 -19.877 1    29.406  ? 68   TRP   A CE2 1 1 
ATOM   525   C  CE3 . TRP   A 1  68  ? -28.114 -25.932 -17.61  1    29.032  ? 68   TRP   A CE3 1 1 
ATOM   526   C  CZ2 . TRP   A 1  68  ? -29.047 -26.464 -20.232 1    30.441  ? 68   TRP   A CZ2 1 1 
ATOM   527   C  CZ3 . TRP   A 1  68  ? -28.615 -27.179 -17.959 1    29.886  ? 68   TRP   A CZ3 1 1 
ATOM   528   C  CH2 . TRP   A 1  68  ? -29.046 -27.441 -19.254 1    30.612  ? 68   TRP   A CH2 1 1 
ATOM   529   N  N   . GLY   A 1  69  ? -27.046 -20.718 -14.998 1    29.346  ? 69   GLY   A N   1 1 
ATOM   530   C  CA  . GLY   A 1  69  ? -26.74  -20.095 -13.715 1    28.721  ? 69   GLY   A CA  1 1 
ATOM   531   C  C   . GLY   A 1  69  ? -27.929 -19.907 -12.788 1    30.875  ? 69   GLY   A C   1 1 
ATOM   532   O  O   . GLY   A 1  69  ? -27.904 -20.361 -11.644 1    32.265  ? 69   GLY   A O   1 1 
ATOM   533   N  N   . GLN   A 1  70  ? -28.999 -19.21  -13.233 1    33.586  ? 70   GLN   A N   1 1 
ATOM   534   C  CA  . GLN   A 1  70  ? -30.136 -19.016 -12.354 1    34.72   ? 70   GLN   A CA  1 1 
ATOM   535   C  C   . GLN   A 1  70  ? -30.911 -20.302 -12.119 1    35.488  ? 70   GLN   A C   1 1 
ATOM   536   O  O   . GLN   A 1  70  ? -31.635 -20.396 -11.132 1    36.656  ? 70   GLN   A O   1 1 
ATOM   537   C  CB  . GLN   A 1  70  ? -31.257 -18.133 -12.901 1    42.192  ? 70   GLN   A CB  1 1 
ATOM   538   C  CG  . GLN   A 1  70  ? -30.683 -16.806 -13.378 1    51.484  ? 70   GLN   A CG  1 1 
ATOM   539   C  CD  . GLN   A 1  70  ? -31.803 -15.813 -13.549 1    58.561  ? 70   GLN   A CD  1 1 
ATOM   540   O  OE1 . GLN   A 1  70  ? -32.034 -15.269 -14.638 1    62.83   ? 70   GLN   A OE1 1 1 
ATOM   541   N  NE2 . GLN   A 1  70  ? -32.528 -15.616 -12.457 1    59.572  ? 70   GLN   A NE2 1 1 
ATOM   542   N  N   . LYS   A 1  71  ? -30.885 -21.229 -13.081 1    35.107  ? 71   LYS   A N   1 1 
ATOM   543   C  CA  . LYS   A 1  71  ? -31.489 -22.534 -12.84  1    35.692  ? 71   LYS   A CA  1 1 
ATOM   544   C  C   . LYS   A 1  71  ? -30.684 -23.28  -11.764 1    36.732  ? 71   LYS   A C   1 1 
ATOM   545   O  O   . LYS   A 1  71  ? -31.292 -23.868 -10.871 1    38.67   ? 71   LYS   A O   1 1 
ATOM   546   C  CB  . LYS   A 1  71  ? -31.6   -23.387 -14.11  1    34.009  ? 71   LYS   A CB  1 1 
ATOM   547   C  CG  . LYS   A 1  71  ? -32.37  -24.712 -13.951 1    33.736  ? 71   LYS   A CG  1 1 
ATOM   548   C  CD  . LYS   A 1  71  ? -33.832 -24.658 -13.516 1    35.461  ? 71   LYS   A CD  1 1 
ATOM   549   C  CE  . LYS   A 1  71  ? -34.658 -23.901 -14.489 1    34.689  ? 71   LYS   A CE  1 1 
ATOM   550   N  NZ  . LYS   A 1  71  ? -35.984 -23.748 -13.897 1    35.197  ? 71   LYS   A NZ  1 1 
ATOM   551   N  N   . ALA   A 1  72  ? -29.347 -23.29  -11.907 1    36.468  ? 72   ALA   A N   1 1 
ATOM   552   C  CA  . ALA   A 1  72  ? -28.449 -23.922 -10.932 1    37.551  ? 72   ALA   A CA  1 1 
ATOM   553   C  C   . ALA   A 1  72  ? -28.723 -23.329 -9.544  1    37.688  ? 72   ALA   A C   1 1 
ATOM   554   O  O   . ALA   A 1  72  ? -29.062 -24.045 -8.619  1    38.662  ? 72   ALA   A O   1 1 
ATOM   555   C  CB  . ALA   A 1  72  ? -27.002 -23.785 -11.345 1    34.533  ? 72   ALA   A CB  1 1 
ATOM   556   N  N   . LYS   A 1  73  ? -28.827 -22.011 -9.447  1    42.617  ? 73   LYS   A N   1 1 
ATOM   557   C  CA  . LYS   A 1  73  ? -29.33  -21.411 -8.213  1    43.9    ? 73   LYS   A CA  1 1 
ATOM   558   C  C   . LYS   A 1  73  ? -30.639 -21.999 -7.741  1    48.833  ? 73   LYS   A C   1 1 
ATOM   559   O  O   . LYS   A 1  73  ? -30.664 -22.636 -6.695  1    55.835  ? 73   LYS   A O   1 1 
ATOM   560   C  CB  . LYS   A 1  73  ? -29.392 -19.894 -8.249  1    48.093  ? 73   LYS   A CB  1 1 
ATOM   561   C  CG  . LYS   A 1  73  ? -27.955 -19.429 -8.397  1    47.17   ? 73   LYS   A CG  1 1 
ATOM   562   C  CD  . LYS   A 1  73  ? -27.917 -18.085 -7.712  1    45.038  ? 73   LYS   A CD  1 1 
ATOM   563   C  CE  . LYS   A 1  73  ? -26.851 -17.365 -8.392  1    45.434  ? 73   LYS   A CE  1 1 
ATOM   564   N  NZ  . LYS   A 1  73  ? -26.797 -16.182 -7.537  1    56.397  ? 73   LYS   A NZ  1 1 
ATOM   565   N  N   . GLU   A 1  74  ? -31.714 -21.777 -8.506  1    48.886  ? 74   GLU   A N   1 1 
ATOM   566   C  CA  . GLU   A 1  74  ? -33.082 -22.072 -8.116  1    47.354  ? 74   GLU   A CA  1 1 
ATOM   567   C  C   . GLU   A 1  74  ? -33.167 -23.475 -7.509  1    44.843  ? 74   GLU   A C   1 1 
ATOM   568   O  O   . GLU   A 1  74  ? -33.845 -23.669 -6.533  1    42.1    ? 74   GLU   A O   1 1 
ATOM   569   C  CB  . GLU   A 1  74  ? -33.927 -21.863 -9.378  1    46.889  ? 74   GLU   A CB  1 1 
ATOM   570   C  CG  . GLU   A 1  74  ? -35.336 -22.456 -9.347  1    52.503  ? 74   GLU   A CG  1 1 
ATOM   571   C  CD  . GLU   A 1  74  ? -36.077 -22.694 -10.675 1    51.904  ? 74   GLU   A CD  1 1 
ATOM   572   O  OE1 . GLU   A 1  74  ? -35.634 -22.278 -11.782 1    48.855  ? 74   GLU   A OE1 1 1 
ATOM   573   O  OE2 . GLU   A 1  74  ? -37.118 -23.378 -10.588 1    51.218  ? 74   GLU   A OE2 1 1 
ATOM   574   N  N   . LEU   A 1  75  ? -32.449 -24.451 -8.071  1    46.676  ? 75   LEU   A N   1 1 
ATOM   575   C  CA  . LEU   A 1  75  ? -32.595 -25.849 -7.668  1    47.831  ? 75   LEU   A CA  1 1 
ATOM   576   C  C   . LEU   A 1  75  ? -31.577 -26.292 -6.606  1    47.382  ? 75   LEU   A C   1 1 
ATOM   577   O  O   . LEU   A 1  75  ? -31.792 -27.296 -5.937  1    46.851  ? 75   LEU   A O   1 1 
ATOM   578   C  CB  . LEU   A 1  75  ? -32.421 -26.739 -8.894  1    46.835  ? 75   LEU   A CB  1 1 
ATOM   579   C  CG  . LEU   A 1  75  ? -33.484 -26.617 -9.986  1    45.609  ? 75   LEU   A CG  1 1 
ATOM   580   C  CD1 . LEU   A 1  75  ? -32.956 -27.49  -11.112 1    45.037  ? 75   LEU   A CD1 1 1 
ATOM   581   C  CD2 . LEU   A 1  75  ? -34.825 -27.049 -9.486  1    48.731  ? 75   LEU   A CD2 1 1 
ATOM   582   N  N   . TYR   A 1  76  ? -30.433 -25.623 -6.49   1    47.763  ? 76   TYR   A N   1 1 
ATOM   583   C  CA  . TYR   A 1  76  ? -29.334 -26.265 -5.778  1    47.856  ? 76   TYR   A CA  1 1 
ATOM   584   C  C   . TYR   A 1  76  ? -28.607 -25.276 -4.864  1    52.975  ? 76   TYR   A C   1 1 
ATOM   585   O  O   . TYR   A 1  76  ? -27.476 -25.544 -4.468  1    51.103  ? 76   TYR   A O   1 1 
ATOM   586   C  CB  . TYR   A 1  76  ? -28.338 -26.809 -6.807  1    46.281  ? 76   TYR   A CB  1 1 
ATOM   587   C  CG  . TYR   A 1  76  ? -28.929 -27.775 -7.818  1    43.507  ? 76   TYR   A CG  1 1 
ATOM   588   C  CD1 . TYR   A 1  76  ? -29.767 -28.796 -7.406  1    44.104  ? 76   TYR   A CD1 1 1 
ATOM   589   C  CD2 . TYR   A 1  76  ? -28.648 -27.648 -9.173  1    41.345  ? 76   TYR   A CD2 1 1 
ATOM   590   C  CE1 . TYR   A 1  76  ? -30.344 -29.669 -8.31   1    44.177  ? 76   TYR   A CE1 1 1 
ATOM   591   C  CE2 . TYR   A 1  76  ? -29.203 -28.521 -10.093 1    42.554  ? 76   TYR   A CE2 1 1 
ATOM   592   C  CZ  . TYR   A 1  76  ? -30.047 -29.532 -9.655  1    43.982  ? 76   TYR   A CZ  1 1 
ATOM   593   O  OH  . TYR   A 1  76  ? -30.612 -30.416 -10.525 1    43.918  ? 76   TYR   A OH  1 1 
ATOM   594   N  N   . GLU   A 1  77  ? -29.249 -24.157 -4.488  1    64.304  ? 77   GLU   A N   1 1 
ATOM   595   C  CA  . GLU   A 1  77  ? -28.514 -23.033 -3.91   1    69.668  ? 77   GLU   A CA  1 1 
ATOM   596   C  C   . GLU   A 1  77  ? -27.775 -23.486 -2.652  1    72.59   ? 77   GLU   A C   1 1 
ATOM   597   O  O   . GLU   A 1  77  ? -26.557 -23.291 -2.554  1    73.435  ? 77   GLU   A O   1 1 
ATOM   598   C  CB  . GLU   A 1  77  ? -29.285 -21.725 -3.683  1    66.999  ? 77   GLU   A CB  1 1 
ATOM   599   C  CG  . GLU   A 1  77  ? -28.389 -20.533 -3.335  1    64.615  ? 77   GLU   A CG  1 1 
ATOM   600   C  CD  . GLU   A 1  77  ? -27.014 -20.287 -3.965  1    62.377  ? 77   GLU   A CD  1 1 
ATOM   601   O  OE1 . GLU   A 1  77  ? -26.507 -21.064 -4.805  1    68.874  ? 77   GLU   A OE1 1 1 
ATOM   602   O  OE2 . GLU   A 1  77  ? -26.408 -19.265 -3.586  1    58.675  ? 77   GLU   A OE2 1 1 
ATOM   603   N  N   . PRO   A 1  78  ? -28.468 -24.112 -1.672  1    70.487  ? 78   PRO   A N   1 1 
ATOM   604   C  CA  . PRO   A 1  78  ? -27.78  -24.662 -0.494  1    73.651  ? 78   PRO   A CA  1 1 
ATOM   605   C  C   . PRO   A 1  78  ? -26.915 -25.891 -0.809  1    68.617  ? 78   PRO   A C   1 1 
ATOM   606   O  O   . PRO   A 1  78  ? -25.671 -25.853 -0.886  1    70.358  ? 78   PRO   A O   1 1 
ATOM   607   C  CB  . PRO   A 1  78  ? -28.981 -25.027 0.426   1    70.976  ? 78   PRO   A CB  1 1 
ATOM   608   C  CG  . PRO   A 1  78  ? -30.164 -24.249 -0.137  1    74.505  ? 78   PRO   A CG  1 1 
ATOM   609   C  CD  . PRO   A 1  78  ? -29.93  -24.309 -1.634  1    76.178  ? 78   PRO   A CD  1 1 
ATOM   610   N  N   . ILE   A 1  79  ? -27.66  -26.968 -1.042  1    63.152  ? 79   ILE   A N   1 1 
ATOM   611   C  CA  . ILE   A 1  79  ? -27.313 -28.373 -1.104  1    60.655  ? 79   ILE   A CA  1 1 
ATOM   612   C  C   . ILE   A 1  79  ? -26.108 -28.687 -2.002  1    54.602  ? 79   ILE   A C   1 1 
ATOM   613   O  O   . ILE   A 1  79  ? -25.634 -29.832 -2.004  1    50.792  ? 79   ILE   A O   1 1 
ATOM   614   C  CB  . ILE   A 1  79  ? -28.595 -29.065 -1.599  1    64.617  ? 79   ILE   A CB  1 1 
ATOM   615   C  CG1 . ILE   A 1  79  ? -28.651 -29.135 -3.137  1    63.677  ? 79   ILE   A CG1 1 1 
ATOM   616   C  CG2 . ILE   A 1  79  ? -29.814 -28.34  -1.008  1    63.155  ? 79   ILE   A CG2 1 1 
ATOM   617   C  CD1 . ILE   A 1  79  ? -30.043 -29.281 -3.722  1    61.416  ? 79   ILE   A CD1 1 1 
ATOM   618   N  N   . TRP   A 1  80  ? -25.658 -27.718 -2.816  1    50.951  ? 80   TRP   A N   1 1 
ATOM   619   C  CA  . TRP   A 1  80  ? -24.624 -28.042 -3.791  1    50.275  ? 80   TRP   A CA  1 1 
ATOM   620   C  C   . TRP   A 1  80  ? -23.298 -28.278 -3.067  1    49.822  ? 80   TRP   A C   1 1 
ATOM   621   O  O   . TRP   A 1  80  ? -22.426 -29.004 -3.554  1    46.215  ? 80   TRP   A O   1 1 
ATOM   622   C  CB  . TRP   A 1  80  ? -24.484 -26.961 -4.876  1    49.277  ? 80   TRP   A CB  1 1 
ATOM   623   C  CG  . TRP   A 1  80  ? -23.712 -25.707 -4.517  1    50.527  ? 80   TRP   A CG  1 1 
ATOM   624   C  CD1 . TRP   A 1  80  ? -24.24  -24.541 -4.026  1    52.26   ? 80   TRP   A CD1 1 1 
ATOM   625   C  CD2 . TRP   A 1  80  ? -22.293 -25.47  -4.683  1    46.637  ? 80   TRP   A CD2 1 1 
ATOM   626   N  NE1 . TRP   A 1  80  ? -23.255 -23.601 -3.874  1    48.694  ? 80   TRP   A NE1 1 1 
ATOM   627   C  CE2 . TRP   A 1  80  ? -22.051 -24.14  -4.258  1    47.623  ? 80   TRP   A CE2 1 1 
ATOM   628   C  CE3 . TRP   A 1  80  ? -21.205 -26.25  -5.129  1    46.018  ? 80   TRP   A CE3 1 1 
ATOM   629   C  CZ2 . TRP   A 1  80  ? -20.769 -23.579 -4.279  1    46.569  ? 80   TRP   A CZ2 1 1 
ATOM   630   C  CZ3 . TRP   A 1  80  ? -19.942 -25.705 -5.145  1    42.56   ? 80   TRP   A CZ3 1 1 
ATOM   631   C  CH2 . TRP   A 1  80  ? -19.733 -24.374 -4.734  1    46.842  ? 80   TRP   A CH2 1 1 
ATOM   632   N  N   . GLN   A 1  81  ? -23.175 -27.649 -1.89   1    46.427  ? 81   GLN   A N   1 1 
ATOM   633   C  CA  . GLN   A 1  81  ? -21.919 -27.69  -1.166  1    49.424  ? 81   GLN   A CA  1 1 
ATOM   634   C  C   . GLN   A 1  81  ? -21.784 -29.024 -0.443  1    45.586  ? 81   GLN   A C   1 1 
ATOM   635   O  O   . GLN   A 1  81  ? -20.669 -29.376 -0.091  1    46.563  ? 81   GLN   A O   1 1 
ATOM   636   C  CB  . GLN   A 1  81  ? -21.867 -26.533 -0.179  1    50.648  ? 81   GLN   A CB  1 1 
ATOM   637   C  CG  . GLN   A 1  81  ? -21.376 -25.258 -0.845  1    53.57   ? 81   GLN   A CG  1 1 
ATOM   638   C  CD  . GLN   A 1  81  ? -21.721 -24.04  -0.023  1    56.184  ? 81   GLN   A CD  1 1 
ATOM   639   O  OE1 . GLN   A 1  81  ? -21.183 -22.964 -0.27   1    54.377  ? 81   GLN   A OE1 1 1 
ATOM   640   N  NE2 . GLN   A 1  81  ? -22.607 -24.208 0.957   1    59.273  ? 81   GLN   A NE2 1 1 
ATOM   641   N  N   . GLN   A 1  82  ? -22.913 -29.738 -0.288  1    45.265  ? 82   GLN   A N   1 1 
ATOM   642   C  CA  . GLN   A 1  82  ? -22.993 -30.986 0.447   1    46.058  ? 82   GLN   A CA  1 1 
ATOM   643   C  C   . GLN   A 1  82  ? -23.009 -32.194 -0.487  1    42.933  ? 82   GLN   A C   1 1 
ATOM   644   O  O   . GLN   A 1  82  ? -23.063 -33.326 -0.031  1    40.137  ? 82   GLN   A O   1 1 
ATOM   645   C  CB  . GLN   A 1  82  ? -24.14  -30.916 1.455   1    48.814  ? 82   GLN   A CB  1 1 
ATOM   646   C  CG  . GLN   A 1  82  ? -23.721 -30.274 2.767   1    51.981  ? 82   GLN   A CG  1 1 
ATOM   647   C  CD  . GLN   A 1  82  ? -24.099 -28.823 2.855   1    53.3    ? 82   GLN   A CD  1 1 
ATOM   648   O  OE1 . GLN   A 1  82  ? -23.78  -28.009 1.98    1    57.651  ? 82   GLN   A OE1 1 1 
ATOM   649   N  NE2 . GLN   A 1  82  ? -24.829 -28.497 3.912   1    57.884  ? 82   GLN   A NE2 1 1 
ATOM   650   N  N   . PHE   A 1  83  ? -22.955 -31.966 -1.809  1    42.81   ? 83   PHE   A N   1 1 
ATOM   651   C  CA  . PHE   A 1  83  ? -22.908 -33.091 -2.753  1    42.109  ? 83   PHE   A CA  1 1 
ATOM   652   C  C   . PHE   A 1  83  ? -21.768 -34.082 -2.433  1    40.716  ? 83   PHE   A C   1 1 
ATOM   653   O  O   . PHE   A 1  83  ? -20.609 -33.723 -2.214  1    40.92   ? 83   PHE   A O   1 1 
ATOM   654   C  CB  . PHE   A 1  83  ? -22.868 -32.724 -4.248  1    39.82   ? 83   PHE   A CB  1 1 
ATOM   655   C  CG  . PHE   A 1  83  ? -24.074 -32.023 -4.877  1    38.636  ? 83   PHE   A CG  1 1 
ATOM   656   C  CD1 . PHE   A 1  83  ? -25.337 -32.063 -4.268  1    40.665  ? 83   PHE   A CD1 1 1 
ATOM   657   C  CD2 . PHE   A 1  83  ? -23.924 -31.293 -6.062  1    37.371  ? 83   PHE   A CD2 1 1 
ATOM   658   C  CE1 . PHE   A 1  83  ? -26.44  -31.409 -4.825  1    43.073  ? 83   PHE   A CE1 1 1 
ATOM   659   C  CE2 . PHE   A 1  83  ? -25.033 -30.648 -6.618  1    39.899  ? 83   PHE   A CE2 1 1 
ATOM   660   C  CZ  . PHE   A 1  83  ? -26.272 -30.673 -5.983  1    41.854  ? 83   PHE   A CZ  1 1 
ATOM   661   N  N   . THR   A 1  84  ? -22.102 -35.357 -2.518  1    41.912  ? 84   THR   A N   1 1 
ATOM   662   C  CA  . THR   A 1  84  ? -21.119 -36.414 -2.304  1    43.918  ? 84   THR   A CA  1 1 
ATOM   663   C  C   . THR   A 1  84  ? -20.074 -36.413 -3.425  1    40.726  ? 84   THR   A C   1 1 
ATOM   664   O  O   . THR   A 1  84  ? -18.933 -36.87  -3.197  1    38.575  ? 84   THR   A O   1 1 
ATOM   665   C  CB  . THR   A 1  84  ? -21.876 -37.734 -2.134  1    45.766  ? 84   THR   A CB  1 1 
ATOM   666   O  OG1 . THR   A 1  84  ? -22.592 -37.52  -0.907  1    50.754  ? 84   THR   A OG1 1 1 
ATOM   667   C  CG2 . THR   A 1  84  ? -21.009 -38.985 -2.095  1    46.773  ? 84   THR   A CG2 1 1 
ATOM   668   N  N   . ASP   A 1  85  ? -20.477 -35.945 -4.636  1    36.781  ? 85   ASP   A N   1 1 
ATOM   669   C  CA  . ASP   A 1  85  ? -19.604 -36.079 -5.803  1    33.708  ? 85   ASP   A CA  1 1 
ATOM   670   C  C   . ASP   A 1  85  ? -18.731 -34.847 -5.851  1    31.1    ? 85   ASP   A C   1 1 
ATOM   671   O  O   . ASP   A 1  85  ? -19.249 -33.79  -6.211  1    30.587  ? 85   ASP   A O   1 1 
ATOM   672   C  CB  . ASP   A 1  85  ? -20.361 -36.254 -7.117  1    33.452  ? 85   ASP   A CB  1 1 
ATOM   673   C  CG  . ASP   A 1  85  ? -19.528 -36.524 -8.38   1    33.495  ? 85   ASP   A CG  1 1 
ATOM   674   O  OD1 . ASP   A 1  85  ? -18.374 -36.131 -8.462  1    31.031  ? 85   ASP   A OD1 1 1 
ATOM   675   O  OD2 . ASP   A 1  85  ? -20.047 -37.15  -9.316  1    38.043  ? 85   ASP   A OD2 1 1 
ATOM   676   N  N   . PRO   A 1  86  ? -17.394 -34.921 -5.62   1    31.005  ? 86   PRO   A N   1 1 
ATOM   677   C  CA  . PRO   A 1  86  ? -16.602 -33.686 -5.577  1    30.644  ? 86   PRO   A CA  1 1 
ATOM   678   C  C   . PRO   A 1  86  ? -16.563 -32.993 -6.933  1    29.517  ? 86   PRO   A C   1 1 
ATOM   679   O  O   . PRO   A 1  86  ? -16.491 -31.79  -6.996  1    29.586  ? 86   PRO   A O   1 1 
ATOM   680   C  CB  . PRO   A 1  86  ? -15.14  -34.138 -5.136  1    29.515  ? 86   PRO   A CB  1 1 
ATOM   681   C  CG  . PRO   A 1  86  ? -15.087 -35.63  -5.48   1    30.669  ? 86   PRO   A CG  1 1 
ATOM   682   C  CD  . PRO   A 1  86  ? -16.557 -36.143 -5.474  1    30.16   ? 86   PRO   A CD  1 1 
ATOM   683   N  N   . GLN   A 1  87  ? -16.462 -33.758 -8.015  1    29.021  ? 87   GLN   A N   1 1 
ATOM   684   C  CA  . GLN   A 1  87  ? -16.385 -33.172 -9.34   1    27.952  ? 87   GLN   A CA  1 1 
ATOM   685   C  C   . GLN   A 1  87  ? -17.691 -32.442 -9.689  1    29.653  ? 87   GLN   A C   1 1 
ATOM   686   O  O   . GLN   A 1  87  ? -17.632 -31.354 -10.27  1    29.333  ? 87   GLN   A O   1 1 
ATOM   687   C  CB  . GLN   A 1  87  ? -16.076 -34.236 -10.39  1    31.812  ? 87   GLN   A CB  1 1 
ATOM   688   C  CG  . GLN   A 1  87  ? -14.648 -34.785 -10.289 1    38.101  ? 87   GLN   A CG  1 1 
ATOM   689   C  CD  . GLN   A 1  87  ? -14.364 -35.717 -11.451 1    51.89   ? 87   GLN   A CD  1 1 
ATOM   690   O  OE1 . GLN   A 1  87  ? -15.048 -35.66  -12.483 1    64.397  ? 87   GLN   A OE1 1 1 
ATOM   691   N  NE2 . GLN   A 1  87  ? -13.389 -36.604 -11.298 1    53.516  ? 87   GLN   A NE2 1 1 
ATOM   692   N  N   . LEU   A 1  88  ? -18.837 -33.035 -9.322  1    29.396  ? 88   LEU   A N   1 1 
ATOM   693   C  CA  . LEU   A 1  88  ? -20.155 -32.41  -9.453  1    30.153  ? 88   LEU   A CA  1 1 
ATOM   694   C  C   . LEU   A 1  88  ? -20.248 -31.111 -8.622  1    31.547  ? 88   LEU   A C   1 1 
ATOM   695   O  O   . LEU   A 1  88  ? -20.805 -30.102 -9.096  1    29.258  ? 88   LEU   A O   1 1 
ATOM   696   C  CB  . LEU   A 1  88  ? -21.245 -33.413 -9.077  1    29.025  ? 88   LEU   A CB  1 1 
ATOM   697   C  CG  . LEU   A 1  88  ? -22.666 -32.869 -9.231  1    30.973  ? 88   LEU   A CG  1 1 
ATOM   698   C  CD1 . LEU   A 1  88  ? -22.782 -32.42  -10.701 1    30.338  ? 88   LEU   A CD1 1 1 
ATOM   699   C  CD2 . LEU   A 1  88  ? -23.743 -33.891 -8.849  1    32.223  ? 88   LEU   A CD2 1 1 
ATOM   700   N  N   . ARG   A 1  89  ? -19.692 -31.088 -7.385  1    31.569  ? 89   ARG   A N   1 1 
ATOM   701   C  CA  . ARG   A 1  89  ? -19.704 -29.795 -6.704  1    32.44   ? 89   ARG   A CA  1 1 
ATOM   702   C  C   . ARG   A 1  89  ? -18.887 -28.766 -7.513  1    29.922  ? 89   ARG   A C   1 1 
ATOM   703   O  O   . ARG   A 1  89  ? -19.194 -27.574 -7.62   1    27.996  ? 89   ARG   A O   1 1 
ATOM   704   C  CB  . ARG   A 1  89  ? -19.051 -29.869 -5.322  1    35.83   ? 89   ARG   A CB  1 1 
ATOM   705   C  CG  . ARG   A 1  89  ? -19.843 -30.651 -4.299  1    37.946  ? 89   ARG   A CG  1 1 
ATOM   706   C  CD  . ARG   A 1  89  ? -19.323 -30.405 -2.879  1    41.199  ? 89   ARG   A CD  1 1 
ATOM   707   N  NE  . ARG   A 1  89  ? -17.898 -30.739 -2.732  1    40.756  ? 89   ARG   A NE  1 1 
ATOM   708   C  CZ  . ARG   A 1  89  ? -17.353 -31.922 -2.446  1    41.923  ? 89   ARG   A CZ  1 1 
ATOM   709   N  NH1 . ARG   A 1  89  ? -16.045 -31.939 -2.176  1    40.389  ? 89   ARG   A NH1 1 1 
ATOM   710   N  NH2 . ARG   A 1  89  ? -18.093 -33.033 -2.358  1    39.572  ? 89   ARG   A NH2 1 1 
ATOM   711   N  N   . ARG   A 1  90  ? -17.772 -29.2   -8.103  1    28.23   ? 90   ARG   A N   1 1 
ATOM   712   C  CA  . ARG   A 1  90  ? -16.943 -28.188 -8.77   1    26.219  ? 90   ARG   A CA  1 1 
ATOM   713   C  C   . ARG   A 1  90  ? -17.672 -27.673 -10.025 1    27.27   ? 90   ARG   A C   1 1 
ATOM   714   O  O   . ARG   A 1  90  ? -17.559 -26.477 -10.383 1    24.934  ? 90   ARG   A O   1 1 
ATOM   715   C  CB  . ARG   A 1  90  ? -15.573 -28.741 -9.188  1    25.703  ? 90   ARG   A CB  1 1 
ATOM   716   C  CG  . ARG   A 1  90  ? -14.654 -28.986 -7.99   1    29.348  ? 90   ARG   A CG  1 1 
ATOM   717   C  CD  . ARG   A 1  90  ? -13.34  -29.765 -8.298  1    31.31   ? 90   ARG   A CD  1 1 
ATOM   718   N  NE  . ARG   A 1  90  ? -12.383 -29.293 -7.284  1    37.102  ? 90   ARG   A NE  1 1 
ATOM   719   C  CZ  . ARG   A 1  90  ? -11.381 -28.425 -7.442  1    37.417  ? 90   ARG   A CZ  1 1 
ATOM   720   N  NH1 . ARG   A 1  90  ? -10.714 -27.966 -6.391  1    40.781  ? 90   ARG   A NH1 1 1 
ATOM   721   N  NH2 . ARG   A 1  90  ? -11.068 -27.955 -8.626  1    32.685  ? 90   ARG   A NH2 1 1 
ATOM   722   N  N   . ILE   A 1  91  ? -18.405 -28.593 -10.695 1    26.224  ? 91   ILE   A N   1 1 
ATOM   723   C  CA  . ILE   A 1  91  ? -19.077 -28.209 -11.917 1    27.996  ? 91   ILE   A CA  1 1 
ATOM   724   C  C   . ILE   A 1  91  ? -20.213 -27.253 -11.583 1    30.287  ? 91   ILE   A C   1 1 
ATOM   725   O  O   . ILE   A 1  91  ? -20.319 -26.188 -12.212 1    27.644  ? 91   ILE   A O   1 1 
ATOM   726   C  CB  . ILE   A 1  91  ? -19.602 -29.433 -12.671 1    28.219  ? 91   ILE   A CB  1 1 
ATOM   727   C  CG1 . ILE   A 1  91  ? -18.444 -30.346 -13.154 1    28.006  ? 91   ILE   A CG1 1 1 
ATOM   728   C  CG2 . ILE   A 1  91  ? -20.526 -28.96  -13.796 1    28.519  ? 91   ILE   A CG2 1 1 
ATOM   729   C  CD1 . ILE   A 1  91  ? -18.918 -31.735 -13.611 1    29.852  ? 91   ILE   A CD1 1 1 
ATOM   730   N  N   . ILE   A 1  92  ? -21.008 -27.625 -10.563 1    29.994  ? 92   ILE   A N   1 1 
ATOM   731   C  CA  . ILE   A 1  92  ? -22.127 -26.779 -10.16  1    30.648  ? 92   ILE   A CA  1 1 
ATOM   732   C  C   . ILE   A 1  92  ? -21.614 -25.431 -9.696  1    28.606  ? 92   ILE   A C   1 1 
ATOM   733   O  O   . ILE   A 1  92  ? -22.239 -24.39  -9.917  1    28.99   ? 92   ILE   A O   1 1 
ATOM   734   C  CB  . ILE   A 1  92  ? -23.011 -27.429 -9.081  1    32.503  ? 92   ILE   A CB  1 1 
ATOM   735   C  CG1 . ILE   A 1  92  ? -23.688 -28.737 -9.56   1    31.614  ? 92   ILE   A CG1 1 1 
ATOM   736   C  CG2 . ILE   A 1  92  ? -24.029 -26.44  -8.481  1    35.896  ? 92   ILE   A CG2 1 1 
ATOM   737   C  CD1 . ILE   A 1  92  ? -24.535 -28.626 -10.82  1    32.357  ? 92   ILE   A CD1 1 1 
ATOM   738   N  N   . GLY   A 1  93  ? -20.547 -25.472 -8.906  1    28.616  ? 93   GLY   A N   1 1 
ATOM   739   C  CA  . GLY   A 1  93  ? -19.957 -24.261 -8.336  1    28.267  ? 93   GLY   A CA  1 1 
ATOM   740   C  C   . GLY   A 1  93  ? -19.584 -23.246 -9.418  1    26.245  ? 93   GLY   A C   1 1 
ATOM   741   O  O   . GLY   A 1  93  ? -19.879 -22.098 -9.266  1    26.905  ? 93   GLY   A O   1 1 
ATOM   742   N  N   . ALA   A 1  94  ? -19.012 -23.7   -10.536 1    26.538  ? 94   ALA   A N   1 1 
ATOM   743   C  CA  . ALA   A 1  94  ? -18.656 -22.887 -11.701 1    26.123  ? 94   ALA   A CA  1 1 
ATOM   744   C  C   . ALA   A 1  94  ? -19.914 -22.339 -12.396 1    28.758  ? 94   ALA   A C   1 1 
ATOM   745   O  O   . ALA   A 1  94  ? -19.987 -21.129 -12.626 1    29.32   ? 94   ALA   A O   1 1 
ATOM   746   C  CB  . ALA   A 1  94  ? -17.881 -23.734 -12.67  1    27.099  ? 94   ALA   A CB  1 1 
ATOM   747   N  N   . VAL   A 1  95  ? -20.896 -23.229 -12.696 1    26.547  ? 95   VAL   A N   1 1 
ATOM   748   C  CA  . VAL   A 1  95  ? -22.135 -22.884 -13.391 1    27.636  ? 95   VAL   A CA  1 1 
ATOM   749   C  C   . VAL   A 1  95  ? -22.869 -21.775 -12.623 1    27.463  ? 95   VAL   A C   1 1 
ATOM   750   O  O   . VAL   A 1  95  ? -23.364 -20.804 -13.205 1    28.025  ? 95   VAL   A O   1 1 
ATOM   751   C  CB  . VAL   A 1  95  ? -23.028 -24.116 -13.711 1    26.984  ? 95   VAL   A CB  1 1 
ATOM   752   C  CG1 . VAL   A 1  95  ? -24.283 -23.716 -14.488 1    27.212  ? 95   VAL   A CG1 1 1 
ATOM   753   C  CG2 . VAL   A 1  95  ? -22.299 -25.141 -14.575 1    27.004  ? 95   VAL   A CG2 1 1 
ATOM   754   N  N   . ARG   A 1  96  ? -22.956 -21.89  -11.296 1    27.956  ? 96   ARG   A N   1 1 
ATOM   755   C  CA  . ARG   A 1  96  ? -23.661 -20.879 -10.52  1    28.315  ? 96   ARG   A CA  1 1 
ATOM   756   C  C   . ARG   A 1  96  ? -22.924 -19.526 -10.405 1    30.765  ? 96   ARG   A C   1 1 
ATOM   757   O  O   . ARG   A 1  96  ? -23.48  -18.586 -9.805  1    31.807  ? 96   ARG   A O   1 1 
ATOM   758   C  CB  . ARG   A 1  96  ? -23.985 -21.486 -9.147  1    34.522  ? 96   ARG   A CB  1 1 
ATOM   759   C  CG  . ARG   A 1  96  ? -24.249 -20.715 -7.854  1    46.085  ? 96   ARG   A CG  1 1 
ATOM   760   C  CD  . ARG   A 1  96  ? -22.911 -20.298 -7.137  1    45.776  ? 96   ARG   A CD  1 1 
ATOM   761   N  NE  . ARG   A 1  96  ? -23.204 -19.25  -6.144  1    52.545  ? 96   ARG   A NE  1 1 
ATOM   762   C  CZ  . ARG   A 1  96  ? -22.67  -18.014 -6.076  1    52.926  ? 96   ARG   A CZ  1 1 
ATOM   763   N  NH1 . ARG   A 1  96  ? -23.226 -17.123 -5.261  1    49.186  ? 96   ARG   A NH1 1 1 
ATOM   764   N  NH2 . ARG   A 1  96  ? -21.602 -17.669 -6.813  1    51.78   ? 96   ARG   A NH2 1 1 
ATOM   765   N  N   . THR   A 1  97  ? -21.68  -19.406 -10.894 1    28.712  ? 97   THR   A N   1 1 
ATOM   766   C  CA  . THR   A 1  97  ? -21.031 -18.089 -10.883 1    30.476  ? 97   THR   A CA  1 1 
ATOM   767   C  C   . THR   A 1  97  ? -21.276 -17.392 -12.217 1    28.278  ? 97   THR   A C   1 1 
ATOM   768   O  O   . THR   A 1  97  ? -20.911 -17.952 -13.257 1    29.523  ? 97   THR   A O   1 1 
ATOM   769   C  CB  . THR   A 1  97  ? -19.539 -18.234 -10.511 1    31.329  ? 97   THR   A CB  1 1 
ATOM   770   O  OG1 . THR   A 1  97  ? -19.729 -18.241 -9.092  1    34.631  ? 97   THR   A OG1 1 1 
ATOM   771   C  CG2 . THR   A 1  97  ? -18.721 -16.993 -10.824 1    28.858  ? 97   THR   A CG2 1 1 
ATOM   772   N  N   . LEU   A 1  98  ? -22.032 -16.277 -12.175 1    31.054  ? 98   LEU   A N   1 1 
ATOM   773   C  CA  . LEU   A 1  98  ? -22.626 -15.665 -13.368 1    31.958  ? 98   LEU   A CA  1 1 
ATOM   774   C  C   . LEU   A 1  98  ? -21.678 -14.646 -14.007 1    29.664  ? 98   LEU   A C   1 1 
ATOM   775   O  O   . LEU   A 1  98  ? -21.707 -14.44  -15.215 1    31.061  ? 98   LEU   A O   1 1 
ATOM   776   C  CB  . LEU   A 1  98  ? -24.047 -15.086 -13.184 1    32.99   ? 98   LEU   A CB  1 1 
ATOM   777   C  CG  . LEU   A 1  98  ? -25.249 -16.047 -13.246 1    33.386  ? 98   LEU   A CG  1 1 
ATOM   778   C  CD1 . LEU   A 1  98  ? -25.409 -16.793 -11.914 1    35.198  ? 98   LEU   A CD1 1 1 
ATOM   779   C  CD2 . LEU   A 1  98  ? -26.59  -15.319 -13.469 1    34.247  ? 98   LEU   A CD2 1 1 
ATOM   780   N  N   . GLY   A 1  99  ? -20.821 -14.028 -13.195 1    27.684  ? 99   GLY   A N   1 1 
ATOM   781   C  CA  . GLY   A 1  99  ? -19.972 -12.932 -13.635 1    25.47   ? 99   GLY   A CA  1 1 
ATOM   782   C  C   . GLY   A 1  99  ? -20.768 -11.864 -14.391 1    22.197  ? 99   GLY   A C   1 1 
ATOM   783   O  O   . GLY   A 1  99  ? -21.802 -11.398 -13.896 1    22.11   ? 99   GLY   A O   1 1 
ATOM   784   N  N   . SER   A 1  100 ? -20.242 -11.487 -15.56  1    22.131  ? 100  SER   A N   1 1 
ATOM   785   C  CA  . SER   A 1  100 ? -20.839 -10.427 -16.385 1    23.962  ? 100  SER   A CA  1 1 
ATOM   786   C  C   . SER   A 1  100 ? -22.306 -10.718 -16.74  1    26      ? 100  SER   A C   1 1 
ATOM   787   O  O   . SER   A 1  100 ? -23.129 -9.8    -17.005 1    27.028  ? 100  SER   A O   1 1 
ATOM   788   C  CB  . SER   A 1  100 ? -19.974 -10.209 -17.585 1    25.316  ? 100  SER   A CB  1 1 
ATOM   789   O  OG  . SER   A 1  100 ? -20.109 -11.311 -18.484 1    25.555  ? 100  SER   A OG  1 1 
ATOM   790   N  N   . ALA   A 1  101 ? -22.701 -12.006 -16.662 1    24.068  ? 101  ALA   A N   1 1 
ATOM   791   C  CA  . ALA   A 1  101 ? -24.107 -12.388 -16.879 1    24.594  ? 101  ALA   A CA  1 1 
ATOM   792   C  C   . ALA   A 1  101 ? -25.03  -11.849 -15.798 1    25.093  ? 101  ALA   A C   1 1 
ATOM   793   O  O   . ALA   A 1  101 ? -26.279 -11.848 -15.949 1    27.093  ? 101  ALA   A O   1 1 
ATOM   794   C  CB  . ALA   A 1  101 ? -24.275 -13.898 -17.081 1    23.547  ? 101  ALA   A CB  1 1 
ATOM   795   N  N   . ASN   A 1  102 ? -24.45  -11.323 -14.704 1    24      ? 102  ASN   A N   1 1 
ATOM   796   C  CA  . ASN   A 1  102 ? -25.292 -10.712 -13.678 1    24.414  ? 102  ASN   A CA  1 1 
ATOM   797   C  C   . ASN   A 1  102 ? -25.741 -9.308  -14.094 1    24.056  ? 102  ASN   A C   1 1 
ATOM   798   O  O   . ASN   A 1  102 ? -26.666 -8.764  -13.52  1    25.351  ? 102  ASN   A O   1 1 
ATOM   799   C  CB  . ASN   A 1  102 ? -24.56  -10.538 -12.35  1    24.065  ? 102  ASN   A CB  1 1 
ATOM   800   C  CG  . ASN   A 1  102 ? -24.586 -11.841 -11.56  1    25.734  ? 102  ASN   A CG  1 1 
ATOM   801   O  OD1 . ASN   A 1  102 ? -25.648 -12.458 -11.388 1    24.548  ? 102  ASN   A OD1 1 1 
ATOM   802   N  ND2 . ASN   A 1  102 ? -23.424 -12.293 -11.115 1    25.443  ? 102  ASN   A ND2 1 1 
ATOM   803   N  N   . LEU   A 1  103 ? -25.032 -8.685  -15.033 1    22.428  ? 103  LEU   A N   1 1 
ATOM   804   C  CA  . LEU   A 1  103 ? -25.412 -7.313  -15.396 1    21.501  ? 103  LEU   A CA  1 1 
ATOM   805   C  C   . LEU   A 1  103 ? -26.736 -7.333  -16.152 1    22.337  ? 103  LEU   A C   1 1 
ATOM   806   O  O   . LEU   A 1  103 ? -26.985 -8.235  -16.94  1    22.253  ? 103  LEU   A O   1 1 
ATOM   807   C  CB  . LEU   A 1  103 ? -24.297 -6.723  -16.255 1    19.834  ? 103  LEU   A CB  1 1 
ATOM   808   C  CG  . LEU   A 1  103 ? -22.893 -6.576  -15.61  1    18.845  ? 103  LEU   A CG  1 1 
ATOM   809   C  CD1 . LEU   A 1  103 ? -21.846 -6.226  -16.659 1    17.481  ? 103  LEU   A CD1 1 1 
ATOM   810   C  CD2 . LEU   A 1  103 ? -23.015 -5.466  -14.529 1    18.597  ? 103  LEU   A CD2 1 1 
ATOM   811   N  N   . PRO   A 1  104 ? -27.563 -6.272  -16.06  1    23.656  ? 104  PRO   A N   1 1 
ATOM   812   C  CA  . PRO   A 1  104 ? -28.723 -6.179  -16.948 1    25.256  ? 104  PRO   A CA  1 1 
ATOM   813   C  C   . PRO   A 1  104 ? -28.2   -6.004  -18.401 1    25.275  ? 104  PRO   A C   1 1 
ATOM   814   O  O   . PRO   A 1  104 ? -27.056 -5.633  -18.61  1    23.791  ? 104  PRO   A O   1 1 
ATOM   815   C  CB  . PRO   A 1  104 ? -29.54  -5.009  -16.366 1    25.796  ? 104  PRO   A CB  1 1 
ATOM   816   C  CG  . PRO   A 1  104 ? -28.561 -4.222  -15.442 1    25.139  ? 104  PRO   A CG  1 1 
ATOM   817   C  CD  . PRO   A 1  104 ? -27.396 -5.142  -15.103 1    23.718  ? 104  PRO   A CD  1 1 
ATOM   818   N  N   . LEU   A 1  105 ? -29.04  -6.259  -19.407 1    25.927  ? 105  LEU   A N   1 1 
ATOM   819   C  CA  . LEU   A 1  105 ? -28.646 -6.258  -20.819 1    26.187  ? 105  LEU   A CA  1 1 
ATOM   820   C  C   . LEU   A 1  105 ? -27.85  -5.007  -21.239 1    24.743  ? 105  LEU   A C   1 1 
ATOM   821   O  O   . LEU   A 1  105 ? -26.801 -5.132  -21.834 1    25.007  ? 105  LEU   A O   1 1 
ATOM   822   C  CB  . LEU   A 1  105 ? -29.922 -6.45   -21.644 1    27.394  ? 105  LEU   A CB  1 1 
ATOM   823   C  CG  . LEU   A 1  105 ? -29.773 -6.442  -23.176 1    28.788  ? 105  LEU   A CG  1 1 
ATOM   824   C  CD1 . LEU   A 1  105 ? -28.705 -7.448  -23.661 1    29.012  ? 105  LEU   A CD1 1 1 
ATOM   825   C  CD2 . LEU   A 1  105 ? -31.083 -6.578  -23.993 1    30.53   ? 105  LEU   A CD2 1 1 
ATOM   826   N  N   . ALA   A 1  106 ? -28.341 -3.791  -20.958 1    25.373  ? 106  ALA   A N   1 1 
ATOM   827   C  CA  . ALA   A 1  106 ? -27.648 -2.576  -21.367 1    24.428  ? 106  ALA   A CA  1 1 
ATOM   828   C  C   . ALA   A 1  106 ? -26.219 -2.602  -20.83  1    23.342  ? 106  ALA   A C   1 1 
ATOM   829   O  O   . ALA   A 1  106 ? -25.281 -2.229  -21.535 1    22.96   ? 106  ALA   A O   1 1 
ATOM   830   C  CB  . ALA   A 1  106 ? -28.419 -1.324  -20.918 1    24.881  ? 106  ALA   A CB  1 1 
ATOM   831   N  N   . LYS   A 1  107 ? -26.038 -3.046  -19.588 1    22.166  ? 107  LYS   A N   1 1 
ATOM   832   C  CA  . LYS   A 1  107 ? -24.702 -3.014  -19.034 1    21.375  ? 107  LYS   A CA  1 1 
ATOM   833   C  C   . LYS   A 1  107 ? -23.865 -4.154  -19.604 1    20.574  ? 107  LYS   A C   1 1 
ATOM   834   O  O   . LYS   A 1  107 ? -22.648 -4.02   -19.745 1    19.154  ? 107  LYS   A O   1 1 
ATOM   835   C  CB  . LYS   A 1  107 ? -24.754 -3.047  -17.504 1    21.45   ? 107  LYS   A CB  1 1 
ATOM   836   C  CG  . LYS   A 1  107 ? -25.102 -1.669  -16.958 1    22.953  ? 107  LYS   A CG  1 1 
ATOM   837   C  CD  . LYS   A 1  107 ? -25.194 -1.657  -15.437 1    25.203  ? 107  LYS   A CD  1 1 
ATOM   838   C  CE  . LYS   A 1  107 ? -25.953 -0.484  -14.924 1    27.941  ? 107  LYS   A CE  1 1 
ATOM   839   N  NZ  . LYS   A 1  107 ? -25.057 -0.217  -13.821 1    29.208  ? 107  LYS   A NZ  1 1 
ATOM   840   N  N   . ARG   A 1  108 ? -24.514 -5.284  -19.912 1    21.944  ? 108  ARG   A N   1 1 
ATOM   841   C  CA  . ARG   A 1  108 ? -23.787 -6.375  -20.56  1    21.485  ? 108  ARG   A CA  1 1 
ATOM   842   C  C   . ARG   A 1  108 ? -23.252 -5.905  -21.916 1    21.551  ? 108  ARG   A C   1 1 
ATOM   843   O  O   . ARG   A 1  108 ? -22.13  -6.268  -22.287 1    22.051  ? 108  ARG   A O   1 1 
ATOM   844   C  CB  . ARG   A 1  108 ? -24.701 -7.573  -20.89  1    23.669  ? 108  ARG   A CB  1 1 
ATOM   845   C  CG  . ARG   A 1  108 ? -24.888 -8.673  -19.861 1    24.281  ? 108  ARG   A CG  1 1 
ATOM   846   C  CD  . ARG   A 1  108 ? -25.907 -9.657  -20.39  1    26.039  ? 108  ARG   A CD  1 1 
ATOM   847   N  NE  . ARG   A 1  108 ? -26.705 -10.102 -19.249 1    26.723  ? 108  ARG   A NE  1 1 
ATOM   848   C  CZ  . ARG   A 1  108 ? -27.593 -11.085 -19.301 1    28.8    ? 108  ARG   A CZ  1 1 
ATOM   849   N  NH1 . ARG   A 1  108 ? -27.942 -11.642 -20.475 1    28.789  ? 108  ARG   A NH1 1 1 
ATOM   850   N  NH2 . ARG   A 1  108 ? -28.093 -11.525 -18.149 1    30.23   ? 108  ARG   A NH2 1 1 
ATOM   851   N  N   . GLN   A 1  109 ? -24.074 -5.152  -22.668 1    22.939  ? 109  GLN   A N   1 1 
ATOM   852   C  CA  . GLN   A 1  109 ? -23.638 -4.646  -23.968 1    24.003  ? 109  GLN   A CA  1 1 
ATOM   853   C  C   . GLN   A 1  109 ? -22.467 -3.669  -23.802 1    22.23   ? 109  GLN   A C   1 1 
ATOM   854   O  O   . GLN   A 1  109 ? -21.534 -3.73   -24.564 1    21.286  ? 109  GLN   A O   1 1 
ATOM   855   C  CB  . GLN   A 1  109 ? -24.809 -4.06   -24.746 1    24.979  ? 109  GLN   A CB  1 1 
ATOM   856   C  CG  . GLN   A 1  109 ? -25.878 -5.116  -25.049 1    27.113  ? 109  GLN   A CG  1 1 
ATOM   857   C  CD  . GLN   A 1  109 ? -27.169 -4.507  -25.521 1    29.605  ? 109  GLN   A CD  1 1 
ATOM   858   O  OE1 . GLN   A 1  109 ? -27.77  -3.676  -24.848 1    30.154  ? 109  GLN   A OE1 1 1 
ATOM   859   N  NE2 . GLN   A 1  109 ? -27.5   -4.764  -26.756 1    31.359  ? 109  GLN   A NE2 1 1 
ATOM   860   N  N   . GLN   A 1  110 ? -22.533 -2.773  -22.811 1    22.242  ? 110  GLN   A N   1 1 
ATOM   861   C  CA  . GLN   A 1  110 ? -21.474 -1.834  -22.474 1    22.126  ? 110  GLN   A CA  1 1 
ATOM   862   C  C   . GLN   A 1  110 ? -20.219 -2.608  -22.093 1    20.24   ? 110  GLN   A C   1 1 
ATOM   863   O  O   . GLN   A 1  110 ? -19.166 -2.277  -22.599 1    19.395  ? 110  GLN   A O   1 1 
ATOM   864   C  CB  . GLN   A 1  110 ? -21.956 -0.963  -21.316 1    26.023  ? 110  GLN   A CB  1 1 
ATOM   865   C  CG  . GLN   A 1  110 ? -21.049 0.219   -20.996 1    31.917  ? 110  GLN   A CG  1 1 
ATOM   866   C  CD  . GLN   A 1  110 ? -21.441 1.008   -19.756 1    36.854  ? 110  GLN   A CD  1 1 
ATOM   867   O  OE1 . GLN   A 1  110 ? -22.587 0.934   -19.256 1    34.52   ? 110  GLN   A OE1 1 1 
ATOM   868   N  NE2 . GLN   A 1  110 ? -20.465 1.777   -19.261 1    35.571  ? 110  GLN   A NE2 1 1 
ATOM   869   N  N   . TYR   A 1  111 ? -20.355 -3.668  -21.279 1    18.616  ? 111  TYR   A N   1 1 
ATOM   870   C  CA  . TYR   A 1  111 ? -19.145 -4.386  -20.844 1    18.341  ? 111  TYR   A CA  1 1 
ATOM   871   C  C   . TYR   A 1  111 ? -18.469 -5.051  -22.049 1    17.587  ? 111  TYR   A C   1 1 
ATOM   872   O  O   . TYR   A 1  111 ? -17.226 -5.065  -22.198 1    16.065  ? 111  TYR   A O   1 1 
ATOM   873   C  CB  . TYR   A 1  111 ? -19.619 -5.476  -19.877 1    18.252  ? 111  TYR   A CB  1 1 
ATOM   874   C  CG  . TYR   A 1  111 ? -18.553 -6.387  -19.303 1    19.583  ? 111  TYR   A CG  1 1 
ATOM   875   C  CD1 . TYR   A 1  111 ? -17.823 -6.013  -18.167 1    18.759  ? 111  TYR   A CD1 1 1 
ATOM   876   C  CD2 . TYR   A 1  111 ? -18.316 -7.636  -19.872 1    19.973  ? 111  TYR   A CD2 1 1 
ATOM   877   C  CE1 . TYR   A 1  111 ? -16.882 -6.871  -17.603 1    20.838  ? 111  TYR   A CE1 1 1 
ATOM   878   C  CE2 . TYR   A 1  111 ? -17.398 -8.505  -19.304 1    21.124  ? 111  TYR   A CE2 1 1 
ATOM   879   C  CZ  . TYR   A 1  111 ? -16.654 -8.111  -18.196 1    21.736  ? 111  TYR   A CZ  1 1 
ATOM   880   O  OH  . TYR   A 1  111 ? -15.713 -8.971  -17.694 1    24.216  ? 111  TYR   A OH  1 1 
ATOM   881   N  N   . ASN   A 1  112 ? -19.299 -5.721  -22.86  1    18.63   ? 112  ASN   A N   1 1 
ATOM   882   C  CA  . ASN   A 1  112 ? -18.769 -6.44   -23.998 1    19.467  ? 112  ASN   A CA  1 1 
ATOM   883   C  C   . ASN   A 1  112 ? -18.113 -5.469  -24.97  1    20.171  ? 112  ASN   A C   1 1 
ATOM   884   O  O   . ASN   A 1  112 ? -17.058 -5.787  -25.48  1    21.576  ? 112  ASN   A O   1 1 
ATOM   885   C  CB  . ASN   A 1  112 ? -19.845 -7.201  -24.759 1    19.727  ? 112  ASN   A CB  1 1 
ATOM   886   C  CG  . ASN   A 1  112 ? -20.457 -8.282  -23.893 1    20.567  ? 112  ASN   A CG  1 1 
ATOM   887   O  OD1 . ASN   A 1  112 ? -19.807 -8.781  -22.96  1    21.365  ? 112  ASN   A OD1 1 1 
ATOM   888   N  ND2 . ASN   A 1  112 ? -21.688 -8.668  -24.186 1    20.913  ? 112  ASN   A ND2 1 1 
ATOM   889   N  N   . ALA   A 1  113 ? -18.724 -4.31   -25.208 1    20.623  ? 113  ALA   A N   1 1 
ATOM   890   C  CA  . ALA   A 1  113 ? -18.125 -3.283  -26.059 1    21.319  ? 113  ALA   A CA  1 1 
ATOM   891   C  C   . ALA   A 1  113 ? -16.796 -2.778  -25.502 1    20.872  ? 113  ALA   A C   1 1 
ATOM   892   O  O   . ALA   A 1  113 ? -15.892 -2.498  -26.285 1    22.216  ? 113  ALA   A O   1 1 
ATOM   893   C  CB  . ALA   A 1  113 ? -19.103 -2.128  -26.336 1    21.871  ? 113  ALA   A CB  1 1 
ATOM   894   N  N   . LEU   A 1  114 ? -16.708 -2.584  -24.183 1    19.103  ? 114  LEU   A N   1 1 
ATOM   895   C  CA  . LEU   A 1  114 ? -15.491 -2.102  -23.582 1    19.616  ? 114  LEU   A CA  1 1 
ATOM   896   C  C   . LEU   A 1  114 ? -14.396 -3.118  -23.837 1    19.824  ? 114  LEU   A C   1 1 
ATOM   897   O  O   . LEU   A 1  114 ? -13.277 -2.731  -24.143 1    20.011  ? 114  LEU   A O   1 1 
ATOM   898   C  CB  . LEU   A 1  114 ? -15.688 -1.809  -22.086 1    18.989  ? 114  LEU   A CB  1 1 
ATOM   899   C  CG  . LEU   A 1  114 ? -16.478 -0.521  -21.801 1    21.244  ? 114  LEU   A CG  1 1 
ATOM   900   C  CD1 . LEU   A 1  114 ? -16.926 -0.641  -20.337 1    21.869  ? 114  LEU   A CD1 1 1 
ATOM   901   C  CD2 . LEU   A 1  114 ? -15.503 0.655   -21.981 1    21.859  ? 114  LEU   A CD2 1 1 
ATOM   902   N  N   . LEU   A 1  115 ? -14.677 -4.413  -23.655 1    20.145  ? 115  LEU   A N   1 1 
ATOM   903   C  CA  . LEU   A 1  115 ? -13.599 -5.391  -23.821 1    20.635  ? 115  LEU   A CA  1 1 
ATOM   904   C  C   . LEU   A 1  115 ? -13.08  -5.302  -25.258 1    20.072  ? 115  LEU   A C   1 1 
ATOM   905   O  O   . LEU   A 1  115 ? -11.889 -5.403  -25.541 1    18.115  ? 115  LEU   A O   1 1 
ATOM   906   C  CB  . LEU   A 1  115 ? -14.099 -6.813  -23.555 1    23.675  ? 115  LEU   A CB  1 1 
ATOM   907   C  CG  . LEU   A 1  115 ? -14.55  -7.16   -22.131 1    27.123  ? 115  LEU   A CG  1 1 
ATOM   908   C  CD1 . LEU   A 1  115 ? -14.756 -8.695  -21.98  1    27.469  ? 115  LEU   A CD1 1 1 
ATOM   909   C  CD2 . LEU   A 1  115 ? -13.502 -6.696  -21.149 1    29.939  ? 115  LEU   A CD2 1 1 
ATOM   910   N  N   . SER   A 1  116 ? -14.013 -5.171  -26.191 1    19.415  ? 116  SER   A N   1 1 
ATOM   911   C  CA  . SER   A 1  116 ? -13.677 -5.179  -27.6   1    21.296  ? 116  SER   A CA  1 1 
ATOM   912   C  C   . SER   A 1  116 ? -12.823 -3.942  -27.938 1    21.68   ? 116  SER   A C   1 1 
ATOM   913   O  O   . SER   A 1  116 ? -11.791 -4.051  -28.616 1    21.97   ? 116  SER   A O   1 1 
ATOM   914   C  CB  . SER   A 1  116 ? -14.973 -5.298  -28.39  1    22.981  ? 116  SER   A CB  1 1 
ATOM   915   O  OG  . SER   A 1  116 ? -14.658 -5.132  -29.748 1    27.865  ? 116  SER   A OG  1 1 
ATOM   916   N  N   . GLN   A 1  117 ? -13.219 -2.756  -27.451 1    20.738  ? 117  GLN   A N   1 1 
ATOM   917   C  CA  . GLN   A 1  117 ? -12.514 -1.53   -27.777 1    21.653  ? 117  GLN   A CA  1 1 
ATOM   918   C  C   . GLN   A 1  117 ? -11.143 -1.509  -27.093 1    21.406  ? 117  GLN   A C   1 1 
ATOM   919   O  O   . GLN   A 1  117 ? -10.187 -1.01   -27.692 1    19.871  ? 117  GLN   A O   1 1 
ATOM   920   C  CB  . GLN   A 1  117 ? -13.242 -0.292  -27.247 1    24.216  ? 117  GLN   A CB  1 1 
ATOM   921   C  CG  . GLN   A 1  117 ? -14.553 -0.008  -27.974 1    32.001  ? 117  GLN   A CG  1 1 
ATOM   922   C  CD  . GLN   A 1  117 ? -15.349 1.076   -27.27  1    45.703  ? 117  GLN   A CD  1 1 
ATOM   923   O  OE1 . GLN   A 1  117 ? -14.812 2.132   -26.898 1    57.107  ? 117  GLN   A OE1 1 1 
ATOM   924   N  NE2 . GLN   A 1  117 ? -16.627 0.801   -27.013 1    55.315  ? 117  GLN   A NE2 1 1 
ATOM   925   N  N   . MET   A 1  118 ? -11.056 -2.035  -25.861 1    18.894  ? 118  MET   A N   1 1 
ATOM   926   C  CA  . MET   A 1  118 ? -9.763  -2.07   -25.164 1    19.386  ? 118  MET   A CA  1 1 
ATOM   927   C  C   . MET   A 1  118 ? -8.79   -2.995  -25.895 1    19.412  ? 118  MET   A C   1 1 
ATOM   928   O  O   . MET   A 1  118 ? -7.634  -2.646  -26.133 1    19.64   ? 118  MET   A O   1 1 
ATOM   929   C  CB  . MET   A 1  118 ? -9.923  -2.487  -23.701 1    17.371  ? 118  MET   A CB  1 1 
ATOM   930   C  CG  . MET   A 1  118 ? -10.522 -1.381  -22.825 1    17.637  ? 118  MET   A CG  1 1 
ATOM   931   S  SD  . MET   A 1  118 ? -10.249 -1.774  -21.078 1    19.622  ? 118  MET   A SD  1 1 
ATOM   932   C  CE  . MET   A 1  118 ? -11.107 -3.322  -20.71  1    18.213  ? 118  MET   A CE  1 1 
ATOM   933   N  N   . SER   A 1  119 ? -9.284  -4.143  -26.356 1    20.345  ? 119  SER   A N   1 1 
ATOM   934   C  CA  . SER   A 1  119 ? -8.467  -5.082  -27.123 1    22.599  ? 119  SER   A CA  1 1 
ATOM   935   C  C   . SER   A 1  119 ? -7.968  -4.436  -28.433 1    23.311  ? 119  SER   A C   1 1 
ATOM   936   O  O   . SER   A 1  119 ? -6.796  -4.539  -28.795 1    22.622  ? 119  SER   A O   1 1 
ATOM   937   C  CB  . SER   A 1  119 ? -9.296  -6.332  -27.383 1    24.933  ? 119  SER   A CB  1 1 
ATOM   938   O  OG  . SER   A 1  119 ? -8.759  -7.159  -28.409 1    31.741  ? 119  SER   A OG  1 1 
ATOM   939   N  N   . ARG   A 1  120 ? -8.857  -3.775  -29.153 1    22.521  ? 120  ARG   A N   1 1 
ATOM   940   C  CA  . ARG   A 1  120 ? -8.526  -3.127  -30.413 1    23.609  ? 120  ARG   A CA  1 1 
ATOM   941   C  C   . ARG   A 1  120 ? -7.519  -1.99   -30.213 1    23.949  ? 120  ARG   A C   1 1 
ATOM   942   O  O   . ARG   A 1  120 ? -6.633  -1.766  -31.042 1    24.898  ? 120  ARG   A O   1 1 
ATOM   943   C  CB  . ARG   A 1  120 ? -9.79   -2.589  -31.098 1    24.941  ? 120  ARG   A CB  1 1 
ATOM   944   C  CG  . ARG   A 1  120 ? -9.469  -1.788  -32.36  1    32.138  ? 120  ARG   A CG  1 1 
ATOM   945   C  CD  . ARG   A 1  120 ? -10.609 -1.034  -33.092 1    38.959  ? 120  ARG   A CD  1 1 
ATOM   946   N  NE  . ARG   A 1  120 ? -11.161 -0.012  -32.197 1    51.066  ? 120  ARG   A NE  1 1 
ATOM   947   C  CZ  . ARG   A 1  120 ? -10.545 1.06    -31.667 1    54.046  ? 120  ARG   A CZ  1 1 
ATOM   948   N  NH1 . ARG   A 1  120 ? -9.399  1.519   -32.16  1    51.121  ? 120  ARG   A NH1 1 1 
ATOM   949   N  NH2 . ARG   A 1  120 ? -11.12  1.686   -30.651 1    56.473  ? 120  ARG   A NH2 1 1 
ATOM   950   N  N   . ILE   A 1  121 ? -7.678  -1.197  -29.146 1    23.069  ? 121  ILE   A N   1 1 
ATOM   951   C  CA  . ILE   A 1  121 ? -6.722  -0.135  -28.912 1    23.003  ? 121  ILE   A CA  1 1 
ATOM   952   C  C   . ILE   A 1  121 ? -5.328  -0.728  -28.746 1    22.12   ? 121  ILE   A C   1 1 
ATOM   953   O  O   . ILE   A 1  121 ? -4.372  -0.223  -29.324 1    23.615  ? 121  ILE   A O   1 1 
ATOM   954   C  CB  . ILE   A 1  121 ? -7.138  0.708   -27.699 1    24.174  ? 121  ILE   A CB  1 1 
ATOM   955   C  CG1 . ILE   A 1  121 ? -8.312  1.608   -28.175 1    26.075  ? 121  ILE   A CG1 1 1 
ATOM   956   C  CG2 . ILE   A 1  121 ? -5.95   1.519   -27.145 1    24.069  ? 121  ILE   A CG2 1 1 
ATOM   957   C  CD1 . ILE   A 1  121 ? -9.073  2.254   -27.05  1    26.899  ? 121  ILE   A CD1 1 1 
ATOM   958   N  N   . TYR   A 1  122 ? -5.214  -1.749  -27.929 1    19.795  ? 122  TYR   A N   1 1 
ATOM   959   C  CA  . TYR   A 1  122 ? -3.881  -2.281  -27.634 1    19.255  ? 122  TYR   A CA  1 1 
ATOM   960   C  C   . TYR   A 1  122 ? -3.267  -2.882  -28.9   1    21.12   ? 122  TYR   A C   1 1 
ATOM   961   O  O   . TYR   A 1  122 ? -2.065  -2.691  -29.192 1    21.724  ? 122  TYR   A O   1 1 
ATOM   962   C  CB  . TYR   A 1  122 ? -4.01   -3.262  -26.465 1    17.865  ? 122  TYR   A CB  1 1 
ATOM   963   C  CG  . TYR   A 1  122 ? -2.644  -3.853  -26.112 1    17.829  ? 122  TYR   A CG  1 1 
ATOM   964   C  CD1 . TYR   A 1  122 ? -2.176  -4.974  -26.765 1    17.957  ? 122  TYR   A CD1 1 1 
ATOM   965   C  CD2 . TYR   A 1  122 ? -1.834  -3.241  -25.146 1    17.17   ? 122  TYR   A CD2 1 1 
ATOM   966   C  CE1 . TYR   A 1  122 ? -0.886  -5.458  -26.51  1    18.051  ? 122  TYR   A CE1 1 1 
ATOM   967   C  CE2 . TYR   A 1  122 ? -0.586  -3.756  -24.833 1    16.572  ? 122  TYR   A CE2 1 1 
ATOM   968   C  CZ  . TYR   A 1  122 ? -0.113  -4.858  -25.514 1    18.969  ? 122  TYR   A CZ  1 1 
ATOM   969   O  OH  . TYR   A 1  122 ? 1.141   -5.321  -25.164 1    19.653  ? 122  TYR   A OH  1 1 
ATOM   970   N  N   A SER   A 1  123 ? -4.053  -3.688  -29.622 0.26 21.201  ? 123  SER   A N   1 1 
ATOM   971   N  N   B SER   A 1  123 ? -4.074  -3.643  -29.649 0.74 21.858  ? 123  SER   A N   1 1 
ATOM   972   C  CA  A SER   A 1  123 ? -3.475  -4.452  -30.717 0.26 22.031  ? 123  SER   A CA  1 1 
ATOM   973   C  CA  B SER   A 1  123 ? -3.536  -4.471  -30.722 0.74 24.191  ? 123  SER   A CA  1 1 
ATOM   974   C  C   A SER   A 1  123 ? -3.06   -3.535  -31.861 0.26 23.534  ? 123  SER   A C   1 1 
ATOM   975   C  C   B SER   A 1  123 ? -3.443  -3.738  -32.061 0.74 25.547  ? 123  SER   A C   1 1 
ATOM   976   O  O   A SER   A 1  123 ? -2.023  -3.775  -32.482 0.26 23.86   ? 123  SER   A O   1 1 
ATOM   977   O  O   B SER   A 1  123 ? -2.916  -4.266  -33.036 0.74 28.895  ? 123  SER   A O   1 1 
ATOM   978   C  CB  A SER   A 1  123 ? -4.366  -5.576  -31.184 0.26 21.837  ? 123  SER   A CB  1 1 
ATOM   979   C  CB  B SER   A 1  123 ? -4.211  -5.839  -30.789 0.74 24.796  ? 123  SER   A CB  1 1 
ATOM   980   O  OG  A SER   A 1  123 ? -5.573  -5.065  -31.719 0.26 21.622  ? 123  SER   A OG  1 1 
ATOM   981   O  OG  B SER   A 1  123 ? -3.635  -6.71   -29.81  0.74 24.521  ? 123  SER   A OG  1 1 
ATOM   982   N  N   . THR   A 1  124 ? -3.84   -2.465  -32.088 1    24.431  ? 124  THR   A N   1 1 
ATOM   983   C  CA  . THR   A 1  124 ? -3.692  -1.666  -33.286 1    26.058  ? 124  THR   A CA  1 1 
ATOM   984   C  C   . THR   A 1  124 ? -2.891  -0.392  -33.015 1    25.819  ? 124  THR   A C   1 1 
ATOM   985   O  O   . THR   A 1  124 ? -2.645  0.37    -33.938 1    27.975  ? 124  THR   A O   1 1 
ATOM   986   C  CB  . THR   A 1  124 ? -5.024  -1.383  -33.999 1    26.618  ? 124  THR   A CB  1 1 
ATOM   987   O  OG1 . THR   A 1  124 ? -5.788  -0.531  -33.155 1    25.398  ? 124  THR   A OG1 1 1 
ATOM   988   C  CG2 . THR   A 1  124 ? -5.82   -2.63   -34.334 1    25.891  ? 124  THR   A CG2 1 1 
ATOM   989   N  N   . ALA   A 1  125 ? -2.422  -0.181  -31.786 1    24.139  ? 125  ALA   A N   1 1 
ATOM   990   C  CA  . ALA   A 1  125 ? -1.641  1.016   -31.5   1    26.03   ? 125  ALA   A CA  1 1 
ATOM   991   C  C   . ALA   A 1  125 ? -0.333  1.011   -32.304 1    25.817  ? 125  ALA   A C   1 1 
ATOM   992   O  O   . ALA   A 1  125 ? 0.267   -0.037  -32.484 1    25.092  ? 125  ALA   A O   1 1 
ATOM   993   C  CB  . ALA   A 1  125 ? -1.335  1.106   -30.017 1    23.945  ? 125  ALA   A CB  1 1 
ATOM   994   N  N   . LYS   A 1  126 ? 0.105   2.191   -32.726 1    27.338  ? 126  LYS   A N   1 1 
ATOM   995   C  CA  . LYS   A 1  126 ? 1.347   2.323   -33.485 1    31.532  ? 126  LYS   A CA  1 1 
ATOM   996   C  C   . LYS   A 1  126 ? 2.191   3.475   -32.947 1    30.415  ? 126  LYS   A C   1 1 
ATOM   997   O  O   . LYS   A 1  126 ? 1.663   4.414   -32.368 1    29.339  ? 126  LYS   A O   1 1 
ATOM   998   C  CB  . LYS   A 1  126 ? 0.89    2.768   -34.87  1    33.89   ? 126  LYS   A CB  1 1 
ATOM   999   C  CG  . LYS   A 1  126 ? 0.087   1.783   -35.692 1    39.224  ? 126  LYS   A CG  1 1 
ATOM   1000  C  CD  . LYS   A 1  126 ? 0.685   0.392   -35.902 1    42.238  ? 126  LYS   A CD  1 1 
ATOM   1001  C  CE  . LYS   A 1  126 ? -0.025  -0.267  -37.08  1    49.66   ? 126  LYS   A CE  1 1 
ATOM   1002  N  NZ  . LYS   A 1  126 ? -1.347  -0.795  -36.7   1    52.712  ? 126  LYS   A NZ  1 1 
ATOM   1003  N  N   . VAL   A 1  127 ? 3.516   3.419   -33.167 1    31.513  ? 127  VAL   A N   1 1 
ATOM   1004  C  CA  . VAL   A 1  127 ? 4.363   4.559   -32.888 1    30.733  ? 127  VAL   A CA  1 1 
ATOM   1005  C  C   . VAL   A 1  127 ? 4.742   5.175   -34.236 1    34.374  ? 127  VAL   A C   1 1 
ATOM   1006  O  O   . VAL   A 1  127 ? 5.194   4.479   -35.145 1    33.46   ? 127  VAL   A O   1 1 
ATOM   1007  C  CB  . VAL   A 1  127 ? 5.614   4.156   -32.086 1    29.866  ? 127  VAL   A CB  1 1 
ATOM   1008  C  CG1 . VAL   A 1  127 ? 6.535   5.345   -31.907 1    31.84   ? 127  VAL   A CG1 1 1 
ATOM   1009  C  CG2 . VAL   A 1  127 ? 5.247   3.538   -30.739 1    29.581  ? 127  VAL   A CG2 1 1 
ATOM   1010  N  N   . CYS   A 1  128 ? 4.547   6.482   -34.351 1    38.006  ? 128  CYS   A N   1 1 
ATOM   1011  C  CA  . CYS   A 1  128 ? 4.787   7.136   -35.628 1    46.341  ? 128  CYS   A CA  1 1 
ATOM   1012  C  C   . CYS   A 1  128 ? 6.055   7.978   -35.567 1    49.136  ? 128  CYS   A C   1 1 
ATOM   1013  O  O   . CYS   A 1  128 ? 6.32    8.605   -34.546 1    48.863  ? 128  CYS   A O   1 1 
ATOM   1014  C  CB  . CYS   A 1  128 ? 3.634   8.063   -35.971 1    47.696  ? 128  CYS   A CB  1 1 
ATOM   1015  S  SG  . CYS   A 1  128 ? 2.098   7.149   -36.257 1    66.664  ? 128  CYS   A SG  1 1 
ATOM   1016  N  N   . LEU   A 1  129 ? 6.824   7.937   -36.667 1    52.959  ? 129  LEU   A N   1 1 
ATOM   1017  C  CA  . LEU   A 1  129 ? 7.758   8.965   -37.121 1    63.95   ? 129  LEU   A CA  1 1 
ATOM   1018  C  C   . LEU   A 1  129 ? 9.206   8.501   -36.892 1    64.339  ? 129  LEU   A C   1 1 
ATOM   1019  O  O   . LEU   A 1  129 ? 10.101  9.318   -37.161 1    65.361  ? 129  LEU   A O   1 1 
ATOM   1020  C  CB  . LEU   A 1  129 ? 7.472   10.398  -36.649 1    68.781  ? 129  LEU   A CB  1 1 
ATOM   1021  C  CG  . LEU   A 1  129 ? 6.073   10.937  -37.009 1    74.275  ? 129  LEU   A CG  1 1 
ATOM   1022  C  CD1 . LEU   A 1  129 ? 5.749   12.332  -36.467 1    71.961  ? 129  LEU   A CD1 1 1 
ATOM   1023  C  CD2 . LEU   A 1  129 ? 5.75    10.832  -38.514 1    73.574  ? 129  LEU   A CD2 1 1 
ATOM   1024  N  N   . THR   A 1  135 ? 4.523   6.442   -41.736 1    52.536  ? 135  THR   A N   1 1 
ATOM   1025  C  CA  . THR   A 1  135 ? 5.408   5.268   -41.537 1    58.857  ? 135  THR   A CA  1 1 
ATOM   1026  C  C   . THR   A 1  135 ? 5.507   4.906   -40.048 1    54.712  ? 135  THR   A C   1 1 
ATOM   1027  O  O   . THR   A 1  135 ? 6.063   5.658   -39.236 1    51.898  ? 135  THR   A O   1 1 
ATOM   1028  C  CB  . THR   A 1  135 ? 6.772   5.548   -42.16  1    65.211  ? 135  THR   A CB  1 1 
ATOM   1029  O  OG1 . THR   A 1  135 ? 6.433   6.507   -43.158 1    70.627  ? 135  THR   A OG1 1 1 
ATOM   1030  C  CG2 . THR   A 1  135 ? 7.413   4.295   -42.739 1    68.725  ? 135  THR   A CG2 1 1 
ATOM   1031  N  N   . CYS   A 1  136 ? 4.986   3.717   -39.715 1    51.632  ? 136  CYS   A N   1 1 
ATOM   1032  C  CA  . CYS   A 1  136 ? 4.52    3.444   -38.359 1    49.23   ? 136  CYS   A CA  1 1 
ATOM   1033  C  C   . CYS   A 1  136 ? 5.048   2.119   -37.837 1    44.853  ? 136  CYS   A C   1 1 
ATOM   1034  O  O   . CYS   A 1  136 ? 4.948   1.087   -38.499 1    44.721  ? 136  CYS   A O   1 1 
ATOM   1035  C  CB  . CYS   A 1  136 ? 2.999   3.343   -38.329 1    49.249  ? 136  CYS   A CB  1 1 
ATOM   1036  S  SG  . CYS   A 1  136 ? 2.21    4.963   -38.495 1    60.248  ? 136  CYS   A SG  1 1 
ATOM   1037  N  N   . TRP   A 1  137 ? 5.52    2.142   -36.597 1    39.439  ? 137  TRP   A N   1 1 
ATOM   1038  C  CA  . TRP   A 1  137 ? 6.014   0.906   -36.02  1    35.553  ? 137  TRP   A CA  1 1 
ATOM   1039  C  C   . TRP   A 1  137 ? 4.913   0.277   -35.177 1    33.561  ? 137  TRP   A C   1 1 
ATOM   1040  O  O   . TRP   A 1  137 ? 4.259   0.969   -34.416 1    35.676  ? 137  TRP   A O   1 1 
ATOM   1041  C  CB  . TRP   A 1  137 ? 7.253   1.197   -35.169 1    38.081  ? 137  TRP   A CB  1 1 
ATOM   1042  C  CG  . TRP   A 1  137 ? 8.454   1.566   -35.992 1    43.554  ? 137  TRP   A CG  1 1 
ATOM   1043  C  CD1 . TRP   A 1  137 ? 8.704   1.21    -37.286 1    48.607  ? 137  TRP   A CD1 1 1 
ATOM   1044  C  CD2 . TRP   A 1  137 ? 9.576   2.357   -35.569 1    46.474  ? 137  TRP   A CD2 1 1 
ATOM   1045  N  NE1 . TRP   A 1  137 ? 9.898   1.734   -37.708 1    50.678  ? 137  TRP   A NE1 1 1 
ATOM   1046  C  CE2 . TRP   A 1  137 ? 10.46   2.436   -36.672 1    50.445  ? 137  TRP   A CE2 1 1 
ATOM   1047  C  CE3 . TRP   A 1  137 ? 9.925   2.991   -34.369 1    51.411  ? 137  TRP   A CE3 1 1 
ATOM   1048  C  CZ2 . TRP   A 1  137 ? 11.659  3.145   -36.616 1    53.442  ? 137  TRP   A CZ2 1 1 
ATOM   1049  C  CZ3 . TRP   A 1  137 ? 11.125  3.676   -34.311 1    54.271  ? 137  TRP   A CZ3 1 1 
ATOM   1050  C  CH2 . TRP   A 1  137 ? 11.98   3.749   -35.42  1    52.139  ? 137  TRP   A CH2 1 1 
ATOM   1051  N  N   . SER   A 1  138 ? 4.717   -1.026  -35.339 1    32.285  ? 138  SER   A N   1 1 
ATOM   1052  C  CA  . SER   A 1  138 ? 3.834   -1.827  -34.52  1    31.021  ? 138  SER   A CA  1 1 
ATOM   1053  C  C   . SER   A 1  138 ? 4.649   -2.392  -33.368 1    28.515  ? 138  SER   A C   1 1 
ATOM   1054  O  O   . SER   A 1  138 ? 5.898   -2.402  -33.418 1    25.955  ? 138  SER   A O   1 1 
ATOM   1055  C  CB  . SER   A 1  138 ? 3.291   -2.957  -35.371 1    35.718  ? 138  SER   A CB  1 1 
ATOM   1056  O  OG  . SER   A 1  138 ? 4.395   -3.706  -35.897 1    42.205  ? 138  SER   A OG  1 1 
ATOM   1057  N  N   . LEU   A 1  139 ? 3.948   -2.879  -32.333 1    25.677  ? 139  LEU   A N   1 1 
ATOM   1058  C  CA  . LEU   A 1  139 ? 4.646   -3.454  -31.195 1    27.166  ? 139  LEU   A CA  1 1 
ATOM   1059  C  C   . LEU   A 1  139 ? 5.436   -4.681  -31.637 1    29.07   ? 139  LEU   A C   1 1 
ATOM   1060  O  O   . LEU   A 1  139 ? 6.612   -4.848  -31.29  1    29.349  ? 139  LEU   A O   1 1 
ATOM   1061  C  CB  . LEU   A 1  139 ? 3.688   -3.805  -30.063 1    24.327  ? 139  LEU   A CB  1 1 
ATOM   1062  C  CG  . LEU   A 1  139 ? 4.303   -4.5    -28.848 1    26.099  ? 139  LEU   A CG  1 1 
ATOM   1063  C  CD1 . LEU   A 1  139 ? 5.445   -3.738  -28.176 1    24.886  ? 139  LEU   A CD1 1 1 
ATOM   1064  C  CD2 . LEU   A 1  139 ? 3.173   -4.724  -27.852 1    26.246  ? 139  LEU   A CD2 1 1 
ATOM   1065  N  N   . ASP   A 1  140 ? 4.751   -5.551  -32.37  1    29.819  ? 140  ASP   A N   1 1 
ATOM   1066  C  CA  . ASP   A 1  140 ? 5.326   -6.787  -32.855 1    30.752  ? 140  ASP   A CA  1 1 
ATOM   1067  C  C   . ASP   A 1  140 ? 5.276   -6.787  -34.386 1    32.098  ? 140  ASP   A C   1 1 
ATOM   1068  O  O   . ASP   A 1  140 ? 4.184   -6.764  -34.938 1    31.097  ? 140  ASP   A O   1 1 
ATOM   1069  C  CB  . ASP   A 1  140 ? 4.567   -7.968  -32.263 1    31.951  ? 140  ASP   A CB  1 1 
ATOM   1070  C  CG  . ASP   A 1  140 ? 5.218   -9.346  -32.414 1    41.577  ? 140  ASP   A CG  1 1 
ATOM   1071  O  OD1 . ASP   A 1  140 ? 6.321   -9.436  -33.057 1    42.859  ? 140  ASP   A OD1 1 1 
ATOM   1072  O  OD2 . ASP   A 1  140 ? 4.626   -10.35  -31.895 1    38.911  ? 140  ASP   A OD2 1 1 
ATOM   1073  N  N   . PRO   A 1  141 ? 6.416   -6.854  -35.134 1    34.547  ? 141  PRO   A N   1 1 
ATOM   1074  C  CA  . PRO   A 1  141 ? 7.765   -6.993  -34.557 1    33.208  ? 141  PRO   A CA  1 1 
ATOM   1075  C  C   . PRO   A 1  141 ? 8.622   -5.759  -34.251 1    31.831  ? 141  PRO   A C   1 1 
ATOM   1076  O  O   . PRO   A 1  141 ? 9.656   -5.856  -33.589 1    32.17   ? 141  PRO   A O   1 1 
ATOM   1077  C  CB  . PRO   A 1  141 ? 8.425   -7.88   -35.669 1    33.593  ? 141  PRO   A CB  1 1 
ATOM   1078  C  CG  . PRO   A 1  141 ? 7.862   -7.319  -36.975 1    35.244  ? 141  PRO   A CG  1 1 
ATOM   1079  C  CD  . PRO   A 1  141 ? 6.442   -6.89   -36.619 1    33.982  ? 141  PRO   A CD  1 1 
ATOM   1080  N  N   . ASP   A 1  142 ? 8.201   -4.599  -34.757 1    31.853  ? 142  ASP   A N   1 1 
ATOM   1081  C  CA  . ASP   A 1  142 ? 9.042   -3.42   -34.86  1    34.025  ? 142  ASP   A CA  1 1 
ATOM   1082  C  C   . ASP   A 1  142 ? 9.592   -2.973  -33.5   1    32.644  ? 142  ASP   A C   1 1 
ATOM   1083  O  O   . ASP   A 1  142 ? 10.806  -2.81   -33.342 1    31.25   ? 142  ASP   A O   1 1 
ATOM   1084  C  CB  . ASP   A 1  142 ? 8.311   -2.29   -35.554 1    34.984  ? 142  ASP   A CB  1 1 
ATOM   1085  C  CG  . ASP   A 1  142 ? 7.798   -2.642  -36.945 1    39.625  ? 142  ASP   A CG  1 1 
ATOM   1086  O  OD1 . ASP   A 1  142 ? 8.491   -3.429  -37.636 1    38.446  ? 142  ASP   A OD1 1 1 
ATOM   1087  O  OD2 . ASP   A 1  142 ? 6.711   -2.118  -37.313 1    43.04   ? 142  ASP   A OD2 1 1 
ATOM   1088  N  N   . LEU   A 1  143 ? 8.7     -2.622  -32.582 1    28.248  ? 143  LEU   A N   1 1 
ATOM   1089  C  CA  . LEU   A 1  143 ? 9.14    -2.101  -31.286 1    28.382  ? 143  LEU   A CA  1 1 
ATOM   1090  C  C   . LEU   A 1  143 ? 9.798   -3.209  -30.455 1    26.961  ? 143  LEU   A C   1 1 
ATOM   1091  O  O   . LEU   A 1  143 ? 10.764  -2.953  -29.745 1    31.029  ? 143  LEU   A O   1 1 
ATOM   1092  C  CB  . LEU   A 1  143 ? 8.027   -1.365  -30.518 1    27.781  ? 143  LEU   A CB  1 1 
ATOM   1093  C  CG  . LEU   A 1  143 ? 7.423   -0.158  -31.244 1    28.909  ? 143  LEU   A CG  1 1 
ATOM   1094  C  CD1 . LEU   A 1  143 ? 6.226   0.328   -30.456 1    28.515  ? 143  LEU   A CD1 1 1 
ATOM   1095  C  CD2 . LEU   A 1  143 ? 8.388   0.99    -31.412 1    29.973  ? 143  LEU   A CD2 1 1 
ATOM   1096  N  N   . THR   A 1  144 ? 9.35    -4.454  -30.604 1    25.876  ? 144  THR   A N   1 1 
ATOM   1097  C  CA  . THR   A 1  144 ? 9.956   -5.563  -29.902 1    26.056  ? 144  THR   A CA  1 1 
ATOM   1098  C  C   . THR   A 1  144 ? 11.44   -5.613  -30.29  1    28.942  ? 144  THR   A C   1 1 
ATOM   1099  O  O   . THR   A 1  144 ? 12.315  -5.647  -29.413 1    26.828  ? 144  THR   A O   1 1 
ATOM   1100  C  CB  . THR   A 1  144 ? 9.226   -6.865  -30.219 1    25.702  ? 144  THR   A CB  1 1 
ATOM   1101  O  OG1 . THR   A 1  144 ? 7.91    -6.677  -29.696 1    26.838  ? 144  THR   A OG1 1 1 
ATOM   1102  C  CG2 . THR   A 1  144 ? 9.71    -8.074  -29.425 1    24.511  ? 144  THR   A CG2 1 1 
ATOM   1103  N  N   . ASN   A 1  145 ? 11.709  -5.54   -31.604 1    27.787  ? 145  ASN   A N   1 1 
ATOM   1104  C  CA  . ASN   A 1  145 ? 13.061  -5.674  -32.111 1    29.399  ? 145  ASN   A CA  1 1 
ATOM   1105  C  C   . ASN   A 1  145 ? 13.927  -4.527  -31.597 1    28.442  ? 145  ASN   A C   1 1 
ATOM   1106  O  O   . ASN   A 1  145 ? 15.061  -4.755  -31.243 1    34.033  ? 145  ASN   A O   1 1 
ATOM   1107  C  CB  . ASN   A 1  145 ? 13.06   -5.86   -33.636 1    31.701  ? 145  ASN   A CB  1 1 
ATOM   1108  C  CG  . ASN   A 1  145 ? 12.662  -7.268  -34.036 1    35.197  ? 145  ASN   A CG  1 1 
ATOM   1109  O  OD1 . ASN   A 1  145 ? 12.643  -8.167  -33.19  1    35.924  ? 145  ASN   A OD1 1 1 
ATOM   1110  N  ND2 . ASN   A 1  145 ? 12.316  -7.502  -35.3   1    35.592  ? 145  ASN   A ND2 1 1 
ATOM   1111  N  N   . ILE   A 1  146 ? 13.423  -3.296  -31.586 1    27.883  ? 146  ILE   A N   1 1 
ATOM   1112  C  CA  . ILE   A 1  146 ? 14.138  -2.143  -31.054 1    28.053  ? 146  ILE   A CA  1 1 
ATOM   1113  C  C   . ILE   A 1  146 ? 14.526  -2.408  -29.596 1    30.536  ? 146  ILE   A C   1 1 
ATOM   1114  O  O   . ILE   A 1  146 ? 15.712  -2.283  -29.255 1    30.212  ? 146  ILE   A O   1 1 
ATOM   1115  C  CB  . ILE   A 1  146 ? 13.388  -0.813  -31.269 1    29.633  ? 146  ILE   A CB  1 1 
ATOM   1116  C  CG1 . ILE   A 1  146 ? 13.196  -0.523  -32.768 1    33.588  ? 146  ILE   A CG1 1 1 
ATOM   1117  C  CG2 . ILE   A 1  146 ? 14.094  0.357   -30.579 1    28.76   ? 146  ILE   A CG2 1 1 
ATOM   1118  C  CD1 . ILE   A 1  146 ? 12.237  0.626   -33.045 1    32.813  ? 146  ILE   A CD1 1 1 
ATOM   1119  N  N   . LEU   A 1  147 ? 13.533  -2.771  -28.754 1    25.488  ? 147  LEU   A N   1 1 
ATOM   1120  C  CA  . LEU   A 1  147 ? 13.803  -3.001  -27.343 1    26.9    ? 147  LEU   A CA  1 1 
ATOM   1121  C  C   . LEU   A 1  147 ? 14.854  -4.105  -27.186 1    27.272  ? 147  LEU   A C   1 1 
ATOM   1122  O  O   . LEU   A 1  147 ? 15.698  -3.996  -26.287 1    25.558  ? 147  LEU   A O   1 1 
ATOM   1123  C  CB  . LEU   A 1  147 ? 12.535  -3.346  -26.566 1    22.302  ? 147  LEU   A CB  1 1 
ATOM   1124  C  CG  . LEU   A 1  147 ? 11.764  -2.108  -26.112 1    23.666  ? 147  LEU   A CG  1 1 
ATOM   1125  C  CD1 . LEU   A 1  147 ? 12.432  -1.543  -24.844 1    23.052  ? 147  LEU   A CD1 1 1 
ATOM   1126  C  CD2 . LEU   A 1  147 ? 11.641  -0.988  -27.14  1    23.586  ? 147  LEU   A CD2 1 1 
ATOM   1127  N  N   . ALA   A 1  148 ? 14.775  -5.152  -28.039 1    27.79   ? 148  ALA   A N   1 1 
ATOM   1128  C  CA  . ALA   A 1  148 ? 15.677  -6.298  -27.949 1    29.654  ? 148  ALA   A CA  1 1 
ATOM   1129  C  C   . ALA   A 1  148 ? 17.108  -5.975  -28.414 1    33.67   ? 148  ALA   A C   1 1 
ATOM   1130  O  O   . ALA   A 1  148 ? 18.061  -6.462  -27.804 1    33.652  ? 148  ALA   A O   1 1 
ATOM   1131  C  CB  . ALA   A 1  148 ? 15.115  -7.516  -28.649 1    29.282  ? 148  ALA   A CB  1 1 
ATOM   1132  N  N   . SER   A 1  149 ? 17.297  -5.129  -29.434 1    34.438  ? 149  SER   A N   1 1 
ATOM   1133  C  CA  . SER   A 1  149 ? 18.623  -5.11   -30.04  1    36.729  ? 149  SER   A CA  1 1 
ATOM   1134  C  C   . SER   A 1  149 ? 19.226  -3.712  -30.154 1    40.543  ? 149  SER   A C   1 1 
ATOM   1135  O  O   . SER   A 1  149 ? 20.411  -3.572  -30.424 1    50.912  ? 149  SER   A O   1 1 
ATOM   1136  C  CB  . SER   A 1  149 ? 18.56   -5.77   -31.382 1    41.152  ? 149  SER   A CB  1 1 
ATOM   1137  O  OG  . SER   A 1  149 ? 17.82   -4.904  -32.235 1    44.584  ? 149  SER   A OG  1 1 
ATOM   1138  N  N   . SER   A 1  150 ? 18.435  -2.648  -30.056 1    38.044  ? 150  SER   A N   1 1 
ATOM   1139  C  CA  . SER   A 1  150 ? 19.058  -1.33   -30.065 1    38.035  ? 150  SER   A CA  1 1 
ATOM   1140  C  C   . SER   A 1  150 ? 19.78   -1.113  -28.727 1    39.888  ? 150  SER   A C   1 1 
ATOM   1141  O  O   . SER   A 1  150 ? 19.328  -1.6    -27.679 1    32.1    ? 150  SER   A O   1 1 
ATOM   1142  C  CB  . SER   A 1  150 ? 18.06   -0.266  -30.347 1    34.824  ? 150  SER   A CB  1 1 
ATOM   1143  O  OG  . SER   A 1  150 ? 18.628  1.008   -30.138 1    38.694  ? 150  SER   A OG  1 1 
ATOM   1144  N  N   . ARG   A 1  151 ? 20.904  -0.383  -28.794 1    35.596  ? 151  ARG   A N   1 1 
ATOM   1145  C  CA  . ARG   A 1  151 ? 21.752  -0.085  -27.652 1    35.319  ? 151  ARG   A CA  1 1 
ATOM   1146  C  C   . ARG   A 1  151 ? 21.968  1.421   -27.671 1    38.889  ? 151  ARG   A C   1 1 
ATOM   1147  O  O   . ARG   A 1  151 ? 22.875  2       -27.057 1    38.903  ? 151  ARG   A O   1 1 
ATOM   1148  C  CB  . ARG   A 1  151 ? 23.013  -0.956  -27.644 1    35.29   ? 151  ARG   A CB  1 1 
ATOM   1149  C  CG  . ARG   A 1  151 ? 22.775  -2.457  -27.657 1    32.236  ? 151  ARG   A CG  1 1 
ATOM   1150  C  CD  . ARG   A 1  151 ? 22.279  -3.127  -26.398 1    36.808  ? 151  ARG   A CD  1 1 
ATOM   1151  N  NE  . ARG   A 1  151 ? 22.212  -4.583  -26.591 1    37.501  ? 151  ARG   A NE  1 1 
ATOM   1152  C  CZ  . ARG   A 1  151 ? 21.19   -5.482  -26.427 1    41.414  ? 151  ARG   A CZ  1 1 
ATOM   1153  N  NH1 . ARG   A 1  151 ? 21.485  -6.769  -26.479 1    39.171  ? 151  ARG   A NH1 1 1 
ATOM   1154  N  NH2 . ARG   A 1  151 ? 19.919  -5.153  -26.128 1    33.181  ? 151  ARG   A NH2 1 1 
ATOM   1155  N  N   . SER   A 1  152 ? 21.056  2.051   -28.399 1    35.416  ? 152  SER   A N   1 1 
ATOM   1156  C  CA  . SER   A 1  152 ? 21.058  3.49    -28.492 1    35.71   ? 152  SER   A CA  1 1 
ATOM   1157  C  C   . SER   A 1  152 ? 20.013  4.001   -27.503 1    34.617  ? 152  SER   A C   1 1 
ATOM   1158  O  O   . SER   A 1  152 ? 18.812  3.739   -27.636 1    31.061  ? 152  SER   A O   1 1 
ATOM   1159  C  CB  . SER   A 1  152 ? 20.793  3.904   -29.925 1    38.391  ? 152  SER   A CB  1 1 
ATOM   1160  O  OG  . SER   A 1  152 ? 20.029  5.096   -29.932 1    38.207  ? 152  SER   A OG  1 1 
ATOM   1161  N  N   . TYR   A 1  153 ? 20.506  4.68    -26.475 1    32.055  ? 153  TYR   A N   1 1 
ATOM   1162  C  CA  . TYR   A 1  153 ? 19.659  5.153   -25.425 1    31.222  ? 153  TYR   A CA  1 1 
ATOM   1163  C  C   . TYR   A 1  153 ? 18.483  5.972   -25.997 1    32.819  ? 153  TYR   A C   1 1 
ATOM   1164  O  O   . TYR   A 1  153 ? 17.364  5.886   -25.518 1    30.263  ? 153  TYR   A O   1 1 
ATOM   1165  C  CB  . TYR   A 1  153 ? 20.561  5.923   -24.461 1    30.181  ? 153  TYR   A CB  1 1 
ATOM   1166  C  CG  . TYR   A 1  153 ? 19.757  6.313   -23.228 1    29.585  ? 153  TYR   A CG  1 1 
ATOM   1167  C  CD1 . TYR   A 1  153 ? 18.824  7.343   -23.291 1    30.495  ? 153  TYR   A CD1 1 1 
ATOM   1168  C  CD2 . TYR   A 1  153 ? 19.929  5.653   -22.002 1    28.861  ? 153  TYR   A CD2 1 1 
ATOM   1169  C  CE1 . TYR   A 1  153 ? 18.069  7.704   -22.177 1    30.887  ? 153  TYR   A CE1 1 1 
ATOM   1170  C  CE2 . TYR   A 1  153 ? 19.156  5.99    -20.89  1    28.316  ? 153  TYR   A CE2 1 1 
ATOM   1171  C  CZ  . TYR   A 1  153 ? 18.225  7.012   -20.985 1    27.774  ? 153  TYR   A CZ  1 1 
ATOM   1172  O  OH  . TYR   A 1  153 ? 17.437  7.41    -19.945 1    27.547  ? 153  TYR   A OH  1 1 
ATOM   1173  N  N   . ALA   A 1  154 ? 18.71   6.739   -27.066 1    31.952  ? 154  ALA   A N   1 1 
ATOM   1174  C  CA  . ALA   A 1  154 ? 17.691  7.626   -27.594 1    32.068  ? 154  ALA   A CA  1 1 
ATOM   1175  C  C   . ALA   A 1  154 ? 16.61   6.859   -28.367 1    31.86   ? 154  ALA   A C   1 1 
ATOM   1176  O  O   . ALA   A 1  154 ? 15.427  7.226   -28.313 1    32.024  ? 154  ALA   A O   1 1 
ATOM   1177  C  CB  . ALA   A 1  154 ? 18.358  8.709   -28.458 1    33.002  ? 154  ALA   A CB  1 1 
ATOM   1178  N  N   . MET   A 1  155 ? 17.029  5.842   -29.124 1    31.818  ? 155  MET   A N   1 1 
ATOM   1179  C  CA  . MET   A 1  155 ? 16.156  4.985   -29.908 1    34.371  ? 155  MET   A CA  1 1 
ATOM   1180  C  C   . MET   A 1  155 ? 15.231  4.181   -28.987 1    30.883  ? 155  MET   A C   1 1 
ATOM   1181  O  O   . MET   A 1  155 ? 14.047  4.059   -29.254 1    30.068  ? 155  MET   A O   1 1 
ATOM   1182  C  CB  . MET   A 1  155 ? 16.971  3.966   -30.713 1    37.641  ? 155  MET   A CB  1 1 
ATOM   1183  C  CG  . MET   A 1  155 ? 16.202  3.247   -31.819 1    43.466  ? 155  MET   A CG  1 1 
ATOM   1184  S  SD  . MET   A 1  155 ? 15.278  4.452   -32.802 1    49.965  ? 155  MET   A SD  1 1 
ATOM   1185  C  CE  . MET   A 1  155 ? 13.545  4.174   -32.408 1    58.242  ? 155  MET   A CE  1 1 
ATOM   1186  N  N   . LEU   A 1  156 ? 15.82   3.516   -27.997 1    27.973  ? 156  LEU   A N   1 1 
ATOM   1187  C  CA  . LEU   A 1  156 ? 15.088  2.763   -26.988 1    25.135  ? 156  LEU   A CA  1 1 
ATOM   1188  C  C   . LEU   A 1  156 ? 14.062  3.656   -26.314 1    24.075  ? 156  LEU   A C   1 1 
ATOM   1189  O  O   . LEU   A 1  156 ? 12.929  3.192   -26.073 1    24.387  ? 156  LEU   A O   1 1 
ATOM   1190  C  CB  . LEU   A 1  156 ? 16.081  2.193   -25.984 1    23.774  ? 156  LEU   A CB  1 1 
ATOM   1191  C  CG  . LEU   A 1  156 ? 17.015  1.12    -26.54  1    23.467  ? 156  LEU   A CG  1 1 
ATOM   1192  C  CD1 . LEU   A 1  156 ? 18.132  0.833   -25.526 1    22.484  ? 156  LEU   A CD1 1 1 
ATOM   1193  C  CD2 . LEU   A 1  156 ? 16.297  -0.154  -26.906 1    20.587  ? 156  LEU   A CD2 1 1 
ATOM   1194  N  N   . LEU   A 1  157 ? 14.446  4.91    -26.049 1    24.057  ? 157  LEU   A N   1 1 
ATOM   1195  C  CA  . LEU   A 1  157 ? 13.581  5.84    -25.352 1    23.96   ? 157  LEU   A CA  1 1 
ATOM   1196  C  C   . LEU   A 1  157 ? 12.382  6.174   -26.233 1    24.941  ? 157  LEU   A C   1 1 
ATOM   1197  O  O   . LEU   A 1  157 ? 11.229  6.222   -25.78  1    21.859  ? 157  LEU   A O   1 1 
ATOM   1198  C  CB  . LEU   A 1  157 ? 14.345  7.085   -24.906 1    25.16   ? 157  LEU   A CB  1 1 
ATOM   1199  C  CG  . LEU   A 1  157 ? 13.542  8.129   -24.143 1    26.123  ? 157  LEU   A CG  1 1 
ATOM   1200  C  CD1 . LEU   A 1  157 ? 13.062  7.506   -22.823 1    27.634  ? 157  LEU   A CD1 1 1 
ATOM   1201  C  CD2 . LEU   A 1  157 ? 14.257  9.426   -23.867 1    27.972  ? 157  LEU   A CD2 1 1 
ATOM   1202  N  N   . PHE   A 1  158 ? 12.705  6.483   -27.497 1    25.772  ? 158  PHE   A N   1 1 
ATOM   1203  C  CA  . PHE   A 1  158 ? 11.674  6.783   -28.465 1    25.635  ? 158  PHE   A CA  1 1 
ATOM   1204  C  C   . PHE   A 1  158 ? 10.647  5.649   -28.501 1    24.519  ? 158  PHE   A C   1 1 
ATOM   1205  O  O   . PHE   A 1  158 ? 9.444   5.927   -28.498 1    24.413  ? 158  PHE   A O   1 1 
ATOM   1206  C  CB  . PHE   A 1  158 ? 12.329  6.983   -29.831 1    27.749  ? 158  PHE   A CB  1 1 
ATOM   1207  C  CG  . PHE   A 1  158 ? 11.272  7.39    -30.83  1    29.278  ? 158  PHE   A CG  1 1 
ATOM   1208  C  CD1 . PHE   A 1  158 ? 10.737  8.678   -30.792 1    31.577  ? 158  PHE   A CD1 1 1 
ATOM   1209  C  CD2 . PHE   A 1  158 ? 10.81   6.483   -31.77  1    29.235  ? 158  PHE   A CD2 1 1 
ATOM   1210  C  CE1 . PHE   A 1  158 ? 9.771   9.068   -31.719 1    34.329  ? 158  PHE   A CE1 1 1 
ATOM   1211  C  CE2 . PHE   A 1  158 ? 9.822   6.871   -32.672 1    30.86   ? 158  PHE   A CE2 1 1 
ATOM   1212  C  CZ  . PHE   A 1  158 ? 9.316   8.151   -32.651 1    32.641  ? 158  PHE   A CZ  1 1 
ATOM   1213  N  N   . ALA   A 1  159 ? 11.123  4.394   -28.576 1    22.721  ? 159  ALA   A N   1 1 
ATOM   1214  C  CA  . ALA   A 1  159 ? 10.245  3.24    -28.678 1    21.617  ? 159  ALA   A CA  1 1 
ATOM   1215  C  C   . ALA   A 1  159 ? 9.445   3.069   -27.373 1    21.129  ? 159  ALA   A C   1 1 
ATOM   1216  O  O   . ALA   A 1  159 ? 8.234   2.791   -27.401 1    20.421  ? 159  ALA   A O   1 1 
ATOM   1217  C  CB  . ALA   A 1  159 ? 11.036  1.986   -28.993 1    20.948  ? 159  ALA   A CB  1 1 
ATOM   1218  N  N   . TRP   A 1  160 ? 10.147  3.148   -26.242 1    19.858  ? 160  TRP   A N   1 1 
ATOM   1219  C  CA  . TRP   A 1  160 ? 9.492   2.988   -24.936 1    18.529  ? 160  TRP   A CA  1 1 
ATOM   1220  C  C   . TRP   A 1  160 ? 8.39    4.033   -24.735 1    18.605  ? 160  TRP   A C   1 1 
ATOM   1221  O  O   . TRP   A 1  160 ? 7.277   3.679   -24.377 1    18.273  ? 160  TRP   A O   1 1 
ATOM   1222  C  CB  . TRP   A 1  160 ? 10.519  3.061   -23.799 1    17.485  ? 160  TRP   A CB  1 1 
ATOM   1223  C  CG  . TRP   A 1  160 ? 9.935   2.671   -22.456 1    16.905  ? 160  TRP   A CG  1 1 
ATOM   1224  C  CD1 . TRP   A 1  160 ? 9.923   1.44    -21.903 1    16.466  ? 160  TRP   A CD1 1 1 
ATOM   1225  C  CD2 . TRP   A 1  160 ? 9.221   3.515   -21.544 1    17.925  ? 160  TRP   A CD2 1 1 
ATOM   1226  N  NE1 . TRP   A 1  160 ? 9.314   1.453   -20.659 1    15.817  ? 160  TRP   A NE1 1 1 
ATOM   1227  C  CE2 . TRP   A 1  160 ? 8.843   2.715   -20.434 1    17.53   ? 160  TRP   A CE2 1 1 
ATOM   1228  C  CE3 . TRP   A 1  160 ? 8.866   4.866   -21.559 1    18.962  ? 160  TRP   A CE3 1 1 
ATOM   1229  C  CZ2 . TRP   A 1  160 ? 8.117   3.233   -19.352 1    19.139  ? 160  TRP   A CZ2 1 1 
ATOM   1230  C  CZ3 . TRP   A 1  160 ? 8.117   5.37    -20.506 1    21.325  ? 160  TRP   A CZ3 1 1 
ATOM   1231  C  CH2 . TRP   A 1  160 ? 7.735   4.57    -19.402 1    19.319  ? 160  TRP   A CH2 1 1 
ATOM   1232  N  N   . GLU   A 1  161 ? 8.714   5.311   -24.905 1    19.197  ? 161  GLU   A N   1 1 
ATOM   1233  C  CA  . GLU   A 1  161 ? 7.762   6.385   -24.661 1    21.399  ? 161  GLU   A CA  1 1 
ATOM   1234  C  C   . GLU   A 1  161 ? 6.634   6.315   -25.691 1    21.438  ? 161  GLU   A C   1 1 
ATOM   1235  O  O   . GLU   A 1  161 ? 5.458   6.467   -25.335 1    19.151  ? 161  GLU   A O   1 1 
ATOM   1236  C  CB  . GLU   A 1  161 ? 8.483   7.729   -24.793 1    24.581  ? 161  GLU   A CB  1 1 
ATOM   1237  C  CG  . GLU   A 1  161 ? 7.584   8.956   -24.671 1    29.614  ? 161  GLU   A CG  1 1 
ATOM   1238  C  CD  . GLU   A 1  161 ? 8.401   10.223  -24.904 1    33.416  ? 161  GLU   A CD  1 1 
ATOM   1239  O  OE1 . GLU   A 1  161 ? 9.205   10.289  -25.876 1    40.72   ? 161  GLU   A OE1 1 1 
ATOM   1240  O  OE2 . GLU   A 1  161 ? 8.211   11.159  -24.119 1    32.873  ? 161  GLU   A OE2 1 1 
ATOM   1241  N  N   . GLY   A 1  162 ? 7.018   6.141   -26.969 1    21.1    ? 162  GLY   A N   1 1 
ATOM   1242  C  CA  . GLY   A 1  162 ? 6.045   6.064   -28.046 1    21.579  ? 162  GLY   A CA  1 1 
ATOM   1243  C  C   . GLY   A 1  162 ? 4.955   5.036   -27.699 1    20.662  ? 162  GLY   A C   1 1 
ATOM   1244  O  O   . GLY   A 1  162 ? 3.749   5.361   -27.803 1    19.669  ? 162  GLY   A O   1 1 
ATOM   1245  N  N   . TRP   A 1  163 ? 5.377   3.803   -27.355 1    19.244  ? 163  TRP   A N   1 1 
ATOM   1246  C  CA  . TRP   A 1  163 ? 4.495   2.692   -27.014 1    18.804  ? 163  TRP   A CA  1 1 
ATOM   1247  C  C   . TRP   A 1  163 ? 3.556   3.013   -25.832 1    19.167  ? 163  TRP   A C   1 1 
ATOM   1248  O  O   . TRP   A 1  163 ? 2.315   2.827   -25.889 1    17.943  ? 163  TRP   A O   1 1 
ATOM   1249  C  CB  . TRP   A 1  163 ? 5.251   1.35    -26.793 1    18.303  ? 163  TRP   A CB  1 1 
ATOM   1250  C  CG  . TRP   A 1  163 ? 4.282   0.263   -26.426 1    17.97   ? 163  TRP   A CG  1 1 
ATOM   1251  C  CD1 . TRP   A 1  163 ? 4.035   -0.369  -25.23  1    17.382  ? 163  TRP   A CD1 1 1 
ATOM   1252  C  CD2 . TRP   A 1  163 ? 3.258   -0.187  -27.331 1    18.857  ? 163  TRP   A CD2 1 1 
ATOM   1253  N  NE1 . TRP   A 1  163 ? 2.963   -1.222  -25.362 1    17.679  ? 163  TRP   A NE1 1 1 
ATOM   1254  C  CE2 . TRP   A 1  163 ? 2.468   -1.112  -26.639 1    18.987  ? 163  TRP   A CE2 1 1 
ATOM   1255  C  CE3 . TRP   A 1  163 ? 2.974   0.112   -28.682 1    21.039  ? 163  TRP   A CE3 1 1 
ATOM   1256  C  CZ2 . TRP   A 1  163 ? 1.387   -1.76   -27.248 1    20.159  ? 163  TRP   A CZ2 1 1 
ATOM   1257  C  CZ3 . TRP   A 1  163 ? 1.883   -0.502  -29.27  1    22.51   ? 163  TRP   A CZ3 1 1 
ATOM   1258  C  CH2 . TRP   A 1  163 ? 1.094   -1.408  -28.546 1    20.684  ? 163  TRP   A CH2 1 1 
ATOM   1259  N  N   . HIS   A 1  164 ? 4.163   3.441   -24.719 1    17.658  ? 164  HIS   A N   1 1 
ATOM   1260  C  CA  . HIS   A 1  164 ? 3.393   3.673   -23.508 1    16.997  ? 164  HIS   A CA  1 1 
ATOM   1261  C  C   . HIS   A 1  164 ? 2.373   4.778   -23.75  1    17.13   ? 164  HIS   A C   1 1 
ATOM   1262  O  O   . HIS   A 1  164 ? 1.225   4.628   -23.319 1    16.894  ? 164  HIS   A O   1 1 
ATOM   1263  C  CB  . HIS   A 1  164 ? 4.316   3.932   -22.3   1    15.655  ? 164  HIS   A CB  1 1 
ATOM   1264  C  CG  . HIS   A 1  164 ? 4.945   2.644   -21.781 1    15.905  ? 164  HIS   A CG  1 1 
ATOM   1265  N  ND1 . HIS   A 1  164 ? 6.059   2.027   -22.336 1    15.046  ? 164  HIS   A ND1 1 1 
ATOM   1266  C  CD2 . HIS   A 1  164 ? 4.576   1.888   -20.752 1    14.79   ? 164  HIS   A CD2 1 1 
ATOM   1267  C  CE1 . HIS   A 1  164 ? 6.322   0.894   -21.686 1    15.434  ? 164  HIS   A CE1 1 1 
ATOM   1268  N  NE2 . HIS   A 1  164 ? 5.446   0.777   -20.677 1    15.992  ? 164  HIS   A NE2 1 1 
ATOM   1269  N  N   . ASN   A 1  165 ? 2.77    5.831   -24.454 1    18.733  ? 165  ASN   A N   1 1 
ATOM   1270  C  CA  . ASN   A 1  165 ? 1.841   6.915   -24.773 1    20.303  ? 165  ASN   A CA  1 1 
ATOM   1271  C  C   . ASN   A 1  165 ? 0.722   6.411   -25.7   1    21.697  ? 165  ASN   A C   1 1 
ATOM   1272  O  O   . ASN   A 1  165 ? -0.439  6.743   -25.515 1    22.184  ? 165  ASN   A O   1 1 
ATOM   1273  C  CB  . ASN   A 1  165 ? 2.535   8.143   -25.365 1    21.921  ? 165  ASN   A CB  1 1 
ATOM   1274  C  CG  . ASN   A 1  165 ? 3.454   8.86    -24.39  1    23.522  ? 165  ASN   A CG  1 1 
ATOM   1275  O  OD1 . ASN   A 1  165 ? 3.414   8.617   -23.182 1    22.649  ? 165  ASN   A OD1 1 1 
ATOM   1276  N  ND2 . ASN   A 1  165 ? 4.258   9.793   -24.878 1    25.681  ? 165  ASN   A ND2 1 1 
ATOM   1277  N  N   . ALA   A 1  166 ? 1.06    5.659   -26.744 1    22.317  ? 166  ALA   A N   1 1 
ATOM   1278  C  CA  . ALA   A 1  166 ? 0.124   5.284   -27.792 1    22.396  ? 166  ALA   A CA  1 1 
ATOM   1279  C  C   . ALA   A 1  166 ? -0.914  4.301   -27.255 1    22.48   ? 166  ALA   A C   1 1 
ATOM   1280  O  O   . ALA   A 1  166 ? -2.111  4.471   -27.526 1    22.009  ? 166  ALA   A O   1 1 
ATOM   1281  C  CB  . ALA   A 1  166 ? 0.888   4.678   -28.965 1    23.006  ? 166  ALA   A CB  1 1 
ATOM   1282  N  N   . ALA   A 1  167 ? -0.472  3.298   -26.462 1    21.568  ? 167  ALA   A N   1 1 
ATOM   1283  C  CA  . ALA   A 1  167 ? -1.354  2.271   -25.944 1    21.83   ? 167  ALA   A CA  1 1 
ATOM   1284  C  C   . ALA   A 1  167 ? -2.046  2.749   -24.674 1    22.741  ? 167  ALA   A C   1 1 
ATOM   1285  O  O   . ALA   A 1  167 ? -3.258  2.608   -24.577 1    23.834  ? 167  ALA   A O   1 1 
ATOM   1286  C  CB  . ALA   A 1  167 ? -0.637  0.947   -25.716 1    20.884  ? 167  ALA   A CB  1 1 
ATOM   1287  N  N   . GLY   A 1  168 ? -1.301  3.336   -23.723 1    20.183  ? 168  GLY   A N   1 1 
ATOM   1288  C  CA  . GLY   A 1  168 ? -1.865  3.575   -22.393 1    17.511  ? 168  GLY   A CA  1 1 
ATOM   1289  C  C   . GLY   A 1  168 ? -2.895  4.71    -22.359 1    18.9    ? 168  GLY   A C   1 1 
ATOM   1290  O  O   . GLY   A 1  168 ? -3.997  4.531   -21.834 1    18.404  ? 168  GLY   A O   1 1 
ATOM   1291  N  N   . ILE   A 1  169 ? -2.551  5.857   -22.959 1    20.014  ? 169  ILE   A N   1 1 
ATOM   1292  C  CA  . ILE   A 1  169 ? -3.341  7.075   -22.821 1    21.999  ? 169  ILE   A CA  1 1 
ATOM   1293  C  C   . ILE   A 1  169 ? -4.808  6.873   -23.251 1    22.615  ? 169  ILE   A C   1 1 
ATOM   1294  O  O   . ILE   A 1  169 ? -5.713  7.195   -22.464 1    23.343  ? 169  ILE   A O   1 1 
ATOM   1295  C  CB  . ILE   A 1  169 ? -2.696  8.316   -23.475 1    21.24   ? 169  ILE   A CB  1 1 
ATOM   1296  C  CG1 . ILE   A 1  169 ? -1.358  8.652   -22.776 1    21.05   ? 169  ILE   A CG1 1 1 
ATOM   1297  C  CG2 . ILE   A 1  169 ? -3.699  9.514   -23.458 1    23.217  ? 169  ILE   A CG2 1 1 
ATOM   1298  C  CD1 . ILE   A 1  169 ? -0.564  9.712   -23.539 1    23.176  ? 169  ILE   A CD1 1 1 
ATOM   1299  N  N   . PRO   A 1  170 ? -5.128  6.34    -24.459 1    22.98   ? 170  PRO   A N   1 1 
ATOM   1300  C  CA  . PRO   A 1  170 ? -6.55   6.145   -24.83  1    23.143  ? 170  PRO   A CA  1 1 
ATOM   1301  C  C   . PRO   A 1  170 ? -7.324  5.082   -24.031 1    20.413  ? 170  PRO   A C   1 1 
ATOM   1302  O  O   . PRO   A 1  170 ? -8.545  5.091   -23.985 1    21.348  ? 170  PRO   A O   1 1 
ATOM   1303  C  CB  . PRO   A 1  170 ? -6.509  5.779   -26.337 1    24.91   ? 170  PRO   A CB  1 1 
ATOM   1304  C  CG  . PRO   A 1  170 ? -5.104  6.189   -26.754 1    27.334  ? 170  PRO   A CG  1 1 
ATOM   1305  C  CD  . PRO   A 1  170 ? -4.186  6.034   -25.556 1    23.527  ? 170  PRO   A CD  1 1 
ATOM   1306  N  N   . LEU   A 1  171 ? -6.631  4.152   -23.403 1    18.924  ? 171  LEU   A N   1 1 
ATOM   1307  C  CA  . LEU   A 1  171 ? -7.256  3.078   -22.639 1    18.639  ? 171  LEU   A CA  1 1 
ATOM   1308  C  C   . LEU   A 1  171 ? -7.825  3.55    -21.304 1    18.712  ? 171  LEU   A C   1 1 
ATOM   1309  O  O   . LEU   A 1  171 ? -8.764  2.925   -20.794 1    20.043  ? 171  LEU   A O   1 1 
ATOM   1310  C  CB  . LEU   A 1  171 ? -6.27   1.94    -22.382 1    17.557  ? 171  LEU   A CB  1 1 
ATOM   1311  C  CG  . LEU   A 1  171 ? -5.92   1.053   -23.578 1    19.397  ? 171  LEU   A CG  1 1 
ATOM   1312  C  CD1 . LEU   A 1  171 ? -4.717  0.114   -23.172 1    20.06   ? 171  LEU   A CD1 1 1 
ATOM   1313  C  CD2 . LEU   A 1  171 ? -7.165  0.193   -23.892 1    18.493  ? 171  LEU   A CD2 1 1 
ATOM   1314  N  N   . LYS   A 1  172 ? -7.259  4.621   -20.738 1    18.087  ? 172  LYS   A N   1 1 
ATOM   1315  C  CA  . LYS   A 1  172 ? -7.545  4.937   -19.342 1    19.401  ? 172  LYS   A CA  1 1 
ATOM   1316  C  C   . LYS   A 1  172 ? -9.066  5.132   -19.137 1    19.253  ? 172  LYS   A C   1 1 
ATOM   1317  O  O   . LYS   A 1  172 ? -9.626  4.593   -18.19  1    19.912  ? 172  LYS   A O   1 1 
ATOM   1318  C  CB  . LYS   A 1  172 ? -6.766  6.167   -18.865 1    18.89   ? 172  LYS   A CB  1 1 
ATOM   1319  C  CG  . LYS   A 1  172 ? -6.863  6.261   -17.341 1    21.018  ? 172  LYS   A CG  1 1 
ATOM   1320  C  CD  . LYS   A 1  172 ? -6.1    7.481   -16.826 1    23.854  ? 172  LYS   A CD  1 1 
ATOM   1321  C  CE  . LYS   A 1  172 ? -6.378  7.469   -15.314 1    27.475  ? 172  LYS   A CE  1 1 
ATOM   1322  N  NZ  . LYS   A 1  172 ? -5.918  8.62    -14.528 1    26.904  ? 172  LYS   A NZ  1 1 
ATOM   1323  N  N   . PRO   A 1  173 ? -9.772  5.975   -19.906 1    20.522  ? 173  PRO   A N   1 1 
ATOM   1324  C  CA  . PRO   A 1  173 ? -11.222 6.139   -19.681 1    20.815  ? 173  PRO   A CA  1 1 
ATOM   1325  C  C   . PRO   A 1  173 ? -12.009 4.831   -19.79  1    20.39   ? 173  PRO   A C   1 1 
ATOM   1326  O  O   . PRO   A 1  173 ? -12.936 4.614   -19.011 1    20.355  ? 173  PRO   A O   1 1 
ATOM   1327  C  CB  . PRO   A 1  173 ? -11.741 7.233   -20.634 1    22.137  ? 173  PRO   A CB  1 1 
ATOM   1328  C  CG  . PRO   A 1  173 ? -10.545 7.554   -21.501 1    23.646  ? 173  PRO   A CG  1 1 
ATOM   1329  C  CD  . PRO   A 1  173 ? -9.253  6.862   -20.971 1    20.546  ? 173  PRO   A CD  1 1 
ATOM   1330  N  N   . LEU   A 1  174 ? -11.604 3.941   -20.708 1    19.072  ? 174  LEU   A N   1 1 
ATOM   1331  C  CA  . LEU   A 1  174 ? -12.287 2.672   -20.883 1    19.57   ? 174  LEU   A CA  1 1 
ATOM   1332  C  C   . LEU   A 1  174 ? -12.037 1.763   -19.674 1    17.853  ? 174  LEU   A C   1 1 
ATOM   1333  O  O   . LEU   A 1  174 ? -12.941 1.061   -19.229 1    17.453  ? 174  LEU   A O   1 1 
ATOM   1334  C  CB  . LEU   A 1  174 ? -11.831 1.967   -22.165 1    20.397  ? 174  LEU   A CB  1 1 
ATOM   1335  C  CG  . LEU   A 1  174 ? -12.399 2.518   -23.493 1    26.837  ? 174  LEU   A CG  1 1 
ATOM   1336  C  CD1 . LEU   A 1  174 ? -11.837 3.846   -23.874 1    29.421  ? 174  LEU   A CD1 1 1 
ATOM   1337  C  CD2 . LEU   A 1  174 ? -12.061 1.505   -24.638 1    25.106  ? 174  LEU   A CD2 1 1 
ATOM   1338  N  N   . TYR   A 1  175 ? -10.779 1.733   -19.208 1    15.644  ? 175  TYR   A N   1 1 
ATOM   1339  C  CA  . TYR   A 1  175 ? -10.411 0.865   -18.109 1    16.555  ? 175  TYR   A CA  1 1 
ATOM   1340  C  C   . TYR   A 1  175 ? -11.203 1.189   -16.842 1    16.529  ? 175  TYR   A C   1 1 
ATOM   1341  O  O   . TYR   A 1  175 ? -11.622 0.271   -16.117 1    15.979  ? 175  TYR   A O   1 1 
ATOM   1342  C  CB  . TYR   A 1  175 ? -8.876  0.845   -17.922 1    15.598  ? 175  TYR   A CB  1 1 
ATOM   1343  C  CG  . TYR   A 1  175 ? -8.502  -0.364  -17.087 1    15.261  ? 175  TYR   A CG  1 1 
ATOM   1344  C  CD1 . TYR   A 1  175 ? -8.394  -1.611  -17.704 1    15.05   ? 175  TYR   A CD1 1 1 
ATOM   1345  C  CD2 . TYR   A 1  175 ? -8.375  -0.275  -15.707 1    14.23   ? 175  TYR   A CD2 1 1 
ATOM   1346  C  CE1 . TYR   A 1  175 ? -8.152  -2.749  -16.94  1    14.519  ? 175  TYR   A CE1 1 1 
ATOM   1347  C  CE2 . TYR   A 1  175 ? -8.103  -1.398  -14.941 1    14.541  ? 175  TYR   A CE2 1 1 
ATOM   1348  C  CZ  . TYR   A 1  175 ? -7.949  -2.631  -15.572 1    13.88   ? 175  TYR   A CZ  1 1 
ATOM   1349  O  OH  . TYR   A 1  175 ? -7.66   -3.765  -14.846 1    14.289  ? 175  TYR   A OH  1 1 
ATOM   1350  N  N   A GLU   A 1  176 ? -11.37  2.482   -16.583 0.59 16.859  ? 176  GLU   A N   1 1 
ATOM   1351  N  N   B GLU   A 1  176 ? -11.377 2.489   -16.575 0.41 16.535  ? 176  GLU   A N   1 1 
ATOM   1352  C  CA  A GLU   A 1  176 ? -12.144 2.951   -15.449 0.59 18.258  ? 176  GLU   A CA  1 1 
ATOM   1353  C  CA  B GLU   A 1  176 ? -12.164 2.959   -15.445 0.41 17.301  ? 176  GLU   A CA  1 1 
ATOM   1354  C  C   A GLU   A 1  176 ? -13.578 2.402   -15.489 0.59 18.084  ? 176  GLU   A C   1 1 
ATOM   1355  C  C   B GLU   A 1  176 ? -13.584 2.386   -15.493 0.41 17.571  ? 176  GLU   A C   1 1 
ATOM   1356  O  O   A GLU   A 1  176 ? -14.082 1.951   -14.445 0.59 16.793  ? 176  GLU   A O   1 1 
ATOM   1357  O  O   B GLU   A 1  176 ? -14.085 1.914   -14.462 0.41 16.707  ? 176  GLU   A O   1 1 
ATOM   1358  C  CB  A GLU   A 1  176 ? -12.102 4.48    -15.426 0.59 20.116  ? 176  GLU   A CB  1 1 
ATOM   1359  C  CB  B GLU   A 1  176 ? -12.232 4.486   -15.339 0.41 18.053  ? 176  GLU   A CB  1 1 
ATOM   1360  C  CG  A GLU   A 1  176 ? -10.695 5.073   -15.44  0.59 21.581  ? 176  GLU   A CG  1 1 
ATOM   1361  C  CG  B GLU   A 1  176 ? -13.238 4.944   -14.284 0.41 18.708  ? 176  GLU   A CG  1 1 
ATOM   1362  C  CD  A GLU   A 1  176 ? -10.839 6.589   -15.446 0.59 24.64   ? 176  GLU   A CD  1 1 
ATOM   1363  C  CD  B GLU   A 1  176 ? -13.348 6.443   -13.979 0.41 19.814  ? 176  GLU   A CD  1 1 
ATOM   1364  O  OE1 A GLU   A 1  176 ? -12.007 6.984   -15.168 0.59 26.347  ? 176  GLU   A OE1 1 1 
ATOM   1365  O  OE1 B GLU   A 1  176 ? -12.587 7.232   -14.566 0.41 19.935  ? 176  GLU   A OE1 1 1 
ATOM   1366  O  OE2 A GLU   A 1  176 ? -9.887  7.372   -15.724 0.59 23.599  ? 176  GLU   A OE2 1 1 
ATOM   1367  O  OE2 B GLU   A 1  176 ? -14.185 6.831   -13.137 0.41 19.696  ? 176  GLU   A OE2 1 1 
ATOM   1368  N  N   . ASP   A 1  177 ? -14.212 2.443   -16.685 1    17.978  ? 177  ASP   A N   1 1 
ATOM   1369  C  CA  . ASP   A 1  177 ? -15.613 2.039   -16.832 1    19.085  ? 177  ASP   A CA  1 1 
ATOM   1370  C  C   . ASP   A 1  177 ? -15.718 0.519   -16.77  1    18.002  ? 177  ASP   A C   1 1 
ATOM   1371  O  O   . ASP   A 1  177 ? -16.626 0.013   -16.134 1    17.368  ? 177  ASP   A O   1 1 
ATOM   1372  C  CB  . ASP   A 1  177 ? -16.23  2.489   -18.153 1    22.181  ? 177  ASP   A CB  1 1 
ATOM   1373  C  CG  . ASP   A 1  177 ? -16.46  3.988   -18.299 1    27.988  ? 177  ASP   A CG  1 1 
ATOM   1374  O  OD1 . ASP   A 1  177 ? -16.296 4.734   -17.3   1    31.616  ? 177  ASP   A OD1 1 1 
ATOM   1375  O  OD2 . ASP   A 1  177 ? -16.78  4.402   -19.424 1    32.033  ? 177  ASP   A OD2 1 1 
ATOM   1376  N  N   . PHE   A 1  178 ? -14.691 -0.176  -17.297 1    16.151  ? 178  PHE   A N   1 1 
ATOM   1377  C  CA  . PHE   A 1  178 ? -14.626 -1.628  -17.252 1    16.345  ? 178  PHE   A CA  1 1 
ATOM   1378  C  C   . PHE   A 1  178 ? -14.563 -2.082  -15.784 1    15.894  ? 178  PHE   A C   1 1 
ATOM   1379  O  O   . PHE   A 1  178 ? -15.263 -3.006  -15.393 1    16.033  ? 178  PHE   A O   1 1 
ATOM   1380  C  CB  . PHE   A 1  178 ? -13.438 -2.206  -18.042 1    16.819  ? 178  PHE   A CB  1 1 
ATOM   1381  C  CG  . PHE   A 1  178 ? -12.987 -3.526  -17.407 1    18.24   ? 178  PHE   A CG  1 1 
ATOM   1382  C  CD1 . PHE   A 1  178 ? -13.627 -4.71   -17.721 1    20.085  ? 178  PHE   A CD1 1 1 
ATOM   1383  C  CD2 . PHE   A 1  178 ? -11.887 -3.584  -16.557 1    20.438  ? 178  PHE   A CD2 1 1 
ATOM   1384  C  CE1 . PHE   A 1  178 ? -13.248 -5.915  -17.12  1    20.321  ? 178  PHE   A CE1 1 1 
ATOM   1385  C  CE2 . PHE   A 1  178 ? -11.49  -4.778  -15.935 1    22.744  ? 178  PHE   A CE2 1 1 
ATOM   1386  C  CZ  . PHE   A 1  178 ? -12.165 -5.96   -16.234 1    22.84   ? 178  PHE   A CZ  1 1 
ATOM   1387  N  N   . THR   A 1  179 ? -13.718 -1.438  -14.978 1    15.933  ? 179  THR   A N   1 1 
ATOM   1388  C  CA  . THR   A 1  179 ? -13.479 -1.808  -13.572 1    15.789  ? 179  THR   A CA  1 1 
ATOM   1389  C  C   . THR   A 1  179 ? -14.783 -1.744  -12.794 1    15.152  ? 179  THR   A C   1 1 
ATOM   1390  O  O   . THR   A 1  179 ? -15.153 -2.665  -12.054 1    14.415  ? 179  THR   A O   1 1 
ATOM   1391  C  CB  . THR   A 1  179 ? -12.453 -0.876  -12.921 1    16.561  ? 179  THR   A CB  1 1 
ATOM   1392  O  OG1 . THR   A 1  179 ? -11.186 -1.245  -13.496 1    19.668  ? 179  THR   A OG1 1 1 
ATOM   1393  C  CG2 . THR   A 1  179 ? -12.389 -1.142  -11.42  1    17.075  ? 179  THR   A CG2 1 1 
ATOM   1394  N  N   . ALA   A 1  180 ? -15.493 -0.623  -12.966 1    15.806  ? 180  ALA   A N   1 1 
ATOM   1395  C  CA  . ALA   A 1  180 ? -16.765 -0.455  -12.273 1    16.06   ? 180  ALA   A CA  1 1 
ATOM   1396  C  C   . ALA   A 1  180 ? -17.776 -1.547  -12.65  1    16.125  ? 180  ALA   A C   1 1 
ATOM   1397  O  O   . ALA   A 1  180 ? -18.464 -2.073  -11.776 1    15.972  ? 180  ALA   A O   1 1 
ATOM   1398  C  CB  . ALA   A 1  180 ? -17.332 0.941   -12.508 1    16.827  ? 180  ALA   A CB  1 1 
ATOM   1399  N  N   . LEU   A 1  181 ? -17.909 -1.883  -13.95  1    15.838  ? 181  LEU   A N   1 1 
ATOM   1400  C  CA  . LEU   A 1  181 ? -18.908 -2.844  -14.391 1    16.474  ? 181  LEU   A CA  1 1 
ATOM   1401  C  C   . LEU   A 1  181 ? -18.499 -4.239  -13.898 1    16.348  ? 181  LEU   A C   1 1 
ATOM   1402  O  O   . LEU   A 1  181 ? -19.346 -5.013  -13.45  1    16.993  ? 181  LEU   A O   1 1 
ATOM   1403  C  CB  . LEU   A 1  181 ? -19.098 -2.829  -15.909 1    16.811  ? 181  LEU   A CB  1 1 
ATOM   1404  C  CG  . LEU   A 1  181 ? -19.862 -1.62   -16.467 1    18.545  ? 181  LEU   A CG  1 1 
ATOM   1405  C  CD1 . LEU   A 1  181 ? -19.573 -1.594  -17.952 1    19.497  ? 181  LEU   A CD1 1 1 
ATOM   1406  C  CD2 . LEU   A 1  181 ? -21.373 -1.774  -16.306 1    19.606  ? 181  LEU   A CD2 1 1 
ATOM   1407  N  N   . SER   A 1  182 ? -17.21  -4.526  -13.957 1    15.811  ? 182  SER   A N   1 1 
ATOM   1408  C  CA  . SER   A 1  182 ? -16.722 -5.848  -13.562 1    16.162  ? 182  SER   A CA  1 1 
ATOM   1409  C  C   . SER   A 1  182 ? -17.061 -6.061  -12.084 1    16.238  ? 182  SER   A C   1 1 
ATOM   1410  O  O   . SER   A 1  182 ? -17.559 -7.123  -11.691 1    18.185  ? 182  SER   A O   1 1 
ATOM   1411  C  CB  . SER   A 1  182 ? -15.221 -5.876  -13.749 1    16.447  ? 182  SER   A CB  1 1 
ATOM   1412  O  OG  . SER   A 1  182 ? -14.729 -7.194  -13.432 1    17.317  ? 182  SER   A OG  1 1 
ATOM   1413  N  N   . ASN   A 1  183 ? -16.743 -5.071  -11.243 1    15.312  ? 183  ASN   A N   1 1 
ATOM   1414  C  CA  . ASN   A 1  183 ? -17.033 -5.146  -9.827  1    15.551  ? 183  ASN   A CA  1 1 
ATOM   1415  C  C   . ASN   A 1  183 ? -18.539 -5.303  -9.584  1    16.724  ? 183  ASN   A C   1 1 
ATOM   1416  O  O   . ASN   A 1  183 ? -18.951 -6.113  -8.776  1    16.577  ? 183  ASN   A O   1 1 
ATOM   1417  C  CB  . ASN   A 1  183 ? -16.577 -3.923  -9.041  1    15.872  ? 183  ASN   A CB  1 1 
ATOM   1418  C  CG  . ASN   A 1  183 ? -15.096 -4      -8.742  1    17.143  ? 183  ASN   A CG  1 1 
ATOM   1419  O  OD1 . ASN   A 1  183 ? -14.485 -5.067  -8.92   1    17.44   ? 183  ASN   A OD1 1 1 
ATOM   1420  N  ND2 . ASN   A 1  183 ? -14.51  -2.865  -8.413  1    16.177  ? 183  ASN   A ND2 1 1 
ATOM   1421  N  N   A GLU   A 1  184 ? -19.36  -4.523  -10.279 0.66 17.05   ? 184  GLU   A N   1 1 
ATOM   1422  N  N   B GLU   A 1  184 ? -19.356 -4.518  -10.288 0.34 17.125  ? 184  GLU   A N   1 1 
ATOM   1423  C  CA  A GLU   A 1  184 ? -20.813 -4.644  -10.126 0.66 18.548  ? 184  GLU   A CA  1 1 
ATOM   1424  C  CA  B GLU   A 1  184 ? -20.81  -4.627  -10.193 0.34 18.429  ? 184  GLU   A CA  1 1 
ATOM   1425  C  C   A GLU   A 1  184 ? -21.312 -6.066  -10.465 0.66 19.091  ? 184  GLU   A C   1 1 
ATOM   1426  C  C   B GLU   A 1  184 ? -21.287 -6.062  -10.442 0.34 19.129  ? 184  GLU   A C   1 1 
ATOM   1427  O  O   A GLU   A 1  184 ? -22.154 -6.633  -9.785  0.66 20.298  ? 184  GLU   A O   1 1 
ATOM   1428  O  O   B GLU   A 1  184 ? -22.108 -6.598  -9.705  0.34 20.126  ? 184  GLU   A O   1 1 
ATOM   1429  C  CB  A GLU   A 1  184 ? -21.458 -3.594  -11.03  0.66 19.834  ? 184  GLU   A CB  1 1 
ATOM   1430  C  CB  B GLU   A 1  184 ? -21.406 -3.792  -11.323 0.34 18.809  ? 184  GLU   A CB  1 1 
ATOM   1431  C  CG  A GLU   A 1  184 ? -22.985 -3.69   -11.01  0.66 22.075  ? 184  GLU   A CG  1 1 
ATOM   1432  C  CG  B GLU   A 1  184 ? -21.543 -2.312  -10.997 0.34 19.412  ? 184  GLU   A CG  1 1 
ATOM   1433  C  CD  A GLU   A 1  184 ? -23.86  -2.716  -11.809 0.66 24.623  ? 184  GLU   A CD  1 1 
ATOM   1434  C  CD  B GLU   A 1  184 ? -22.135 -1.564  -12.185 0.34 19.764  ? 184  GLU   A CD  1 1 
ATOM   1435  O  OE1 A GLU   A 1  184 ? -23.464 -1.588  -12.175 0.66 27.142  ? 184  GLU   A OE1 1 1 
ATOM   1436  O  OE1 B GLU   A 1  184 ? -23.168 -2.049  -12.72  0.34 20.845  ? 184  GLU   A OE1 1 1 
ATOM   1437  O  OE2 A GLU   A 1  184 ? -24.994 -3.117  -12.075 0.66 25.386  ? 184  GLU   A OE2 1 1 
ATOM   1438  O  OE2 B GLU   A 1  184 ? -21.554 -0.526  -12.573 0.34 19.223  ? 184  GLU   A OE2 1 1 
ATOM   1439  N  N   . ALA   A 1  185 ? -20.757 -6.678  -11.493 1    19.587  ? 185  ALA   A N   1 1 
ATOM   1440  C  CA  . ALA   A 1  185 ? -21.07  -8.048  -11.887 1    20.546  ? 185  ALA   A CA  1 1 
ATOM   1441  C  C   . ALA   A 1  185 ? -20.715 -9.045  -10.777 1    21.246  ? 185  ALA   A C   1 1 
ATOM   1442  O  O   . ALA   A 1  185 ? -21.579 -9.802  -10.327 1    22.282  ? 185  ALA   A O   1 1 
ATOM   1443  C  CB  . ALA   A 1  185 ? -20.272 -8.336  -13.144 1    19.737  ? 185  ALA   A CB  1 1 
ATOM   1444  N  N   . TYR   A 1  186 ? -19.46  -9.015  -10.298 1    20.685  ? 186  TYR   A N   1 1 
ATOM   1445  C  CA  . TYR   A 1  186 ? -18.978 -10.028 -9.38   1    20.595  ? 186  TYR   A CA  1 1 
ATOM   1446  C  C   . TYR   A 1  186 ? -19.538 -9.827  -7.986  1    20.018  ? 186  TYR   A C   1 1 
ATOM   1447  O  O   . TYR   A 1  186 ? -19.636 -10.784 -7.198  1    20.496  ? 186  TYR   A O   1 1 
ATOM   1448  C  CB  . TYR   A 1  186 ? -17.449 -10.136 -9.378  1    19.074  ? 186  TYR   A CB  1 1 
ATOM   1449  C  CG  . TYR   A 1  186 ? -17.12  -10.933 -10.608 1    21.371  ? 186  TYR   A CG  1 1 
ATOM   1450  C  CD1 . TYR   A 1  186 ? -17.316 -12.307 -10.624 1    23.059  ? 186  TYR   A CD1 1 1 
ATOM   1451  C  CD2 . TYR   A 1  186 ? -16.661 -10.306 -11.756 1    23.224  ? 186  TYR   A CD2 1 1 
ATOM   1452  C  CE1 . TYR   A 1  186 ? -17.042 -13.049 -11.756 1    22.345  ? 186  TYR   A CE1 1 1 
ATOM   1453  C  CE2 . TYR   A 1  186 ? -16.338 -11.049 -12.883 1    25.285  ? 186  TYR   A CE2 1 1 
ATOM   1454  C  CZ  . TYR   A 1  186 ? -16.516 -12.42  -12.861 1    25.197  ? 186  TYR   A CZ  1 1 
ATOM   1455  O  OH  . TYR   A 1  186 ? -16.288 -13.156 -13.978 1    26.693  ? 186  TYR   A OH  1 1 
ATOM   1456  N  N   . LYS   A 1  187 ? -19.862 -8.59   -7.652  1    20.78   ? 187  LYS   A N   1 1 
ATOM   1457  C  CA  . LYS   A 1  187 ? -20.433 -8.359  -6.347  1    24.754  ? 187  LYS   A CA  1 1 
ATOM   1458  C  C   . LYS   A 1  187 ? -21.805 -9.063  -6.231  1    27.452  ? 187  LYS   A C   1 1 
ATOM   1459  O  O   . LYS   A 1  187 ? -22.209 -9.467  -5.145  1    25.671  ? 187  LYS   A O   1 1 
ATOM   1460  C  CB  . LYS   A 1  187 ? -20.631 -6.854  -6.108  1    31.191  ? 187  LYS   A CB  1 1 
ATOM   1461  C  CG  . LYS   A 1  187 ? -20.861 -6.519  -4.611  1    41.603  ? 187  LYS   A CG  1 1 
ATOM   1462  C  CD  . LYS   A 1  187 ? -21.921 -5.482  -4.234  1    52.589  ? 187  LYS   A CD  1 1 
ATOM   1463  C  CE  . LYS   A 1  187 ? -22.425 -5.688  -2.825  1    57.333  ? 187  LYS   A CE  1 1 
ATOM   1464  N  NZ  . LYS   A 1  187 ? -23.561 -4.811  -2.504  1    68.034  ? 187  LYS   A NZ  1 1 
ATOM   1465  N  N   . GLN   A 1  188 ? -22.514 -9.3    -7.342  1    27.567  ? 188  GLN   A N   1 1 
ATOM   1466  C  CA  . GLN   A 1  188 ? -23.758 -10.08  -7.247  1    30.924  ? 188  GLN   A CA  1 1 
ATOM   1467  C  C   . GLN   A 1  188 ? -23.49  -11.595 -7.183  1    30.614  ? 188  GLN   A C   1 1 
ATOM   1468  O  O   . GLN   A 1  188 ? -24.401 -12.375 -6.94   1    32.189  ? 188  GLN   A O   1 1 
ATOM   1469  C  CB  . GLN   A 1  188 ? -24.688 -9.773  -8.413  1    31.737  ? 188  GLN   A CB  1 1 
ATOM   1470  C  CG  . GLN   A 1  188 ? -25.291 -8.371  -8.339  1    39.549  ? 188  GLN   A CG  1 1 
ATOM   1471  C  CD  . GLN   A 1  188 ? -25.959 -8.003  -9.648  1    51.098  ? 188  GLN   A CD  1 1 
ATOM   1472  O  OE1 . GLN   A 1  188 ? -25.387 -7.294  -10.494 1    57.27   ? 188  GLN   A OE1 1 1 
ATOM   1473  N  NE2 . GLN   A 1  188 ? -27.146 -8.557  -9.867  1    56.415  ? 188  GLN   A NE2 1 1 
ATOM   1474  N  N   . ASP   A 1  189 ? -22.249 -12.031 -7.388  1    29.114  ? 189  ASP   A N   1 1 
ATOM   1475  C  CA  . ASP   A 1  189 ? -21.883 -13.414 -7.115  1    28.278  ? 189  ASP   A CA  1 1 
ATOM   1476  C  C   . ASP   A 1  189 ? -21.464 -13.544 -5.64   1    29.526  ? 189  ASP   A C   1 1 
ATOM   1477  O  O   . ASP   A 1  189 ? -21.131 -14.63  -5.21   1    32.807  ? 189  ASP   A O   1 1 
ATOM   1478  C  CB  . ASP   A 1  189 ? -20.83  -13.927 -8.1    1    29.239  ? 189  ASP   A CB  1 1 
ATOM   1479  C  CG  . ASP   A 1  189 ? -21.196 -13.997 -9.59   1    30.33   ? 189  ASP   A CG  1 1 
ATOM   1480  O  OD1 . ASP   A 1  189 ? -22.289 -14.57  -9.948  1    32.464  ? 189  ASP   A OD1 1 1 
ATOM   1481  O  OD2 . ASP   A 1  189 ? -20.341 -13.577 -10.414 1    30.037  ? 189  ASP   A OD2 1 1 
ATOM   1482  N  N   . GLY   A 1  190 ? -21.486 -12.471 -4.843  1    28.996  ? 190  GLY   A N   1 1 
ATOM   1483  C  CA  . GLY   A 1  190 ? -21.066 -12.483 -3.445  1    29.454  ? 190  GLY   A CA  1 1 
ATOM   1484  C  C   . GLY   A 1  190 ? -19.567 -12.156 -3.209  1    28.93   ? 190  GLY   A C   1 1 
ATOM   1485  O  O   . GLY   A 1  190 ? -19.11  -12.283 -2.096  1    30.76   ? 190  GLY   A O   1 1 
ATOM   1486  N  N   . PHE   A 1  191 ? -18.809 -11.672 -4.196  1    28.058  ? 191  PHE   A N   1 1 
ATOM   1487  C  CA  . PHE   A 1  191 ? -17.401 -11.299 -4.016  1    25.681  ? 191  PHE   A CA  1 1 
ATOM   1488  C  C   . PHE   A 1  191 ? -17.304 -9.82   -3.668  1    26.083  ? 191  PHE   A C   1 1 
ATOM   1489  O  O   . PHE   A 1  191 ? -18.075 -9.025  -4.206  1    28.634  ? 191  PHE   A O   1 1 
ATOM   1490  C  CB  . PHE   A 1  191 ? -16.546 -11.64  -5.244  1    23.282  ? 191  PHE   A CB  1 1 
ATOM   1491  C  CG  . PHE   A 1  191 ? -16.509 -13.145 -5.447  1    24.633  ? 191  PHE   A CG  1 1 
ATOM   1492  C  CD1 . PHE   A 1  191 ? -15.565 -13.921 -4.762  1    22.502  ? 191  PHE   A CD1 1 1 
ATOM   1493  C  CD2 . PHE   A 1  191 ? -17.465 -13.784 -6.252  1    24.202  ? 191  PHE   A CD2 1 1 
ATOM   1494  C  CE1 . PHE   A 1  191 ? -15.548 -15.3   -4.912  1    23.43   ? 191  PHE   A CE1 1 1 
ATOM   1495  C  CE2 . PHE   A 1  191 ? -17.437 -15.166 -6.411  1    25.664  ? 191  PHE   A CE2 1 1 
ATOM   1496  C  CZ  . PHE   A 1  191 ? -16.469 -15.921 -5.739  1    24.043  ? 191  PHE   A CZ  1 1 
ATOM   1497  N  N   . THR   A 1  192 ? -16.366 -9.442  -2.782  1    24.6    ? 192  THR   A N   1 1 
ATOM   1498  C  CA  . THR   A 1  192 ? -16.2   -8.03   -2.446  1    25.291  ? 192  THR   A CA  1 1 
ATOM   1499  C  C   . THR   A 1  192 ? -15.773 -7.177  -3.668  1    21.987  ? 192  THR   A C   1 1 
ATOM   1500  O  O   . THR   A 1  192 ? -16.156 -6.015  -3.788  1    21.854  ? 192  THR   A O   1 1 
ATOM   1501  C  CB  . THR   A 1  192 ? -15.293 -7.925  -1.216  1    29.927  ? 192  THR   A CB  1 1 
ATOM   1502  O  OG1 . THR   A 1  192 ? -15.321 -6.544  -0.886  1    38.749  ? 192  THR   A OG1 1 1 
ATOM   1503  C  CG2 . THR   A 1  192 ? -13.861 -8.328  -1.457  1    25.107  ? 192  THR   A CG2 1 1 
ATOM   1504  N  N   . ASP   A 1  193 ? -15.055 -7.78   -4.624  1    19.188  ? 193  ASP   A N   1 1 
ATOM   1505  C  CA  . ASP   A 1  193 ? -14.628 -7.114  -5.842  1    17.644  ? 193  ASP   A CA  1 1 
ATOM   1506  C  C   . ASP   A 1  193 ? -14.11  -8.187  -6.79   1    16.655  ? 193  ASP   A C   1 1 
ATOM   1507  O  O   . ASP   A 1  193 ? -13.975 -9.367  -6.413  1    15.685  ? 193  ASP   A O   1 1 
ATOM   1508  C  CB  . ASP   A 1  193 ? -13.598 -6.022  -5.592  1    18.385  ? 193  ASP   A CB  1 1 
ATOM   1509  C  CG  . ASP   A 1  193 ? -12.304 -6.473  -4.934  1    20.119  ? 193  ASP   A CG  1 1 
ATOM   1510  O  OD1 . ASP   A 1  193 ? -11.578 -7.281  -5.575  1    18.304  ? 193  ASP   A OD1 1 1 
ATOM   1511  O  OD2 . ASP   A 1  193 ? -12.097 -6.085  -3.729  1    21.464  ? 193  ASP   A OD2 1 1 
ATOM   1512  N  N   . THR   A 1  194 ? -13.768 -7.78   -8.023  1    15.442  ? 194  THR   A N   1 1 
ATOM   1513  C  CA  . THR   A 1  194 ? -13.371 -8.749  -9.038  1    15.217  ? 194  THR   A CA  1 1 
ATOM   1514  C  C   . THR   A 1  194 ? -12.061 -9.457  -8.619  1    15.574  ? 194  THR   A C   1 1 
ATOM   1515  O  O   . THR   A 1  194 ? -11.877 -10.648 -8.911  1    15.375  ? 194  THR   A O   1 1 
ATOM   1516  C  CB  . THR   A 1  194 ? -13.206 -8.041  -10.409 1    14.351  ? 194  THR   A CB  1 1 
ATOM   1517  O  OG1 . THR   A 1  194 ? -14.424 -7.335  -10.783 1    15.416  ? 194  THR   A OG1 1 1 
ATOM   1518  C  CG2 . THR   A 1  194 ? -12.808 -9.035  -11.498 1    14.123  ? 194  THR   A CG2 1 1 
ATOM   1519  N  N   . GLY   A 1  195 ? -11.13  -8.742  -7.972  1    15.188  ? 195  GLY   A N   1 1 
ATOM   1520  C  CA  . GLY   A 1  195 ? -9.84   -9.362  -7.619  1    15.535  ? 195  GLY   A CA  1 1 
ATOM   1521  C  C   . GLY   A 1  195 ? -10.052 -10.464 -6.569  1    16.534  ? 195  GLY   A C   1 1 
ATOM   1522  O  O   . GLY   A 1  195 ? -9.394  -11.51  -6.618  1    16.899  ? 195  GLY   A O   1 1 
ATOM   1523  N  N   . ALA   A 1  196 ? -11.101 -10.332 -5.732  1    15.806  ? 196  ALA   A N   1 1 
ATOM   1524  C  CA  . ALA   A 1  196 ? -11.394 -11.388 -4.763  1    15.227  ? 196  ALA   A CA  1 1 
ATOM   1525  C  C   . ALA   A 1  196 ? -11.871 -12.642 -5.504  1    15.833  ? 196  ALA   A C   1 1 
ATOM   1526  O  O   . ALA   A 1  196 ? -11.565 -13.775 -5.116  1    14.95   ? 196  ALA   A O   1 1 
ATOM   1527  C  CB  . ALA   A 1  196 ? -12.443 -10.979 -3.692  1    14.761  ? 196  ALA   A CB  1 1 
ATOM   1528  N  N   . TYR   A 1  197 ? -12.707 -12.44  -6.53   1    15.609  ? 197  TYR   A N   1 1 
ATOM   1529  C  CA  . TYR   A 1  197 ? -13.077 -13.582 -7.339  1    15.929  ? 197  TYR   A CA  1 1 
ATOM   1530  C  C   . TYR   A 1  197 ? -11.834 -14.167 -8.035  1    15.966  ? 197  TYR   A C   1 1 
ATOM   1531  O  O   . TYR   A 1  197 ? -11.706 -15.395 -8.044  1    18.167  ? 197  TYR   A O   1 1 
ATOM   1532  C  CB  . TYR   A 1  197 ? -14.182 -13.17  -8.3    1    16.5    ? 197  TYR   A CB  1 1 
ATOM   1533  C  CG  . TYR   A 1  197 ? -14.373 -14.225 -9.386  1    17.287  ? 197  TYR   A CG  1 1 
ATOM   1534  C  CD1 . TYR   A 1  197 ? -14.845 -15.498 -9.061  1    18.769  ? 197  TYR   A CD1 1 1 
ATOM   1535  C  CD2 . TYR   A 1  197 ? -14.048 -13.941 -10.689 1    18.221  ? 197  TYR   A CD2 1 1 
ATOM   1536  C  CE1 . TYR   A 1  197 ? -15.03  -16.46  -10.048 1    20.636  ? 197  TYR   A CE1 1 1 
ATOM   1537  C  CE2 . TYR   A 1  197 ? -14.225 -14.885 -11.696 1    21.342  ? 197  TYR   A CE2 1 1 
ATOM   1538  C  CZ  . TYR   A 1  197 ? -14.746 -16.12  -11.358 1    20.225  ? 197  TYR   A CZ  1 1 
ATOM   1539  O  OH  . TYR   A 1  197 ? -14.838 -17.043 -12.334 1    25.691  ? 197  TYR   A OH  1 1 
ATOM   1540  N  N   . TRP   A 1  198 ? -10.959 -13.359 -8.598  1    14.4    ? 198  TRP   A N   1 1 
ATOM   1541  C  CA  . TRP   A 1  198 ? -9.824  -13.979 -9.284  1    15.879  ? 198  TRP   A CA  1 1 
ATOM   1542  C  C   . TRP   A 1  198 ? -8.955  -14.797 -8.29   1    16.268  ? 198  TRP   A C   1 1 
ATOM   1543  O  O   . TRP   A 1  198 ? -8.483  -15.894 -8.63   1    16.144  ? 198  TRP   A O   1 1 
ATOM   1544  C  CB  . TRP   A 1  198 ? -8.945  -12.956 -10.022 1    15.484  ? 198  TRP   A CB  1 1 
ATOM   1545  C  CG  . TRP   A 1  198 ? -9.574  -12.256 -11.204 1    16.115  ? 198  TRP   A CG  1 1 
ATOM   1546  C  CD1 . TRP   A 1  198 ? -10.757 -12.507 -11.856 1    15.978  ? 198  TRP   A CD1 1 1 
ATOM   1547  C  CD2 . TRP   A 1  198 ? -8.887  -11.237 -11.936 1    15.904  ? 198  TRP   A CD2 1 1 
ATOM   1548  N  NE1 . TRP   A 1  198 ? -10.893 -11.649 -12.905 1    15.439  ? 198  TRP   A NE1 1 1 
ATOM   1549  C  CE2 . TRP   A 1  198 ? -9.736  -10.906 -13.015 1    16.414  ? 198  TRP   A CE2 1 1 
ATOM   1550  C  CE3 . TRP   A 1  198 ? -7.613  -10.61  -11.799 1    13.303  ? 198  TRP   A CE3 1 1 
ATOM   1551  C  CZ2 . TRP   A 1  198 ? -9.358  -9.929  -13.932 1    14.886  ? 198  TRP   A CZ2 1 1 
ATOM   1552  C  CZ3 . TRP   A 1  198 ? -7.223  -9.726  -12.794 1    13.266  ? 198  TRP   A CZ3 1 1 
ATOM   1553  C  CH2 . TRP   A 1  198 ? -8.096  -9.389  -13.829 1    14.19   ? 198  TRP   A CH2 1 1 
ATOM   1554  N  N   . ARG   A 1  199 ? -8.734  -14.258 -7.093  1    14.495  ? 199  ARG   A N   1 1 
ATOM   1555  C  CA  . ARG   A 1  199 ? -7.954  -14.964 -6.064  1    16.645  ? 199  ARG   A CA  1 1 
ATOM   1556  C  C   . ARG   A 1  199 ? -8.643  -16.267 -5.61   1    17.954  ? 199  ARG   A C   1 1 
ATOM   1557  O  O   . ARG   A 1  199 ? -7.974  -17.229 -5.23   1    17.473  ? 199  ARG   A O   1 1 
ATOM   1558  C  CB  . ARG   A 1  199 ? -7.63   -14.093 -4.819  1    15.134  ? 199  ARG   A CB  1 1 
ATOM   1559  C  CG  . ARG   A 1  199 ? -6.797  -12.863 -5.151  1    16.241  ? 199  ARG   A CG  1 1 
ATOM   1560  C  CD  . ARG   A 1  199 ? -6.396  -11.996 -3.962  1    16.511  ? 199  ARG   A CD  1 1 
ATOM   1561  N  NE  . ARG   A 1  199 ? -7.552  -11.534 -3.187  1    17.426  ? 199  ARG   A NE  1 1 
ATOM   1562  C  CZ  . ARG   A 1  199 ? -8.07   -10.314 -3.422  1    18.052  ? 199  ARG   A CZ  1 1 
ATOM   1563  N  NH1 . ARG   A 1  199 ? -9.079  -9.908  -2.658  1    17.248  ? 199  ARG   A NH1 1 1 
ATOM   1564  N  NH2 . ARG   A 1  199 ? -7.588  -9.57   -4.443  1    15.642  ? 199  ARG   A NH2 1 1 
ATOM   1565  N  N   . SER   A 1  200 ? -9.987  -16.335 -5.623  1    17.187  ? 200  SER   A N   1 1 
ATOM   1566  C  CA  . SER   A 1  200 ? -10.693 -17.532 -5.164  1    18.914  ? 200  SER   A CA  1 1 
ATOM   1567  C  C   . SER   A 1  200 ? -10.321 -18.787 -5.977  1    19.922  ? 200  SER   A C   1 1 
ATOM   1568  O  O   . SER   A 1  200 ? -10.455 -19.905 -5.47   1    20.121  ? 200  SER   A O   1 1 
ATOM   1569  C  CB  . SER   A 1  200 ? -12.246 -17.331 -5.16   1    19.903  ? 200  SER   A CB  1 1 
ATOM   1570  O  OG  . SER   A 1  200 ? -12.686 -17.459 -6.502  1    20.509  ? 200  SER   A OG  1 1 
ATOM   1571  N  N   . TRP   A 1  201 ? -9.791  -18.63  -7.206  1    18.813  ? 201  TRP   A N   1 1 
ATOM   1572  C  CA  . TRP   A 1  201 ? -9.413  -19.783 -8.001  1    21.999  ? 201  TRP   A CA  1 1 
ATOM   1573  C  C   . TRP   A 1  201 ? -8.275  -20.583 -7.328  1    24.433  ? 201  TRP   A C   1 1 
ATOM   1574  O  O   . TRP   A 1  201 ? -7.977  -21.678 -7.792  1    22.868  ? 201  TRP   A O   1 1 
ATOM   1575  C  CB  . TRP   A 1  201 ? -8.906  -19.368 -9.399  1    23.76   ? 201  TRP   A CB  1 1 
ATOM   1576  C  CG  . TRP   A 1  201 ? -9.923  -18.647 -10.235 1    24.235  ? 201  TRP   A CG  1 1 
ATOM   1577  C  CD1 . TRP   A 1  201 ? -11.279 -18.804 -10.204 1    26.194  ? 201  TRP   A CD1 1 1 
ATOM   1578  C  CD2 . TRP   A 1  201 ? -9.644  -17.629 -11.209 1    25.207  ? 201  TRP   A CD2 1 1 
ATOM   1579  N  NE1 . TRP   A 1  201 ? -11.871 -17.967 -11.123 1    28.152  ? 201  TRP   A NE1 1 1 
ATOM   1580  C  CE2 . TRP   A 1  201 ? -10.897 -17.212 -11.734 1    27.334  ? 201  TRP   A CE2 1 1 
ATOM   1581  C  CE3 . TRP   A 1  201 ? -8.461  -17.036 -11.686 1    23.782  ? 201  TRP   A CE3 1 1 
ATOM   1582  C  CZ2 . TRP   A 1  201 ? -11.006 -16.236 -12.725 1    26.297  ? 201  TRP   A CZ2 1 1 
ATOM   1583  C  CZ3 . TRP   A 1  201 ? -8.575  -16.05  -12.638 1    26.944  ? 201  TRP   A CZ3 1 1 
ATOM   1584  C  CH2 . TRP   A 1  201 ? -9.828  -15.674 -13.158 1    29.846  ? 201  TRP   A CH2 1 1 
ATOM   1585  N  N   . TYR   A 1  202 ? -7.557  -19.996 -6.352  1    20.878  ? 202  TYR   A N   1 1 
ATOM   1586  C  CA  . TYR   A 1  202 ? -6.426  -20.694 -5.763  1    19.407  ? 202  TYR   A CA  1 1 
ATOM   1587  C  C   . TYR   A 1  202 ? -6.91   -21.462 -4.531  1    23.166  ? 202  TYR   A C   1 1 
ATOM   1588  O  O   . TYR   A 1  202 ? -6.156  -22.217 -3.896  1    23.2    ? 202  TYR   A O   1 1 
ATOM   1589  C  CB  . TYR   A 1  202 ? -5.252  -19.754 -5.479  1    16.988  ? 202  TYR   A CB  1 1 
ATOM   1590  C  CG  . TYR   A 1  202 ? -4.608  -19.383 -6.798  1    16.425  ? 202  TYR   A CG  1 1 
ATOM   1591  C  CD1 . TYR   A 1  202 ? -5.08   -18.274 -7.504  1    16.219  ? 202  TYR   A CD1 1 1 
ATOM   1592  C  CD2 . TYR   A 1  202 ? -3.59   -20.159 -7.355  1    15.475  ? 202  TYR   A CD2 1 1 
ATOM   1593  C  CE1 . TYR   A 1  202 ? -4.53   -17.932 -8.727  1    16.299  ? 202  TYR   A CE1 1 1 
ATOM   1594  C  CE2 . TYR   A 1  202 ? -3.03   -19.805 -8.576  1    15.049  ? 202  TYR   A CE2 1 1 
ATOM   1595  C  CZ  . TYR   A 1  202 ? -3.524  -18.713 -9.264  1    14.18   ? 202  TYR   A CZ  1 1 
ATOM   1596  O  OH  . TYR   A 1  202 ? -3.029  -18.312 -10.476 1    13.913  ? 202  TYR   A OH  1 1 
ATOM   1597  N  N   . ASN   A 1  203 ? -8.191  -21.284 -4.188  1    22.7    ? 203  ASN   A N   1 1 
ATOM   1598  C  CA  . ASN   A 1  203 ? -8.793  -21.983 -3.074  1    27.672  ? 203  ASN   A CA  1 1 
ATOM   1599  C  C   . ASN   A 1  203 ? -7.843  -22.092 -1.871  1    30.409  ? 203  ASN   A C   1 1 
ATOM   1600  O  O   . ASN   A 1  203 ? -7.524  -23.197 -1.397  1    28.924  ? 203  ASN   A O   1 1 
ATOM   1601  C  CB  . ASN   A 1  203 ? -9.376  -23.315 -3.535  1    32.862  ? 203  ASN   A CB  1 1 
ATOM   1602  C  CG  . ASN   A 1  203 ? -10.313 -23.817 -2.47   1    39.629  ? 203  ASN   A CG  1 1 
ATOM   1603  O  OD1 . ASN   A 1  203 ? -11.1   -23.035 -1.909  1    43.296  ? 203  ASN   A OD1 1 1 
ATOM   1604  N  ND2 . ASN   A 1  203 ? -10.173 -25.08  -2.109  1    36.613  ? 203  ASN   A ND2 1 1 
ATOM   1605  N  N   . SER   A 1  204 ? -7.374  -20.939 -1.388  1    26.984  ? 204  SER   A N   1 1 
ATOM   1606  C  CA  . SER   A 1  204 ? -6.384  -20.941 -0.329  1    29.94   ? 204  SER   A CA  1 1 
ATOM   1607  C  C   . SER   A 1  204 ? -6.643  -19.717 0.551   1    30.023  ? 204  SER   A C   1 1 
ATOM   1608  O  O   . SER   A 1  204 ? -6.512  -18.571 0.111   1    29.684  ? 204  SER   A O   1 1 
ATOM   1609  C  CB  . SER   A 1  204 ? -5.006  -20.946 -0.987  1    33.478  ? 204  SER   A CB  1 1 
ATOM   1610  O  OG  . SER   A 1  204 ? -3.948  -21.019 -0.045  1    44.497  ? 204  SER   A OG  1 1 
ATOM   1611  N  N   . PRO   A 1  205 ? -7.088  -19.841 1.816   1    34.238  ? 205  PRO   A N   1 1 
ATOM   1612  C  CA  . PRO   A 1  205 ? -7.4    -18.623 2.581   1    33.752  ? 205  PRO   A CA  1 1 
ATOM   1613  C  C   . PRO   A 1  205 ? -6.181  -17.753 2.895   1    35.48   ? 205  PRO   A C   1 1 
ATOM   1614  O  O   . PRO   A 1  205 ? -6.357  -16.582 3.223   1    38.765  ? 205  PRO   A O   1 1 
ATOM   1615  C  CB  . PRO   A 1  205 ? -8.124  -19.15  3.86    1    34.335  ? 205  PRO   A CB  1 1 
ATOM   1616  C  CG  . PRO   A 1  205 ? -7.545  -20.542 3.977   1    37.627  ? 205  PRO   A CG  1 1 
ATOM   1617  C  CD  . PRO   A 1  205 ? -7.367  -21.086 2.547   1    32.46   ? 205  PRO   A CD  1 1 
ATOM   1618  N  N   . THR   A 1  206 ? -4.954  -18.312 2.839   1    29.053  ? 206  THR   A N   1 1 
ATOM   1619  C  CA  . THR   A 1  206 ? -3.783  -17.494 3.142   1    28.29   ? 206  THR   A CA  1 1 
ATOM   1620  C  C   . THR   A 1  206 ? -3.019  -17.133 1.846   1    29.033  ? 206  THR   A C   1 1 
ATOM   1621  O  O   . THR   A 1  206 ? -1.838  -16.797 1.917   1    24.918  ? 206  THR   A O   1 1 
ATOM   1622  C  CB  . THR   A 1  206 ? -2.868  -18.204 4.149   1    28.596  ? 206  THR   A CB  1 1 
ATOM   1623  O  OG1 . THR   A 1  206 ? -2.671  -19.487 3.554   1    30.206  ? 206  THR   A OG1 1 1 
ATOM   1624  C  CG2 . THR   A 1  206 ? -3.479  -18.422 5.53    1    31.349  ? 206  THR   A CG2 1 1 
ATOM   1625  N  N   . PHE   A 1  207 ? -3.67   -17.186 0.671   1    24.58   ? 207  PHE   A N   1 1 
ATOM   1626  C  CA  . PHE   A 1  207 ? -3.003  -16.927 -0.613  1    23.397  ? 207  PHE   A CA  1 1 
ATOM   1627  C  C   . PHE   A 1  207 ? -2.058  -15.723 -0.624  1    22.565  ? 207  PHE   A C   1 1 
ATOM   1628  O  O   . PHE   A 1  207 ? -0.883  -15.863 -0.992  1    21.249  ? 207  PHE   A O   1 1 
ATOM   1629  C  CB  . PHE   A 1  207 ? -4.048  -16.748 -1.716  1    22.626  ? 207  PHE   A CB  1 1 
ATOM   1630  C  CG  . PHE   A 1  207 ? -3.494  -16.754 -3.126  1    20.895  ? 207  PHE   A CG  1 1 
ATOM   1631  C  CD1 . PHE   A 1  207 ? -2.631  -17.755 -3.567  1    20.487  ? 207  PHE   A CD1 1 1 
ATOM   1632  C  CD2 . PHE   A 1  207 ? -3.857  -15.75  -4.021  1    21.647  ? 207  PHE   A CD2 1 1 
ATOM   1633  C  CE1 . PHE   A 1  207 ? -2.16   -17.746 -4.884  1    19.158  ? 207  PHE   A CE1 1 1 
ATOM   1634  C  CE2 . PHE   A 1  207 ? -3.384  -15.767 -5.324  1    17.765  ? 207  PHE   A CE2 1 1 
ATOM   1635  C  CZ  . PHE   A 1  207 ? -2.569  -16.778 -5.752  1    18.601  ? 207  PHE   A CZ  1 1 
ATOM   1636  N  N   . GLU   A 1  208 ? -2.535  -14.527 -0.271  1    21.979  ? 208  GLU   A N   1 1 
ATOM   1637  C  CA  . GLU   A 1  208 ? -1.707  -13.318 -0.356  1    22.388  ? 208  GLU   A CA  1 1 
ATOM   1638  C  C   . GLU   A 1  208 ? -0.483  -13.392 0.568   1    22.101  ? 208  GLU   A C   1 1 
ATOM   1639  O  O   . GLU   A 1  208 ? 0.611   -13.027 0.122   1    19.682  ? 208  GLU   A O   1 1 
ATOM   1640  C  CB  . GLU   A 1  208 ? -2.45   -11.991 -0.092  1    24.795  ? 208  GLU   A CB  1 1 
ATOM   1641  C  CG  . GLU   A 1  208 ? -3.446  -11.731 -1.219  1    29.117  ? 208  GLU   A CG  1 1 
ATOM   1642  C  CD  . GLU   A 1  208 ? -4.26   -10.465 -1.024  1    34.321  ? 208  GLU   A CD  1 1 
ATOM   1643  O  OE1 . GLU   A 1  208 ? -3.624  -9.382  -1.234  1    32.563  ? 208  GLU   A OE1 1 1 
ATOM   1644  O  OE2 . GLU   A 1  208 ? -5.473  -10.574 -0.625  1    33.517  ? 208  GLU   A OE2 1 1 
ATOM   1645  N  N   . ASP   A 1  209 ? -0.674  -13.87  1.806   1    21.05   ? 209  ASP   A N   1 1 
ATOM   1646  C  CA  . ASP   A 1  209 ? 0.433   -14.08  2.738   1    26.568  ? 209  ASP   A CA  1 1 
ATOM   1647  C  C   . ASP   A 1  209 ? 1.404   -15.16  2.259   1    24.388  ? 209  ASP   A C   1 1 
ATOM   1648  O  O   . ASP   A 1  209 ? 2.623   -14.994 2.382   1    23.723  ? 209  ASP   A O   1 1 
ATOM   1649  C  CB  . ASP   A 1  209 ? -0.051  -14.596 4.087   1    32.107  ? 209  ASP   A CB  1 1 
ATOM   1650  C  CG  . ASP   A 1  209 ? -0.879  -13.587 4.849   1    38.937  ? 209  ASP   A CG  1 1 
ATOM   1651  O  OD1 . ASP   A 1  209 ? -0.862  -12.397 4.428   1    39.985  ? 209  ASP   A OD1 1 1 
ATOM   1652  O  OD2 . ASP   A 1  209 ? -1.584  -14.018 5.806   1    48.388  ? 209  ASP   A OD2 1 1 
ATOM   1653  N  N   . ASP   A 1  210 ? 0.883   -16.256 1.688   1    25.077  ? 210  ASP   A N   1 1 
ATOM   1654  C  CA  . ASP   A 1  210 ? 1.73    -17.312 1.122   1    23.78   ? 210  ASP   A CA  1 1 
ATOM   1655  C  C   . ASP   A 1  210 ? 2.652   -16.762 0.023   1    22.749  ? 210  ASP   A C   1 1 
ATOM   1656  O  O   . ASP   A 1  210 ? 3.852   -17.081 -0.007  1    19.638  ? 210  ASP   A O   1 1 
ATOM   1657  C  CB  . ASP   A 1  210 ? 0.907   -18.494 0.656   1    25.374  ? 210  ASP   A CB  1 1 
ATOM   1658  C  CG  . ASP   A 1  210 ? 0.236   -19.224 1.818   1    32.843  ? 210  ASP   A CG  1 1 
ATOM   1659  O  OD1 . ASP   A 1  210 ? 0.617   -18.954 2.993   1    34.006  ? 210  ASP   A OD1 1 1 
ATOM   1660  O  OD2 . ASP   A 1  210 ? -0.668  -20.027 1.534   1    39.233  ? 210  ASP   A OD2 1 1 
ATOM   1661  N  N   . LEU   A 1  211 ? 2.103   -15.871 -0.822  1    19.373  ? 211  LEU   A N   1 1 
ATOM   1662  C  CA  . LEU   A 1  211 ? 2.864   -15.294 -1.942  1    17.907  ? 211  LEU   A CA  1 1 
ATOM   1663  C  C   . LEU   A 1  211 ? 3.886   -14.322 -1.375  1    17.73   ? 211  LEU   A C   1 1 
ATOM   1664  O  O   . LEU   A 1  211 ? 4.996   -14.253 -1.887  1    18.012  ? 211  LEU   A O   1 1 
ATOM   1665  C  CB  . LEU   A 1  211 ? 1.895   -14.523 -2.859  1    19.074  ? 211  LEU   A CB  1 1 
ATOM   1666  C  CG  . LEU   A 1  211 ? 0.874   -15.344 -3.667  1    20.221  ? 211  LEU   A CG  1 1 
ATOM   1667  C  CD1 . LEU   A 1  211 ? -0.235  -14.419 -4.224  1    21.418  ? 211  LEU   A CD1 1 1 
ATOM   1668  C  CD2 . LEU   A 1  211 ? 1.512   -16.058 -4.826  1    20.933  ? 211  LEU   A CD2 1 1 
ATOM   1669  N  N   . GLU   A 1  212 ? 3.493   -13.534 -0.351  1    18.085  ? 212  GLU   A N   1 1 
ATOM   1670  C  CA  . GLU   A 1  212 ? 4.415   -12.569 0.221   1    21.055  ? 212  GLU   A CA  1 1 
ATOM   1671  C  C   . GLU   A 1  212 ? 5.613   -13.317 0.807   1    22.64   ? 212  GLU   A C   1 1 
ATOM   1672  O  O   . GLU   A 1  212 ? 6.746   -12.859 0.661   1    22.433  ? 212  GLU   A O   1 1 
ATOM   1673  C  CB  . GLU   A 1  212 ? 3.752   -11.562 1.169   1    24.107  ? 212  GLU   A CB  1 1 
ATOM   1674  C  CG  . GLU   A 1  212 ? 4.735   -10.666 1.909   1    33.982  ? 212  GLU   A CG  1 1 
ATOM   1675  C  CD  . GLU   A 1  212 ? 4.173   -9.446  2.63    1    51.989  ? 212  GLU   A CD  1 1 
ATOM   1676  O  OE1 . GLU   A 1  212 ? 3.259   -9.685  3.451   1    55.563  ? 212  GLU   A OE1 1 1 
ATOM   1677  O  OE2 . GLU   A 1  212 ? 4.621   -8.274  2.404   1    66.088  ? 212  GLU   A OE2 1 1 
ATOM   1678  N  N   . HIS   A 1  213 ? 5.361   -14.468 1.432   1    22.502  ? 213  HIS   A N   1 1 
ATOM   1679  C  CA  . HIS   A 1  213 ? 6.411   -15.248 2.077   1    26.565  ? 213  HIS   A CA  1 1 
ATOM   1680  C  C   . HIS   A 1  213 ? 7.364   -15.832 1.031   1    24.793  ? 213  HIS   A C   1 1 
ATOM   1681  O  O   . HIS   A 1  213 ? 8.591   -15.907 1.241   1    22.079  ? 213  HIS   A O   1 1 
ATOM   1682  C  CB  . HIS   A 1  213 ? 5.796   -16.267 3.041   1    28.821  ? 213  HIS   A CB  1 1 
ATOM   1683  C  CG  . HIS   A 1  213 ? 5.11    -15.614 4.225   1    45.644  ? 213  HIS   A CG  1 1 
ATOM   1684  N  ND1 . HIS   A 1  213 ? 4.512   -16.347 5.243   1    51.992  ? 213  HIS   A ND1 1 1 
ATOM   1685  C  CD2 . HIS   A 1  213 ? 4.837   -14.31  4.528   1    51.292  ? 213  HIS   A CD2 1 1 
ATOM   1686  C  CE1 . HIS   A 1  213 ? 3.952   -15.532 6.142   1    49.791  ? 213  HIS   A CE1 1 1 
ATOM   1687  N  NE2 . HIS   A 1  213 ? 4.136   -14.287 5.73    1    57.243  ? 213  HIS   A NE2 1 1 
ATOM   1688  N  N   . LEU   A 1  214 ? 6.787   -16.267 -0.1    1    21.82   ? 214  LEU   A N   1 1 
ATOM   1689  C  CA  . LEU   A 1  214 ? 7.56    -16.739 -1.23   1    21.419  ? 214  LEU   A CA  1 1 
ATOM   1690  C  C   . LEU   A 1  214 ? 8.461   -15.621 -1.703  1    18.615  ? 214  LEU   A C   1 1 
ATOM   1691  O  O   . LEU   A 1  214 ? 9.67    -15.846 -1.897  1    18.152  ? 214  LEU   A O   1 1 
ATOM   1692  C  CB  . LEU   A 1  214 ? 6.771   -17.262 -2.45   1    21.282  ? 214  LEU   A CB  1 1 
ATOM   1693  C  CG  . LEU   A 1  214 ? 6.08    -18.611 -2.277  1    26.425  ? 214  LEU   A CG  1 1 
ATOM   1694  C  CD1 . LEU   A 1  214 ? 5.209   -18.893 -3.526  1    25.474  ? 214  LEU   A CD1 1 1 
ATOM   1695  C  CD2 . LEU   A 1  214 ? 7.171   -19.683 -2.109  1    25.637  ? 214  LEU   A CD2 1 1 
ATOM   1696  N  N   . TYR   A 1  215 ? 7.843   -14.452 -1.957  1    17.599  ? 215  TYR   A N   1 1 
ATOM   1697  C  CA  . TYR   A 1  215 ? 8.578   -13.316 -2.496  1    17.825  ? 215  TYR   A CA  1 1 
ATOM   1698  C  C   . TYR   A 1  215 ? 9.777   -12.963 -1.58   1    19.326  ? 215  TYR   A C   1 1 
ATOM   1699  O  O   . TYR   A 1  215 ? 10.878  -12.665 -2.081  1    17.013  ? 215  TYR   A O   1 1 
ATOM   1700  C  CB  . TYR   A 1  215 ? 7.724   -12.083 -2.828  1    18.966  ? 215  TYR   A CB  1 1 
ATOM   1701  C  CG  . TYR   A 1  215 ? 8.6     -11.181 -3.686  1    20.035  ? 215  TYR   A CG  1 1 
ATOM   1702  C  CD1 . TYR   A 1  215 ? 8.802   -11.519 -5.015  1    23.104  ? 215  TYR   A CD1 1 1 
ATOM   1703  C  CD2 . TYR   A 1  215 ? 9.217   -10.04  -3.186  1    19.435  ? 215  TYR   A CD2 1 1 
ATOM   1704  C  CE1 . TYR   A 1  215 ? 9.633   -10.792 -5.84   1    24.228  ? 215  TYR   A CE1 1 1 
ATOM   1705  C  CE2 . TYR   A 1  215 ? 10.027  -9.276  -4.009  1    20.696  ? 215  TYR   A CE2 1 1 
ATOM   1706  C  CZ  . TYR   A 1  215 ? 10.237  -9.665  -5.326  1    23.081  ? 215  TYR   A CZ  1 1 
ATOM   1707  O  OH  . TYR   A 1  215 ? 11.08   -9.013  -6.164  1    24.925  ? 215  TYR   A OH  1 1 
ATOM   1708  N  N   . GLN   A 1  216 ? 9.569   -13.016 -0.252  1    16.743  ? 216  GLN   A N   1 1 
ATOM   1709  C  CA  . GLN   A 1  216 ? 10.657  -12.671 0.667   1    19.662  ? 216  GLN   A CA  1 1 
ATOM   1710  C  C   . GLN   A 1  216 ? 11.884  -13.559 0.481   1    19.582  ? 216  GLN   A C   1 1 
ATOM   1711  O  O   . GLN   A 1  216 ? 12.98   -13.08  0.688   1    20.54   ? 216  GLN   A O   1 1 
ATOM   1712  C  CB  . GLN   A 1  216 ? 10.317  -12.706 2.155   1    24.281  ? 216  GLN   A CB  1 1 
ATOM   1713  C  CG  . GLN   A 1  216 ? 9.251   -11.661 2.505   1    33.193  ? 216  GLN   A CG  1 1 
ATOM   1714  C  CD  . GLN   A 1  216 ? 8.757   -11.829 3.926   1    43.987  ? 216  GLN   A CD  1 1 
ATOM   1715  O  OE1 . GLN   A 1  216 ? 9.174   -12.771 4.625   1    46.101  ? 216  GLN   A OE1 1 1 
ATOM   1716  N  NE2 . GLN   A 1  216 ? 7.868   -10.937 4.361   1    39.256  ? 216  GLN   A NE2 1 1 
ATOM   1717  N  N   . GLN   A 1  217 ? 11.702  -14.832 0.134   1    19.137  ? 217  GLN   A N   1 1 
ATOM   1718  C  CA  . GLN   A 1  217 ? 12.812  -15.749 -0.065  1    21.518  ? 217  GLN   A CA  1 1 
ATOM   1719  C  C   . GLN   A 1  217 ? 13.512  -15.498 -1.403  1    19.75   ? 217  GLN   A C   1 1 
ATOM   1720  O  O   . GLN   A 1  217 ? 14.703  -15.796 -1.568  1    18.9    ? 217  GLN   A O   1 1 
ATOM   1721  C  CB  . GLN   A 1  217 ? 12.27   -17.176 -0.112  1    24.045  ? 217  GLN   A CB  1 1 
ATOM   1722  C  CG  . GLN   A 1  217 ? 11.633  -17.667 1.18    1    30.406  ? 217  GLN   A CG  1 1 
ATOM   1723  C  CD  . GLN   A 1  217 ? 11.38   -19.151 1.056   1    34.126  ? 217  GLN   A CD  1 1 
ATOM   1724  O  OE1 . GLN   A 1  217 ? 12.31   -19.964 1.137   1    37.964  ? 217  GLN   A OE1 1 1 
ATOM   1725  N  NE2 . GLN   A 1  217 ? 10.133  -19.517 0.805   1    31.436  ? 217  GLN   A NE2 1 1 
ATOM   1726  N  N   . LEU   A 1  218 ? 12.785  -14.949 -2.372  1    17.957  ? 218  LEU   A N   1 1 
ATOM   1727  C  CA  . LEU   A 1  218 ? 13.346  -14.802 -3.711  1    17.386  ? 218  LEU   A CA  1 1 
ATOM   1728  C  C   . LEU   A 1  218 ? 13.976  -13.434 -3.861  1    17.107  ? 218  LEU   A C   1 1 
ATOM   1729  O  O   . LEU   A 1  218 ? 14.782  -13.23  -4.753  1    18.088  ? 218  LEU   A O   1 1 
ATOM   1730  C  CB  . LEU   A 1  218 ? 12.206  -14.963 -4.716  1    15.763  ? 218  LEU   A CB  1 1 
ATOM   1731  C  CG  . LEU   A 1  218 ? 11.568  -16.34  -4.69   1    17.473  ? 218  LEU   A CG  1 1 
ATOM   1732  C  CD1 . LEU   A 1  218 ? 10.303  -16.283 -5.545  1    19.394  ? 218  LEU   A CD1 1 1 
ATOM   1733  C  CD2 . LEU   A 1  218 ? 12.472  -17.408 -5.312  1    21.156  ? 218  LEU   A CD2 1 1 
ATOM   1734  N  N   . GLU   A 1  219 ? 13.515  -12.468 -3.054  1    16.841  ? 219  GLU   A N   1 1 
ATOM   1735  C  CA  . GLU   A 1  219 ? 13.948  -11.094 -3.248  1    17.233  ? 219  GLU   A CA  1 1 
ATOM   1736  C  C   . GLU   A 1  219 ? 15.486  -10.951 -3.253  1    18.454  ? 219  GLU   A C   1 1 
ATOM   1737  O  O   . GLU   A 1  219 ? 16.023  -10.181 -4.026  1    17.188  ? 219  GLU   A O   1 1 
ATOM   1738  C  CB  . GLU   A 1  219 ? 13.393  -10.164 -2.178  1    20.906  ? 219  GLU   A CB  1 1 
ATOM   1739  C  CG  . GLU   A 1  219 ? 13.505  -8.731  -2.677  1    28.788  ? 219  GLU   A CG  1 1 
ATOM   1740  C  CD  . GLU   A 1  219 ? 12.92   -7.583  -1.886  1    39.819  ? 219  GLU   A CD  1 1 
ATOM   1741  O  OE1 . GLU   A 1  219 ? 12.508  -7.82   -0.732  1    40.05   ? 219  GLU   A OE1 1 1 
ATOM   1742  O  OE2 . GLU   A 1  219 ? 12.86   -6.455  -2.449  1    47.262  ? 219  GLU   A OE2 1 1 
ATOM   1743  N  N   . PRO   A 1  220 ? 16.274  -11.547 -2.326  1    18.916  ? 220  PRO   A N   1 1 
ATOM   1744  C  CA  . PRO   A 1  220 ? 17.726  -11.359 -2.383  1    20.244  ? 220  PRO   A CA  1 1 
ATOM   1745  C  C   . PRO   A 1  220 ? 18.34   -11.745 -3.738  1    19.868  ? 220  PRO   A C   1 1 
ATOM   1746  O  O   . PRO   A 1  220 ? 19.356  -11.149 -4.1    1    21.398  ? 220  PRO   A O   1 1 
ATOM   1747  C  CB  . PRO   A 1  220 ? 18.28   -12.261 -1.276  1    20.398  ? 220  PRO   A CB  1 1 
ATOM   1748  C  CG  . PRO   A 1  220 ? 17.079  -12.435 -0.313  1    20.624  ? 220  PRO   A CG  1 1 
ATOM   1749  C  CD  . PRO   A 1  220 ? 15.841  -12.428 -1.215  1    20.381  ? 220  PRO   A CD  1 1 
ATOM   1750  N  N   . LEU   A 1  221 ? 17.811  -12.804 -4.408  1    18.166  ? 221  LEU   A N   1 1 
ATOM   1751  C  CA  . LEU   A 1  221 ? 18.382  -13.266 -5.665  1    17.221  ? 221  LEU   A CA  1 1 
ATOM   1752  C  C   . LEU   A 1  221 ? 18.181  -12.117 -6.657  1    17.385  ? 221  LEU   A C   1 1 
ATOM   1753  O  O   . LEU   A 1  221 ? 19.044  -11.784 -7.484  1    15.306  ? 221  LEU   A O   1 1 
ATOM   1754  C  CB  . LEU   A 1  221 ? 17.671  -14.537 -6.177  1    18.243  ? 221  LEU   A CB  1 1 
ATOM   1755  C  CG  . LEU   A 1  221 ? 18.19   -15.869 -5.627  1    21.21   ? 221  LEU   A CG  1 1 
ATOM   1756  C  CD1 . LEU   A 1  221 ? 18.115  -15.933 -4.117  1    22.459  ? 221  LEU   A CD1 1 1 
ATOM   1757  C  CD2 . LEU   A 1  221 ? 17.484  -17.055 -6.335  1    19.33   ? 221  LEU   A CD2 1 1 
ATOM   1758  N  N   . TYR   A 1  222 ? 16.955  -11.554 -6.631  1    15.064  ? 222  TYR   A N   1 1 
ATOM   1759  C  CA  . TYR   A 1  222 ? 16.649  -10.475 -7.562  1    14.559  ? 222  TYR   A CA  1 1 
ATOM   1760  C  C   . TYR   A 1  222 ? 17.538  -9.267  -7.296  1    14.468  ? 222  TYR   A C   1 1 
ATOM   1761  O  O   . TYR   A 1  222 ? 18.043  -8.657  -8.23   1    15.479  ? 222  TYR   A O   1 1 
ATOM   1762  C  CB  . TYR   A 1  222 ? 15.168  -10.079 -7.546  1    13.138  ? 222  TYR   A CB  1 1 
ATOM   1763  C  CG  . TYR   A 1  222 ? 14.943  -8.94   -8.523  1    14.387  ? 222  TYR   A CG  1 1 
ATOM   1764  C  CD1 . TYR   A 1  222 ? 14.88   -9.174  -9.911  1    14.297  ? 222  TYR   A CD1 1 1 
ATOM   1765  C  CD2 . TYR   A 1  222 ? 14.765  -7.612  -8.084  1    15.173  ? 222  TYR   A CD2 1 1 
ATOM   1766  C  CE1 . TYR   A 1  222 ? 14.789  -8.12   -10.814 1    14.328  ? 222  TYR   A CE1 1 1 
ATOM   1767  C  CE2 . TYR   A 1  222 ? 14.572  -6.572  -8.995  1    14.297  ? 222  TYR   A CE2 1 1 
ATOM   1768  C  CZ  . TYR   A 1  222 ? 14.579  -6.828  -10.362 1    13.661  ? 222  TYR   A CZ  1 1 
ATOM   1769  O  OH  . TYR   A 1  222 ? 14.392  -5.849  -11.306 1    12.867  ? 222  TYR   A OH  1 1 
ATOM   1770  N  N   . LEU   A 1  223 ? 17.736  -8.904  -6.031  1    14.631  ? 223  LEU   A N   1 1 
ATOM   1771  C  CA  . LEU   A 1  223 ? 18.512  -7.705  -5.736  1    15.315  ? 223  LEU   A CA  1 1 
ATOM   1772  C  C   . LEU   A 1  223 ? 19.951  -7.885  -6.248  1    14.971  ? 223  LEU   A C   1 1 
ATOM   1773  O  O   . LEU   A 1  223 ? 20.528  -6.921  -6.698  1    15.303  ? 223  LEU   A O   1 1 
ATOM   1774  C  CB  . LEU   A 1  223 ? 18.577  -7.361  -4.233  1    17.107  ? 223  LEU   A CB  1 1 
ATOM   1775  C  CG  . LEU   A 1  223 ? 17.238  -6.945  -3.583  1    21.43   ? 223  LEU   A CG  1 1 
ATOM   1776  C  CD1 . LEU   A 1  223 ? 17.372  -6.666  -2.059  1    21.495  ? 223  LEU   A CD1 1 1 
ATOM   1777  C  CD2 . LEU   A 1  223 ? 16.602  -5.78   -4.323  1    23.24   ? 223  LEU   A CD2 1 1 
ATOM   1778  N  N   . ASN   A 1  224 ? 20.539  -9.075  -6.094  1    15.264  ? 224  ASN   A N   1 1 
ATOM   1779  C  CA  . ASN   A 1  224 ? 21.909  -9.284  -6.555  1    16.206  ? 224  ASN   A CA  1 1 
ATOM   1780  C  C   . ASN   A 1  224 ? 21.985  -9.271  -8.086  1    16.001  ? 224  ASN   A C   1 1 
ATOM   1781  O  O   . ASN   A 1  224 ? 22.951  -8.732  -8.687  1    17.142  ? 224  ASN   A O   1 1 
ATOM   1782  C  CB  . ASN   A 1  224 ? 22.514  -10.548 -5.947  1    17.25   ? 224  ASN   A CB  1 1 
ATOM   1783  C  CG  . ASN   A 1  224 ? 23.047  -10.229 -4.559  1    19.698  ? 224  ASN   A CG  1 1 
ATOM   1784  O  OD1 . ASN   A 1  224 ? 24.144  -9.685  -4.429  1    21.397  ? 224  ASN   A OD1 1 1 
ATOM   1785  N  ND2 . ASN   A 1  224 ? 22.319  -10.593 -3.518  1    18.813  ? 224  ASN   A ND2 1 1 
ATOM   1786  N  N   . LEU   A 1  225 ? 20.996  -9.894  -8.728  1    15.223  ? 225  LEU   A N   1 1 
ATOM   1787  C  CA  . LEU   A 1  225 ? 20.985  -9.895  -10.207 1    15.102  ? 225  LEU   A CA  1 1 
ATOM   1788  C  C   . LEU   A 1  225 ? 20.903  -8.455  -10.748 1    15.914  ? 225  LEU   A C   1 1 
ATOM   1789  O  O   . LEU   A 1  225 ? 21.632  -8.016  -11.655 1    15.481  ? 225  LEU   A O   1 1 
ATOM   1790  C  CB  . LEU   A 1  225 ? 19.813  -10.719 -10.742 1    13.693  ? 225  LEU   A CB  1 1 
ATOM   1791  C  CG  . LEU   A 1  225 ? 19.729  -10.675 -12.271 1    14.679  ? 225  LEU   A CG  1 1 
ATOM   1792  C  CD1 . LEU   A 1  225 ? 20.828  -11.628 -12.768 1    14.091  ? 225  LEU   A CD1 1 1 
ATOM   1793  C  CD2 . LEU   A 1  225 ? 18.409  -11.281 -12.7   1    14.692  ? 225  LEU   A CD2 1 1 
ATOM   1794  N  N   . HIS   A 1  226 ? 19.979  -7.675  -10.171 1    16.07   ? 226  HIS   A N   1 1 
ATOM   1795  C  CA  . HIS   A 1  226 ? 19.762  -6.25   -10.47  1    16.194  ? 226  HIS   A CA  1 1 
ATOM   1796  C  C   . HIS   A 1  226 ? 21.043  -5.434  -10.361 1    16.442  ? 226  HIS   A C   1 1 
ATOM   1797  O  O   . HIS   A 1  226 ? 21.401  -4.685  -11.276 1    17.504  ? 226  HIS   A O   1 1 
ATOM   1798  C  CB  . HIS   A 1  226 ? 18.604  -5.698  -9.599  1    14.978  ? 226  HIS   A CB  1 1 
ATOM   1799  C  CG  . HIS   A 1  226 ? 18.289  -4.231  -9.703  1    14.627  ? 226  HIS   A CG  1 1 
ATOM   1800  N  ND1 . HIS   A 1  226 ? 19.026  -3.227  -9.131  1    14.617  ? 226  HIS   A ND1 1 1 
ATOM   1801  C  CD2 . HIS   A 1  226 ? 17.199  -3.614  -10.281 1    14.216  ? 226  HIS   A CD2 1 1 
ATOM   1802  C  CE1 . HIS   A 1  226 ? 18.48   -2.061  -9.434  1    14.921  ? 226  HIS   A CE1 1 1 
ATOM   1803  N  NE2 . HIS   A 1  226 ? 17.364  -2.274  -10.096 1    14.464  ? 226  HIS   A NE2 1 1 
ATOM   1804  N  N   . ALA   A 1  227 ? 21.732  -5.569  -9.243  1    16.127  ? 227  ALA   A N   1 1 
ATOM   1805  C  CA  . ALA   A 1  227 ? 22.924  -4.78   -8.984  1    16.486  ? 227  ALA   A CA  1 1 
ATOM   1806  C  C   . ALA   A 1  227 ? 24.016  -5.09   -10.013 1    17.052  ? 227  ALA   A C   1 1 
ATOM   1807  O  O   . ALA   A 1  227 ? 24.714  -4.189  -10.478 1    17.137  ? 227  ALA   A O   1 1 
ATOM   1808  C  CB  . ALA   A 1  227 ? 23.415  -5      -7.543  1    16.396  ? 227  ALA   A CB  1 1 
ATOM   1809  N  N   . PHE   A 1  228 ? 24.112  -6.365  -10.374 1    17.267  ? 228  PHE   A N   1 1 
ATOM   1810  C  CA  . PHE   A 1  228 ? 25.164  -6.801  -11.261 1    18.574  ? 228  PHE   A CA  1 1 
ATOM   1811  C  C   . PHE   A 1  228 ? 24.838  -6.265  -12.654 1    18.05   ? 228  PHE   A C   1 1 
ATOM   1812  O  O   . PHE   A 1  228 ? 25.723  -5.816  -13.392 1    17.901  ? 228  PHE   A O   1 1 
ATOM   1813  C  CB  . PHE   A 1  228 ? 25.122  -8.334  -11.227 1    19.828  ? 228  PHE   A CB  1 1 
ATOM   1814  C  CG  . PHE   A 1  228 ? 26.152  -8.97   -12.153 1    22.959  ? 228  PHE   A CG  1 1 
ATOM   1815  C  CD1 . PHE   A 1  228 ? 27.479  -9.066  -11.75  1    25.817  ? 228  PHE   A CD1 1 1 
ATOM   1816  C  CD2 . PHE   A 1  228 ? 25.779  -9.523  -13.375 1    24.239  ? 228  PHE   A CD2 1 1 
ATOM   1817  C  CE1 . PHE   A 1  228 ? 28.432  -9.636  -12.576 1    28.262  ? 228  PHE   A CE1 1 1 
ATOM   1818  C  CE2 . PHE   A 1  228 ? 26.756  -10.079 -14.204 1    26.975  ? 228  PHE   A CE2 1 1 
ATOM   1819  C  CZ  . PHE   A 1  228 ? 28.052  -10.133 -13.801 1    27.99   ? 228  PHE   A CZ  1 1 
ATOM   1820  N  N   . VAL   A 1  229 ? 23.568  -6.371  -13.049 1    16.175  ? 229  VAL   A N   1 1 
ATOM   1821  C  CA  . VAL   A 1  229 ? 23.15   -5.878  -14.355 1    16.064  ? 229  VAL   A CA  1 1 
ATOM   1822  C  C   . VAL   A 1  229 ? 23.289  -4.351  -14.439 1    15.938  ? 229  VAL   A C   1 1 
ATOM   1823  O  O   . VAL   A 1  229 ? 23.778  -3.793  -15.433 1    16.894  ? 229  VAL   A O   1 1 
ATOM   1824  C  CB  . VAL   A 1  229 ? 21.71   -6.349  -14.677 1    15.635  ? 229  VAL   A CB  1 1 
ATOM   1825  C  CG1 . VAL   A 1  229 ? 21.185  -5.638  -15.922 1    15.652  ? 229  VAL   A CG1 1 1 
ATOM   1826  C  CG2 . VAL   A 1  229 ? 21.642  -7.88   -14.837 1    16.146  ? 229  VAL   A CG2 1 1 
ATOM   1827  N  N   . ARG   A 1  230 ? 22.91   -3.658  -13.37  1    15.983  ? 230  ARG   A N   1 1 
ATOM   1828  C  CA  . ARG   A 1  230 ? 23.054  -2.208  -13.282 1    16.279  ? 230  ARG   A CA  1 1 
ATOM   1829  C  C   . ARG   A 1  230 ? 24.507  -1.791  -13.557 1    17.959  ? 230  ARG   A C   1 1 
ATOM   1830  O  O   . ARG   A 1  230 ? 24.75   -0.826  -14.306 1    17.944  ? 230  ARG   A O   1 1 
ATOM   1831  C  CB  . ARG   A 1  230 ? 22.483  -1.62   -11.984 1    16.197  ? 230  ARG   A CB  1 1 
ATOM   1832  C  CG  . ARG   A 1  230 ? 22.462  -0.102  -11.892 1    17.059  ? 230  ARG   A CG  1 1 
ATOM   1833  C  CD  . ARG   A 1  230 ? 21.799  0.358   -10.561 1    17.961  ? 230  ARG   A CD  1 1 
ATOM   1834  N  NE  . ARG   A 1  230 ? 22.459  -0.313  -9.426  1    18.302  ? 230  ARG   A NE  1 1 
ATOM   1835  C  CZ  . ARG   A 1  230 ? 21.901  -0.392  -8.198  1    18.36   ? 230  ARG   A CZ  1 1 
ATOM   1836  N  NH1 . ARG   A 1  230 ? 20.802  0.313   -7.923  1    17.645  ? 230  ARG   A NH1 1 1 
ATOM   1837  N  NH2 . ARG   A 1  230 ? 22.492  -1.071  -7.217  1    17.883  ? 230  ARG   A NH2 1 1 
ATOM   1838  N  N   . ARG   A 1  231 ? 25.457  -2.532  -12.972 1    18.785  ? 231  ARG   A N   1 1 
ATOM   1839  C  CA  . ARG   A 1  231 ? 26.886  -2.277  -13.19  1    20.289  ? 231  ARG   A CA  1 1 
ATOM   1840  C  C   . ARG   A 1  231 ? 27.274  -2.426  -14.676 1    20.638  ? 231  ARG   A C   1 1 
ATOM   1841  O  O   . ARG   A 1  231 ? 28.015  -1.616  -15.235 1    21.106  ? 231  ARG   A O   1 1 
ATOM   1842  C  CB  . ARG   A 1  231 ? 27.673  -3.218  -12.256 1    21.146  ? 231  ARG   A CB  1 1 
ATOM   1843  C  CG  . ARG   A 1  231 ? 29.183  -3.164  -12.49  1    24.805  ? 231  ARG   A CG  1 1 
ATOM   1844  C  CD  . ARG   A 1  231 ? 29.745  -1.764  -12.258 1    28.497  ? 231  ARG   A CD  1 1 
ATOM   1845  N  NE  . ARG   A 1  231 ? 29.604  -1.42   -10.841 1    31.338  ? 231  ARG   A NE  1 1 
ATOM   1846  C  CZ  . ARG   A 1  231 ? 30.176  -0.368  -10.227 1    35.67   ? 231  ARG   A CZ  1 1 
ATOM   1847  N  NH1 . ARG   A 1  231 ? 30.953  0.463   -10.896 1    35.493  ? 231  ARG   A NH1 1 1 
ATOM   1848  N  NH2 . ARG   A 1  231 ? 29.958  -0.167  -8.923  1    34.985  ? 231  ARG   A NH2 1 1 
ATOM   1849  N  N   . ALA   A 1  232 ? 26.798  -3.518  -15.312 1    21.074  ? 232  ALA   A N   1 1 
ATOM   1850  C  CA  . ALA   A 1  232 ? 27.04   -3.777  -16.73  1    20.685  ? 232  ALA   A CA  1 1 
ATOM   1851  C  C   . ALA   A 1  232 ? 26.445  -2.634  -17.552 1    20.569  ? 232  ALA   A C   1 1 
ATOM   1852  O  O   . ALA   A 1  232 ? 27.101  -2.107  -18.427 1    21.243  ? 232  ALA   A O   1 1 
ATOM   1853  C  CB  . ALA   A 1  232 ? 26.417  -5.106  -17.106 1    19.662  ? 232  ALA   A CB  1 1 
ATOM   1854  N  N   . LEU   A 1  233 ? 25.236  -2.164  -17.226 1    19.072  ? 233  LEU   A N   1 1 
ATOM   1855  C  CA  . LEU   A 1  233 ? 24.673  -1.063  -18.001 1    19.907  ? 233  LEU   A CA  1 1 
ATOM   1856  C  C   . LEU   A 1  233 ? 25.433  0.245   -17.809 1    20.86   ? 233  LEU   A C   1 1 
ATOM   1857  O  O   . LEU   A 1  233 ? 25.549  1.063   -18.732 1    20.945  ? 233  LEU   A O   1 1 
ATOM   1858  C  CB  . LEU   A 1  233 ? 23.224  -0.853  -17.577 1    18.382  ? 233  LEU   A CB  1 1 
ATOM   1859  C  CG  . LEU   A 1  233 ? 22.314  -2.026  -17.96  1    18.273  ? 233  LEU   A CG  1 1 
ATOM   1860  C  CD1 . LEU   A 1  233 ? 20.932  -1.847  -17.259 1    17.372  ? 233  LEU   A CD1 1 1 
ATOM   1861  C  CD2 . LEU   A 1  233 ? 22.205  -2.135  -19.51  1    19.233  ? 233  LEU   A CD2 1 1 
ATOM   1862  N  N   . HIS   A 1  234 ? 25.923  0.467   -16.583 1    21.436  ? 234  HIS   A N   1 1 
ATOM   1863  C  CA  . HIS   A 1  234 ? 26.695  1.677   -16.297 1    23.389  ? 234  HIS   A CA  1 1 
ATOM   1864  C  C   . HIS   A 1  234 ? 27.954  1.695   -17.168 1    24.719  ? 234  HIS   A C   1 1 
ATOM   1865  O  O   . HIS   A 1  234 ? 28.327  2.74    -17.689 1    24.307  ? 234  HIS   A O   1 1 
ATOM   1866  C  CB  . HIS   A 1  234 ? 26.941  1.782   -14.782 1    23.624  ? 234  HIS   A CB  1 1 
ATOM   1867  C  CG  . HIS   A 1  234 ? 27.723  2.961   -14.364 1    27.129  ? 234  HIS   A CG  1 1 
ATOM   1868  N  ND1 . HIS   A 1  234 ? 29.093  2.877   -14.249 1    28.38   ? 234  HIS   A ND1 1 1 
ATOM   1869  C  CD2 . HIS   A 1  234 ? 27.377  4.217   -14.057 1    27.529  ? 234  HIS   A CD2 1 1 
ATOM   1870  C  CE1 . HIS   A 1  234 ? 29.549  4.056   -13.877 1    30.567  ? 234  HIS   A CE1 1 1 
ATOM   1871  N  NE2 . HIS   A 1  234 ? 28.519  4.885   -13.759 1    29.733  ? 234  HIS   A NE2 1 1 
ATOM   1872  N  N   . ARG   A 1  235 ? 28.603  0.531   -17.314 1    26.087  ? 235  ARG   A N   1 1 
ATOM   1873  C  CA  . ARG   A 1  235 ? 29.839  0.496   -18.089 1    29.522  ? 235  ARG   A CA  1 1 
ATOM   1874  C  C   . ARG   A 1  235 ? 29.559  0.799   -19.561 1    28.972  ? 235  ARG   A C   1 1 
ATOM   1875  O  O   . ARG   A 1  235 ? 30.465  1.216   -20.259 1    30.395  ? 235  ARG   A O   1 1 
ATOM   1876  C  CB  . ARG   A 1  235 ? 30.676  -0.791  -18.134 1    32.693  ? 235  ARG   A CB  1 1 
ATOM   1877  C  CG  . ARG   A 1  235 ? 31.132  -1.455  -16.843 1    39.984  ? 235  ARG   A CG  1 1 
ATOM   1878  C  CD  . ARG   A 1  235 ? 31.799  -2.843  -17.084 1    47.296  ? 235  ARG   A CD  1 1 
ATOM   1879  N  NE  . ARG   A 1  235 ? 31.842  -3.725  -15.902 1    62.483  ? 235  ARG   A NE  1 1 
ATOM   1880  C  CZ  . ARG   A 1  235 ? 32.365  -3.518  -14.66  1    68.294  ? 235  ARG   A CZ  1 1 
ATOM   1881  N  NH1 . ARG   A 1  235 ? 32.308  -4.469  -13.726 1    65.71   ? 235  ARG   A NH1 1 1 
ATOM   1882  N  NH2 . ARG   A 1  235 ? 32.94   -2.369  -14.337 1    70.32   ? 235  ARG   A NH2 1 1 
ATOM   1883  N  N   . ARG   A 1  236 ? 28.326  0.602   -20.033 1    28.786  ? 236  ARG   A N   1 1 
ATOM   1884  C  CA  . ARG   A 1  236 ? 27.978  0.854   -21.427 1    29.951  ? 236  ARG   A CA  1 1 
ATOM   1885  C  C   . ARG   A 1  236 ? 27.322  2.215   -21.614 1    30.161  ? 236  ARG   A C   1 1 
ATOM   1886  O  O   . ARG   A 1  236 ? 27.61   2.869   -22.605 1    30.379  ? 236  ARG   A O   1 1 
ATOM   1887  C  CB  . ARG   A 1  236 ? 27.005  -0.174  -22.01  1    32.012  ? 236  ARG   A CB  1 1 
ATOM   1888  C  CG  . ARG   A 1  236 ? 27.734  -1.429  -21.561 1    39.287  ? 236  ARG   A CG  1 1 
ATOM   1889  C  CD  . ARG   A 1  236 ? 28.031  -2.404  -22.696 1    50.349  ? 236  ARG   A CD  1 1 
ATOM   1890  N  NE  . ARG   A 1  236 ? 28.952  -3.531  -22.474 1    54.79   ? 236  ARG   A NE  1 1 
ATOM   1891  C  CZ  . ARG   A 1  236 ? 29.202  -4.286  -21.403 1    58.823  ? 236  ARG   A CZ  1 1 
ATOM   1892  N  NH1 . ARG   A 1  236 ? 28.738  -3.971  -20.187 1    45.983  ? 236  ARG   A NH1 1 1 
ATOM   1893  N  NH2 . ARG   A 1  236 ? 30.011  -5.329  -21.575 1    59.213  ? 236  ARG   A NH2 1 1 
ATOM   1894  N  N   . TYR   A 1  237 ? 26.417  2.607   -20.695 1    27.592  ? 237  TYR   A N   1 1 
ATOM   1895  C  CA  . TYR   A 1  237 ? 25.643  3.818   -20.887 1    28.263  ? 237  TYR   A CA  1 1 
ATOM   1896  C  C   . TYR   A 1  237 ? 26.267  5       -20.169 1    29.522  ? 237  TYR   A C   1 1 
ATOM   1897  O  O   . TYR   A 1  237 ? 25.931  6.113   -20.521 1    32.437  ? 237  TYR   A O   1 1 
ATOM   1898  C  CB  . TYR   A 1  237 ? 24.18   3.627   -20.479 1    25.806  ? 237  TYR   A CB  1 1 
ATOM   1899  C  CG  . TYR   A 1  237 ? 23.481  2.693   -21.456 1    26.493  ? 237  TYR   A CG  1 1 
ATOM   1900  C  CD1 . TYR   A 1  237 ? 23.119  3.159   -22.722 1    28.683  ? 237  TYR   A CD1 1 1 
ATOM   1901  C  CD2 . TYR   A 1  237 ? 23.248  1.362   -21.152 1    25.276  ? 237  TYR   A CD2 1 1 
ATOM   1902  C  CE1 . TYR   A 1  237 ? 22.448  2.355   -23.626 1    29.698  ? 237  TYR   A CE1 1 1 
ATOM   1903  C  CE2 . TYR   A 1  237 ? 22.575  0.543   -22.057 1    26.353  ? 237  TYR   A CE2 1 1 
ATOM   1904  C  CZ  . TYR   A 1  237 ? 22.209  1.023   -23.31  1    28.913  ? 237  TYR   A CZ  1 1 
ATOM   1905  O  OH  . TYR   A 1  237 ? 21.511  0.235   -24.2   1    30.079  ? 237  TYR   A OH  1 1 
ATOM   1906  N  N   . GLY   A 1  238 ? 27.119  4.775   -19.161 1    29.268  ? 238  GLY   A N   1 1 
ATOM   1907  C  CA  . GLY   A 1  238 ? 27.766  5.88    -18.492 1    30.454  ? 238  GLY   A CA  1 1 
ATOM   1908  C  C   . GLY   A 1  238 ? 26.95   6.415   -17.316 1    31.422  ? 238  GLY   A C   1 1 
ATOM   1909  O  O   . GLY   A 1  238 ? 25.777  6.123   -17.15  1    28.332  ? 238  GLY   A O   1 1 
ATOM   1910  N  N   . ASP   A 1  239 ? 27.591  7.289   -16.545 1    34.176  ? 239  ASP   A N   1 1 
ATOM   1911  C  CA  . ASP   A 1  239 ? 27.135  7.823   -15.28  1    37.297  ? 239  ASP   A CA  1 1 
ATOM   1912  C  C   . ASP   A 1  239 ? 25.961  8.785   -15.455 1    37.799  ? 239  ASP   A C   1 1 
ATOM   1913  O  O   . ASP   A 1  239 ? 25.139  8.971   -14.55  1    38.304  ? 239  ASP   A O   1 1 
ATOM   1914  C  CB  . ASP   A 1  239 ? 28.304  8.489   -14.564 1    44.818  ? 239  ASP   A CB  1 1 
ATOM   1915  C  CG  . ASP   A 1  239 ? 28.074  8.615   -13.068 1    57.773  ? 239  ASP   A CG  1 1 
ATOM   1916  O  OD1 . ASP   A 1  239 ? 28.023  7.541   -12.404 1    57.628  ? 239  ASP   A OD1 1 1 
ATOM   1917  O  OD2 . ASP   A 1  239 ? 27.904  9.772   -12.583 1    61.651  ? 239  ASP   A OD2 1 1 
ATOM   1918  N  N   . ARG   A 1  240 ? 25.857  9.401   -16.625 1    35.341  ? 240  ARG   A N   1 1 
ATOM   1919  C  CA  . ARG   A 1  240 ? 24.733  10.29   -16.819 1    35.182  ? 240  ARG   A CA  1 1 
ATOM   1920  C  C   . ARG   A 1  240 ? 23.405  9.531   -16.888 1    32.919  ? 240  ARG   A C   1 1 
ATOM   1921  O  O   . ARG   A 1  240 ? 22.405  10.024  -16.382 1    31.739  ? 240  ARG   A O   1 1 
ATOM   1922  C  CB  . ARG   A 1  240 ? 25.108  11.169  -18.007 1    40.698  ? 240  ARG   A CB  1 1 
ATOM   1923  C  CG  . ARG   A 1  240 ? 23.969  11.91   -18.681 1    43.795  ? 240  ARG   A CG  1 1 
ATOM   1924  C  CD  . ARG   A 1  240 ? 24.539  12.98   -19.611 1    49.4    ? 240  ARG   A CD  1 1 
ATOM   1925  N  NE  . ARG   A 1  240 ? 23.471  13.563  -20.437 1    55.717  ? 240  ARG   A NE  1 1 
ATOM   1926  C  CZ  . ARG   A 1  240 ? 22.547  14.49   -20.107 1    58.469  ? 240  ARG   A CZ  1 1 
ATOM   1927  N  NH1 . ARG   A 1  240 ? 22.601  15.145  -18.942 1    53.098  ? 240  ARG   A NH1 1 1 
ATOM   1928  N  NH2 . ARG   A 1  240 ? 21.586  14.773  -20.991 1    53.955  ? 240  ARG   A NH2 1 1 
ATOM   1929  N  N   . TYR   A 1  241 ? 23.372  8.316   -17.449 1    29.106  ? 241  TYR   A N   1 1 
ATOM   1930  C  CA  . TYR   A 1  241 ? 22.089  7.657   -17.655 1    28.211  ? 241  TYR   A CA  1 1 
ATOM   1931  C  C   . TYR   A 1  241 ? 21.843  6.506   -16.677 1    24.763  ? 241  TYR   A C   1 1 
ATOM   1932  O  O   . TYR   A 1  241 ? 20.747  5.982   -16.65  1    22.418  ? 241  TYR   A O   1 1 
ATOM   1933  C  CB  . TYR   A 1  241 ? 22.073  7.147   -19.108 1    30.45   ? 241  TYR   A CB  1 1 
ATOM   1934  C  CG  . TYR   A 1  241 ? 21.915  8.271   -20.121 1    32.256  ? 241  TYR   A CG  1 1 
ATOM   1935  C  CD1 . TYR   A 1  241 ? 20.858  9.185   -19.999 1    34.42   ? 241  TYR   A CD1 1 1 
ATOM   1936  C  CD2 . TYR   A 1  241 ? 22.843  8.473   -21.145 1    35.029  ? 241  TYR   A CD2 1 1 
ATOM   1937  C  CE1 . TYR   A 1  241 ? 20.699  10.23   -20.899 1    37.818  ? 241  TYR   A CE1 1 1 
ATOM   1938  C  CE2 . TYR   A 1  241 ? 22.687  9.505   -22.054 1    38.656  ? 241  TYR   A CE2 1 1 
ATOM   1939  C  CZ  . TYR   A 1  241 ? 21.621  10.385  -21.932 1    45.196  ? 241  TYR   A CZ  1 1 
ATOM   1940  O  OH  . TYR   A 1  241 ? 21.497  11.422  -22.833 1    52.607  ? 241  TYR   A OH  1 1 
ATOM   1941  N  N   . ILE   A 1  242 ? 22.887  6.026   -15.99  1    23.239  ? 242  ILE   A N   1 1 
ATOM   1942  C  CA  . ILE   A 1  242 ? 22.794  4.954   -15.008 1    22.448  ? 242  ILE   A CA  1 1 
ATOM   1943  C  C   . ILE   A 1  242 ? 23.357  5.481   -13.701 1    22.257  ? 242  ILE   A C   1 1 
ATOM   1944  O  O   . ILE   A 1  242 ? 24.461  6.025   -13.673 1    23.491  ? 242  ILE   A O   1 1 
ATOM   1945  C  CB  . ILE   A 1  242 ? 23.583  3.686   -15.425 1    23.085  ? 242  ILE   A CB  1 1 
ATOM   1946  C  CG1 . ILE   A 1  242 ? 23.104  3.126   -16.781 1    22.592  ? 242  ILE   A CG1 1 1 
ATOM   1947  C  CG2 . ILE   A 1  242 ? 23.475  2.635   -14.325 1    21.677  ? 242  ILE   A CG2 1 1 
ATOM   1948  C  CD1 . ILE   A 1  242 ? 21.778  2.392   -16.684 1    22.304  ? 242  ILE   A CD1 1 1 
ATOM   1949  N  N   . ASN   A 1  243 ? 22.578  5.299   -12.645 1    21.55   ? 243  ASN   A N   1 1 
ATOM   1950  C  CA  . ASN   A 1  243 ? 22.88   5.662   -11.264 1    21.364  ? 243  ASN   A CA  1 1 
ATOM   1951  C  C   . ASN   A 1  243 ? 23.094  4.349   -10.505 1    20.39   ? 243  ASN   A C   1 1 
ATOM   1952  O  O   . ASN   A 1  243 ? 22.155  3.558   -10.314 1    19.129  ? 243  ASN   A O   1 1 
ATOM   1953  C  CB  . ASN   A 1  243 ? 21.76   6.547   -10.714 1    22.211  ? 243  ASN   A CB  1 1 
ATOM   1954  C  CG  . ASN   A 1  243 ? 21.949  7.019   -9.287  1    22.833  ? 243  ASN   A CG  1 1 
ATOM   1955  O  OD1 . ASN   A 1  243 ? 22.795  6.498   -8.555  1    23.066  ? 243  ASN   A OD1 1 1 
ATOM   1956  N  ND2 . ASN   A 1  243 ? 21.082  7.934   -8.857  1    23.182  ? 243  ASN   A ND2 1 1 
ATOM   1957  N  N   . LEU   A 1  244 ? 24.35   4.124   -10.095 1    20.639  ? 244  LEU   A N   1 1 
ATOM   1958  C  CA  . LEU   A 1  244 ? 24.738  2.903   -9.416  1    20.904  ? 244  LEU   A CA  1 1 
ATOM   1959  C  C   . LEU   A 1  244 ? 24.039  2.753   -8.062  1    21      ? 244  LEU   A C   1 1 
ATOM   1960  O  O   . LEU   A 1  244 ? 24.128  1.674   -7.475  1    20.087  ? 244  LEU   A O   1 1 
ATOM   1961  C  CB  . LEU   A 1  244 ? 26.261  2.897   -9.239  1    22.279  ? 244  LEU   A CB  1 1 
ATOM   1962  C  CG  . LEU   A 1  244 ? 27.035  2.758   -10.559 1    23.176  ? 244  LEU   A CG  1 1 
ATOM   1963  C  CD1 . LEU   A 1  244 ? 28.578  2.917   -10.356 1    24.618  ? 244  LEU   A CD1 1 1 
ATOM   1964  C  CD2 . LEU   A 1  244 ? 26.701  1.414   -11.119 1    22.135  ? 244  LEU   A CD2 1 1 
ATOM   1965  N  N   . ARG   A 1  245 ? 23.322  3.784   -7.602  1    21.631  ? 245  ARG   A N   1 1 
ATOM   1966  C  CA  . ARG   A 1  245 ? 22.576  3.65    -6.346  1    22.308  ? 245  ARG   A CA  1 1 
ATOM   1967  C  C   . ARG   A 1  245 ? 21.078  3.908   -6.52   1    21.745  ? 245  ARG   A C   1 1 
ATOM   1968  O  O   . ARG   A 1  245 ? 20.346  3.973   -5.517  1    20.795  ? 245  ARG   A O   1 1 
ATOM   1969  C  CB  . ARG   A 1  245 ? 23.125  4.528   -5.207  1    25.065  ? 245  ARG   A CB  1 1 
ATOM   1970  C  CG  . ARG   A 1  245 ? 24.553  4.122   -4.842  1    29.051  ? 245  ARG   A CG  1 1 
ATOM   1971  C  CD  . ARG   A 1  245 ? 25.18   4.874   -3.691  1    33.52   ? 245  ARG   A CD  1 1 
ATOM   1972  N  NE  . ARG   A 1  245 ? 25.261  6.297   -4.042  1    42.529  ? 245  ARG   A NE  1 1 
ATOM   1973  C  CZ  . ARG   A 1  245 ? 25.907  7.256   -3.36   1    49.223  ? 245  ARG   A CZ  1 1 
ATOM   1974  N  NH1 . ARG   A 1  245 ? 26.797  6.945   -2.417  1    50.929  ? 245  ARG   A NH1 1 1 
ATOM   1975  N  NH2 . ARG   A 1  245 ? 25.682  8.53    -3.652  1    47.708  ? 245  ARG   A NH2 1 1 
ATOM   1976  N  N   . GLY   A 1  246 ? 20.626  3.995   -7.783  1    21.113  ? 246  GLY   A N   1 1 
ATOM   1977  C  CA  . GLY   A 1  246 ? 19.252  4.355   -8.1    1    19.031  ? 246  GLY   A CA  1 1 
ATOM   1978  C  C   . GLY   A 1  246 ? 18.604  3.262   -8.958  1    19.098  ? 246  GLY   A C   1 1 
ATOM   1979  O  O   . GLY   A 1  246 ? 19.227  2.264   -9.293  1    18.177  ? 246  GLY   A O   1 1 
ATOM   1980  N  N   . PRO   A 1  247 ? 17.294  3.397   -9.292  1    17.226  ? 247  PRO   A N   1 1 
ATOM   1981  C  CA  . PRO   A 1  247 ? 16.587  2.436   -10.13  1    17.084  ? 247  PRO   A CA  1 1 
ATOM   1982  C  C   . PRO   A 1  247 ? 17.133  2.473   -11.559 1    16.908  ? 247  PRO   A C   1 1 
ATOM   1983  O  O   . PRO   A 1  247 ? 17.71   3.469   -11.977 1    17.589  ? 247  PRO   A O   1 1 
ATOM   1984  C  CB  . PRO   A 1  247 ? 15.093  2.862   -10.1   1    16.362  ? 247  PRO   A CB  1 1 
ATOM   1985  C  CG  . PRO   A 1  247 ? 15.074  3.873   -8.947  1    17.248  ? 247  PRO   A CG  1 1 
ATOM   1986  C  CD  . PRO   A 1  247 ? 16.458  4.552   -8.917  1    17.633  ? 247  PRO   A CD  1 1 
ATOM   1987  N  N   . ILE   A 1  248 ? 17.007  1.343   -12.263 1    16.038  ? 248  ILE   A N   1 1 
ATOM   1988  C  CA  . ILE   A 1  248 ? 17.475  1.287   -13.641 1    15.624  ? 248  ILE   A CA  1 1 
ATOM   1989  C  C   . ILE   A 1  248 ? 16.407  1.92    -14.516 1    15.941  ? 248  ILE   A C   1 1 
ATOM   1990  O  O   . ILE   A 1  248 ? 15.246  1.571   -14.329 1    15.056  ? 248  ILE   A O   1 1 
ATOM   1991  C  CB  . ILE   A 1  248 ? 17.688  -0.19   -14.038 1    15.321  ? 248  ILE   A CB  1 1 
ATOM   1992  C  CG1 . ILE   A 1  248 ? 18.779  -0.806  -13.129 1    15.851  ? 248  ILE   A CG1 1 1 
ATOM   1993  C  CG2 . ILE   A 1  248 ? 18.139  -0.251  -15.499 1    16.307  ? 248  ILE   A CG2 1 1 
ATOM   1994  C  CD1 . ILE   A 1  248 ? 18.953  -2.322  -13.301 1    16.188  ? 248  ILE   A CD1 1 1 
ATOM   1995  N  N   . PRO   A 1  249 ? 16.756  2.769   -15.522 1    16.313  ? 249  PRO   A N   1 1 
ATOM   1996  C  CA  . PRO   A 1  249 ? 15.768  3.231   -16.504 1    17.283  ? 249  PRO   A CA  1 1 
ATOM   1997  C  C   . PRO   A 1  249 ? 15.061  2.057   -17.192 1    17.376  ? 249  PRO   A C   1 1 
ATOM   1998  O  O   . PRO   A 1  249 ? 15.704  1.091   -17.586 1    18.176  ? 249  PRO   A O   1 1 
ATOM   1999  C  CB  . PRO   A 1  249 ? 16.604  4.089   -17.491 1    18.217  ? 249  PRO   A CB  1 1 
ATOM   2000  C  CG  . PRO   A 1  249 ? 17.755  4.552   -16.628 1    17.762  ? 249  PRO   A CG  1 1 
ATOM   2001  C  CD  . PRO   A 1  249 ? 18.098  3.351   -15.731 1    16.894  ? 249  PRO   A CD  1 1 
ATOM   2002  N  N   . ALA   A 1  250 ? 13.733  2.172   -17.373 1    16.134  ? 250  ALA   A N   1 1 
ATOM   2003  C  CA  . ALA   A 1  250 ? 12.92   0.992   -17.588 1    16.689  ? 250  ALA   A CA  1 1 
ATOM   2004  C  C   . ALA   A 1  250 ? 13.012  0.536   -19.051 1    17.832  ? 250  ALA   A C   1 1 
ATOM   2005  O  O   . ALA   A 1  250 ? 12.449  -0.5    -19.361 1    18.048  ? 250  ALA   A O   1 1 
ATOM   2006  C  CB  . ALA   A 1  250 ? 11.46   1.309   -17.186 1    17.486  ? 250  ALA   A CB  1 1 
ATOM   2007  N  N   . HIS   A 1  251 ? 13.732  1.267   -19.935 1    17.072  ? 251  HIS   A N   1 1 
ATOM   2008  C  CA  . HIS   A 1  251 ? 13.783  0.894   -21.341 1    18.666  ? 251  HIS   A CA  1 1 
ATOM   2009  C  C   . HIS   A 1  251 ? 15.146  0.26    -21.732 1    19.441  ? 251  HIS   A C   1 1 
ATOM   2010  O  O   . HIS   A 1  251 ? 15.364  -0.074  -22.89  1    18.528  ? 251  HIS   A O   1 1 
ATOM   2011  C  CB  . HIS   A 1  251 ? 13.541  2.15    -22.184 1    18.945  ? 251  HIS   A CB  1 1 
ATOM   2012  C  CG  . HIS   A 1  251 ? 14.652  3.151   -22.044 1    21.508  ? 251  HIS   A CG  1 1 
ATOM   2013  N  ND1 . HIS   A 1  251 ? 15.146  3.565   -20.821 1    21.638  ? 251  HIS   A ND1 1 1 
ATOM   2014  C  CD2 . HIS   A 1  251 ? 15.343  3.853   -22.976 1    23.002  ? 251  HIS   A CD2 1 1 
ATOM   2015  C  CE1 . HIS   A 1  251 ? 16.038  4.509   -20.996 1    23.069  ? 251  HIS   A CE1 1 1 
ATOM   2016  N  NE2 . HIS   A 1  251 ? 16.183  4.71    -22.294 1    24.083  ? 251  HIS   A NE2 1 1 
ATOM   2017  N  N   . LEU   A 1  252 ? 15.982  -0.063  -20.739 1    17.567  ? 252  LEU   A N   1 1 
ATOM   2018  C  CA  . LEU   A 1  252 ? 17.323  -0.546  -21.083 1    20.211  ? 252  LEU   A CA  1 1 
ATOM   2019  C  C   . LEU   A 1  252 ? 17.485  -2.048  -20.831 1    19.113  ? 252  LEU   A C   1 1 
ATOM   2020  O  O   . LEU   A 1  252 ? 18.599  -2.547  -20.946 1    21.28   ? 252  LEU   A O   1 1 
ATOM   2021  C  CB  . LEU   A 1  252 ? 18.382  0.234   -20.29  1    19.658  ? 252  LEU   A CB  1 1 
ATOM   2022  C  CG  . LEU   A 1  252 ? 18.363  1.75    -20.441 1    21.364  ? 252  LEU   A CG  1 1 
ATOM   2023  C  CD1 . LEU   A 1  252 ? 19.477  2.395   -19.547 1    23.228  ? 252  LEU   A CD1 1 1 
ATOM   2024  C  CD2 . LEU   A 1  252 ? 18.582  2.044   -21.924 1    23.152  ? 252  LEU   A CD2 1 1 
ATOM   2025  N  N   . LEU   A 1  253 ? 16.402  -2.787  -20.537 1    18.463  ? 253  LEU   A N   1 1 
ATOM   2026  C  CA  . LEU   A 1  253 ? 16.567  -4.155  -20.087 1    17.592  ? 253  LEU   A CA  1 1 
ATOM   2027  C  C   . LEU   A 1  253 ? 16.177  -5.178  -21.159 1    17.76   ? 253  LEU   A C   1 1 
ATOM   2028  O  O   . LEU   A 1  253 ? 16.155  -6.369  -20.847 1    18.963  ? 253  LEU   A O   1 1 
ATOM   2029  C  CB  . LEU   A 1  253 ? 15.905  -4.376  -18.715 1    16.187  ? 253  LEU   A CB  1 1 
ATOM   2030  C  CG  . LEU   A 1  253 ? 16.564  -3.494  -17.639 1    17.031  ? 253  LEU   A CG  1 1 
ATOM   2031  C  CD1 . LEU   A 1  253 ? 15.611  -3.22   -16.498 1    16.989  ? 253  LEU   A CD1 1 1 
ATOM   2032  C  CD2 . LEU   A 1  253 ? 17.824  -4.234  -17.107 1    15.592  ? 253  LEU   A CD2 1 1 
ATOM   2033  N  N   . GLY   A 1  254 ? 15.929  -4.737  -22.408 1    18.386  ? 254  GLY   A N   1 1 
ATOM   2034  C  CA  . GLY   A 1  254 ? 15.802  -5.698  -23.502 1    19.935  ? 254  GLY   A CA  1 1 
ATOM   2035  C  C   . GLY   A 1  254 ? 14.353  -5.985  -23.898 1    23.437  ? 254  GLY   A C   1 1 
ATOM   2036  O  O   . GLY   A 1  254 ? 14.073  -6.757  -24.834 1    26.205  ? 254  GLY   A O   1 1 
ATOM   2037  N  N   . ASP   A 1  255 ? 13.42   -5.441  -23.107 1    22.631  ? 255  ASP   A N   1 1 
ATOM   2038  C  CA  . ASP   A 1  255 ? 12.024  -5.828  -23.215 1    20.719  ? 255  ASP   A CA  1 1 
ATOM   2039  C  C   . ASP   A 1  255 ? 11.176  -4.578  -22.938 1    18.34   ? 255  ASP   A C   1 1 
ATOM   2040  O  O   . ASP   A 1  255 ? 11.502  -3.782  -22.046 1    17.766  ? 255  ASP   A O   1 1 
ATOM   2041  C  CB  . ASP   A 1  255 ? 11.814  -6.897  -22.16  1    24.651  ? 255  ASP   A CB  1 1 
ATOM   2042  C  CG  . ASP   A 1  255 ? 10.412  -7.412  -22     1    25.708  ? 255  ASP   A CG  1 1 
ATOM   2043  O  OD1 . ASP   A 1  255 ? 10.08   -8.394  -22.692 1    34.343  ? 255  ASP   A OD1 1 1 
ATOM   2044  O  OD2 . ASP   A 1  255 ? 9.645   -6.804  -21.216 1    27.793  ? 255  ASP   A OD2 1 1 
ATOM   2045  N  N   . MET   A 1  256 ? 10.03   -4.443  -23.619 1    17.051  ? 256  MET   A N   1 1 
ATOM   2046  C  CA  . MET   A 1  256 ? 9.168   -3.258  -23.406 1    17.036  ? 256  MET   A CA  1 1 
ATOM   2047  C  C   . MET   A 1  256 ? 8.729   -3.081  -21.926 1    16.287  ? 256  MET   A C   1 1 
ATOM   2048  O  O   . MET   A 1  256 ? 8.485   -1.955  -21.458 1    16.818  ? 256  MET   A O   1 1 
ATOM   2049  C  CB  . MET   A 1  256 ? 7.915   -3.376  -24.296 1    17.695  ? 256  MET   A CB  1 1 
ATOM   2050  C  CG  . MET   A 1  256 ? 7.012   -2.068  -24.328 1    16.799  ? 256  MET   A CG  1 1 
ATOM   2051  S  SD  . MET   A 1  256 ? 7.855   -0.563  -24.857 1    19.537  ? 256  MET   A SD  1 1 
ATOM   2052  C  CE  . MET   A 1  256 ? 7.845   -0.935  -26.618 1    16.518  ? 256  MET   A CE  1 1 
ATOM   2053  N  N   . TRP   A 1  257 ? 8.536   -4.182  -21.196 1    14.944  ? 257  TRP   A N   1 1 
ATOM   2054  C  CA  . TRP   A 1  257 ? 8.098   -4.116  -19.81  1    15.059  ? 257  TRP   A CA  1 1 
ATOM   2055  C  C   . TRP   A 1  257 ? 9.199   -4.315  -18.771 1    15.495  ? 257  TRP   A C   1 1 
ATOM   2056  O  O   . TRP   A 1  257 ? 8.889   -4.373  -17.575 1    14.368  ? 257  TRP   A O   1 1 
ATOM   2057  C  CB  . TRP   A 1  257 ? 6.884   -5.005  -19.541 1    14.288  ? 257  TRP   A CB  1 1 
ATOM   2058  C  CG  . TRP   A 1  257 ? 5.866   -4.676  -20.593 1    15.733  ? 257  TRP   A CG  1 1 
ATOM   2059  C  CD1 . TRP   A 1  257 ? 4.975   -3.64   -20.546 1    17.582  ? 257  TRP   A CD1 1 1 
ATOM   2060  C  CD2 . TRP   A 1  257 ? 5.721   -5.291  -21.902 1    16.329  ? 257  TRP   A CD2 1 1 
ATOM   2061  N  NE1 . TRP   A 1  257 ? 4.258   -3.61   -21.712 1    17.179  ? 257  TRP   A NE1 1 1 
ATOM   2062  C  CE2 . TRP   A 1  257 ? 4.686   -4.592  -22.563 1    16.978  ? 257  TRP   A CE2 1 1 
ATOM   2063  C  CE3 . TRP   A 1  257 ? 6.354   -6.346  -22.58  1    18.918  ? 257  TRP   A CE3 1 1 
ATOM   2064  C  CZ2 . TRP   A 1  257 ? 4.298   -4.9    -23.868 1    18.4    ? 257  TRP   A CZ2 1 1 
ATOM   2065  C  CZ3 . TRP   A 1  257 ? 5.975   -6.663  -23.877 1    18.474  ? 257  TRP   A CZ3 1 1 
ATOM   2066  C  CH2 . TRP   A 1  257 ? 5.002   -5.901  -24.526 1    19.209  ? 257  TRP   A CH2 1 1 
ATOM   2067  N  N   . ALA   A 1  258 ? 10.439  -4.461  -19.233 1    15.28   ? 258  ALA   A N   1 1 
ATOM   2068  C  CA  . ALA   A 1  258 ? 11.562  -4.828  -18.382 1    16.545  ? 258  ALA   A CA  1 1 
ATOM   2069  C  C   . ALA   A 1  258 ? 11.237  -6.143  -17.671 1    17.399  ? 258  ALA   A C   1 1 
ATOM   2070  O  O   . ALA   A 1  258 ? 11.694  -6.365  -16.544 1    16.797  ? 258  ALA   A O   1 1 
ATOM   2071  C  CB  . ALA   A 1  258 ? 11.94   -3.691  -17.399 1    14.662  ? 258  ALA   A CB  1 1 
ATOM   2072  N  N   . GLN   A 1  259 ? 10.48   -7.032  -18.317 1    16.24   ? 259  GLN   A N   1 1 
ATOM   2073  C  CA  . GLN   A 1  259 ? 9.958   -8.147  -17.532 1    16.914  ? 259  GLN   A CA  1 1 
ATOM   2074  C  C   . GLN   A 1  259 ? 10.835  -9.378  -17.689 1    19.086  ? 259  GLN   A C   1 1 
ATOM   2075  O  O   . GLN   A 1  259 ? 10.803  -10.29  -16.874 1    19.73   ? 259  GLN   A O   1 1 
ATOM   2076  C  CB  . GLN   A 1  259 ? 8.547   -8.617  -17.867 1    17.896  ? 259  GLN   A CB  1 1 
ATOM   2077  C  CG  . GLN   A 1  259 ? 8.436   -9.228  -19.249 1    22.229  ? 259  GLN   A CG  1 1 
ATOM   2078  C  CD  . GLN   A 1  259 ? 6.995   -9.48   -19.633 1    26.735  ? 259  GLN   A CD  1 1 
ATOM   2079  O  OE1 . GLN   A 1  259 ? 6.198   -8.536  -19.695 1    25.46   ? 259  GLN   A OE1 1 1 
ATOM   2080  N  NE2 . GLN   A 1  259 ? 6.662   -10.736 -19.926 1    26.551  ? 259  GLN   A NE2 1 1 
ATOM   2081  N  N   . SER   A 1  260 ? 11.57   -9.433  -18.768 1    20.006  ? 260  SER   A N   1 1 
ATOM   2082  C  CA  . SER   A 1  260 ? 12.647  -10.386 -18.649 1    22.823  ? 260  SER   A CA  1 1 
ATOM   2083  C  C   . SER   A 1  260 ? 13.808  -9.852  -19.445 1    20.443  ? 260  SER   A C   1 1 
ATOM   2084  O  O   . SER   A 1  260 ? 13.645  -9.02   -20.346 1    19.509  ? 260  SER   A O   1 1 
ATOM   2085  C  CB  . SER   A 1  260 ? 12.259  -11.762 -19.094 1    32.942  ? 260  SER   A CB  1 1 
ATOM   2086  O  OG  . SER   A 1  260 ? 12.104  -11.686 -20.5   1    33.487  ? 260  SER   A OG  1 1 
ATOM   2087  N  N   . TRP   A 1  261 ? 14.988  -10.219 -18.962 1    17.021  ? 261  TRP   A N   1 1 
ATOM   2088  C  CA  . TRP   A 1  261 ? 16.148  -9.494  -19.41  1    17.956  ? 261  TRP   A CA  1 1 
ATOM   2089  C  C   . TRP   A 1  261 ? 17.034  -10.342 -20.304 1    17.92   ? 261  TRP   A C   1 1 
ATOM   2090  O  O   . TRP   A 1  261 ? 18.159  -9.947  -20.544 1    18.872  ? 261  TRP   A O   1 1 
ATOM   2091  C  CB  . TRP   A 1  261 ? 16.937  -9.023  -18.164 1    16.497  ? 261  TRP   A CB  1 1 
ATOM   2092  C  CG  . TRP   A 1  261 ? 16.176  -8.173  -17.195 1    15.56   ? 261  TRP   A CG  1 1 
ATOM   2093  C  CD1 . TRP   A 1  261 ? 14.876  -7.685  -17.275 1    16.363  ? 261  TRP   A CD1 1 1 
ATOM   2094  C  CD2 . TRP   A 1  261 ? 16.696  -7.724  -15.925 1    15.142  ? 261  TRP   A CD2 1 1 
ATOM   2095  N  NE1 . TRP   A 1  261 ? 14.591  -6.922  -16.172 1    14.573  ? 261  TRP   A NE1 1 1 
ATOM   2096  C  CE2 . TRP   A 1  261 ? 15.697  -6.941  -15.328 1    14.63   ? 261  TRP   A CE2 1 1 
ATOM   2097  C  CE3 . TRP   A 1  261 ? 17.93   -7.906  -15.264 1    14.686  ? 261  TRP   A CE3 1 1 
ATOM   2098  C  CZ2 . TRP   A 1  261 ? 15.876  -6.341  -14.069 1    14.929  ? 261  TRP   A CZ2 1 1 
ATOM   2099  C  CZ3 . TRP   A 1  261 ? 18.092  -7.339  -14.014 1    14.86   ? 261  TRP   A CZ3 1 1 
ATOM   2100  C  CH2 . TRP   A 1  261 ? 17.06   -6.579  -13.409 1    15.268  ? 261  TRP   A CH2 1 1 
ATOM   2101  N  N   . GLU   A 1  262 ? 16.54   -11.478 -20.807 1    20.82   ? 262  GLU   A N   1 1 
ATOM   2102  C  CA  . GLU   A 1  262 ? 17.359  -12.339 -21.668 1    25.743  ? 262  GLU   A CA  1 1 
ATOM   2103  C  C   . GLU   A 1  262 ? 18.081  -11.595 -22.81  1    24.869  ? 262  GLU   A C   1 1 
ATOM   2104  O  O   . GLU   A 1  262 ? 19.2    -11.948 -23.188 1    21.644  ? 262  GLU   A O   1 1 
ATOM   2105  C  CB  . GLU   A 1  262 ? 16.619  -13.582 -22.181 1    32.403  ? 262  GLU   A CB  1 1 
ATOM   2106  C  CG  . GLU   A 1  262 ? 15.243  -13.318 -22.814 1    39.921  ? 262  GLU   A CG  1 1 
ATOM   2107  C  CD  . GLU   A 1  262 ? 14.039  -13.332 -21.834 1    51.889  ? 262  GLU   A CD  1 1 
ATOM   2108  O  OE1 . GLU   A 1  262 ? 14.033  -12.515 -20.847 1    37.846  ? 262  GLU   A OE1 1 1 
ATOM   2109  O  OE2 . GLU   A 1  262 ? 13.06   -14.13  -22.035 1    53.566  ? 262  GLU   A OE2 1 1 
ATOM   2110  N  N   . ASN   A 1  263 ? 17.48   -10.531 -23.378 1    23.253  ? 263  ASN   A N   1 1 
ATOM   2111  C  CA  . ASN   A 1  263 ? 18.062  -9.827  -24.51  1    25.591  ? 263  ASN   A CA  1 1 
ATOM   2112  C  C   . ASN   A 1  263 ? 19.299  -9.004  -24.207 1    24.756  ? 263  ASN   A C   1 1 
ATOM   2113  O  O   . ASN   A 1  263 ? 19.971  -8.544  -25.144 1    26.474  ? 263  ASN   A O   1 1 
ATOM   2114  C  CB  . ASN   A 1  263 ? 17.062  -8.868  -25.162 1    29.547  ? 263  ASN   A CB  1 1 
ATOM   2115  C  CG  . ASN   A 1  263 ? 16.01   -9.668  -25.867 1    28.48   ? 263  ASN   A CG  1 1 
ATOM   2116  O  OD1 . ASN   A 1  263 ? 14.825  -9.605  -25.524 1    38.319  ? 263  ASN   A OD1 1 1 
ATOM   2117  N  ND2 . ASN   A 1  263 ? 16.434  -10.411 -26.871 1    27.856  ? 263  ASN   A ND2 1 1 
ATOM   2118  N  N   . ILE   A 1  264 ? 19.625  -8.766  -22.93  1    20.969  ? 264  ILE   A N   1 1 
ATOM   2119  C  CA  . ILE   A 1  264 ? 20.865  -8.051  -22.726 1    20.773  ? 264  ILE   A CA  1 1 
ATOM   2120  C  C   . ILE   A 1  264 ? 21.933  -9.038  -22.223 1    20.508  ? 264  ILE   A C   1 1 
ATOM   2121  O  O   . ILE   A 1  264 ? 22.97   -8.621  -21.689 1    20.881  ? 264  ILE   A O   1 1 
ATOM   2122  C  CB  . ILE   A 1  264 ? 20.656  -6.87   -21.758 1    21.929  ? 264  ILE   A CB  1 1 
ATOM   2123  C  CG1 . ILE   A 1  264 ? 20.077  -7.363  -20.448 1    22.247  ? 264  ILE   A CG1 1 1 
ATOM   2124  C  CG2 . ILE   A 1  264 ? 19.762  -5.785  -22.356 1    22.764  ? 264  ILE   A CG2 1 1 
ATOM   2125  C  CD1 . ILE   A 1  264 ? 20.568  -6.58   -19.256 1    27.223  ? 264  ILE   A CD1 1 1 
ATOM   2126  N  N   . TYR   A 1  265 ? 21.682  -10.327 -22.412 1    19.506  ? 265  TYR   A N   1 1 
ATOM   2127  C  CA  . TYR   A 1  265 ? 22.674  -11.364 -22.092 1    20.716  ? 265  TYR   A CA  1 1 
ATOM   2128  C  C   . TYR   A 1  265 ? 24.05   -11.002 -22.642 1    22.708  ? 265  TYR   A C   1 1 
ATOM   2129  O  O   . TYR   A 1  265 ? 25.047  -11.051 -21.9   1    21.755  ? 265  TYR   A O   1 1 
ATOM   2130  C  CB  . TYR   A 1  265 ? 22.164  -12.751 -22.475 1    19.394  ? 265  TYR   A CB  1 1 
ATOM   2131  C  CG  . TYR   A 1  265 ? 23.235  -13.837 -22.241 1    20.244  ? 265  TYR   A CG  1 1 
ATOM   2132  C  CD1 . TYR   A 1  265 ? 23.598  -14.201 -20.943 1    19.203  ? 265  TYR   A CD1 1 1 
ATOM   2133  C  CD2 . TYR   A 1  265 ? 23.891  -14.448 -23.32  1    21.005  ? 265  TYR   A CD2 1 1 
ATOM   2134  C  CE1 . TYR   A 1  265 ? 24.482  -15.237 -20.719 1    20.24   ? 265  TYR   A CE1 1 1 
ATOM   2135  C  CE2 . TYR   A 1  265 ? 24.816  -15.47  -23.101 1    21.909  ? 265  TYR   A CE2 1 1 
ATOM   2136  C  CZ  . TYR   A 1  265 ? 25.128  -15.838 -21.786 1    21.152  ? 265  TYR   A CZ  1 1 
ATOM   2137  O  OH  . TYR   A 1  265 ? 26.046  -16.801 -21.475 1    22.055  ? 265  TYR   A OH  1 1 
ATOM   2138  N  N   . ASP   A 1  266 ? 24.13   -10.591 -23.939 1    24.612  ? 266  ASP   A N   1 1 
ATOM   2139  C  CA  . ASP   A 1  266 ? 25.432  -10.33  -24.55  1    30.187  ? 266  ASP   A CA  1 1 
ATOM   2140  C  C   . ASP   A 1  266 ? 26.18   -9.246  -23.799 1    29.195  ? 266  ASP   A C   1 1 
ATOM   2141  O  O   . ASP   A 1  266 ? 27.382  -9.243  -23.822 1    28.072  ? 266  ASP   A O   1 1 
ATOM   2142  C  CB  . ASP   A 1  266 ? 25.406  -10.103 -26.059 1    34.938  ? 266  ASP   A CB  1 1 
ATOM   2143  C  CG  . ASP   A 1  266 ? 24.165  -9.39   -26.612 1    42.04   ? 266  ASP   A CG  1 1 
ATOM   2144  O  OD1 . ASP   A 1  266 ? 23.744  -8.375  -25.998 1    35.426  ? 266  ASP   A OD1 1 1 
ATOM   2145  O  OD2 . ASP   A 1  266 ? 23.621  -9.841  -27.688 1    47.895  ? 266  ASP   A OD2 1 1 
ATOM   2146  N  N   . MET   A 1  267 ? 25.484  -8.348  -23.077 1    27.861  ? 267  MET   A N   1 1 
ATOM   2147  C  CA  . MET   A 1  267 ? 26.204  -7.3    -22.376 1    28.487  ? 267  MET   A CA  1 1 
ATOM   2148  C  C   . MET   A 1  267 ? 26.58   -7.715  -20.965 1    25.737  ? 267  MET   A C   1 1 
ATOM   2149  O  O   . MET   A 1  267 ? 27.353  -7.012  -20.338 1    30.206  ? 267  MET   A O   1 1 
ATOM   2150  C  CB  . MET   A 1  267 ? 25.289  -6.089  -22.125 1    30.949  ? 267  MET   A CB  1 1 
ATOM   2151  C  CG  . MET   A 1  267 ? 25.09   -5.244  -23.36  1    37.314  ? 267  MET   A CG  1 1 
ATOM   2152  S  SD  . MET   A 1  267 ? 24.54   -3.588  -22.876 1    39.574  ? 267  MET   A SD  1 1 
ATOM   2153  C  CE  . MET   A 1  267 ? 22.871  -4.228  -23.079 1    27.777  ? 267  MET   A CE  1 1 
ATOM   2154  N  N   . VAL   A 1  268 ? 26.035  -8.814  -20.442 1    22.695  ? 268  VAL   A N   1 1 
ATOM   2155  C  CA  . VAL   A 1  268 ? 26.307  -9.127  -19.037 1    23.357  ? 268  VAL   A CA  1 1 
ATOM   2156  C  C   . VAL   A 1  268 ? 27.093  -10.45  -18.85  1    24.656  ? 268  VAL   A C   1 1 
ATOM   2157  O  O   . VAL   A 1  268 ? 27.447  -10.791 -17.716 1    24.544  ? 268  VAL   A O   1 1 
ATOM   2158  C  CB  . VAL   A 1  268 ? 25.042  -9.153  -18.174 1    23.297  ? 268  VAL   A CB  1 1 
ATOM   2159  C  CG1 . VAL   A 1  268 ? 24.294  -7.806  -18.145 1    24.969  ? 268  VAL   A CG1 1 1 
ATOM   2160  C  CG2 . VAL   A 1  268 ? 24.083  -10.22  -18.664 1    21.997  ? 268  VAL   A CG2 1 1 
ATOM   2161  N  N   . VAL   A 1  269 ? 27.262  -11.244 -19.917 1    24.877  ? 269  VAL   A N   1 1 
ATOM   2162  C  CA  . VAL   A 1  269 ? 27.781  -12.608 -19.831 1    24.633  ? 269  VAL   A CA  1 1 
ATOM   2163  C  C   . VAL   A 1  269 ? 29.121  -12.58  -19.103 1    25.775  ? 269  VAL   A C   1 1 
ATOM   2164  O  O   . VAL   A 1  269 ? 30.051  -11.938 -19.547 1    26.199  ? 269  VAL   A O   1 1 
ATOM   2165  C  CB  . VAL   A 1  269 ? 27.887  -13.268 -21.223 1    25.33   ? 269  VAL   A CB  1 1 
ATOM   2166  C  CG1 . VAL   A 1  269 ? 28.526  -12.358 -22.251 1    24.913  ? 269  VAL   A CG1 1 1 
ATOM   2167  C  CG2 . VAL   A 1  269 ? 28.614  -14.63  -21.222 1    26.582  ? 269  VAL   A CG2 1 1 
ATOM   2168  N  N   . PRO   A 1  270 ? 29.273  -13.246 -17.938 1    27.016  ? 270  PRO   A N   1 1 
ATOM   2169  C  CA  . PRO   A 1  270 ? 30.553  -13.171 -17.241 1    28.888  ? 270  PRO   A CA  1 1 
ATOM   2170  C  C   . PRO   A 1  270 ? 31.717  -13.825 -17.95  1    27.613  ? 270  PRO   A C   1 1 
ATOM   2171  O  O   . PRO   A 1  270 ? 32.801  -13.295 -17.84  1    32.175  ? 270  PRO   A O   1 1 
ATOM   2172  C  CB  . PRO   A 1  270 ? 30.237  -13.801 -15.908 1    30.132  ? 270  PRO   A CB  1 1 
ATOM   2173  C  CG  . PRO   A 1  270 ? 29.16   -14.723 -16.275 1    29.712  ? 270  PRO   A CG  1 1 
ATOM   2174  C  CD  . PRO   A 1  270 ? 28.212  -13.934 -17.176 1    28.079  ? 270  PRO   A CD  1 1 
ATOM   2175  N  N   . PHE   A 1  271 ? 31.51   -14.92  -18.73  1    25.49   ? 271  PHE   A N   1 1 
ATOM   2176  C  CA  . PHE   A 1  271 ? 32.655  -15.592 -19.354 1    26.665  ? 271  PHE   A CA  1 1 
ATOM   2177  C  C   . PHE   A 1  271 ? 32.481  -15.682 -20.872 1    27.356  ? 271  PHE   A C   1 1 
ATOM   2178  O  O   . PHE   A 1  271 ? 32.182  -16.727 -21.442 1    25.492  ? 271  PHE   A O   1 1 
ATOM   2179  C  CB  . PHE   A 1  271 ? 33.023  -16.939 -18.696 1    26.135  ? 271  PHE   A CB  1 1 
ATOM   2180  C  CG  . PHE   A 1  271 ? 33.202  -16.768 -17.187 1    26.018  ? 271  PHE   A CG  1 1 
ATOM   2181  C  CD1 . PHE   A 1  271 ? 34.394  -16.28  -16.662 1    27.517  ? 271  PHE   A CD1 1 1 
ATOM   2182  C  CD2 . PHE   A 1  271 ? 32.152  -17.058 -16.323 1    24.882  ? 271  PHE   A CD2 1 1 
ATOM   2183  C  CE1 . PHE   A 1  271 ? 34.525  -16.101 -15.29  1    28.687  ? 271  PHE   A CE1 1 1 
ATOM   2184  C  CE2 . PHE   A 1  271 ? 32.291  -16.899 -14.955 1    26.451  ? 271  PHE   A CE2 1 1 
ATOM   2185  C  CZ  . PHE   A 1  271 ? 33.456  -16.4   -14.437 1    25.87   ? 271  PHE   A CZ  1 1 
ATOM   2186  N  N   . PRO   A 1  272 ? 32.681  -14.562 -21.597 1    33.069  ? 272  PRO   A N   1 1 
ATOM   2187  C  CA  . PRO   A 1  272 ? 32.66   -14.582 -23.067 1    37.539  ? 272  PRO   A CA  1 1 
ATOM   2188  C  C   . PRO   A 1  272 ? 33.519  -15.564 -23.879 1    41.144  ? 272  PRO   A C   1 1 
ATOM   2189  O  O   . PRO   A 1  272 ? 33.232  -15.765 -25.051 1    45.906  ? 272  PRO   A O   1 1 
ATOM   2190  C  CB  . PRO   A 1  272 ? 32.967  -13.114 -23.428 1    38.728  ? 272  PRO   A CB  1 1 
ATOM   2191  C  CG  . PRO   A 1  272 ? 33.742  -12.599 -22.207 1    37.129  ? 272  PRO   A CG  1 1 
ATOM   2192  C  CD  . PRO   A 1  272 ? 33.014  -13.237 -21.032 1    33.723  ? 272  PRO   A CD  1 1 
ATOM   2193  N  N   . ASP   A 1  273 ? 34.523  -16.235 -23.299 1    38.675  ? 273  ASP   A N   1 1 
ATOM   2194  C  CA  . ASP   A 1  273 ? 35.315  -17.18  -24.091 1    40.424  ? 273  ASP   A CA  1 1 
ATOM   2195  C  C   . ASP   A 1  273 ? 34.664  -18.572 -24.219 1    36.245  ? 273  ASP   A C   1 1 
ATOM   2196  O  O   . ASP   A 1  273 ? 35.125  -19.459 -24.967 1    35.914  ? 273  ASP   A O   1 1 
ATOM   2197  C  CB  . ASP   A 1  273 ? 36.766  -17.171 -23.62  1    48.182  ? 273  ASP   A CB  1 1 
ATOM   2198  C  CG  . ASP   A 1  273 ? 37.797  -16.821 -24.691 1    61.146  ? 273  ASP   A CG  1 1 
ATOM   2199  O  OD1 . ASP   A 1  273 ? 37.514  -15.902 -25.508 1    64.137  ? 273  ASP   A OD1 1 1 
ATOM   2200  O  OD2 . ASP   A 1  273 ? 38.909  -17.428 -24.678 1    65.251  ? 273  ASP   A OD2 1 1 
ATOM   2201  N  N   . LYS   A 1  274 ? 33.564  -18.766 -23.498 1    33.238  ? 274  LYS   A N   1 1 
ATOM   2202  C  CA  . LYS   A 1  274 ? 32.875  -20.04  -23.433 1    34.003  ? 274  LYS   A CA  1 1 
ATOM   2203  C  C   . LYS   A 1  274 ? 31.826  -20.078 -24.547 1    36.216  ? 274  LYS   A C   1 1 
ATOM   2204  O  O   . LYS   A 1  274 ? 31.572  -19.07  -25.199 1    37.301  ? 274  LYS   A O   1 1 
ATOM   2205  C  CB  . LYS   A 1  274 ? 32.36   -20.234 -21.999 1    30.014  ? 274  LYS   A CB  1 1 
ATOM   2206  C  CG  . LYS   A 1  274 ? 33.439  -20.362 -20.923 1    33.819  ? 274  LYS   A CG  1 1 
ATOM   2207  C  CD  . LYS   A 1  274 ? 34.485  -21.44  -21.264 1    34.315  ? 274  LYS   A CD  1 1 
ATOM   2208  C  CE  . LYS   A 1  274 ? 35.333  -21.909 -20.139 1    38.16   ? 274  LYS   A CE  1 1 
ATOM   2209  N  NZ  . LYS   A 1  274 ? 36.406  -22.782 -20.634 1    39.872  ? 274  LYS   A NZ  1 1 
ATOM   2210  N  N   . PRO   A 1  275 ? 31.163  -21.23  -24.793 1    37.605  ? 275  PRO   A N   1 1 
ATOM   2211  C  CA  . PRO   A 1  275 ? 30.218  -21.344 -25.921 1    35.351  ? 275  PRO   A CA  1 1 
ATOM   2212  C  C   . PRO   A 1  275 ? 29.173  -20.239 -25.771 1    31.078  ? 275  PRO   A C   1 1 
ATOM   2213  O  O   . PRO   A 1  275 ? 28.771  -19.95  -24.667 1    26.513  ? 275  PRO   A O   1 1 
ATOM   2214  C  CB  . PRO   A 1  275 ? 29.585  -22.754 -25.635 1    35.028  ? 275  PRO   A CB  1 1 
ATOM   2215  C  CG  . PRO   A 1  275 ? 30.717  -23.494 -24.911 1    40.031  ? 275  PRO   A CG  1 1 
ATOM   2216  C  CD  . PRO   A 1  275 ? 31.199  -22.438 -23.939 1    36.985  ? 275  PRO   A CD  1 1 
ATOM   2217  N  N   . ASN   A 1  276 ? 28.738  -19.664 -26.895 1    33.081  ? 276  ASN   A N   1 1 
ATOM   2218  C  CA  . ASN   A 1  276 ? 27.711  -18.641 -26.915 1    31.259  ? 276  ASN   A CA  1 1 
ATOM   2219  C  C   . ASN   A 1  276 ? 26.337  -19.309 -26.768 1    29.353  ? 276  ASN   A C   1 1 
ATOM   2220  O  O   . ASN   A 1  276 ? 25.879  -20.011 -27.665 1    30.096  ? 276  ASN   A O   1 1 
ATOM   2221  C  CB  . ASN   A 1  276 ? 27.887  -17.811 -28.186 1    35.486  ? 276  ASN   A CB  1 1 
ATOM   2222  C  CG  . ASN   A 1  276 ? 26.788  -16.773 -28.294 1    34.206  ? 276  ASN   A CG  1 1 
ATOM   2223  O  OD1 . ASN   A 1  276 ? 26.032  -16.522 -27.338 1    37.585  ? 276  ASN   A OD1 1 1 
ATOM   2224  N  ND2 . ASN   A 1  276 ? 26.682  -16.149 -29.452 1    37.376  ? 276  ASN   A ND2 1 1 
ATOM   2225  N  N   . LEU   A 1  277 ? 25.653  -19.073 -25.643 1    26.709  ? 277  LEU   A N   1 1 
ATOM   2226  C  CA  . LEU   A 1  277 ? 24.412  -19.763 -25.292 1    28.012  ? 277  LEU   A CA  1 1 
ATOM   2227  C  C   . LEU   A 1  277 ? 23.168  -19.097 -25.872 1    29.455  ? 277  LEU   A C   1 1 
ATOM   2228  O  O   . LEU   A 1  277 ? 22.043  -19.587 -25.657 1    28.415  ? 277  LEU   A O   1 1 
ATOM   2229  C  CB  . LEU   A 1  277 ? 24.275  -19.784 -23.778 1    25.614  ? 277  LEU   A CB  1 1 
ATOM   2230  C  CG  . LEU   A 1  277 ? 25.329  -20.637 -23.075 1    27.65   ? 277  LEU   A CG  1 1 
ATOM   2231  C  CD1 . LEU   A 1  277 ? 25.013  -20.566 -21.603 1    26.252  ? 277  LEU   A CD1 1 1 
ATOM   2232  C  CD2 . LEU   A 1  277 ? 25.195  -22.089 -23.607 1    28.966  ? 277  LEU   A CD2 1 1 
ATOM   2233  N  N   . ASP   A 1  278 ? 23.354  -17.942 -26.505 1    28.758  ? 278  ASP   A N   1 1 
ATOM   2234  C  CA  . ASP   A 1  278 ? 22.193  -17.411 -27.201 1    36.508  ? 278  ASP   A CA  1 1 
ATOM   2235  C  C   . ASP   A 1  278 ? 22.332  -17.869 -28.653 1    29.854  ? 278  ASP   A C   1 1 
ATOM   2236  O  O   . ASP   A 1  278 ? 23.228  -17.459 -29.353 1    31.438  ? 278  ASP   A O   1 1 
ATOM   2237  C  CB  . ASP   A 1  278 ? 21.816  -15.967 -26.831 1    38.656  ? 278  ASP   A CB  1 1 
ATOM   2238  C  CG  . ASP   A 1  278 ? 20.965  -15.264 -27.895 1    54.578  ? 278  ASP   A CG  1 1 
ATOM   2239  O  OD1 . ASP   A 1  278 ? 19.98   -15.893 -28.356 1    46.665  ? 278  ASP   A OD1 1 1 
ATOM   2240  O  OD2 . ASP   A 1  278 ? 21.337  -14.131 -28.337 1    61.078  ? 278  ASP   A OD2 1 1 
ATOM   2241  N  N   . VAL   A 1  279 ? 21.496  -18.822 -29.05  1    29.123  ? 279  VAL   A N   1 1 
ATOM   2242  C  CA  . VAL   A 1  279 ? 21.71   -19.483 -30.317 1    27.301  ? 279  VAL   A CA  1 1 
ATOM   2243  C  C   . VAL   A 1  279 ? 20.898  -18.799 -31.415 1    27.943  ? 279  VAL   A C   1 1 
ATOM   2244  O  O   . VAL   A 1  279 ? 20.807  -19.36  -32.529 1    26.236  ? 279  VAL   A O   1 1 
ATOM   2245  C  CB  . VAL   A 1  279 ? 21.25   -20.945 -30.105 1    28.301  ? 279  VAL   A CB  1 1 
ATOM   2246  C  CG1 . VAL   A 1  279 ? 22.126  -21.671 -29.081 1    29.989  ? 279  VAL   A CG1 1 1 
ATOM   2247  C  CG2 . VAL   A 1  279 ? 19.732  -21.096 -29.851 1    25.068  ? 279  VAL   A CG2 1 1 
ATOM   2248  N  N   . THR   A 1  280 ? 20.264  -17.641 -31.099 1    26.74   ? 280  THR   A N   1 1 
ATOM   2249  C  CA  . THR   A 1  280 ? 19.546  -16.915 -32.151 1    29.431  ? 280  THR   A CA  1 1 
ATOM   2250  C  C   . THR   A 1  280 ? 20.383  -16.823 -33.43  1    30.924  ? 280  THR   A C   1 1 
ATOM   2251  O  O   . THR   A 1  280 ? 19.924  -17.14  -34.524 1    31.39   ? 280  THR   A O   1 1 
ATOM   2252  C  CB  . THR   A 1  280 ? 19.06   -15.52  -31.735 1    28.269  ? 280  THR   A CB  1 1 
ATOM   2253  O  OG1 . THR   A 1  280 ? 18.22   -15.704 -30.61  1    26.107  ? 280  THR   A OG1 1 1 
ATOM   2254  C  CG2 . THR   A 1  280 ? 18.36   -14.816 -32.886 1    28.293  ? 280  THR   A CG2 1 1 
ATOM   2255  N  N   . SER   A 1  281 ? 21.644  -16.399 -33.313 1    35.026  ? 281  SER   A N   1 1 
ATOM   2256  C  CA  . SER   A 1  281 ? 22.377  -16.193 -34.563 1    37.811  ? 281  SER   A CA  1 1 
ATOM   2257  C  C   . SER   A 1  281 ? 22.51   -17.496 -35.347 1    34.634  ? 281  SER   A C   1 1 
ATOM   2258  O  O   . SER   A 1  281 ? 22.435  -17.488 -36.567 1    36.344  ? 281  SER   A O   1 1 
ATOM   2259  C  CB  . SER   A 1  281 ? 23.701  -15.479 -34.378 1    43.428  ? 281  SER   A CB  1 1 
ATOM   2260  O  OG  . SER   A 1  281 ? 24.606  -16.333 -33.699 1    50.972  ? 281  SER   A OG  1 1 
ATOM   2261  N  N   . THR   A 1  282 ? 22.6    -18.635 -34.653 1    32.982  ? 282  THR   A N   1 1 
ATOM   2262  C  CA  . THR   A 1  282 ? 22.709  -19.94  -35.303 1    31.343  ? 282  THR   A CA  1 1 
ATOM   2263  C  C   . THR   A 1  282 ? 21.39   -20.322 -35.986 1    29.358  ? 282  THR   A C   1 1 
ATOM   2264  O  O   . THR   A 1  282 ? 21.403  -20.869 -37.101 1    30.432  ? 282  THR   A O   1 1 
ATOM   2265  C  CB  . THR   A 1  282 ? 23.189  -20.993 -34.287 1    32.38   ? 282  THR   A CB  1 1 
ATOM   2266  O  OG1 . THR   A 1  282 ? 24.433  -20.536 -33.761 1    32.734  ? 282  THR   A OG1 1 1 
ATOM   2267  C  CG2 . THR   A 1  282 ? 23.474  -22.361 -34.884 1    31.04   ? 282  THR   A CG2 1 1 
ATOM   2268  N  N   . MET   A 1  283 ? 20.252  -20.065 -35.307 1    27.597  ? 283  MET   A N   1 1 
ATOM   2269  C  CA  . MET   A 1  283 ? 18.963  -20.351 -35.933 1    27.57   ? 283  MET   A CA  1 1 
ATOM   2270  C  C   . MET   A 1  283 ? 18.854  -19.579 -37.257 1    28.021  ? 283  MET   A C   1 1 
ATOM   2271  O  O   . MET   A 1  283 ? 18.433  -20.128 -38.25  1    27.688  ? 283  MET   A O   1 1 
ATOM   2272  C  CB  . MET   A 1  283 ? 17.803  -19.94  -35.008 1    24.693  ? 283  MET   A CB  1 1 
ATOM   2273  C  CG  . MET   A 1  283 ? 17.771  -20.74  -33.7   1    24.56   ? 283  MET   A CG  1 1 
ATOM   2274  S  SD  . MET   A 1  283 ? 16.515  -20.212 -32.516 1    25.28   ? 283  MET   A SD  1 1 
ATOM   2275  C  CE  . MET   A 1  283 ? 14.962  -20.636 -33.328 1    25.293  ? 283  MET   A CE  1 1 
ATOM   2276  N  N   . LEU   A 1  284 ? 19.248  -18.305 -37.254 1    30.475  ? 284  LEU   A N   1 1 
ATOM   2277  C  CA  . LEU   A 1  284 ? 19.27   -17.478 -38.47  1    35.08   ? 284  LEU   A CA  1 1 
ATOM   2278  C  C   . LEU   A 1  284 ? 20.233  -18.044 -39.507 1    36.939  ? 284  LEU   A C   1 1 
ATOM   2279  O  O   . LEU   A 1  284 ? 19.842  -18.336 -40.638 1    38.803  ? 284  LEU   A O   1 1 
ATOM   2280  C  CB  . LEU   A 1  284 ? 19.665  -16.061 -38.035 1    40.925  ? 284  LEU   A CB  1 1 
ATOM   2281  C  CG  . LEU   A 1  284 ? 18.607  -15.337 -37.198 1    41.599  ? 284  LEU   A CG  1 1 
ATOM   2282  C  CD1 . LEU   A 1  284 ? 19.16   -14.026 -36.639 1    46.311  ? 284  LEU   A CD1 1 1 
ATOM   2283  C  CD2 . LEU   A 1  284 ? 17.396  -15.097 -38.1   1    44.905  ? 284  LEU   A CD2 1 1 
ATOM   2284  N  N   . GLN   A 1  285 ? 21.479  -18.301 -39.083 1    35.183  ? 285  GLN   A N   1 1 
ATOM   2285  C  CA  . GLN   A 1  285 ? 22.462  -18.853 -40     1    37.798  ? 285  GLN   A CA  1 1 
ATOM   2286  C  C   . GLN   A 1  285 ? 21.885  -20.12  -40.625 1    35.63   ? 285  GLN   A C   1 1 
ATOM   2287  O  O   . GLN   A 1  285 ? 22.055  -20.344 -41.811 1    34.46   ? 285  GLN   A O   1 1 
ATOM   2288  C  CB  . GLN   A 1  285 ? 23.834  -18.98  -39.336 1    38.233  ? 285  GLN   A CB  1 1 
ATOM   2289  C  CG  . GLN   A 1  285 ? 24.932  -19.549 -40.228 1    51.132  ? 285  GLN   A CG  1 1 
ATOM   2290  C  CD  . GLN   A 1  285 ? 25.113  -21.031 -40.003 1    56.104  ? 285  GLN   A CD  1 1 
ATOM   2291  O  OE1 . GLN   A 1  285 ? 25.102  -21.499 -38.851 1    57.99   ? 285  GLN   A OE1 1 1 
ATOM   2292  N  NE2 . GLN   A 1  285 ? 25.239  -21.778 -41.093 1    55.657  ? 285  GLN   A NE2 1 1 
ATOM   2293  N  N   . GLN   A 1  286 ? 21.174  -20.945 -39.839 1    33.213  ? 286  GLN   A N   1 1 
ATOM   2294  C  CA  . GLN   A 1  286 ? 20.764  -22.255 -40.349 1    33.062  ? 286  GLN   A CA  1 1 
ATOM   2295  C  C   . GLN   A 1  286 ? 19.437  -22.189 -41.111 1    33.796  ? 286  GLN   A C   1 1 
ATOM   2296  O  O   . GLN   A 1  286 ? 19.003  -23.176 -41.703 1    34.823  ? 286  GLN   A O   1 1 
ATOM   2297  C  CB  . GLN   A 1  286 ? 20.554  -23.188 -39.143 1    33.205  ? 286  GLN   A CB  1 1 
ATOM   2298  C  CG  . GLN   A 1  286 ? 21.804  -23.973 -38.75  1    32.551  ? 286  GLN   A CG  1 1 
ATOM   2299  C  CD  . GLN   A 1  286 ? 21.672  -24.833 -37.501 1    33.696  ? 286  GLN   A CD  1 1 
ATOM   2300  O  OE1 . GLN   A 1  286 ? 20.583  -25.047 -36.952 1    31.498  ? 286  GLN   A OE1 1 1 
ATOM   2301  N  NE2 . GLN   A 1  286 ? 22.802  -25.381 -37.051 1    35.116  ? 286  GLN   A NE2 1 1 
ATOM   2302  N  N   . GLY   A 1  287 ? 18.737  -21.048 -41.055 1    33.25   ? 287  GLY   A N   1 1 
ATOM   2303  C  CA  . GLY   A 1  287 ? 17.536  -20.98  -41.873 1    34.699  ? 287  GLY   A CA  1 1 
ATOM   2304  C  C   . GLY   A 1  287 ? 16.263  -21.485 -41.187 1    32.473  ? 287  GLY   A C   1 1 
ATOM   2305  O  O   . GLY   A 1  287 ? 15.359  -21.956 -41.876 1    33.183  ? 287  GLY   A O   1 1 
ATOM   2306  N  N   . TRP   A 1  288 ? 16.184  -21.393 -39.847 1    28.479  ? 288  TRP   A N   1 1 
ATOM   2307  C  CA  . TRP   A 1  288 ? 14.98   -21.845 -39.173 1    27.083  ? 288  TRP   A CA  1 1 
ATOM   2308  C  C   . TRP   A 1  288 ? 13.839  -20.883 -39.519 1    27.072  ? 288  TRP   A C   1 1 
ATOM   2309  O  O   . TRP   A 1  288 ? 14.059  -19.673 -39.533 1    26.896  ? 288  TRP   A O   1 1 
ATOM   2310  C  CB  . TRP   A 1  288 ? 15.205  -21.785 -37.646 1    25.837  ? 288  TRP   A CB  1 1 
ATOM   2311  C  CG  . TRP   A 1  288 ? 16.069  -22.898 -37.114 1    26.142  ? 288  TRP   A CG  1 1 
ATOM   2312  C  CD1 . TRP   A 1  288 ? 17.388  -23.16  -37.425 1    27.327  ? 288  TRP   A CD1 1 1 
ATOM   2313  C  CD2 . TRP   A 1  288 ? 15.675  -23.864 -36.119 1    24.961  ? 288  TRP   A CD2 1 1 
ATOM   2314  N  NE1 . TRP   A 1  288 ? 17.824  -24.264 -36.733 1    26.416  ? 288  TRP   A NE1 1 1 
ATOM   2315  C  CE2 . TRP   A 1  288 ? 16.807  -24.689 -35.892 1    25.083  ? 288  TRP   A CE2 1 1 
ATOM   2316  C  CE3 . TRP   A 1  288 ? 14.505  -24.065 -35.37  1    25.462  ? 288  TRP   A CE3 1 1 
ATOM   2317  C  CZ2 . TRP   A 1  288 ? 16.769  -25.725 -34.959 1    24.244  ? 288  TRP   A CZ2 1 1 
ATOM   2318  C  CZ3 . TRP   A 1  288 ? 14.482  -25.068 -34.418 1    25.342  ? 288  TRP   A CZ3 1 1 
ATOM   2319  C  CH2 . TRP   A 1  288 ? 15.605  -25.89  -34.229 1    24.471  ? 288  TRP   A CH2 1 1 
ATOM   2320  N  N   . GLN   A 1  289 ? 12.626  -21.427 -39.61  1    26.728  ? 289  GLN   A N   1 1 
ATOM   2321  C  CA  . GLN   A 1  289 ? 11.385  -20.678 -39.769 1    28.989  ? 289  GLN   A CA  1 1 
ATOM   2322  C  C   . GLN   A 1  289 ? 10.395  -21.061 -38.667 1    26.707  ? 289  GLN   A C   1 1 
ATOM   2323  O  O   . GLN   A 1  289 ? 10.605  -22.057 -37.966 1    25.996  ? 289  GLN   A O   1 1 
ATOM   2324  C  CB  . GLN   A 1  289 ? 10.733  -21.108 -41.096 1    32.015  ? 289  GLN   A CB  1 1 
ATOM   2325  C  CG  . GLN   A 1  289 ? 11.582  -20.9   -42.348 1    40.212  ? 289  GLN   A CG  1 1 
ATOM   2326  C  CD  . GLN   A 1  289 ? 11.867  -19.441 -42.644 1    45.717  ? 289  GLN   A CD  1 1 
ATOM   2327  O  OE1 . GLN   A 1  289 ? 11.74   -18.566 -41.777 1    46.163  ? 289  GLN   A OE1 1 1 
ATOM   2328  N  NE2 . GLN   A 1  289 ? 12.27   -19.164 -43.878 1    53.714  ? 289  GLN   A NE2 1 1 
ATOM   2329  N  N   . ALA   A 1  290 ? 9.251   -20.352 -38.587 1    24.923  ? 290  ALA   A N   1 1 
ATOM   2330  C  CA  . ALA   A 1  290 ? 8.235   -20.666 -37.593 1    23.918  ? 290  ALA   A CA  1 1 
ATOM   2331  C  C   . ALA   A 1  290 ? 7.9     -22.151 -37.633 1    24.883  ? 290  ALA   A C   1 1 
ATOM   2332  O  O   . ALA   A 1  290 ? 7.803   -22.797 -36.595 1    22.489  ? 290  ALA   A O   1 1 
ATOM   2333  C  CB  . ALA   A 1  290 ? 6.958   -19.837 -37.748 1    23.463  ? 290  ALA   A CB  1 1 
ATOM   2334  N  N   . THR   A 1  291 ? 7.705   -22.687 -38.835 1    26.075  ? 291  THR   A N   1 1 
ATOM   2335  C  CA  . THR   A 1  291 ? 7.273   -24.072 -38.908 1    29.862  ? 291  THR   A CA  1 1 
ATOM   2336  C  C   . THR   A 1  291 ? 8.296   -25.04  -38.276 1    27.652  ? 291  THR   A C   1 1 
ATOM   2337  O  O   . THR   A 1  291 ? 7.896   -25.923 -37.521 1    28.354  ? 291  THR   A O   1 1 
ATOM   2338  C  CB  . THR   A 1  291 ? 6.887   -24.398 -40.358 1    36.413  ? 291  THR   A CB  1 1 
ATOM   2339  O  OG1 . THR   A 1  291 ? 5.655   -25.097 -40.186 1    47.548  ? 291  THR   A OG1 1 1 
ATOM   2340  C  CG2 . THR   A 1  291 ? 7.915   -25.268 -41.037 1    38.311  ? 291  THR   A CG2 1 1 
ATOM   2341  N  N   . HIS   A 1  292 ? 9.607   -24.849 -38.452 1    27.956  ? 292  HIS   A N   1 1 
ATOM   2342  C  CA  . HIS   A 1  292 ? 10.605  -25.716 -37.812 1    26.251  ? 292  HIS   A CA  1 1 
ATOM   2343  C  C   . HIS   A 1  292 ? 10.489  -25.619 -36.286 1    24.424  ? 292  HIS   A C   1 1 
ATOM   2344  O  O   . HIS   A 1  292 ? 10.573  -26.619 -35.561 1    22.886  ? 292  HIS   A O   1 1 
ATOM   2345  C  CB  . HIS   A 1  292 ? 12.049  -25.332 -38.188 1    29.306  ? 292  HIS   A CB  1 1 
ATOM   2346  C  CG  . HIS   A 1  292 ? 12.28   -25.252 -39.66  1    32.583  ? 292  HIS   A CG  1 1 
ATOM   2347  N  ND1 . HIS   A 1  292 ? 12.002  -24.106 -40.375 1    34.789  ? 292  HIS   A ND1 1 1 
ATOM   2348  C  CD2 . HIS   A 1  292 ? 12.69   -26.166 -40.573 1    35.546  ? 292  HIS   A CD2 1 1 
ATOM   2349  C  CE1 . HIS   A 1  292 ? 12.25   -24.318 -41.675 1    38.248  ? 292  HIS   A CE1 1 1 
ATOM   2350  N  NE2 . HIS   A 1  292 ? 12.664  -25.561 -41.824 1    35.82   ? 292  HIS   A NE2 1 1 
ATOM   2351  N  N   . MET   A 1  293 ? 10.268  -24.397 -35.798 1    21.449  ? 293  MET   A N   1 1 
ATOM   2352  C  CA  . MET   A 1  293 ? 10.188  -24.172 -34.362 1    20.444  ? 293  MET   A CA  1 1 
ATOM   2353  C  C   . MET   A 1  293 ? 9.071   -25     -33.746 1    19.114  ? 293  MET   A C   1 1 
ATOM   2354  O  O   . MET   A 1  293 ? 9.243   -25.587 -32.677 1    17.409  ? 293  MET   A O   1 1 
ATOM   2355  C  CB  . MET   A 1  293 ? 10.005  -22.67  -34.078 1    20.469  ? 293  MET   A CB  1 1 
ATOM   2356  C  CG  . MET   A 1  293 ? 11.215  -21.897 -34.623 1    22.873  ? 293  MET   A CG  1 1 
ATOM   2357  S  SD  . MET   A 1  293 ? 11.114  -20.092 -34.663 1    26.781  ? 293  MET   A SD  1 1 
ATOM   2358  C  CE  . MET   A 1  293 ? 11.026  -19.777 -32.882 1    22.676  ? 293  MET   A CE  1 1 
ATOM   2359  N  N   . PHE   A 1  294 ? 7.873   -24.963 -34.372 1    18.7    ? 294  PHE   A N   1 1 
ATOM   2360  C  CA  . PHE   A 1  294 ? 6.722   -25.653 -33.81  1    18.341  ? 294  PHE   A CA  1 1 
ATOM   2361  C  C   . PHE   A 1  294 ? 6.919   -27.179 -33.945 1    18.659  ? 294  PHE   A C   1 1 
ATOM   2362  O  O   . PHE   A 1  294 ? 6.51    -27.951 -33.078 1    18.807  ? 294  PHE   A O   1 1 
ATOM   2363  C  CB  . PHE   A 1  294 ? 5.416   -25.249 -34.553 1    18.322  ? 294  PHE   A CB  1 1 
ATOM   2364  C  CG  . PHE   A 1  294 ? 4.884   -23.941 -33.979 1    18.136  ? 294  PHE   A CG  1 1 
ATOM   2365  C  CD1 . PHE   A 1  294 ? 5.383   -22.716 -34.419 1    19.046  ? 294  PHE   A CD1 1 1 
ATOM   2366  C  CD2 . PHE   A 1  294 ? 3.943   -23.936 -32.944 1    18.1    ? 294  PHE   A CD2 1 1 
ATOM   2367  C  CE1 . PHE   A 1  294 ? 4.95    -21.515 -33.854 1    18.55   ? 294  PHE   A CE1 1 1 
ATOM   2368  C  CE2 . PHE   A 1  294 ? 3.542   -22.744 -32.364 1    17.581  ? 294  PHE   A CE2 1 1 
ATOM   2369  C  CZ  . PHE   A 1  294 ? 4.01    -21.54  -32.849 1    17.845  ? 294  PHE   A CZ  1 1 
ATOM   2370  N  N   . ARG   A 1  295 ? 7.533   -27.631 -35.028 1    19.311  ? 295  ARG   A N   1 1 
ATOM   2371  C  CA  . ARG   A 1  295 ? 7.799   -29.063 -35.171 1    20.774  ? 295  ARG   A CA  1 1 
ATOM   2372  C  C   . ARG   A 1  295 ? 8.863   -29.575 -34.176 1    20.546  ? 295  ARG   A C   1 1 
ATOM   2373  O  O   . ARG   A 1  295 ? 8.771   -30.683 -33.63  1    19.938  ? 295  ARG   A O   1 1 
ATOM   2374  C  CB  . ARG   A 1  295 ? 8.194   -29.385 -36.61  1    22.922  ? 295  ARG   A CB  1 1 
ATOM   2375  C  CG  . ARG   A 1  295 ? 7.081   -29.246 -37.65  1    24.844  ? 295  ARG   A CG  1 1 
ATOM   2376  C  CD  . ARG   A 1  295 ? 6.088   -30.391 -37.453 1    25.302  ? 295  ARG   A CD  1 1 
ATOM   2377  N  NE  . ARG   A 1  295 ? 5.008   -30.284 -38.449 1    26.167  ? 295  ARG   A NE  1 1 
ATOM   2378  C  CZ  . ARG   A 1  295 ? 4.01    -31.132 -38.592 1    26.685  ? 295  ARG   A CZ  1 1 
ATOM   2379  N  NH1 . ARG   A 1  295 ? 3.886   -32.155 -37.753 1    26.893  ? 295  ARG   A NH1 1 1 
ATOM   2380  N  NH2 . ARG   A 1  295 ? 3.117   -30.917 -39.539 1    27.366  ? 295  ARG   A NH2 1 1 
ATOM   2381  N  N   . VAL   A 1  296 ? 9.862   -28.758 -33.911 1    20.927  ? 296  VAL   A N   1 1 
ATOM   2382  C  CA  . VAL   A 1  296 ? 10.865  -29.218 -32.943 1    20.915  ? 296  VAL   A CA  1 1 
ATOM   2383  C  C   . VAL   A 1  296 ? 10.231  -29.292 -31.537 1    19.629  ? 296  VAL   A C   1 1 
ATOM   2384  O  O   . VAL   A 1  296 ? 10.462  -30.244 -30.804 1    19.353  ? 296  VAL   A O   1 1 
ATOM   2385  C  CB  . VAL   A 1  296 ? 12.099  -28.303 -33.061 1    21.6    ? 296  VAL   A CB  1 1 
ATOM   2386  C  CG1 . VAL   A 1  296 ? 13.073  -28.49  -31.914 1    21.904  ? 296  VAL   A CG1 1 1 
ATOM   2387  C  CG2 . VAL   A 1  296 ? 12.798  -28.477 -34.412 1    23.599  ? 296  VAL   A CG2 1 1 
ATOM   2388  N  N   . ALA   A 1  297 ? 9.367   -28.334 -31.186 1    18.923  ? 297  ALA   A N   1 1 
ATOM   2389  C  CA  . ALA   A 1  297 ? 8.621   -28.296 -29.924 1    18.414  ? 297  ALA   A CA  1 1 
ATOM   2390  C  C   . ALA   A 1  297 ? 7.784   -29.559 -29.834 1    18.757  ? 297  ALA   A C   1 1 
ATOM   2391  O  O   . ALA   A 1  297 ? 7.785   -30.222 -28.823 1    17.675  ? 297  ALA   A O   1 1 
ATOM   2392  C  CB  . ALA   A 1  297 ? 7.735   -27.044 -29.792 1    17.407  ? 297  ALA   A CB  1 1 
ATOM   2393  N  N   . GLU   A 1  298 ? 7.039   -29.857 -30.912 1    19.743  ? 298  GLU   A N   1 1 
ATOM   2394  C  CA  . GLU   A 1  298 ? 6.15    -30.999 -30.909 1    20.905  ? 298  GLU   A CA  1 1 
ATOM   2395  C  C   . GLU   A 1  298 ? 6.922   -32.29  -30.629 1    22.135  ? 298  GLU   A C   1 1 
ATOM   2396  O  O   . GLU   A 1  298 ? 6.448   -33.172 -29.886 1    22.372  ? 298  GLU   A O   1 1 
ATOM   2397  C  CB  . GLU   A 1  298 ? 5.497   -31.064 -32.295 1    22.198  ? 298  GLU   A CB  1 1 
ATOM   2398  C  CG  . GLU   A 1  298 ? 4.571   -32.265 -32.414 1    24.496  ? 298  GLU   A CG  1 1 
ATOM   2399  C  CD  . GLU   A 1  298 ? 4.039   -32.466 -33.823 1    28.354  ? 298  GLU   A CD  1 1 
ATOM   2400  O  OE1 . GLU   A 1  298 ? 4.834   -32.476 -34.803 1    29.186  ? 298  GLU   A OE1 1 1 
ATOM   2401  O  OE2 . GLU   A 1  298 ? 2.796   -32.578 -33.924 1    30.409  ? 298  GLU   A OE2 1 1 
ATOM   2402  N  N   . GLU   A 1  299 ? 8.116   -32.416 -31.255 1    21.233  ? 299  GLU   A N   1 1 
ATOM   2403  C  CA  . GLU   A 1  299 ? 8.895   -33.634 -31.145 1    22.991  ? 299  GLU   A CA  1 1 
ATOM   2404  C  C   . GLU   A 1  299 ? 9.343   -33.849 -29.685 1    21.021  ? 299  GLU   A C   1 1 
ATOM   2405  O  O   . GLU   A 1  299 ? 9.41    -34.979 -29.228 1    21.074  ? 299  GLU   A O   1 1 
ATOM   2406  C  CB  . GLU   A 1  299 ? 9.99    -33.66  -32.225 1    23.529  ? 299  GLU   A CB  1 1 
ATOM   2407  C  CG  . GLU   A 1  299 ? 10.636  -35.024 -32.467 1    26.751  ? 299  GLU   A CG  1 1 
ATOM   2408  C  CD  . GLU   A 1  299 ? 11.629  -35.447 -31.393 1    29.476  ? 299  GLU   A CD  1 1 
ATOM   2409  O  OE1 . GLU   A 1  299 ? 12.357  -34.569 -30.866 1    27.934  ? 299  GLU   A OE1 1 1 
ATOM   2410  O  OE2 . GLU   A 1  299 ? 11.674  -36.668 -31.034 1    32.832  ? 299  GLU   A OE2 1 1 
ATOM   2411  N  N   . PHE   A 1  300 ? 9.624   -32.778 -28.951 1    20.071  ? 300  PHE   A N   1 1 
ATOM   2412  C  CA  . PHE   A 1  300 ? 9.89    -32.912 -27.513 1    19.652  ? 300  PHE   A CA  1 1 
ATOM   2413  C  C   . PHE   A 1  300 ? 8.691   -33.574 -26.804 1    19.088  ? 300  PHE   A C   1 1 
ATOM   2414  O  O   . PHE   A 1  300 ? 8.856   -34.529 -26.062 1    18.554  ? 300  PHE   A O   1 1 
ATOM   2415  C  CB  . PHE   A 1  300 ? 10.367  -31.582 -26.923 1    18.775  ? 300  PHE   A CB  1 1 
ATOM   2416  C  CG  . PHE   A 1  300 ? 11.103  -31.724 -25.593 1    19.175  ? 300  PHE   A CG  1 1 
ATOM   2417  C  CD1 . PHE   A 1  300 ? 10.443  -32.2   -24.461 1    19.92   ? 300  PHE   A CD1 1 1 
ATOM   2418  C  CD2 . PHE   A 1  300 ? 12.466  -31.471 -25.508 1    19.377  ? 300  PHE   A CD2 1 1 
ATOM   2419  C  CE1 . PHE   A 1  300 ? 11.103  -32.342 -23.222 1    20.642  ? 300  PHE   A CE1 1 1 
ATOM   2420  C  CE2 . PHE   A 1  300 ? 13.134  -31.622 -24.269 1    20.675  ? 300  PHE   A CE2 1 1 
ATOM   2421  C  CZ  . PHE   A 1  300 ? 12.442  -32.057 -23.138 1    20.047  ? 300  PHE   A CZ  1 1 
ATOM   2422  N  N   . PHE   A 1  301 ? 7.482   -33.079 -27.06  1    19.005  ? 301  PHE   A N   1 1 
ATOM   2423  C  CA  . PHE   A 1  301 ? 6.274   -33.634 -26.476 1    21.422  ? 301  PHE   A CA  1 1 
ATOM   2424  C  C   . PHE   A 1  301 ? 6.115   -35.114 -26.834 1    23.203  ? 301  PHE   A C   1 1 
ATOM   2425  O  O   . PHE   A 1  301 ? 5.857   -35.927 -25.941 1    23.239  ? 301  PHE   A O   1 1 
ATOM   2426  C  CB  . PHE   A 1  301 ? 4.996   -32.843 -26.8   1    20.986  ? 301  PHE   A CB  1 1 
ATOM   2427  C  CG  . PHE   A 1  301 ? 4.861   -31.518 -26.067 1    21.913  ? 301  PHE   A CG  1 1 
ATOM   2428  C  CD1 . PHE   A 1  301 ? 5.396   -30.343 -26.603 1    23.493  ? 301  PHE   A CD1 1 1 
ATOM   2429  C  CD2 . PHE   A 1  301 ? 4.226   -31.447 -24.828 1    21.516  ? 301  PHE   A CD2 1 1 
ATOM   2430  C  CE1 . PHE   A 1  301 ? 5.306   -29.122 -25.921 1    22.631  ? 301  PHE   A CE1 1 1 
ATOM   2431  C  CE2 . PHE   A 1  301 ? 4.109   -30.227 -24.166 1    21.093  ? 301  PHE   A CE2 1 1 
ATOM   2432  C  CZ  . PHE   A 1  301 ? 4.65    -29.056 -24.703 1    21.328  ? 301  PHE   A CZ  1 1 
ATOM   2433  N  N   . THR   A 1  302 ? 6.269   -35.475 -28.125 1    22.577  ? 302  THR   A N   1 1 
ATOM   2434  C  CA  . THR   A 1  302 ? 6.15    -36.868 -28.485 1    22.852  ? 302  THR   A CA  1 1 
ATOM   2435  C  C   . THR   A 1  302 ? 7.28    -37.747 -27.921 1    22.22   ? 302  THR   A C   1 1 
ATOM   2436  O  O   . THR   A 1  302 ? 7.022   -38.929 -27.727 1    21.937  ? 302  THR   A O   1 1 
ATOM   2437  C  CB  . THR   A 1  302 ? 5.905   -37.071 -29.99  1    25.558  ? 302  THR   A CB  1 1 
ATOM   2438  O  OG1 . THR   A 1  302 ? 7.059   -36.553 -30.645 1    25.678  ? 302  THR   A OG1 1 1 
ATOM   2439  C  CG2 . THR   A 1  302 ? 4.657   -36.332 -30.483 1    26.002  ? 302  THR   A CG2 1 1 
ATOM   2440  N  N   . SER   A 1  303 ? 8.501   -37.212 -27.708 1    21.305  ? 303  SER   A N   1 1 
ATOM   2441  C  CA  . SER   A 1  303 ? 9.619   -37.955 -27.112 1    21.905  ? 303  SER   A CA  1 1 
ATOM   2442  C  C   . SER   A 1  303 ? 9.229   -38.471 -25.718 1    22.258  ? 303  SER   A C   1 1 
ATOM   2443  O  O   . SER   A 1  303 ? 9.7     -39.517 -25.261 1    22.598  ? 303  SER   A O   1 1 
ATOM   2444  C  CB  . SER   A 1  303 ? 10.872  -37.107 -26.989 1    20.842  ? 303  SER   A CB  1 1 
ATOM   2445  O  OG  . SER   A 1  303 ? 10.924  -36.297 -25.806 1    21.254  ? 303  SER   A OG  1 1 
ATOM   2446  N  N   . LEU   A 1  304 ? 8.326   -37.731 -25.077 1    21.026  ? 304  LEU   A N   1 1 
ATOM   2447  C  CA  . LEU   A 1  304 ? 7.853   -38.06  -23.737 1    22.056  ? 304  LEU   A CA  1 1 
ATOM   2448  C  C   . LEU   A 1  304 ? 6.628   -38.98  -23.824 1    24.532  ? 304  LEU   A C   1 1 
ATOM   2449  O  O   . LEU   A 1  304 ? 6.04    -39.287 -22.792 1    25.219  ? 304  LEU   A O   1 1 
ATOM   2450  C  CB  . LEU   A 1  304 ? 7.451   -36.771 -23.007 1    20.405  ? 304  LEU   A CB  1 1 
ATOM   2451  C  CG  . LEU   A 1  304 ? 8.519   -35.699 -22.753 1    19.271  ? 304  LEU   A CG  1 1 
ATOM   2452  C  CD1 . LEU   A 1  304 ? 7.989   -34.482 -22.017 1    18.233  ? 304  LEU   A CD1 1 1 
ATOM   2453  C  CD2 . LEU   A 1  304 ? 9.643   -36.275 -21.957 1    20.152  ? 304  LEU   A CD2 1 1 
ATOM   2454  N  N   . GLU   A 1  305 ? 6.235   -39.399 -25.041 1    24.684  ? 305  GLU   A N   1 1 
ATOM   2455  C  CA  . GLU   A 1  305 ? 4.974   -40.101 -25.296 1    27.007  ? 305  GLU   A CA  1 1 
ATOM   2456  C  C   . GLU   A 1  305 ? 3.772   -39.267 -24.867 1    26.582  ? 305  GLU   A C   1 1 
ATOM   2457  O  O   . GLU   A 1  305 ? 2.745   -39.818 -24.489 1    30.178  ? 305  GLU   A O   1 1 
ATOM   2458  C  CB  . GLU   A 1  305 ? 4.791   -41.457 -24.61  1    31.69   ? 305  GLU   A CB  1 1 
ATOM   2459  C  CG  . GLU   A 1  305 ? 5.701   -42.551 -25.164 1    39.33   ? 305  GLU   A CG  1 1 
ATOM   2460  C  CD  . GLU   A 1  305 ? 5.736   -43.833 -24.323 1    48.125  ? 305  GLU   A CD  1 1 
ATOM   2461  O  OE1 . GLU   A 1  305 ? 5.234   -43.926 -23.156 1    49.251  ? 305  GLU   A OE1 1 1 
ATOM   2462  O  OE2 . GLU   A 1  305 ? 6.29    -44.787 -24.887 1    48.519  ? 305  GLU   A OE2 1 1 
ATOM   2463  N  N   . LEU   A 1  306 ? 3.86    -37.939 -24.947 1    24.57   ? 306  LEU   A N   1 1 
ATOM   2464  C  CA  . LEU   A 1  306 ? 2.633   -37.147 -24.941 1    23.755  ? 306  LEU   A CA  1 1 
ATOM   2465  C  C   . LEU   A 1  306 ? 2.073   -37.022 -26.373 1    24.8    ? 306  LEU   A C   1 1 
ATOM   2466  O  O   . LEU   A 1  306 ? 2.67    -37.558 -27.323 1    25.589  ? 306  LEU   A O   1 1 
ATOM   2467  C  CB  . LEU   A 1  306 ? 2.998   -35.809 -24.286 1    22.222  ? 306  LEU   A CB  1 1 
ATOM   2468  C  CG  . LEU   A 1  306 ? 3.426   -35.928 -22.811 1    24.648  ? 306  LEU   A CG  1 1 
ATOM   2469  C  CD1 . LEU   A 1  306 ? 3.774   -34.57  -22.228 1    24.016  ? 306  LEU   A CD1 1 1 
ATOM   2470  C  CD2 . LEU   A 1  306 ? 2.338   -36.571 -21.957 1    26.779  ? 306  LEU   A CD2 1 1 
ATOM   2471  N  N   . SER   A 1  307 ? 0.897   -36.374 -26.561 1    22.852  ? 307  SER   A N   1 1 
ATOM   2472  C  CA  . SER   A 1  307 ? 0.275   -36.414 -27.882 1    24.553  ? 307  SER   A CA  1 1 
ATOM   2473  C  C   . SER   A 1  307 ? 0.945   -35.447 -28.863 1    23.41   ? 307  SER   A C   1 1 
ATOM   2474  O  O   . SER   A 1  307 ? 1.34    -34.322 -28.495 1    21.058  ? 307  SER   A O   1 1 
ATOM   2475  C  CB  . SER   A 1  307 ? -1.203  -36.014 -27.809 1    26.108  ? 307  SER   A CB  1 1 
ATOM   2476  O  OG  . SER   A 1  307 ? -1.78   -36.761 -26.762 1    31.094  ? 307  SER   A OG  1 1 
ATOM   2477  N  N   . PRO   A 1  308 ? 1.013   -35.823 -30.165 1    24.233  ? 308  PRO   A N   1 1 
ATOM   2478  C  CA  . PRO   A 1  308 ? 1.406   -34.905 -31.239 1    24.569  ? 308  PRO   A CA  1 1 
ATOM   2479  C  C   . PRO   A 1  308 ? 0.303   -33.854 -31.389 1    24.352  ? 308  PRO   A C   1 1 
ATOM   2480  O  O   . PRO   A 1  308 ? -0.806  -34.038 -30.875 1    23.906  ? 308  PRO   A O   1 1 
ATOM   2481  C  CB  . PRO   A 1  308 ? 1.48    -35.856 -32.511 1    25.167  ? 308  PRO   A CB  1 1 
ATOM   2482  C  CG  . PRO   A 1  308 ? 0.394   -36.869 -32.206 1    26.159  ? 308  PRO   A CG  1 1 
ATOM   2483  C  CD  . PRO   A 1  308 ? 0.727   -37.165 -30.697 1    26.61   ? 308  PRO   A CD  1 1 
ATOM   2484  N  N   . MET   A 1  309 ? 0.636   -32.755 -32.082 1    23.75   ? 309  MET   A N   1 1 
ATOM   2485  C  CA  . MET   A 1  309 ? -0.374  -31.782 -32.481 1    25.399  ? 309  MET   A CA  1 1 
ATOM   2486  C  C   . MET   A 1  309 ? -1.283  -32.432 -33.536 1    26.463  ? 309  MET   A C   1 1 
ATOM   2487  O  O   . MET   A 1  309 ? -0.808  -33.045 -34.507 1    28.794  ? 309  MET   A O   1 1 
ATOM   2488  C  CB  . MET   A 1  309 ? 0.274   -30.481 -32.995 1    24.165  ? 309  MET   A CB  1 1 
ATOM   2489  C  CG  . MET   A 1  309 ? 1.169   -29.76  -32.033 1    25.085  ? 309  MET   A CG  1 1 
ATOM   2490  S  SD  . MET   A 1  309 ? 0.265   -29.288 -30.54  1    25.379  ? 309  MET   A SD  1 1 
ATOM   2491  C  CE  . MET   A 1  309 ? 0.798   -30.548 -29.355 1    25.048  ? 309  MET   A CE  1 1 
ATOM   2492  N  N   . PRO   A 1  310 ? -2.636  -32.379 -33.392 1    25.794  ? 310  PRO   A N   1 1 
ATOM   2493  C  CA  . PRO   A 1  310 ? -3.513  -32.97  -34.397 1    25.038  ? 310  PRO   A CA  1 1 
ATOM   2494  C  C   . PRO   A 1  310 ? -3.459  -32.223 -35.735 1    24.915  ? 310  PRO   A C   1 1 
ATOM   2495  O  O   . PRO   A 1  310 ? -3.069  -31.063 -35.806 1    23.277  ? 310  PRO   A O   1 1 
ATOM   2496  C  CB  . PRO   A 1  310 ? -4.952  -32.855 -33.778 1    26.164  ? 310  PRO   A CB  1 1 
ATOM   2497  C  CG  . PRO   A 1  310 ? -4.831  -31.687 -32.817 1    24.26   ? 310  PRO   A CG  1 1 
ATOM   2498  C  CD  . PRO   A 1  310 ? -3.38   -31.767 -32.272 1    24.807  ? 310  PRO   A CD  1 1 
ATOM   2499  N  N   . PRO   A 1  311 ? -3.977  -32.826 -36.826 1    25.531  ? 311  PRO   A N   1 1 
ATOM   2500  C  CA  . PRO   A 1  311 ? -4.071  -32.139 -38.114 1    27.113  ? 311  PRO   A CA  1 1 
ATOM   2501  C  C   . PRO   A 1  311 ? -4.798  -30.804 -38.055 1    26.571  ? 311  PRO   A C   1 1 
ATOM   2502  O  O   . PRO   A 1  311 ? -4.349  -29.848 -38.687 1    26.859  ? 311  PRO   A O   1 1 
ATOM   2503  C  CB  . PRO   A 1  311 ? -4.776  -33.094 -39.07  1    27.818  ? 311  PRO   A CB  1 1 
ATOM   2504  C  CG  . PRO   A 1  311 ? -4.73   -34.424 -38.353 1    28.226  ? 311  PRO   A CG  1 1 
ATOM   2505  C  CD  . PRO   A 1  311 ? -4.502  -34.194 -36.854 1    26.813  ? 311  PRO   A CD  1 1 
ATOM   2506  N  N   . GLU   A 1  312 ? -5.878  -30.729 -37.261 1    26.709  ? 312  GLU   A N   1 1 
ATOM   2507  C  CA  . GLU   A 1  312 ? -6.647  -29.493 -37.14  1    25.819  ? 312  GLU   A CA  1 1 
ATOM   2508  C  C   . GLU   A 1  312 ? -5.788  -28.353 -36.581 1    24.13   ? 312  GLU   A C   1 1 
ATOM   2509  O  O   . GLU   A 1  312 ? -6.017  -27.191 -36.941 1    23.364  ? 312  GLU   A O   1 1 
ATOM   2510  C  CB  . GLU   A 1  312 ? -7.764  -29.718 -36.139 1    27.864  ? 312  GLU   A CB  1 1 
ATOM   2511  C  CG  . GLU   A 1  312 ? -8.867  -30.625 -36.676 1    30.505  ? 312  GLU   A CG  1 1 
ATOM   2512  C  CD  . GLU   A 1  312 ? -8.643  -32.124 -36.531 1    34.33   ? 312  GLU   A CD  1 1 
ATOM   2513  O  OE1 . GLU   A 1  312 ? -7.529  -32.593 -36.158 1    35.361  ? 312  GLU   A OE1 1 1 
ATOM   2514  O  OE2 . GLU   A 1  312 ? -9.613  -32.846 -36.831 1    37.142  ? 312  GLU   A OE2 1 1 
ATOM   2515  N  N   . PHE   A 1  313 ? -4.797  -28.683 -35.745 1    22.526  ? 313  PHE   A N   1 1 
ATOM   2516  C  CA  . PHE   A 1  313 ? -3.857  -27.704 -35.208 1    21.788  ? 313  PHE   A CA  1 1 
ATOM   2517  C  C   . PHE   A 1  313 ? -3.038  -27.112 -36.358 1    22.298  ? 313  PHE   A C   1 1 
ATOM   2518  O  O   . PHE   A 1  313 ? -2.938  -25.886 -36.454 1    22.485  ? 313  PHE   A O   1 1 
ATOM   2519  C  CB  . PHE   A 1  313 ? -2.941  -28.292 -34.122 1    21.094  ? 313  PHE   A CB  1 1 
ATOM   2520  C  CG  . PHE   A 1  313 ? -1.799  -27.383 -33.714 1    20.317  ? 313  PHE   A CG  1 1 
ATOM   2521  C  CD1 . PHE   A 1  313 ? -0.582  -27.446 -34.387 1    20.088  ? 313  PHE   A CD1 1 1 
ATOM   2522  C  CD2 . PHE   A 1  313 ? -1.957  -26.458 -32.681 1    19.131  ? 313  PHE   A CD2 1 1 
ATOM   2523  C  CE1 . PHE   A 1  313 ? 0.439   -26.6   -34.044 1    19.563  ? 313  PHE   A CE1 1 1 
ATOM   2524  C  CE2 . PHE   A 1  313 ? -0.914  -25.629 -32.297 1    18.846  ? 313  PHE   A CE2 1 1 
ATOM   2525  C  CZ  . PHE   A 1  313 ? 0.307   -25.707 -32.969 1    19.229  ? 313  PHE   A CZ  1 1 
ATOM   2526  N  N   . TRP   A 1  314 ? -2.443  -27.966 -37.202 1    22.498  ? 314  TRP   A N   1 1 
ATOM   2527  C  CA  . TRP   A 1  314 ? -1.578  -27.487 -38.284 1    24.091  ? 314  TRP   A CA  1 1 
ATOM   2528  C  C   . TRP   A 1  314 ? -2.393  -26.754 -39.363 1    26.587  ? 314  TRP   A C   1 1 
ATOM   2529  O  O   . TRP   A 1  314 ? -1.932  -25.787 -39.949 1    27.622  ? 314  TRP   A O   1 1 
ATOM   2530  C  CB  . TRP   A 1  314 ? -0.809  -28.666 -38.904 1    24.256  ? 314  TRP   A CB  1 1 
ATOM   2531  C  CG  . TRP   A 1  314 ? 0.09    -29.298 -37.872 1    23.427  ? 314  TRP   A CG  1 1 
ATOM   2532  C  CD1 . TRP   A 1  314 ? -0.069  -30.508 -37.256 1    23.037  ? 314  TRP   A CD1 1 1 
ATOM   2533  C  CD2 . TRP   A 1  314 ? 1.3     -28.719 -37.315 1    22.93   ? 314  TRP   A CD2 1 1 
ATOM   2534  N  NE1 . TRP   A 1  314 ? 0.984   -30.73  -36.401 1    22.726  ? 314  TRP   A NE1 1 1 
ATOM   2535  C  CE2 . TRP   A 1  314 ? 1.806   -29.647 -36.372 1    22.295  ? 314  TRP   A CE2 1 1 
ATOM   2536  C  CE3 . TRP   A 1  314 ? 1.991   -27.518 -37.52  1    23.306  ? 314  TRP   A CE3 1 1 
ATOM   2537  C  CZ2 . TRP   A 1  314 ? 2.972   -29.425 -35.629 1    21.705  ? 314  TRP   A CZ2 1 1 
ATOM   2538  C  CZ3 . TRP   A 1  314 ? 3.147   -27.289 -36.781 1    22.495  ? 314  TRP   A CZ3 1 1 
ATOM   2539  C  CH2 . TRP   A 1  314 ? 3.615   -28.231 -35.851 1    21.645  ? 314  TRP   A CH2 1 1 
ATOM   2540  N  N   . GLU   A 1  315 ? -3.645  -27.16  -39.563 1    27.268  ? 315  GLU   A N   1 1 
ATOM   2541  C  CA  . GLU   A 1  315 ? -4.436  -26.569 -40.641 1    29.898  ? 315  GLU   A CA  1 1 
ATOM   2542  C  C   . GLU   A 1  315 ? -5.012  -25.222 -40.188 1    28.517  ? 315  GLU   A C   1 1 
ATOM   2543  O  O   . GLU   A 1  315 ? -5.308  -24.372 -41.021 1    29.9    ? 315  GLU   A O   1 1 
ATOM   2544  C  CB  . GLU   A 1  315 ? -5.575  -27.503 -41.068 1    33.031  ? 315  GLU   A CB  1 1 
ATOM   2545  C  CG  . GLU   A 1  315 ? -5.08   -28.766 -41.769 1    38.692  ? 315  GLU   A CG  1 1 
ATOM   2546  C  CD  . GLU   A 1  315 ? -4.499  -28.414 -43.135 1    47.89   ? 315  GLU   A CD  1 1 
ATOM   2547  O  OE1 . GLU   A 1  315 ? -5.323  -27.992 -43.976 1    56.375  ? 315  GLU   A OE1 1 1 
ATOM   2548  O  OE2 . GLU   A 1  315 ? -3.265  -28.522 -43.388 1    57.076  ? 315  GLU   A OE2 1 1 
ATOM   2549  N  N   . GLY   A 1  316 ? -5.247  -25.062 -38.891 1    26.562  ? 316  GLY   A N   1 1 
ATOM   2550  C  CA  . GLY   A 1  316 ? -6.026  -23.927 -38.388 1    26.43   ? 316  GLY   A CA  1 1 
ATOM   2551  C  C   . GLY   A 1  316 ? -5.187  -22.831 -37.736 1    25.374  ? 316  GLY   A C   1 1 
ATOM   2552  O  O   . GLY   A 1  316 ? -5.642  -21.699 -37.618 1    23.704  ? 316  GLY   A O   1 1 
ATOM   2553  N  N   . SER   A 1  317 ? -3.915  -23.131 -37.404 1    24.818  ? 317  SER   A N   1 1 
ATOM   2554  C  CA  . SER   A 1  317 ? -3.151  -22.25  -36.537 1    24.04   ? 317  SER   A CA  1 1 
ATOM   2555  C  C   . SER   A 1  317 ? -2.653  -21.055 -37.347 1    25.247  ? 317  SER   A C   1 1 
ATOM   2556  O  O   . SER   A 1  317 ? -2.448  -21.151 -38.559 1    24.368  ? 317  SER   A O   1 1 
ATOM   2557  C  CB  . SER   A 1  317 ? -1.994  -23.008 -35.904 1    22.782  ? 317  SER   A CB  1 1 
ATOM   2558  O  OG  . SER   A 1  317 ? -2.445  -23.791 -34.802 1    21.215  ? 317  SER   A OG  1 1 
ATOM   2559  N  N   . MET   A 1  318 ? -2.377  -19.943 -36.66  1    23.726  ? 318  MET   A N   1 1 
ATOM   2560  C  CA  . MET   A 1  318 ? -1.707  -18.829 -37.32  1    25.006  ? 318  MET   A CA  1 1 
ATOM   2561  C  C   . MET   A 1  318 ? -0.293  -18.713 -36.755 1    23.857  ? 318  MET   A C   1 1 
ATOM   2562  O  O   . MET   A 1  318 ? -0.174  -18.351 -35.58  1    22.076  ? 318  MET   A O   1 1 
ATOM   2563  C  CB  . MET   A 1  318 ? -2.403  -17.498 -36.996 1    25.233  ? 318  MET   A CB  1 1 
ATOM   2564  C  CG  . MET   A 1  318 ? -1.91   -16.409 -37.91  1    27.88   ? 318  MET   A CG  1 1 
ATOM   2565  S  SD  . MET   A 1  318 ? -2.423  -14.776 -37.313 1    31.561  ? 318  MET   A SD  1 1 
ATOM   2566  C  CE  . MET   A 1  318 ? -1.225  -14.346 -36.046 1    25.758  ? 318  MET   A CE  1 1 
ATOM   2567  N  N   . LEU   A 1  319 ? 0.751   -19.057 -37.552 1    24.795  ? 319  LEU   A N   1 1 
ATOM   2568  C  CA  . LEU   A 1  319 ? 2.082   -19.31  -36.935 1    25.611  ? 319  LEU   A CA  1 1 
ATOM   2569  C  C   . LEU   A 1  319 ? 3.103   -18.258 -37.362 1    27.434  ? 319  LEU   A C   1 1 
ATOM   2570  O  O   . LEU   A 1  319 ? 4.238   -18.275 -36.914 1    28.812  ? 319  LEU   A O   1 1 
ATOM   2571  C  CB  . LEU   A 1  319 ? 2.638   -20.715 -37.199 1    27.573  ? 319  LEU   A CB  1 1 
ATOM   2572  C  CG  . LEU   A 1  319 ? 1.766   -21.926 -36.793 1    26.794  ? 319  LEU   A CG  1 1 
ATOM   2573  C  CD1 . LEU   A 1  319 ? 2.457   -23.246 -37.186 1    30.185  ? 319  LEU   A CD1 1 1 
ATOM   2574  C  CD2 . LEU   A 1  319 ? 1.403   -21.936 -35.344 1    26.791  ? 319  LEU   A CD2 1 1 
ATOM   2575  N  N   . GLU   A 1  320 ? 2.71    -17.369 -38.278 1    27.689  ? 320  GLU   A N   1 1 
ATOM   2576  C  CA  . GLU   A 1  320 ? 3.444   -16.171 -38.623 1    30.84   ? 320  GLU   A CA  1 1 
ATOM   2577  C  C   . GLU   A 1  320 ? 2.443   -15.011 -38.671 1    31.589  ? 320  GLU   A C   1 1 
ATOM   2578  O  O   . GLU   A 1  320 ? 1.262   -15.238 -38.962 1    31.016  ? 320  GLU   A O   1 1 
ATOM   2579  C  CB  . GLU   A 1  320 ? 4.028   -16.323 -40.029 1    33.907  ? 320  GLU   A CB  1 1 
ATOM   2580  C  CG  . GLU   A 1  320 ? 5.23    -17.256 -40.036 1    38.942  ? 320  GLU   A CG  1 1 
ATOM   2581  C  CD  . GLU   A 1  320 ? 5.743   -17.572 -41.424 1    47.512  ? 320  GLU   A CD  1 1 
ATOM   2582  O  OE1 . GLU   A 1  320 ? 5.227   -17.002 -42.413 1    57.055  ? 320  GLU   A OE1 1 1 
ATOM   2583  O  OE2 . GLU   A 1  320 ? 6.671   -18.409 -41.507 1    49.216  ? 320  GLU   A OE2 1 1 
ATOM   2584  N  N   . LYS   A 1  321 ? 2.935   -13.79  -38.387 1    30.512  ? 321  LYS   A N   1 1 
ATOM   2585  C  CA  . LYS   A 1  321 ? 2.232   -12.57  -38.771 1    31.957  ? 321  LYS   A CA  1 1 
ATOM   2586  C  C   . LYS   A 1  321 ? 1.821   -12.574 -40.248 1    32.606  ? 321  LYS   A C   1 1 
ATOM   2587  O  O   . LYS   A 1  321 ? 2.676   -12.709 -41.137 1    31.482  ? 321  LYS   A O   1 1 
ATOM   2588  C  CB  . LYS   A 1  321 ? 3.122   -11.355 -38.518 1    32.262  ? 321  LYS   A CB  1 1 
ATOM   2589  C  CG  . LYS   A 1  321 ? 2.181   -10.145 -38.504 1    35.866  ? 321  LYS   A CG  1 1 
ATOM   2590  C  CD  . LYS   A 1  321 ? 2.789   -8.946  -37.799 1    36.793  ? 321  LYS   A CD  1 1 
ATOM   2591  C  CE  . LYS   A 1  321 ? 2.008   -7.726  -38.201 1    39.851  ? 321  LYS   A CE  1 1 
ATOM   2592  N  NZ  . LYS   A 1  321 ? 2.31    -6.708  -37.201 1    38.241  ? 321  LYS   A NZ  1 1 
ATOM   2593  N  N   . PRO   A 1  322 ? 0.51    -12.434 -40.589 1    33.03   ? 322  PRO   A N   1 1 
ATOM   2594  C  CA  . PRO   A 1  322 ? 0.093   -12.328 -42.009 1    35.735  ? 322  PRO   A CA  1 1 
ATOM   2595  C  C   . PRO   A 1  322 ? 0.769   -11.223 -42.827 1    40.076  ? 322  PRO   A C   1 1 
ATOM   2596  O  O   . PRO   A 1  322 ? 0.959   -10.099 -42.357 1    41.021  ? 322  PRO   A O   1 1 
ATOM   2597  C  CB  . PRO   A 1  322 ? -1.405  -12.075 -41.942 1    34.376  ? 322  PRO   A CB  1 1 
ATOM   2598  C  CG  . PRO   A 1  322 ? -1.824  -12.675 -40.62  1    32.318  ? 322  PRO   A CG  1 1 
ATOM   2599  C  CD  . PRO   A 1  322 ? -0.631  -12.518 -39.666 1    30.247  ? 322  PRO   A CD  1 1 
ATOM   2600  N  N   . ALA   A 1  323 ? 1.167   -11.575 -44.04  1    44.112  ? 323  ALA   A N   1 1 
ATOM   2601  C  CA  . ALA   A 1  323 ? 1.839   -10.659 -44.95  1    56.168  ? 323  ALA   A CA  1 1 
ATOM   2602  C  C   . ALA   A 1  323 ? 0.803   -9.905  -45.778 1    61.814  ? 323  ALA   A C   1 1 
ATOM   2603  O  O   . ALA   A 1  323 ? 1.112   -8.864  -46.361 1    67.57   ? 323  ALA   A O   1 1 
ATOM   2604  C  CB  . ALA   A 1  323 ? 2.801   -11.425 -45.85  1    52.529  ? 323  ALA   A CB  1 1 
ATOM   2605  N  N   . ASP   A 1  324 ? -0.429  -10.431 -45.795 1    64.376  ? 324  ASP   A N   1 1 
ATOM   2606  C  CA  . ASP   A 1  324 ? -1.451  -10.018 -46.749 1    72.394  ? 324  ASP   A CA  1 1 
ATOM   2607  C  C   . ASP   A 1  324 ? -2.001  -8.624  -46.436 1    71.273  ? 324  ASP   A C   1 1 
ATOM   2608  O  O   . ASP   A 1  324 ? -2.942  -8.194  -47.09  1    87.526  ? 324  ASP   A O   1 1 
ATOM   2609  C  CB  . ASP   A 1  324 ? -2.603  -11.011 -46.774 1    70.644  ? 324  ASP   A CB  1 1 
ATOM   2610  C  CG  . ASP   A 1  324 ? -3.489  -10.997 -45.532 1    69.924  ? 324  ASP   A CG  1 1 
ATOM   2611  O  OD1 . ASP   A 1  324 ? -3.151  -10.271 -44.561 1    68.2    ? 324  ASP   A OD1 1 1 
ATOM   2612  O  OD2 . ASP   A 1  324 ? -4.521  -11.707 -45.538 1    69.386  ? 324  ASP   A OD2 1 1 
ATOM   2613  N  N   . GLY   A 1  325 ? -1.432  -7.926  -45.446 1    71.287  ? 325  GLY   A N   1 1 
ATOM   2614  C  CA  . GLY   A 1  325 ? -1.982  -6.667  -44.965 1    74.331  ? 325  GLY   A CA  1 1 
ATOM   2615  C  C   . GLY   A 1  325 ? -3.312  -6.831  -44.212 1    75.973  ? 325  GLY   A C   1 1 
ATOM   2616  O  O   . GLY   A 1  325 ? -4.367  -6.429  -44.707 1    79.832  ? 325  GLY   A O   1 1 
ATOM   2617  N  N   . ARG   A 1  326 ? -3.262  -7.396  -42.997 1    63.534  ? 326  ARG   A N   1 1 
ATOM   2618  C  CA  . ARG   A 1  326 ? -4.428  -7.503  -42.128 1    53.026  ? 326  ARG   A CA  1 1 
ATOM   2619  C  C   . ARG   A 1  326 ? -3.971  -7.215  -40.7   1    49.794  ? 326  ARG   A C   1 1 
ATOM   2620  O  O   . ARG   A 1  326 ? -2.85   -7.556  -40.346 1    50.564  ? 326  ARG   A O   1 1 
ATOM   2621  C  CB  . ARG   A 1  326 ? -5.123  -8.819  -42.51  1    51.216  ? 326  ARG   A CB  1 1 
ATOM   2622  C  CG  . ARG   A 1  326 ? -5.482  -9.86   -41.467 1    48.523  ? 326  ARG   A CG  1 1 
ATOM   2623  C  CD  . ARG   A 1  326 ? -6.178  -11.064 -42.078 1    52.061  ? 326  ARG   A CD  1 1 
ATOM   2624  N  NE  . ARG   A 1  326 ? -5.367  -12.109 -42.725 1    56.314  ? 326  ARG   A NE  1 1 
ATOM   2625  C  CZ  . ARG   A 1  326 ? -5.095  -13.309 -42.206 1    50.707  ? 326  ARG   A CZ  1 1 
ATOM   2626  N  NH1 . ARG   A 1  326 ? -5.5    -13.611 -40.987 1    47.514  ? 326  ARG   A NH1 1 1 
ATOM   2627  N  NH2 . ARG   A 1  326 ? -4.383  -14.194 -42.882 1    51.439  ? 326  ARG   A NH2 1 1 
ATOM   2628  N  N   . GLU   A 1  327 ? -4.775  -6.488  -39.91  1    44.204  ? 327  GLU   A N   1 1 
ATOM   2629  C  CA  . GLU   A 1  327 ? -4.488  -6.299  -38.496 1    45.301  ? 327  GLU   A CA  1 1 
ATOM   2630  C  C   . GLU   A 1  327 ? -4.761  -7.606  -37.746 1    39.332  ? 327  GLU   A C   1 1 
ATOM   2631  O  O   . GLU   A 1  327 ? -5.781  -8.249  -37.978 1    38.323  ? 327  GLU   A O   1 1 
ATOM   2632  C  CB  . GLU   A 1  327 ? -5.331  -5.195  -37.853 1    45.992  ? 327  GLU   A CB  1 1 
ATOM   2633  C  CG  . GLU   A 1  327 ? -5.233  -3.809  -38.496 1    50.338  ? 327  GLU   A CG  1 1 
ATOM   2634  C  CD  . GLU   A 1  327 ? -4.135  -2.929  -37.918 1    60.66   ? 327  GLU   A CD  1 1 
ATOM   2635  O  OE1 . GLU   A 1  327 ? -3.931  -1.874  -38.548 1    69.141  ? 327  GLU   A OE1 1 1 
ATOM   2636  O  OE2 . GLU   A 1  327 ? -3.493  -3.249  -36.869 1    56.032  ? 327  GLU   A OE2 1 1 
ATOM   2637  N  N   . VAL   A 1  328 ? -3.855  -7.99   -36.83  1    35.162  ? 328  VAL   A N   1 1 
ATOM   2638  C  CA  . VAL   A 1  328 ? -4.07   -9.171  -36.015 1    29.974  ? 328  VAL   A CA  1 1 
ATOM   2639  C  C   . VAL   A 1  328 ? -3.673  -8.822  -34.587 1    27.527  ? 328  VAL   A C   1 1 
ATOM   2640  O  O   . VAL   A 1  328 ? -3.001  -7.827  -34.378 1    30.581  ? 328  VAL   A O   1 1 
ATOM   2641  C  CB  . VAL   A 1  328 ? -3.291  -10.419 -36.491 1    32.235  ? 328  VAL   A CB  1 1 
ATOM   2642  C  CG1 . VAL   A 1  328 ? -3.656  -10.864 -37.884 1    29.397  ? 328  VAL   A CG1 1 1 
ATOM   2643  C  CG2 . VAL   A 1  328 ? -1.783  -10.261 -36.323 1    30.203  ? 328  VAL   A CG2 1 1 
ATOM   2644  N  N   . VAL   A 1  329 ? -4.082  -9.631  -33.611 1    25.116  ? 329  VAL   A N   1 1 
ATOM   2645  C  CA  . VAL   A 1  329 ? -3.555  -9.507  -32.267 1    25.011  ? 329  VAL   A CA  1 1 
ATOM   2646  C  C   . VAL   A 1  329 ? -2.246  -10.309 -32.286 1    28.758  ? 329  VAL   A C   1 1 
ATOM   2647  O  O   . VAL   A 1  329 ? -2.28   -11.519 -32.474 1    28.185  ? 329  VAL   A O   1 1 
ATOM   2648  C  CB  . VAL   A 1  329 ? -4.506  -10.143 -31.24  1    22.339  ? 329  VAL   A CB  1 1 
ATOM   2649  C  CG1 . VAL   A 1  329 ? -3.893  -10.188 -29.837 1    19.283  ? 329  VAL   A CG1 1 1 
ATOM   2650  C  CG2 . VAL   A 1  329 ? -5.821  -9.359  -31.114 1    23.388  ? 329  VAL   A CG2 1 1 
ATOM   2651  N  N   . CYS   A 1  330 ? -1.101  -9.657  -32.089 1    32.144  ? 330  CYS   A N   1 1 
ATOM   2652  C  CA  . CYS   A 1  330 ? 0.139   -10.412 -32.25  1    31.535  ? 330  CYS   A CA  1 1 
ATOM   2653  C  C   . CYS   A 1  330 ? 0.547   -11.193 -31.002 1    30.894  ? 330  CYS   A C   1 1 
ATOM   2654  O  O   . CYS   A 1  330 ? 1.277   -12.18  -31.144 1    34.062  ? 330  CYS   A O   1 1 
ATOM   2655  C  CB  . CYS   A 1  330 ? 1.282   -9.574  -32.771 1    33.298  ? 330  CYS   A CB  1 1 
ATOM   2656  S  SG  . CYS   A 1  330 ? 1.416   -9.733  -34.571 1    41.124  ? 330  CYS   A SG  1 1 
ATOM   2657  N  N   . HIS   A 1  331 ? 0.069   -10.786 -29.817 1    25.504  ? 331  HIS   A N   1 1 
ATOM   2658  C  CA  . HIS   A 1  331 ? 0.472   -11.427 -28.572 1    24.034  ? 331  HIS   A CA  1 1 
ATOM   2659  C  C   . HIS   A 1  331 ? 0.144   -12.917 -28.687 1    22.445  ? 331  HIS   A C   1 1 
ATOM   2660  O  O   . HIS   A 1  331 ? -0.99   -13.275 -29.042 1    22.888  ? 331  HIS   A O   1 1 
ATOM   2661  C  CB  . HIS   A 1  331 ? -0.33   -10.849 -27.405 1    23.751  ? 331  HIS   A CB  1 1 
ATOM   2662  C  CG  . HIS   A 1  331 ? 0.161   -11.336 -26.097 1    24.268  ? 331  HIS   A CG  1 1 
ATOM   2663  N  ND1 . HIS   A 1  331 ? 1.084   -10.582 -25.406 1    27.401  ? 331  HIS   A ND1 1 1 
ATOM   2664  C  CD2 . HIS   A 1  331 ? -0.014  -12.467 -25.395 1    22.556  ? 331  HIS   A CD2 1 1 
ATOM   2665  C  CE1 . HIS   A 1  331 ? 1.424   -11.227 -24.291 1    25.969  ? 331  HIS   A CE1 1 1 
ATOM   2666  N  NE2 . HIS   A 1  331 ? 0.766   -12.359 -24.243 1    23.737  ? 331  HIS   A NE2 1 1 
ATOM   2667  N  N   . ALA   A 1  332 ? 1.122   -13.79  -28.389 1    19.737  ? 332  ALA   A N   1 1 
ATOM   2668  C  CA  . ALA   A 1  332 ? 0.995   -15.239 -28.615 1    19.825  ? 332  ALA   A CA  1 1 
ATOM   2669  C  C   . ALA   A 1  332 ? -0.095  -15.808 -27.707 1    18.824  ? 332  ALA   A C   1 1 
ATOM   2670  O  O   . ALA   A 1  332 ? -0.13   -15.463 -26.517 1    19.543  ? 332  ALA   A O   1 1 
ATOM   2671  C  CB  . ALA   A 1  332 ? 2.289   -15.956 -28.235 1    17.987  ? 332  ALA   A CB  1 1 
ATOM   2672  N  N   . SER   A 1  333 ? -0.905  -16.744 -28.217 1    17.765  ? 333  SER   A N   1 1 
ATOM   2673  C  CA  . SER   A 1  333 ? -1.942  -17.347 -27.396 1    18.131  ? 333  SER   A CA  1 1 
ATOM   2674  C  C   . SER   A 1  333 ? -2.303  -18.735 -27.899 1    18.643  ? 333  SER   A C   1 1 
ATOM   2675  O  O   . SER   A 1  333 ? -2.15   -19.03  -29.089 1    20.225  ? 333  SER   A O   1 1 
ATOM   2676  C  CB  . SER   A 1  333 ? -3.207  -16.454 -27.298 1    19.28   ? 333  SER   A CB  1 1 
ATOM   2677  O  OG  . SER   A 1  333 ? -3.602  -16.009 -28.593 1    21.912  ? 333  SER   A OG  1 1 
ATOM   2678  N  N   . ALA   A 1  334 ? -2.789  -19.566 -26.966 1    17.158  ? 334  ALA   A N   1 1 
ATOM   2679  C  CA  . ALA   A 1  334 ? -3.271  -20.912 -27.249 1    17.486  ? 334  ALA   A CA  1 1 
ATOM   2680  C  C   . ALA   A 1  334 ? -4.8    -20.955 -27.083 1    18.707  ? 334  ALA   A C   1 1 
ATOM   2681  O  O   . ALA   A 1  334 ? -5.32   -20.406 -26.113 1    19.09   ? 334  ALA   A O   1 1 
ATOM   2682  C  CB  . ALA   A 1  334 ? -2.696  -21.859 -26.236 1    16.798  ? 334  ALA   A CB  1 1 
ATOM   2683  N  N   . TRP   A 1  335 ? -5.461  -21.78  -27.899 1    17.596  ? 335  TRP   A N   1 1 
ATOM   2684  C  CA  . TRP   A 1  335 ? -6.897  -21.695 -28.061 1    19.518  ? 335  TRP   A CA  1 1 
ATOM   2685  C  C   . TRP   A 1  335 ? -7.529  -23.074 -28.01  1    20.158  ? 335  TRP   A C   1 1 
ATOM   2686  O  O   . TRP   A 1  335 ? -7.203  -23.957 -28.8   1    21.023  ? 335  TRP   A O   1 1 
ATOM   2687  C  CB  . TRP   A 1  335 ? -7.259  -21.067 -29.415 1    20.715  ? 335  TRP   A CB  1 1 
ATOM   2688  C  CG  . TRP   A 1  335 ? -6.882  -19.633 -29.535 1    21.639  ? 335  TRP   A CG  1 1 
ATOM   2689  C  CD1 . TRP   A 1  335 ? -5.616  -19.134 -29.583 1    21.569  ? 335  TRP   A CD1 1 1 
ATOM   2690  C  CD2 . TRP   A 1  335 ? -7.78   -18.508 -29.648 1    22.732  ? 335  TRP   A CD2 1 1 
ATOM   2691  N  NE1 . TRP   A 1  335 ? -5.644  -17.771 -29.672 1    21.812  ? 335  TRP   A NE1 1 1 
ATOM   2692  C  CE2 . TRP   A 1  335 ? -6.96   -17.357 -29.701 1    22.26   ? 335  TRP   A CE2 1 1 
ATOM   2693  C  CE3 . TRP   A 1  335 ? -9.175  -18.374 -29.701 1    22.987  ? 335  TRP   A CE3 1 1 
ATOM   2694  C  CZ2 . TRP   A 1  335 ? -7.482  -16.083 -29.852 1    22.174  ? 335  TRP   A CZ2 1 1 
ATOM   2695  C  CZ3 . TRP   A 1  335 ? -9.693  -17.103 -29.809 1    21.893  ? 335  TRP   A CZ3 1 1 
ATOM   2696  C  CH2 . TRP   A 1  335 ? -8.863  -15.983 -29.903 1    23.138  ? 335  TRP   A CH2 1 1 
ATOM   2697  N  N   . ASP   A 1  336 ? -8.43   -23.247 -27.039 1    20.182  ? 336  ASP   A N   1 1 
ATOM   2698  C  CA  . ASP   A 1  336 ? -9.271  -24.422 -26.989 1    20.415  ? 336  ASP   A CA  1 1 
ATOM   2699  C  C   . ASP   A 1  336 ? -10.646 -23.996 -27.521 1    21.645  ? 336  ASP   A C   1 1 
ATOM   2700  O  O   . ASP   A 1  336 ? -11.179 -23.046 -27.007 1    19.515  ? 336  ASP   A O   1 1 
ATOM   2701  C  CB  . ASP   A 1  336 ? -9.349  -24.871 -25.543 1    20.597  ? 336  ASP   A CB  1 1 
ATOM   2702  C  CG  . ASP   A 1  336 ? -9.97   -26.249 -25.355 1    23.843  ? 336  ASP   A CG  1 1 
ATOM   2703  O  OD1 . ASP   A 1  336 ? -10.617 -26.732 -26.317 1    23.321  ? 336  ASP   A OD1 1 1 
ATOM   2704  O  OD2 . ASP   A 1  336 ? -9.799  -26.842 -24.23  1    26.924  ? 336  ASP   A OD2 1 1 
ATOM   2705  N  N   . PHE   A 1  337 ? -11.168 -24.649 -28.578 1    22.127  ? 337  PHE   A N   1 1 
ATOM   2706  C  CA  . PHE   A 1  337 ? -12.493 -24.395 -29.084 1    23.002  ? 337  PHE   A CA  1 1 
ATOM   2707  C  C   . PHE   A 1  337 ? -13.593 -25.177 -28.355 1    24.264  ? 337  PHE   A C   1 1 
ATOM   2708  O  O   . PHE   A 1  337 ? -14.763 -24.985 -28.703 1    25.708  ? 337  PHE   A O   1 1 
ATOM   2709  C  CB  . PHE   A 1  337 ? -12.505 -24.624 -30.612 1    24.594  ? 337  PHE   A CB  1 1 
ATOM   2710  C  CG  . PHE   A 1  337 ? -11.733 -23.535 -31.347 1    24.345  ? 337  PHE   A CG  1 1 
ATOM   2711  C  CD1 . PHE   A 1  337 ? -10.329 -23.496 -31.342 1    23.642  ? 337  PHE   A CD1 1 1 
ATOM   2712  C  CD2 . PHE   A 1  337 ? -12.408 -22.543 -32.042 1    24.653  ? 337  PHE   A CD2 1 1 
ATOM   2713  C  CE1 . PHE   A 1  337 ? -9.642  -22.468 -31.975 1    23.503  ? 337  PHE   A CE1 1 1 
ATOM   2714  C  CE2 . PHE   A 1  337 ? -11.713 -21.533 -32.701 1    25.312  ? 337  PHE   A CE2 1 1 
ATOM   2715  C  CZ  . PHE   A 1  337 ? -10.333 -21.486 -32.662 1    24.607  ? 337  PHE   A CZ  1 1 
ATOM   2716  N  N   . TYR   A 1  338 ? -13.261 -26.075 -27.409 1    24.739  ? 338  TYR   A N   1 1 
ATOM   2717  C  CA  . TYR   A 1  338 ? -14.247 -26.807 -26.615 1    27.207  ? 338  TYR   A CA  1 1 
ATOM   2718  C  C   . TYR   A 1  338 ? -15.103 -27.802 -27.427 1    29.754  ? 338  TYR   A C   1 1 
ATOM   2719  O  O   . TYR   A 1  338 ? -16.175 -28.206 -26.975 1    28.477  ? 338  TYR   A O   1 1 
ATOM   2720  C  CB  . TYR   A 1  338 ? -15.148 -25.837 -25.823 1    27.883  ? 338  TYR   A CB  1 1 
ATOM   2721  C  CG  . TYR   A 1  338 ? -14.313 -25.212 -24.702 1    28.748  ? 338  TYR   A CG  1 1 
ATOM   2722  C  CD1 . TYR   A 1  338 ? -14.174 -25.841 -23.474 1    29.273  ? 338  TYR   A CD1 1 1 
ATOM   2723  C  CD2 . TYR   A 1  338 ? -13.682 -23.982 -24.86  1    30.679  ? 338  TYR   A CD2 1 1 
ATOM   2724  C  CE1 . TYR   A 1  338 ? -13.333 -25.326 -22.497 1    31.849  ? 338  TYR   A CE1 1 1 
ATOM   2725  C  CE2 . TYR   A 1  338 ? -12.876 -23.43  -23.872 1    31.953  ? 338  TYR   A CE2 1 1 
ATOM   2726  C  CZ  . TYR   A 1  338 ? -12.714 -24.109 -22.676 1    32.782  ? 338  TYR   A CZ  1 1 
ATOM   2727  O  OH  . TYR   A 1  338 ? -11.968 -23.597 -21.653 1    38.147  ? 338  TYR   A OH  1 1 
ATOM   2728  N  N   . ASN   A 1  339 ? -14.644 -28.255 -28.595 1    28.498  ? 339  ASN   A N   1 1 
ATOM   2729  C  CA  . ASN   A 1  339 ? -15.409 -29.252 -29.346 1    28.402  ? 339  ASN   A CA  1 1 
ATOM   2730  C  C   . ASN   A 1  339 ? -14.576 -30.524 -29.406 1    28.887  ? 339  ASN   A C   1 1 
ATOM   2731  O  O   . ASN   A 1  339 ? -14.832 -31.438 -30.171 1    30.192  ? 339  ASN   A O   1 1 
ATOM   2732  C  CB  . ASN   A 1  339 ? -15.781 -28.752 -30.742 1    30.195  ? 339  ASN   A CB  1 1 
ATOM   2733  C  CG  . ASN   A 1  339 ? -14.582 -28.489 -31.636 1    28.854  ? 339  ASN   A CG  1 1 
ATOM   2734  O  OD1 . ASN   A 1  339 ? -13.419 -28.6   -31.221 1    26.494  ? 339  ASN   A OD1 1 1 
ATOM   2735  N  ND2 . ASN   A 1  339 ? -14.835 -28.158 -32.894 1    28.379  ? 339  ASN   A ND2 1 1 
ATOM   2736  N  N   . ARG   A 1  340 ? -13.481 -30.526 -28.654 1    28.207  ? 340  ARG   A N   1 1 
ATOM   2737  C  CA  . ARG   A 1  340 ? -12.63  -31.701 -28.531 1    31.471  ? 340  ARG   A CA  1 1 
ATOM   2738  C  C   . ARG   A 1  340 ? -11.882 -32.02  -29.828 1    31.399  ? 340  ARG   A C   1 1 
ATOM   2739  O  O   . ARG   A 1  340 ? -11.264 -33.064 -29.91  1    32.198  ? 340  ARG   A O   1 1 
ATOM   2740  C  CB  . ARG   A 1  340 ? -13.364 -32.947 -28.047 1    36.961  ? 340  ARG   A CB  1 1 
ATOM   2741  C  CG  . ARG   A 1  340 ? -13.871 -32.699 -26.635 1    37.745  ? 340  ARG   A CG  1 1 
ATOM   2742  C  CD  . ARG   A 1  340 ? -14.522 -33.972 -26.188 1    42.65   ? 340  ARG   A CD  1 1 
ATOM   2743  N  NE  . ARG   A 1  340 ? -15.797 -33.812 -26.878 1    50.57   ? 340  ARG   A NE  1 1 
ATOM   2744  C  CZ  . ARG   A 1  340 ? -17.018 -33.907 -26.36  1    58.346  ? 340  ARG   A CZ  1 1 
ATOM   2745  N  NH1 . ARG   A 1  340 ? -17.166 -34.108 -25.049 1    51.994  ? 340  ARG   A NH1 1 1 
ATOM   2746  N  NH2 . ARG   A 1  340 ? -18.069 -33.823 -27.192 1    54.071  ? 340  ARG   A NH2 1 1 
ATOM   2747  N  N   . LYS   A 1  341 ? -11.862 -31.085 -30.782 1    31.133  ? 341  LYS   A N   1 1 
ATOM   2748  C  CA  . LYS   A 1  341 ? -11.309 -31.313 -32.105 1    31.875  ? 341  LYS   A CA  1 1 
ATOM   2749  C  C   . LYS   A 1  341 ? -10.361 -30.181 -32.496 1    29.866  ? 341  LYS   A C   1 1 
ATOM   2750  O  O   . LYS   A 1  341 ? -9.272  -30.463 -32.996 1    29.463  ? 341  LYS   A O   1 1 
ATOM   2751  C  CB  . LYS   A 1  341 ? -12.465 -31.381 -33.117 1    34.995  ? 341  LYS   A CB  1 1 
ATOM   2752  C  CG  . LYS   A 1  341 ? -12.771 -32.775 -33.59  1    47.449  ? 341  LYS   A CG  1 1 
ATOM   2753  C  CD  . LYS   A 1  341 ? -12.791 -33.869 -32.522 1    56.131  ? 341  LYS   A CD  1 1 
ATOM   2754  C  CE  . LYS   A 1  341 ? -13.001 -35.228 -33.136 1    58.649  ? 341  LYS   A CE  1 1 
ATOM   2755  N  NZ  . LYS   A 1  341 ? -13.237 -36.24  -32.106 1    61.672  ? 341  LYS   A NZ  1 1 
ATOM   2756  N  N   . ASP   A 1  342 ? -10.803 -28.922 -32.326 1    27.258  ? 342  ASP   A N   1 1 
ATOM   2757  C  CA  . ASP   A 1  342 ? -10.043 -27.775 -32.778 1    27.366  ? 342  ASP   A CA  1 1 
ATOM   2758  C  C   . ASP   A 1  342 ? -9.225  -27.186 -31.632 1    25.363  ? 342  ASP   A C   1 1 
ATOM   2759  O  O   . ASP   A 1  342 ? -9.753  -26.819 -30.59  1    23.831  ? 342  ASP   A O   1 1 
ATOM   2760  C  CB  . ASP   A 1  342 ? -10.922 -26.694 -33.389 1    28.009  ? 342  ASP   A CB  1 1 
ATOM   2761  C  CG  . ASP   A 1  342 ? -11.504 -27.165 -34.719 1    32.744  ? 342  ASP   A CG  1 1 
ATOM   2762  O  OD1 . ASP   A 1  342 ? -10.735 -27.215 -35.697 1    30.287  ? 342  ASP   A OD1 1 1 
ATOM   2763  O  OD2 . ASP   A 1  342 ? -12.687 -27.553 -34.743 1    33.415  ? 342  ASP   A OD2 1 1 
ATOM   2764  N  N   . PHE   A 1  343 ? -7.922  -27.078 -31.873 1    23.594  ? 343  PHE   A N   1 1 
ATOM   2765  C  CA  . PHE   A 1  343 ? -7.025  -26.493 -30.871 1    21.771  ? 343  PHE   A CA  1 1 
ATOM   2766  C  C   . PHE   A 1  343 ? -5.956  -25.798 -31.701 1    20.845  ? 343  PHE   A C   1 1 
ATOM   2767  O  O   . PHE   A 1  343 ? -5.571  -26.379 -32.711 1    22.677  ? 343  PHE   A O   1 1 
ATOM   2768  C  CB  . PHE   A 1  343 ? -6.272  -27.615 -30.162 1    20.988  ? 343  PHE   A CB  1 1 
ATOM   2769  C  CG  . PHE   A 1  343 ? -7.175  -28.636 -29.488 1    21.08   ? 343  PHE   A CG  1 1 
ATOM   2770  C  CD1 . PHE   A 1  343 ? -7.625  -28.42  -28.183 1    20.504  ? 343  PHE   A CD1 1 1 
ATOM   2771  C  CD2 . PHE   A 1  343 ? -7.603  -29.775 -30.165 1    22.662  ? 343  PHE   A CD2 1 1 
ATOM   2772  C  CE1 . PHE   A 1  343 ? -8.442  -29.344 -27.564 1    20.997  ? 343  PHE   A CE1 1 1 
ATOM   2773  C  CE2 . PHE   A 1  343 ? -8.426  -30.713 -29.536 1    22.761  ? 343  PHE   A CE2 1 1 
ATOM   2774  C  CZ  . PHE   A 1  343 ? -8.809  -30.497 -28.22  1    21.891  ? 343  PHE   A CZ  1 1 
ATOM   2775  N  N   . ARG   A 1  344 ? -5.626  -24.543 -31.383 1    18.141  ? 344  ARG   A N   1 1 
ATOM   2776  C  CA  . ARG   A 1  344 ? -4.857  -23.71  -32.274 1    19.012  ? 344  ARG   A CA  1 1 
ATOM   2777  C  C   . ARG   A 1  344 ? -3.917  -22.802 -31.498 1    18.415  ? 344  ARG   A C   1 1 
ATOM   2778  O  O   . ARG   A 1  344 ? -4.181  -22.467 -30.338 1    18.153  ? 344  ARG   A O   1 1 
ATOM   2779  C  CB  . ARG   A 1  344 ? -5.732  -22.791 -33.127 1    19.327  ? 344  ARG   A CB  1 1 
ATOM   2780  C  CG  . ARG   A 1  344 ? -6.574  -23.563 -34.129 1    21.135  ? 344  ARG   A CG  1 1 
ATOM   2781  C  CD  . ARG   A 1  344 ? -7.418  -22.536 -34.903 1    22.435  ? 344  ARG   A CD  1 1 
ATOM   2782  N  NE  . ARG   A 1  344 ? -8.418  -23.291 -35.649 1    24.705  ? 344  ARG   A NE  1 1 
ATOM   2783  C  CZ  . ARG   A 1  344 ? -9.28   -22.709 -36.495 1    28.412  ? 344  ARG   A CZ  1 1 
ATOM   2784  N  NH1 . ARG   A 1  344 ? -9.361  -21.388 -36.576 1    27.115  ? 344  ARG   A NH1 1 1 
ATOM   2785  N  NH2 . ARG   A 1  344 ? -10.076 -23.45  -37.242 1    29.53   ? 344  ARG   A NH2 1 1 
ATOM   2786  N  N   . ILE   A 1  345 ? -2.813  -22.418 -32.181 1    18.868  ? 345  ILE   A N   1 1 
ATOM   2787  C  CA  . ILE   A 1  345 ? -1.989  -21.368 -31.617 1    17.949  ? 345  ILE   A CA  1 1 
ATOM   2788  C  C   . ILE   A 1  345 ? -2.058  -20.187 -32.583 1    18.194  ? 345  ILE   A C   1 1 
ATOM   2789  O  O   . ILE   A 1  345 ? -2.129  -20.379 -33.787 1    18.892  ? 345  ILE   A O   1 1 
ATOM   2790  C  CB  . ILE   A 1  345 ? -0.536  -21.854 -31.361 1    17.04   ? 345  ILE   A CB  1 1 
ATOM   2791  C  CG1 . ILE   A 1  345 ? -0.48   -22.661 -30.021 1    16.015  ? 345  ILE   A CG1 1 1 
ATOM   2792  C  CG2 . ILE   A 1  345 ? 0.364   -20.617 -31.282 1    15.913  ? 345  ILE   A CG2 1 1 
ATOM   2793  C  CD1 . ILE   A 1  345 ? 0.777   -23.557 -29.82  1    14.999  ? 345  ILE   A CD1 1 1 
ATOM   2794  N  N   . LYS   A 1  346 ? -2.051  -18.977 -32.023 1    18.704  ? 346  LYS   A N   1 1 
ATOM   2795  C  CA  . LYS   A 1  346 ? -1.966  -17.777 -32.826 1    21.545  ? 346  LYS   A CA  1 1 
ATOM   2796  C  C   . LYS   A 1  346 ? -0.692  -17.091 -32.316 1    20.848  ? 346  LYS   A C   1 1 
ATOM   2797  O  O   . LYS   A 1  346 ? -0.681  -16.599 -31.202 1    19.547  ? 346  LYS   A O   1 1 
ATOM   2798  C  CB  . LYS   A 1  346 ? -3.259  -16.945 -32.604 1    21.222  ? 346  LYS   A CB  1 1 
ATOM   2799  C  CG  . LYS   A 1  346 ? -3.167  -15.598 -33.252 1    24.023  ? 346  LYS   A CG  1 1 
ATOM   2800  C  CD  . LYS   A 1  346 ? -4.253  -14.561 -32.939 1    24.549  ? 346  LYS   A CD  1 1 
ATOM   2801  C  CE  . LYS   A 1  346 ? -4.351  -14.088 -31.518 1    26.553  ? 346  LYS   A CE  1 1 
ATOM   2802  N  NZ  . LYS   A 1  346 ? -3.165  -14.148 -30.653 1    26.343  ? 346  LYS   A NZ  1 1 
ATOM   2803  N  N   . GLN   A 1  347 ? 0.361   -17.033 -33.147 1    21.706  ? 347  GLN   A N   1 1 
ATOM   2804  C  CA  . GLN   A 1  347 ? 1.6     -16.429 -32.686 1    21.977  ? 347  GLN   A CA  1 1 
ATOM   2805  C  C   . GLN   A 1  347 ? 2.252   -15.761 -33.905 1    22.644  ? 347  GLN   A C   1 1 
ATOM   2806  O  O   . GLN   A 1  347 ? 2.354   -16.398 -34.966 1    24.37   ? 347  GLN   A O   1 1 
ATOM   2807  C  CB  . GLN   A 1  347 ? 2.523   -17.51  -32.073 1    21.991  ? 347  GLN   A CB  1 1 
ATOM   2808  C  CG  . GLN   A 1  347 ? 3.914   -16.988 -31.697 1    21.565  ? 347  GLN   A CG  1 1 
ATOM   2809  C  CD  . GLN   A 1  347 ? 4.738   -17.965 -30.882 1    20.838  ? 347  GLN   A CD  1 1 
ATOM   2810  O  OE1 . GLN   A 1  347 ? 4.199   -18.913 -30.301 1    20.872  ? 347  GLN   A OE1 1 1 
ATOM   2811  N  NE2 . GLN   A 1  347 ? 6.036   -17.692 -30.752 1    21.053  ? 347  GLN   A NE2 1 1 
ATOM   2812  N  N   . CYS   A 1  348 ? 2.714   -14.495 -33.743 1    20.958  ? 348  CYS   A N   1 1 
ATOM   2813  C  CA  . CYS   A 1  348 ? 3.468   -13.814 -34.781 1    22.725  ? 348  CYS   A CA  1 1 
ATOM   2814  C  C   . CYS   A 1  348 ? 4.942   -14.218 -34.641 1    22.745  ? 348  CYS   A C   1 1 
ATOM   2815  O  O   . CYS   A 1  348 ? 5.791   -13.439 -34.195 1    22.13   ? 348  CYS   A O   1 1 
ATOM   2816  C  CB  . CYS   A 1  348 ? 3.233   -12.304 -34.723 1    26.329  ? 348  CYS   A CB  1 1 
ATOM   2817  S  SG  . CYS   A 1  348 ? 1.502   -11.854 -35.111 1    29.342  ? 348  CYS   A SG  1 1 
ATOM   2818  N  N   . THR   A 1  349 ? 5.227   -15.465 -34.986 1    23.286  ? 349  THR   A N   1 1 
ATOM   2819  C  CA  . THR   A 1  349 ? 6.5     -16.037 -34.563 1    23.158  ? 349  THR   A CA  1 1 
ATOM   2820  C  C   . THR   A 1  349 ? 7.669   -15.342 -35.24  1    22.756  ? 349  THR   A C   1 1 
ATOM   2821  O  O   . THR   A 1  349 ? 7.622   -15.092 -36.428 1    23.422  ? 349  THR   A O   1 1 
ATOM   2822  C  CB  . THR   A 1  349 ? 6.531   -17.518 -34.903 1    24.14   ? 349  THR   A CB  1 1 
ATOM   2823  O  OG1 . THR   A 1  349 ? 5.347   -18.098 -34.381 1    23.754  ? 349  THR   A OG1 1 1 
ATOM   2824  C  CG2 . THR   A 1  349 ? 7.671   -18.213 -34.182 1    25.136  ? 349  THR   A CG2 1 1 
ATOM   2825  N  N   . ARG   A 1  350 ? 8.705   -15.038 -34.457 1    22.878  ? 350  ARG   A N   1 1 
ATOM   2826  C  CA  . ARG   A 1  350 ? 9.977   -14.543 -34.988 1    24.23   ? 350  ARG   A CA  1 1 
ATOM   2827  C  C   . ARG   A 1  350 ? 11.064  -15.572 -34.63  1    24.184  ? 350  ARG   A C   1 1 
ATOM   2828  O  O   . ARG   A 1  350 ? 10.901  -16.352 -33.708 1    20.875  ? 350  ARG   A O   1 1 
ATOM   2829  C  CB  . ARG   A 1  350 ? 10.377  -13.189 -34.381 1    24.635  ? 350  ARG   A CB  1 1 
ATOM   2830  C  CG  . ARG   A 1  350 ? 9.432   -12.054 -34.763 1    29.458  ? 350  ARG   A CG  1 1 
ATOM   2831  C  CD  . ARG   A 1  350 ? 9.647   -10.876 -33.854 1    29.42   ? 350  ARG   A CD  1 1 
ATOM   2832  N  NE  . ARG   A 1  350 ? 9.199   -11.175 -32.492 1    31.163  ? 350  ARG   A NE  1 1 
ATOM   2833  C  CZ  . ARG   A 1  350 ? 9.964   -11.241 -31.44  1    30.73   ? 350  ARG   A CZ  1 1 
ATOM   2834  N  NH1 . ARG   A 1  350 ? 11.28   -11.076 -31.552 1    29.413  ? 350  ARG   A NH1 1 1 
ATOM   2835  N  NH2 . ARG   A 1  350 ? 9.405   -11.536 -30.3   1    33.958  ? 350  ARG   A NH2 1 1 
ATOM   2836  N  N   . VAL   A 1  351 ? 12.115  -15.62  -35.436 1    25.954  ? 351  VAL   A N   1 1 
ATOM   2837  C  CA  . VAL   A 1  351 ? 13.135  -16.653 -35.304 1    27.862  ? 351  VAL   A CA  1 1 
ATOM   2838  C  C   . VAL   A 1  351 ? 14.194  -16.154 -34.325 1    26.674  ? 351  VAL   A C   1 1 
ATOM   2839  O  O   . VAL   A 1  351 ? 15.165  -15.476 -34.712 1    28.847  ? 351  VAL   A O   1 1 
ATOM   2840  C  CB  . VAL   A 1  351 ? 13.74   -16.985 -36.674 1    27.387  ? 351  VAL   A CB  1 1 
ATOM   2841  C  CG1 . VAL   A 1  351 ? 14.722  -18.165 -36.577 1    28.519  ? 351  VAL   A CG1 1 1 
ATOM   2842  C  CG2 . VAL   A 1  351 ? 12.641  -17.348 -37.667 1    30.136  ? 351  VAL   A CG2 1 1 
ATOM   2843  N  N   . THR   A 1  352 ? 13.989  -16.531 -33.066 1    25.389  ? 352  THR   A N   1 1 
ATOM   2844  C  CA  . THR   A 1  352 ? 14.862  -16.167 -31.963 1    25.775  ? 352  THR   A CA  1 1 
ATOM   2845  C  C   . THR   A 1  352 ? 14.787  -17.305 -30.937 1    24.225  ? 352  THR   A C   1 1 
ATOM   2846  O  O   . THR   A 1  352 ? 13.758  -17.981 -30.802 1    20.58   ? 352  THR   A O   1 1 
ATOM   2847  C  CB  . THR   A 1  352 ? 14.49   -14.84  -31.27  1    26.095  ? 352  THR   A CB  1 1 
ATOM   2848  O  OG1 . THR   A 1  352 ? 13.352  -15.072 -30.423 1    26.128  ? 352  THR   A OG1 1 1 
ATOM   2849  C  CG2 . THR   A 1  352 ? 14.368  -13.604 -32.154 1    26.52   ? 352  THR   A CG2 1 1 
ATOM   2850  N  N   . MET   A 1  353 ? 15.83   -17.406 -30.103 1    23.386  ? 353  MET   A N   1 1 
ATOM   2851  C  CA  . MET   A 1  353 ? 15.825  -18.349 -28.987 1    23.647  ? 353  MET   A CA  1 1 
ATOM   2852  C  C   . MET   A 1  353 ? 14.654  -18.078 -28.022 1    24.384  ? 353  MET   A C   1 1 
ATOM   2853  O  O   . MET   A 1  353 ? 13.943  -19.01  -27.622 1    22.851  ? 353  MET   A O   1 1 
ATOM   2854  C  CB  . MET   A 1  353 ? 17.198  -18.362 -28.283 1    25.263  ? 353  MET   A CB  1 1 
ATOM   2855  C  CG  . MET   A 1  353 ? 17.26   -19.392 -27.168 1    28.586  ? 353  MET   A CG  1 1 
ATOM   2856  S  SD  . MET   A 1  353 ? 18.957  -19.302 -26.544 1    33.422  ? 353  MET   A SD  1 1 
ATOM   2857  C  CE  . MET   A 1  353 ? 18.881  -20.959 -25.828 1    34.952  ? 353  MET   A CE  1 1 
ATOM   2858  N  N   . ASP   A 1  354 ? 14.389  -16.822 -27.633 1    24.766  ? 354  ASP   A N   1 1 
ATOM   2859  C  CA  . ASP   A 1  354 ? 13.269  -16.655 -26.697 1    23.898  ? 354  ASP   A CA  1 1 
ATOM   2860  C  C   . ASP   A 1  354 ? 11.907  -17.02  -27.321 1    20.622  ? 354  ASP   A C   1 1 
ATOM   2861  O  O   . ASP   A 1  354 ? 10.988  -17.435 -26.622 1    18.217  ? 354  ASP   A O   1 1 
ATOM   2862  C  CB  . ASP   A 1  354 ? 13.194  -15.289 -26.042 1    27.963  ? 354  ASP   A CB  1 1 
ATOM   2863  C  CG  . ASP   A 1  354 ? 12.905  -14.173 -27.03  1    37.512  ? 354  ASP   A CG  1 1 
ATOM   2864  O  OD1 . ASP   A 1  354 ? 13.869  -13.706 -27.69  1    41.09   ? 354  ASP   A OD1 1 1 
ATOM   2865  O  OD2 . ASP   A 1  354 ? 11.702  -13.802 -27.155 1    49.171  ? 354  ASP   A OD2 1 1 
ATOM   2866  N  N   . GLN   A 1  355 ? 11.757  -16.797 -28.615 1    19.592  ? 355  GLN   A N   1 1 
ATOM   2867  C  CA  . GLN   A 1  355 ? 10.54   -17.222 -29.308 1    20.145  ? 355  GLN   A CA  1 1 
ATOM   2868  C  C   . GLN   A 1  355 ? 10.395  -18.739 -29.337 1    19.154  ? 355  GLN   A C   1 1 
ATOM   2869  O  O   . GLN   A 1  355 ? 9.29    -19.258 -29.224 1    17.933  ? 355  GLN   A O   1 1 
ATOM   2870  C  CB  . GLN   A 1  355 ? 10.507  -16.662 -30.733 1    21.174  ? 355  GLN   A CB  1 1 
ATOM   2871  C  CG  . GLN   A 1  355 ? 10.11   -15.188 -30.692 1    22.343  ? 355  GLN   A CG  1 1 
ATOM   2872  C  CD  . GLN   A 1  355 ? 8.592   -15.011 -30.624 1    23.332  ? 355  GLN   A CD  1 1 
ATOM   2873  O  OE1 . GLN   A 1  355 ? 7.903   -15.366 -31.573 1    22.374  ? 355  GLN   A OE1 1 1 
ATOM   2874  N  NE2 . GLN   A 1  355 ? 8.054   -14.583 -29.484 1    21.013  ? 355  GLN   A NE2 1 1 
ATOM   2875  N  N   . LEU   A 1  356 ? 11.521  -19.467 -29.449 1    18.212  ? 356  LEU   A N   1 1 
ATOM   2876  C  CA  . LEU   A 1  356 ? 11.456  -20.901 -29.317 1    18.097  ? 356  LEU   A CA  1 1 
ATOM   2877  C  C   . LEU   A 1  356 ? 10.903  -21.262 -27.932 1    17.385  ? 356  LEU   A C   1 1 
ATOM   2878  O  O   . LEU   A 1  356 ? 10.086  -22.169 -27.835 1    17.78   ? 356  LEU   A O   1 1 
ATOM   2879  C  CB  . LEU   A 1  356 ? 12.858  -21.473 -29.491 1    18.816  ? 356  LEU   A CB  1 1 
ATOM   2880  C  CG  . LEU   A 1  356 ? 12.886  -23.001 -29.563 1    20.04   ? 356  LEU   A CG  1 1 
ATOM   2881  C  CD1 . LEU   A 1  356 ? 12.041  -23.577 -30.759 1    21.259  ? 356  LEU   A CD1 1 1 
ATOM   2882  C  CD2 . LEU   A 1  356 ? 14.404  -23.344 -29.639 1    20.78   ? 356  LEU   A CD2 1 1 
ATOM   2883  N  N   A SER   A 1  357 ? 11.321  -20.552 -26.86  0.82 17.187  ? 357  SER   A N   1 1 
ATOM   2884  N  N   B SER   A 1  357 ? 11.344  -20.534 -26.893 0.18 17.098  ? 357  SER   A N   1 1 
ATOM   2885  C  CA  A SER   A 1  357 ? 10.73   -20.784 -25.546 0.82 16.099  ? 357  SER   A CA  1 1 
ATOM   2886  C  CA  B SER   A 1  357 ? 10.796  -20.643 -25.549 0.18 16.398  ? 357  SER   A CA  1 1 
ATOM   2887  C  C   A SER   A 1  357 ? 9.228   -20.466 -25.519 0.82 16.189  ? 357  SER   A C   1 1 
ATOM   2888  C  C   B SER   A 1  357 ? 9.279   -20.476 -25.564 0.18 16.41   ? 357  SER   A C   1 1 
ATOM   2889  O  O   A SER   A 1  357 ? 8.463   -21.197 -24.905 0.82 15.271  ? 357  SER   A O   1 1 
ATOM   2890  O  O   B SER   A 1  357 ? 8.552   -21.338 -25.076 0.18 16.123  ? 357  SER   A O   1 1 
ATOM   2891  C  CB  A SER   A 1  357 ? 11.471  -20.07  -24.38  0.82 17.205  ? 357  SER   A CB  1 1 
ATOM   2892  C  CB  B SER   A 1  357 ? 11.412  -19.627 -24.61  0.18 16.169  ? 357  SER   A CB  1 1 
ATOM   2893  O  OG  A SER   A 1  357 ? 12.809  -20.563 -24.286 0.82 17.981  ? 357  SER   A OG  1 1 
ATOM   2894  O  OG  B SER   A 1  357 ? 10.467  -19.263 -23.612 0.18 15.492  ? 357  SER   A OG  1 1 
ATOM   2895  N  N   . THR   A 1  358 ? 8.83    -19.329 -26.081 1    16.521  ? 358  THR   A N   1 1 
ATOM   2896  C  CA  . THR   A 1  358 ? 7.413   -19.01  -26.196 1    17.583  ? 358  THR   A CA  1 1 
ATOM   2897  C  C   . THR   A 1  358 ? 6.648   -20.111 -26.958 1    16.936  ? 358  THR   A C   1 1 
ATOM   2898  O  O   . THR   A 1  358 ? 5.518   -20.347 -26.608 1    16.821  ? 358  THR   A O   1 1 
ATOM   2899  C  CB  . THR   A 1  358 ? 7.203   -17.664 -26.905 1    18.592  ? 358  THR   A CB  1 1 
ATOM   2900  O  OG1 . THR   A 1  358 ? 7.812   -16.713 -26.043 1    19.492  ? 358  THR   A OG1 1 1 
ATOM   2901  C  CG2 . THR   A 1  358 ? 5.729   -17.24  -26.967 1    19.69   ? 358  THR   A CG2 1 1 
ATOM   2902  N  N   . VAL   A 1  359 ? 7.174   -20.636 -28.079 1    18.128  ? 359  VAL   A N   1 1 
ATOM   2903  C  CA  . VAL   A 1  359 ? 6.555   -21.764 -28.804 1    17.721  ? 359  VAL   A CA  1 1 
ATOM   2904  C  C   . VAL   A 1  359 ? 6.245   -22.93  -27.854 1    16.648  ? 359  VAL   A C   1 1 
ATOM   2905  O  O   . VAL   A 1  359 ? 5.105   -23.417 -27.798 1    15.495  ? 359  VAL   A O   1 1 
ATOM   2906  C  CB  . VAL   A 1  359 ? 7.35    -22.206 -30.055 1    18.917  ? 359  VAL   A CB  1 1 
ATOM   2907  C  CG1 . VAL   A 1  359 ? 6.805   -23.5   -30.663 1    18.432  ? 359  VAL   A CG1 1 1 
ATOM   2908  C  CG2 . VAL   A 1  359 ? 7.334   -21.075 -31.09  1    18.19   ? 359  VAL   A CG2 1 1 
ATOM   2909  N  N   . HIS   A 1  360 ? 7.212   -23.288 -26.994 1    15.629  ? 360  HIS   A N   1 1 
ATOM   2910  C  CA  . HIS   A 1  360 ? 7.023   -24.356 -26.008 1    15.773  ? 360  HIS   A CA  1 1 
ATOM   2911  C  C   . HIS   A 1  360 ? 5.955   -23.974 -24.967 1    15.185  ? 360  HIS   A C   1 1 
ATOM   2912  O  O   . HIS   A 1  360 ? 5.164   -24.818 -24.573 1    14.074  ? 360  HIS   A O   1 1 
ATOM   2913  C  CB  . HIS   A 1  360 ? 8.341   -24.748 -25.293 1    16.219  ? 360  HIS   A CB  1 1 
ATOM   2914  C  CG  . HIS   A 1  360 ? 9.278   -25.527 -26.166 1    18.635  ? 360  HIS   A CG  1 1 
ATOM   2915  N  ND1 . HIS   A 1  360 ? 10.067  -24.935 -27.147 1    20.42   ? 360  HIS   A ND1 1 1 
ATOM   2916  C  CD2 . HIS   A 1  360 ? 9.533   -26.854 -26.235 1    19.557  ? 360  HIS   A CD2 1 1 
ATOM   2917  C  CE1 . HIS   A 1  360 ? 10.802  -25.868 -27.77  1    19.884  ? 360  HIS   A CE1 1 1 
ATOM   2918  N  NE2 . HIS   A 1  360 ? 10.46   -27.045 -27.24  1    20.813  ? 360  HIS   A NE2 1 1 
ATOM   2919  N  N   . HIS   A 1  361 ? 5.978   -22.724 -24.507 1    14.83   ? 361  HIS   A N   1 1 
ATOM   2920  C  CA  . HIS   A 1  361 ? 5.022   -22.236 -23.528 1    15.982  ? 361  HIS   A CA  1 1 
ATOM   2921  C  C   . HIS   A 1  361 ? 3.6     -22.469 -24.086 1    16.165  ? 361  HIS   A C   1 1 
ATOM   2922  O  O   . HIS   A 1  361 ? 2.718   -22.995 -23.384 1    15.351  ? 361  HIS   A O   1 1 
ATOM   2923  C  CB  . HIS   A 1  361 ? 5.306   -20.752 -23.24  1    15.336  ? 361  HIS   A CB  1 1 
ATOM   2924  C  CG  . HIS   A 1  361 ? 4.284   -20.228 -22.259 1    15.902  ? 361  HIS   A CG  1 1 
ATOM   2925  N  ND1 . HIS   A 1  361 ? 4.367   -20.248 -20.862 1    15.559  ? 361  HIS   A ND1 1 1 
ATOM   2926  C  CD2 . HIS   A 1  361 ? 3.075   -19.678 -22.555 1    17.092  ? 361  HIS   A CD2 1 1 
ATOM   2927  C  CE1 . HIS   A 1  361 ? 3.201   -19.779 -20.358 1    16.402  ? 361  HIS   A CE1 1 1 
ATOM   2928  N  NE2 . HIS   A 1  361 ? 2.453   -19.399 -21.336 1    16.377  ? 361  HIS   A NE2 1 1 
ATOM   2929  N  N   . GLU   A 1  362 ? 3.389   -22.044 -25.342 1    16.254  ? 362  GLU   A N   1 1 
ATOM   2930  C  CA  . GLU   A 1  362 ? 2.047   -22.048 -25.925 1    17.575  ? 362  GLU   A CA  1 1 
ATOM   2931  C  C   . GLU   A 1  362 ? 1.666   -23.504 -26.238 1    17.99   ? 362  GLU   A C   1 1 
ATOM   2932  O  O   . GLU   A 1  362 ? 0.517   -23.93  -26.058 1    17.414  ? 362  GLU   A O   1 1 
ATOM   2933  C  CB  . GLU   A 1  362 ? 1.983   -21.264 -27.245 1    17.806  ? 362  GLU   A CB  1 1 
ATOM   2934  C  CG  . GLU   A 1  362 ? 2.218   -19.767 -27.098 1    19.912  ? 362  GLU   A CG  1 1 
ATOM   2935  C  CD  . GLU   A 1  362 ? 1.339   -19.064 -26.054 1    23.65   ? 362  GLU   A CD  1 1 
ATOM   2936  O  OE1 . GLU   A 1  362 ? 0.108   -19.352 -25.828 1    21.979  ? 362  GLU   A OE1 1 1 
ATOM   2937  O  OE2 . GLU   A 1  362 ? 1.964   -18.146 -25.478 1    24.041  ? 362  GLU   A OE2 1 1 
ATOM   2938  N  N   . MET   A 1  363 ? 2.638   -24.285 -26.705 1    16.492  ? 363  MET   A N   1 1 
ATOM   2939  C  CA  . MET   A 1  363 ? 2.366   -25.711 -26.928 1    17.683  ? 363  MET   A CA  1 1 
ATOM   2940  C  C   . MET   A 1  363 ? 2.07    -26.468 -25.633 1    15.344  ? 363  MET   A C   1 1 
ATOM   2941  O  O   . MET   A 1  363 ? 1.355   -27.465 -25.66  1    15.634  ? 363  MET   A O   1 1 
ATOM   2942  C  CB  . MET   A 1  363 ? 3.464   -26.393 -27.741 1    18.634  ? 363  MET   A CB  1 1 
ATOM   2943  C  CG  . MET   A 1  363 ? 2.996   -27.712 -28.37  1    24.045  ? 363  MET   A CG  1 1 
ATOM   2944  S  SD  . MET   A 1  363 ? 4.22    -28.378 -29.542 1    26.073  ? 363  MET   A SD  1 1 
ATOM   2945  C  CE  . MET   A 1  363 ? 3.904   -27.121 -30.796 1    26.399  ? 363  MET   A CE  1 1 
ATOM   2946  N  N   . GLY   A 1  364 ? 2.62    -26.031 -24.471 1    14.234  ? 364  GLY   A N   1 1 
ATOM   2947  C  CA  . GLY   A 1  364 ? 2.215   -26.627 -23.208 1    13.094  ? 364  GLY   A CA  1 1 
ATOM   2948  C  C   . GLY   A 1  364 ? 0.693   -26.449 -22.944 1    14.167  ? 364  GLY   A C   1 1 
ATOM   2949  O  O   . GLY   A 1  364 ? 0.034   -27.329 -22.419 1    13.941  ? 364  GLY   A O   1 1 
ATOM   2950  N  N   . HIS   A 1  365 ? 0.176   -25.265 -23.218 1    13.761  ? 365  HIS   A N   1 1 
ATOM   2951  C  CA  . HIS   A 1  365 ? -1.271  -25.01  -23.158 1    15.181  ? 365  HIS   A CA  1 1 
ATOM   2952  C  C   . HIS   A 1  365 ? -2.014  -26.034 -24.038 1    16.089  ? 365  HIS   A C   1 1 
ATOM   2953  O  O   . HIS   A 1  365 ? -2.981  -26.699 -23.598 1    17.343  ? 365  HIS   A O   1 1 
ATOM   2954  C  CB  . HIS   A 1  365 ? -1.553  -23.545 -23.538 1    15.606  ? 365  HIS   A CB  1 1 
ATOM   2955  C  CG  . HIS   A 1  365 ? -1.116  -22.46  -22.599 1    16.843  ? 365  HIS   A CG  1 1 
ATOM   2956  N  ND1 . HIS   A 1  365 ? -1.358  -22.602 -21.243 1    18.455  ? 365  HIS   A ND1 1 1 
ATOM   2957  C  CD2 . HIS   A 1  365 ? -0.528  -21.263 -22.737 1    17.74   ? 365  HIS   A CD2 1 1 
ATOM   2958  C  CE1 . HIS   A 1  365 ? -0.971  -21.506 -20.609 1    17.518  ? 365  HIS   A CE1 1 1 
ATOM   2959  N  NE2 . HIS   A 1  365 ? -0.408  -20.7   -21.479 1    18.395  ? 365  HIS   A NE2 1 1 
ATOM   2960  N  N   . ILE   A 1  366 ? -1.598  -26.133 -25.307 1    15.57   ? 366  ILE   A N   1 1 
ATOM   2961  C  CA  . ILE   A 1  366 ? -2.274  -27.06  -26.203 1    16.839  ? 366  ILE   A CA  1 1 
ATOM   2962  C  C   . ILE   A 1  366 ? -2.229  -28.481 -25.645 1    17.419  ? 366  ILE   A C   1 1 
ATOM   2963  O  O   . ILE   A 1  366 ? -3.228  -29.204 -25.728 1    17.662  ? 366  ILE   A O   1 1 
ATOM   2964  C  CB  . ILE   A 1  366 ? -1.69   -27.032 -27.63  1    17.749  ? 366  ILE   A CB  1 1 
ATOM   2965  C  CG1 . ILE   A 1  366 ? -1.845  -25.611 -28.305 1    18.117  ? 366  ILE   A CG1 1 1 
ATOM   2966  C  CG2 . ILE   A 1  366 ? -2.342  -28.172 -28.454 1    19.517  ? 366  ILE   A CG2 1 1 
ATOM   2967  C  CD1 . ILE   A 1  366 ? -3.307  -25.171 -28.607 1    18.448  ? 366  ILE   A CD1 1 1 
ATOM   2968  N  N   . GLN   A 1  367 ? -1.05   -28.937 -25.156 1    16.361  ? 367  GLN   A N   1 1 
ATOM   2969  C  CA  . GLN   A 1  367 ? -0.953  -30.29  -24.642 1    16.683  ? 367  GLN   A CA  1 1 
ATOM   2970  C  C   . GLN   A 1  367 ? -1.953  -30.514 -23.485 1    18.236  ? 367  GLN   A C   1 1 
ATOM   2971  O  O   . GLN   A 1  367 ? -2.538  -31.592 -23.408 1    17.993  ? 367  GLN   A O   1 1 
ATOM   2972  C  CB  . GLN   A 1  367 ? 0.472   -30.57  -24.145 1    16.353  ? 367  GLN   A CB  1 1 
ATOM   2973  C  CG  . GLN   A 1  367 ? 0.716   -32.05  -23.869 1    18.265  ? 367  GLN   A CG  1 1 
ATOM   2974  C  CD  . GLN   A 1  367 ? 0.547   -32.979 -25.049 1    20.967  ? 367  GLN   A CD  1 1 
ATOM   2975  O  OE1 . GLN   A 1  367 ? -0.058  -34.046 -24.903 1    21.876  ? 367  GLN   A OE1 1 1 
ATOM   2976  N  NE2 . GLN   A 1  367 ? 1.109   -32.631 -26.213 1    20.823  ? 367  GLN   A NE2 1 1 
ATOM   2977  N  N   . TYR   A 1  368 ? -2.113  -29.528 -22.57  1    16.564  ? 368  TYR   A N   1 1 
ATOM   2978  C  CA  . TYR   A 1  368 ? -3.08   -29.651 -21.482 1    18.125  ? 368  TYR   A CA  1 1 
ATOM   2979  C  C   . TYR   A 1  368 ? -4.491  -29.819 -22.074 1    18.456  ? 368  TYR   A C   1 1 
ATOM   2980  O  O   . TYR   A 1  368 ? -5.219  -30.719 -21.691 1    19.908  ? 368  TYR   A O   1 1 
ATOM   2981  C  CB  . TYR   A 1  368 ? -3.084  -28.321 -20.718 1    17.096  ? 368  TYR   A CB  1 1 
ATOM   2982  C  CG  . TYR   A 1  368 ? -3.075  -28.464 -19.213 1    17.164  ? 368  TYR   A CG  1 1 
ATOM   2983  C  CD1 . TYR   A 1  368 ? -3.818  -29.443 -18.559 1    17.84   ? 368  TYR   A CD1 1 1 
ATOM   2984  C  CD2 . TYR   A 1  368 ? -2.331  -27.588 -18.47  1    16.803  ? 368  TYR   A CD2 1 1 
ATOM   2985  C  CE1 . TYR   A 1  368 ? -3.839  -29.523 -17.174 1    18.4    ? 368  TYR   A CE1 1 1 
ATOM   2986  C  CE2 . TYR   A 1  368 ? -2.304  -27.682 -17.096 1    17.594  ? 368  TYR   A CE2 1 1 
ATOM   2987  C  CZ  . TYR   A 1  368 ? -3.062  -28.637 -16.449 1    18.669  ? 368  TYR   A CZ  1 1 
ATOM   2988  O  OH  . TYR   A 1  368 ? -3.029  -28.663 -15.092 1    18.686  ? 368  TYR   A OH  1 1 
ATOM   2989  N  N   . TYR   A 1  369 ? -4.836  -29.01  -23.056 1    18.394  ? 369  TYR   A N   1 1 
ATOM   2990  C  CA  . TYR   A 1  369 ? -6.195  -29.083 -23.606 1    18.81   ? 369  TYR   A CA  1 1 
ATOM   2991  C  C   . TYR   A 1  369 ? -6.421  -30.444 -24.269 1    19.861  ? 369  TYR   A C   1 1 
ATOM   2992  O  O   . TYR   A 1  369 ? -7.499  -31.029 -24.194 1    19.414  ? 369  TYR   A O   1 1 
ATOM   2993  C  CB  . TYR   A 1  369 ? -6.375  -28.138 -24.777 1    17.757  ? 369  TYR   A CB  1 1 
ATOM   2994  C  CG  . TYR   A 1  369 ? -6.109  -26.665 -24.57  1    16.926  ? 369  TYR   A CG  1 1 
ATOM   2995  C  CD1 . TYR   A 1  369 ? -6.266  -26.089 -23.325 1    15.822  ? 369  TYR   A CD1 1 1 
ATOM   2996  C  CD2 . TYR   A 1  369 ? -5.754  -25.867 -25.669 1    16.697  ? 369  TYR   A CD2 1 1 
ATOM   2997  C  CE1 . TYR   A 1  369 ? -6.036  -24.745 -23.16  1    15.889  ? 369  TYR   A CE1 1 1 
ATOM   2998  C  CE2 . TYR   A 1  369 ? -5.56   -24.501 -25.506 1    17.004  ? 369  TYR   A CE2 1 1 
ATOM   2999  C  CZ  . TYR   A 1  369 ? -5.7    -23.95  -24.242 1    17.05   ? 369  TYR   A CZ  1 1 
ATOM   3000  O  OH  . TYR   A 1  369 ? -5.51   -22.632 -24.01  1    18.771  ? 369  TYR   A OH  1 1 
ATOM   3001  N  N   . LEU   A 1  370 ? -5.386  -30.983 -24.941 1    20.532  ? 370  LEU   A N   1 1 
ATOM   3002  C  CA  . LEU   A 1  370 ? -5.466  -32.326 -25.53  1    21.011  ? 370  LEU   A CA  1 1 
ATOM   3003  C  C   . LEU   A 1  370 ? -5.657  -33.4   -24.466 1    21.487  ? 370  LEU   A C   1 1 
ATOM   3004  O  O   . LEU   A 1  370 ? -6.311  -34.413 -24.73  1    22.563  ? 370  LEU   A O   1 1 
ATOM   3005  C  CB  . LEU   A 1  370 ? -4.245  -32.718 -26.381 1    20.994  ? 370  LEU   A CB  1 1 
ATOM   3006  C  CG  . LEU   A 1  370 ? -3.893  -31.748 -27.519 1    21.57   ? 370  LEU   A CG  1 1 
ATOM   3007  C  CD1 . LEU   A 1  370 ? -2.585  -32.134 -28.202 1    20.3    ? 370  LEU   A CD1 1 1 
ATOM   3008  C  CD2 . LEU   A 1  370 ? -5.027  -31.85  -28.514 1    21.824  ? 370  LEU   A CD2 1 1 
ATOM   3009  N  N   . GLN   A 1  371 ? -4.992  -33.257 -23.309 1    19.115  ? 371  GLN   A N   1 1 
ATOM   3010  C  CA  . GLN   A 1  371 ? -5.091  -34.334 -22.339 1    20.329  ? 371  GLN   A CA  1 1 
ATOM   3011  C  C   . GLN   A 1  371 ? -6.413  -34.3   -21.549 1    20.292  ? 371  GLN   A C   1 1 
ATOM   3012  O  O   . GLN   A 1  371 ? -6.875  -35.334 -21.092 1    21.112  ? 371  GLN   A O   1 1 
ATOM   3013  C  CB  . GLN   A 1  371 ? -3.923  -34.267 -21.364 1    22.277  ? 371  GLN   A CB  1 1 
ATOM   3014  C  CG  . GLN   A 1  371 ? -2.592  -34.536 -22.055 1    22.062  ? 371  GLN   A CG  1 1 
ATOM   3015  C  CD  . GLN   A 1  371 ? -2.471  -35.944 -22.563 1    24.203  ? 371  GLN   A CD  1 1 
ATOM   3016  O  OE1 . GLN   A 1  371 ? -3.126  -36.893 -22.107 1    25.996  ? 371  GLN   A OE1 1 1 
ATOM   3017  N  NE2 . GLN   A 1  371 ? -1.583  -36.104 -23.522 1    26.949  ? 371  GLN   A NE2 1 1 
ATOM   3018  N  N   . TYR   A 1  372 ? -7.044  -33.149 -21.427 1    20.462  ? 372  TYR   A N   1 1 
ATOM   3019  C  CA  . TYR   A 1  372 ? -8.256  -33.097 -20.603 1    22.784  ? 372  TYR   A CA  1 1 
ATOM   3020  C  C   . TYR   A 1  372 ? -9.533  -32.987 -21.427 1    24.239  ? 372  TYR   A C   1 1 
ATOM   3021  O  O   . TYR   A 1  372 ? -10.61  -32.719 -20.862 1    23.368  ? 372  TYR   A O   1 1 
ATOM   3022  C  CB  . TYR   A 1  372 ? -8.219  -32.002 -19.533 1    20.277  ? 372  TYR   A CB  1 1 
ATOM   3023  C  CG  . TYR   A 1  372 ? -8.027  -30.529 -19.814 1    19.072  ? 372  TYR   A CG  1 1 
ATOM   3024  C  CD1 . TYR   A 1  372 ? -8.703  -29.833 -20.808 1    17.952  ? 372  TYR   A CD1 1 1 
ATOM   3025  C  CD2 . TYR   A 1  372 ? -7.199  -29.804 -18.963 1    17.727  ? 372  TYR   A CD2 1 1 
ATOM   3026  C  CE1 . TYR   A 1  372 ? -8.523  -28.464 -20.991 1    17.894  ? 372  TYR   A CE1 1 1 
ATOM   3027  C  CE2 . TYR   A 1  372 ? -7.016  -28.432 -19.129 1    17.061  ? 372  TYR   A CE2 1 1 
ATOM   3028  C  CZ  . TYR   A 1  372 ? -7.679  -27.762 -20.126 1    17.31   ? 372  TYR   A CZ  1 1 
ATOM   3029  O  OH  . TYR   A 1  372 ? -7.501  -26.417 -20.254 1    18.071  ? 372  TYR   A OH  1 1 
ATOM   3030  N  N   . LYS   A 1  373 ? -9.413  -33.188 -22.75  1    25.01   ? 373  LYS   A N   1 1 
ATOM   3031  C  CA  . LYS   A 1  373 ? -10.492 -32.823 -23.666 1    25.984  ? 373  LYS   A CA  1 1 
ATOM   3032  C  C   . LYS   A 1  373 ? -11.762 -33.625 -23.353 1    28.207  ? 373  LYS   A C   1 1 
ATOM   3033  O  O   . LYS   A 1  373 ? -12.882 -33.207 -23.745 1    28.881  ? 373  LYS   A O   1 1 
ATOM   3034  C  CB  . LYS   A 1  373 ? -10.159 -33.014 -25.155 1    25.38   ? 373  LYS   A CB  1 1 
ATOM   3035  C  CG  . LYS   A 1  373 ? -9.773  -34.437 -25.564 1    27.091  ? 373  LYS   A CG  1 1 
ATOM   3036  C  CD  . LYS   A 1  373 ? -9.469  -34.412 -27.065 1    29.175  ? 373  LYS   A CD  1 1 
ATOM   3037  C  CE  . LYS   A 1  373 ? -9.391  -35.723 -27.794 1    32.888  ? 373  LYS   A CE  1 1 
ATOM   3038  N  NZ  . LYS   A 1  373 ? -8.222  -36.252 -27.117 1    35.256  ? 373  LYS   A NZ  1 1 
ATOM   3039  N  N   . ASP   A 1  374 ? -11.573 -34.747 -22.655 1    27.635  ? 374  ASP   A N   1 1 
ATOM   3040  C  CA  . ASP   A 1  374 ? -12.658 -35.672 -22.363 1    35.989  ? 374  ASP   A CA  1 1 
ATOM   3041  C  C   . ASP   A 1  374 ? -13.385 -35.361 -21.039 1    35.244  ? 374  ASP   A C   1 1 
ATOM   3042  O  O   . ASP   A 1  374 ? -14.442 -35.918 -20.761 1    37.664  ? 374  ASP   A O   1 1 
ATOM   3043  C  CB  . ASP   A 1  374 ? -12.241 -37.109 -22.656 1    37.6    ? 374  ASP   A CB  1 1 
ATOM   3044  C  CG  . ASP   A 1  374 ? -12.179 -37.408 -24.15  1    41.932  ? 374  ASP   A CG  1 1 
ATOM   3045  O  OD1 . ASP   A 1  374 ? -13.078 -36.919 -24.891 1    44.825  ? 374  ASP   A OD1 1 1 
ATOM   3046  O  OD2 . ASP   A 1  374 ? -11.246 -38.112 -24.574 1    43.907  ? 374  ASP   A OD2 1 1 
ATOM   3047  N  N   . LEU   A 1  375 ? -12.898 -34.386 -20.275 1    32.31   ? 375  LEU   A N   1 1 
ATOM   3048  C  CA  . LEU   A 1  375 ? -13.575 -34.012 -19.046 1    30.572  ? 375  LEU   A CA  1 1 
ATOM   3049  C  C   . LEU   A 1  375 ? -14.823 -33.193 -19.39  1    31.134  ? 375  LEU   A C   1 1 
ATOM   3050  O  O   . LEU   A 1  375 ? -14.924 -32.559 -20.444 1    28.457  ? 375  LEU   A O   1 1 
ATOM   3051  C  CB  . LEU   A 1  375 ? -12.659 -33.216 -18.101 1    27.825  ? 375  LEU   A CB  1 1 
ATOM   3052  C  CG  . LEU   A 1  375 ? -11.354 -33.928 -17.659 1    26.664  ? 375  LEU   A CG  1 1 
ATOM   3053  C  CD1 . LEU   A 1  375 ? -10.565 -33.082 -16.657 1    25.93   ? 375  LEU   A CD1 1 1 
ATOM   3054  C  CD2 . LEU   A 1  375 ? -11.52  -35.358 -17.188 1    27.178  ? 375  LEU   A CD2 1 1 
ATOM   3055  N  N   . PRO   A 1  376 ? -15.763 -33.068 -18.427 1    32.423  ? 376  PRO   A N   1 1 
ATOM   3056  C  CA  . PRO   A 1  376 ? -16.821 -32.058 -18.507 1    31.539  ? 376  PRO   A CA  1 1 
ATOM   3057  C  C   . PRO   A 1  376 ? -16.263 -30.675 -18.736 1    30.432  ? 376  PRO   A C   1 1 
ATOM   3058  O  O   . PRO   A 1  376 ? -15.262 -30.289 -18.096 1    30.852  ? 376  PRO   A O   1 1 
ATOM   3059  C  CB  . PRO   A 1  376 ? -17.479 -32.163 -17.114 1    33.924  ? 376  PRO   A CB  1 1 
ATOM   3060  C  CG  . PRO   A 1  376 ? -17.333 -33.639 -16.775 1    34.028  ? 376  PRO   A CG  1 1 
ATOM   3061  C  CD  . PRO   A 1  376 ? -15.917 -33.995 -17.289 1    33.855  ? 376  PRO   A CD  1 1 
ATOM   3062  N  N   . VAL   A 1  377 ? -16.926 -29.929 -19.624 1    28.562  ? 377  VAL   A N   1 1 
ATOM   3063  C  CA  . VAL   A 1  377 ? -16.482 -28.588 -19.972 1    30.93   ? 377  VAL   A CA  1 1 
ATOM   3064  C  C   . VAL   A 1  377 ? -16.039 -27.769 -18.753 1    29.666  ? 377  VAL   A C   1 1 
ATOM   3065  O  O   . VAL   A 1  377 ? -15.109 -26.983 -18.904 1    26.732  ? 377  VAL   A O   1 1 
ATOM   3066  C  CB  . VAL   A 1  377 ? -17.485 -27.744 -20.782 1    37.798  ? 377  VAL   A CB  1 1 
ATOM   3067  C  CG1 . VAL   A 1  377 ? -17.387 -28.071 -22.262 1    39.659  ? 377  VAL   A CG1 1 1 
ATOM   3068  C  CG2 . VAL   A 1  377 ? -18.904 -27.921 -20.269 1    35.767  ? 377  VAL   A CG2 1 1 
ATOM   3069  N  N   . SER   A 1  378 ? -16.73  -27.859 -17.597 1    27.714  ? 378  SER   A N   1 1 
ATOM   3070  C  CA  . SER   A 1  378 ? -16.382 -26.947 -16.502 1    26.612  ? 378  SER   A CA  1 1 
ATOM   3071  C  C   . SER   A 1  378 ? -15.004 -27.26  -15.892 1    25.961  ? 378  SER   A C   1 1 
ATOM   3072  O  O   . SER   A 1  378 ? -14.383 -26.383 -15.283 1    25.44   ? 378  SER   A O   1 1 
ATOM   3073  C  CB  . SER   A 1  378 ? -17.42  -26.959 -15.424 1    27.22   ? 378  SER   A CB  1 1 
ATOM   3074  O  OG  . SER   A 1  378 ? -18.683 -26.507 -15.924 1    30.12   ? 378  SER   A OG  1 1 
ATOM   3075  N  N   . LEU   A 1  379 ? -14.567 -28.509 -16.041 1    25.213  ? 379  LEU   A N   1 1 
ATOM   3076  C  CA  . LEU   A 1  379 ? -13.298 -28.961 -15.486 1    25.675  ? 379  LEU   A CA  1 1 
ATOM   3077  C  C   . LEU   A 1  379 ? -12.163 -28.955 -16.509 1    24.98   ? 379  LEU   A C   1 1 
ATOM   3078  O  O   . LEU   A 1  379 ? -11.102 -29.521 -16.23  1    25.807  ? 379  LEU   A O   1 1 
ATOM   3079  C  CB  . LEU   A 1  379 ? -13.59  -30.401 -15.076 1    24.239  ? 379  LEU   A CB  1 1 
ATOM   3080  C  CG  . LEU   A 1  379 ? -14.799 -30.557 -14.143 1    25.414  ? 379  LEU   A CG  1 1 
ATOM   3081  C  CD1 . LEU   A 1  379 ? -14.758 -32.003 -13.678 1    25.181  ? 379  LEU   A CD1 1 1 
ATOM   3082  C  CD2 . LEU   A 1  379 ? -14.655 -29.528 -13.022 1    24.401  ? 379  LEU   A CD2 1 1 
ATOM   3083  N  N   . ARG   A 1  380 ? -12.385 -28.348 -17.67  1    24.686  ? 380  ARG   A N   1 1 
ATOM   3084  C  CA  . ARG   A 1  380 ? -11.338 -28.231 -18.701 1    23.743  ? 380  ARG   A CA  1 1 
ATOM   3085  C  C   . ARG   A 1  380 ? -10.493 -26.997 -18.423 1    21.002  ? 380  ARG   A C   1 1 
ATOM   3086  O  O   . ARG   A 1  380 ? -10.559 -25.984 -19.121 1    21.053  ? 380  ARG   A O   1 1 
ATOM   3087  C  CB  . ARG   A 1  380 ? -11.962 -28.288 -20.112 1    23.663  ? 380  ARG   A CB  1 1 
ATOM   3088  C  CG  . ARG   A 1  380 ? -12.365 -29.716 -20.476 1    25.924  ? 380  ARG   A CG  1 1 
ATOM   3089  C  CD  . ARG   A 1  380 ? -12.928 -29.676 -21.94  1    25.762  ? 380  ARG   A CD  1 1 
ATOM   3090  N  NE  . ARG   A 1  380 ? -13.908 -30.715 -22.246 1    26.952  ? 380  ARG   A NE  1 1 
ATOM   3091  C  CZ  . ARG   A 1  380 ? -14.751 -30.61  -23.279 1    25.72   ? 380  ARG   A CZ  1 1 
ATOM   3092  N  NH1 . ARG   A 1  380 ? -14.584 -29.684 -24.2   1    26.129  ? 380  ARG   A NH1 1 1 
ATOM   3093  N  NH2 . ARG   A 1  380 ? -15.724 -31.461 -23.387 1    25.188  ? 380  ARG   A NH2 1 1 
ATOM   3094  N  N   . ARG   A 1  381 ? -9.705  -27.063 -17.343 1    21.112  ? 381  ARG   A N   1 1 
ATOM   3095  C  CA  . ARG   A 1  381 ? -8.944  -25.917 -16.89  1    21.312  ? 381  ARG   A CA  1 1 
ATOM   3096  C  C   . ARG   A 1  381 ? -7.742  -26.523 -16.163 1    18.894  ? 381  ARG   A C   1 1 
ATOM   3097  O  O   . ARG   A 1  381 ? -7.774  -27.697 -15.888 1    19.885  ? 381  ARG   A O   1 1 
ATOM   3098  C  CB  . ARG   A 1  381 ? -9.714  -25.057 -15.87  1    24.742  ? 381  ARG   A CB  1 1 
ATOM   3099  C  CG  . ARG   A 1  381 ? -10.932 -24.21  -16.253 1    33.682  ? 381  ARG   A CG  1 1 
ATOM   3100  C  CD  . ARG   A 1  381 ? -10.63  -22.866 -16.966 1    39.736  ? 381  ARG   A CD  1 1 
ATOM   3101  N  NE  . ARG   A 1  381 ? -9.827  -23.192 -18.159 1    52.361  ? 381  ARG   A NE  1 1 
ATOM   3102  C  CZ  . ARG   A 1  381 ? -9.185  -22.385 -18.999 1    50.478  ? 381  ARG   A CZ  1 1 
ATOM   3103  N  NH1 . ARG   A 1  381 ? -9.475  -21.094 -19.031 1    47.461  ? 381  ARG   A NH1 1 1 
ATOM   3104  N  NH2 . ARG   A 1  381 ? -8.261  -22.891 -19.814 1    46.797  ? 381  ARG   A NH2 1 1 
ATOM   3105  N  N   . GLY   A 1  382 ? -6.761  -25.725 -15.809 1    18.053  ? 382  GLY   A N   1 1 
ATOM   3106  C  CA  . GLY   A 1  382 ? -5.585  -26.298 -15.148 1    19.051  ? 382  GLY   A CA  1 1 
ATOM   3107  C  C   . GLY   A 1  382 ? -5.995  -26.547 -13.683 1    19.102  ? 382  GLY   A C   1 1 
ATOM   3108  O  O   . GLY   A 1  382 ? -7.044  -26.066 -13.28  1    19.332  ? 382  GLY   A O   1 1 
ATOM   3109  N  N   . ALA   A 1  383 ? -5.223  -27.318 -12.919 1    17.768  ? 383  ALA   A N   1 1 
ATOM   3110  C  CA  . ALA   A 1  383 ? -5.586  -27.533 -11.524 1    19.65   ? 383  ALA   A CA  1 1 
ATOM   3111  C  C   . ALA   A 1  383 ? -5.63   -26.177 -10.783 1    18.769  ? 383  ALA   A C   1 1 
ATOM   3112  O  O   . ALA   A 1  383 ? -6.459  -25.978 -9.926  1    18.696  ? 383  ALA   A O   1 1 
ATOM   3113  C  CB  . ALA   A 1  383 ? -4.681  -28.563 -10.906 1    20.188  ? 383  ALA   A CB  1 1 
ATOM   3114  N  N   . ASN   A 1  384 ? -4.785  -25.209 -11.143 1    16.654  ? 384  ASN   A N   1 1 
ATOM   3115  C  CA  . ASN   A 1  384 ? -5.065  -23.812 -10.875 1    16.615  ? 384  ASN   A CA  1 1 
ATOM   3116  C  C   . ASN   A 1  384 ? -4.522  -23.114 -12.103 1    17.83   ? 384  ASN   A C   1 1 
ATOM   3117  O  O   . ASN   A 1  384 ? -3.888  -23.788 -12.936 1    18.082  ? 384  ASN   A O   1 1 
ATOM   3118  C  CB  . ASN   A 1  384 ? -4.54   -23.357 -9.509  1    16.496  ? 384  ASN   A CB  1 1 
ATOM   3119  C  CG  . ASN   A 1  384 ? -3.027  -23.321 -9.358  1    14.898  ? 384  ASN   A CG  1 1 
ATOM   3120  O  OD1 . ASN   A 1  384 ? -2.323  -22.864 -10.258 1    15.124  ? 384  ASN   A OD1 1 1 
ATOM   3121  N  ND2 . ASN   A 1  384 ? -2.533  -23.638 -8.17   1    15.627  ? 384  ASN   A ND2 1 1 
ATOM   3122  N  N   . PRO   A 1  385 ? -4.729  -21.787 -12.301 1    17.254  ? 385  PRO   A N   1 1 
ATOM   3123  C  CA  . PRO   A 1  385 ? -4.179  -21.163 -13.497 1    16.863  ? 385  PRO   A CA  1 1 
ATOM   3124  C  C   . PRO   A 1  385 ? -2.646  -21.182 -13.64  1    15.938  ? 385  PRO   A C   1 1 
ATOM   3125  O  O   . PRO   A 1  385 ? -2.13   -21.142 -14.763 1    15.311  ? 385  PRO   A O   1 1 
ATOM   3126  C  CB  . PRO   A 1  385 ? -4.739  -19.724 -13.44  1    15.891  ? 385  PRO   A CB  1 1 
ATOM   3127  C  CG  . PRO   A 1  385 ? -6.023  -19.915 -12.607 1    16.647  ? 385  PRO   A CG  1 1 
ATOM   3128  C  CD  . PRO   A 1  385 ? -5.637  -20.903 -11.506 1    16.885  ? 385  PRO   A CD  1 1 
ATOM   3129  N  N   . GLY   A 1  386 ? -1.923  -21.226 -12.51  1    17.613  ? 386  GLY   A N   1 1 
ATOM   3130  C  CA  . GLY   A 1  386 ? -0.467  -21.288 -12.594 1    15.288  ? 386  GLY   A CA  1 1 
ATOM   3131  C  C   . GLY   A 1  386 ? 0.037   -22.622 -13.165 1    15.945  ? 386  GLY   A C   1 1 
ATOM   3132  O  O   . GLY   A 1  386 ? 1.11    -22.638 -13.781 1    16.043  ? 386  GLY   A O   1 1 
ATOM   3133  N  N   . PHE   A 1  387 ? -0.71   -23.699 -12.939 1    15.213  ? 387  PHE   A N   1 1 
ATOM   3134  C  CA  . PHE   A 1  387 ? -0.38   -24.989 -13.544 1    17.437  ? 387  PHE   A CA  1 1 
ATOM   3135  C  C   . PHE   A 1  387 ? -0.393  -24.87  -15.076 1    18.008  ? 387  PHE   A C   1 1 
ATOM   3136  O  O   . PHE   A 1  387 ? 0.485   -25.426 -15.694 1    16.512  ? 387  PHE   A O   1 1 
ATOM   3137  C  CB  . PHE   A 1  387 ? -1.313  -26.147 -13.232 1    16.934  ? 387  PHE   A CB  1 1 
ATOM   3138  C  CG  . PHE   A 1  387 ? -1.086  -26.85  -11.901 1    17.6    ? 387  PHE   A CG  1 1 
ATOM   3139  C  CD1 . PHE   A 1  387 ? -0.979  -26.115 -10.716 1    18.203  ? 387  PHE   A CD1 1 1 
ATOM   3140  C  CD2 . PHE   A 1  387 ? -0.975  -28.228 -11.843 1    18.813  ? 387  PHE   A CD2 1 1 
ATOM   3141  C  CE1 . PHE   A 1  387 ? -0.762  -26.745 -9.519  1    19.506  ? 387  PHE   A CE1 1 1 
ATOM   3142  C  CE2 . PHE   A 1  387 ? -0.806  -28.873 -10.617 1    21.164  ? 387  PHE   A CE2 1 1 
ATOM   3143  C  CZ  . PHE   A 1  387 ? -0.663  -28.112 -9.469  1    20.377  ? 387  PHE   A CZ  1 1 
ATOM   3144  N  N   . HIS   A 1  388 ? -1.439  -24.253 -15.67  1    16.289  ? 388  HIS   A N   1 1 
ATOM   3145  C  CA  . HIS   A 1  388 ? -1.496  -24.188 -17.126 1    17.611  ? 388  HIS   A CA  1 1 
ATOM   3146  C  C   . HIS   A 1  388 ? -0.302  -23.391 -17.629 1    17.661  ? 388  HIS   A C   1 1 
ATOM   3147  O  O   . HIS   A 1  388 ? 0.242   -23.662 -18.686 1    18.566  ? 388  HIS   A O   1 1 
ATOM   3148  C  CB  . HIS   A 1  388 ? -2.808  -23.464 -17.486 1    18.564  ? 388  HIS   A CB  1 1 
ATOM   3149  C  CG  . HIS   A 1  388 ? -3.576  -24.159 -18.533 1    20.174  ? 388  HIS   A CG  1 1 
ATOM   3150  N  ND1 . HIS   A 1  388 ? -3.102  -24.411 -19.812 1    20.291  ? 388  HIS   A ND1 1 1 
ATOM   3151  C  CD2 . HIS   A 1  388 ? -4.866  -24.615 -18.469 1    20.797  ? 388  HIS   A CD2 1 1 
ATOM   3152  C  CE1 . HIS   A 1  388 ? -4.093  -25.01  -20.507 1    21.238  ? 388  HIS   A CE1 1 1 
ATOM   3153  N  NE2 . HIS   A 1  388 ? -5.124  -25.225 -19.672 1    20.719  ? 388  HIS   A NE2 1 1 
ATOM   3154  N  N   . GLU   A 1  389 ? 0.115   -22.364 -16.875 1    16.696  ? 389  GLU   A N   1 1 
ATOM   3155  C  CA  . GLU   A 1  389 ? 1.235   -21.551 -17.313 1    17.037  ? 389  GLU   A CA  1 1 
ATOM   3156  C  C   . GLU   A 1  389 ? 2.575   -22.288 -17.138 1    15.632  ? 389  GLU   A C   1 1 
ATOM   3157  O  O   . GLU   A 1  389 ? 3.561   -21.843 -17.694 1    19.365  ? 389  GLU   A O   1 1 
ATOM   3158  C  CB  . GLU   A 1  389 ? 1.338   -20.217 -16.571 1    16.854  ? 389  GLU   A CB  1 1 
ATOM   3159  C  CG  . GLU   A 1  389 ? 0.085   -19.338 -16.767 1    16.929  ? 389  GLU   A CG  1 1 
ATOM   3160  C  CD  . GLU   A 1  389 ? -0.346  -19.209 -18.228 1    18.619  ? 389  GLU   A CD  1 1 
ATOM   3161  O  OE1 . GLU   A 1  389 ? -1.558  -19.074 -18.598 1    17.398  ? 389  GLU   A OE1 1 1 
ATOM   3162  O  OE2 . GLU   A 1  389 ? 0.599   -19.166 -19.039 1    16.78   ? 389  GLU   A OE2 1 1 
ATOM   3163  N  N   . ALA   A 1  390 ? 2.658   -23.326 -16.321 1    14.284  ? 390  ALA   A N   1 1 
ATOM   3164  C  CA  . ALA   A 1  390 ? 3.983   -23.905 -16.094 1    16.276  ? 390  ALA   A CA  1 1 
ATOM   3165  C  C   . ALA   A 1  390 ? 4.326   -25.071 -17.043 1    16.773  ? 390  ALA   A C   1 1 
ATOM   3166  O  O   . ALA   A 1  390 ? 5.491   -25.483 -17.094 1    16.647  ? 390  ALA   A O   1 1 
ATOM   3167  C  CB  . ALA   A 1  390 ? 4.082   -24.384 -14.666 1    14.773  ? 390  ALA   A CB  1 1 
ATOM   3168  N  N   . ILE   A 1  391 ? 3.351   -25.631 -17.757 1    15.672  ? 391  ILE   A N   1 1 
ATOM   3169  C  CA  . ILE   A 1  391 ? 3.602   -26.893 -18.479 1    16.52   ? 391  ILE   A CA  1 1 
ATOM   3170  C  C   . ILE   A 1  391 ? 4.7     -26.692 -19.537 1    16.641  ? 391  ILE   A C   1 1 
ATOM   3171  O  O   . ILE   A 1  391 ? 5.695   -27.462 -19.62  1    17.394  ? 391  ILE   A O   1 1 
ATOM   3172  C  CB  . ILE   A 1  391 ? 2.32    -27.417 -19.18  1    18.463  ? 391  ILE   A CB  1 1 
ATOM   3173  C  CG1 . ILE   A 1  391 ? 1.183   -27.63  -18.18  1    18.092  ? 391  ILE   A CG1 1 1 
ATOM   3174  C  CG2 . ILE   A 1  391 ? 2.662   -28.711 -19.966 1    18.203  ? 391  ILE   A CG2 1 1 
ATOM   3175  C  CD1 . ILE   A 1  391 ? 1.633   -28.382 -16.918 1    19.412  ? 391  ILE   A CD1 1 1 
ATOM   3176  N  N   . GLY   A 1  392 ? 4.473   -25.735 -20.443 1    15.369  ? 392  GLY   A N   1 1 
ATOM   3177  C  CA  . GLY   A 1  392 ? 5.475   -25.559 -21.519 1    16.831  ? 392  GLY   A CA  1 1 
ATOM   3178  C  C   . GLY   A 1  392 ? 6.837   -25.068 -21.038 1    16.993  ? 392  GLY   A C   1 1 
ATOM   3179  O  O   . GLY   A 1  392 ? 7.916   -25.429 -21.603 1    17.91   ? 392  GLY   A O   1 1 
ATOM   3180  N  N   . ASP   A 1  393 ? 6.813   -24.218 -19.978 1    17.248  ? 393  ASP   A N   1 1 
ATOM   3181  C  CA  . ASP   A 1  393 ? 8.039   -23.685 -19.408 1    18.213  ? 393  ASP   A CA  1 1 
ATOM   3182  C  C   . ASP   A 1  393 ? 8.868   -24.853 -18.83  1    18.179  ? 393  ASP   A C   1 1 
ATOM   3183  O  O   . ASP   A 1  393 ? 10.078  -24.832 -18.932 1    18.504  ? 393  ASP   A O   1 1 
ATOM   3184  C  CB  . ASP   A 1  393 ? 7.791   -22.586 -18.368 1    21.836  ? 393  ASP   A CB  1 1 
ATOM   3185  C  CG  . ASP   A 1  393 ? 7.328   -21.212 -18.882 1    27.114  ? 393  ASP   A CG  1 1 
ATOM   3186  O  OD1 . ASP   A 1  393 ? 6.757   -21.142 -20.025 1    25.585  ? 393  ASP   A OD1 1 1 
ATOM   3187  O  OD2 . ASP   A 1  393 ? 7.594   -20.177 -18.16  1    30.332  ? 393  ASP   A OD2 1 1 
ATOM   3188  N  N   . VAL   A 1  394 ? 8.245   -25.847 -18.197 1    18.649  ? 394  VAL   A N   1 1 
ATOM   3189  C  CA  . VAL   A 1  394 ? 9.052   -26.962 -17.665 1    21.327  ? 394  VAL   A CA  1 1 
ATOM   3190  C  C   . VAL   A 1  394 ? 9.802   -27.653 -18.786 1    19.731  ? 394  VAL   A C   1 1 
ATOM   3191  O  O   . VAL   A 1  394 ? 10.972  -28.01  -18.6   1    18.923  ? 394  VAL   A O   1 1 
ATOM   3192  C  CB  . VAL   A 1  394 ? 8.211   -27.997 -16.877 1    23.361  ? 394  VAL   A CB  1 1 
ATOM   3193  C  CG1 . VAL   A 1  394 ? 9.092   -29.088 -16.285 1    26.649  ? 394  VAL   A CG1 1 1 
ATOM   3194  C  CG2 . VAL   A 1  394 ? 7.514   -27.302 -15.723 1    22.028  ? 394  VAL   A CG2 1 1 
ATOM   3195  N  N   . LEU   A 1  395 ? 9.118   -27.935 -19.913 1    19.501  ? 395  LEU   A N   1 1 
ATOM   3196  C  CA  . LEU   A 1  395 ? 9.862   -28.567 -20.99  1    20.876  ? 395  LEU   A CA  1 1 
ATOM   3197  C  C   . LEU   A 1  395 ? 10.953  -27.631 -21.498 1    19.254  ? 395  LEU   A C   1 1 
ATOM   3198  O  O   . LEU   A 1  395 ? 12.062  -28.08  -21.82  1    19.6    ? 395  LEU   A O   1 1 
ATOM   3199  C  CB  . LEU   A 1  395 ? 8.939   -28.965 -22.158 1    25.578  ? 395  LEU   A CB  1 1 
ATOM   3200  C  CG  . LEU   A 1  395 ? 8.234   -30.322 -22.069 1    29.628  ? 395  LEU   A CG  1 1 
ATOM   3201  C  CD1 . LEU   A 1  395 ? 7.509   -30.469 -20.754 1    28.732  ? 395  LEU   A CD1 1 1 
ATOM   3202  C  CD2 . LEU   A 1  395 ? 7.217   -30.473 -23.225 1    33.211  ? 395  LEU   A CD2 1 1 
ATOM   3203  N  N   . ALA   A 1  396 ? 10.653  -26.32  -21.606 1    18.05   ? 396  ALA   A N   1 1 
ATOM   3204  C  CA  . ALA   A 1  396 ? 11.638  -25.386 -22.143 1    19.13   ? 396  ALA   A CA  1 1 
ATOM   3205  C  C   . ALA   A 1  396 ? 12.875  -25.36  -21.237 1    18.918  ? 396  ALA   A C   1 1 
ATOM   3206  O  O   . ALA   A 1  396 ? 13.961  -25.007 -21.712 1    20.408  ? 396  ALA   A O   1 1 
ATOM   3207  C  CB  . ALA   A 1  396 ? 11.126  -23.959 -22.29  1    16.841  ? 396  ALA   A CB  1 1 
ATOM   3208  N  N   . LEU   A 1  397 ? 12.725  -25.674 -19.942 1    17.596  ? 397  LEU   A N   1 1 
ATOM   3209  C  CA  . LEU   A 1  397 ? 13.92   -25.76  -19.075 1    17.031  ? 397  LEU   A CA  1 1 
ATOM   3210  C  C   . LEU   A 1  397 ? 14.895  -26.825 -19.567 1    18.343  ? 397  LEU   A C   1 1 
ATOM   3211  O  O   . LEU   A 1  397 ? 16.119  -26.676 -19.467 1    19.918  ? 397  LEU   A O   1 1 
ATOM   3212  C  CB  . LEU   A 1  397 ? 13.575  -26.048 -17.597 1    18.337  ? 397  LEU   A CB  1 1 
ATOM   3213  C  CG  . LEU   A 1  397 ? 12.842  -24.923 -16.85  1    18.547  ? 397  LEU   A CG  1 1 
ATOM   3214  C  CD1 . LEU   A 1  397 ? 12.404  -25.311 -15.394 1    17.166  ? 397  LEU   A CD1 1 1 
ATOM   3215  C  CD2 . LEU   A 1  397 ? 13.783  -23.708 -16.771 1    20.424  ? 397  LEU   A CD2 1 1 
ATOM   3216  N  N   . SER   A 1  398 ? 14.376  -27.949 -20.061 1    18.167  ? 398  SER   A N   1 1 
ATOM   3217  C  CA  . SER   A 1  398 ? 15.258  -29.003 -20.555 1    17.139  ? 398  SER   A CA  1 1 
ATOM   3218  C  C   . SER   A 1  398 ? 15.814  -28.526 -21.897 1    18.324  ? 398  SER   A C   1 1 
ATOM   3219  O  O   . SER   A 1  398 ? 16.991  -28.717 -22.203 1    17.604  ? 398  SER   A O   1 1 
ATOM   3220  C  CB  . SER   A 1  398 ? 14.478  -30.301 -20.786 1    17.915  ? 398  SER   A CB  1 1 
ATOM   3221  O  OG  . SER   A 1  398 ? 14.29   -31.011 -19.566 1    18.768  ? 398  SER   A OG  1 1 
ATOM   3222  N  N   . VAL   A 1  399 ? 14.94   -27.905 -22.711 1    17.343  ? 399  VAL   A N   1 1 
ATOM   3223  C  CA  . VAL   A 1  399 ? 15.346  -27.59  -24.068 1    19.051  ? 399  VAL   A CA  1 1 
ATOM   3224  C  C   . VAL   A 1  399 ? 16.532  -26.629 -24.044 1    19.752  ? 399  VAL   A C   1 1 
ATOM   3225  O  O   . VAL   A 1  399 ? 17.339  -26.692 -24.946 1    22.238  ? 399  VAL   A O   1 1 
ATOM   3226  C  CB  . VAL   A 1  399 ? 14.167  -27.003 -24.878 1    18.022  ? 399  VAL   A CB  1 1 
ATOM   3227  C  CG1 . VAL   A 1  399 ? 14.657  -26.355 -26.189 1    17.64   ? 399  VAL   A CG1 1 1 
ATOM   3228  C  CG2 . VAL   A 1  399 ? 13.157  -28.108 -25.15  1    17.479  ? 399  VAL   A CG2 1 1 
ATOM   3229  N  N   . SER   A 1  400 ? 16.544  -25.642 -23.121 1    20.554  ? 400  SER   A N   1 1 
ATOM   3230  C  CA  . SER   A 1  400 ? 17.533  -24.571 -23.164 1    22.711  ? 400  SER   A CA  1 1 
ATOM   3231  C  C   . SER   A 1  400 ? 18.893  -25.062 -22.672 1    21.42   ? 400  SER   A C   1 1 
ATOM   3232  O  O   . SER   A 1  400 ? 19.911  -24.388 -22.824 1    21.02   ? 400  SER   A O   1 1 
ATOM   3233  C  CB  . SER   A 1  400 ? 17.09   -23.363 -22.349 1    25.308  ? 400  SER   A CB  1 1 
ATOM   3234  O  OG  . SER   A 1  400 ? 17.016  -23.706 -20.977 1    25.981  ? 400  SER   A OG  1 1 
ATOM   3235  N  N   . THR   A 1  401 ? 18.946  -26.254 -22.083 1    19.644  ? 401  THR   A N   1 1 
ATOM   3236  C  CA  . THR   A 1  401 ? 20.263  -26.708 -21.64  1    19.175  ? 401  THR   A CA  1 1 
ATOM   3237  C  C   . THR   A 1  401 ? 21.265  -26.767 -22.79  1    20.23   ? 401  THR   A C   1 1 
ATOM   3238  O  O   . THR   A 1  401 ? 21.009  -27.282 -23.872 1    20.979  ? 401  THR   A O   1 1 
ATOM   3239  C  CB  . THR   A 1  401 ? 20.234  -28.045 -20.874 1    19.823  ? 401  THR   A CB  1 1 
ATOM   3240  O  OG1 . THR   A 1  401 ? 19.718  -29.095 -21.694 1    18.88   ? 401  THR   A OG1 1 1 
ATOM   3241  C  CG2 . THR   A 1  401 ? 19.35   -28.018 -19.634 1    19.617  ? 401  THR   A CG2 1 1 
ATOM   3242  N  N   . PRO   A 1  402 ? 22.552  -26.466 -22.511 1    21.432  ? 402  PRO   A N   1 1 
ATOM   3243  C  CA  . PRO   A 1  402 ? 23.589  -26.681 -23.518 1    21.613  ? 402  PRO   A CA  1 1 
ATOM   3244  C  C   . PRO   A 1  402 ? 23.605  -28.089 -24.102 1    23.054  ? 402  PRO   A C   1 1 
ATOM   3245  O  O   . PRO   A 1  402 ? 23.736  -28.292 -25.303 1    22.488  ? 402  PRO   A O   1 1 
ATOM   3246  C  CB  . PRO   A 1  402 ? 24.909  -26.264 -22.821 1    21.959  ? 402  PRO   A CB  1 1 
ATOM   3247  C  CG  . PRO   A 1  402 ? 24.464  -25.327 -21.77  1    21.578  ? 402  PRO   A CG  1 1 
ATOM   3248  C  CD  . PRO   A 1  402 ? 23.013  -25.692 -21.343 1    20.431  ? 402  PRO   A CD  1 1 
ATOM   3249  N  N   . GLU   A 1  403 ? 23.428  -29.104 -23.262 1    24.013  ? 403  GLU   A N   1 1 
ATOM   3250  C  CA  . GLU   A 1  403 ? 23.499  -30.44  -23.828 1    26.942  ? 403  GLU   A CA  1 1 
ATOM   3251  C  C   . GLU   A 1  403 ? 22.323  -30.658 -24.795 1    24.054  ? 403  GLU   A C   1 1 
ATOM   3252  O  O   . GLU   A 1  403 ? 22.479  -31.313 -25.841 1    23.294  ? 403  GLU   A O   1 1 
ATOM   3253  C  CB  . GLU   A 1  403 ? 23.274  -31.365 -22.637 1    34.709  ? 403  GLU   A CB  1 1 
ATOM   3254  C  CG  . GLU   A 1  403 ? 23.865  -32.754 -22.847 1    49.102  ? 403  GLU   A CG  1 1 
ATOM   3255  C  CD  . GLU   A 1  403 ? 23.396  -33.818 -21.853 1    61.045  ? 403  GLU   A CD  1 1 
ATOM   3256  O  OE1 . GLU   A 1  403 ? 22.378  -33.663 -21.099 1    62.342  ? 403  GLU   A OE1 1 1 
ATOM   3257  O  OE2 . GLU   A 1  403 ? 24.109  -34.851 -21.867 1    65.508  ? 403  GLU   A OE2 1 1 
ATOM   3258  N  N   . HIS   A 1  404 ? 21.12   -30.191 -24.402 1    21.387  ? 404  HIS   A N   1 1 
ATOM   3259  C  CA  . HIS   A 1  404 ? 19.993  -30.386 -25.307 1    19.812  ? 404  HIS   A CA  1 1 
ATOM   3260  C  C   . HIS   A 1  404 ? 20.176  -29.609 -26.626 1    19.633  ? 404  HIS   A C   1 1 
ATOM   3261  O  O   . HIS   A 1  404 ? 19.95   -30.137 -27.719 1    19.845  ? 404  HIS   A O   1 1 
ATOM   3262  C  CB  . HIS   A 1  404 ? 18.654  -30.006 -24.649 1    18.664  ? 404  HIS   A CB  1 1 
ATOM   3263  C  CG  . HIS   A 1  404 ? 17.533  -30.452 -25.558 1    19.137  ? 404  HIS   A CG  1 1 
ATOM   3264  N  ND1 . HIS   A 1  404 ? 17.07   -31.749 -25.538 1    20.304  ? 404  HIS   A ND1 1 1 
ATOM   3265  C  CD2 . HIS   A 1  404 ? 16.813  -29.815 -26.52  1    19.765  ? 404  HIS   A CD2 1 1 
ATOM   3266  C  CE1 . HIS   A 1  404 ? 16.131  -31.901 -26.505 1    21.232  ? 404  HIS   A CE1 1 1 
ATOM   3267  N  NE2 . HIS   A 1  404 ? 16.006  -30.747 -27.145 1    20.674  ? 404  HIS   A NE2 1 1 
ATOM   3268  N  N   . LEU   A 1  405 ? 20.57   -28.333 -26.527 1    19.236  ? 405  LEU   A N   1 1 
ATOM   3269  C  CA  . LEU   A 1  405 ? 20.835  -27.53  -27.719 1    19.819  ? 405  LEU   A CA  1 1 
ATOM   3270  C  C   . LEU   A 1  405 ? 21.841  -28.238 -28.618 1    21.53   ? 405  LEU   A C   1 1 
ATOM   3271  O  O   . LEU   A 1  405 ? 21.748  -28.199 -29.841 1    21.108  ? 405  LEU   A O   1 1 
ATOM   3272  C  CB  . LEU   A 1  405 ? 21.362  -26.152 -27.322 1    20.228  ? 405  LEU   A CB  1 1 
ATOM   3273  C  CG  . LEU   A 1  405 ? 20.39   -25.313 -26.484 1    19.621  ? 405  LEU   A CG  1 1 
ATOM   3274  C  CD1 . LEU   A 1  405 ? 21.081  -24.072 -25.97  1    20.018  ? 405  LEU   A CD1 1 1 
ATOM   3275  C  CD2 . LEU   A 1  405 ? 19.195  -24.913 -27.369 1    19.954  ? 405  LEU   A CD2 1 1 
ATOM   3276  N  N   . HIS   A 1  406 ? 22.852  -28.861 -28.011 1    22.755  ? 406  HIS   A N   1 1 
ATOM   3277  C  CA  . HIS   A 1  406 ? 23.786  -29.629 -28.838 1    25.105  ? 406  HIS   A CA  1 1 
ATOM   3278  C  C   . HIS   A 1  406 ? 23.066  -30.729 -29.611 1    26.293  ? 406  HIS   A C   1 1 
ATOM   3279  O  O   . HIS   A 1  406 ? 23.409  -30.984 -30.777 1    25.205  ? 406  HIS   A O   1 1 
ATOM   3280  C  CB  . HIS   A 1  406 ? 24.95   -30.163 -28.005 1    26.863  ? 406  HIS   A CB  1 1 
ATOM   3281  C  CG  . HIS   A 1  406 ? 25.919  -30.964 -28.798 1    29.798  ? 406  HIS   A CG  1 1 
ATOM   3282  N  ND1 . HIS   A 1  406 ? 26.83   -30.36  -29.633 1    32.156  ? 406  HIS   A ND1 1 1 
ATOM   3283  C  CD2 . HIS   A 1  406 ? 26.135  -32.284 -28.911 1    32.587  ? 406  HIS   A CD2 1 1 
ATOM   3284  C  CE1 . HIS   A 1  406 ? 27.597  -31.297 -30.212 1    35.061  ? 406  HIS   A CE1 1 1 
ATOM   3285  N  NE2 . HIS   A 1  406 ? 27.169  -32.476 -29.805 1    34.157  ? 406  HIS   A NE2 1 1 
ATOM   3286  N  N   . LYS   A 1  407 ? 22.115  -31.429 -28.948 1    26.081  ? 407  LYS   A N   1 1 
ATOM   3287  C  CA  . LYS   A 1  407 ? 21.481  -32.57  -29.612 1    27.529  ? 407  LYS   A CA  1 1 
ATOM   3288  C  C   . LYS   A 1  407 ? 20.616  -32.089 -30.784 1    27.004  ? 407  LYS   A C   1 1 
ATOM   3289  O  O   . LYS   A 1  407 ? 20.408  -32.814 -31.749 1    28.364  ? 407  LYS   A O   1 1 
ATOM   3290  C  CB  . LYS   A 1  407 ? 20.48   -33.384 -28.776 1    30.852  ? 407  LYS   A CB  1 1 
ATOM   3291  C  CG  . LYS   A 1  407 ? 21.062  -34.17  -27.61  1    36.341  ? 407  LYS   A CG  1 1 
ATOM   3292  C  CD  . LYS   A 1  407 ? 20.004  -34.499 -26.546 1    39.138  ? 407  LYS   A CD  1 1 
ATOM   3293  C  CE  . LYS   A 1  407 ? 20.644  -35.142 -25.337 1    42.708  ? 407  LYS   A CE  1 1 
ATOM   3294  N  NZ  . LYS   A 1  407 ? 19.725  -35.151 -24.194 1    39.332  ? 407  LYS   A NZ  1 1 
ATOM   3295  N  N   . ILE   A 1  408 ? 20.08   -30.872 -30.728 1    25.396  ? 408  ILE   A N   1 1 
ATOM   3296  C  CA  . ILE   A 1  408 ? 19.241  -30.431 -31.843 1    25.687  ? 408  ILE   A CA  1 1 
ATOM   3297  C  C   . ILE   A 1  408 ? 20.015  -29.556 -32.851 1    26.084  ? 408  ILE   A C   1 1 
ATOM   3298  O  O   . ILE   A 1  408 ? 19.413  -28.803 -33.609 1    26.585  ? 408  ILE   A O   1 1 
ATOM   3299  C  CB  . ILE   A 1  408 ? 17.94   -29.802 -31.324 1    25.274  ? 408  ILE   A CB  1 1 
ATOM   3300  C  CG1 . ILE   A 1  408 ? 18.217  -28.522 -30.507 1    23.912  ? 408  ILE   A CG1 1 1 
ATOM   3301  C  CG2 . ILE   A 1  408 ? 17.217  -30.875 -30.499 1    24.366  ? 408  ILE   A CG2 1 1 
ATOM   3302  C  CD1 . ILE   A 1  408 ? 16.981  -27.708 -30.144 1    23.469  ? 408  ILE   A CD1 1 1 
ATOM   3303  N  N   . GLY   A 1  409 ? 21.346  -29.58  -32.81  1    25.428  ? 409  GLY   A N   1 1 
ATOM   3304  C  CA  . GLY   A 1  409 ? 22.148  -28.908 -33.825 1    27.391  ? 409  GLY   A CA  1 1 
ATOM   3305  C  C   . GLY   A 1  409 ? 22.325  -27.405 -33.615 1    26.842  ? 409  GLY   A C   1 1 
ATOM   3306  O  O   . GLY   A 1  409 ? 22.771  -26.736 -34.537 1    28.775  ? 409  GLY   A O   1 1 
ATOM   3307  N  N   . LEU   A 1  410 ? 22.068  -26.895 -32.41  1    25.159  ? 410  LEU   A N   1 1 
ATOM   3308  C  CA  . LEU   A 1  410 ? 22.098  -25.451 -32.14  1    25.04   ? 410  LEU   A CA  1 1 
ATOM   3309  C  C   . LEU   A 1  410 ? 23.346  -25.009 -31.35  1    26.03   ? 410  LEU   A C   1 1 
ATOM   3310  O  O   . LEU   A 1  410 ? 23.573  -23.818 -31.119 1    25.82   ? 410  LEU   A O   1 1 
ATOM   3311  C  CB  . LEU   A 1  410 ? 20.823  -24.959 -31.479 1    23.194  ? 410  LEU   A CB  1 1 
ATOM   3312  C  CG  . LEU   A 1  410 ? 19.582  -24.946 -32.385 1    22.973  ? 410  LEU   A CG  1 1 
ATOM   3313  C  CD1 . LEU   A 1  410 ? 18.328  -24.493 -31.652 1    20.919  ? 410  LEU   A CD1 1 1 
ATOM   3314  C  CD2 . LEU   A 1  410 ? 19.753  -24.181 -33.7   1    23.847  ? 410  LEU   A CD2 1 1 
ATOM   3315  N  N   . LEU   A 1  411 ? 24.221  -25.953 -31.001 1    26.497  ? 411  LEU   A N   1 1 
ATOM   3316  C  CA  . LEU   A 1  411 ? 25.339  -25.543 -30.184 1    27.203  ? 411  LEU   A CA  1 1 
ATOM   3317  C  C   . LEU   A 1  411 ? 26.392  -26.61  -30.39  1    30.481  ? 411  LEU   A C   1 1 
ATOM   3318  O  O   . LEU   A 1  411 ? 26.267  -27.716 -29.881 1    31.762  ? 411  LEU   A O   1 1 
ATOM   3319  C  CB  . LEU   A 1  411 ? 24.917  -25.399 -28.712 1    28.347  ? 411  LEU   A CB  1 1 
ATOM   3320  C  CG  . LEU   A 1  411 ? 25.944  -24.752 -27.779 1    30.276  ? 411  LEU   A CG  1 1 
ATOM   3321  C  CD1 . LEU   A 1  411 ? 26.209  -23.3   -28.243 1    30.761  ? 411  LEU   A CD1 1 1 
ATOM   3322  C  CD2 . LEU   A 1  411 ? 25.32   -24.748 -26.377 1    29.334  ? 411  LEU   A CD2 1 1 
ATOM   3323  N  N   . ASP   A 1  412 ? 27.438  -26.25  -31.118 1    33.401  ? 412  ASP   A N   1 1 
ATOM   3324  C  CA  . ASP   A 1  412 ? 28.431  -27.25  -31.531 1    41.657  ? 412  ASP   A CA  1 1 
ATOM   3325  C  C   . ASP   A 1  412 ? 29.415  -27.572 -30.424 1    40.975  ? 412  ASP   A C   1 1 
ATOM   3326  O  O   . ASP   A 1  412 ? 29.824  -28.717 -30.276 1    42.792  ? 412  ASP   A O   1 1 
ATOM   3327  C  CB  . ASP   A 1  412 ? 29.103  -26.917 -32.847 1    48.371  ? 412  ASP   A CB  1 1 
ATOM   3328  C  CG  . ASP   A 1  412 ? 28.442  -27.644 -34.009 1    62.434  ? 412  ASP   A CG  1 1 
ATOM   3329  O  OD1 . ASP   A 1  412 ? 27.186  -27.807 -33.97  1    62.37   ? 412  ASP   A OD1 1 1 
ATOM   3330  O  OD2 . ASP   A 1  412 ? 29.185  -28.08  -34.926 1    72.755  ? 412  ASP   A OD2 1 1 
ATOM   3331  N  N   . ARG   A 1  413 ? 29.786  -26.572 -29.634 1    43.124  ? 413  ARG   A N   1 1 
ATOM   3332  C  CA  . ARG   A 1  413 ? 30.786  -26.845 -28.608 1    44.002  ? 413  ARG   A CA  1 1 
ATOM   3333  C  C   . ARG   A 1  413 ? 30.032  -27.332 -27.365 1    43.421  ? 413  ARG   A C   1 1 
ATOM   3334  O  O   . ARG   A 1  413 ? 29.057  -26.712 -26.958 1    34.91   ? 413  ARG   A O   1 1 
ATOM   3335  C  CB  . ARG   A 1  413 ? 31.572  -25.539 -28.417 1    43.375  ? 413  ARG   A CB  1 1 
ATOM   3336  C  CG  . ARG   A 1  413 ? 33.045  -25.478 -28.046 1    42.812  ? 413  ARG   A CG  1 1 
ATOM   3337  C  CD  . ARG   A 1  413 ? 33.315  -24.04  -27.644 1    40.395  ? 413  ARG   A CD  1 1 
ATOM   3338  N  NE  . ARG   A 1  413 ? 34.079  -24.047 -26.388 1    44.178  ? 413  ARG   A NE  1 1 
ATOM   3339  C  CZ  . ARG   A 1  413 ? 34.527  -22.996 -25.656 1    43.919  ? 413  ARG   A CZ  1 1 
ATOM   3340  N  NH1 . ARG   A 1  413 ? 35.225  -23.214 -24.542 1    43.058  ? 413  ARG   A NH1 1 1 
ATOM   3341  N  NH2 . ARG   A 1  413 ? 34.315  -21.751 -26.06  1    41.346  ? 413  ARG   A NH2 1 1 
ATOM   3342  N  N   . VAL   A 1  414 ? 30.495  -28.437 -26.772 1    42.17   ? 414  VAL   A N   1 1 
ATOM   3343  C  CA  . VAL   A 1  414 ? 29.99   -28.901 -25.486 1    44.433  ? 414  VAL   A CA  1 1 
ATOM   3344  C  C   . VAL   A 1  414 ? 31.056  -28.562 -24.439 1    41.357  ? 414  VAL   A C   1 1 
ATOM   3345  O  O   . VAL   A 1  414 ? 32.247  -28.74  -24.693 1    45.761  ? 414  VAL   A O   1 1 
ATOM   3346  C  CB  . VAL   A 1  414 ? 29.916  -30.441 -25.655 1    52.382  ? 414  VAL   A CB  1 1 
ATOM   3347  C  CG1 . VAL   A 1  414 ? 29.037  -31.093 -24.588 1    52.55   ? 414  VAL   A CG1 1 1 
ATOM   3348  C  CG2 . VAL   A 1  414 ? 29.506  -30.889 -27.065 1    48.892  ? 414  VAL   A CG2 1 1 
ATOM   3349  N  N   . THR   A 1  415 ? 30.68   -28.058 -23.274 1    34.315  ? 415  THR   A N   1 1 
ATOM   3350  C  CA  . THR   A 1  415 ? 31.667  -27.847 -22.219 1    36.618  ? 415  THR   A CA  1 1 
ATOM   3351  C  C   . THR   A 1  415 ? 30.964  -28.235 -20.921 1    35.295  ? 415  THR   A C   1 1 
ATOM   3352  O  O   . THR   A 1  415 ? 29.737  -28.128 -20.859 1    37.183  ? 415  THR   A O   1 1 
ATOM   3353  C  CB  . THR   A 1  415 ? 32.168  -26.391 -22.14  1    37.482  ? 415  THR   A CB  1 1 
ATOM   3354  O  OG1 . THR   A 1  415 ? 30.997  -25.573 -22.035 1    37.92   ? 415  THR   A OG1 1 1 
ATOM   3355  C  CG2 . THR   A 1  415 ? 33.023  -25.937 -23.316 1    36.473  ? 415  THR   A CG2 1 1 
ATOM   3356  N  N   . ASN   A 1  416 ? 31.709  -28.723 -19.926 1    31.687  ? 416  ASN   A N   1 1 
ATOM   3357  C  CA  . ASN   A 1  416 ? 31.092  -28.92  -18.624 1    31.36   ? 416  ASN   A CA  1 1 
ATOM   3358  C  C   . ASN   A 1  416 ? 32.062  -28.412 -17.559 1    30.203  ? 416  ASN   A C   1 1 
ATOM   3359  O  O   . ASN   A 1  416 ? 32.85   -29.185 -17.051 1    33.13   ? 416  ASN   A O   1 1 
ATOM   3360  C  CB  . ASN   A 1  416 ? 30.689  -30.383 -18.416 1    32.133  ? 416  ASN   A CB  1 1 
ATOM   3361  C  CG  . ASN   A 1  416 ? 29.901  -30.61  -17.139 1    32.89   ? 416  ASN   A CG  1 1 
ATOM   3362  O  OD1 . ASN   A 1  416 ? 29.264  -29.696 -16.61  1    30.165  ? 416  ASN   A OD1 1 1 
ATOM   3363  N  ND2 . ASN   A 1  416 ? 29.889  -31.829 -16.642 1    35.037  ? 416  ASN   A ND2 1 1 
ATOM   3364  N  N   . ASP   A 1  417 ? 32.076  -27.105 -17.291 1    28.207  ? 417  ASP   A N   1 1 
ATOM   3365  C  CA  . ASP   A 1  417 ? 33.013  -26.535 -16.343 1    28.353  ? 417  ASP   A CA  1 1 
ATOM   3366  C  C   . ASP   A 1  417 ? 32.311  -25.413 -15.598 1    25.794  ? 417  ASP   A C   1 1 
ATOM   3367  O  O   . ASP   A 1  417 ? 31.22   -25.006 -15.997 1    23.603  ? 417  ASP   A O   1 1 
ATOM   3368  C  CB  . ASP   A 1  417 ? 34.222  -25.959 -17.065 1    30.963  ? 417  ASP   A CB  1 1 
ATOM   3369  C  CG  . ASP   A 1  417 ? 33.839  -25.129 -18.286 1    34.88   ? 417  ASP   A CG  1 1 
ATOM   3370  O  OD1 . ASP   A 1  417 ? 33.412  -23.978 -18.107 1    31.155  ? 417  ASP   A OD1 1 1 
ATOM   3371  O  OD2 . ASP   A 1  417 ? 33.962  -25.652 -19.412 1    40.709  ? 417  ASP   A OD2 1 1 
ATOM   3372  N  N   . THR   A 1  418 ? 32.969  -24.882 -14.559 1    24.922  ? 418  THR   A N   1 1 
ATOM   3373  C  CA  . THR   A 1  418 ? 32.26   -23.965 -13.692 1    24.532  ? 418  THR   A CA  1 1 
ATOM   3374  C  C   . THR   A 1  418 ? 31.935  -22.677 -14.451 1    24.274  ? 418  THR   A C   1 1 
ATOM   3375  O  O   . THR   A 1  418 ? 30.872  -22.105 -14.202 1    21.401  ? 418  THR   A O   1 1 
ATOM   3376  C  CB  . THR   A 1  418 ? 32.91   -23.711 -12.328 1    26.436  ? 418  THR   A CB  1 1 
ATOM   3377  O  OG1 . THR   A 1  418 ? 34.19   -23.253 -12.748 1    27.695  ? 418  THR   A OG1 1 1 
ATOM   3378  C  CG2 . THR   A 1  418 ? 33.227  -25.002 -11.584 1    26.647  ? 418  THR   A CG2 1 1 
ATOM   3379  N  N   . GLU   A 1  419 ? 32.811  -22.237 -15.369 1    23.927  ? 419  GLU   A N   1 1 
ATOM   3380  C  CA  . GLU   A 1  419 ? 32.468  -20.959 -15.979 1    24.43   ? 419  GLU   A CA  1 1 
ATOM   3381  C  C   . GLU   A 1  419 ? 31.268  -21.104 -16.913 1    22.531  ? 419  GLU   A C   1 1 
ATOM   3382  O  O   . GLU   A 1  419 ? 30.443  -20.195 -16.974 1    21.451  ? 419  GLU   A O   1 1 
ATOM   3383  C  CB  . GLU   A 1  419 ? 33.622  -20.369 -16.791 1    27.575  ? 419  GLU   A CB  1 1 
ATOM   3384  C  CG  . GLU   A 1  419 ? 34.816  -20     -15.909 1    32.322  ? 419  GLU   A CG  1 1 
ATOM   3385  C  CD  . GLU   A 1  419 ? 35.711  -21.19  -15.564 1    38.328  ? 419  GLU   A CD  1 1 
ATOM   3386  O  OE1 . GLU   A 1  419 ? 35.544  -22.407 -15.967 1    35.897  ? 419  GLU   A OE1 1 1 
ATOM   3387  O  OE2 . GLU   A 1  419 ? 36.699  -20.838 -14.861 1    53.306  ? 419  GLU   A OE2 1 1 
ATOM   3388  N  N   . SER   A 1  420 ? 31.218  -22.19  -17.708 1    22.205  ? 420  SER   A N   1 1 
ATOM   3389  C  CA  . SER   A 1  420 ? 30.069  -22.386 -18.593 1    22.633  ? 420  SER   A CA  1 1 
ATOM   3390  C  C   . SER   A 1  420 ? 28.798  -22.499 -17.794 1    21.615  ? 420  SER   A C   1 1 
ATOM   3391  O  O   . SER   A 1  420 ? 27.731  -22.068 -18.278 1    19.714  ? 420  SER   A O   1 1 
ATOM   3392  C  CB  . SER   A 1  420 ? 30.197  -23.649 -19.424 1    24.001  ? 420  SER   A CB  1 1 
ATOM   3393  O  OG  . SER   A 1  420 ? 31.39   -23.537 -20.189 1    25.388  ? 420  SER   A OG  1 1 
ATOM   3394  N  N   . ASP   A 1  421 ? 28.896  -23.079 -16.586 1    21.371  ? 421  ASP   A N   1 1 
ATOM   3395  C  CA  . ASP   A 1  421 ? 27.687  -23.222 -15.78  1    22.669  ? 421  ASP   A CA  1 1 
ATOM   3396  C  C   . ASP   A 1  421 ? 27.191  -21.865 -15.272 1    20.76   ? 421  ASP   A C   1 1 
ATOM   3397  O  O   . ASP   A 1  421 ? 25.979  -21.618 -15.234 1    19.805  ? 421  ASP   A O   1 1 
ATOM   3398  C  CB  . ASP   A 1  421 ? 27.895  -24.068 -14.537 1    28.196  ? 421  ASP   A CB  1 1 
ATOM   3399  C  CG  . ASP   A 1  421 ? 27.357  -25.497 -14.532 1    38.147  ? 421  ASP   A CG  1 1 
ATOM   3400  O  OD1 . ASP   A 1  421 ? 26.553  -25.871 -15.456 1    40.156  ? 421  ASP   A OD1 1 1 
ATOM   3401  O  OD2 . ASP   A 1  421 ? 27.717  -26.229 -13.559 1    44.955  ? 421  ASP   A OD2 1 1 
ATOM   3402  N  N   . ILE   A 1  422 ? 28.121  -21.012 -14.82  1    20.688  ? 422  ILE   A N   1 1 
ATOM   3403  C  CA  . ILE   A 1  422 ? 27.728  -19.665 -14.419 1    18.72   ? 422  ILE   A CA  1 1 
ATOM   3404  C  C   . ILE   A 1  422 ? 27.066  -18.935 -15.606 1    17.939  ? 422  ILE   A C   1 1 
ATOM   3405  O  O   . ILE   A 1  422 ? 26.044  -18.26  -15.411 1    17.396  ? 422  ILE   A O   1 1 
ATOM   3406  C  CB  . ILE   A 1  422 ? 28.91   -18.885 -13.837 1    20.056  ? 422  ILE   A CB  1 1 
ATOM   3407  C  CG1 . ILE   A 1  422 ? 29.425  -19.461 -12.47  1    21.039  ? 422  ILE   A CG1 1 1 
ATOM   3408  C  CG2 . ILE   A 1  422 ? 28.608  -17.388 -13.767 1    18.997  ? 422  ILE   A CG2 1 1 
ATOM   3409  C  CD1 . ILE   A 1  422 ? 28.292  -19.737 -11.509 1    22.466  ? 422  ILE   A CD1 1 1 
ATOM   3410  N  N   . ASN   A 1  423 ? 27.665  -19.02  -16.801 1    18.627  ? 423  ASN   A N   1 1 
ATOM   3411  C  CA  . ASN   A 1  423 ? 27.092  -18.356 -17.969 1    18.087  ? 423  ASN   A CA  1 1 
ATOM   3412  C  C   . ASN   A 1  423 ? 25.658  -18.832 -18.144 1    16.959  ? 423  ASN   A C   1 1 
ATOM   3413  O  O   . ASN   A 1  423 ? 24.734  -18.032 -18.326 1    15.603  ? 423  ASN   A O   1 1 
ATOM   3414  C  CB  . ASN   A 1  423 ? 27.865  -18.634 -19.262 1    18.723  ? 423  ASN   A CB  1 1 
ATOM   3415  C  CG  . ASN   A 1  423 ? 29.114  -17.79  -19.444 1    20.199  ? 423  ASN   A CG  1 1 
ATOM   3416  O  OD1 . ASN   A 1  423 ? 29.393  -16.854 -18.66  1    20.667  ? 423  ASN   A OD1 1 1 
ATOM   3417  N  ND2 . ASN   A 1  423 ? 29.863  -18.106 -20.478 1    20.901  ? 423  ASN   A ND2 1 1 
ATOM   3418  N  N   . TYR   A 1  424 ? 25.461  -20.158 -18.116 1    17.357  ? 424  TYR   A N   1 1 
ATOM   3419  C  CA  . TYR   A 1  424 ? 24.113  -20.669 -18.349 1    17.565  ? 424  TYR   A CA  1 1 
ATOM   3420  C  C   . TYR   A 1  424 ? 23.173  -20.205 -17.248 1    17.115  ? 424  TYR   A C   1 1 
ATOM   3421  O  O   . TYR   A 1  424 ? 22.063  -19.739 -17.539 1    14.433  ? 424  TYR   A O   1 1 
ATOM   3422  C  CB  . TYR   A 1  424 ? 24.151  -22.205 -18.456 1    18.41   ? 424  TYR   A CB  1 1 
ATOM   3423  C  CG  . TYR   A 1  424 ? 22.773  -22.794 -18.613 1    18.122  ? 424  TYR   A CG  1 1 
ATOM   3424  C  CD1 . TYR   A 1  424 ? 22.043  -22.603 -19.797 1    18.417  ? 424  TYR   A CD1 1 1 
ATOM   3425  C  CD2 . TYR   A 1  424 ? 22.183  -23.531 -17.576 1    18.327  ? 424  TYR   A CD2 1 1 
ATOM   3426  C  CE1 . TYR   A 1  424 ? 20.757  -23.109 -19.922 1    18.95   ? 424  TYR   A CE1 1 1 
ATOM   3427  C  CE2 . TYR   A 1  424 ? 20.888  -24.013 -17.697 1    18.608  ? 424  TYR   A CE2 1 1 
ATOM   3428  C  CZ  . TYR   A 1  424 ? 20.207  -23.875 -18.902 1    19.951  ? 424  TYR   A CZ  1 1 
ATOM   3429  O  OH  . TYR   A 1  424 ? 18.912  -24.332 -19.116 1    21.306  ? 424  TYR   A OH  1 1 
ATOM   3430  N  N   . LEU   A 1  425 ? 23.606  -20.344 -15.972 1    17.482  ? 425  LEU   A N   1 1 
ATOM   3431  C  CA  . LEU   A 1  425 ? 22.673  -19.979 -14.899 1    17.234  ? 425  LEU   A CA  1 1 
ATOM   3432  C  C   . LEU   A 1  425 ? 22.349  -18.469 -14.886 1    17.66   ? 425  LEU   A C   1 1 
ATOM   3433  O  O   . LEU   A 1  425 ? 21.233  -18.013 -14.559 1    15.877  ? 425  LEU   A O   1 1 
ATOM   3434  C  CB  . LEU   A 1  425 ? 23.215  -20.468 -13.548 1    17.097  ? 425  LEU   A CB  1 1 
ATOM   3435  C  CG  . LEU   A 1  425 ? 23.125  -21.969 -13.276 1    18.4    ? 425  LEU   A CG  1 1 
ATOM   3436  C  CD1 . LEU   A 1  425 ? 23.902  -22.282 -11.998 1    18.985  ? 425  LEU   A CD1 1 1 
ATOM   3437  C  CD2 . LEU   A 1  425 ? 21.662  -22.419 -13.207 1    18.539  ? 425  LEU   A CD2 1 1 
ATOM   3438  N  N   . LEU   A 1  426 ? 23.32   -17.655 -15.317 1    18.242  ? 426  LEU   A N   1 1 
ATOM   3439  C  CA  . LEU   A 1  426 ? 23.065  -16.224 -15.398 1    17.92   ? 426  LEU   A CA  1 1 
ATOM   3440  C  C   . LEU   A 1  426 ? 22.055  -15.963 -16.508 1    17.574  ? 426  LEU   A C   1 1 
ATOM   3441  O  O   . LEU   A 1  426 ? 21.098  -15.183 -16.35  1    16.537  ? 426  LEU   A O   1 1 
ATOM   3442  C  CB  . LEU   A 1  426 ? 24.42   -15.562 -15.673 1    20.316  ? 426  LEU   A CB  1 1 
ATOM   3443  C  CG  . LEU   A 1  426 ? 24.42   -14.039 -15.601 1    25.272  ? 426  LEU   A CG  1 1 
ATOM   3444  C  CD1 . LEU   A 1  426 ? 23.901  -13.542 -16.945 1    25.508  ? 426  LEU   A CD1 1 1 
ATOM   3445  C  CD2 . LEU   A 1  426 ? 23.558  -13.482 -14.444 1    23.283  ? 426  LEU   A CD2 1 1 
ATOM   3446  N  N   . LYS   A 1  427 ? 22.237  -16.639 -17.643 1    17.506  ? 427  LYS   A N   1 1 
ATOM   3447  C  CA  . LYS   A 1  427 ? 21.273  -16.428 -18.715 1    17.507  ? 427  LYS   A CA  1 1 
ATOM   3448  C  C   . LYS   A 1  427 ? 19.861  -16.821 -18.243 1    16.641  ? 427  LYS   A C   1 1 
ATOM   3449  O  O   . LYS   A 1  427 ? 18.897  -16.091 -18.513 1    15.768  ? 427  LYS   A O   1 1 
ATOM   3450  C  CB  . LYS   A 1  427 ? 21.626  -17.226 -19.967 1    19.15   ? 427  LYS   A CB  1 1 
ATOM   3451  C  CG  . LYS   A 1  427 ? 20.54   -17.001 -21.079 1    20.627  ? 427  LYS   A CG  1 1 
ATOM   3452  C  CD  . LYS   A 1  427 ? 21.188  -17.312 -22.429 1    23.813  ? 427  LYS   A CD  1 1 
ATOM   3453  C  CE  . LYS   A 1  427 ? 20.266  -17.154 -23.645 1    28.369  ? 427  LYS   A CE  1 1 
ATOM   3454  N  NZ  . LYS   A 1  427 ? 19.143  -18.077 -23.406 1    32.44   ? 427  LYS   A NZ  1 1 
ATOM   3455  N  N   . MET   A 1  428 ? 19.722  -17.997 -17.614 1    15.709  ? 428  MET   A N   1 1 
ATOM   3456  C  CA  . MET   A 1  428 ? 18.44   -18.389 -17.006 1    16.922  ? 428  MET   A CA  1 1 
ATOM   3457  C  C   . MET   A 1  428 ? 17.891  -17.414 -15.938 1    15.924  ? 428  MET   A C   1 1 
ATOM   3458  O  O   . MET   A 1  428 ? 16.669  -17.171 -15.829 1    14.395  ? 428  MET   A O   1 1 
ATOM   3459  C  CB  . MET   A 1  428 ? 18.524  -19.806 -16.42  1    17.708  ? 428  MET   A CB  1 1 
ATOM   3460  C  CG  . MET   A 1  428 ? 18.78   -20.871 -17.472 1    21.685  ? 428  MET   A CG  1 1 
ATOM   3461  S  SD  . MET   A 1  428 ? 17.709  -20.864 -18.935 1    27.164  ? 428  MET   A SD  1 1 
ATOM   3462  C  CE  . MET   A 1  428 ? 16.136  -21.136 -18.089 1    21.179  ? 428  MET   A CE  1 1 
ATOM   3463  N  N   . ALA   A 1  429 ? 18.761  -16.874 -15.072 1    14.593  ? 429  ALA   A N   1 1 
ATOM   3464  C  CA  . ALA   A 1  429 ? 18.337  -15.832 -14.148 1    14.689  ? 429  ALA   A CA  1 1 
ATOM   3465  C  C   . ALA   A 1  429 ? 17.805  -14.598 -14.898 1    14.976  ? 429  ALA   A C   1 1 
ATOM   3466  O  O   . ALA   A 1  429 ? 16.794  -14.038 -14.46  1    14.021  ? 429  ALA   A O   1 1 
ATOM   3467  C  CB  . ALA   A 1  429 ? 19.465  -15.409 -13.245 1    14.776  ? 429  ALA   A CB  1 1 
ATOM   3468  N  N   . LEU   A 1  430 ? 18.421  -14.199 -16.032 1    14.396  ? 430  LEU   A N   1 1 
ATOM   3469  C  CA  . LEU   A 1  430 ? 17.87   -13.009 -16.708 1    15.837  ? 430  LEU   A CA  1 1 
ATOM   3470  C  C   . LEU   A 1  430 ? 16.42   -13.256 -17.167 1    16.358  ? 430  LEU   A C   1 1 
ATOM   3471  O  O   . LEU   A 1  430 ? 15.606  -12.327 -17.303 1    15.504  ? 430  LEU   A O   1 1 
ATOM   3472  C  CB  . LEU   A 1  430 ? 18.727  -12.606 -17.921 1    14.817  ? 430  LEU   A CB  1 1 
ATOM   3473  C  CG  . LEU   A 1  430 ? 20.147  -12.137 -17.577 1    15.44   ? 430  LEU   A CG  1 1 
ATOM   3474  C  CD1 . LEU   A 1  430 ? 20.994  -12.005 -18.903 1    15.534  ? 430  LEU   A CD1 1 1 
ATOM   3475  C  CD2 . LEU   A 1  430 ? 20.132  -10.809 -16.827 1    14.802  ? 430  LEU   A CD2 1 1 
ATOM   3476  N  N   . GLU   A 1  431 ? 16.116  -14.526 -17.467 1    18.25   ? 431  GLU   A N   1 1 
ATOM   3477  C  CA  . GLU   A 1  431 ? 14.799  -14.908 -17.946 1    19.937  ? 431  GLU   A CA  1 1 
ATOM   3478  C  C   . GLU   A 1  431 ? 13.843  -15.144 -16.771 1    19.666  ? 431  GLU   A C   1 1 
ATOM   3479  O  O   . GLU   A 1  431 ? 12.679  -14.777 -16.813 1    20.639  ? 431  GLU   A O   1 1 
ATOM   3480  C  CB  . GLU   A 1  431 ? 14.984  -16.144 -18.839 1    21.294  ? 431  GLU   A CB  1 1 
ATOM   3481  C  CG  . GLU   A 1  431 ? 13.643  -16.672 -19.336 1    30.743  ? 431  GLU   A CG  1 1 
ATOM   3482  C  CD  . GLU   A 1  431 ? 13.811  -17.868 -20.278 1    37.673  ? 431  GLU   A CD  1 1 
ATOM   3483  O  OE1 . GLU   A 1  431 ? 12.772  -18.476 -20.6   1    37.778  ? 431  GLU   A OE1 1 1 
ATOM   3484  O  OE2 . GLU   A 1  431 ? 14.966  -18.169 -20.696 1    40.117  ? 431  GLU   A OE2 1 1 
ATOM   3485  N  N   . LYS   A 1  432 ? 14.308  -15.814 -15.724 1    16.246  ? 432  LYS   A N   1 1 
ATOM   3486  C  CA  . LYS   A 1  432 ? 13.389  -16.331 -14.718 1    15.092  ? 432  LYS   A CA  1 1 
ATOM   3487  C  C   . LYS   A 1  432 ? 13.376  -15.486 -13.443 1    15.86   ? 432  LYS   A C   1 1 
ATOM   3488  O  O   . LYS   A 1  432 ? 12.291  -15.227 -12.884 1    17.745  ? 432  LYS   A O   1 1 
ATOM   3489  C  CB  . LYS   A 1  432 ? 13.714  -17.758 -14.268 1    15.719  ? 432  LYS   A CB  1 1 
ATOM   3490  C  CG  . LYS   A 1  432 ? 13.724  -18.726 -15.495 1    18.817  ? 432  LYS   A CG  1 1 
ATOM   3491  C  CD  . LYS   A 1  432 ? 12.29   -18.942 -15.991 1    19.197  ? 432  LYS   A CD  1 1 
ATOM   3492  C  CE  . LYS   A 1  432 ? 12.279  -19.873 -17.218 1    22.041  ? 432  LYS   A CE  1 1 
ATOM   3493  N  NZ  . LYS   A 1  432 ? 10.936  -20.177 -17.74  1    19.707  ? 432  LYS   A NZ  1 1 
ATOM   3494  N  N   A ILE   A 1  433 ? 14.566  -15.125 -12.922 0.6  14.073  ? 433  ILE   A N   1 1 
ATOM   3495  N  N   B ILE   A 1  433 ? 14.567  -15.106 -12.95  0.4  14.336  ? 433  ILE   A N   1 1 
ATOM   3496  C  CA  A ILE   A 1  433 ? 14.61   -14.36  -11.678 0.6  12.98   ? 433  ILE   A CA  1 1 
ATOM   3497  C  CA  B ILE   A 1  433 ? 14.664  -14.332 -11.72  0.4  13.247  ? 433  ILE   A CA  1 1 
ATOM   3498  C  C   A ILE   A 1  433 ? 14.206  -12.901 -11.935 0.6  13.026  ? 433  ILE   A C   1 1 
ATOM   3499  C  C   B ILE   A 1  433 ? 14.188  -12.905 -11.957 0.4  13.139  ? 433  ILE   A C   1 1 
ATOM   3500  O  O   A ILE   A 1  433 ? 13.474  -12.319 -11.119 0.6  12.764  ? 433  ILE   A O   1 1 
ATOM   3501  O  O   B ILE   A 1  433 ? 13.446  -12.351 -11.136 0.4  12.913  ? 433  ILE   A O   1 1 
ATOM   3502  C  CB  A ILE   A 1  433 ? 15.994  -14.488 -10.994 0.6  12.629  ? 433  ILE   A CB  1 1 
ATOM   3503  C  CB  B ILE   A 1  433 ? 16.12   -14.319 -11.221 0.4  12.889  ? 433  ILE   A CB  1 1 
ATOM   3504  C  CG1 A ILE   A 1  433 ? 16.311  -15.965 -10.622 0.6  12.271  ? 433  ILE   A CG1 1 1 
ATOM   3505  C  CG1 B ILE   A 1  433 ? 16.525  -15.713 -10.782 0.4  12.645  ? 433  ILE   A CG1 1 1 
ATOM   3506  C  CG2 A ILE   A 1  433 ? 16.022  -13.559 -9.768  0.6  12.88   ? 433  ILE   A CG2 1 1 
ATOM   3507  C  CG2 B ILE   A 1  433 ? 16.262  -13.263 -10.115 0.4  13.04   ? 433  ILE   A CG2 1 1 
ATOM   3508  C  CD1 A ILE   A 1  433 ? 17.76   -16.268 -10.194 0.6  12.134  ? 433  ILE   A CD1 1 1 
ATOM   3509  C  CD1 B ILE   A 1  433 ? 15.663  -16.303 -9.674  0.4  11.941  ? 433  ILE   A CD1 1 1 
ATOM   3510  N  N   . ALA   A 1  434 ? 14.642  -12.298 -13.066 1    13.004  ? 434  ALA   A N   1 1 
ATOM   3511  C  CA  . ALA   A 1  434 ? 14.249  -10.92  -13.344 1    13.219  ? 434  ALA   A CA  1 1 
ATOM   3512  C  C   . ALA   A 1  434 ? 12.713  -10.755 -13.48  1    13.185  ? 434  ALA   A C   1 1 
ATOM   3513  O  O   . ALA   A 1  434 ? 12.197  -9.676  -13.22  1    13.455  ? 434  ALA   A O   1 1 
ATOM   3514  C  CB  . ALA   A 1  434 ? 14.902  -10.43  -14.613 1    13.746  ? 434  ALA   A CB  1 1 
ATOM   3515  N  N   . PHE   A 1  435 ? 12.008  -11.766 -13.954 1    12.636  ? 435  PHE   A N   1 1 
ATOM   3516  C  CA  . PHE   A 1  435 ? 10.535  -11.726 -14.087 1    12.531  ? 435  PHE   A CA  1 1 
ATOM   3517  C  C   . PHE   A 1  435 ? 9.804   -11.662 -12.738 1    13.649  ? 435  PHE   A C   1 1 
ATOM   3518  O  O   . PHE   A 1  435 ? 8.7     -11.084 -12.624 1    14.403  ? 435  PHE   A O   1 1 
ATOM   3519  C  CB  . PHE   A 1  435 ? 10.116  -12.989 -14.865 1    12.73   ? 435  PHE   A CB  1 1 
ATOM   3520  C  CG  . PHE   A 1  435 ? 8.603   -13.002 -15.103 1    13.67   ? 435  PHE   A CG  1 1 
ATOM   3521  C  CD1 . PHE   A 1  435 ? 8.073   -12.257 -16.165 1    15.013  ? 435  PHE   A CD1 1 1 
ATOM   3522  C  CD2 . PHE   A 1  435 ? 7.73    -13.708 -14.264 1    14.682  ? 435  PHE   A CD2 1 1 
ATOM   3523  C  CE1 . PHE   A 1  435 ? 6.666   -12.191 -16.366 1    14.296  ? 435  PHE   A CE1 1 1 
ATOM   3524  C  CE2 . PHE   A 1  435 ? 6.323   -13.63  -14.457 1    13.843  ? 435  PHE   A CE2 1 1 
ATOM   3525  C  CZ  . PHE   A 1  435 ? 5.826   -12.909 -15.518 1    13.031  ? 435  PHE   A CZ  1 1 
ATOM   3526  N  N   . LEU   A 1  436 ? 10.362  -12.294 -11.7   1    13.712  ? 436  LEU   A N   1 1 
ATOM   3527  C  CA  . LEU   A 1  436 ? 9.646   -12.506 -10.443 1    15.189  ? 436  LEU   A CA  1 1 
ATOM   3528  C  C   . LEU   A 1  436 ? 8.934   -11.253 -9.909  1    15.082  ? 436  LEU   A C   1 1 
ATOM   3529  O  O   . LEU   A 1  436 ? 7.736   -11.35  -9.576  1    14.527  ? 436  LEU   A O   1 1 
ATOM   3530  C  CB  . LEU   A 1  436 ? 10.506  -13.186 -9.382  1    14.797  ? 436  LEU   A CB  1 1 
ATOM   3531  C  CG  . LEU   A 1  436 ? 10.93   -14.631 -9.719  1    16.438  ? 436  LEU   A CG  1 1 
ATOM   3532  C  CD1 . LEU   A 1  436 ? 11.996  -15.102 -8.687  1    16.693  ? 436  LEU   A CD1 1 1 
ATOM   3533  C  CD2 . LEU   A 1  436 ? 9.749   -15.595 -9.769  1    15.661  ? 436  LEU   A CD2 1 1 
ATOM   3534  N  N   . PRO   A 1  437 ? 9.662   -10.127 -9.717  1    15.784  ? 437  PRO   A N   1 1 
ATOM   3535  C  CA  . PRO   A 1  437 ? 9.079   -8.898  -9.156  1    15.044  ? 437  PRO   A CA  1 1 
ATOM   3536  C  C   . PRO   A 1  437 ? 7.947   -8.477  -10.078 1    15.883  ? 437  PRO   A C   1 1 
ATOM   3537  O  O   . PRO   A 1  437 ? 6.922   -8.036  -9.586  1    14.87   ? 437  PRO   A O   1 1 
ATOM   3538  C  CB  . PRO   A 1  437 ? 10.172  -7.836  -9.198  1    16.655  ? 437  PRO   A CB  1 1 
ATOM   3539  C  CG  . PRO   A 1  437 ? 11.33   -8.466  -10.011 1    17.166  ? 437  PRO   A CG  1 1 
ATOM   3540  C  CD  . PRO   A 1  437 ? 11.128  -9.974  -9.936  1    16.437  ? 437  PRO   A CD  1 1 
ATOM   3541  N  N   . PHE   A 1  438 ? 8.126   -8.59   -11.395 1    14.11   ? 438  PHE   A N   1 1 
ATOM   3542  C  CA  . PHE   A 1  438 ? 7.06    -8.097  -12.281 1    15.033  ? 438  PHE   A CA  1 1 
ATOM   3543  C  C   . PHE   A 1  438 ? 5.837   -9.002  -12.191 1    15.43   ? 438  PHE   A C   1 1 
ATOM   3544  O  O   . PHE   A 1  438 ? 4.694   -8.532  -12.143 1    15.227  ? 438  PHE   A O   1 1 
ATOM   3545  C  CB  . PHE   A 1  438 ? 7.592   -8.022  -13.707 1    14.111  ? 438  PHE   A CB  1 1 
ATOM   3546  C  CG  . PHE   A 1  438 ? 6.583   -7.432  -14.692 1    14.547  ? 438  PHE   A CG  1 1 
ATOM   3547  C  CD1 . PHE   A 1  438 ? 6.371   -6.065  -14.739 1    15.128  ? 438  PHE   A CD1 1 1 
ATOM   3548  C  CD2 . PHE   A 1  438 ? 5.867   -8.261  -15.562 1    13.655  ? 438  PHE   A CD2 1 1 
ATOM   3549  C  CE1 . PHE   A 1  438 ? 5.417   -5.503  -15.612 1    15.804  ? 438  PHE   A CE1 1 1 
ATOM   3550  C  CE2 . PHE   A 1  438 ? 4.956   -7.697  -16.492 1    14.841  ? 438  PHE   A CE2 1 1 
ATOM   3551  C  CZ  . PHE   A 1  438 ? 4.74    -6.324  -16.515 1    16.178  ? 438  PHE   A CZ  1 1 
ATOM   3552  N  N   . GLY   A 1  439 ? 6.059   -10.329 -12.268 1    14.35   ? 439  GLY   A N   1 1 
ATOM   3553  C  CA  . GLY   A 1  439 ? 4.991   -11.295 -12.075 1    12.464  ? 439  GLY   A CA  1 1 
ATOM   3554  C  C   . GLY   A 1  439 ? 4.233   -11.074 -10.773 1    15.684  ? 439  GLY   A C   1 1 
ATOM   3555  O  O   . GLY   A 1  439 ? 3.027   -11.327 -10.741 1    14.328  ? 439  GLY   A O   1 1 
ATOM   3556  N  N   . TYR   A 1  440 ? 4.915   -10.619 -9.696  1    14.028  ? 440  TYR   A N   1 1 
ATOM   3557  C  CA  . TYR   A 1  440 ? 4.228   -10.459 -8.43   1    14.389  ? 440  TYR   A CA  1 1 
ATOM   3558  C  C   . TYR   A 1  440 ? 3.441   -9.133  -8.429  1    14.954  ? 440  TYR   A C   1 1 
ATOM   3559  O  O   . TYR   A 1  440 ? 2.279   -9.074  -7.948  1    17.575  ? 440  TYR   A O   1 1 
ATOM   3560  C  CB  . TYR   A 1  440 ? 5.336   -10.345 -7.388  1    16.012  ? 440  TYR   A CB  1 1 
ATOM   3561  C  CG  . TYR   A 1  440 ? 4.823   -10.394 -5.953  1    18.752  ? 440  TYR   A CG  1 1 
ATOM   3562  C  CD1 . TYR   A 1  440 ? 3.642   -11.024 -5.616  1    21.841  ? 440  TYR   A CD1 1 1 
ATOM   3563  C  CD2 . TYR   A 1  440 ? 5.475   -9.701  -4.96   1    20.887  ? 440  TYR   A CD2 1 1 
ATOM   3564  C  CE1 . TYR   A 1  440 ? 3.162   -11.016 -4.306  1    24.294  ? 440  TYR   A CE1 1 1 
ATOM   3565  C  CE2 . TYR   A 1  440 ? 5.076   -9.773  -3.628  1    24.021  ? 440  TYR   A CE2 1 1 
ATOM   3566  C  CZ  . TYR   A 1  440 ? 3.882   -10.382 -3.301  1    23.081  ? 440  TYR   A CZ  1 1 
ATOM   3567  O  OH  . TYR   A 1  440 ? 3.47    -10.387 -1.98   1    20.767  ? 440  TYR   A OH  1 1 
ATOM   3568  N  N   . LEU   A 1  441 ? 3.999   -8.084  -9.043  1    13.54   ? 441  LEU   A N   1 1 
ATOM   3569  C  CA  . LEU   A 1  441 ? 3.472   -6.73   -8.826  1    13.925  ? 441  LEU   A CA  1 1 
ATOM   3570  C  C   . LEU   A 1  441 ? 2.212   -6.446  -9.635  1    13.907  ? 441  LEU   A C   1 1 
ATOM   3571  O  O   . LEU   A 1  441 ? 1.43    -5.566  -9.258  1    15.128  ? 441  LEU   A O   1 1 
ATOM   3572  C  CB  . LEU   A 1  441 ? 4.475   -5.596  -9.003  1    13.681  ? 441  LEU   A CB  1 1 
ATOM   3573  C  CG  . LEU   A 1  441 ? 4.893   -5.249  -10.457 1    12.646  ? 441  LEU   A CG  1 1 
ATOM   3574  C  CD1 . LEU   A 1  441 ? 3.99    -4.218  -11.177 1    12.173  ? 441  LEU   A CD1 1 1 
ATOM   3575  C  CD2 . LEU   A 1  441 ? 6.362   -4.747  -10.425 1    12.657  ? 441  LEU   A CD2 1 1 
ATOM   3576  N  N   . VAL   A 1  442 ? 2.066   -7.047  -10.831 1    11.858  ? 442  VAL   A N   1 1 
ATOM   3577  C  CA  . VAL   A 1  442 ? 0.999   -6.638  -11.731 1    12.588  ? 442  VAL   A CA  1 1 
ATOM   3578  C  C   . VAL   A 1  442 ? -0.376  -6.794  -11.076 1    12.121  ? 442  VAL   A C   1 1 
ATOM   3579  O  O   . VAL   A 1  442 ? -1.22   -5.88   -11.181 1    13.867  ? 442  VAL   A O   1 1 
ATOM   3580  C  CB  . VAL   A 1  442 ? 1.044   -7.382  -13.101 1    12.5    ? 442  VAL   A CB  1 1 
ATOM   3581  C  CG1 . VAL   A 1  442 ? -0.208  -7.133  -13.955 1    13.169  ? 442  VAL   A CG1 1 1 
ATOM   3582  C  CG2 . VAL   A 1  442 ? 2.275   -6.985  -13.951 1    12.643  ? 442  VAL   A CG2 1 1 
ATOM   3583  N  N   . ASP   A 1  443 ? -0.675  -7.952  -10.47  1    11.75   ? 443  ASP   A N   1 1 
ATOM   3584  C  CA  . ASP   A 1  443 ? -1.982  -8.123  -9.846  1    13.647  ? 443  ASP   A CA  1 1 
ATOM   3585  C  C   . ASP   A 1  443 ? -2.02   -7.427  -8.491  1    13.324  ? 443  ASP   A C   1 1 
ATOM   3586  O  O   . ASP   A 1  443 ? -3.118  -7.18   -7.987  1    14.096  ? 443  ASP   A O   1 1 
ATOM   3587  C  CB  . ASP   A 1  443 ? -2.461  -9.569  -9.822  1    14.826  ? 443  ASP   A CB  1 1 
ATOM   3588  C  CG  . ASP   A 1  443 ? -3.086  -10.021 -11.15  1    16.315  ? 443  ASP   A CG  1 1 
ATOM   3589  O  OD1 . ASP   A 1  443 ? -3.153  -9.17   -12.082 1    15.65   ? 443  ASP   A OD1 1 1 
ATOM   3590  O  OD2 . ASP   A 1  443 ? -3.414  -11.23  -11.26  1    16.576  ? 443  ASP   A OD2 1 1 
ATOM   3591  N  N   . GLN   A 1  444 ? -0.86   -7.128  -7.879  1    13.206  ? 444  GLN   A N   1 1 
ATOM   3592  C  CA  . GLN   A 1  444 ? -1.017  -6.262  -6.692  1    14.429  ? 444  GLN   A CA  1 1 
ATOM   3593  C  C   . GLN   A 1  444 ? -1.59   -4.901  -7.122  1    13.324  ? 444  GLN   A C   1 1 
ATOM   3594  O  O   . GLN   A 1  444 ? -2.463  -4.327  -6.428  1    14.627  ? 444  GLN   A O   1 1 
ATOM   3595  C  CB  . GLN   A 1  444 ? 0.273   -5.894  -5.953  1    16.507  ? 444  GLN   A CB  1 1 
ATOM   3596  C  CG  . GLN   A 1  444 ? 0.948   -7.154  -5.421  1    23.493  ? 444  GLN   A CG  1 1 
ATOM   3597  C  CD  . GLN   A 1  444 ? 2.003   -6.879  -4.384  1    28.452  ? 444  GLN   A CD  1 1 
ATOM   3598  O  OE1 . GLN   A 1  444 ? 1.793   -6.059  -3.481  1    30.769  ? 444  GLN   A OE1 1 1 
ATOM   3599  N  NE2 . GLN   A 1  444 ? 3.156   -7.524  -4.571  1    27.981  ? 444  GLN   A NE2 1 1 
ATOM   3600  N  N   . TRP   A 1  445 ? -1.132  -4.406  -8.284  1    11.629  ? 445  TRP   A N   1 1 
ATOM   3601  C  CA  . TRP   A 1  445 ? -1.686  -3.182  -8.815  1    11.971  ? 445  TRP   A CA  1 1 
ATOM   3602  C  C   . TRP   A 1  445 ? -3.194  -3.372  -9.072  1    12.111  ? 445  TRP   A C   1 1 
ATOM   3603  O  O   . TRP   A 1  445 ? -4.042  -2.527  -8.671  1    11.759  ? 445  TRP   A O   1 1 
ATOM   3604  C  CB  . TRP   A 1  445 ? -0.931  -2.738  -10.088 1    11.708  ? 445  TRP   A CB  1 1 
ATOM   3605  C  CG  . TRP   A 1  445 ? -1.527  -1.472  -10.645 1    12.937  ? 445  TRP   A CG  1 1 
ATOM   3606  C  CD1 . TRP   A 1  445 ? -1.211  -0.198  -10.267 1    14.456  ? 445  TRP   A CD1 1 1 
ATOM   3607  C  CD2 . TRP   A 1  445 ? -2.494  -1.334  -11.708 1    13.787  ? 445  TRP   A CD2 1 1 
ATOM   3608  N  NE1 . TRP   A 1  445 ? -2.012  0.708   -10.938 1    14.469  ? 445  TRP   A NE1 1 1 
ATOM   3609  C  CE2 . TRP   A 1  445 ? -2.743  0.046   -11.878 1    14.868  ? 445  TRP   A CE2 1 1 
ATOM   3610  C  CE3 . TRP   A 1  445 ? -3.137  -2.251  -12.548 1    13.925  ? 445  TRP   A CE3 1 1 
ATOM   3611  C  CZ2 . TRP   A 1  445 ? -3.648  0.541   -12.812 1    16.333  ? 445  TRP   A CZ2 1 1 
ATOM   3612  C  CZ3 . TRP   A 1  445 ? -4.055  -1.761  -13.453 1    14.53   ? 445  TRP   A CZ3 1 1 
ATOM   3613  C  CH2 . TRP   A 1  445 ? -4.293  -0.403  -13.582 1    15.348  ? 445  TRP   A CH2 1 1 
ATOM   3614  N  N   . ARG   A 1  446 ? -3.54   -4.43   -9.823  1    11.921  ? 446  ARG   A N   1 1 
ATOM   3615  C  CA  . ARG   A 1  446 ? -4.938  -4.564  -10.199 1    13.495  ? 446  ARG   A CA  1 1 
ATOM   3616  C  C   . ARG   A 1  446 ? -5.871  -4.932  -9.051  1    13.357  ? 446  ARG   A C   1 1 
ATOM   3617  O  O   . ARG   A 1  446 ? -7.035  -4.569  -9.085  1    12.912  ? 446  ARG   A O   1 1 
ATOM   3618  C  CB  . ARG   A 1  446 ? -4.815  -5.541  -11.359 1    15.912  ? 446  ARG   A CB  1 1 
ATOM   3619  C  CG  . ARG   A 1  446 ? -6.069  -5.829  -12.134 1    18.78   ? 446  ARG   A CG  1 1 
ATOM   3620  C  CD  . ARG   A 1  446 ? -5.748  -6.135  -13.599 1    18.264  ? 446  ARG   A CD  1 1 
ATOM   3621  N  NE  . ARG   A 1  446 ? -4.802  -7.276  -13.695 1    15.792  ? 446  ARG   A NE  1 1 
ATOM   3622  C  CZ  . ARG   A 1  446 ? -4.604  -8.034  -14.802 1    17.222  ? 446  ARG   A CZ  1 1 
ATOM   3623  N  NH1 . ARG   A 1  446 ? -5.327  -7.826  -15.89  1    13.316  ? 446  ARG   A NH1 1 1 
ATOM   3624  N  NH2 . ARG   A 1  446 ? -3.674  -9.012  -14.8   1    15.297  ? 446  ARG   A NH2 1 1 
ATOM   3625  N  N   . TRP   A 1  447 ? -5.376  -5.691  -8.063  1    12.759  ? 447  TRP   A N   1 1 
ATOM   3626  C  CA  . TRP   A 1  447 ? -6.212  -5.955  -6.888  1    13.638  ? 447  TRP   A CA  1 1 
ATOM   3627  C  C   . TRP   A 1  447 ? -6.523  -4.64   -6.179  1    14.414  ? 447  TRP   A C   1 1 
ATOM   3628  O  O   . TRP   A 1  447 ? -7.649  -4.481  -5.716  1    13.677  ? 447  TRP   A O   1 1 
ATOM   3629  C  CB  . TRP   A 1  447 ? -5.505  -6.891  -5.904  1    13.802  ? 447  TRP   A CB  1 1 
ATOM   3630  C  CG  . TRP   A 1  447 ? -5.314  -8.273  -6.469  1    13.633  ? 447  TRP   A CG  1 1 
ATOM   3631  C  CD1 . TRP   A 1  447 ? -5.992  -8.891  -7.494  1    13.832  ? 447  TRP   A CD1 1 1 
ATOM   3632  C  CD2 . TRP   A 1  447 ? -4.374  -9.249  -5.957  1    15.133  ? 447  TRP   A CD2 1 1 
ATOM   3633  N  NE1 . TRP   A 1  447 ? -5.495  -10.166 -7.693  1    15.884  ? 447  TRP   A NE1 1 1 
ATOM   3634  C  CE2 . TRP   A 1  447 ? -4.511  -10.416 -6.756  1    15.11   ? 447  TRP   A CE2 1 1 
ATOM   3635  C  CE3 . TRP   A 1  447 ? -3.409  -9.201  -4.931  1    15.221  ? 447  TRP   A CE3 1 1 
ATOM   3636  C  CZ2 . TRP   A 1  447 ? -3.71   -11.559 -6.57   1    14.668  ? 447  TRP   A CZ2 1 1 
ATOM   3637  C  CZ3 . TRP   A 1  447 ? -2.634  -10.335 -4.736  1    15.007  ? 447  TRP   A CZ3 1 1 
ATOM   3638  C  CH2 . TRP   A 1  447 ? -2.779  -11.466 -5.57   1    14.708  ? 447  TRP   A CH2 1 1 
ATOM   3639  N  N   . GLY   A 1  448 ? -5.561  -3.691  -6.192  1    14.689  ? 448  GLY   A N   1 1 
ATOM   3640  C  CA  . GLY   A 1  448 ? -5.832  -2.409  -5.539  1    14.303  ? 448  GLY   A CA  1 1 
ATOM   3641  C  C   . GLY   A 1  448 ? -6.854  -1.592  -6.34   1    14.159  ? 448  GLY   A C   1 1 
ATOM   3642  O  O   . GLY   A 1  448 ? -7.608  -0.793  -5.794  1    13.86   ? 448  GLY   A O   1 1 
ATOM   3643  N  N   . VAL   A 1  449 ? -6.783  -1.696  -7.667  1    13.804  ? 449  VAL   A N   1 1 
ATOM   3644  C  CA  . VAL   A 1  449 ? -7.745  -0.969  -8.481  1    14.126  ? 449  VAL   A CA  1 1 
ATOM   3645  C  C   . VAL   A 1  449 ? -9.143  -1.584  -8.268  1    14.767  ? 449  VAL   A C   1 1 
ATOM   3646  O  O   . VAL   A 1  449 ? -10.134 -0.878  -8.073  1    17.205  ? 449  VAL   A O   1 1 
ATOM   3647  C  CB  . VAL   A 1  449 ? -7.307  -0.985  -9.96   1    14.322  ? 449  VAL   A CB  1 1 
ATOM   3648  C  CG1 . VAL   A 1  449 ? -8.489  -0.519  -10.842 1    15.056  ? 449  VAL   A CG1 1 1 
ATOM   3649  C  CG2 . VAL   A 1  449 ? -6.014  -0.222  -10.258 1    14.186  ? 449  VAL   A CG2 1 1 
ATOM   3650  N  N   . PHE   A 1  450 ? -9.265  -2.921  -8.282  1    14.731  ? 450  PHE   A N   1 1 
ATOM   3651  C  CA  . PHE   A 1  450 ? -10.579 -3.537  -8.098  1    14.896  ? 450  PHE   A CA  1 1 
ATOM   3652  C  C   . PHE   A 1  450 ? -11.114 -3.257  -6.697  1    15.845  ? 450  PHE   A C   1 1 
ATOM   3653  O  O   . PHE   A 1  450 ? -12.31  -3.063  -6.535  1    15.432  ? 450  PHE   A O   1 1 
ATOM   3654  C  CB  . PHE   A 1  450 ? -10.513 -5.059  -8.304  1    14.38   ? 450  PHE   A CB  1 1 
ATOM   3655  C  CG  . PHE   A 1  450 ? -10.465 -5.473  -9.782  1    15.065  ? 450  PHE   A CG  1 1 
ATOM   3656  C  CD1 . PHE   A 1  450 ? -11.45  -5.028  -10.688 1    15.987  ? 450  PHE   A CD1 1 1 
ATOM   3657  C  CD2 . PHE   A 1  450 ? -9.541  -6.434  -10.209 1    16.322  ? 450  PHE   A CD2 1 1 
ATOM   3658  C  CE1 . PHE   A 1  450 ? -11.405 -5.438  -12.03  1    16.112  ? 450  PHE   A CE1 1 1 
ATOM   3659  C  CE2 . PHE   A 1  450 ? -9.51   -6.873  -11.535 1    16.027  ? 450  PHE   A CE2 1 1 
ATOM   3660  C  CZ  . PHE   A 1  450 ? -10.467 -6.379  -12.438 1    16.683  ? 450  PHE   A CZ  1 1 
ATOM   3661  N  N   . SER   A 1  451 ? -10.258 -3.197  -5.686  1    15.324  ? 451  SER   A N   1 1 
ATOM   3662  C  CA  . SER   A 1  451 ? -10.819 -2.989  -4.366  1    17.22   ? 451  SER   A CA  1 1 
ATOM   3663  C  C   . SER   A 1  451 ? -11.1   -1.498  -4.133  1    19.092  ? 451  SER   A C   1 1 
ATOM   3664  O  O   . SER   A 1  451 ? -11.718 -1.165  -3.122  1    17.997  ? 451  SER   A O   1 1 
ATOM   3665  C  CB  . SER   A 1  451 ? -9.886  -3.472  -3.288  1    19.137  ? 451  SER   A CB  1 1 
ATOM   3666  O  OG  . SER   A 1  451 ? -8.777  -2.583  -3.258  1    18.298  ? 451  SER   A OG  1 1 
ATOM   3667  N  N   . GLY   A 1  452 ? -10.668 -0.623  -5.062  1    18.302  ? 452  GLY   A N   1 1 
ATOM   3668  C  CA  . GLY   A 1  452 ? -10.89  0.816   -4.866  1    18.954  ? 452  GLY   A CA  1 1 
ATOM   3669  C  C   . GLY   A 1  452 ? -9.775  1.502   -4.05   1    18.221  ? 452  GLY   A C   1 1 
ATOM   3670  O  O   . GLY   A 1  452 ? -9.773  2.716   -3.893  1    20.222  ? 452  GLY   A O   1 1 
ATOM   3671  N  N   . ARG   A 1  453 ? -8.797  0.781   -3.527  1    17.847  ? 453  ARG   A N   1 1 
ATOM   3672  C  CA  . ARG   A 1  453 ? -7.611  1.418   -2.938  1    19.732  ? 453  ARG   A CA  1 1 
ATOM   3673  C  C   . ARG   A 1  453 ? -6.841  2.311   -3.934  1    18.061  ? 453  ARG   A C   1 1 
ATOM   3674  O  O   . ARG   A 1  453 ? -6.231  3.308   -3.538  1    18.349  ? 453  ARG   A O   1 1 
ATOM   3675  C  CB  . ARG   A 1  453 ? -6.639  0.386   -2.334  1    22.576  ? 453  ARG   A CB  1 1 
ATOM   3676  C  CG  . ARG   A 1  453 ? -7.419  -0      -1.078  1    34.64   ? 453  ARG   A CG  1 1 
ATOM   3677  C  CD  . ARG   A 1  453 ? -6.626  -0.952  -0.206  1    51.437  ? 453  ARG   A CD  1 1 
ATOM   3678  N  NE  . ARG   A 1  453 ? -7.315  -1.402  1.018   1    68.325  ? 453  ARG   A NE  1 1 
ATOM   3679  C  CZ  . ARG   A 1  453 ? -6.876  -1.144  2.26    1    76.161  ? 453  ARG   A CZ  1 1 
ATOM   3680  N  NH1 . ARG   A 1  453 ? -6.05   -0.127  2.494   1    81.037  ? 453  ARG   A NH1 1 1 
ATOM   3681  N  NH2 . ARG   A 1  453 ? -7.298  -1.878  3.276   1    68.456  ? 453  ARG   A NH2 1 1 
ATOM   3682  N  N   . THR   A 1  454 ? -6.781  1.911   -5.213  1    16.842  ? 454  THR   A N   1 1 
ATOM   3683  C  CA  . THR   A 1  454 ? -6.226  2.735   -6.278  1    15.576  ? 454  THR   A CA  1 1 
ATOM   3684  C  C   . THR   A 1  454 ? -7.387  3.247   -7.159  1    15.505  ? 454  THR   A C   1 1 
ATOM   3685  O  O   . THR   A 1  454 ? -7.844  2.532   -8.063  1    14.675  ? 454  THR   A O   1 1 
ATOM   3686  C  CB  . THR   A 1  454 ? -5.242  1.889   -7.105  1    15.923  ? 454  THR   A CB  1 1 
ATOM   3687  O  OG1 . THR   A 1  454 ? -4.239  1.412   -6.194  1    15.11   ? 454  THR   A OG1 1 1 
ATOM   3688  C  CG2 . THR   A 1  454 ? -4.585  2.714   -8.215  1    14.064  ? 454  THR   A CG2 1 1 
ATOM   3689  N  N   . PRO   A 1  455 ? -7.882  4.486   -6.929  1    15.985  ? 455  PRO   A N   1 1 
ATOM   3690  C  CA  . PRO   A 1  455 ? -8.86   5.118   -7.804  1    16.568  ? 455  PRO   A CA  1 1 
ATOM   3691  C  C   . PRO   A 1  455 ? -8.169  5.586   -9.075  1    17.55   ? 455  PRO   A C   1 1 
ATOM   3692  O  O   . PRO   A 1  455 ? -6.936  5.634   -9.164  1    16.763  ? 455  PRO   A O   1 1 
ATOM   3693  C  CB  . PRO   A 1  455 ? -9.406  6.353   -6.966  1    18.257  ? 455  PRO   A CB  1 1 
ATOM   3694  C  CG  . PRO   A 1  455 ? -8.218  6.686   -6.085  1    18.598  ? 455  PRO   A CG  1 1 
ATOM   3695  C  CD  . PRO   A 1  455 ? -7.568  5.336   -5.746  1    16.25   ? 455  PRO   A CD  1 1 
ATOM   3696  N  N   . PRO   A 1  456 ? -8.939  5.933   -10.121 1    18.605  ? 456  PRO   A N   1 1 
ATOM   3697  C  CA  . PRO   A 1  456 ? -8.322  6.499   -11.343 1    18.447  ? 456  PRO   A CA  1 1 
ATOM   3698  C  C   . PRO   A 1  456 ? -7.299  7.607   -11.142 1    18.207  ? 456  PRO   A C   1 1 
ATOM   3699  O  O   . PRO   A 1  456 ? -6.324  7.63    -11.878 1    18.847  ? 456  PRO   A O   1 1 
ATOM   3700  C  CB  . PRO   A 1  456 ? -9.492  6.985   -12.215 1    19.099  ? 456  PRO   A CB  1 1 
ATOM   3701  C  CG  . PRO   A 1  456 ? -10.67  6.129   -11.699 1    19.059  ? 456  PRO   A CG  1 1 
ATOM   3702  C  CD  . PRO   A 1  456 ? -10.393 5.74    -10.223 1    18.408  ? 456  PRO   A CD  1 1 
ATOM   3703  N  N   . SER   A 1  457 ? -7.495  8.48    -10.132 1    18.766  ? 457  SER   A N   1 1 
ATOM   3704  C  CA  . SER   A 1  457 ? -6.571  9.578   -9.858  1    19.394  ? 457  SER   A CA  1 1 
ATOM   3705  C  C   . SER   A 1  457 ? -5.173  9.095   -9.419  1    17.819  ? 457  SER   A C   1 1 
ATOM   3706  O  O   . SER   A 1  457 ? -4.236  9.901   -9.374  1    18.487  ? 457  SER   A O   1 1 
ATOM   3707  C  CB  . SER   A 1  457 ? -7.14   10.517  -8.772  1    21.884  ? 457  SER   A CB  1 1 
ATOM   3708  O  OG  . SER   A 1  457 ? -7.19   9.718   -7.593  1    20.771  ? 457  SER   A OG  1 1 
ATOM   3709  N  N   . ARG   A 1  458 ? -5.025  7.8     -9.133  1    15.735  ? 458  ARG   A N   1 1 
ATOM   3710  C  CA  . ARG   A 1  458 ? -3.723  7.289   -8.715  1    14.628  ? 458  ARG   A CA  1 1 
ATOM   3711  C  C   . ARG   A 1  458 ? -3.302  6.076   -9.532  1    13.652  ? 458  ARG   A C   1 1 
ATOM   3712  O  O   . ARG   A 1  458 ? -2.36   5.36    -9.11   1    13.275  ? 458  ARG   A O   1 1 
ATOM   3713  C  CB  . ARG   A 1  458 ? -3.755  6.855   -7.236  1    15.415  ? 458  ARG   A CB  1 1 
ATOM   3714  C  CG  . ARG   A 1  458 ? -3.763  8.069   -6.304  1    16.052  ? 458  ARG   A CG  1 1 
ATOM   3715  C  CD  . ARG   A 1  458 ? -3.379  7.719   -4.85   1    17.183  ? 458  ARG   A CD  1 1 
ATOM   3716  N  NE  . ARG   A 1  458 ? -4.49   7.024   -4.172  1    18.317  ? 458  ARG   A NE  1 1 
ATOM   3717  C  CZ  . ARG   A 1  458 ? -5.606  7.573   -3.681  1    19.474  ? 458  ARG   A CZ  1 1 
ATOM   3718  N  NH1 . ARG   A 1  458 ? -5.859  8.875   -3.796  1    20.991  ? 458  ARG   A NH1 1 1 
ATOM   3719  N  NH2 . ARG   A 1  458 ? -6.443  6.811   -2.984  1    20.401  ? 458  ARG   A NH2 1 1 
ATOM   3720  N  N   . TYR   A 1  459 ? -3.924  5.83    -10.702 1    13.033  ? 459  TYR   A N   1 1 
ATOM   3721  C  CA  . TYR   A 1  459 ? -3.543  4.599   -11.402 1    12.642  ? 459  TYR   A CA  1 1 
ATOM   3722  C  C   . TYR   A 1  459 ? -2.031  4.591   -11.744 1    12.182  ? 459  TYR   A C   1 1 
ATOM   3723  O  O   . TYR   A 1  459 ? -1.4    3.531   -11.612 1    11.73   ? 459  TYR   A O   1 1 
ATOM   3724  C  CB  . TYR   A 1  459 ? -4.272  4.515   -12.755 1    14.118  ? 459  TYR   A CB  1 1 
ATOM   3725  C  CG  . TYR   A 1  459 ? -5.648  3.926   -12.845 1    15.83   ? 459  TYR   A CG  1 1 
ATOM   3726  C  CD1 . TYR   A 1  459 ? -6.375  3.509   -11.738 1    15.381  ? 459  TYR   A CD1 1 1 
ATOM   3727  C  CD2 . TYR   A 1  459 ? -6.272  3.906   -14.103 1    18.065  ? 459  TYR   A CD2 1 1 
ATOM   3728  C  CE1 . TYR   A 1  459 ? -7.666  3.009   -11.886 1    17.068  ? 459  TYR   A CE1 1 1 
ATOM   3729  C  CE2 . TYR   A 1  459 ? -7.575  3.443   -14.245 1    19.827  ? 459  TYR   A CE2 1 1 
ATOM   3730  C  CZ  . TYR   A 1  459 ? -8.257  2.976   -13.138 1    18.297  ? 459  TYR   A CZ  1 1 
ATOM   3731  O  OH  . TYR   A 1  459 ? -9.541  2.541   -13.271 1    19.489  ? 459  TYR   A OH  1 1 
ATOM   3732  N  N   . ASN   A 1  460 ? -1.477  5.717   -12.262 1    12.134  ? 460  ASN   A N   1 1 
ATOM   3733  C  CA  . ASN   A 1  460 ? -0.06   5.694   -12.673 1    13.244  ? 460  ASN   A CA  1 1 
ATOM   3734  C  C   . ASN   A 1  460 ? 0.884   5.873   -11.487 1    14.035  ? 460  ASN   A C   1 1 
ATOM   3735  O  O   . ASN   A 1  460 ? 1.927   5.227   -11.448 1    14.644  ? 460  ASN   A O   1 1 
ATOM   3736  C  CB  . ASN   A 1  460 ? 0.248   6.786   -13.69  1    13.076  ? 460  ASN   A CB  1 1 
ATOM   3737  C  CG  . ASN   A 1  460 ? 1.066   6.241   -14.836 1    13.844  ? 460  ASN   A CG  1 1 
ATOM   3738  O  OD1 . ASN   A 1  460 ? 0.839   5.115   -15.316 1    14.72   ? 460  ASN   A OD1 1 1 
ATOM   3739  N  ND2 . ASN   A 1  460 ? 2.095   6.976   -15.214 1    13.91   ? 460  ASN   A ND2 1 1 
ATOM   3740  N  N   . PHE   A 1  461 ? 0.465   6.684   -10.496 1    14.288  ? 461  PHE   A N   1 1 
ATOM   3741  C  CA  . PHE   A 1  461 ? 1.229   6.871   -9.266  1    14.724  ? 461  PHE   A CA  1 1 
ATOM   3742  C  C   . PHE   A 1  461 ? 1.448   5.513   -8.573  1    14.056  ? 461  PHE   A C   1 1 
ATOM   3743  O  O   . PHE   A 1  461 ? 2.579   5.167   -8.225  1    13.372  ? 461  PHE   A O   1 1 
ATOM   3744  C  CB  . PHE   A 1  461 ? 0.493   7.911   -8.414  1    16.36   ? 461  PHE   A CB  1 1 
ATOM   3745  C  CG  . PHE   A 1  461 ? 0.97    8.151   -6.966  1    16.168  ? 461  PHE   A CG  1 1 
ATOM   3746  C  CD1 . PHE   A 1  461 ? 2.221   8.69    -6.696  1    16.198  ? 461  PHE   A CD1 1 1 
ATOM   3747  C  CD2 . PHE   A 1  461 ? 0.139   7.848   -5.892  1    16.754  ? 461  PHE   A CD2 1 1 
ATOM   3748  C  CE1 . PHE   A 1  461 ? 2.639   8.979   -5.385  1    16.342  ? 461  PHE   A CE1 1 1 
ATOM   3749  C  CE2 . PHE   A 1  461 ? 0.531   8.158   -4.566  1    17.706  ? 461  PHE   A CE2 1 1 
ATOM   3750  C  CZ  . PHE   A 1  461 ? 1.794   8.739   -4.33   1    16.843  ? 461  PHE   A CZ  1 1 
ATOM   3751  N  N   . ASP   A 1  462 ? 0.389   4.711   -8.465  1    14.108  ? 462  ASP   A N   1 1 
ATOM   3752  C  CA  . ASP   A 1  462 ? 0.455   3.417   -7.8    1    14.234  ? 462  ASP   A CA  1 1 
ATOM   3753  C  C   . ASP   A 1  462 ? 1.221   2.393   -8.628  1    14.057  ? 462  ASP   A C   1 1 
ATOM   3754  O  O   . ASP   A 1  462 ? 1.925   1.556   -8.052  1    12.66   ? 462  ASP   A O   1 1 
ATOM   3755  C  CB  . ASP   A 1  462 ? -0.947  2.983   -7.364  1    15.708  ? 462  ASP   A CB  1 1 
ATOM   3756  C  CG  . ASP   A 1  462 ? -1.417  3.64    -6.078  1    18.753  ? 462  ASP   A CG  1 1 
ATOM   3757  O  OD1 . ASP   A 1  462 ? -0.667  4.507   -5.539  1    19.325  ? 462  ASP   A OD1 1 1 
ATOM   3758  O  OD2 . ASP   A 1  462 ? -2.561  3.331   -5.603  1    20.363  ? 462  ASP   A OD2 1 1 
ATOM   3759  N  N   . TRP   A 1  463 ? 1.082   2.476   -9.964  1    13.231  ? 463  TRP   A N   1 1 
ATOM   3760  C  CA  . TRP   A 1  463 ? 1.8     1.589   -10.845 1    13.289  ? 463  TRP   A CA  1 1 
ATOM   3761  C  C   . TRP   A 1  463 ? 3.294   1.821   -10.715 1    12.829  ? 463  TRP   A C   1 1 
ATOM   3762  O  O   . TRP   A 1  463 ? 4.036   0.866   -10.443 1    12.271  ? 463  TRP   A O   1 1 
ATOM   3763  C  CB  . TRP   A 1  463 ? 1.378   1.842   -12.314 1    13.746  ? 463  TRP   A CB  1 1 
ATOM   3764  C  CG  . TRP   A 1  463 ? 2.179   1.087   -13.331 1    14.578  ? 463  TRP   A CG  1 1 
ATOM   3765  C  CD1 . TRP   A 1  463 ? 3.061   1.635   -14.213 1    16.162  ? 463  TRP   A CD1 1 1 
ATOM   3766  C  CD2 . TRP   A 1  463 ? 2.043   -0.288  -13.699 1    14.487  ? 463  TRP   A CD2 1 1 
ATOM   3767  N  NE1 . TRP   A 1  463 ? 3.583   0.677   -15.039 1    15.448  ? 463  TRP   A NE1 1 1 
ATOM   3768  C  CE2 . TRP   A 1  463 ? 2.941   -0.507  -14.773 1    15.758  ? 463  TRP   A CE2 1 1 
ATOM   3769  C  CE3 . TRP   A 1  463 ? 1.282   -1.37   -13.2   1    14.945  ? 463  TRP   A CE3 1 1 
ATOM   3770  C  CZ2 . TRP   A 1  463 ? 3.073   -1.767  -15.387 1    16.012  ? 463  TRP   A CZ2 1 1 
ATOM   3771  C  CZ3 . TRP   A 1  463 ? 1.411   -2.607  -13.827 1    15.234  ? 463  TRP   A CZ3 1 1 
ATOM   3772  C  CH2 . TRP   A 1  463 ? 2.297   -2.792  -14.892 1    15.604  ? 463  TRP   A CH2 1 1 
ATOM   3773  N  N   . TRP   A 1  464 ? 3.706   3.086   -10.75  1    13.591  ? 464  TRP   A N   1 1 
ATOM   3774  C  CA  . TRP   A 1  464 ? 5.146   3.338   -10.648 1    14.129  ? 464  TRP   A CA  1 1 
ATOM   3775  C  C   . TRP   A 1  464 ? 5.699   3.138   -9.231  1    13.729  ? 464  TRP   A C   1 1 
ATOM   3776  O  O   . TRP   A 1  464 ? 6.889   2.792   -9.059  1    13.286  ? 464  TRP   A O   1 1 
ATOM   3777  C  CB  . TRP   A 1  464 ? 5.507   4.715   -11.246 1    14.793  ? 464  TRP   A CB  1 1 
ATOM   3778  C  CG  . TRP   A 1  464 ? 5.49    4.577   -12.747 1    17.057  ? 464  TRP   A CG  1 1 
ATOM   3779  C  CD1 . TRP   A 1  464 ? 4.579   5.047   -13.654 1    17.972  ? 464  TRP   A CD1 1 1 
ATOM   3780  C  CD2 . TRP   A 1  464 ? 6.452   3.828   -13.498 1    16.506  ? 464  TRP   A CD2 1 1 
ATOM   3781  N  NE1 . TRP   A 1  464 ? 4.942   4.637   -14.914 1    15.888  ? 464  TRP   A NE1 1 1 
ATOM   3782  C  CE2 . TRP   A 1  464 ? 6.06    3.875   -14.848 1    17.502  ? 464  TRP   A CE2 1 1 
ATOM   3783  C  CE3 . TRP   A 1  464 ? 7.612   3.128   -13.147 1    18.03   ? 464  TRP   A CE3 1 1 
ATOM   3784  C  CZ2 . TRP   A 1  464 ? 6.806   3.264   -15.875 1    16.613  ? 464  TRP   A CZ2 1 1 
ATOM   3785  C  CZ3 . TRP   A 1  464 ? 8.372   2.558   -14.153 1    17.549  ? 464  TRP   A CZ3 1 1 
ATOM   3786  C  CH2 . TRP   A 1  464 ? 7.959   2.633   -15.487 1    17.41   ? 464  TRP   A CH2 1 1 
ATOM   3787  N  N   . TYR   A 1  465 ? 4.831   3.278   -8.233  1    13.796  ? 465  TYR   A N   1 1 
ATOM   3788  C  CA  . TYR   A 1  465 ? 5.234   2.991   -6.852  1    13.163  ? 465  TYR   A CA  1 1 
ATOM   3789  C  C   . TYR   A 1  465 ? 5.683   1.513   -6.798  1    12.818  ? 465  TYR   A C   1 1 
ATOM   3790  O  O   . TYR   A 1  465 ? 6.781   1.162   -6.314  1    12.113  ? 465  TYR   A O   1 1 
ATOM   3791  C  CB  . TYR   A 1  465 ? 4.07    3.258   -5.869  1    14.34   ? 465  TYR   A CB  1 1 
ATOM   3792  C  CG  . TYR   A 1  465 ? 4.412   2.632   -4.505  1    15.472  ? 465  TYR   A CG  1 1 
ATOM   3793  C  CD1 . TYR   A 1  465 ? 5.268   3.305   -3.61   1    17.703  ? 465  TYR   A CD1 1 1 
ATOM   3794  C  CD2 . TYR   A 1  465 ? 3.965   1.355   -4.151  1    16.443  ? 465  TYR   A CD2 1 1 
ATOM   3795  C  CE1 . TYR   A 1  465 ? 5.643   2.747   -2.382  1    17.522  ? 465  TYR   A CE1 1 1 
ATOM   3796  C  CE2 . TYR   A 1  465 ? 4.385   0.751   -2.942  1    17.401  ? 465  TYR   A CE2 1 1 
ATOM   3797  C  CZ  . TYR   A 1  465 ? 5.185   1.476   -2.054  1    18.261  ? 465  TYR   A CZ  1 1 
ATOM   3798  O  OH  . TYR   A 1  465 ? 5.615   0.924   -0.882  1    17.585  ? 465  TYR   A OH  1 1 
ATOM   3799  N  N   . LEU   A 1  466 ? 4.863   0.653   -7.394  1    12.524  ? 466  LEU   A N   1 1 
ATOM   3800  C  CA  . LEU   A 1  466 ? 5.074   -0.793  -7.38   1    12.61   ? 466  LEU   A CA  1 1 
ATOM   3801  C  C   . LEU   A 1  466 ? 6.241   -1.17   -8.301  1    12.867  ? 466  LEU   A C   1 1 
ATOM   3802  O  O   . LEU   A 1  466 ? 6.961   -2.063  -7.931  1    13.487  ? 466  LEU   A O   1 1 
ATOM   3803  C  CB  . LEU   A 1  466 ? 3.826   -1.571  -7.772  1    12.467  ? 466  LEU   A CB  1 1 
ATOM   3804  C  CG  . LEU   A 1  466 ? 2.676   -1.526  -6.748  1    12.791  ? 466  LEU   A CG  1 1 
ATOM   3805  C  CD1 . LEU   A 1  466 ? 1.352   -2.022  -7.356  1    13.24   ? 466  LEU   A CD1 1 1 
ATOM   3806  C  CD2 . LEU   A 1  466 ? 3.03    -2.391  -5.54   1    13.397  ? 466  LEU   A CD2 1 1 
ATOM   3807  N  N   . ARG   A 1  467 ? 6.33    -0.589  -9.502  1    12.798  ? 467  ARG   A N   1 1 
ATOM   3808  C  CA  . ARG   A 1  467 ? 7.44    -0.879  -10.405 1    13.945  ? 467  ARG   A CA  1 1 
ATOM   3809  C  C   . ARG   A 1  467 ? 8.77    -0.556  -9.723  1    13.281  ? 467  ARG   A C   1 1 
ATOM   3810  O  O   . ARG   A 1  467 ? 9.742   -1.325  -9.822  1    14.204  ? 467  ARG   A O   1 1 
ATOM   3811  C  CB  . ARG   A 1  467 ? 7.251   -0.066  -11.696 1    14.438  ? 467  ARG   A CB  1 1 
ATOM   3812  C  CG  . ARG   A 1  467 ? 5.99    -0.491  -12.458 1    15.439  ? 467  ARG   A CG  1 1 
ATOM   3813  C  CD  . ARG   A 1  467 ? 6.247   -1.651  -13.442 1    16.124  ? 467  ARG   A CD  1 1 
ATOM   3814  N  NE  . ARG   A 1  467 ? 6.715   -0.998  -14.683 1    17.372  ? 467  ARG   A NE  1 1 
ATOM   3815  C  CZ  . ARG   A 1  467 ? 7.247   -1.616  -15.753 1    18.081  ? 467  ARG   A CZ  1 1 
ATOM   3816  N  NH1 . ARG   A 1  467 ? 7.747   -2.853  -15.659 1    15.93   ? 467  ARG   A NH1 1 1 
ATOM   3817  N  NH2 . ARG   A 1  467 ? 7.471   -0.905  -16.848 1    18.753  ? 467  ARG   A NH2 1 1 
ATOM   3818  N  N   . THR   A 1  468 ? 8.85    0.588   -9.024  1    13.768  ? 468  THR   A N   1 1 
ATOM   3819  C  CA  . THR   A 1  468 ? 10.071  0.951   -8.332  1    14.885  ? 468  THR   A CA  1 1 
ATOM   3820  C  C   . THR   A 1  468 ? 10.311  -0.005  -7.157  1    15.726  ? 468  THR   A C   1 1 
ATOM   3821  O  O   . THR   A 1  468 ? 11.445  -0.498  -6.968  1    15.332  ? 468  THR   A O   1 1 
ATOM   3822  C  CB  . THR   A 1  468 ? 10.014  2.425   -7.889  1    17.527  ? 468  THR   A CB  1 1 
ATOM   3823  O  OG1 . THR   A 1  468 ? 9.903   3.081   -9.138  1    19.55   ? 468  THR   A OG1 1 1 
ATOM   3824  C  CG2 . THR   A 1  468 ? 11.325  2.909   -7.288  1    19.525  ? 468  THR   A CG2 1 1 
ATOM   3825  N  N   . LYS   A 1  469 ? 9.271   -0.16   -6.31   1    13.453  ? 469  LYS   A N   1 1 
ATOM   3826  C  CA  . LYS   A 1  469 ? 9.362   -0.963  -5.091  1    13.527  ? 469  LYS   A CA  1 1 
ATOM   3827  C  C   . LYS   A 1  469 ? 9.931   -2.355  -5.383  1    13.206  ? 469  LYS   A C   1 1 
ATOM   3828  O  O   . LYS   A 1  469 ? 10.826  -2.779  -4.674  1    13.378  ? 469  LYS   A O   1 1 
ATOM   3829  C  CB  . LYS   A 1  469 ? 8.027   -1.129  -4.349  1    13.584  ? 469  LYS   A CB  1 1 
ATOM   3830  C  CG  . LYS   A 1  469 ? 8.019   -2.114  -3.207  1    14.334  ? 469  LYS   A CG  1 1 
ATOM   3831  C  CD  . LYS   A 1  469 ? 6.704   -2.203  -2.439  1    15.378  ? 469  LYS   A CD  1 1 
ATOM   3832  C  CE  . LYS   A 1  469 ? 6.812   -3.135  -1.251  1    18.005  ? 469  LYS   A CE  1 1 
ATOM   3833  N  NZ  . LYS   A 1  469 ? 5.459   -3.251  -0.671  1    19.069  ? 469  LYS   A NZ  1 1 
ATOM   3834  N  N   . TYR   A 1  470 ? 9.358   -3.058  -6.372  1    12.812  ? 470  TYR   A N   1 1 
ATOM   3835  C  CA  . TYR   A 1  470 ? 9.689   -4.462  -6.654  1    12.971  ? 470  TYR   A CA  1 1 
ATOM   3836  C  C   . TYR   A 1  470 ? 10.802  -4.587  -7.691  1    13.3    ? 470  TYR   A C   1 1 
ATOM   3837  O  O   . TYR   A 1  470 ? 11.805  -5.297  -7.445  1    14.598  ? 470  TYR   A O   1 1 
ATOM   3838  C  CB  . TYR   A 1  470 ? 8.428   -5.202  -7.124  1    12.32   ? 470  TYR   A CB  1 1 
ATOM   3839  C  CG  . TYR   A 1  470 ? 7.542   -5.451  -5.917  1    13.687  ? 470  TYR   A CG  1 1 
ATOM   3840  C  CD1 . TYR   A 1  470 ? 7.92    -6.397  -4.964  1    13.686  ? 470  TYR   A CD1 1 1 
ATOM   3841  C  CD2 . TYR   A 1  470 ? 6.323   -4.77   -5.753  1    14.107  ? 470  TYR   A CD2 1 1 
ATOM   3842  C  CE1 . TYR   A 1  470 ? 7.169   -6.642  -3.818  1    15.983  ? 470  TYR   A CE1 1 1 
ATOM   3843  C  CE2 . TYR   A 1  470 ? 5.56    -5.044  -4.621  1    15.244  ? 470  TYR   A CE2 1 1 
ATOM   3844  C  CZ  . TYR   A 1  470 ? 5.965   -5.982  -3.683  1    16.483  ? 470  TYR   A CZ  1 1 
ATOM   3845  O  OH  . TYR   A 1  470 ? 5.167   -6.26   -2.603  1    20.701  ? 470  TYR   A OH  1 1 
ATOM   3846  N  N   . GLN   A 1  471 ? 10.634  -3.927  -8.844  1    12.89   ? 471  GLN   A N   1 1 
ATOM   3847  C  CA  . GLN   A 1  471 ? 11.589  -4.096  -9.932  1    13.533  ? 471  GLN   A CA  1 1 
ATOM   3848  C  C   . GLN   A 1  471 ? 12.808  -3.184  -9.769  1    14.238  ? 471  GLN   A C   1 1 
ATOM   3849  O  O   . GLN   A 1  471 ? 13.844  -3.499  -10.371 1    14.081  ? 471  GLN   A O   1 1 
ATOM   3850  C  CB  . GLN   A 1  471 ? 11.016  -3.874  -11.337 1    14.329  ? 471  GLN   A CB  1 1 
ATOM   3851  C  CG  . GLN   A 1  471 ? 10.166  -5.056  -11.791 1    14.337  ? 471  GLN   A CG  1 1 
ATOM   3852  C  CD  . GLN   A 1  471 ? 9.573   -4.767  -13.151 1    15.366  ? 471  GLN   A CD  1 1 
ATOM   3853  O  OE1 . GLN   A 1  471 ? 8.579   -4.024  -13.267 1    15.675  ? 471  GLN   A OE1 1 1 
ATOM   3854  N  NE2 . GLN   A 1  471 ? 10.161  -5.34   -14.2   1    13.374  ? 471  GLN   A NE2 1 1 
ATOM   3855  N  N   . GLY   A 1  472 ? 12.706  -2.042  -9.041  1    14.013  ? 472  GLY   A N   1 1 
ATOM   3856  C  CA  . GLY   A 1  472 ? 13.882  -1.16   -8.97   1    15.605  ? 472  GLY   A CA  1 1 
ATOM   3857  C  C   . GLY   A 1  472 ? 14.189  -0.544  -10.341 1    16.115  ? 472  GLY   A C   1 1 
ATOM   3858  O  O   . GLY   A 1  472 ? 15.338  -0.436  -10.769 1    17.361  ? 472  GLY   A O   1 1 
ATOM   3859  N  N   . ILE   A 1  473 ? 13.132  -0.138  -11.064 1    16.216  ? 473  ILE   A N   1 1 
ATOM   3860  C  CA  . ILE   A 1  473 ? 13.279  0.585   -12.322 1    15.962  ? 473  ILE   A CA  1 1 
ATOM   3861  C  C   . ILE   A 1  473 ? 12.519  1.904   -12.18  1    17.05   ? 473  ILE   A C   1 1 
ATOM   3862  O  O   . ILE   A 1  473 ? 11.682  2.011   -11.279 1    17.145  ? 473  ILE   A O   1 1 
ATOM   3863  C  CB  . ILE   A 1  473 ? 12.693  -0.217  -13.505 1    15.903  ? 473  ILE   A CB  1 1 
ATOM   3864  C  CG1 . ILE   A 1  473 ? 11.15   -0.501  -13.33  1    16.54   ? 473  ILE   A CG1 1 1 
ATOM   3865  C  CG2 . ILE   A 1  473 ? 13.51   -1.503  -13.697 1    16.325  ? 473  ILE   A CG2 1 1 
ATOM   3866  C  CD1 . ILE   A 1  473 ? 10.506  -1.353  -14.44  1    15.065  ? 473  ILE   A CD1 1 1 
ATOM   3867  N  N   . CYS   A 1  474 ? 12.773  2.831   -13.108 1    16.341  ? 474  CYS   A N   1 1 
ATOM   3868  C  CA  . CYS   A 1  474 ? 12.127  4.143   -13.074 1    17.674  ? 474  CYS   A CA  1 1 
ATOM   3869  C  C   . CYS   A 1  474 ? 11.771  4.468   -14.515 1    18.395  ? 474  CYS   A C   1 1 
ATOM   3870  O  O   . CYS   A 1  474 ? 12.504  4.082   -15.405 1    19.63   ? 474  CYS   A O   1 1 
ATOM   3871  C  CB  . CYS   A 1  474 ? 13.071  5.207   -12.5   1    17.423  ? 474  CYS   A CB  1 1 
ATOM   3872  S  SG  . CYS   A 1  474 ? 14.651  5.333   -13.399 1    21.175  ? 474  CYS   A SG  1 1 
ATOM   3873  N  N   . PRO   A 1  475 ? 10.725  5.273   -14.786 1    18.862  ? 475  PRO   A N   1 1 
ATOM   3874  C  CA  . PRO   A 1  475 ? 10.417  5.657   -16.161 1    19.245  ? 475  PRO   A CA  1 1 
ATOM   3875  C  C   . PRO   A 1  475 ? 11.489  6.597   -16.702 1    20.418  ? 475  PRO   A C   1 1 
ATOM   3876  O  O   . PRO   A 1  475 ? 11.991  7.466   -15.975 1    19.305  ? 475  PRO   A O   1 1 
ATOM   3877  C  CB  . PRO   A 1  475 ? 9.037   6.333   -16.068 1    18.599  ? 475  PRO   A CB  1 1 
ATOM   3878  C  CG  . PRO   A 1  475 ? 8.95    6.834   -14.641 1    18.255  ? 475  PRO   A CG  1 1 
ATOM   3879  C  CD  . PRO   A 1  475 ? 9.796   5.87    -13.795 1    18.806  ? 475  PRO   A CD  1 1 
ATOM   3880  N  N   . PRO   A 1  476 ? 11.908  6.402   -17.981 1    20.92   ? 476  PRO   A N   1 1 
ATOM   3881  C  CA  . PRO   A 1  476 ? 12.942  7.247   -18.573 1    23.997  ? 476  PRO   A CA  1 1 
ATOM   3882  C  C   . PRO   A 1  476 ? 12.501  8.636   -19.017 1    25.646  ? 476  PRO   A C   1 1 
ATOM   3883  O  O   . PRO   A 1  476 ? 13.357  9.439   -19.35  1    29.362  ? 476  PRO   A O   1 1 
ATOM   3884  C  CB  . PRO   A 1  476 ? 13.512  6.419   -19.725 1    22.787  ? 476  PRO   A CB  1 1 
ATOM   3885  C  CG  . PRO   A 1  476 ? 12.388  5.504   -20.116 1    22.869  ? 476  PRO   A CG  1 1 
ATOM   3886  C  CD  . PRO   A 1  476 ? 11.439  5.324   -18.887 1    21.638  ? 476  PRO   A CD  1 1 
ATOM   3887  N  N   . VAL   A 1  477 ? 11.183  8.938   -18.95  1    23.55   ? 477  VAL   A N   1 1 
ATOM   3888  C  CA  . VAL   A 1  477 ? 10.647  10.282  -19.159 1    22.863  ? 477  VAL   A CA  1 1 
ATOM   3889  C  C   . VAL   A 1  477 ? 9.622   10.547  -18.044 1    22.556  ? 477  VAL   A C   1 1 
ATOM   3890  O  O   . VAL   A 1  477 ? 9.136   9.599   -17.414 1    20.725  ? 477  VAL   A O   1 1 
ATOM   3891  C  CB  . VAL   A 1  477 ? 10.036  10.505  -20.571 1    24.742  ? 477  VAL   A CB  1 1 
ATOM   3892  C  CG1 . VAL   A 1  477 ? 11.089  10.32   -21.698 1    23.821  ? 477  VAL   A CG1 1 1 
ATOM   3893  C  CG2 . VAL   A 1  477 ? 8.828   9.599   -20.827 1    22.047  ? 477  VAL   A CG2 1 1 
ATOM   3894  N  N   . THR   A 1  478 ? 9.325   11.817  -17.752 1    23.236  ? 478  THR   A N   1 1 
ATOM   3895  C  CA  . THR   A 1  478 ? 8.351   12.119  -16.703 1    24.005  ? 478  THR   A CA  1 1 
ATOM   3896  C  C   . THR   A 1  478 ? 6.993   11.516  -17.061 1    22.919  ? 478  THR   A C   1 1 
ATOM   3897  O  O   . THR   A 1  478 ? 6.602   11.504  -18.233 1    23.088  ? 478  THR   A O   1 1 
ATOM   3898  C  CB  . THR   A 1  478 ? 8.267   13.637  -16.565 1    27.911  ? 478  THR   A CB  1 1 
ATOM   3899  O  OG1 . THR   A 1  478 ? 9.66    13.9    -16.402 1    30.077  ? 478  THR   A OG1 1 1 
ATOM   3900  C  CG2 . THR   A 1  478 ? 7.442   14.048  -15.353 1    25.583  ? 478  THR   A CG2 1 1 
ATOM   3901  N  N   . ARG   A 1  479 ? 6.263   10.969  -16.074 1    22.308  ? 479  ARG   A N   1 1 
ATOM   3902  C  CA  . ARG   A 1  479 ? 4.881   10.524  -16.335 1    20.091  ? 479  ARG   A CA  1 1 
ATOM   3903  C  C   . ARG   A 1  479 ? 3.949   11.277  -15.391 1    21.222  ? 479  ARG   A C   1 1 
ATOM   3904  O  O   . ARG   A 1  479 ? 4.368   11.734  -14.327 1    22.236  ? 479  ARG   A O   1 1 
ATOM   3905  C  CB  . ARG   A 1  479 ? 4.647   9.047   -16.017 1    17.697  ? 479  ARG   A CB  1 1 
ATOM   3906  C  CG  . ARG   A 1  479 ? 5.799   8.176   -16.545 1    17.35   ? 479  ARG   A CG  1 1 
ATOM   3907  C  CD  . ARG   A 1  479 ? 6.013   8.22    -18.059 1    17.059  ? 479  ARG   A CD  1 1 
ATOM   3908  N  NE  . ARG   A 1  479 ? 4.942   7.58    -18.835 1    16.915  ? 479  ARG   A NE  1 1 
ATOM   3909  C  CZ  . ARG   A 1  479 ? 4.594   7.882   -20.082 1    17.276  ? 479  ARG   A CZ  1 1 
ATOM   3910  N  NH1 . ARG   A 1  479 ? 3.674   7.157   -20.705 1    16.844  ? 479  ARG   A NH1 1 1 
ATOM   3911  N  NH2 . ARG   A 1  479 ? 5.147   8.911   -20.715 1    17.979  ? 479  ARG   A NH2 1 1 
ATOM   3912  N  N   . ASN   A 1  480 ? 2.682   11.387  -15.769 1    20.012  ? 480  ASN   A N   1 1 
ATOM   3913  C  CA  . ASN   A 1  480 ? 1.701   11.974  -14.877 1    19.406  ? 480  ASN   A CA  1 1 
ATOM   3914  C  C   . ASN   A 1  480 ? 0.411   11.161  -14.982 1    18.937  ? 480  ASN   A C   1 1 
ATOM   3915  O  O   . ASN   A 1  480 ? 0.427   10.118  -15.622 1    17.259  ? 480  ASN   A O   1 1 
ATOM   3916  C  CB  . ASN   A 1  480 ? 1.541   13.474  -15.112 1    20.959  ? 480  ASN   A CB  1 1 
ATOM   3917  C  CG  . ASN   A 1  480 ? 1.059   13.761  -16.523 1    23.74   ? 480  ASN   A CG  1 1 
ATOM   3918  O  OD1 . ASN   A 1  480 ? 0.22    13.04   -17.077 1    22.276  ? 480  ASN   A OD1 1 1 
ATOM   3919  N  ND2 . ASN   A 1  480 ? 1.571   14.817  -17.115 1    27.323  ? 480  ASN   A ND2 1 1 
ATOM   3920  N  N   . GLU   A 1  481 ? -0.693  11.623  -14.357 1    19.334  ? 481  GLU   A N   1 1 
ATOM   3921  C  CA  . GLU   A 1  481 ? -1.893  10.798  -14.367 1    20.007  ? 481  GLU   A CA  1 1 
ATOM   3922  C  C   . GLU   A 1  481 ? -2.671  10.822  -15.697 1    21.943  ? 481  GLU   A C   1 1 
ATOM   3923  O  O   . GLU   A 1  481 ? -3.653  10.103  -15.846 1    22.871  ? 481  GLU   A O   1 1 
ATOM   3924  C  CB  . GLU   A 1  481 ? -2.851  11.159  -13.246 1    21.866  ? 481  GLU   A CB  1 1 
ATOM   3925  C  CG  . GLU   A 1  481 ? -2.371  10.511  -11.962 1    21.533  ? 481  GLU   A CG  1 1 
ATOM   3926  C  CD  . GLU   A 1  481 ? -2.186  8.984   -11.892 1    19.568  ? 481  GLU   A CD  1 1 
ATOM   3927  O  OE1 . GLU   A 1  481 ? -2.718  8.103   -12.651 1    20.146  ? 481  GLU   A OE1 1 1 
ATOM   3928  O  OE2 . GLU   A 1  481 ? -1.549  8.709   -10.881 1    18.42   ? 481  GLU   A OE2 1 1 
ATOM   3929  N  N   . THR   A 1  482 ? -2.245  11.606  -16.671 1    21.832  ? 482  THR   A N   1 1 
ATOM   3930  C  CA  . THR   A 1  482 ? -2.763  11.39   -18.022 1    23.119  ? 482  THR   A CA  1 1 
ATOM   3931  C  C   . THR   A 1  482 ? -2.228  10.096  -18.614 1    20.3    ? 482  THR   A C   1 1 
ATOM   3932  O  O   . THR   A 1  482 ? -2.909  9.456   -19.402 1    20.905  ? 482  THR   A O   1 1 
ATOM   3933  C  CB  . THR   A 1  482 ? -2.455  12.597  -18.904 1    26.964  ? 482  THR   A CB  1 1 
ATOM   3934  O  OG1 . THR   A 1  482 ? -3.196  13.639  -18.253 1    30.232  ? 482  THR   A OG1 1 1 
ATOM   3935  C  CG2 . THR   A 1  482 ? -2.919  12.41   -20.34  1    28.153  ? 482  THR   A CG2 1 1 
ATOM   3936  N  N   . HIS   A 1  483 ? -0.99   9.724   -18.271 1    18.977  ? 483  HIS   A N   1 1 
ATOM   3937  C  CA  . HIS   A 1  483 ? -0.468  8.424   -18.655 1    18.451  ? 483  HIS   A CA  1 1 
ATOM   3938  C  C   . HIS   A 1  483 ? -1.133  7.264   -17.905 1    18.205  ? 483  HIS   A C   1 1 
ATOM   3939  O  O   . HIS   A 1  483 ? -1.571  7.384   -16.739 1    17.357  ? 483  HIS   A O   1 1 
ATOM   3940  C  CB  . HIS   A 1  483 ? 1.068   8.381   -18.498 1    16.986  ? 483  HIS   A CB  1 1 
ATOM   3941  C  CG  . HIS   A 1  483 ? 1.683   9.516   -19.258 1    17.81   ? 483  HIS   A CG  1 1 
ATOM   3942  N  ND1 . HIS   A 1  483 ? 2.353   10.549  -18.632 1    18.053  ? 483  HIS   A ND1 1 1 
ATOM   3943  C  CD2 . HIS   A 1  483 ? 1.584   9.843   -20.551 1    17.492  ? 483  HIS   A CD2 1 1 
ATOM   3944  C  CE1 . HIS   A 1  483 ? 2.727   11.44   -19.549 1    19.572  ? 483  HIS   A CE1 1 1 
ATOM   3945  N  NE2 . HIS   A 1  483 ? 2.266   11.006  -20.734 1    19.366  ? 483  HIS   A NE2 1 1 
ATOM   3946  N  N   . PHE   A 1  484 ? -1.148  6.106   -18.572 1    16.07   ? 484  PHE   A N   1 1 
ATOM   3947  C  CA  . PHE   A 1  484 ? -1.764  4.923   -18.007 1    15.202  ? 484  PHE   A CA  1 1 
ATOM   3948  C  C   . PHE   A 1  484 ? -0.874  3.773   -18.419 1    15.026  ? 484  PHE   A C   1 1 
ATOM   3949  O  O   . PHE   A 1  484 ? -1.195  3.019   -19.351 1    15.197  ? 484  PHE   A O   1 1 
ATOM   3950  C  CB  . PHE   A 1  484 ? -3.241  4.794   -18.444 1    15.964  ? 484  PHE   A CB  1 1 
ATOM   3951  C  CG  . PHE   A 1  484 ? -3.937  3.514   -17.992 1    17.2    ? 484  PHE   A CG  1 1 
ATOM   3952  C  CD1 . PHE   A 1  484 ? -3.73   3       -16.691 1    17.379  ? 484  PHE   A CD1 1 1 
ATOM   3953  C  CD2 . PHE   A 1  484 ? -4.775  2.797   -18.862 1    16.654  ? 484  PHE   A CD2 1 1 
ATOM   3954  C  CE1 . PHE   A 1  484 ? -4.41   1.858   -16.257 1    17.894  ? 484  PHE   A CE1 1 1 
ATOM   3955  C  CE2 . PHE   A 1  484 ? -5.4    1.634   -18.421 1    16.183  ? 484  PHE   A CE2 1 1 
ATOM   3956  C  CZ  . PHE   A 1  484 ? -5.246  1.161   -17.117 1    16.903  ? 484  PHE   A CZ  1 1 
ATOM   3957  N  N   . ASP   A 1  485 ? 0.307   3.737   -17.776 1    15.15   ? 485  ASP   A N   1 1 
ATOM   3958  C  CA  . ASP   A 1  485 ? 1.38    2.838   -18.166 1    15.303  ? 485  ASP   A CA  1 1 
ATOM   3959  C  C   . ASP   A 1  485 ? 1.026   1.38    -17.976 1    16.035  ? 485  ASP   A C   1 1 
ATOM   3960  O  O   . ASP   A 1  485 ? 1.45    0.558   -18.788 1    16.466  ? 485  ASP   A O   1 1 
ATOM   3961  C  CB  . ASP   A 1  485 ? 2.698   3.269   -17.543 1    14.273  ? 485  ASP   A CB  1 1 
ATOM   3962  C  CG  . ASP   A 1  485 ? 3.096   4.623   -18.095 1    15.952  ? 485  ASP   A CG  1 1 
ATOM   3963  O  OD1 . ASP   A 1  485 ? 2.743   4.905   -19.305 1    16.705  ? 485  ASP   A OD1 1 1 
ATOM   3964  O  OD2 . ASP   A 1  485 ? 3.702   5.412   -17.344 1    15.688  ? 485  ASP   A OD2 1 1 
ATOM   3965  N  N   . ALA   A 1  486 ? 0.21    1.063   -16.945 1    15.891  ? 486  ALA   A N   1 1 
ATOM   3966  C  CA  . ALA   A 1  486 ? -0.327  -0.28   -16.791 1    15.599  ? 486  ALA   A CA  1 1 
ATOM   3967  C  C   . ALA   A 1  486 ? -1.076  -0.734  -18.053 1    14.951  ? 486  ALA   A C   1 1 
ATOM   3968  O  O   . ALA   A 1  486 ? -1.025  -1.905  -18.372 1    14.52   ? 486  ALA   A O   1 1 
ATOM   3969  C  CB  . ALA   A 1  486 ? -1.216  -0.385  -15.523 1    14.636  ? 486  ALA   A CB  1 1 
ATOM   3970  N  N   . GLY   A 1  487 ? -1.773  0.159   -18.735 1    15.096  ? 487  GLY   A N   1 1 
ATOM   3971  C  CA  . GLY   A 1  487 ? -2.574  -0.209  -19.91  1    16.095  ? 487  GLY   A CA  1 1 
ATOM   3972  C  C   . GLY   A 1  487 ? -1.7    -0.586  -21.113 1    16.723  ? 487  GLY   A C   1 1 
ATOM   3973  O  O   . GLY   A 1  487 ? -2.2    -1.18   -22.08  1    17.096  ? 487  GLY   A O   1 1 
ATOM   3974  N  N   . ALA   A 1  488 ? -0.41   -0.221  -21.081 1    15.137  ? 488  ALA   A N   1 1 
ATOM   3975  C  CA  . ALA   A 1  488 ? 0.508   -0.592  -22.151 1    14.959  ? 488  ALA   A CA  1 1 
ATOM   3976  C  C   . ALA   A 1  488 ? 0.998   -2.039  -22.07  1    15.692  ? 488  ALA   A C   1 1 
ATOM   3977  O  O   . ALA   A 1  488 ? 1.907   -2.397  -22.839 1    16.539  ? 488  ALA   A O   1 1 
ATOM   3978  C  CB  . ALA   A 1  488 ? 1.707   0.353   -22.263 1    15.372  ? 488  ALA   A CB  1 1 
ATOM   3979  N  N   . LYS   A 1  489 ? 0.53    -2.826  -21.113 1    13.804  ? 489  LYS   A N   1 1 
ATOM   3980  C  CA  . LYS   A 1  489 ? 0.889   -4.244  -21.069 1    15.309  ? 489  LYS   A CA  1 1 
ATOM   3981  C  C   . LYS   A 1  489 ? -0.352  -5.05   -21.47  1    16.594  ? 489  LYS   A C   1 1 
ATOM   3982  O  O   . LYS   A 1  489 ? -1.377  -4.896  -20.81  1    17.022  ? 489  LYS   A O   1 1 
ATOM   3983  C  CB  . LYS   A 1  489 ? 1.209   -4.542  -19.586 1    16.366  ? 489  LYS   A CB  1 1 
ATOM   3984  C  CG  . LYS   A 1  489 ? 1.424   -6.004  -19.227 1    17.908  ? 489  LYS   A CG  1 1 
ATOM   3985  C  CD  . LYS   A 1  489 ? 2.648   -6.564  -19.954 1    18.812  ? 489  LYS   A CD  1 1 
ATOM   3986  C  CE  . LYS   A 1  489 ? 2.719   -8.083  -19.739 1    20.161  ? 489  LYS   A CE  1 1 
ATOM   3987  N  NZ  . LYS   A 1  489 ? 3.681   -8.64   -20.703 1    18.747  ? 489  LYS   A NZ  1 1 
ATOM   3988  N  N   . PHE   A 1  490 ? -0.226  -5.999  -22.4   1    14.857  ? 490  PHE   A N   1 1 
ATOM   3989  C  CA  . PHE   A 1  490 ? -1.317  -6.78   -22.979 1    14.873  ? 490  PHE   A CA  1 1 
ATOM   3990  C  C   . PHE   A 1  490 ? -2.407  -7.221  -21.99  1    14.288  ? 490  PHE   A C   1 1 
ATOM   3991  O  O   . PHE   A 1  490 ? -3.59   -7.003  -22.201 1    13.428  ? 490  PHE   A O   1 1 
ATOM   3992  C  CB  . PHE   A 1  490 ? -0.749  -8.026  -23.698 1    15.308  ? 490  PHE   A CB  1 1 
ATOM   3993  C  CG  . PHE   A 1  490 ? -1.862  -8.902  -24.264 1    17.626  ? 490  PHE   A CG  1 1 
ATOM   3994  C  CD1 . PHE   A 1  490 ? -2.318  -8.7    -25.557 1    18.119  ? 490  PHE   A CD1 1 1 
ATOM   3995  C  CD2 . PHE   A 1  490 ? -2.404  -9.94   -23.497 1    17.445  ? 490  PHE   A CD2 1 1 
ATOM   3996  C  CE1 . PHE   A 1  490 ? -3.316  -9.521  -26.094 1    21.671  ? 490  PHE   A CE1 1 1 
ATOM   3997  C  CE2 . PHE   A 1  490 ? -3.404  -10.742 -24.033 1    20.519  ? 490  PHE   A CE2 1 1 
ATOM   3998  C  CZ  . PHE   A 1  490 ? -3.87   -10.522 -25.309 1    20.413  ? 490  PHE   A CZ  1 1 
ATOM   3999  N  N   . HIS   A 1  491 ? -2.027  -7.835  -20.873 1    13.066  ? 491  HIS   A N   1 1 
ATOM   4000  C  CA  . HIS   A 1  491 ? -2.997  -8.502  -20.045 1    13.6    ? 491  HIS   A CA  1 1 
ATOM   4001  C  C   . HIS   A 1  491 ? -3.947  -7.526  -19.307 1    13.08   ? 491  HIS   A C   1 1 
ATOM   4002  O  O   . HIS   A 1  491 ? -4.987  -7.999  -18.823 1    13.745  ? 491  HIS   A O   1 1 
ATOM   4003  C  CB  . HIS   A 1  491 ? -2.247  -9.211  -18.921 1    13.651  ? 491  HIS   A CB  1 1 
ATOM   4004  C  CG  . HIS   A 1  491 ? -1.303  -10.249 -19.513 1    12.594  ? 491  HIS   A CG  1 1 
ATOM   4005  N  ND1 . HIS   A 1  491 ? -0.213  -9.939  -20.295 1    13.874  ? 491  HIS   A ND1 1 1 
ATOM   4006  C  CD2 . HIS   A 1  491 ? -1.375  -11.585 -19.427 1    12.647  ? 491  HIS   A CD2 1 1 
ATOM   4007  C  CE1 . HIS   A 1  491 ? 0.354   -11.081 -20.669 1    13.706  ? 491  HIS   A CE1 1 1 
ATOM   4008  N  NE2 . HIS   A 1  491 ? -0.352  -12.067 -20.163 1    13.549  ? 491  HIS   A NE2 1 1 
ATOM   4009  N  N   . VAL   A 1  492 ? -3.598  -6.236  -19.25  1    12.373  ? 492  VAL   A N   1 1 
ATOM   4010  C  CA  . VAL   A 1  492 ? -4.43   -5.215  -18.618 1    13.825  ? 492  VAL   A CA  1 1 
ATOM   4011  C  C   . VAL   A 1  492 ? -5.706  -4.944  -19.438 1    13.872  ? 492  VAL   A C   1 1 
ATOM   4012  O  O   . VAL   A 1  492 ? -6.835  -5.19   -18.97  1    14.648  ? 492  VAL   A O   1 1 
ATOM   4013  C  CB  . VAL   A 1  492 ? -3.661  -3.977  -18.09  1    14.875  ? 492  VAL   A CB  1 1 
ATOM   4014  C  CG1 . VAL   A 1  492 ? -4.583  -2.905  -17.478 1    14.068  ? 492  VAL   A CG1 1 1 
ATOM   4015  C  CG2 . VAL   A 1  492 ? -2.629  -4.446  -17.006 1    13.156  ? 492  VAL   A CG2 1 1 
ATOM   4016  N  N   . PRO   A 1  493 ? -5.584  -4.383  -20.65  1    14.203  ? 493  PRO   A N   1 1 
ATOM   4017  C  CA  . PRO   A 1  493 ? -6.728  -4.184  -21.53  1    14.344  ? 493  PRO   A CA  1 1 
ATOM   4018  C  C   . PRO   A 1  493 ? -7.428  -5.493  -21.905 1    16.154  ? 493  PRO   A C   1 1 
ATOM   4019  O  O   . PRO   A 1  493 ? -8.644  -5.486  -22.189 1    17.034  ? 493  PRO   A O   1 1 
ATOM   4020  C  CB  . PRO   A 1  493 ? -6.133  -3.413  -22.762 1    15.084  ? 493  PRO   A CB  1 1 
ATOM   4021  C  CG  . PRO   A 1  493 ? -4.605  -3.828  -22.717 1    13.775  ? 493  PRO   A CG  1 1 
ATOM   4022  C  CD  . PRO   A 1  493 ? -4.316  -3.868  -21.235 1    13.919  ? 493  PRO   A CD  1 1 
ATOM   4023  N  N   . ASN   A 1  494 ? -6.674  -6.6    -21.942 1    15.926  ? 494  ASN   A N   1 1 
ATOM   4024  C  CA  . ASN   A 1  494 ? -7.222  -7.881  -22.363 1    18.09   ? 494  ASN   A CA  1 1 
ATOM   4025  C  C   . ASN   A 1  494 ? -7.802  -8.63   -21.17  1    17.826  ? 494  ASN   A C   1 1 
ATOM   4026  O  O   . ASN   A 1  494 ? -8.265  -9.747  -21.309 1    19.151  ? 494  ASN   A O   1 1 
ATOM   4027  C  CB  . ASN   A 1  494 ? -6.239  -8.731  -23.171 1    19.723  ? 494  ASN   A CB  1 1 
ATOM   4028  C  CG  . ASN   A 1  494 ? -6.124  -8.121  -24.558 1    24.633  ? 494  ASN   A CG  1 1 
ATOM   4029  O  OD1 . ASN   A 1  494 ? -6.984  -8.329  -25.443 1    24.829  ? 494  ASN   A OD1 1 1 
ATOM   4030  N  ND2 . ASN   A 1  494 ? -5.113  -7.265  -24.734 1    21.678  ? 494  ASN   A ND2 1 1 
ATOM   4031  N  N   . VAL   A 1  495 ? -7.7    -8.036  -19.987 1    15.842  ? 495  VAL   A N   1 1 
ATOM   4032  C  CA  . VAL   A 1  495 ? -8.376  -8.601  -18.835 1    16.288  ? 495  VAL   A CA  1 1 
ATOM   4033  C  C   . VAL   A 1  495 ? -7.932  -10.044 -18.576 1    17.243  ? 495  VAL   A C   1 1 
ATOM   4034  O  O   . VAL   A 1  495 ? -8.758  -10.896 -18.301 1    18.656  ? 495  VAL   A O   1 1 
ATOM   4035  C  CB  . VAL   A 1  495 ? -9.906  -8.425  -18.853 1    17.522  ? 495  VAL   A CB  1 1 
ATOM   4036  C  CG1 . VAL   A 1  495 ? -10.353 -8.65   -17.415 1    21.076  ? 495  VAL   A CG1 1 1 
ATOM   4037  C  CG2 . VAL   A 1  495 ? -10.24  -6.983  -19.203 1    16.98   ? 495  VAL   A CG2 1 1 
ATOM   4038  N  N   . THR   A 1  496 ? -6.611  -10.313 -18.605 1    15.143  ? 496  THR   A N   1 1 
ATOM   4039  C  CA  . THR   A 1  496 ? -6.124  -11.656 -18.296 1    16.557  ? 496  THR   A CA  1 1 
ATOM   4040  C  C   . THR   A 1  496 ? -5.409  -11.552 -16.95  1    14.551  ? 496  THR   A C   1 1 
ATOM   4041  O  O   . THR   A 1  496 ? -4.509  -10.73  -16.862 1    15.629  ? 496  THR   A O   1 1 
ATOM   4042  C  CB  . THR   A 1  496 ? -5.066  -12.048 -19.339 1    17.466  ? 496  THR   A CB  1 1 
ATOM   4043  O  OG1 . THR   A 1  496 ? -5.748  -12.061 -20.588 1    22.681  ? 496  THR   A OG1 1 1 
ATOM   4044  C  CG2 . THR   A 1  496 ? -4.525  -13.452 -19.105 1    17.203  ? 496  THR   A CG2 1 1 
ATOM   4045  N  N   . PRO   A 1  497 ? -5.736  -12.331 -15.902 1    13.262  ? 497  PRO   A N   1 1 
ATOM   4046  C  CA  . PRO   A 1  497 ? -5.046  -12.189 -14.6   1    13.942  ? 497  PRO   A CA  1 1 
ATOM   4047  C  C   . PRO   A 1  497 ? -3.568  -12.58  -14.748 1    14.886  ? 497  PRO   A C   1 1 
ATOM   4048  O  O   . PRO   A 1  497 ? -3.216  -13.24  -15.75  1    15.976  ? 497  PRO   A O   1 1 
ATOM   4049  C  CB  . PRO   A 1  497 ? -5.772  -13.174 -13.656 1    13.194  ? 497  PRO   A CB  1 1 
ATOM   4050  C  CG  . PRO   A 1  497 ? -7.123  -13.318 -14.361 1    14.122  ? 497  PRO   A CG  1 1 
ATOM   4051  C  CD  . PRO   A 1  497 ? -6.871  -13.27  -15.878 1    15.037  ? 497  PRO   A CD  1 1 
ATOM   4052  N  N   . TYR   A 1  498 ? -2.743  -12.068 -13.823 1    13.38   ? 498  TYR   A N   1 1 
ATOM   4053  C  CA  . TYR   A 1  498 ? -1.28   -12.079 -13.937 1    13.176  ? 498  TYR   A CA  1 1 
ATOM   4054  C  C   . TYR   A 1  498 ? -0.632  -12.95  -12.875 1    13.516  ? 498  TYR   A C   1 1 
ATOM   4055  O  O   . TYR   A 1  498 ? 0.444   -13.552 -13.128 1    13.714  ? 498  TYR   A O   1 1 
ATOM   4056  C  CB  . TYR   A 1  498 ? -0.64   -10.686 -14.024 1    12.637  ? 498  TYR   A CB  1 1 
ATOM   4057  C  CG  . TYR   A 1  498 ? 0.554   -10.716 -14.96  1    12.247  ? 498  TYR   A CG  1 1 
ATOM   4058  C  CD1 . TYR   A 1  498 ? 0.363   -10.74  -16.342 1    12.507  ? 498  TYR   A CD1 1 1 
ATOM   4059  C  CD2 . TYR   A 1  498 ? 1.853   -10.735 -14.446 1    12.602  ? 498  TYR   A CD2 1 1 
ATOM   4060  C  CE1 . TYR   A 1  498 ? 1.435   -10.718 -17.232 1    13.368  ? 498  TYR   A CE1 1 1 
ATOM   4061  C  CE2 . TYR   A 1  498 ? 2.942   -10.717 -15.315 1    13.586  ? 498  TYR   A CE2 1 1 
ATOM   4062  C  CZ  . TYR   A 1  498 ? 2.728   -10.763 -16.699 1    14.81   ? 498  TYR   A CZ  1 1 
ATOM   4063  O  OH  . TYR   A 1  498 ? 3.783   -10.754 -17.551 1    15.487  ? 498  TYR   A OH  1 1 
ATOM   4064  N  N   . ILE   A 1  499 ? -1.279  -13.08  -11.696 1    13.836  ? 499  ILE   A N   1 1 
ATOM   4065  C  CA  . ILE   A 1  499 ? -0.583  -13.742 -10.595 1    14.005  ? 499  ILE   A CA  1 1 
ATOM   4066  C  C   . ILE   A 1  499 ? -0.198  -15.171 -11.008 1    13.633  ? 499  ILE   A C   1 1 
ATOM   4067  O  O   . ILE   A 1  499 ? 0.779   -15.725 -10.492 1    13.283  ? 499  ILE   A O   1 1 
ATOM   4068  C  CB  . ILE   A 1  499 ? -1.378  -13.672 -9.262  1    13.621  ? 499  ILE   A CB  1 1 
ATOM   4069  C  CG1 . ILE   A 1  499 ? -0.496  -14.002 -8.021  1    16.378  ? 499  ILE   A CG1 1 1 
ATOM   4070  C  CG2 . ILE   A 1  499 ? -2.609  -14.558 -9.283  1    13.251  ? 499  ILE   A CG2 1 1 
ATOM   4071  C  CD1 . ILE   A 1  499 ? 0.678   -13.029 -7.832  1    14.591  ? 499  ILE   A CD1 1 1 
ATOM   4072  N  N   . ARG   A 1  500 ? -0.974  -15.792 -11.904 1    13.325  ? 500  ARG   A N   1 1 
ATOM   4073  C  CA  . ARG   A 1  500 ? -0.644  -17.122 -12.388 1    12.709  ? 500  ARG   A CA  1 1 
ATOM   4074  C  C   . ARG   A 1  500 ? 0.811   -17.228 -12.888 1    11.37   ? 500  ARG   A C   1 1 
ATOM   4075  O  O   . ARG   A 1  500 ? 1.37    -18.333 -12.821 1    11.804  ? 500  ARG   A O   1 1 
ATOM   4076  C  CB  . ARG   A 1  500 ? -1.54   -17.503 -13.595 1    12.182  ? 500  ARG   A CB  1 1 
ATOM   4077  C  CG  . ARG   A 1  500 ? -1.525  -16.391 -14.663 1    13.659  ? 500  ARG   A CG  1 1 
ATOM   4078  C  CD  . ARG   A 1  500 ? -2.61   -16.515 -15.803 1    16.86   ? 500  ARG   A CD  1 1 
ATOM   4079  N  NE  . ARG   A 1  500 ? -3.928  -16.617 -15.163 1    16.323  ? 500  ARG   A NE  1 1 
ATOM   4080  C  CZ  . ARG   A 1  500 ? -5.135  -16.716 -15.842 1    19.463  ? 500  ARG   A CZ  1 1 
ATOM   4081  N  NH1 . ARG   A 1  500 ? -5.158  -16.821 -17.188 1    17.449  ? 500  ARG   A NH1 1 1 
ATOM   4082  N  NH2 . ARG   A 1  500 ? -6.25   -16.888 -15.151 1    16.086  ? 500  ARG   A NH2 1 1 
ATOM   4083  N  N   . TYR   A 1  501 ? 1.404   -16.166 -13.43  1    11.661  ? 501  TYR   A N   1 1 
ATOM   4084  C  CA  . TYR   A 1  501 ? 2.778   -16.291 -13.958 1    11.496  ? 501  TYR   A CA  1 1 
ATOM   4085  C  C   . TYR   A 1  501 ? 3.825   -16.277 -12.859 1    13.09   ? 501  TYR   A C   1 1 
ATOM   4086  O  O   . TYR   A 1  501 ? 4.784   -17.05  -12.91  1    12.809  ? 501  TYR   A O   1 1 
ATOM   4087  C  CB  . TYR   A 1  501 ? 3.134   -15.16  -14.907 1    12.103  ? 501  TYR   A CB  1 1 
ATOM   4088  C  CG  . TYR   A 1  501 ? 2.19    -15.144 -16.104 1    13.211  ? 501  TYR   A CG  1 1 
ATOM   4089  C  CD1 . TYR   A 1  501 ? 2.255   -16.156 -17.083 1    14.003  ? 501  TYR   A CD1 1 1 
ATOM   4090  C  CD2 . TYR   A 1  501 ? 1.196   -14.165 -16.243 1    14.425  ? 501  TYR   A CD2 1 1 
ATOM   4091  C  CE1 . TYR   A 1  501 ? 1.418   -16.146 -18.195 1    13.885  ? 501  TYR   A CE1 1 1 
ATOM   4092  C  CE2 . TYR   A 1  501 ? 0.304   -14.195 -17.32  1    13.881  ? 501  TYR   A CE2 1 1 
ATOM   4093  C  CZ  . TYR   A 1  501 ? 0.418   -15.179 -18.285 1    16.752  ? 501  TYR   A CZ  1 1 
ATOM   4094  O  OH  . TYR   A 1  501 ? -0.49   -15.149 -19.322 1    15.138  ? 501  TYR   A OH  1 1 
ATOM   4095  N  N   . PHE   A 1  502 ? 3.557   -15.518 -11.814 1    14.382  ? 502  PHE   A N   1 1 
ATOM   4096  C  CA  . PHE   A 1  502 ? 4.306   -15.602 -10.575 1    15.154  ? 502  PHE   A CA  1 1 
ATOM   4097  C  C   . PHE   A 1  502 ? 4.287   -17.025 -10.044 1    15.457  ? 502  PHE   A C   1 1 
ATOM   4098  O  O   . PHE   A 1  502 ? 5.352   -17.546 -9.728  1    14.174  ? 502  PHE   A O   1 1 
ATOM   4099  C  CB  . PHE   A 1  502 ? 4.01    -14.53  -9.527  1    14.94   ? 502  PHE   A CB  1 1 
ATOM   4100  C  CG  . PHE   A 1  502 ? 4.886   -14.613 -8.269  1    15.829  ? 502  PHE   A CG  1 1 
ATOM   4101  C  CD1 . PHE   A 1  502 ? 6.178   -14.089 -8.246  1    16.813  ? 502  PHE   A CD1 1 1 
ATOM   4102  C  CD2 . PHE   A 1  502 ? 4.418   -15.259 -7.139  1    16.347  ? 502  PHE   A CD2 1 1 
ATOM   4103  C  CE1 . PHE   A 1  502 ? 6.921   -14.147 -7.065  1    16.072  ? 502  PHE   A CE1 1 1 
ATOM   4104  C  CE2 . PHE   A 1  502 ? 5.169   -15.34  -5.948  1    17.529  ? 502  PHE   A CE2 1 1 
ATOM   4105  C  CZ  . PHE   A 1  502 ? 6.417   -14.773 -5.927  1    17.289  ? 502  PHE   A CZ  1 1 
ATOM   4106  N  N   . VAL   A 1  503 ? 3.096   -17.59  -9.898  1    14.498  ? 503  VAL   A N   1 1 
ATOM   4107  C  CA  . VAL   A 1  503 ? 2.915   -18.944 -9.398  1    14.711  ? 503  VAL   A CA  1 1 
ATOM   4108  C  C   . VAL   A 1  503 ? 3.681   -19.909 -10.326 1    15.548  ? 503  VAL   A C   1 1 
ATOM   4109  O  O   . VAL   A 1  503 ? 4.354   -20.84  -9.826  1    14.493  ? 503  VAL   A O   1 1 
ATOM   4110  C  CB  . VAL   A 1  503 ? 1.391   -19.304 -9.345  1    13.935  ? 503  VAL   A CB  1 1 
ATOM   4111  C  CG1 . VAL   A 1  503 ? 1.104   -20.787 -9.036  1    13.768  ? 503  VAL   A CG1 1 1 
ATOM   4112  C  CG2 . VAL   A 1  503 ? 0.707   -18.453 -8.258  1    13.428  ? 503  VAL   A CG2 1 1 
ATOM   4113  N  N   . SER   A 1  504 ? 3.503   -19.729 -11.641 1    12.648  ? 504  SER   A N   1 1 
ATOM   4114  C  CA  . SER   A 1  504 ? 4.108   -20.725 -12.502 1    14.534  ? 504  SER   A CA  1 1 
ATOM   4115  C  C   . SER   A 1  504 ? 5.645   -20.614 -12.491 1    14.112  ? 504  SER   A C   1 1 
ATOM   4116  O  O   . SER   A 1  504 ? 6.253   -21.657 -12.694 1    15.949  ? 504  SER   A O   1 1 
ATOM   4117  C  CB  . SER   A 1  504 ? 3.668   -20.693 -13.911 1    15.098  ? 504  SER   A CB  1 1 
ATOM   4118  O  OG  . SER   A 1  504 ? 3.999   -19.455 -14.445 1    23.046  ? 504  SER   A OG  1 1 
ATOM   4119  N  N   . PHE   A 1  505 ? 6.244   -19.43  -12.297 1    13.686  ? 505  PHE   A N   1 1 
ATOM   4120  C  CA  . PHE   A 1  505 ? 7.725   -19.305 -12.272 1    15.579  ? 505  PHE   A CA  1 1 
ATOM   4121  C  C   . PHE   A 1  505 ? 8.337   -20.05  -11.083 1    17.199  ? 505  PHE   A C   1 1 
ATOM   4122  O  O   . PHE   A 1  505 ? 9.489   -20.491 -11.14  1    18.594  ? 505  PHE   A O   1 1 
ATOM   4123  C  CB  . PHE   A 1  505 ? 8.181   -17.85  -12.446 1    15.598  ? 505  PHE   A CB  1 1 
ATOM   4124  C  CG  . PHE   A 1  505 ? 8.275   -17.404 -13.894 1    17.401  ? 505  PHE   A CG  1 1 
ATOM   4125  C  CD1 . PHE   A 1  505 ? 7.183   -17.523 -14.756 1    17.315  ? 505  PHE   A CD1 1 1 
ATOM   4126  C  CD2 . PHE   A 1  505 ? 9.483   -16.907 -14.395 1    18.628  ? 505  PHE   A CD2 1 1 
ATOM   4127  C  CE1 . PHE   A 1  505 ? 7.253   -17.052 -16.046 1    16.61   ? 505  PHE   A CE1 1 1 
ATOM   4128  C  CE2 . PHE   A 1  505 ? 9.55    -16.447 -15.712 1    19.496  ? 505  PHE   A CE2 1 1 
ATOM   4129  C  CZ  . PHE   A 1  505 ? 8.449   -16.569 -16.562 1    18.999  ? 505  PHE   A CZ  1 1 
ATOM   4130  N  N   . VAL   A 1  506 ? 7.568   -20.177 -10.007 1    15.899  ? 506  VAL   A N   1 1 
ATOM   4131  C  CA  . VAL   A 1  506 ? 7.973   -20.936 -8.847  1    16.62   ? 506  VAL   A CA  1 1 
ATOM   4132  C  C   . VAL   A 1  506 ? 7.678   -22.407 -9.093  1    16.612  ? 506  VAL   A C   1 1 
ATOM   4133  O  O   . VAL   A 1  506 ? 8.535   -23.29  -8.925  1    14.861  ? 506  VAL   A O   1 1 
ATOM   4134  C  CB  . VAL   A 1  506 ? 7.32    -20.39  -7.565  1    18.133  ? 506  VAL   A CB  1 1 
ATOM   4135  C  CG1 . VAL   A 1  506 ? 7.442   -21.324 -6.353  1    18.991  ? 506  VAL   A CG1 1 1 
ATOM   4136  C  CG2 . VAL   A 1  506 ? 7.79    -18.944 -7.309  1    16.306  ? 506  VAL   A CG2 1 1 
ATOM   4137  N  N   . LEU   A 1  507 ? 6.432   -22.657 -9.5    1    15.205  ? 507  LEU   A N   1 1 
ATOM   4138  C  CA  . LEU   A 1  507 ? 6.015   -24.038 -9.633  1    16.973  ? 507  LEU   A CA  1 1 
ATOM   4139  C  C   . LEU   A 1  507 ? 6.841   -24.762 -10.71  1    14.162  ? 507  LEU   A C   1 1 
ATOM   4140  O  O   . LEU   A 1  507 ? 7.053   -25.947 -10.588 1    13.701  ? 507  LEU   A O   1 1 
ATOM   4141  C  CB  . LEU   A 1  507 ? 4.568   -23.871 -10.082 1    17.793  ? 507  LEU   A CB  1 1 
ATOM   4142  C  CG  . LEU   A 1  507 ? 3.626   -25.058 -9.992  1    20.375  ? 507  LEU   A CG  1 1 
ATOM   4143  C  CD1 . LEU   A 1  507 ? 3.412   -25.559 -8.564  1    22.565  ? 507  LEU   A CD1 1 1 
ATOM   4144  C  CD2 . LEU   A 1  507 ? 2.25    -24.607 -10.562 1    22.661  ? 507  LEU   A CD2 1 1 
ATOM   4145  N  N   . GLN   A 1  508 ? 7.27    -24.082 -11.77  1    13.976  ? 508  GLN   A N   1 1 
ATOM   4146  C  CA  . GLN   A 1  508 ? 7.917   -24.882 -12.812 1    15.101  ? 508  GLN   A CA  1 1 
ATOM   4147  C  C   . GLN   A 1  508 ? 9.2     -25.549 -12.303 1    14.443  ? 508  GLN   A C   1 1 
ATOM   4148  O  O   . GLN   A 1  508 ? 9.572   -26.621 -12.785 1    14.566  ? 508  GLN   A O   1 1 
ATOM   4149  C  CB  . GLN   A 1  508 ? 8.241   -24.052 -14.054 1    14.436  ? 508  GLN   A CB  1 1 
ATOM   4150  C  CG  . GLN   A 1  508 ? 9.163   -22.847 -13.839 1    15.742  ? 508  GLN   A CG  1 1 
ATOM   4151  C  CD  . GLN   A 1  508 ? 9.142   -21.939 -15.062 1    18.466  ? 508  GLN   A CD  1 1 
ATOM   4152  O  OE1 . GLN   A 1  508 ? 10.138  -21.841 -15.784 1    19.906  ? 508  GLN   A OE1 1 1 
ATOM   4153  N  NE2 . GLN   A 1  508 ? 7.987   -21.297 -15.335 1    16.61   ? 508  GLN   A NE2 1 1 
ATOM   4154  N  N   . PHE   A 1  509 ? 9.859   -24.94  -11.292 1    13.929  ? 509  PHE   A N   1 1 
ATOM   4155  C  CA  . PHE   A 1  509 ? 11.068  -25.56  -10.756 1    13.718  ? 509  PHE   A CA  1 1 
ATOM   4156  C  C   . PHE   A 1  509 ? 10.687  -26.735 -9.865  1    15.191  ? 509  PHE   A C   1 1 
ATOM   4157  O  O   . PHE   A 1  509 ? 11.426  -27.719 -9.793  1    15.237  ? 509  PHE   A O   1 1 
ATOM   4158  C  CB  . PHE   A 1  509 ? 11.927  -24.556 -9.974  1    13.329  ? 509  PHE   A CB  1 1 
ATOM   4159  C  CG  . PHE   A 1  509 ? 12.491  -23.58  -10.977 1    13.504  ? 509  PHE   A CG  1 1 
ATOM   4160  C  CD1 . PHE   A 1  509 ? 13.672  -23.91  -11.663 1    14.219  ? 509  PHE   A CD1 1 1 
ATOM   4161  C  CD2 . PHE   A 1  509 ? 11.832  -22.366 -11.275 1    13.601  ? 509  PHE   A CD2 1 1 
ATOM   4162  C  CE1 . PHE   A 1  509 ? 14.204  -23.05  -12.636 1    15.133  ? 509  PHE   A CE1 1 1 
ATOM   4163  C  CE2 . PHE   A 1  509 ? 12.341  -21.522 -12.258 1    14.531  ? 509  PHE   A CE2 1 1 
ATOM   4164  C  CZ  . PHE   A 1  509 ? 13.588  -21.812 -12.887 1    14.763  ? 509  PHE   A CZ  1 1 
ATOM   4165  N  N   . GLN   A 1  510 ? 9.501   -26.683 -9.207  1    14.604  ? 510  GLN   A N   1 1 
ATOM   4166  C  CA  . GLN   A 1  510 ? 9.076   -27.863 -8.456  1    14.892  ? 510  GLN   A CA  1 1 
ATOM   4167  C  C   . GLN   A 1  510 ? 8.785   -29.005 -9.423  1    14.586  ? 510  GLN   A C   1 1 
ATOM   4168  O  O   . GLN   A 1  510 ? 9.175   -30.152 -9.164  1    14.846  ? 510  GLN   A O   1 1 
ATOM   4169  C  CB  . GLN   A 1  510 ? 7.799   -27.641 -7.612  1    16.419  ? 510  GLN   A CB  1 1 
ATOM   4170  C  CG  . GLN   A 1  510 ? 7.957   -26.461 -6.647  1    18.088  ? 510  GLN   A CG  1 1 
ATOM   4171  C  CD  . GLN   A 1  510 ? 6.73    -26.164 -5.804  1    19.024  ? 510  GLN   A CD  1 1 
ATOM   4172  O  OE1 . GLN   A 1  510 ? 6.201   -25.056 -5.893  1    21.612  ? 510  GLN   A OE1 1 1 
ATOM   4173  N  NE2 . GLN   A 1  510 ? 6.324   -27.107 -4.965  1    20.098  ? 510  GLN   A NE2 1 1 
ATOM   4174  N  N   . PHE   A 1  511 ? 8.121   -28.693 -10.536 1    14.623  ? 511  PHE   A N   1 1 
ATOM   4175  C  CA  . PHE   A 1  511 ? 7.82    -29.76  -11.487 1    15.761  ? 511  PHE   A CA  1 1 
ATOM   4176  C  C   . PHE   A 1  511 ? 9.135   -30.331 -12.069 1    16.028  ? 511  PHE   A C   1 1 
ATOM   4177  O  O   . PHE   A 1  511 ? 9.286   -31.543 -12.255 1    17.699  ? 511  PHE   A O   1 1 
ATOM   4178  C  CB  . PHE   A 1  511 ? 7.047   -29.083 -12.635 1    16.696  ? 511  PHE   A CB  1 1 
ATOM   4179  C  CG  . PHE   A 1  511 ? 5.574   -28.814 -12.367 1    19.625  ? 511  PHE   A CG  1 1 
ATOM   4180  C  CD1 . PHE   A 1  511 ? 5.025   -29.088 -11.121 1    19.681  ? 511  PHE   A CD1 1 1 
ATOM   4181  C  CD2 . PHE   A 1  511 ? 4.76    -28.238 -13.362 1    21.768  ? 511  PHE   A CD2 1 1 
ATOM   4182  C  CE1 . PHE   A 1  511 ? 3.685   -28.763 -10.867 1    22.009  ? 511  PHE   A CE1 1 1 
ATOM   4183  C  CE2 . PHE   A 1  511 ? 3.421   -27.986 -13.117 1    20.877  ? 511  PHE   A CE2 1 1 
ATOM   4184  C  CZ  . PHE   A 1  511 ? 2.896   -28.266 -11.865 1    21.176  ? 511  PHE   A CZ  1 1 
ATOM   4185  N  N   . HIS   A 1  512 ? 10.036  -29.432 -12.445 1    16.3    ? 512  HIS   A N   1 1 
ATOM   4186  C  CA  . HIS   A 1  512 ? 11.312  -29.822 -13.063 1    17.041  ? 512  HIS   A CA  1 1 
ATOM   4187  C  C   . HIS   A 1  512 ? 12.023  -30.793 -12.139 1    17.378  ? 512  HIS   A C   1 1 
ATOM   4188  O  O   . HIS   A 1  512 ? 12.494  -31.851 -12.578 1    17.338  ? 512  HIS   A O   1 1 
ATOM   4189  C  CB  . HIS   A 1  512 ? 12.125  -28.559 -13.415 1    17.084  ? 512  HIS   A CB  1 1 
ATOM   4190  C  CG  . HIS   A 1  512 ? 13.395  -28.8   -14.14  1    17.894  ? 512  HIS   A CG  1 1 
ATOM   4191  N  ND1 . HIS   A 1  512 ? 13.442  -29.355 -15.393 1    19.534  ? 512  HIS   A ND1 1 1 
ATOM   4192  C  CD2 . HIS   A 1  512 ? 14.641  -28.575 -13.75  1    18.87   ? 512  HIS   A CD2 1 1 
ATOM   4193  C  CE1 . HIS   A 1  512 ? 14.734  -29.432 -15.769 1    21.309  ? 512  HIS   A CE1 1 1 
ATOM   4194  N  NE2 . HIS   A 1  512 ? 15.482  -28.977 -14.763 1    21.158  ? 512  HIS   A NE2 1 1 
ATOM   4195  N  N   . GLU   A 1  513 ? 12.149  -30.392 -10.863 1    17.453  ? 513  GLU   A N   1 1 
ATOM   4196  C  CA  . GLU   A 1  513 ? 12.825  -31.239 -9.919  1    18.476  ? 513  GLU   A CA  1 1 
ATOM   4197  C  C   . GLU   A 1  513 ? 12.192  -32.632 -9.875  1    19.111  ? 513  GLU   A C   1 1 
ATOM   4198  O  O   . GLU   A 1  513 ? 12.898  -33.664 -9.835  1    18.469  ? 513  GLU   A O   1 1 
ATOM   4199  C  CB  . GLU   A 1  513 ? 12.989  -30.566 -8.551  1    21.84   ? 513  GLU   A CB  1 1 
ATOM   4200  C  CG  . GLU   A 1  513 ? 13.565  -31.544 -7.524  1    25.284  ? 513  GLU   A CG  1 1 
ATOM   4201  C  CD  . GLU   A 1  513 ? 13.584  -30.872 -6.166  1    31.669  ? 513  GLU   A CD  1 1 
ATOM   4202  O  OE1 . GLU   A 1  513 ? 12.489  -30.562 -5.63   1    29.078  ? 513  GLU   A OE1 1 1 
ATOM   4203  O  OE2 . GLU   A 1  513 ? 14.699  -30.622 -5.658  1    35.681  ? 513  GLU   A OE2 1 1 
ATOM   4204  N  N   . ALA   A 1  514 ? 10.853  -32.684 -9.813  1    17.84   ? 514  ALA   A N   1 1 
ATOM   4205  C  CA  . ALA   A 1  514 ? 10.184  -33.972 -9.745  1    18.339  ? 514  ALA   A CA  1 1 
ATOM   4206  C  C   . ALA   A 1  514 ? 10.346  -34.794 -11.033 1    17.702  ? 514  ALA   A C   1 1 
ATOM   4207  O  O   . ALA   A 1  514 ? 10.414  -36.015 -10.936 1    18.273  ? 514  ALA   A O   1 1 
ATOM   4208  C  CB  . ALA   A 1  514 ? 8.671   -33.745 -9.439  1    18.628  ? 514  ALA   A CB  1 1 
ATOM   4209  N  N   . LEU   A 1  515 ? 10.255  -34.163 -12.219 1    17.44   ? 515  LEU   A N   1 1 
ATOM   4210  C  CA  . LEU   A 1  515 ? 10.34   -34.942 -13.454 1    17.612  ? 515  LEU   A CA  1 1 
ATOM   4211  C  C   . LEU   A 1  515 ? 11.772  -35.443 -13.693 1    17.879  ? 515  LEU   A C   1 1 
ATOM   4212  O  O   . LEU   A 1  515 ? 11.946  -36.583 -14.095 1    18.328  ? 515  LEU   A O   1 1 
ATOM   4213  C  CB  . LEU   A 1  515 ? 9.917   -34.008 -14.57  1    17.429  ? 515  LEU   A CB  1 1 
ATOM   4214  C  CG  . LEU   A 1  515 ? 8.439   -33.607 -14.54  1    17.694  ? 515  LEU   A CG  1 1 
ATOM   4215  C  CD1 . LEU   A 1  515 ? 8.22    -32.681 -15.763 1    17.618  ? 515  LEU   A CD1 1 1 
ATOM   4216  C  CD2 . LEU   A 1  515 ? 7.515   -34.806 -14.529 1    18.61   ? 515  LEU   A CD2 1 1 
ATOM   4217  N  N   . CYS   A 1  516 ? 12.75   -34.631 -13.336 1    18.417  ? 516  CYS   A N   1 1 
ATOM   4218  C  CA  . CYS   A 1  516 ? 14.169  -35.041 -13.344 1    21.323  ? 516  CYS   A CA  1 1 
ATOM   4219  C  C   . CYS   A 1  516 ? 14.393  -36.258 -12.461 1    23.88   ? 516  CYS   A C   1 1 
ATOM   4220  O  O   . CYS   A 1  516 ? 15.132  -37.203 -12.855 1    25.884  ? 516  CYS   A O   1 1 
ATOM   4221  C  CB  . CYS   A 1  516 ? 15.073  -33.868 -12.988 1    22.711  ? 516  CYS   A CB  1 1 
ATOM   4222  S  SG  . CYS   A 1  516 ? 14.969  -32.643 -14.338 1    27.064  ? 516  CYS   A SG  1 1 
ATOM   4223  N  N   . LYS   A 1  517 ? 13.768  -36.232 -11.269 1    23.961  ? 517  LYS   A N   1 1 
ATOM   4224  C  CA  . LYS   A 1  517 ? 13.966  -37.369 -10.383 1    26.32   ? 517  LYS   A CA  1 1 
ATOM   4225  C  C   . LYS   A 1  517 ? 13.302  -38.607 -10.999 1    25.711  ? 517  LYS   A C   1 1 
ATOM   4226  O  O   . LYS   A 1  517 ? 13.865  -39.696 -11.001 1    22.966  ? 517  LYS   A O   1 1 
ATOM   4227  C  CB  . LYS   A 1  517 ? 13.389  -37.174 -8.98   1    29.316  ? 517  LYS   A CB  1 1 
ATOM   4228  C  CG  . LYS   A 1  517 ? 13.371  -38.463 -8.139  1    34.752  ? 517  LYS   A CG  1 1 
ATOM   4229  C  CD  . LYS   A 1  517 ? 12.738  -38.01  -6.83   1    44.029  ? 517  LYS   A CD  1 1 
ATOM   4230  C  CE  . LYS   A 1  517 ? 12.466  -39.149 -5.902  1    55.318  ? 517  LYS   A CE  1 1 
ATOM   4231  N  NZ  . LYS   A 1  517 ? 12.254  -38.671 -4.528  1    58.71   ? 517  LYS   A NZ  1 1 
ATOM   4232  N  N   . GLU   A 1  518 ? 12.097  -38.425 -11.553 1    23.979  ? 518  GLU   A N   1 1 
ATOM   4233  C  CA  . GLU   A 1  518 ? 11.362  -39.555 -12.088 1    26.225  ? 518  GLU   A CA  1 1 
ATOM   4234  C  C   . GLU   A 1  518 ? 12.118  -40.096 -13.299 1    27.587  ? 518  GLU   A C   1 1 
ATOM   4235  O  O   . GLU   A 1  518 ? 12.111  -41.299 -13.524 1    29.921  ? 518  GLU   A O   1 1 
ATOM   4236  C  CB  . GLU   A 1  518 ? 9.947   -39.065 -12.437 1    26.707  ? 518  GLU   A CB  1 1 
ATOM   4237  C  CG  . GLU   A 1  518 ? 9.054   -40.186 -12.968 1    33.225  ? 518  GLU   A CG  1 1 
ATOM   4238  C  CD  . GLU   A 1  518 ? 8.604   -41.223 -11.928 1    38.716  ? 518  GLU   A CD  1 1 
ATOM   4239  O  OE1 . GLU   A 1  518 ? 7.865   -42.187 -12.298 1    40.293  ? 518  GLU   A OE1 1 1 
ATOM   4240  O  OE2 . GLU   A 1  518 ? 9.02    -41.094 -10.747 1    38.534  ? 518  GLU   A OE2 1 1 
ATOM   4241  N  N   . ALA   A 1  519 ? 12.8    -39.213 -14.038 1    25.92   ? 519  ALA   A N   1 1 
ATOM   4242  C  CA  . ALA   A 1  519 ? 13.555  -39.581 -15.221 1    27.252  ? 519  ALA   A CA  1 1 
ATOM   4243  C  C   . ALA   A 1  519 ? 14.768  -40.429 -14.842 1    28.915  ? 519  ALA   A C   1 1 
ATOM   4244  O  O   . ALA   A 1  519 ? 15.415  -40.99  -15.716 1    31.042  ? 519  ALA   A O   1 1 
ATOM   4245  C  CB  . ALA   A 1  519 ? 13.991  -38.33  -15.93  1    24.614  ? 519  ALA   A CB  1 1 
ATOM   4246  N  N   . GLY   A 1  520 ? 15.073  -40.547 -13.547 1    27.04   ? 520  GLY   A N   1 1 
ATOM   4247  C  CA  . GLY   A 1  520 ? 16.271  -41.272 -13.135 1    28.007  ? 520  GLY   A CA  1 1 
ATOM   4248  C  C   . GLY   A 1  520 ? 17.54   -40.427 -13.242 1    28.548  ? 520  GLY   A C   1 1 
ATOM   4249  O  O   . GLY   A 1  520 ? 18.647  -40.925 -13.04  1    30.731  ? 520  GLY   A O   1 1 
ATOM   4250  N  N   . TYR   A 1  521 ? 17.398  -39.124 -13.464 1    27.083  ? 521  TYR   A N   1 1 
ATOM   4251  C  CA  . TYR   A 1  521 ? 18.54   -38.249 -13.62  1    30.336  ? 521  TYR   A CA  1 1 
ATOM   4252  C  C   . TYR   A 1  521 ? 19.228  -37.944 -12.273 1    33.497  ? 521  TYR   A C   1 1 
ATOM   4253  O  O   . TYR   A 1  521 ? 18.581  -37.66  -11.256 1    31.931  ? 521  TYR   A O   1 1 
ATOM   4254  C  CB  . TYR   A 1  521 ? 18.095  -37.005 -14.397 1    29.939  ? 521  TYR   A CB  1 1 
ATOM   4255  C  CG  . TYR   A 1  521 ? 19.199  -35.967 -14.422 1    30.381  ? 521  TYR   A CG  1 1 
ATOM   4256  C  CD1 . TYR   A 1  521 ? 20.248  -36.068 -15.328 1    31.646  ? 521  TYR   A CD1 1 1 
ATOM   4257  C  CD2 . TYR   A 1  521 ? 19.206  -34.918 -13.51  1    29.282  ? 521  TYR   A CD2 1 1 
ATOM   4258  C  CE1 . TYR   A 1  521 ? 21.281  -35.14  -15.351 1    33.602  ? 521  TYR   A CE1 1 1 
ATOM   4259  C  CE2 . TYR   A 1  521 ? 20.222  -33.981 -13.526 1    30.465  ? 521  TYR   A CE2 1 1 
ATOM   4260  C  CZ  . TYR   A 1  521 ? 21.224  -34.068 -14.476 1    30.464  ? 521  TYR   A CZ  1 1 
ATOM   4261  O  OH  . TYR   A 1  521 ? 22.217  -33.146 -14.457 1    35.217  ? 521  TYR   A OH  1 1 
ATOM   4262  N  N   . GLU   A 1  522 ? 20.573  -37.957 -12.276 1    35.425  ? 522  GLU   A N   1 1 
ATOM   4263  C  CA  . GLU   A 1  522 ? 21.307  -37.931 -11.017 1    38.412  ? 522  GLU   A CA  1 1 
ATOM   4264  C  C   . GLU   A 1  522 ? 22.397  -36.853 -10.937 1    37.324  ? 522  GLU   A C   1 1 
ATOM   4265  O  O   . GLU   A 1  522 ? 23.256  -36.933 -10.074 1    46.368  ? 522  GLU   A O   1 1 
ATOM   4266  C  CB  . GLU   A 1  522 ? 21.863  -39.329 -10.726 1    41.786  ? 522  GLU   A CB  1 1 
ATOM   4267  C  CG  . GLU   A 1  522 ? 20.764  -40.341 -10.401 1    49.163  ? 522  GLU   A CG  1 1 
ATOM   4268  C  CD  . GLU   A 1  522 ? 21.184  -41.688 -9.826  1    59.852  ? 522  GLU   A CD  1 1 
ATOM   4269  O  OE1 . GLU   A 1  522 ? 20.696  -42.001 -8.714  1    61.341  ? 522  GLU   A OE1 1 1 
ATOM   4270  O  OE2 . GLU   A 1  522 ? 21.989  -42.422 -10.453 1    59.355  ? 522  GLU   A OE2 1 1 
ATOM   4271  N  N   . GLY   A 1  523 ? 22.391  -35.825 -11.79  1    36.862  ? 523  GLY   A N   1 1 
ATOM   4272  C  CA  . GLY   A 1  523 ? 23.384  -34.773 -11.623 1    32.807  ? 523  GLY   A CA  1 1 
ATOM   4273  C  C   . GLY   A 1  523 ? 22.753  -33.463 -11.17  1    29.438  ? 523  GLY   A C   1 1 
ATOM   4274  O  O   . GLY   A 1  523 ? 21.619  -33.456 -10.667 1    27.948  ? 523  GLY   A O   1 1 
ATOM   4275  N  N   . PRO   A 1  524 ? 23.446  -32.329 -11.408 1    26.075  ? 524  PRO   A N   1 1 
ATOM   4276  C  CA  . PRO   A 1  524 ? 22.98   -31.01  -10.979 1    24.947  ? 524  PRO   A CA  1 1 
ATOM   4277  C  C   . PRO   A 1  524 ? 21.6    -30.745 -11.609 1    24.835  ? 524  PRO   A C   1 1 
ATOM   4278  O  O   . PRO   A 1  524 ? 21.354  -31.076 -12.774 1    23.488  ? 524  PRO   A O   1 1 
ATOM   4279  C  CB  . PRO   A 1  524 ? 24.06   -30.068 -11.571 1    24.567  ? 524  PRO   A CB  1 1 
ATOM   4280  C  CG  . PRO   A 1  524 ? 25.29   -30.96  -11.717 1    25.453  ? 524  PRO   A CG  1 1 
ATOM   4281  C  CD  . PRO   A 1  524 ? 24.704  -32.27  -12.176 1    26.481  ? 524  PRO   A CD  1 1 
ATOM   4282  N  N   . LEU   A 1  525 ? 20.719  -30.118 -10.845 1    21.816  ? 525  LEU   A N   1 1 
ATOM   4283  C  CA  . LEU   A 1  525 ? 19.337  -29.958 -11.322 1    23.301  ? 525  LEU   A CA  1 1 
ATOM   4284  C  C   . LEU   A 1  525 ? 19.284  -29.112 -12.598 1    21.098  ? 525  LEU   A C   1 1 
ATOM   4285  O  O   . LEU   A 1  525 ? 18.496  -29.392 -13.506 1    21.267  ? 525  LEU   A O   1 1 
ATOM   4286  C  CB  . LEU   A 1  525 ? 18.498  -29.36  -10.181 1    23.511  ? 525  LEU   A CB  1 1 
ATOM   4287  C  CG  . LEU   A 1  525 ? 17.058  -28.94  -10.52  1    27.585  ? 525  LEU   A CG  1 1 
ATOM   4288  C  CD1 . LEU   A 1  525 ? 16.335  -30.173 -11.11  1    27.014  ? 525  LEU   A CD1 1 1 
ATOM   4289  C  CD2 . LEU   A 1  525 ? 16.363  -28.315 -9.272  1    26.095  ? 525  LEU   A CD2 1 1 
ATOM   4290  N  N   . HIS   A 1  526 ? 20.184  -28.143 -12.737 1    20.582  ? 526  HIS   A N   1 1 
ATOM   4291  C  CA  . HIS   A 1  526 ? 20.166  -27.253 -13.888 1    20.139  ? 526  HIS   A CA  1 1 
ATOM   4292  C  C   . HIS   A 1  526 ? 20.742  -27.895 -15.159 1    20.35   ? 526  HIS   A C   1 1 
ATOM   4293  O  O   . HIS   A 1  526 ? 20.8    -27.214 -16.174 1    21.485  ? 526  HIS   A O   1 1 
ATOM   4294  C  CB  . HIS   A 1  526 ? 20.871  -25.941 -13.567 1    20.142  ? 526  HIS   A CB  1 1 
ATOM   4295  C  CG  . HIS   A 1  526 ? 22.346  -26.114 -13.292 1    23.89   ? 526  HIS   A CG  1 1 
ATOM   4296  N  ND1 . HIS   A 1  526 ? 22.827  -26.506 -12.058 1    26.712  ? 526  HIS   A ND1 1 1 
ATOM   4297  C  CD2 . HIS   A 1  526 ? 23.392  -25.971 -14.078 1    23.233  ? 526  HIS   A CD2 1 1 
ATOM   4298  C  CE1 . HIS   A 1  526 ? 24.167  -26.612 -12.108 1    26.752  ? 526  HIS   A CE1 1 1 
ATOM   4299  N  NE2 . HIS   A 1  526 ? 24.514  -26.25  -13.32  1    26.354  ? 526  HIS   A NE2 1 1 
ATOM   4300  N  N   . GLN   A 1  527 ? 21.263  -29.136 -15.105 1    19.866  ? 527  GLN   A N   1 1 
ATOM   4301  C  CA  . GLN   A 1  527 ? 21.785  -29.77  -16.299 1    21.136  ? 527  GLN   A CA  1 1 
ATOM   4302  C  C   . GLN   A 1  527 ? 20.847  -30.897 -16.7   1    22.559  ? 527  GLN   A C   1 1 
ATOM   4303  O  O   . GLN   A 1  527 ? 21.142  -31.681 -17.572 1    24.333  ? 527  GLN   A O   1 1 
ATOM   4304  C  CB  . GLN   A 1  527 ? 23.225  -30.287 -16.105 1    22.58   ? 527  GLN   A CB  1 1 
ATOM   4305  C  CG  . GLN   A 1  527 ? 24.172  -29.131 -15.851 1    25.368  ? 527  GLN   A CG  1 1 
ATOM   4306  C  CD  . GLN   A 1  527 ? 25.623  -29.543 -15.663 1    32.245  ? 527  GLN   A CD  1 1 
ATOM   4307  O  OE1 . GLN   A 1  527 ? 25.92   -30.604 -15.114 1    31.857  ? 527  GLN   A OE1 1 1 
ATOM   4308  N  NE2 . GLN   A 1  527 ? 26.544  -28.704 -16.116 1    32.368  ? 527  GLN   A NE2 1 1 
ATOM   4309  N  N   . CYS   A 1  528 ? 19.69   -30.999 -16.065 1    21.737  ? 528  CYS   A N   1 1 
ATOM   4310  C  CA  . CYS   A 1  528 ? 18.843  -32.136 -16.367 1    22.696  ? 528  CYS   A CA  1 1 
ATOM   4311  C  C   . CYS   A 1  528 ? 18.091  -31.852 -17.689 1    21.864  ? 528  CYS   A C   1 1 
ATOM   4312  O  O   . CYS   A 1  528 ? 17.593  -30.744 -17.901 1    20.529  ? 528  CYS   A O   1 1 
ATOM   4313  C  CB  . CYS   A 1  528 ? 17.838  -32.284 -15.227 1    24.946  ? 528  CYS   A CB  1 1 
ATOM   4314  S  SG  . CYS   A 1  528 ? 16.43   -33.32  -15.687 1    30.083  ? 528  CYS   A SG  1 1 
ATOM   4315  N  N   . ASP   A 1  529 ? 17.999  -32.874 -18.547 1    21.039  ? 529  ASP   A N   1 1 
ATOM   4316  C  CA  . ASP   A 1  529 ? 17.179  -32.812 -19.758 1    20.692  ? 529  ASP   A CA  1 1 
ATOM   4317  C  C   . ASP   A 1  529 ? 16.265  -34.04  -19.734 1    18.996  ? 529  ASP   A C   1 1 
ATOM   4318  O  O   . ASP   A 1  529 ? 16.786  -35.161 -19.764 1    18.188  ? 529  ASP   A O   1 1 
ATOM   4319  C  CB  . ASP   A 1  529 ? 18.114  -32.714 -20.976 1    20.921  ? 529  ASP   A CB  1 1 
ATOM   4320  C  CG  . ASP   A 1  529 ? 17.421  -32.849 -22.326 1    20.88   ? 529  ASP   A CG  1 1 
ATOM   4321  O  OD1 . ASP   A 1  529 ? 16.182  -32.662 -22.341 1    20.795  ? 529  ASP   A OD1 1 1 
ATOM   4322  O  OD2 . ASP   A 1  529 ? 18.092  -33.181 -23.355 1    22.863  ? 529  ASP   A OD2 1 1 
ATOM   4323  N  N   . ILE   A 1  530 ? 14.919  -33.826 -19.667 1    17.837  ? 530  ILE   A N   1 1 
ATOM   4324  C  CA  . ILE   A 1  530 ? 13.998  -34.945 -19.586 1    18.664  ? 530  ILE   A CA  1 1 
ATOM   4325  C  C   . ILE   A 1  530 ? 13.65   -35.499 -20.972 1    19.005  ? 530  ILE   A C   1 1 
ATOM   4326  O  O   . ILE   A 1  530 ? 12.785  -36.389 -21.062 1    18.887  ? 530  ILE   A O   1 1 
ATOM   4327  C  CB  . ILE   A 1  530 ? 12.718  -34.579 -18.791 1    19.441  ? 530  ILE   A CB  1 1 
ATOM   4328  C  CG1 . ILE   A 1  530 ? 11.853  -33.513 -19.458 1    19.475  ? 530  ILE   A CG1 1 1 
ATOM   4329  C  CG2 . ILE   A 1  530 ? 13.119  -34.151 -17.354 1    19.497  ? 530  ILE   A CG2 1 1 
ATOM   4330  C  CD1 . ILE   A 1  530 ? 10.496  -33.34  -18.764 1    23.293  ? 530  ILE   A CD1 1 1 
ATOM   4331  N  N   . TYR   A 1  531 ? 14.229  -34.895 -22.035 1    18.353  ? 531  TYR   A N   1 1 
ATOM   4332  C  CA  . TYR   A 1  531 ? 14.023  -35.394 -23.406 1    18.884  ? 531  TYR   A CA  1 1 
ATOM   4333  C  C   . TYR   A 1  531 ? 14.026  -36.923 -23.471 1    19.146  ? 531  TYR   A C   1 1 
ATOM   4334  O  O   . TYR   A 1  531 ? 14.953  -37.578 -23.006 1    19.044  ? 531  TYR   A O   1 1 
ATOM   4335  C  CB  . TYR   A 1  531 ? 15.144  -34.912 -24.337 1    19.507  ? 531  TYR   A CB  1 1 
ATOM   4336  C  CG  . TYR   A 1  531 ? 14.925  -35.159 -25.834 1    21.338  ? 531  TYR   A CG  1 1 
ATOM   4337  C  CD1 . TYR   A 1  531 ? 13.74   -34.749 -26.468 1    21.779  ? 531  TYR   A CD1 1 1 
ATOM   4338  C  CD2 . TYR   A 1  531 ? 15.936  -35.741 -26.609 1    23.23   ? 531  TYR   A CD2 1 1 
ATOM   4339  C  CE1 . TYR   A 1  531 ? 13.6    -34.895 -27.843 1    23.14   ? 531  TYR   A CE1 1 1 
ATOM   4340  C  CE2 . TYR   A 1  531 ? 15.775  -35.954 -27.975 1    25.06   ? 531  TYR   A CE2 1 1 
ATOM   4341  C  CZ  . TYR   A 1  531 ? 14.625  -35.472 -28.582 1    24.743  ? 531  TYR   A CZ  1 1 
ATOM   4342  O  OH  . TYR   A 1  531 ? 14.443  -35.633 -29.917 1    26.271  ? 531  TYR   A OH  1 1 
ATOM   4343  N  N   . ARG   A 1  532 ? 13.025  -37.508 -24.133 1    19.471  ? 532  ARG   A N   1 1 
ATOM   4344  C  CA  . ARG   A 1  532 ? 12.934  -38.95  -24.372 1    21.536  ? 532  ARG   A CA  1 1 
ATOM   4345  C  C   . ARG   A 1  532 ? 12.649  -39.777 -23.09  1    22.869  ? 532  ARG   A C   1 1 
ATOM   4346  O  O   . ARG   A 1  532 ? 12.668  -41.013 -23.131 1    24.03   ? 532  ARG   A O   1 1 
ATOM   4347  C  CB  . ARG   A 1  532 ? 14.14   -39.528 -25.127 1    23.777  ? 532  ARG   A CB  1 1 
ATOM   4348  C  CG  . ARG   A 1  532 ? 14.173  -39.264 -26.623 1    24.525  ? 532  ARG   A CG  1 1 
ATOM   4349  C  CD  . ARG   A 1  532 ? 15.535  -39.565 -27.26  1    28.671  ? 532  ARG   A CD  1 1 
ATOM   4350  N  NE  . ARG   A 1  532 ? 15.319  -39.328 -28.707 1    29.989  ? 532  ARG   A NE  1 1 
ATOM   4351  C  CZ  . ARG   A 1  532 ? 16.298  -39.225 -29.575 1    31.665  ? 532  ARG   A CZ  1 1 
ATOM   4352  N  NH1 . ARG   A 1  532 ? 17.538  -39.481 -29.194 1    30.145  ? 532  ARG   A NH1 1 1 
ATOM   4353  N  NH2 . ARG   A 1  532 ? 16.003  -38.919 -30.831 1    32.982  ? 532  ARG   A NH2 1 1 
ATOM   4354  N  N   . SER   A 1  533 ? 12.375  -39.127 -21.947 1    22.294  ? 533  SER   A N   1 1 
ATOM   4355  C  CA  . SER   A 1  533 ? 11.966  -39.862 -20.741 1    22.273  ? 533  SER   A CA  1 1 
ATOM   4356  C  C   . SER   A 1  533 ? 10.476  -40.172 -20.754 1    22.451  ? 533  SER   A C   1 1 
ATOM   4357  O  O   . SER   A 1  533 ? 9.653   -39.277 -20.48  1    20.155  ? 533  SER   A O   1 1 
ATOM   4358  C  CB  . SER   A 1  533 ? 12.304  -39.106 -19.469 1    22.255  ? 533  SER   A CB  1 1 
ATOM   4359  O  OG  . SER   A 1  533 ? 11.921  -39.902 -18.357 1    22.017  ? 533  SER   A OG  1 1 
ATOM   4360  N  N   . THR   A 1  534 ? 10.138  -41.429 -21.078 1    24.904  ? 534  THR   A N   1 1 
ATOM   4361  C  CA  . THR   A 1  534 ? 8.723   -41.799 -21.073 1    27.113  ? 534  THR   A CA  1 1 
ATOM   4362  C  C   . THR   A 1  534 ? 8.182   -41.897 -19.627 1    26.771  ? 534  THR   A C   1 1 
ATOM   4363  O  O   . THR   A 1  534 ? 7.007   -41.612 -19.4   1    25.795  ? 534  THR   A O   1 1 
ATOM   4364  C  CB  . THR   A 1  534 ? 8.464   -43.015 -21.978 1    31.323  ? 534  THR   A CB  1 1 
ATOM   4365  O  OG1 . THR   A 1  534 ? 9.132   -44.131 -21.41  1    32.248  ? 534  THR   A OG1 1 1 
ATOM   4366  C  CG2 . THR   A 1  534 ? 8.913   -42.772 -23.414 1    30.037  ? 534  THR   A CG2 1 1 
ATOM   4367  N  N   . LYS   A 1  535 ? 9.047   -42.176 -18.637 1    26.649  ? 535  LYS   A N   1 1 
ATOM   4368  C  CA  . LYS   A 1  535 ? 8.638   -42.124 -17.235 1    28.387  ? 535  LYS   A CA  1 1 
ATOM   4369  C  C   . LYS   A 1  535 ? 8.225   -40.703 -16.834 1    26.711  ? 535  LYS   A C   1 1 
ATOM   4370  O  O   . LYS   A 1  535 ? 7.17    -40.516 -16.187 1    23.951  ? 535  LYS   A O   1 1 
ATOM   4371  C  CB  . LYS   A 1  535 ? 9.807   -42.437 -16.295 1    32.701  ? 535  LYS   A CB  1 1 
ATOM   4372  C  CG  . LYS   A 1  535 ? 10.295  -43.88  -16.4   1    43.366  ? 535  LYS   A CG  1 1 
ATOM   4373  C  CD  . LYS   A 1  535 ? 9.381   -44.912 -15.741 1    51.476  ? 535  LYS   A CD  1 1 
ATOM   4374  C  CE  . LYS   A 1  535 ? 9.249   -44.89  -14.233 1    56.871  ? 535  LYS   A CE  1 1 
ATOM   4375  N  NZ  . LYS   A 1  535 ? 10.529  -45.089 -13.543 1    62.605  ? 535  LYS   A NZ  1 1 
ATOM   4376  N  N   . ALA   A 1  536 ? 9.088   -39.704 -17.159 1    24.023  ? 536  ALA   A N   1 1 
ATOM   4377  C  CA  . ALA   A 1  536 ? 8.752   -38.305 -16.871 1    22.53   ? 536  ALA   A CA  1 1 
ATOM   4378  C  C   . ALA   A 1  536 ? 7.444   -37.94  -17.553 1    22.129  ? 536  ALA   A C   1 1 
ATOM   4379  O  O   . ALA   A 1  536 ? 6.588   -37.203 -16.995 1    21.046  ? 536  ALA   A O   1 1 
ATOM   4380  C  CB  . ALA   A 1  536 ? 9.87    -37.393 -17.318 1    21.898  ? 536  ALA   A CB  1 1 
ATOM   4381  N  N   . GLY   A 1  537 ? 7.272   -38.461 -18.793 1    21.149  ? 537  GLY   A N   1 1 
ATOM   4382  C  CA  . GLY   A 1  537 ? 6.068   -38.121 -19.528 1    21.182  ? 537  GLY   A CA  1 1 
ATOM   4383  C  C   . GLY   A 1  537 ? 4.782   -38.618 -18.861 1    21.366  ? 537  GLY   A C   1 1 
ATOM   4384  O  O   . GLY   A 1  537 ? 3.81    -37.871 -18.802 1    22.304  ? 537  GLY   A O   1 1 
ATOM   4385  N  N   . ALA   A 1  538 ? 4.792   -39.838 -18.348 1    23.027  ? 538  ALA   A N   1 1 
ATOM   4386  C  CA  . ALA   A 1  538 ? 3.67    -40.468 -17.651 1    24.082  ? 538  ALA   A CA  1 1 
ATOM   4387  C  C   . ALA   A 1  538 ? 3.313   -39.665 -16.395 1    23.685  ? 538  ALA   A C   1 1 
ATOM   4388  O  O   . ALA   A 1  538 ? 2.128   -39.468 -16.087 1    25.114  ? 538  ALA   A O   1 1 
ATOM   4389  C  CB  . ALA   A 1  538 ? 4.032   -41.925 -17.313 1    23.973  ? 538  ALA   A CB  1 1 
ATOM   4390  N  N   . LYS   A 1  539 ? 4.328   -39.185 -15.684 1    23.496  ? 539  LYS   A N   1 1 
ATOM   4391  C  CA  . LYS   A 1  539 ? 4.062   -38.384 -14.498 1    23.646  ? 539  LYS   A CA  1 1 
ATOM   4392  C  C   . LYS   A 1  539 ? 3.408   -37.046 -14.877 1    23.14   ? 539  LYS   A C   1 1 
ATOM   4393  O  O   . LYS   A 1  539 ? 2.42    -36.634 -14.275 1    24.535  ? 539  LYS   A O   1 1 
ATOM   4394  C  CB  . LYS   A 1  539 ? 5.326   -38.366 -13.64  1    24.583  ? 539  LYS   A CB  1 1 
ATOM   4395  C  CG  . LYS   A 1  539 ? 5.138   -37.521 -12.376 1    28.463  ? 539  LYS   A CG  1 1 
ATOM   4396  C  CD  . LYS   A 1  539 ? 6.377   -37.313 -11.518 1    31.993  ? 539  LYS   A CD  1 1 
ATOM   4397  C  CE  . LYS   A 1  539 ? 6.421   -38.467 -10.602 1    35.366  ? 539  LYS   A CE  1 1 
ATOM   4398  N  NZ  . LYS   A 1  539 ? 5.661   -38.005 -9.433  1    31.517  ? 539  LYS   A NZ  1 1 
ATOM   4399  N  N   . LEU   A 1  540 ? 3.944   -36.343 -15.888 1    21.841  ? 540  LEU   A N   1 1 
ATOM   4400  C  CA  . LEU   A 1  540 ? 3.303   -35.142 -16.359 1    21.93   ? 540  LEU   A CA  1 1 
ATOM   4401  C  C   . LEU   A 1  540 ? 1.866   -35.391 -16.863 1    22.065  ? 540  LEU   A C   1 1 
ATOM   4402  O  O   . LEU   A 1  540 ? 0.952   -34.569 -16.667 1    20.55   ? 540  LEU   A O   1 1 
ATOM   4403  C  CB  . LEU   A 1  540 ? 4.239   -34.538 -17.399 1    22.359  ? 540  LEU   A CB  1 1 
ATOM   4404  C  CG  . LEU   A 1  540 ? 3.855   -33.144 -17.897 1    26.338  ? 540  LEU   A CG  1 1 
ATOM   4405  C  CD1 . LEU   A 1  540 ? 3.741   -32.177 -16.748 1    24.941  ? 540  LEU   A CD1 1 1 
ATOM   4406  C  CD2 . LEU   A 1  540 ? 4.946   -32.626 -18.877 1    28.893  ? 540  LEU   A CD2 1 1 
ATOM   4407  N  N   A ARG   A 1  541 ? 1.678   -36.513 -17.555 0.36 22.409  ? 541  ARG   A N   1 1 
ATOM   4408  N  N   B ARG   A 1  541 ? 1.658   -36.533 -17.515 0.64 22.676  ? 541  ARG   A N   1 1 
ATOM   4409  C  CA  A ARG   A 1  541 ? 0.376   -36.807 -18.125 0.36 23.323  ? 541  ARG   A CA  1 1 
ATOM   4410  C  CA  B ARG   A 1  541 ? 0.375   -36.846 -18.132 0.64 24.296  ? 541  ARG   A CA  1 1 
ATOM   4411  C  C   A ARG   A 1  541 ? -0.666  -36.813 -17.01  0.36 23.817  ? 541  ARG   A C   1 1 
ATOM   4412  C  C   B ARG   A 1  541 ? -0.715  -36.991 -17.069 0.64 24.53   ? 541  ARG   A C   1 1 
ATOM   4413  O  O   A ARG   A 1  541 ? -1.726  -36.208 -17.155 0.36 23.389  ? 541  ARG   A O   1 1 
ATOM   4414  O  O   B ARG   A 1  541 ? -1.886  -36.703 -17.309 0.64 24.825  ? 541  ARG   A O   1 1 
ATOM   4415  C  CB  A ARG   A 1  541 ? 0.375   -38.12  -18.921 0.36 24.081  ? 541  ARG   A CB  1 1 
ATOM   4416  C  CB  B ARG   A 1  541 ? 0.491   -38.143 -18.955 0.64 25.803  ? 541  ARG   A CB  1 1 
ATOM   4417  C  CG  A ARG   A 1  541 ? -0.863  -38.321 -19.791 0.36 24.762  ? 541  ARG   A CG  1 1 
ATOM   4418  C  CG  B ARG   A 1  541 ? -0.674  -38.486 -19.883 0.64 28.717  ? 541  ARG   A CG  1 1 
ATOM   4419  C  CD  A ARG   A 1  541 ? -0.626  -39.471 -20.775 0.36 25.849  ? 541  ARG   A CD  1 1 
ATOM   4420  C  CD  B ARG   A 1  541 ? -0.303  -39.571 -20.923 0.64 30.437  ? 541  ARG   A CD  1 1 
ATOM   4421  N  NE  A ARG   A 1  541 ? -1.791  -39.833 -21.586 0.36 26.24   ? 541  ARG   A NE  1 1 
ATOM   4422  N  NE  B ARG   A 1  541 ? 0.039   -40.839 -20.272 0.64 32.284  ? 541  ARG   A NE  1 1 
ATOM   4423  C  CZ  A ARG   A 1  541 ? -1.911  -39.776 -22.914 0.36 26.954  ? 541  ARG   A CZ  1 1 
ATOM   4424  C  CZ  B ARG   A 1  541 ? 1.206   -41.503 -20.238 0.64 32.902  ? 541  ARG   A CZ  1 1 
ATOM   4425  N  NH1 A ARG   A 1  541 ? -0.936  -39.297 -23.692 0.36 25.321  ? 541  ARG   A NH1 1 1 
ATOM   4426  N  NH1 B ARG   A 1  541 ? 2.26    -41.108 -20.955 0.64 29.916  ? 541  ARG   A NH1 1 1 
ATOM   4427  N  NH2 A ARG   A 1  541 ? -3.044  -40.222 -23.445 0.36 27.6    ? 541  ARG   A NH2 1 1 
ATOM   4428  N  NH2 B ARG   A 1  541 ? 1.292   -42.552 -19.431 0.64 32.441  ? 541  ARG   A NH2 1 1 
ATOM   4429  N  N   . LYS   A 1  542 ? -0.339  -37.466 -15.886 1    24.975  ? 542  LYS   A N   1 1 
ATOM   4430  C  CA  . LYS   A 1  542 ? -1.309  -37.602 -14.799 1    27.703  ? 542  LYS   A CA  1 1 
ATOM   4431  C  C   . LYS   A 1  542 ? -1.797  -36.221 -14.345 1    24.341  ? 542  LYS   A C   1 1 
ATOM   4432  O  O   . LYS   A 1  542 ? -2.99   -36.039 -14.137 1    25.724  ? 542  LYS   A O   1 1 
ATOM   4433  C  CB  . LYS   A 1  542 ? -0.707  -38.36  -13.623 1    27.384  ? 542  LYS   A CB  1 1 
ATOM   4434  C  CG  . LYS   A 1  542 ? -0.817  -39.844 -13.852 1    36.589  ? 542  LYS   A CG  1 1 
ATOM   4435  C  CD  . LYS   A 1  542 ? -0.123  -40.672 -12.773 1    48.637  ? 542  LYS   A CD  1 1 
ATOM   4436  C  CE  . LYS   A 1  542 ? -0.315  -42.151 -13.036 1    56.234  ? 542  LYS   A CE  1 1 
ATOM   4437  N  NZ  . LYS   A 1  542 ? 0.87    -42.939 -12.668 1    58.452  ? 542  LYS   A NZ  1 1 
ATOM   4438  N  N   . VAL   A 1  543 ? -0.904  -35.235 -14.345 1    21.723  ? 543  VAL   A N   1 1 
ATOM   4439  C  CA  . VAL   A 1  543 ? -1.295  -33.875 -14.018 1    21.546  ? 543  VAL   A CA  1 1 
ATOM   4440  C  C   . VAL   A 1  543 ? -2.237  -33.383 -15.105 1    22.832  ? 543  VAL   A C   1 1 
ATOM   4441  O  O   . VAL   A 1  543 ? -3.302  -32.879 -14.788 1    22.494  ? 543  VAL   A O   1 1 
ATOM   4442  C  CB  . VAL   A 1  543 ? -0.118  -32.896 -13.834 1    20.213  ? 543  VAL   A CB  1 1 
ATOM   4443  C  CG1 . VAL   A 1  543 ? -0.586  -31.442 -13.689 1    20.444  ? 543  VAL   A CG1 1 1 
ATOM   4444  C  CG2 . VAL   A 1  543 ? 0.736   -33.313 -12.66  1    20.533  ? 543  VAL   A CG2 1 1 
ATOM   4445  N  N   . LEU   A 1  544 ? -1.806  -33.492 -16.373 1    22.206  ? 544  LEU   A N   1 1 
ATOM   4446  C  CA  . LEU   A 1  544 ? -2.565  -32.861 -17.45  1    20.827  ? 544  LEU   A CA  1 1 
ATOM   4447  C  C   . LEU   A 1  544 ? -3.993  -33.426 -17.512 1    20.841  ? 544  LEU   A C   1 1 
ATOM   4448  O  O   . LEU   A 1  544 ? -4.941  -32.655 -17.634 1    20.135  ? 544  LEU   A O   1 1 
ATOM   4449  C  CB  . LEU   A 1  544 ? -1.818  -32.964 -18.775 1    20.226  ? 544  LEU   A CB  1 1 
ATOM   4450  C  CG  . LEU   A 1  544 ? -0.369  -32.473 -18.72  1    22.373  ? 544  LEU   A CG  1 1 
ATOM   4451  C  CD1 . LEU   A 1  544 ? 0.26    -32.504 -20.123 1    22.234  ? 544  LEU   A CD1 1 1 
ATOM   4452  C  CD2 . LEU   A 1  544 ? -0.45   -31.03  -18.155 1    20.872  ? 544  LEU   A CD2 1 1 
ATOM   4453  N  N   . ARG   A 1  545 ? -4.114  -34.738 -17.349 1    21.76   ? 545  ARG   A N   1 1 
ATOM   4454  C  CA  . ARG   A 1  545 ? -5.381  -35.447 -17.429 1    27.8    ? 545  ARG   A CA  1 1 
ATOM   4455  C  C   . ARG   A 1  545 ? -6.357  -35.024 -16.329 1    28.14   ? 545  ARG   A C   1 1 
ATOM   4456  O  O   . ARG   A 1  545 ? -7.546  -35.135 -16.563 1    27.941  ? 545  ARG   A O   1 1 
ATOM   4457  C  CB  . ARG   A 1  545 ? -5.288  -36.977 -17.55  1    28.197  ? 545  ARG   A CB  1 1 
ATOM   4458  C  CG  . ARG   A 1  545 ? -4.61   -37.331 -18.874 1    35.548  ? 545  ARG   A CG  1 1 
ATOM   4459  C  CD  . ARG   A 1  545 ? -4.743  -38.823 -19.205 1    38.238  ? 545  ARG   A CD  1 1 
ATOM   4460  N  NE  . ARG   A 1  545 ? -6.081  -39.125 -19.731 1    44.021  ? 545  ARG   A NE  1 1 
ATOM   4461  C  CZ  . ARG   A 1  545 ? -6.502  -38.939 -20.979 1    46.678  ? 545  ARG   A CZ  1 1 
ATOM   4462  N  NH1 . ARG   A 1  545 ? -5.728  -38.397 -21.913 1    46.376  ? 545  ARG   A NH1 1 1 
ATOM   4463  N  NH2 . ARG   A 1  545 ? -7.713  -39.317 -21.297 1    44.419  ? 545  ARG   A NH2 1 1 
ATOM   4464  N  N   . ALA   A 1  546 ? -5.876  -34.479 -15.199 1    26.402  ? 546  ALA   A N   1 1 
ATOM   4465  C  CA  . ALA   A 1  546 ? -6.757  -34.138 -14.084 1    26.742  ? 546  ALA   A CA  1 1 
ATOM   4466  C  C   . ALA   A 1  546 ? -7.583  -32.885 -14.385 1    26.249  ? 546  ALA   A C   1 1 
ATOM   4467  O  O   . ALA   A 1  546 ? -8.647  -32.717 -13.813 1    28.241  ? 546  ALA   A O   1 1 
ATOM   4468  C  CB  . ALA   A 1  546 ? -5.932  -33.96  -12.823 1    25.625  ? 546  ALA   A CB  1 1 
ATOM   4469  N  N   . GLY   A 1  547 ? -7.119  -31.986 -15.258 1    22.958  ? 547  GLY   A N   1 1 
ATOM   4470  C  CA  . GLY   A 1  547 ? -7.789  -30.697 -15.405 1    23.531  ? 547  GLY   A CA  1 1 
ATOM   4471  C  C   . GLY   A 1  547 ? -7.978  -30.077 -14.013 1    25.555  ? 547  GLY   A C   1 1 
ATOM   4472  O  O   . GLY   A 1  547 ? -7.083  -30.209 -13.186 1    23.467  ? 547  GLY   A O   1 1 
ATOM   4473  N  N   . SER   A 1  548 ? -9.175  -29.528 -13.743 1    23.785  ? 548  SER   A N   1 1 
ATOM   4474  C  CA  . SER   A 1  548 ? -9.506  -28.9   -12.475 1    23.829  ? 548  SER   A CA  1 1 
ATOM   4475  C  C   . SER   A 1  548 ? -10.482 -29.803 -11.745 1    26.824  ? 548  SER   A C   1 1 
ATOM   4476  O  O   . SER   A 1  548 ? -11.287 -29.365 -10.921 1    26.491  ? 548  SER   A O   1 1 
ATOM   4477  C  CB  . SER   A 1  548 ? -10.062 -27.507 -12.674 1    24.392  ? 548  SER   A CB  1 1 
ATOM   4478  O  OG  . SER   A 1  548 ? -11.255 -27.579 -13.464 1    26.824  ? 548  SER   A OG  1 1 
ATOM   4479  N  N   . SER   A 1  549 ? -10.378 -31.095 -12.037 1    27.377  ? 549  SER   A N   1 1 
ATOM   4480  C  CA  . SER   A 1  549 ? -11.296 -32.028 -11.425 1    28.366  ? 549  SER   A CA  1 1 
ATOM   4481  C  C   . SER   A 1  549 ? -10.966 -32.272 -9.953  1    31.12   ? 549  SER   A C   1 1 
ATOM   4482  O  O   . SER   A 1  549 ? -11.815 -32.8   -9.241  1    28.082  ? 549  SER   A O   1 1 
ATOM   4483  C  CB  . SER   A 1  549 ? -11.311 -33.337 -12.197 1    29.081  ? 549  SER   A CB  1 1 
ATOM   4484  O  OG  . SER   A 1  549 ? -10.061 -33.992 -11.994 1    34.317  ? 549  SER   A OG  1 1 
ATOM   4485  N  N   . ARG   A 1  550 ? -9.709  -32.015 -9.529  1    29.455  ? 550  ARG   A N   1 1 
ATOM   4486  C  CA  . ARG   A 1  550 ? -9.287  -32.304 -8.153  1    28.644  ? 550  ARG   A CA  1 1 
ATOM   4487  C  C   . ARG   A 1  550 ? -8.529  -31.114 -7.57   1    26.699  ? 550  ARG   A C   1 1 
ATOM   4488  O  O   . ARG   A 1  550 ? -7.927  -30.339 -8.322  1    24.647  ? 550  ARG   A O   1 1 
ATOM   4489  C  CB  . ARG   A 1  550 ? -8.243  -33.417 -8.064  1    28.811  ? 550  ARG   A CB  1 1 
ATOM   4490  C  CG  . ARG   A 1  550 ? -8.857  -34.76  -8.439  1    37.249  ? 550  ARG   A CG  1 1 
ATOM   4491  C  CD  . ARG   A 1  550 ? -8.047  -35.838 -7.697  1    43.161  ? 550  ARG   A CD  1 1 
ATOM   4492  N  NE  . ARG   A 1  550 ? -6.864  -36.148 -8.493  1    43.963  ? 550  ARG   A NE  1 1 
ATOM   4493  C  CZ  . ARG   A 1  550 ? -5.564  -36.266 -8.184  1    49.047  ? 550  ARG   A CZ  1 1 
ATOM   4494  N  NH1 . ARG   A 1  550 ? -5.118  -36.302 -6.928  1    42.426  ? 550  ARG   A NH1 1 1 
ATOM   4495  N  NH2 . ARG   A 1  550 ? -4.725  -36.392 -9.202  1    43.081  ? 550  ARG   A NH2 1 1 
ATOM   4496  N  N   . PRO   A 1  551 ? -8.552  -30.892 -6.233  1    25.582  ? 551  PRO   A N   1 1 
ATOM   4497  C  CA  . PRO   A 1  551 ? -7.901  -29.705 -5.641  1    24.376  ? 551  PRO   A CA  1 1 
ATOM   4498  C  C   . PRO   A 1  551 ? -6.435  -29.633 -6.068  1    21.322  ? 551  PRO   A C   1 1 
ATOM   4499  O  O   . PRO   A 1  551 ? -5.756  -30.655 -6.032  1    20.479  ? 551  PRO   A O   1 1 
ATOM   4500  C  CB  . PRO   A 1  551 ? -8.021  -29.961 -4.104  1    27.601  ? 551  PRO   A CB  1 1 
ATOM   4501  C  CG  . PRO   A 1  551 ? -9.177  -30.927 -3.951  1    29.333  ? 551  PRO   A CG  1 1 
ATOM   4502  C  CD  . PRO   A 1  551 ? -9.207  -31.762 -5.238  1    29.247  ? 551  PRO   A CD  1 1 
ATOM   4503  N  N   . TRP   A 1  552 ? -5.955  -28.44  -6.451  1    19.783  ? 552  TRP   A N   1 1 
ATOM   4504  C  CA  . TRP   A 1  552 ? -4.591  -28.356 -6.956  1    20.331  ? 552  TRP   A CA  1 1 
ATOM   4505  C  C   . TRP   A 1  552 ? -3.569  -28.822 -5.918  1    20.461  ? 552  TRP   A C   1 1 
ATOM   4506  O  O   . TRP   A 1  552 ? -2.53   -29.379 -6.286  1    19.092  ? 552  TRP   A O   1 1 
ATOM   4507  C  CB  . TRP   A 1  552 ? -4.266  -26.954 -7.452  1    18.96   ? 552  TRP   A CB  1 1 
ATOM   4508  C  CG  . TRP   A 1  552 ? -4.16   -25.909 -6.367  1    20.106  ? 552  TRP   A CG  1 1 
ATOM   4509  C  CD1 . TRP   A 1  552 ? -5.143  -25.004 -6.003  1    19.784  ? 552  TRP   A CD1 1 1 
ATOM   4510  C  CD2 . TRP   A 1  552 ? -2.976  -25.578 -5.599  1    19.904  ? 552  TRP   A CD2 1 1 
ATOM   4511  N  NE1 . TRP   A 1  552 ? -4.635  -24.162 -5.032  1    22.436  ? 552  TRP   A NE1 1 1 
ATOM   4512  C  CE2 . TRP   A 1  552 ? -3.307  -24.459 -4.796  1    20.655  ? 552  TRP   A CE2 1 1 
ATOM   4513  C  CE3 . TRP   A 1  552 ? -1.661  -26.076 -5.543  1    22.395  ? 552  TRP   A CE3 1 1 
ATOM   4514  C  CZ2 . TRP   A 1  552 ? -2.393  -23.861 -3.923  1    22.733  ? 552  TRP   A CZ2 1 1 
ATOM   4515  C  CZ3 . TRP   A 1  552 ? -0.747  -25.487 -4.683  1    24.302  ? 552  TRP   A CZ3 1 1 
ATOM   4516  C  CH2 . TRP   A 1  552 ? -1.11   -24.378 -3.896  1    24.189  ? 552  TRP   A CH2 1 1 
ATOM   4517  N  N   . GLN   A 1  553 ? -3.879  -28.63  -4.617  1    20.938  ? 553  GLN   A N   1 1 
ATOM   4518  C  CA  . GLN   A 1  553 ? -2.942  -29.018 -3.57   1    21.494  ? 553  GLN   A CA  1 1 
ATOM   4519  C  C   . GLN   A 1  553 ? -2.656  -30.525 -3.585  1    23.145  ? 553  GLN   A C   1 1 
ATOM   4520  O  O   . GLN   A 1  553 ? -1.516  -30.938 -3.283  1    22.347  ? 553  GLN   A O   1 1 
ATOM   4521  C  CB  . GLN   A 1  553 ? -3.353  -28.574 -2.16   1    21.893  ? 553  GLN   A CB  1 1 
ATOM   4522  C  CG  . GLN   A 1  553 ? -3.467  -27.056 -2.053  1    20.9    ? 553  GLN   A CG  1 1 
ATOM   4523  C  CD  . GLN   A 1  553 ? -4.867  -26.483 -2.316  1    21.817  ? 553  GLN   A CD  1 1 
ATOM   4524  O  OE1 . GLN   A 1  553 ? -5.664  -27.029 -3.078  1    21.368  ? 553  GLN   A OE1 1 1 
ATOM   4525  N  NE2 . GLN   A 1  553 ? -5.161  -25.298 -1.795  1    19.748  ? 553  GLN   A NE2 1 1 
ATOM   4526  N  N   . GLU   A 1  554 ? -3.69   -31.339 -3.848  1    22.866  ? 554  GLU   A N   1 1 
ATOM   4527  C  CA  . GLU   A 1  554 ? -3.537  -32.792 -3.942  1    24.939  ? 554  GLU   A CA  1 1 
ATOM   4528  C  C   . GLU   A 1  554 ? -2.904  -33.259 -5.258  1    23.837  ? 554  GLU   A C   1 1 
ATOM   4529  O  O   . GLU   A 1  554 ? -2.167  -34.25  -5.267  1    24.091  ? 554  GLU   A O   1 1 
ATOM   4530  C  CB  . GLU   A 1  554 ? -4.894  -33.495 -3.916  1    30.081  ? 554  GLU   A CB  1 1 
ATOM   4531  C  CG  . GLU   A 1  554 ? -5.708  -33.205 -2.66   1    39.45   ? 554  GLU   A CG  1 1 
ATOM   4532  C  CD  . GLU   A 1  554 ? -7.029  -33.979 -2.591  1    50.538  ? 554  GLU   A CD  1 1 
ATOM   4533  O  OE1 . GLU   A 1  554 ? -7.373  -34.814 -3.497  1    54.823  ? 554  GLU   A OE1 1 1 
ATOM   4534  O  OE2 . GLU   A 1  554 ? -7.742  -33.709 -1.589  1    55.646  ? 554  GLU   A OE2 1 1 
ATOM   4535  N  N   . VAL   A 1  555 ? -3.242  -32.622 -6.39   1    23.028  ? 555  VAL   A N   1 1 
ATOM   4536  C  CA  . VAL   A 1  555 ? -2.51   -32.899 -7.624  1    22.68   ? 555  VAL   A CA  1 1 
ATOM   4537  C  C   . VAL   A 1  555 ? -0.997  -32.626 -7.465  1    21.838  ? 555  VAL   A C   1 1 
ATOM   4538  O  O   . VAL   A 1  555 ? -0.162  -33.477 -7.824  1    20.631  ? 555  VAL   A O   1 1 
ATOM   4539  C  CB  . VAL   A 1  555 ? -3.158  -32.097 -8.759  1    21.672  ? 555  VAL   A CB  1 1 
ATOM   4540  C  CG1 . VAL   A 1  555 ? -2.43   -32.368 -10.06  1    21.375  ? 555  VAL   A CG1 1 1 
ATOM   4541  C  CG2 . VAL   A 1  555 ? -4.658  -32.432 -8.916  1    21.017  ? 555  VAL   A CG2 1 1 
ATOM   4542  N  N   . LEU   A 1  556 ? -0.637  -31.467 -6.897  1    21.197  ? 556  LEU   A N   1 1 
ATOM   4543  C  CA  . LEU   A 1  556 ? 0.753   -31.097 -6.597  1    20.364  ? 556  LEU   A CA  1 1 
ATOM   4544  C  C   . LEU   A 1  556 ? 1.429   -32.149 -5.726  1    23.51   ? 556  LEU   A C   1 1 
ATOM   4545  O  O   . LEU   A 1  556 ? 2.52    -32.625 -6.035  1    22.756  ? 556  LEU   A O   1 1 
ATOM   4546  C  CB  . LEU   A 1  556 ? 0.848   -29.722 -5.95   1    19.515  ? 556  LEU   A CB  1 1 
ATOM   4547  C  CG  . LEU   A 1  556 ? 2.269   -29.173 -5.815  1    19.311  ? 556  LEU   A CG  1 1 
ATOM   4548  C  CD1 . LEU   A 1  556 ? 2.986   -29.096 -7.164  1    18.096  ? 556  LEU   A CD1 1 1 
ATOM   4549  C  CD2 . LEU   A 1  556 ? 2.216   -27.763 -5.191  1    21.371  ? 556  LEU   A CD2 1 1 
ATOM   4550  N  N   . LYS   A 1  557 ? 0.752   -32.543 -4.644  1    23.876  ? 557  LYS   A N   1 1 
ATOM   4551  C  CA  . LYS   A 1  557 ? 1.317   -33.523 -3.731  1    29.794  ? 557  LYS   A CA  1 1 
ATOM   4552  C  C   . LYS   A 1  557 ? 1.583   -34.871 -4.416  1    28.025  ? 557  LYS   A C   1 1 
ATOM   4553  O  O   . LYS   A 1  557 ? 2.645   -35.447 -4.223  1    28.085  ? 557  LYS   A O   1 1 
ATOM   4554  C  CB  . LYS   A 1  557 ? 0.443   -33.676 -2.485  1    33.546  ? 557  LYS   A CB  1 1 
ATOM   4555  C  CG  . LYS   A 1  557 ? 1.046   -34.632 -1.498  1    40.477  ? 557  LYS   A CG  1 1 
ATOM   4556  C  CD  . LYS   A 1  557 ? 0.233   -34.538 -0.208  1    50.464  ? 557  LYS   A CD  1 1 
ATOM   4557  C  CE  . LYS   A 1  557 ? 0.78    -35.467 0.851   1    62.287  ? 557  LYS   A CE  1 1 
ATOM   4558  N  NZ  . LYS   A 1  557 ? 2.247   -35.411 0.866   1    66.271  ? 557  LYS   A NZ  1 1 
ATOM   4559  N  N   . ASP   A 1  558 ? 0.661   -35.347 -5.253  1    25.751  ? 558  ASP   A N   1 1 
ATOM   4560  C  CA  . ASP   A 1  558 ? 0.894   -36.576 -5.998  1    28.625  ? 558  ASP   A CA  1 1 
ATOM   4561  C  C   . ASP   A 1  558 ? 2.106   -36.411 -6.916  1    28.962  ? 558  ASP   A C   1 1 
ATOM   4562  O  O   . ASP   A 1  558 ? 2.828   -37.372 -7.141  1    31.819  ? 558  ASP   A O   1 1 
ATOM   4563  C  CB  . ASP   A 1  558 ? -0.296  -36.931 -6.892  1    32.408  ? 558  ASP   A CB  1 1 
ATOM   4564  C  CG  . ASP   A 1  558 ? -1.536  -37.445 -6.173  1    38.348  ? 558  ASP   A CG  1 1 
ATOM   4565  O  OD1 . ASP   A 1  558 ? -1.433  -37.65  -4.939  1    40.714  ? 558  ASP   A OD1 1 1 
ATOM   4566  O  OD2 . ASP   A 1  558 ? -2.594  -37.631 -6.84   1    40.465  ? 558  ASP   A OD2 1 1 
ATOM   4567  N  N   . MET   A 1  559 ? 2.291   -35.208 -7.484  1    26.766  ? 559  MET   A N   1 1 
ATOM   4568  C  CA  . MET   A 1  559 ? 3.335   -35.014 -8.471  1    26.343  ? 559  MET   A CA  1 1 
ATOM   4569  C  C   . MET   A 1  559 ? 4.702   -34.862 -7.797  1    26.843  ? 559  MET   A C   1 1 
ATOM   4570  O  O   . MET   A 1  559 ? 5.658   -35.501 -8.237  1    24.61   ? 559  MET   A O   1 1 
ATOM   4571  C  CB  . MET   A 1  559 ? 3.116   -33.818 -9.386  1    24.568  ? 559  MET   A CB  1 1 
ATOM   4572  C  CG  . MET   A 1  559 ? 3.954   -34.026 -10.66  1    30.56   ? 559  MET   A CG  1 1 
ATOM   4573  S  SD  . MET   A 1  559 ? 4.022   -32.322 -11.21  1    35.103  ? 559  MET   A SD  1 1 
ATOM   4574  C  CE  . MET   A 1  559 ? 4.835   -32.457 -12.825 1    33.119  ? 559  MET   A CE  1 1 
ATOM   4575  N  N   . VAL   A 1  560 ? 4.778   -34.015 -6.769  1    24.211  ? 560  VAL   A N   1 1 
ATOM   4576  C  CA  . VAL   A 1  560 ? 6.056   -33.523 -6.281  1    26.626  ? 560  VAL   A CA  1 1 
ATOM   4577  C  C   . VAL   A 1  560 ? 6.221   -33.928 -4.819  1    28.359  ? 560  VAL   A C   1 1 
ATOM   4578  O  O   . VAL   A 1  560 ? 7.316   -33.788 -4.264  1    29.686  ? 560  VAL   A O   1 1 
ATOM   4579  C  CB  . VAL   A 1  560 ? 6.314   -32.017 -6.517  1    25.22   ? 560  VAL   A CB  1 1 
ATOM   4580  C  CG1 . VAL   A 1  560 ? 5.955   -31.587 -7.966  1    25.127  ? 560  VAL   A CG1 1 1 
ATOM   4581  C  CG2 . VAL   A 1  560 ? 5.566   -31.092 -5.537  1    24.285  ? 560  VAL   A CG2 1 1 
ATOM   4582  N  N   . GLY   A 1  561 ? 5.155   -34.45  -4.197  1    26.41   ? 561  GLY   A N   1 1 
ATOM   4583  C  CA  . GLY   A 1  561 ? 5.269   -34.952 -2.828  1    27.194  ? 561  GLY   A CA  1 1 
ATOM   4584  C  C   . GLY   A 1  561 ? 5.147   -33.845 -1.783  1    28.241  ? 561  GLY   A C   1 1 
ATOM   4585  O  O   . GLY   A 1  561 ? 5.397   -34.054 -0.607  1    28.871  ? 561  GLY   A O   1 1 
ATOM   4586  N  N   . LEU   A 1  562 ? 4.699   -32.664 -2.193  1    27.987  ? 562  LEU   A N   1 1 
ATOM   4587  C  CA  . LEU   A 1  562 ? 4.437   -31.59  -1.262  1    30.971  ? 562  LEU   A CA  1 1 
ATOM   4588  C  C   . LEU   A 1  562 ? 3.132   -30.936 -1.697  1    28.692  ? 562  LEU   A C   1 1 
ATOM   4589  O  O   . LEU   A 1  562 ? 2.845   -30.868 -2.902  1    27.207  ? 562  LEU   A O   1 1 
ATOM   4590  C  CB  . LEU   A 1  562 ? 5.612   -30.621 -1.417  1    33.4    ? 562  LEU   A CB  1 1 
ATOM   4591  C  CG  . LEU   A 1  562 ? 5.523   -29.37  -0.544  1    39.234  ? 562  LEU   A CG  1 1 
ATOM   4592  C  CD1 . LEU   A 1  562 ? 5.711   -29.724 0.941   1    36.186  ? 562  LEU   A CD1 1 1 
ATOM   4593  C  CD2 . LEU   A 1  562 ? 6.563   -28.41  -1.047  1    39.892  ? 562  LEU   A CD2 1 1 
ATOM   4594  N  N   . ASP   A 1  563 ? 2.359   -30.413 -0.744  1    28.108  ? 563  ASP   A N   1 1 
ATOM   4595  C  CA  . ASP   A 1  563 ? 1.041   -29.904 -1.132  1    27.722  ? 563  ASP   A CA  1 1 
ATOM   4596  C  C   . ASP   A 1  563 ? 0.985   -28.373 -1.197  1    26.987  ? 563  ASP   A C   1 1 
ATOM   4597  O  O   . ASP   A 1  563 ? -0.092  -27.805 -1.061  1    27.417  ? 563  ASP   A O   1 1 
ATOM   4598  C  CB  . ASP   A 1  563 ? -0.022  -30.417 -0.176  1    31.721  ? 563  ASP   A CB  1 1 
ATOM   4599  C  CG  . ASP   A 1  563 ? 0.064   -29.798 1.215   1    38.675  ? 563  ASP   A CG  1 1 
ATOM   4600  O  OD1 . ASP   A 1  563 ? 0.939   -28.924 1.435   1    37.322  ? 563  ASP   A OD1 1 1 
ATOM   4601  O  OD2 . ASP   A 1  563 ? -0.774  -30.153 2.06    1    46.939  ? 563  ASP   A OD2 1 1 
ATOM   4602  N  N   . ALA   A 1  564 ? 2.098   -27.69  -1.477  1    25.068  ? 564  ALA   A N   1 1 
ATOM   4603  C  CA  . ALA   A 1  564 ? 2.178   -26.229 -1.458  1    22.132  ? 564  ALA   A CA  1 1 
ATOM   4604  C  C   . ALA   A 1  564 ? 3.249   -25.748 -2.443  1    21.092  ? 564  ALA   A C   1 1 
ATOM   4605  O  O   . ALA   A 1  564 ? 4.239   -26.452 -2.68   1    19.789  ? 564  ALA   A O   1 1 
ATOM   4606  C  CB  . ALA   A 1  564 ? 2.575   -25.759 -0.039  1    22.89   ? 564  ALA   A CB  1 1 
ATOM   4607  N  N   . LEU   A 1  565 ? 3.104   -24.5   -2.893  1    19.947  ? 565  LEU   A N   1 1 
ATOM   4608  C  CA  . LEU   A 1  565 ? 4.176   -23.819 -3.605  1    21.142  ? 565  LEU   A CA  1 1 
ATOM   4609  C  C   . LEU   A 1  565 ? 5.381   -23.737 -2.675  1    23.522  ? 565  LEU   A C   1 1 
ATOM   4610  O  O   . LEU   A 1  565 ? 5.234   -23.538 -1.48   1    22.242  ? 565  LEU   A O   1 1 
ATOM   4611  C  CB  . LEU   A 1  565 ? 3.741   -22.398 -3.919  1    22.075  ? 565  LEU   A CB  1 1 
ATOM   4612  C  CG  . LEU   A 1  565 ? 2.538   -22.219 -4.831  1    27.179  ? 565  LEU   A CG  1 1 
ATOM   4613  C  CD1 . LEU   A 1  565 ? 2.417   -20.709 -5.079  1    27.315  ? 565  LEU   A CD1 1 1 
ATOM   4614  C  CD2 . LEU   A 1  565 ? 2.863   -22.921 -6.159  1    26.784  ? 565  LEU   A CD2 1 1 
ATOM   4615  N  N   . ASP   A 1  566 ? 6.579   -23.904 -3.229  1    21.557  ? 566  ASP   A N   1 1 
ATOM   4616  C  CA  . ASP   A 1  566 ? 7.775   -23.922 -2.395  1    21.82   ? 566  ASP   A CA  1 1 
ATOM   4617  C  C   . ASP   A 1  566 ? 8.907   -23.377 -3.267  1    20.77   ? 566  ASP   A C   1 1 
ATOM   4618  O  O   . ASP   A 1  566 ? 8.982   -23.772 -4.435  1    20.199  ? 566  ASP   A O   1 1 
ATOM   4619  C  CB  . ASP   A 1  566 ? 8.115   -25.366 -2.101  1    25.419  ? 566  ASP   A CB  1 1 
ATOM   4620  C  CG  . ASP   A 1  566 ? 9.389   -25.578 -1.274  1    33.617  ? 566  ASP   A CG  1 1 
ATOM   4621  O  OD1 . ASP   A 1  566 ? 9.817   -24.611 -0.593  1    38.123  ? 566  ASP   A OD1 1 1 
ATOM   4622  O  OD2 . ASP   A 1  566 ? 9.98    -26.691 -1.348  1    39.191  ? 566  ASP   A OD2 1 1 
ATOM   4623  N  N   . ALA   A 1  567 ? 9.626   -22.361 -2.774  1    19.33   ? 567  ALA   A N   1 1 
ATOM   4624  C  CA  . ALA   A 1  567 ? 10.768  -21.762 -3.462  1    19.922  ? 567  ALA   A CA  1 1 
ATOM   4625  C  C   . ALA   A 1  567 ? 12.034  -22.649 -3.441  1    19.573  ? 567  ALA   A C   1 1 
ATOM   4626  O  O   . ALA   A 1  567 ? 12.973  -22.335 -4.162  1    18.918  ? 567  ALA   A O   1 1 
ATOM   4627  C  CB  . ALA   A 1  567 ? 11.095  -20.375 -2.864  1    20.369  ? 567  ALA   A CB  1 1 
ATOM   4628  N  N   . GLN   A 1  568 ? 12.111  -23.688 -2.601  1    20.149  ? 568  GLN   A N   1 1 
ATOM   4629  C  CA  . GLN   A 1  568 ? 13.335  -24.496 -2.5    1    23.094  ? 568  GLN   A CA  1 1 
ATOM   4630  C  C   . GLN   A 1  568 ? 13.837  -25.024 -3.857  1    20.993  ? 568  GLN   A C   1 1 
ATOM   4631  O  O   . GLN   A 1  568 ? 15.05   -25.05  -4.112  1    19.92   ? 568  GLN   A O   1 1 
ATOM   4632  C  CB  . GLN   A 1  568 ? 13.31   -25.592 -1.436  1    29.054  ? 568  GLN   A CB  1 1 
ATOM   4633  C  CG  . GLN   A 1  568 ? 13.488  -25.051 -0.03   1    35.734  ? 568  GLN   A CG  1 1 
ATOM   4634  C  CD  . GLN   A 1  568 ? 14.819  -24.337 0.106   1    44.244  ? 568  GLN   A CD  1 1 
ATOM   4635  O  OE1 . GLN   A 1  568 ? 15.886  -24.9   -0.159  1    47.303  ? 568  GLN   A OE1 1 1 
ATOM   4636  N  NE2 . GLN   A 1  568 ? 14.76   -23.057 0.443   1    50.376  ? 568  GLN   A NE2 1 1 
ATOM   4637  N  N   . PRO   A 1  569 ? 13.001  -25.61  -4.734  1    19.12   ? 569  PRO   A N   1 1 
ATOM   4638  C  CA  . PRO   A 1  569 ? 13.539  -26.093 -6.014  1    18.89   ? 569  PRO   A CA  1 1 
ATOM   4639  C  C   . PRO   A 1  569 ? 14.183  -25.001 -6.861  1    17.203  ? 569  PRO   A C   1 1 
ATOM   4640  O  O   . PRO   A 1  569 ? 15.261  -25.241 -7.425  1    16.922  ? 569  PRO   A O   1 1 
ATOM   4641  C  CB  . PRO   A 1  569 ? 12.296  -26.732 -6.665  1    16.342  ? 569  PRO   A CB  1 1 
ATOM   4642  C  CG  . PRO   A 1  569 ? 11.609  -27.306 -5.402  1    17.639  ? 569  PRO   A CG  1 1 
ATOM   4643  C  CD  . PRO   A 1  569 ? 11.617  -26.081 -4.48   1    17.846  ? 569  PRO   A CD  1 1 
ATOM   4644  N  N   . LEU   A 1  570 ? 13.523  -23.833 -6.925  1    15.223  ? 570  LEU   A N   1 1 
ATOM   4645  C  CA  . LEU   A 1  570 ? 14.111  -22.729 -7.677  1    15.266  ? 570  LEU   A CA  1 1 
ATOM   4646  C  C   . LEU   A 1  570 ? 15.447  -22.302 -7.048  1    15.523  ? 570  LEU   A C   1 1 
ATOM   4647  O  O   . LEU   A 1  570 ? 16.441  -22.059 -7.75   1    15.681  ? 570  LEU   A O   1 1 
ATOM   4648  C  CB  . LEU   A 1  570 ? 13.114  -21.576 -7.727  1    13.666  ? 570  LEU   A CB  1 1 
ATOM   4649  C  CG  . LEU   A 1  570 ? 13.568  -20.31  -8.465  1    15.571  ? 570  LEU   A CG  1 1 
ATOM   4650  C  CD1 . LEU   A 1  570 ? 12.296  -19.529 -8.708  1    14.249  ? 570  LEU   A CD1 1 1 
ATOM   4651  C  CD2 . LEU   A 1  570 ? 14.5    -19.427 -7.613  1    15.123  ? 570  LEU   A CD2 1 1 
ATOM   4652  N  N   . LEU   A 1  571 ? 15.527  -22.197 -5.699  1    15.809  ? 571  LEU   A N   1 1 
ATOM   4653  C  CA  . LEU   A 1  571 ? 16.807  -21.835 -5.052  1    16.709  ? 571  LEU   A CA  1 1 
ATOM   4654  C  C   . LEU   A 1  571 ? 17.925  -22.836 -5.361  1    17.179  ? 571  LEU   A C   1 1 
ATOM   4655  O  O   . LEU   A 1  571 ? 19.108  -22.45  -5.553  1    17.85   ? 571  LEU   A O   1 1 
ATOM   4656  C  CB  . LEU   A 1  571 ? 16.687  -21.673 -3.531  1    17.821  ? 571  LEU   A CB  1 1 
ATOM   4657  C  CG  . LEU   A 1  571 ? 15.68   -20.577 -3.124  1    19.726  ? 571  LEU   A CG  1 1 
ATOM   4658  C  CD1 . LEU   A 1  571 ? 15.375  -20.528 -1.595  1    22.039  ? 571  LEU   A CD1 1 1 
ATOM   4659  C  CD2 . LEU   A 1  571 ? 16.089  -19.227 -3.607  1    19.793  ? 571  LEU   A CD2 1 1 
ATOM   4660  N  N   . LYS   A 1  572 ? 17.574  -24.113 -5.287  1    17.241  ? 572  LYS   A N   1 1 
ATOM   4661  C  CA  . LYS   A 1  572 ? 18.489  -25.196 -5.58   1    19.995  ? 572  LYS   A CA  1 1 
ATOM   4662  C  C   . LYS   A 1  572 ? 19.01   -25.095 -7.019  1    19.308  ? 572  LYS   A C   1 1 
ATOM   4663  O  O   . LYS   A 1  572 ? 20.22   -25.208 -7.268  1    18.621  ? 572  LYS   A O   1 1 
ATOM   4664  C  CB  . LYS   A 1  572 ? 17.788  -26.505 -5.271  1    24.189  ? 572  LYS   A CB  1 1 
ATOM   4665  C  CG  . LYS   A 1  572 ? 18.729  -27.665 -5.407  1    34.801  ? 572  LYS   A CG  1 1 
ATOM   4666  C  CD  . LYS   A 1  572 ? 17.836  -28.838 -5.029  1    46.854  ? 572  LYS   A CD  1 1 
ATOM   4667  C  CE  . LYS   A 1  572 ? 18.49   -30.174 -5.235  1    56.012  ? 572  LYS   A CE  1 1 
ATOM   4668  N  NZ  . LYS   A 1  572 ? 17.39   -31.141 -5.41   1    57.192  ? 572  LYS   A NZ  1 1 
ATOM   4669  N  N   . TYR   A 1  573 ? 18.108  -24.797 -7.954  1    16.548  ? 573  TYR   A N   1 1 
ATOM   4670  C  CA  . TYR   A 1  573 ? 18.524  -24.736 -9.355  1    16.432  ? 573  TYR   A CA  1 1 
ATOM   4671  C  C   . TYR   A 1  573 ? 19.563  -23.627 -9.553  1    16.309  ? 573  TYR   A C   1 1 
ATOM   4672  O  O   . TYR   A 1  573 ? 20.505  -23.797 -10.355 1    17.029  ? 573  TYR   A O   1 1 
ATOM   4673  C  CB  . TYR   A 1  573 ? 17.247  -24.479 -10.156 1    14.409  ? 573  TYR   A CB  1 1 
ATOM   4674  C  CG  . TYR   A 1  573 ? 17.428  -24.318 -11.666 1    13.719  ? 573  TYR   A CG  1 1 
ATOM   4675  C  CD1 . TYR   A 1  573 ? 17.918  -23.125 -12.196 1    13.152  ? 573  TYR   A CD1 1 1 
ATOM   4676  C  CD2 . TYR   A 1  573 ? 17.043  -25.349 -12.519 1    13.396  ? 573  TYR   A CD2 1 1 
ATOM   4677  C  CE1 . TYR   A 1  573 ? 18.035  -22.994 -13.579 1    13.726  ? 573  TYR   A CE1 1 1 
ATOM   4678  C  CE2 . TYR   A 1  573 ? 17.178  -25.25  -13.907 1    13.657  ? 573  TYR   A CE2 1 1 
ATOM   4679  C  CZ  . TYR   A 1  573 ? 17.637  -24.049 -14.423 1    13.939  ? 573  TYR   A CZ  1 1 
ATOM   4680  O  OH  . TYR   A 1  573 ? 17.695  -23.906 -15.783 1    15.195  ? 573  TYR   A OH  1 1 
ATOM   4681  N  N   . PHE   A 1  574 ? 19.328  -22.486 -8.911  1    14.62   ? 574  PHE   A N   1 1 
ATOM   4682  C  CA  . PHE   A 1  574 ? 20.114  -21.289 -9.116  1    15.556  ? 574  PHE   A CA  1 1 
ATOM   4683  C  C   . PHE   A 1  574 ? 21.3    -21.16  -8.142  1    16.709  ? 574  PHE   A C   1 1 
ATOM   4684  O  O   . PHE   A 1  574 ? 22.094  -20.263 -8.347  1    17.002  ? 574  PHE   A O   1 1 
ATOM   4685  C  CB  . PHE   A 1  574 ? 19.308  -19.98  -9.023  1    14.762  ? 574  PHE   A CB  1 1 
ATOM   4686  C  CG  . PHE   A 1  574 ? 18.495  -19.824 -10.288 1    14.523  ? 574  PHE   A CG  1 1 
ATOM   4687  C  CD1 . PHE   A 1  574 ? 19.139  -19.451 -11.479 1    15.109  ? 574  PHE   A CD1 1 1 
ATOM   4688  C  CD2 . PHE   A 1  574 ? 17.106  -20.001 -10.273 1    14.113  ? 574  PHE   A CD2 1 1 
ATOM   4689  C  CE1 . PHE   A 1  574 ? 18.402  -19.29  -12.654 1    14.913  ? 574  PHE   A CE1 1 1 
ATOM   4690  C  CE2 . PHE   A 1  574 ? 16.356  -19.889 -11.456 1    13.435  ? 574  PHE   A CE2 1 1 
ATOM   4691  C  CZ  . PHE   A 1  574 ? 16.983  -19.452 -12.632 1    13.342  ? 574  PHE   A CZ  1 1 
ATOM   4692  N  N   . GLN   A 1  575 ? 21.467  -22.084 -7.191  1    17.302  ? 575  GLN   A N   1 1 
ATOM   4693  C  CA  . GLN   A 1  575 ? 22.393  -21.914 -6.077  1    19.772  ? 575  GLN   A CA  1 1 
ATOM   4694  C  C   . GLN   A 1  575 ? 23.815  -21.449 -6.473  1    18.745  ? 575  GLN   A C   1 1 
ATOM   4695  O  O   . GLN   A 1  575 ? 24.387  -20.54  -5.829  1    18.423  ? 575  GLN   A O   1 1 
ATOM   4696  C  CB  . GLN   A 1  575 ? 22.473  -23.278 -5.395  1    25.233  ? 575  GLN   A CB  1 1 
ATOM   4697  C  CG  . GLN   A 1  575 ? 23.351  -23.3   -4.148  1    36.251  ? 575  GLN   A CG  1 1 
ATOM   4698  C  CD  . GLN   A 1  575 ? 23.276  -24.642 -3.438  1    46.097  ? 575  GLN   A CD  1 1 
ATOM   4699  O  OE1 . GLN   A 1  575 ? 22.674  -25.599 -3.947  1    56.613  ? 575  GLN   A OE1 1 1 
ATOM   4700  N  NE2 . GLN   A 1  575 ? 23.827  -24.716 -2.23   1    56.291  ? 575  GLN   A NE2 1 1 
ATOM   4701  N  N   . LEU   A 1  576 ? 24.415  -22.049 -7.516  1    18.786  ? 576  LEU   A N   1 1 
ATOM   4702  C  CA  . LEU   A 1  576 ? 25.789  -21.67  -7.951  1    19.906  ? 576  LEU   A CA  1 1 
ATOM   4703  C  C   . LEU   A 1  576 ? 25.896  -20.205 -8.394  1    19.407  ? 576  LEU   A C   1 1 
ATOM   4704  O  O   . LEU   A 1  576 ? 26.802  -19.52  -7.972  1    19.536  ? 576  LEU   A O   1 1 
ATOM   4705  C  CB  . LEU   A 1  576 ? 26.248  -22.549 -9.109  1    20.026  ? 576  LEU   A CB  1 1 
ATOM   4706  C  CG  . LEU   A 1  576 ? 26.493  -24.014 -8.753  1    22.1    ? 576  LEU   A CG  1 1 
ATOM   4707  C  CD1 . LEU   A 1  576 ? 26.712  -24.785 -10.06  1    21.738  ? 576  LEU   A CD1 1 1 
ATOM   4708  C  CD2 . LEU   A 1  576 ? 27.713  -24.081 -7.844  1    23.741  ? 576  LEU   A CD2 1 1 
ATOM   4709  N  N   . VAL   A 1  577 ? 24.907  -19.698 -9.17   1    18.53   ? 577  VAL   A N   1 1 
ATOM   4710  C  CA  . VAL   A 1  577 ? 24.976  -18.306 -9.598  1    18.276  ? 577  VAL   A CA  1 1 
ATOM   4711  C  C   . VAL   A 1  577 ? 24.486  -17.358 -8.481  1    18.504  ? 577  VAL   A C   1 1 
ATOM   4712  O  O   . VAL   A 1  577 ? 24.927  -16.23  -8.442  1    18.836  ? 577  VAL   A O   1 1 
ATOM   4713  C  CB  . VAL   A 1  577 ? 24.247  -18.09  -10.94  1    17.482  ? 577  VAL   A CB  1 1 
ATOM   4714  C  CG1 . VAL   A 1  577 ? 22.706  -17.936 -10.776 1    16.181  ? 577  VAL   A CG1 1 1 
ATOM   4715  C  CG2 . VAL   A 1  577 ? 24.767  -16.895 -11.737 1    17.675  ? 577  VAL   A CG2 1 1 
ATOM   4716  N  N   . THR   A 1  578 ? 23.571  -17.799 -7.587  1    18.268  ? 578  THR   A N   1 1 
ATOM   4717  C  CA  . THR   A 1  578 ? 23.208  -16.987 -6.441  1    18.543  ? 578  THR   A CA  1 1 
ATOM   4718  C  C   . THR   A 1  578 ? 24.48   -16.636 -5.66   1    19.828  ? 578  THR   A C   1 1 
ATOM   4719  O  O   . THR   A 1  578 ? 24.719  -15.48  -5.297  1    19.845  ? 578  THR   A O   1 1 
ATOM   4720  C  CB  . THR   A 1  578 ? 22.187  -17.735 -5.579  1    18.877  ? 578  THR   A CB  1 1 
ATOM   4721  O  OG1 . THR   A 1  578 ? 21.003  -17.948 -6.35   1    19.048  ? 578  THR   A OG1 1 1 
ATOM   4722  C  CG2 . THR   A 1  578 ? 21.809  -16.968 -4.325  1    19.481  ? 578  THR   A CG2 1 1 
ATOM   4723  N  N   . GLN   A 1  579 ? 25.259  -17.665 -5.366  1    20.691  ? 579  GLN   A N   1 1 
ATOM   4724  C  CA  . GLN   A 1  579 ? 26.48   -17.457 -4.613  1    22.686  ? 579  GLN   A CA  1 1 
ATOM   4725  C  C   . GLN   A 1  579 ? 27.486  -16.624 -5.428  1    22.02   ? 579  GLN   A C   1 1 
ATOM   4726  O  O   . GLN   A 1  579 ? 28.121  -15.727 -4.895  1    22.686  ? 579  GLN   A O   1 1 
ATOM   4727  C  CB  . GLN   A 1  579 ? 26.951  -18.851 -4.174  1    25.171  ? 579  GLN   A CB  1 1 
ATOM   4728  C  CG  . GLN   A 1  579 ? 28.357  -18.82  -3.588  1    32.616  ? 579  GLN   A CG  1 1 
ATOM   4729  C  CD  . GLN   A 1  579 ? 28.414  -18.244 -2.191  1    40.125  ? 579  GLN   A CD  1 1 
ATOM   4730  O  OE1 . GLN   A 1  579 ? 29.499  -17.919 -1.687  1    51.73   ? 579  GLN   A OE1 1 1 
ATOM   4731  N  NE2 . GLN   A 1  579 ? 27.271  -18.142 -1.525  1    37.519  ? 579  GLN   A NE2 1 1 
ATOM   4732  N  N   . TRP   A 1  580 ? 27.633  -16.868 -6.732  1    20.407  ? 580  TRP   A N   1 1 
ATOM   4733  C  CA  . TRP   A 1  580 ? 28.618  -16.125 -7.522  1    20.616  ? 580  TRP   A CA  1 1 
ATOM   4734  C  C   . TRP   A 1  580 ? 28.272  -14.636 -7.599  1    20.615  ? 580  TRP   A C   1 1 
ATOM   4735  O  O   . TRP   A 1  580 ? 29.153  -13.791 -7.531  1    20.272  ? 580  TRP   A O   1 1 
ATOM   4736  C  CB  . TRP   A 1  580 ? 28.715  -16.739 -8.931  1    21.306  ? 580  TRP   A CB  1 1 
ATOM   4737  C  CG  . TRP   A 1  580 ? 29.771  -16.131 -9.832  1    23.669  ? 580  TRP   A CG  1 1 
ATOM   4738  C  CD1 . TRP   A 1  580 ? 31.08   -16.485 -9.902  1    24.847  ? 580  TRP   A CD1 1 1 
ATOM   4739  C  CD2 . TRP   A 1  580 ? 29.588  -15.082 -10.804 1    23.537  ? 580  TRP   A CD2 1 1 
ATOM   4740  N  NE1 . TRP   A 1  580 ? 31.724  -15.714 -10.838 1    25.707  ? 580  TRP   A NE1 1 1 
ATOM   4741  C  CE2 . TRP   A 1  580 ? 30.845  -14.852 -11.409 1    24.99   ? 580  TRP   A CE2 1 1 
ATOM   4742  C  CE3 . TRP   A 1  580 ? 28.491  -14.313 -11.224 1    23.679  ? 580  TRP   A CE3 1 1 
ATOM   4743  C  CZ2 . TRP   A 1  580 ? 31.016  -13.898 -12.416 1    25.043  ? 580  TRP   A CZ2 1 1 
ATOM   4744  C  CZ3 . TRP   A 1  580 ? 28.638  -13.406 -12.252 1    23.425  ? 580  TRP   A CZ3 1 1 
ATOM   4745  C  CH2 . TRP   A 1  580 ? 29.897  -13.157 -12.793 1    24.415  ? 580  TRP   A CH2 1 1 
ATOM   4746  N  N   . LEU   A 1  581 ? 26.968  -14.304 -7.821  1    19.253  ? 581  LEU   A N   1 1 
ATOM   4747  C  CA  . LEU   A 1  581 ? 26.548  -12.919 -7.939  1    19.693  ? 581  LEU   A CA  1 1 
ATOM   4748  C  C   . LEU   A 1  581 ? 26.747  -12.156 -6.618  1    21.509  ? 581  LEU   A C   1 1 
ATOM   4749  O  O   . LEU   A 1  581 ? 27.155  -10.991 -6.642  1    21.919  ? 581  LEU   A O   1 1 
ATOM   4750  C  CB  . LEU   A 1  581 ? 25.097  -12.821 -8.421  1    19.957  ? 581  LEU   A CB  1 1 
ATOM   4751  C  CG  . LEU   A 1  581 ? 24.882  -13.131 -9.914  1    19.745  ? 581  LEU   A CG  1 1 
ATOM   4752  C  CD1 . LEU   A 1  581 ? 23.401  -13.46  -10.12  1    18.998  ? 581  LEU   A CD1 1 1 
ATOM   4753  C  CD2 . LEU   A 1  581 ? 25.231  -11.831 -10.634 1    20.251  ? 581  LEU   A CD2 1 1 
ATOM   4754  N  N   . GLN   A 1  582 ? 26.474  -12.806 -5.478  1    21.026  ? 582  GLN   A N   1 1 
ATOM   4755  C  CA  . GLN   A 1  582 ? 26.651  -12.164 -4.191  1    24.225  ? 582  GLN   A CA  1 1 
ATOM   4756  C  C   . GLN   A 1  582 ? 28.137  -11.87  -3.978  1    25.535  ? 582  GLN   A C   1 1 
ATOM   4757  O  O   . GLN   A 1  582 ? 28.51   -10.742 -3.62   1    25.45   ? 582  GLN   A O   1 1 
ATOM   4758  C  CB  . GLN   A 1  582 ? 26.058  -13.143 -3.183  1    28.965  ? 582  GLN   A CB  1 1 
ATOM   4759  C  CG  . GLN   A 1  582 ? 26.185  -12.764 -1.714  1    39.45   ? 582  GLN   A CG  1 1 
ATOM   4760  C  CD  . GLN   A 1  582 ? 25.495  -13.794 -0.835  1    46.36   ? 582  GLN   A CD  1 1 
ATOM   4761  O  OE1 . GLN   A 1  582 ? 24.29   -14.051 -0.975  1    48.565  ? 582  GLN   A OE1 1 1 
ATOM   4762  N  NE2 . GLN   A 1  582 ? 26.266  -14.448 0.025   1    45.68   ? 582  GLN   A NE2 1 1 
ATOM   4763  N  N   . GLU   A 1  583 ? 28.983  -12.837 -4.318  1    24.514  ? 583  GLU   A N   1 1 
ATOM   4764  C  CA  . GLU   A 1  583 ? 30.429  -12.622 -4.172  1    26.812  ? 583  GLU   A CA  1 1 
ATOM   4765  C  C   . GLU   A 1  583 ? 30.934  -11.538 -5.138  1    25.873  ? 583  GLU   A C   1 1 
ATOM   4766  O  O   . GLU   A 1  583 ? 31.692  -10.647 -4.761  1    26.829  ? 583  GLU   A O   1 1 
ATOM   4767  C  CB  . GLU   A 1  583 ? 31.242  -13.873 -4.491  1    29.738  ? 583  GLU   A CB  1 1 
ATOM   4768  C  CG  . GLU   A 1  583 ? 31.115  -15.026 -3.503  1    36.863  ? 583  GLU   A CG  1 1 
ATOM   4769  C  CD  . GLU   A 1  583 ? 31.532  -16.381 -4.114  1    42.532  ? 583  GLU   A CD  1 1 
ATOM   4770  O  OE1 . GLU   A 1  583 ? 31.817  -16.541 -5.342  1    45.763  ? 583  GLU   A OE1 1 1 
ATOM   4771  O  OE2 . GLU   A 1  583 ? 31.535  -17.328 -3.33   1    42.765  ? 583  GLU   A OE2 1 1 
ATOM   4772  N  N   . GLN   A 1  584 ? 30.456  -11.538 -6.387  1    24.782  ? 584  GLN   A N   1 1 
ATOM   4773  C  CA  . GLN   A 1  584 ? 30.866  -10.495 -7.314  1    25.142  ? 584  GLN   A CA  1 1 
ATOM   4774  C  C   . GLN   A 1  584 ? 30.394  -9.106  -6.848  1    24.525  ? 584  GLN   A C   1 1 
ATOM   4775  O  O   . GLN   A 1  584 ? 31.098  -8.122  -7.028  1    23.586  ? 584  GLN   A O   1 1 
ATOM   4776  C  CB  . GLN   A 1  584 ? 30.338  -10.775 -8.727  1    27.018  ? 584  GLN   A CB  1 1 
ATOM   4777  C  CG  . GLN   A 1  584 ? 30.937  -12.033 -9.363  1    28.068  ? 584  GLN   A CG  1 1 
ATOM   4778  C  CD  . GLN   A 1  584 ? 32.419  -11.893 -9.602  1    33.955  ? 584  GLN   A CD  1 1 
ATOM   4779  O  OE1 . GLN   A 1  584 ? 32.858  -10.978 -10.311 1    32.685  ? 584  GLN   A OE1 1 1 
ATOM   4780  N  NE2 . GLN   A 1  584 ? 33.197  -12.741 -8.941  1    38.226  ? 584  GLN   A NE2 1 1 
ATOM   4781  N  N   . ASN   A 1  585 ? 29.14   -8.99   -6.393  1    21.864  ? 585  ASN   A N   1 1 
ATOM   4782  C  CA  . ASN   A 1  585 ? 28.652  -7.668  -6.068  1    23.087  ? 585  ASN   A CA  1 1 
ATOM   4783  C  C   . ASN   A 1  585 ? 29.454  -7.119  -4.881  1    25.024  ? 585  ASN   A C   1 1 
ATOM   4784  O  O   . ASN   A 1  585 ? 29.744  -5.934  -4.843  1    25.574  ? 585  ASN   A O   1 1 
ATOM   4785  C  CB  . ASN   A 1  585 ? 27.166  -7.75   -5.761  1    20.447  ? 585  ASN   A CB  1 1 
ATOM   4786  C  CG  . ASN   A 1  585 ? 26.328  -7.879  -7.01   1    19.822  ? 585  ASN   A CG  1 1 
ATOM   4787  O  OD1 . ASN   A 1  585 ? 26.709  -7.327  -8.041  1    20.427  ? 585  ASN   A OD1 1 1 
ATOM   4788  N  ND2 . ASN   A 1  585 ? 25.107  -8.407  -6.896  1    18.164  ? 585  ASN   A ND2 1 1 
ATOM   4789  N  N   . GLN   A 1  586 ? 29.826  -8.006  -3.941  1    27.689  ? 586  GLN   A N   1 1 
ATOM   4790  C  CA  . GLN   A 1  586 ? 30.649  -7.627  -2.797  1    33.571  ? 586  GLN   A CA  1 1 
ATOM   4791  C  C   . GLN   A 1  586 ? 32.03   -7.135  -3.226  1    34.54   ? 586  GLN   A C   1 1 
ATOM   4792  O  O   . GLN   A 1  586 ? 32.498  -6.068  -2.826  1    32.698  ? 586  GLN   A O   1 1 
ATOM   4793  C  CB  . GLN   A 1  586 ? 30.785  -8.751  -1.767  1    38.659  ? 586  GLN   A CB  1 1 
ATOM   4794  C  CG  . GLN   A 1  586 ? 29.463  -9.066  -1.078  1    49.115  ? 586  GLN   A CG  1 1 
ATOM   4795  C  CD  . GLN   A 1  586 ? 29.62   -9.994  0.106   1    59.711  ? 586  GLN   A CD  1 1 
ATOM   4796  O  OE1 . GLN   A 1  586 ? 30.721  -10.141 0.653   1    64.164  ? 586  GLN   A OE1 1 1 
ATOM   4797  N  NE2 . GLN   A 1  586 ? 28.507  -10.58  0.537   1    58.556  ? 586  GLN   A NE2 1 1 
ATOM   4798  N  N   . GLN   A 1  587 ? 32.71   -7.916  -4.05   1    35.726  ? 587  GLN   A N   1 1 
ATOM   4799  C  CA  . GLN   A 1  587 ? 34.035  -7.512  -4.476  1    37.7    ? 587  GLN   A CA  1 1 
ATOM   4800  C  C   . GLN   A 1  587 ? 33.953  -6.182  -5.212  1    37.369  ? 587  GLN   A C   1 1 
ATOM   4801  O  O   . GLN   A 1  587 ? 34.889  -5.396  -5.192  1    34.64   ? 587  GLN   A O   1 1 
ATOM   4802  C  CB  . GLN   A 1  587 ? 34.605  -8.571  -5.404  1    41.022  ? 587  GLN   A CB  1 1 
ATOM   4803  C  CG  . GLN   A 1  587 ? 35.361  -9.656  -4.652  1    54.405  ? 587  GLN   A CG  1 1 
ATOM   4804  C  CD  . GLN   A 1  587 ? 35.408  -10.934 -5.453  1    59.951  ? 587  GLN   A CD  1 1 
ATOM   4805  O  OE1 . GLN   A 1  587 ? 35.821  -10.945 -6.621  1    64.242  ? 587  GLN   A OE1 1 1 
ATOM   4806  N  NE2 . GLN   A 1  587 ? 34.931  -12.007 -4.839  1    59.716  ? 587  GLN   A NE2 1 1 
ATOM   4807  N  N   . ASN   A 1  588 ? 32.834  -5.945  -5.898  1    35.068  ? 588  ASN   A N   1 1 
ATOM   4808  C  CA  . ASN   A 1  588 ? 32.777  -4.726  -6.679  1    35.314  ? 588  ASN   A CA  1 1 
ATOM   4809  C  C   . ASN   A 1  588 ? 32.313  -3.566  -5.811  1    34.418  ? 588  ASN   A C   1 1 
ATOM   4810  O  O   . ASN   A 1  588 ? 32.213  -2.468  -6.319  1    36.418  ? 588  ASN   A O   1 1 
ATOM   4811  C  CB  . ASN   A 1  588 ? 31.853  -4.844  -7.89   1    37.165  ? 588  ASN   A CB  1 1 
ATOM   4812  C  CG  . ASN   A 1  588 ? 32.323  -5.871  -8.899  1    41.265  ? 588  ASN   A CG  1 1 
ATOM   4813  O  OD1 . ASN   A 1  588 ? 31.531  -6.33   -9.723  1    44.557  ? 588  ASN   A OD1 1 1 
ATOM   4814  N  ND2 . ASN   A 1  588 ? 33.569  -6.3    -8.832  1    40.789  ? 588  ASN   A ND2 1 1 
ATOM   4815  N  N   . GLY   A 1  589 ? 31.916  -3.822  -4.555  1    35.688  ? 589  GLY   A N   1 1 
ATOM   4816  C  CA  . GLY   A 1  589 ? 31.411  -2.79   -3.655  1    33.649  ? 589  GLY   A CA  1 1 
ATOM   4817  C  C   . GLY   A 1  589 ? 30.038  -2.253  -4.063  1    35.543  ? 589  GLY   A C   1 1 
ATOM   4818  O  O   . GLY   A 1  589 ? 29.773  -1.056  -3.949  1    34.871  ? 589  GLY   A O   1 1 
ATOM   4819  N  N   . GLU   A 1  590 ? 29.161  -3.131  -4.545  1    30.258  ? 590  GLU   A N   1 1 
ATOM   4820  C  CA  . GLU   A 1  590 ? 27.875  -2.645  -5.022  1    30.749  ? 590  GLU   A CA  1 1 
ATOM   4821  C  C   . GLU   A 1  590 ? 26.973  -2.289  -3.847  1    30.418  ? 590  GLU   A C   1 1 
ATOM   4822  O  O   . GLU   A 1  590 ? 27.152  -2.754  -2.729  1    30.914  ? 590  GLU   A O   1 1 
ATOM   4823  C  CB  . GLU   A 1  590 ? 27.103  -3.768  -5.69   1    28.789  ? 590  GLU   A CB  1 1 
ATOM   4824  C  CG  . GLU   A 1  590 ? 27.621  -4.052  -7.081  1    29.115  ? 590  GLU   A CG  1 1 
ATOM   4825  C  CD  . GLU   A 1  590 ? 27.924  -2.924  -8.053  1    32.19   ? 590  GLU   A CD  1 1 
ATOM   4826  O  OE1 . GLU   A 1  590 ? 27.557  -1.737  -7.963  1    30.905  ? 590  GLU   A OE1 1 1 
ATOM   4827  O  OE2 . GLU   A 1  590 ? 28.642  -3.325  -8.972  1    33.966  ? 590  GLU   A OE2 1 1 
ATOM   4828  N  N   . VAL   A 1  591 ? 26.035  -1.383  -4.093  1    32.585  ? 591  VAL   A N   1 1 
ATOM   4829  C  CA  . VAL   A 1  591 ? 24.948  -1.222  -3.147  1    34.059  ? 591  VAL   A CA  1 1 
ATOM   4830  C  C   . VAL   A 1  591 ? 23.782  -2.093  -3.618  1    30.614  ? 591  VAL   A C   1 1 
ATOM   4831  O  O   . VAL   A 1  591 ? 23.356  -2.021  -4.769  1    32.792  ? 591  VAL   A O   1 1 
ATOM   4832  C  CB  . VAL   A 1  591 ? 24.6    0.271   -2.948  1    35.881  ? 591  VAL   A CB  1 1 
ATOM   4833  C  CG1 . VAL   A 1  591 ? 23.615  0.45    -1.806  1    38.254  ? 591  VAL   A CG1 1 1 
ATOM   4834  C  CG2 . VAL   A 1  591 ? 25.86   1.06    -2.59   1    40.074  ? 591  VAL   A CG2 1 1 
ATOM   4835  N  N   . LEU   A 1  592 ? 23.273  -2.962  -2.754  1    27.635  ? 592  LEU   A N   1 1 
ATOM   4836  C  CA  . LEU   A 1  592 ? 22.131  -3.752  -3.181  1    28.545  ? 592  LEU   A CA  1 1 
ATOM   4837  C  C   . LEU   A 1  592 ? 20.915  -2.848  -3.014  1    28.561  ? 592  LEU   A C   1 1 
ATOM   4838  O  O   . LEU   A 1  592 ? 20.867  -2.063  -2.066  1    31.072  ? 592  LEU   A O   1 1 
ATOM   4839  C  CB  . LEU   A 1  592 ? 22      -5.042  -2.377  1    29.149  ? 592  LEU   A CB  1 1 
ATOM   4840  C  CG  . LEU   A 1  592 ? 23.18   -6.001  -2.561  1    35.766  ? 592  LEU   A CG  1 1 
ATOM   4841  C  CD1 . LEU   A 1  592 ? 22.841  -7.335  -1.956  1    35.744  ? 592  LEU   A CD1 1 1 
ATOM   4842  C  CD2 . LEU   A 1  592 ? 23.544  -6.164  -4.054  1    34.16   ? 592  LEU   A CD2 1 1 
ATOM   4843  N  N   . GLY   A 1  593 ? 19.988  -2.889  -3.976  1    24.963  ? 593  GLY   A N   1 1 
ATOM   4844  C  CA  . GLY   A 1  593 ? 18.817  -2.023  -3.856  1    22.904  ? 593  GLY   A CA  1 1 
ATOM   4845  C  C   . GLY   A 1  593 ? 19.072  -0.653  -4.494  1    20.758  ? 593  GLY   A C   1 1 
ATOM   4846  O  O   . GLY   A 1  593 ? 20.098  -0.41   -5.162  1    19.556  ? 593  GLY   A O   1 1 
ATOM   4847  N  N   . TRP   A 1  594 ? 18.08   0.232   -4.351  1    18.782  ? 594  TRP   A N   1 1 
ATOM   4848  C  CA  . TRP   A 1  594 ? 18.119  1.501   -5.062  1    18.449  ? 594  TRP   A CA  1 1 
ATOM   4849  C  C   . TRP   A 1  594 ? 17.753  2.61    -4.075  1    20.14   ? 594  TRP   A C   1 1 
ATOM   4850  O  O   . TRP   A 1  594 ? 16.64   3.174   -4.155  1    21.68   ? 594  TRP   A O   1 1 
ATOM   4851  C  CB  . TRP   A 1  594 ? 17.156  1.476   -6.283  1    18.084  ? 594  TRP   A CB  1 1 
ATOM   4852  C  CG  . TRP   A 1  594 ? 15.906  0.656   -6.057  1    17.027  ? 594  TRP   A CG  1 1 
ATOM   4853  C  CD1 . TRP   A 1  594 ? 14.658  1.097   -5.681  1    16.807  ? 594  TRP   A CD1 1 1 
ATOM   4854  C  CD2 . TRP   A 1  594 ? 15.797  -0.78   -6.194  1    17.344  ? 594  TRP   A CD2 1 1 
ATOM   4855  N  NE1 . TRP   A 1  594 ? 13.794  0.036   -5.589  1    16.724  ? 594  TRP   A NE1 1 1 
ATOM   4856  C  CE2 . TRP   A 1  594 ? 14.47   -1.129  -5.866  1    16.482  ? 594  TRP   A CE2 1 1 
ATOM   4857  C  CE3 . TRP   A 1  594 ? 16.721  -1.803  -6.546  1    18.838  ? 594  TRP   A CE3 1 1 
ATOM   4858  C  CZ2 . TRP   A 1  594 ? 14.018  -2.448  -5.891  1    16.291  ? 594  TRP   A CZ2 1 1 
ATOM   4859  C  CZ3 . TRP   A 1  594 ? 16.276  -3.109  -6.587  1    18.985  ? 594  TRP   A CZ3 1 1 
ATOM   4860  C  CH2 . TRP   A 1  594 ? 14.943  -3.431  -6.243  1    16.844  ? 594  TRP   A CH2 1 1 
ATOM   4861  N  N   . PRO   A 1  595 ? 18.651  2.971   -3.122  1    21.203  ? 595  PRO   A N   1 1 
ATOM   4862  C  CA  . PRO   A 1  595 ? 18.334  3.99    -2.099  1    21.822  ? 595  PRO   A CA  1 1 
ATOM   4863  C  C   . PRO   A 1  595 ? 18.035  5.393   -2.642  1    23.915  ? 595  PRO   A C   1 1 
ATOM   4864  O  O   . PRO   A 1  595 ? 17.414  6.198   -1.954  1    22.891  ? 595  PRO   A O   1 1 
ATOM   4865  C  CB  . PRO   A 1  595 ? 19.54   3.986   -1.142  1    21.49   ? 595  PRO   A CB  1 1 
ATOM   4866  C  CG  . PRO   A 1  595 ? 20.669  3.406   -1.985  1    21.575  ? 595  PRO   A CG  1 1 
ATOM   4867  C  CD  . PRO   A 1  595 ? 20.005  2.413   -2.946  1    19.793  ? 595  PRO   A CD  1 1 
ATOM   4868  N  N   . GLU   A 1  596 ? 18.516  5.701   -3.861  1    23.421  ? 596  GLU   A N   1 1 
ATOM   4869  C  CA  . GLU   A 1  596 ? 18.151  6.969   -4.485  1    23.739  ? 596  GLU   A CA  1 1 
ATOM   4870  C  C   . GLU   A 1  596 ? 16.87   6.783   -5.284  1    21.364  ? 596  GLU   A C   1 1 
ATOM   4871  O  O   . GLU   A 1  596 ? 16.864  6.927   -6.511  1    22.321  ? 596  GLU   A O   1 1 
ATOM   4872  C  CB  . GLU   A 1  596 ? 19.3    7.487   -5.359  1    25.746  ? 596  GLU   A CB  1 1 
ATOM   4873  C  CG  . GLU   A 1  596 ? 20.559  7.792   -4.538  1    28.97   ? 596  GLU   A CG  1 1 
ATOM   4874  C  CD  . GLU   A 1  596 ? 21.795  8.486   -5.132  1    34.717  ? 596  GLU   A CD  1 1 
ATOM   4875  O  OE1 . GLU   A 1  596 ? 21.695  9.088   -6.23   1    35.043  ? 596  GLU   A OE1 1 1 
ATOM   4876  O  OE2 . GLU   A 1  596 ? 22.887  8.476   -4.488  1    36.497  ? 596  GLU   A OE2 1 1 
ATOM   4877  N  N   . TYR   A 1  597 ? 15.802  6.447   -4.575  1    20.047  ? 597  TYR   A N   1 1 
ATOM   4878  C  CA  . TYR   A 1  597 ? 14.526  6.03    -5.136  1    19.596  ? 597  TYR   A CA  1 1 
ATOM   4879  C  C   . TYR   A 1  597 ? 13.884  7.127   -5.992  1    19.625  ? 597  TYR   A C   1 1 
ATOM   4880  O  O   . TYR   A 1  597 ? 12.979  6.845   -6.762  1    21.073  ? 597  TYR   A O   1 1 
ATOM   4881  C  CB  . TYR   A 1  597 ? 13.517  5.585   -4.059  1    18.192  ? 597  TYR   A CB  1 1 
ATOM   4882  C  CG  . TYR   A 1  597 ? 13.25   6.669   -3.02   1    18.868  ? 597  TYR   A CG  1 1 
ATOM   4883  C  CD1 . TYR   A 1  597 ? 12.258  7.629   -3.254  1    18.504  ? 597  TYR   A CD1 1 1 
ATOM   4884  C  CD2 . TYR   A 1  597 ? 13.982  6.728   -1.812  1    19.025  ? 597  TYR   A CD2 1 1 
ATOM   4885  C  CE1 . TYR   A 1  597 ? 12.007  8.643   -2.328  1    19.41   ? 597  TYR   A CE1 1 1 
ATOM   4886  C  CE2 . TYR   A 1  597 ? 13.75   7.765   -0.905  1    19.933  ? 597  TYR   A CE2 1 1 
ATOM   4887  C  CZ  . TYR   A 1  597 ? 12.752  8.711   -1.159  1    19.669  ? 597  TYR   A CZ  1 1 
ATOM   4888  O  OH  . TYR   A 1  597 ? 12.519  9.757   -0.264  1    19.986  ? 597  TYR   A OH  1 1 
ATOM   4889  N  N   . GLN   A 1  598 ? 14.252  8.38    -5.789  1    20.736  ? 598  GLN   A N   1 1 
ATOM   4890  C  CA  . GLN   A 1  598 ? 13.622  9.473   -6.498  1    23.483  ? 598  GLN   A CA  1 1 
ATOM   4891  C  C   . GLN   A 1  598 ? 14.353  9.745   -7.808  1    24.518  ? 598  GLN   A C   1 1 
ATOM   4892  O  O   . GLN   A 1  598 ? 13.923  10.573  -8.574  1    25.771  ? 598  GLN   A O   1 1 
ATOM   4893  C  CB  . GLN   A 1  598 ? 13.854  10.793  -5.748  1    24.874  ? 598  GLN   A CB  1 1 
ATOM   4894  C  CG  . GLN   A 1  598 ? 12.593  11.359  -5.124  1    26.658  ? 598  GLN   A CG  1 1 
ATOM   4895  C  CD  . GLN   A 1  598 ? 12.791  12.762  -4.561  1    30.96   ? 598  GLN   A CD  1 1 
ATOM   4896  O  OE1 . GLN   A 1  598 ? 12.922  12.957  -3.347  1    29.225  ? 598  GLN   A OE1 1 1 
ATOM   4897  N  NE2 . GLN   A 1  598 ? 12.874  13.763  -5.445  1    33.131  ? 598  GLN   A NE2 1 1 
ATOM   4898  N  N   . TRP   A 1  599 ? 15.457  9.049   -8.092  1    24.592  ? 599  TRP   A N   1 1 
ATOM   4899  C  CA  . TRP   A 1  599 ? 16.263  9.449   -9.241  1    25.148  ? 599  TRP   A CA  1 1 
ATOM   4900  C  C   . TRP   A 1  599 ? 15.585  9.007   -10.544 1    24.38   ? 599  TRP   A C   1 1 
ATOM   4901  O  O   . TRP   A 1  599 ? 15.049  7.893   -10.652 1    23.59   ? 599  TRP   A O   1 1 
ATOM   4902  C  CB  . TRP   A 1  599 ? 17.649  8.813   -9.101  1    24.069  ? 599  TRP   A CB  1 1 
ATOM   4903  C  CG  . TRP   A 1  599 ? 18.533  9.059   -10.294 1    24.262  ? 599  TRP   A CG  1 1 
ATOM   4904  C  CD1 . TRP   A 1  599 ? 19.346  10.127  -10.506 1    24.326  ? 599  TRP   A CD1 1 1 
ATOM   4905  C  CD2 . TRP   A 1  599 ? 18.653  8.211   -11.453 1    23.511  ? 599  TRP   A CD2 1 1 
ATOM   4906  N  NE1 . TRP   A 1  599 ? 19.988  9.985   -11.702 1    25.32   ? 599  TRP   A NE1 1 1 
ATOM   4907  C  CE2 . TRP   A 1  599 ? 19.565  8.843   -12.326 1    24.463  ? 599  TRP   A CE2 1 1 
ATOM   4908  C  CE3 . TRP   A 1  599 ? 18.042  7.017   -11.844 1    22.07   ? 599  TRP   A CE3 1 1 
ATOM   4909  C  CZ2 . TRP   A 1  599 ? 19.936  8.299   -13.559 1    23.78   ? 599  TRP   A CZ2 1 1 
ATOM   4910  C  CZ3 . TRP   A 1  599 ? 18.411  6.477   -13.054 1    21.13   ? 599  TRP   A CZ3 1 1 
ATOM   4911  C  CH2 . TRP   A 1  599 ? 19.313  7.125   -13.905 1    22.494  ? 599  TRP   A CH2 1 1 
ATOM   4912  N  N   . HIS   A 1  600 ? 15.659  9.88    -11.564 1    27.364  ? 600  HIS   A N   1 1 
ATOM   4913  C  CA  . HIS   A 1  600 ? 15.276  9.498   -12.924 1    25.513  ? 600  HIS   A CA  1 1 
ATOM   4914  C  C   . HIS   A 1  600 ? 16.355  10.006  -13.882 1    25.359  ? 600  HIS   A C   1 1 
ATOM   4915  O  O   . HIS   A 1  600 ? 17.022  10.989  -13.592 1    25.344  ? 600  HIS   A O   1 1 
ATOM   4916  C  CB  . HIS   A 1  600 ? 14.003  10.228  -13.35  1    26.17   ? 600  HIS   A CB  1 1 
ATOM   4917  C  CG  . HIS   A 1  600 ? 12.795  9.718   -12.619 1    27.584  ? 600  HIS   A CG  1 1 
ATOM   4918  N  ND1 . HIS   A 1  600 ? 12.561  9.981   -11.277 1    27.271  ? 600  HIS   A ND1 1 1 
ATOM   4919  C  CD2 . HIS   A 1  600 ? 11.792  8.94    -13.039 1    24.417  ? 600  HIS   A CD2 1 1 
ATOM   4920  C  CE1 . HIS   A 1  600 ? 11.429  9.394   -10.902 1    26.106  ? 600  HIS   A CE1 1 1 
ATOM   4921  N  NE2 . HIS   A 1  600 ? 10.976  8.737   -11.964 1    26.642  ? 600  HIS   A NE2 1 1 
ATOM   4922  N  N   . PRO   A 1  601 ? 16.582  9.364   -15.053 1    23.985  ? 601  PRO   A N   1 1 
ATOM   4923  C  CA  . PRO   A 1  601 ? 17.695  9.802   -15.928 1    24.808  ? 601  PRO   A CA  1 1 
ATOM   4924  C  C   . PRO   A 1  601 ? 17.321  11.122  -16.618 1    26.979  ? 601  PRO   A C   1 1 
ATOM   4925  O  O   . PRO   A 1  601 ? 16.141  11.406  -16.765 1    26.612  ? 601  PRO   A O   1 1 
ATOM   4926  C  CB  . PRO   A 1  601 ? 17.801  8.601   -16.894 1    23.211  ? 601  PRO   A CB  1 1 
ATOM   4927  C  CG  . PRO   A 1  601 ? 16.35   8.124   -17.024 1    22.697  ? 601  PRO   A CG  1 1 
ATOM   4928  C  CD  . PRO   A 1  601 ? 15.883  8.155   -15.533 1    21.94   ? 601  PRO   A CD  1 1 
ATOM   4929  N  N   . PRO   A 1  602 ? 18.254  11.982  -17.07  1    29.051  ? 602  PRO   A N   1 1 
ATOM   4930  C  CA  . PRO   A 1  602 ? 17.86   13.165  -17.862 1    31.013  ? 602  PRO   A CA  1 1 
ATOM   4931  C  C   . PRO   A 1  602 ? 17.455  12.709  -19.27  1    32.807  ? 602  PRO   A C   1 1 
ATOM   4932  O  O   . PRO   A 1  602 ? 17.631  11.532  -19.636 1    33.256  ? 602  PRO   A O   1 1 
ATOM   4933  C  CB  . PRO   A 1  602 ? 19.09   14.059  -17.826 1    30.873  ? 602  PRO   A CB  1 1 
ATOM   4934  C  CG  . PRO   A 1  602 ? 20.26   13.082  -17.703 1    32.383  ? 602  PRO   A CG  1 1 
ATOM   4935  C  CD  . PRO   A 1  602 ? 19.716  11.838  -16.923 1    30.332  ? 602  PRO   A CD  1 1 
ATOM   4936  N  N   . LEU   A 1  603 ? 16.864  13.622  -20.051 1    34.103  ? 603  LEU   A N   1 1 
ATOM   4937  C  CA  . LEU   A 1  603 ? 16.608  13.381  -21.47  1    36.265  ? 603  LEU   A CA  1 1 
ATOM   4938  C  C   . LEU   A 1  603 ? 17.921  13.479  -22.249 1    35.627  ? 603  LEU   A C   1 1 
ATOM   4939  O  O   . LEU   A 1  603 ? 18.779  14.285  -21.905 1    33.664  ? 603  LEU   A O   1 1 
ATOM   4940  C  CB  . LEU   A 1  603 ? 15.637  14.437  -22.009 1    40.052  ? 603  LEU   A CB  1 1 
ATOM   4941  C  CG  . LEU   A 1  603 ? 14.16   14.294  -21.626 1    40.272  ? 603  LEU   A CG  1 1 
ATOM   4942  C  CD1 . LEU   A 1  603 ? 13.404  15.338  -22.427 1    40.889  ? 603  LEU   A CD1 1 1 
ATOM   4943  C  CD2 . LEU   A 1  603 ? 13.598  12.915  -21.904 1    36.958  ? 603  LEU   A CD2 1 1 
ATOM   4944  N  N   . PRO   A 1  604 ? 18.099  12.688  -23.326 1    37.151  ? 604  PRO   A N   1 1 
ATOM   4945  C  CA  . PRO   A 1  604 ? 19.148  12.969  -24.328 1    39.631  ? 604  PRO   A CA  1 1 
ATOM   4946  C  C   . PRO   A 1  604 ? 19.138  14.404  -24.867 1    44.953  ? 604  PRO   A C   1 1 
ATOM   4947  O  O   . PRO   A 1  604 ? 18.076  14.97   -25.093 1    44.545  ? 604  PRO   A O   1 1 
ATOM   4948  C  CB  . PRO   A 1  604 ? 18.852  11.964  -25.442 1    39.17   ? 604  PRO   A CB  1 1 
ATOM   4949  C  CG  . PRO   A 1  604 ? 18.016  10.874  -24.768 1    35.33   ? 604  PRO   A CG  1 1 
ATOM   4950  C  CD  . PRO   A 1  604 ? 17.251  11.53   -23.656 1    33.451  ? 604  PRO   A CD  1 1 
ATOM   4951  N  N   . ASP   A 1  605 ? 20.316  15.02   -25.088 1    51.615  ? 605  ASP   A N   1 1 
ATOM   4952  C  CA  . ASP   A 1  605 ? 20.328  16.366  -25.657 1    55.715  ? 605  ASP   A CA  1 1 
ATOM   4953  C  C   . ASP   A 1  605 ? 19.623  16.33   -27.013 1    57.188  ? 605  ASP   A C   1 1 
ATOM   4954  O  O   . ASP   A 1  605 ? 19.869  15.435  -27.825 1    58.037  ? 605  ASP   A O   1 1 
ATOM   4955  C  CB  . ASP   A 1  605 ? 21.722  16.976  -25.705 1    63.848  ? 605  ASP   A CB  1 1 
ATOM   4956  C  CG  . ASP   A 1  605 ? 22.449  17.107  -24.371 1    69.858  ? 605  ASP   A CG  1 1 
ATOM   4957  O  OD1 . ASP   A 1  605 ? 22.048  17.955  -23.545 1    70.986  ? 605  ASP   A OD1 1 1 
ATOM   4958  O  OD2 . ASP   A 1  605 ? 23.409  16.344  -24.153 1    75.604  ? 605  ASP   A OD2 1 1 
ATOM   4959  N  N   . ASN   A 1  606 ? 18.693  17.262  -27.223 1    58.05   ? 606  ASN   A N   1 1 
ATOM   4960  C  CA  . ASN   A 1  606 ? 17.912  17.292  -28.457 1    69.895  ? 606  ASN   A CA  1 1 
ATOM   4961  C  C   . ASN   A 1  606 ? 17.283  15.921  -28.732 1    65.291  ? 606  ASN   A C   1 1 
ATOM   4962  O  O   . ASN   A 1  606 ? 17.597  15.254  -29.718 1    68.418  ? 606  ASN   A O   1 1 
ATOM   4963  C  CB  . ASN   A 1  606 ? 18.716  17.786  -29.663 1    82.107  ? 606  ASN   A CB  1 1 
ATOM   4964  C  CG  . ASN   A 1  606 ? 19.25   19.199  -29.537 1    82.714  ? 606  ASN   A CG  1 1 
ATOM   4965  O  OD1 . ASN   A 1  606 ? 18.503  20.177  -29.695 1    82.603  ? 606  ASN   A OD1 1 1 
ATOM   4966  N  ND2 . ASN   A 1  606 ? 20.554  19.323  -29.318 1    77.06   ? 606  ASN   A ND2 1 1 
ATOM   4967  N  N   . TYR   A 1  607 ? 16.432  15.484  -27.81  1    57.399  ? 607  TYR   A N   1 1 
ATOM   4968  C  CA  . TYR   A 1  607 ? 15.514  14.391  -28.065 1    54.05   ? 607  TYR   A CA  1 1 
ATOM   4969  C  C   . TYR   A 1  607 ? 14.155  15.04   -28.318 1    51.784  ? 607  TYR   A C   1 1 
ATOM   4970  O  O   . TYR   A 1  607 ? 13.895  16.095  -27.752 1    52.743  ? 607  TYR   A O   1 1 
ATOM   4971  C  CB  . TYR   A 1  607 ? 15.55   13.457  -26.846 1    52.926  ? 607  TYR   A CB  1 1 
ATOM   4972  C  CG  . TYR   A 1  607 ? 14.505  12.342  -26.887 1    52.491  ? 607  TYR   A CG  1 1 
ATOM   4973  C  CD1 . TYR   A 1  607 ? 14.765  11.114  -27.516 1    47.299  ? 607  TYR   A CD1 1 1 
ATOM   4974  C  CD2 . TYR   A 1  607 ? 13.253  12.526  -26.293 1    51.803  ? 607  TYR   A CD2 1 1 
ATOM   4975  C  CE1 . TYR   A 1  607 ? 13.805  10.12   -27.594 1    44.17   ? 607  TYR   A CE1 1 1 
ATOM   4976  C  CE2 . TYR   A 1  607 ? 12.289  11.532  -26.356 1    51.644  ? 607  TYR   A CE2 1 1 
ATOM   4977  C  CZ  . TYR   A 1  607 ? 12.559  10.336  -27.012 1    50.208  ? 607  TYR   A CZ  1 1 
ATOM   4978  O  OH  . TYR   A 1  607 ? 11.57   9.375   -27.035 1    51.335  ? 607  TYR   A OH  1 1 
ATOM   4979  N  N   . PRO   A 1  608 ? 13.271  14.512  -29.205 1    51.466  ? 608  PRO   A N   1 1 
ATOM   4980  C  CA  . PRO   A 1  608 ? 13.611  13.402  -30.107 1    49.954  ? 608  PRO   A CA  1 1 
ATOM   4981  C  C   . PRO   A 1  608 ? 14.037  13.671  -31.559 1    56.677  ? 608  PRO   A C   1 1 
ATOM   4982  O  O   . PRO   A 1  608 ? 13.775  12.857  -32.448 1    55.224  ? 608  PRO   A O   1 1 
ATOM   4983  C  CB  . PRO   A 1  608 ? 12.276  12.607  -30.008 1    45.917  ? 608  PRO   A CB  1 1 
ATOM   4984  C  CG  . PRO   A 1  608 ? 11.193  13.672  -29.875 1    46.03   ? 608  PRO   A CG  1 1 
ATOM   4985  C  CD  . PRO   A 1  608 ? 11.852  14.916  -29.302 1    47.462  ? 608  PRO   A CD  1 1 
ATOM   4986  N  N   . GLU   A 1  609 ? 14.763  14.77   -31.81  1    63.273  ? 609  GLU   A N   1 1 
ATOM   4987  C  CA  . GLU   A 1  609 ? 14.876  15.314  -33.166 1    66.562  ? 609  GLU   A CA  1 1 
ATOM   4988  C  C   . GLU   A 1  609 ? 15.79   14.477  -34.087 1    61.175  ? 609  GLU   A C   1 1 
ATOM   4989  O  O   . GLU   A 1  609 ? 16.52   13.607  -33.568 1    58.436  ? 609  GLU   A O   1 1 
ATOM   4990  C  CB  . GLU   A 1  609 ? 15.346  16.765  -33.104 1    75.343  ? 609  GLU   A CB  1 1 
ATOM   4991  C  CG  . GLU   A 1  609 ? 14.443  17.638  -32.237 1    84.65   ? 609  GLU   A CG  1 1 
ATOM   4992  C  CD  . GLU   A 1  609 ? 15.106  18.936  -31.81  1    99.338  ? 609  GLU   A CD  1 1 
ATOM   4993  O  OE1 . GLU   A 1  609 ? 16.356  19.047  -31.874 1    100.221 ? 609  GLU   A OE1 1 1 
ATOM   4994  O  OE2 . GLU   A 1  609 ? 14.348  19.855  -31.431 1    109.368 ? 609  GLU   A OE2 1 1 
ATOM   4995  N  N   . ASP   B 1  2   ? 11.124  -4.93   45.146  1    63.136  ? 2    ASP   B N   1 2 
ATOM   4996  C  CA  . ASP   B 1  2   ? 10.541  -4.769  46.503  1    66.675  ? 2    ASP   B CA  1 2 
ATOM   4997  C  C   . ASP   B 1  2   ? 9.493   -5.843  46.786  1    68.681  ? 2    ASP   B C   1 2 
ATOM   4998  O  O   . ASP   B 1  2   ? 8.532   -6.005  46.02   1    66.216  ? 2    ASP   B O   1 2 
ATOM   4999  C  CB  . ASP   B 1  2   ? 9.923   -3.416  46.822  1    66.007  ? 2    ASP   B CB  1 2 
ATOM   5000  C  CG  . ASP   B 1  2   ? 9.381   -3.337  48.253  1    72.466  ? 2    ASP   B CG  1 2 
ATOM   5001  O  OD1 . ASP   B 1  2   ? 10.115  -3.733  49.203  1    73.891  ? 2    ASP   B OD1 1 2 
ATOM   5002  O  OD2 . ASP   B 1  2   ? 8.21    -2.926  48.428  1    74.872  ? 2    ASP   B OD2 1 2 
ATOM   5003  N  N   . PRO   B 1  3   ? 9.671   -6.551  47.93   1    67.822  ? 3    PRO   B N   1 2 
ATOM   5004  C  CA  . PRO   B 1  3   ? 8.685   -7.49   48.476  1    72.155  ? 3    PRO   B CA  1 2 
ATOM   5005  C  C   . PRO   B 1  3   ? 7.222   -7.043  48.546  1    73.662  ? 3    PRO   B C   1 2 
ATOM   5006  O  O   . PRO   B 1  3   ? 6.346   -7.736  48.027  1    76.197  ? 3    PRO   B O   1 2 
ATOM   5007  C  CB  . PRO   B 1  3   ? 9.267   -7.849  49.882  1    73.485  ? 3    PRO   B CB  1 2 
ATOM   5008  C  CG  . PRO   B 1  3   ? 10.763  -7.633  49.734  1    73.091  ? 3    PRO   B CG  1 2 
ATOM   5009  C  CD  . PRO   B 1  3   ? 10.882  -6.457  48.756  1    71.244  ? 3    PRO   B CD  1 2 
ATOM   5010  N  N   . GLY   B 1  4   ? 6.975   -5.872  49.161  1    75.985  ? 4    GLY   B N   1 2 
ATOM   5011  C  CA  . GLY   B 1  4   ? 5.664   -5.233  49.251  1    74.194  ? 4    GLY   B CA  1 2 
ATOM   5012  C  C   . GLY   B 1  4   ? 5.079   -4.83   47.894  1    72.406  ? 4    GLY   B C   1 2 
ATOM   5013  O  O   . GLY   B 1  4   ? 3.924   -4.406  47.827  1    73.488  ? 4    GLY   B O   1 2 
ATOM   5014  N  N   . LEU   B 1  5   ? 5.883   -4.931  46.821  1    70.958  ? 5    LEU   B N   1 2 
ATOM   5015  C  CA  . LEU   B 1  5   ? 5.446   -4.697  45.446  1    69.396  ? 5    LEU   B CA  1 2 
ATOM   5016  C  C   . LEU   B 1  5   ? 5.085   -6.013  44.742  1    68.148  ? 5    LEU   B C   1 2 
ATOM   5017  O  O   . LEU   B 1  5   ? 4.277   -6.025  43.802  1    62.909  ? 5    LEU   B O   1 2 
ATOM   5018  C  CB  . LEU   B 1  5   ? 6.516   -3.923  44.661  1    69.647  ? 5    LEU   B CB  1 2 
ATOM   5019  C  CG  . LEU   B 1  5   ? 6.789   -2.478  45.116  1    71.779  ? 5    LEU   B CG  1 2 
ATOM   5020  C  CD1 . LEU   B 1  5   ? 8       -1.899  44.368  1    72.372  ? 5    LEU   B CD1 1 2 
ATOM   5021  C  CD2 . LEU   B 1  5   ? 5.579   -1.513  45.064  1    68.052  ? 5    LEU   B CD2 1 2 
ATOM   5022  N  N   . GLN   B 1  6   ? 5.714   -7.112  45.198  1    73.909  ? 6    GLN   B N   1 2 
ATOM   5023  C  CA  . GLN   B 1  6   ? 5.578   -8.425  44.59   1    72.781  ? 6    GLN   B CA  1 2 
ATOM   5024  C  C   . GLN   B 1  6   ? 4.256   -9.045  45.019  1    72.688  ? 6    GLN   B C   1 2 
ATOM   5025  O  O   . GLN   B 1  6   ? 3.827   -8.854  46.154  1    76.605  ? 6    GLN   B O   1 2 
ATOM   5026  C  CB  . GLN   B 1  6   ? 6.826   -9.226  44.919  1    80.762  ? 6    GLN   B CB  1 2 
ATOM   5027  C  CG  . GLN   B 1  6   ? 8.023   -8.765  44.096  1    84.274  ? 6    GLN   B CG  1 2 
ATOM   5028  C  CD  . GLN   B 1  6   ? 9.338   -9.077  44.773  1    88.42   ? 6    GLN   B CD  1 2 
ATOM   5029  O  OE1 . GLN   B 1  6   ? 10.203  -8.213  44.966  1    87.149  ? 6    GLN   B OE1 1 2 
ATOM   5030  N  NE2 . GLN   B 1  6   ? 9.477   -10.334 45.158  1    89.921  ? 6    GLN   B NE2 1 2 
ATOM   5031  N  N   . PRO   B 1  7   ? 3.583   -9.799  44.117  1    71.172  ? 7    PRO   B N   1 2 
ATOM   5032  C  CA  . PRO   B 1  7   ? 2.146   -10.095 44.255  1    71.592  ? 7    PRO   B CA  1 2 
ATOM   5033  C  C   . PRO   B 1  7   ? 1.723   -11.066 45.36   1    75.725  ? 7    PRO   B C   1 2 
ATOM   5034  O  O   . PRO   B 1  7   ? 2.512   -11.897 45.813  1    78.775  ? 7    PRO   B O   1 2 
ATOM   5035  C  CB  . PRO   B 1  7   ? 1.769   -10.625 42.859  1    70.021  ? 7    PRO   B CB  1 2 
ATOM   5036  C  CG  . PRO   B 1  7   ? 3.056   -11.266 42.367  1    70.52   ? 7    PRO   B CG  1 2 
ATOM   5037  C  CD  . PRO   B 1  7   ? 4.201   -10.423 42.925  1    68.902  ? 7    PRO   B CD  1 2 
ATOM   5038  N  N   . GLY   B 1  8   ? 0.472   -10.941 45.819  1    75.48   ? 8    GLY   B N   1 2 
ATOM   5039  C  CA  . GLY   B 1  8   ? 0.028   -11.794 46.907  1    78.602  ? 8    GLY   B CA  1 2 
ATOM   5040  C  C   . GLY   B 1  8   ? -0.425  -13.144 46.364  1    80.154  ? 8    GLY   B C   1 2 
ATOM   5041  O  O   . GLY   B 1  8   ? -0.39   -13.388 45.157  1    80.401  ? 8    GLY   B O   1 2 
ATOM   5042  N  N   . GLN   B 1  9   ? -0.858  -14.016 47.254  1    77.939  ? 9    GLN   B N   1 2 
ATOM   5043  C  CA  . GLN   B 1  9   ? -1.641  -15.117 46.72   1    82.762  ? 9    GLN   B CA  1 2 
ATOM   5044  C  C   . GLN   B 1  9   ? -3.143  -14.551 46.61   1    81.712  ? 9    GLN   B C   1 2 
ATOM   5045  O  O   . GLN   B 1  9   ? -3.688  -13.685 47.31   1    87.491  ? 9    GLN   B O   1 2 
ATOM   5046  C  CB  . GLN   B 1  9   ? -1.265  -16.422 47.452  1    90.938  ? 9    GLN   B CB  1 2 
ATOM   5047  C  CG  . GLN   B 1  9   ? 0.126   -16.945 47.079  1    91.956  ? 9    GLN   B CG  1 2 
ATOM   5048  C  CD  . GLN   B 1  9   ? 0.968   -17.417 48.246  1    95.483  ? 9    GLN   B CD  1 2 
ATOM   5049  O  OE1 . GLN   B 1  9   ? 2.202   -17.435 48.17   1    95.763  ? 9    GLN   B OE1 1 2 
ATOM   5050  N  NE2 . GLN   B 1  9   ? 0.322   -17.781 49.344  1    99.489  ? 9    GLN   B NE2 1 2 
ATOM   5051  N  N   . PHE   B 1  10  ? -3.818  -15.485 45.731  1    82.161  ? 10   PHE   B N   1 2 
ATOM   5052  C  CA  . PHE   B 1  10  ? -5.242  -15.326 45.499  1    85.296  ? 10   PHE   B CA  1 2 
ATOM   5053  C  C   . PHE   B 1  10  ? -5.782  -16.537 44.755  1    89.65   ? 10   PHE   B C   1 2 
ATOM   5054  O  O   . PHE   B 1  10  ? -5.083  -17.094 43.903  1    87.027  ? 10   PHE   B O   1 2 
ATOM   5055  C  CB  . PHE   B 1  10  ? -5.553  -14.208 44.509  1    83.559  ? 10   PHE   B CB  1 2 
ATOM   5056  C  CG  . PHE   B 1  10  ? -5.062  -12.848 44.984  1    82.725  ? 10   PHE   B CG  1 2 
ATOM   5057  C  CD1 . PHE   B 1  10  ? -3.726  -12.468 44.793  1    79.316  ? 10   PHE   B CD1 1 2 
ATOM   5058  C  CD2 . PHE   B 1  10  ? -5.923  -11.979 45.652  1    84.064  ? 10   PHE   B CD2 1 2 
ATOM   5059  C  CE1 . PHE   B 1  10  ? -3.268  -11.246 45.267  1    80.316  ? 10   PHE   B CE1 1 2 
ATOM   5060  C  CE2 . PHE   B 1  10  ? -5.465  -10.747 46.102  1    82.451  ? 10   PHE   B CE2 1 2 
ATOM   5061  C  CZ  . PHE   B 1  10  ? -4.142  -10.387 45.907  1    82.541  ? 10   PHE   B CZ  1 2 
ATOM   5062  N  N   . SER   B 1  11  ? -7.052  -16.868 45.065  1    94.367  ? 11   SER   B N   1 2 
ATOM   5063  C  CA  . SER   B 1  11  ? -7.8    -17.937 44.417  1    96.329  ? 11   SER   B CA  1 2 
ATOM   5064  C  C   . SER   B 1  11  ? -8.134  -17.61  42.954  1    95.879  ? 11   SER   B C   1 2 
ATOM   5065  O  O   . SER   B 1  11  ? -8.122  -16.442 42.514  1    85.932  ? 11   SER   B O   1 2 
ATOM   5066  C  CB  . SER   B 1  11  ? -9.027  -18.316 45.211  1    97.624  ? 11   SER   B CB  1 2 
ATOM   5067  O  OG  . SER   B 1  11  ? -9.877  -17.141 45.415  1    93.478  ? 11   SER   B OG  1 2 
ATOM   5068  N  N   . ALA   B 1  12  ? -8.43   -18.703 42.226  1    97.543  ? 12   ALA   B N   1 2 
ATOM   5069  C  CA  . ALA   B 1  12  ? -8.673  -18.688 40.789  1    96.552  ? 12   ALA   B CA  1 2 
ATOM   5070  C  C   . ALA   B 1  12  ? -10.204 -18.753 40.57   1    97.675  ? 12   ALA   B C   1 2 
ATOM   5071  O  O   . ALA   B 1  12  ? -10.917 -19.991 40.58   1    104.225 ? 12   ALA   B O   1 2 
ATOM   5072  C  CB  . ALA   B 1  12  ? -7.953  -19.873 40.155  1    97.859  ? 12   ALA   B CB  1 2 
ATOM   5073  N  N   . ASP   B 1  13  ? -10.732 -17.444 40.422  1    96.924  ? 13   ASP   B N   1 2 
ATOM   5074  C  CA  . ASP   B 1  13  ? -12.179 -17.264 40.376  1    99.246  ? 13   ASP   B CA  1 2 
ATOM   5075  C  C   . ASP   B 1  13  ? -12.439 -15.76  40.427  1    96.733  ? 13   ASP   B C   1 2 
ATOM   5076  O  O   . ASP   B 1  13  ? -11.496 -14.963 40.649  1    94.926  ? 13   ASP   B O   1 2 
ATOM   5077  C  CB  . ASP   B 1  13  ? -12.91  -18.098 41.429  1    107.84  ? 13   ASP   B CB  1 2 
ATOM   5078  C  CG  . ASP   B 1  13  ? -13.112 -17.441 42.793  1    110.668 ? 13   ASP   B CG  1 2 
ATOM   5079  O  OD1 . ASP   B 1  13  ? -12.741 -16.231 42.945  1    106.033 ? 13   ASP   B OD1 1 2 
ATOM   5080  O  OD2 . ASP   B 1  13  ? -13.66  -18.118 43.687  1    116.006 ? 13   ASP   B OD2 1 2 
ATOM   5081  N  N   . GLU   B 1  14  ? -13.72  -15.392 40.241  1    96.14   ? 14   GLU   B N   1 2 
ATOM   5082  C  CA  . GLU   B 1  14  ? -14.094 -14.012 39.953  1    92.467  ? 14   GLU   B CA  1 2 
ATOM   5083  C  C   . GLU   B 1  14  ? -13.87  -13.111 41.17   1    89.914  ? 14   GLU   B C   1 2 
ATOM   5084  O  O   . GLU   B 1  14  ? -13.458 -11.956 41.012  1    84.232  ? 14   GLU   B O   1 2 
ATOM   5085  C  CB  . GLU   B 1  14  ? -15.524 -13.893 39.435  1    92.011  ? 14   GLU   B CB  1 2 
ATOM   5086  C  CG  . GLU   B 1  14  ? -15.915 -12.425 39.29   1    89.791  ? 14   GLU   B CG  1 2 
ATOM   5087  C  CD  . GLU   B 1  14  ? -16.815 -12.097 38.121  1    87.886  ? 14   GLU   B CD  1 2 
ATOM   5088  O  OE1 . GLU   B 1  14  ? -17.323 -13.082 37.497  1    86.335  ? 14   GLU   B OE1 1 2 
ATOM   5089  O  OE2 . GLU   B 1  14  ? -16.936 -10.869 37.827  1    81.81   ? 14   GLU   B OE2 1 2 
ATOM   5090  N  N   . ALA   B 1  15  ? -14.164 -13.672 42.338  1    92.341  ? 15   ALA   B N   1 2 
ATOM   5091  C  CA  . ALA   B 1  15  ? -14.002 -13.066 43.657  1    88.965  ? 15   ALA   B CA  1 2 
ATOM   5092  C  C   . ALA   B 1  15  ? -12.501 -12.719 43.862  1    84.875  ? 15   ALA   B C   1 2 
ATOM   5093  O  O   . ALA   B 1  15  ? -12.057 -11.408 43.946  1    84.76   ? 15   ALA   B O   1 2 
ATOM   5094  C  CB  . ALA   B 1  15  ? -14.498 -14.045 44.682  1    88.573  ? 15   ALA   B CB  1 2 
ATOM   5095  N  N   . GLY   B 1  16  ? -11.723 -13.904 43.961  1    87.724  ? 16   GLY   B N   1 2 
ATOM   5096  C  CA  . GLY   B 1  16  ? -10.27  -13.838 44.016  1    87.131  ? 16   GLY   B CA  1 2 
ATOM   5097  C  C   . GLY   B 1  16  ? -9.766  -12.736 43.11   1    81.81   ? 16   GLY   B C   1 2 
ATOM   5098  O  O   . GLY   B 1  16  ? -9.078  -11.83  43.591  1    77.343  ? 16   GLY   B O   1 2 
ATOM   5099  N  N   . ALA   B 1  17  ? -10.178 -12.776 41.826  1    80.532  ? 17   ALA   B N   1 2 
ATOM   5100  C  CA  . ALA   B 1  17  ? -9.739  -11.78  40.861  1    75.845  ? 17   ALA   B CA  1 2 
ATOM   5101  C  C   . ALA   B 1  17  ? -10.197 -10.364 41.228  1    73.652  ? 17   ALA   B C   1 2 
ATOM   5102  O  O   . ALA   B 1  17  ? -9.552  -9.405  40.821  1    67.804  ? 17   ALA   B O   1 2 
ATOM   5103  C  CB  . ALA   B 1  17  ? -10.09  -12.148 39.406  1    75.915  ? 17   ALA   B CB  1 2 
ATOM   5104  N  N   . GLN   B 1  18  ? -11.304 -10.228 41.978  1    73.707  ? 18   GLN   B N   1 2 
ATOM   5105  C  CA  . GLN   B 1  18  ? -11.78  -8.917  42.423  1    75.408  ? 18   GLN   B CA  1 2 
ATOM   5106  C  C   . GLN   B 1  18  ? -10.796 -8.309  43.434  1    72.049  ? 18   GLN   B C   1 2 
ATOM   5107  O  O   . GLN   B 1  18  ? -10.528 -7.104  43.407  1    72.145  ? 18   GLN   B O   1 2 
ATOM   5108  C  CB  . GLN   B 1  18  ? -13.195 -9.005  43.022  1    80.753  ? 18   GLN   B CB  1 2 
ATOM   5109  C  CG  . GLN   B 1  18  ? -14.357 -9.027  42.025  1    83.183  ? 18   GLN   B CG  1 2 
ATOM   5110  C  CD  . GLN   B 1  18  ? -14.939 -7.659  41.721  1    83.832  ? 18   GLN   B CD  1 2 
ATOM   5111  O  OE1 . GLN   B 1  18  ? -15.479 -6.972  42.605  1    84.618  ? 18   GLN   B OE1 1 2 
ATOM   5112  N  NE2 . GLN   B 1  18  ? -14.821 -7.247  40.465  1    75.794  ? 18   GLN   B NE2 1 2 
ATOM   5113  N  N   . LEU   B 1  19  ? -10.251 -9.177  44.305  1    70.576  ? 19   LEU   B N   1 2 
ATOM   5114  C  CA  . LEU   B 1  19  ? -9.285  -8.801  45.328  1    68.686  ? 19   LEU   B CA  1 2 
ATOM   5115  C  C   . LEU   B 1  19  ? -7.936  -8.524  44.649  1    65.183  ? 19   LEU   B C   1 2 
ATOM   5116  O  O   . LEU   B 1  19  ? -7.29   -7.526  44.968  1    62.245  ? 19   LEU   B O   1 2 
ATOM   5117  C  CB  . LEU   B 1  19  ? -9.198  -9.801  46.496  1    70.315  ? 19   LEU   B CB  1 2 
ATOM   5118  C  CG  . LEU   B 1  19  ? -10.323 -9.808  47.552  1    72.148  ? 19   LEU   B CG  1 2 
ATOM   5119  C  CD1 . LEU   B 1  19  ? -10.007 -10.802 48.65   1    75.268  ? 19   LEU   B CD1 1 2 
ATOM   5120  C  CD2 . LEU   B 1  19  ? -10.756 -8.46   48.2    1    70.048  ? 19   LEU   B CD2 1 2 
ATOM   5121  N  N   . PHE   B 1  20  ? -7.589  -9.364  43.66   1    64.151  ? 20   PHE   B N   1 2 
ATOM   5122  C  CA  . PHE   B 1  20  ? -6.324  -9.331  42.939  1    62.47   ? 20   PHE   B CA  1 2 
ATOM   5123  C  C   . PHE   B 1  20  ? -6.107  -7.938  42.36   1    60.989  ? 20   PHE   B C   1 2 
ATOM   5124  O  O   . PHE   B 1  20  ? -5.07   -7.31   42.599  1    61.334  ? 20   PHE   B O   1 2 
ATOM   5125  C  CB  . PHE   B 1  20  ? -6.227  -10.454 41.891  1    62.168  ? 20   PHE   B CB  1 2 
ATOM   5126  C  CG  . PHE   B 1  20  ? -5.02   -10.411 40.947  1    60.14   ? 20   PHE   B CG  1 2 
ATOM   5127  C  CD1 . PHE   B 1  20  ? -5.051  -9.657  39.776  1    58.17   ? 20   PHE   B CD1 1 2 
ATOM   5128  C  CD2 . PHE   B 1  20  ? -3.854  -11.127 41.229  1    61.46   ? 20   PHE   B CD2 1 2 
ATOM   5129  C  CE1 . PHE   B 1  20  ? -3.955  -9.594  38.903  1    56.634  ? 20   PHE   B CE1 1 2 
ATOM   5130  C  CE2 . PHE   B 1  20  ? -2.759  -11.076 40.366  1    58.884  ? 20   PHE   B CE2 1 2 
ATOM   5131  C  CZ  . PHE   B 1  20  ? -2.809  -10.318 39.207  1    57.591  ? 20   PHE   B CZ  1 2 
ATOM   5132  N  N   . ALA   B 1  21  ? -7.069  -7.505  41.525  1    61.386  ? 21   ALA   B N   1 2 
ATOM   5133  C  CA  . ALA   B 1  21  ? -7.09   -6.193  40.907  1    58.565  ? 21   ALA   B CA  1 2 
ATOM   5134  C  C   . ALA   B 1  21  ? -6.899  -5.091  41.957  1    57.904  ? 21   ALA   B C   1 2 
ATOM   5135  O  O   . ALA   B 1  21  ? -6.104  -4.187  41.753  1    54      ? 21   ALA   B O   1 2 
ATOM   5136  C  CB  . ALA   B 1  21  ? -8.359  -6.022  40.097  1    58.147  ? 21   ALA   B CB  1 2 
ATOM   5137  N  N   . GLN   B 1  22  ? -7.593  -5.162  43.102  1    61.096  ? 22   GLN   B N   1 2 
ATOM   5138  C  CA  . GLN   B 1  22  ? -7.419  -4.109  44.102  1    63.099  ? 22   GLN   B CA  1 2 
ATOM   5139  C  C   . GLN   B 1  22  ? -5.978  -4.128  44.626  1    64.391  ? 22   GLN   B C   1 2 
ATOM   5140  O  O   . GLN   B 1  22  ? -5.356  -3.097  44.834  1    66.857  ? 22   GLN   B O   1 2 
ATOM   5141  C  CB  . GLN   B 1  22  ? -8.42   -4.104  45.259  1    63.176  ? 22   GLN   B CB  1 2 
ATOM   5142  C  CG  . GLN   B 1  22  ? -9.886  -4.086  44.843  1    62.719  ? 22   GLN   B CG  1 2 
ATOM   5143  C  CD  . GLN   B 1  22  ? -10.818 -4.49   45.973  1    66.513  ? 22   GLN   B CD  1 2 
ATOM   5144  O  OE1 . GLN   B 1  22  ? -10.413 -4.694  47.123  1    67.152  ? 22   GLN   B OE1 1 2 
ATOM   5145  N  NE2 . GLN   B 1  22  ? -12.095 -4.617  45.651  1    67.81   ? 22   GLN   B NE2 1 2 
ATOM   5146  N  N   . SER   B 1  23  ? -5.44   -5.323  44.809  1    65.531  ? 23   SER   B N   1 2 
ATOM   5147  C  CA  . SER   B 1  23  ? -4.054  -5.479  45.19   1    65.871  ? 23   SER   B CA  1 2 
ATOM   5148  C  C   . SER   B 1  23  ? -3.132  -4.957  44.078  1    66.083  ? 23   SER   B C   1 2 
ATOM   5149  O  O   . SER   B 1  23  ? -2.087  -4.374  44.366  1    66.835  ? 23   SER   B O   1 2 
ATOM   5150  C  CB  . SER   B 1  23  ? -3.807  -6.917  45.547  1    65.817  ? 23   SER   B CB  1 2 
ATOM   5151  O  OG  . SER   B 1  23  ? -2.765  -6.943  46.497  1    65.445  ? 23   SER   B OG  1 2 
ATOM   5152  N  N   . TYR   B 1  24  ? -3.533  -5.105  42.809  1    63.384  ? 24   TYR   B N   1 2 
ATOM   5153  C  CA  . TYR   B 1  24  ? -2.64   -4.723  41.715  1    61.179  ? 24   TYR   B CA  1 2 
ATOM   5154  C  C   . TYR   B 1  24  ? -2.431  -3.208  41.718  1    62.508  ? 24   TYR   B C   1 2 
ATOM   5155  O  O   . TYR   B 1  24  ? -1.303  -2.717  41.781  1    62.099  ? 24   TYR   B O   1 2 
ATOM   5156  C  CB  . TYR   B 1  24  ? -3.146  -5.241  40.365  1    58.589  ? 24   TYR   B CB  1 2 
ATOM   5157  C  CG  . TYR   B 1  24  ? -2.47   -4.667  39.12   1    57.693  ? 24   TYR   B CG  1 2 
ATOM   5158  C  CD1 . TYR   B 1  24  ? -1.215  -5.116  38.72   1    57.694  ? 24   TYR   B CD1 1 2 
ATOM   5159  C  CD2 . TYR   B 1  24  ? -3.088  -3.684  38.346  1    56.673  ? 24   TYR   B CD2 1 2 
ATOM   5160  C  CE1 . TYR   B 1  24  ? -0.599  -4.623  37.581  1    55.353  ? 24   TYR   B CE1 1 2 
ATOM   5161  C  CE2 . TYR   B 1  24  ? -2.458  -3.146  37.231  1    55.68   ? 24   TYR   B CE2 1 2 
ATOM   5162  C  CZ  . TYR   B 1  24  ? -1.22   -3.637  36.846  1    55.866  ? 24   TYR   B CZ  1 2 
ATOM   5163  O  OH  . TYR   B 1  24  ? -0.585  -3.17   35.74   1    54.893  ? 24   TYR   B OH  1 2 
ATOM   5164  N  N   . GLN   B 1  25  ? -3.566  -2.501  41.678  1    65.966  ? 25   GLN   B N   1 2 
ATOM   5165  C  CA  . GLN   B 1  25  ? -3.691  -1.066  41.501  1    64.578  ? 25   GLN   B CA  1 2 
ATOM   5166  C  C   . GLN   B 1  25  ? -3.116  -0.334  42.713  1    69.4    ? 25   GLN   B C   1 2 
ATOM   5167  O  O   . GLN   B 1  25  ? -2.952  0.888   42.72   1    70.678  ? 25   GLN   B O   1 2 
ATOM   5168  C  CB  . GLN   B 1  25  ? -5.161  -0.897  41.126  1    63.742  ? 25   GLN   B CB  1 2 
ATOM   5169  C  CG  . GLN   B 1  25  ? -5.387  -1.197  39.644  1    68.54   ? 25   GLN   B CG  1 2 
ATOM   5170  C  CD  . GLN   B 1  25  ? -6.833  -1.354  39.222  1    67.883  ? 25   GLN   B CD  1 2 
ATOM   5171  O  OE1 . GLN   B 1  25  ? -7.245  -0.793  38.198  1    62.035  ? 25   GLN   B OE1 1 2 
ATOM   5172  N  NE2 . GLN   B 1  25  ? -7.604  -2.13   39.985  1    62.765  ? 25   GLN   B NE2 1 2 
ATOM   5173  N  N   . SER   B 1  26  ? -2.738  -1.131  43.709  1    71.74   ? 26   SER   B N   1 2 
ATOM   5174  C  CA  . SER   B 1  26  ? -2.293  -0.63   44.992  1    74.114  ? 26   SER   B CA  1 2 
ATOM   5175  C  C   . SER   B 1  26  ? -0.814  -0.289  44.886  1    73.128  ? 26   SER   B C   1 2 
ATOM   5176  O  O   . SER   B 1  26  ? -0.356  0.741   45.367  1    75.589  ? 26   SER   B O   1 2 
ATOM   5177  C  CB  . SER   B 1  26  ? -2.519  -1.683  46.04   1    72.574  ? 26   SER   B CB  1 2 
ATOM   5178  O  OG  . SER   B 1  26  ? -2.635  -1.058  47.299  1    80.344  ? 26   SER   B OG  1 2 
ATOM   5179  N  N   . SER   B 1  27  ? -0.075  -1.163  44.212  1    70.003  ? 27   SER   B N   1 2 
ATOM   5180  C  CA  . SER   B 1  27  ? 1.368   -1.064  44.287  1    66.292  ? 27   SER   B CA  1 2 
ATOM   5181  C  C   . SER   B 1  27  ? 1.848   -0.394  43.009  1    60.303  ? 27   SER   B C   1 2 
ATOM   5182  O  O   . SER   B 1  27  ? 2.907   0.255   42.957  1    55.826  ? 27   SER   B O   1 2 
ATOM   5183  C  CB  . SER   B 1  27  ? 1.955   -2.431  44.529  1    67.547  ? 27   SER   B CB  1 2 
ATOM   5184  O  OG  . SER   B 1  27  ? 1.26    -3.061  45.6    1    62.699  ? 27   SER   B OG  1 2 
ATOM   5185  N  N   . ALA   B 1  28  ? 0.973   -0.504  42.007  1    60.494  ? 28   ALA   B N   1 2 
ATOM   5186  C  CA  . ALA   B 1  28  ? 1.204   0.108   40.708  1    56.845  ? 28   ALA   B CA  1 2 
ATOM   5187  C  C   . ALA   B 1  28  ? 1.239   1.635   40.838  1    57.903  ? 28   ALA   B C   1 2 
ATOM   5188  O  O   . ALA   B 1  28  ? 2.098   2.26    40.235  1    59.598  ? 28   ALA   B O   1 2 
ATOM   5189  C  CB  . ALA   B 1  28  ? 0.202   -0.402  39.687  1    55.896  ? 28   ALA   B CB  1 2 
ATOM   5190  N  N   . GLU   B 1  29  ? 0.355   2.223   41.671  1    60.906  ? 29   GLU   B N   1 2 
ATOM   5191  C  CA  . GLU   B 1  29  ? 0.347   3.654   41.982  1    60.279  ? 29   GLU   B CA  1 2 
ATOM   5192  C  C   . GLU   B 1  29  ? 1.76    4.142   42.334  1    55.32   ? 29   GLU   B C   1 2 
ATOM   5193  O  O   . GLU   B 1  29  ? 2.205   5.157   41.816  1    53.748  ? 29   GLU   B O   1 2 
ATOM   5194  C  CB  . GLU   B 1  29  ? -0.835  3.991   42.904  1    68.513  ? 29   GLU   B CB  1 2 
ATOM   5195  C  CG  . GLU   B 1  29  ? -0.887  5.421   43.444  1    75.18   ? 29   GLU   B CG  1 2 
ATOM   5196  C  CD  . GLU   B 1  29  ? -2.263  5.937   43.868  1    83.476  ? 29   GLU   B CD  1 2 
ATOM   5197  O  OE1 . GLU   B 1  29  ? -3.029  6.387   42.989  1    82.361  ? 29   GLU   B OE1 1 2 
ATOM   5198  O  OE2 . GLU   B 1  29  ? -2.595  5.891   45.076  1    90.84   ? 29   GLU   B OE2 1 2 
ATOM   5199  N  N   . GLN   B 1  30  ? 2.503   3.362   43.121  1    56.425  ? 30   GLN   B N   1 2 
ATOM   5200  C  CA  . GLN   B 1  30  ? 3.824   3.735   43.618  1    57.21   ? 30   GLN   B CA  1 2 
ATOM   5201  C  C   . GLN   B 1  30  ? 4.861   3.615   42.503  1    54.872  ? 30   GLN   B C   1 2 
ATOM   5202  O  O   . GLN   B 1  30  ? 5.842   4.363   42.482  1    55.055  ? 30   GLN   B O   1 2 
ATOM   5203  C  CB  . GLN   B 1  30  ? 4.224   2.817   44.781  1    60.207  ? 30   GLN   B CB  1 2 
ATOM   5204  C  CG  . GLN   B 1  30  ? 5.033   3.516   45.876  1    62.89   ? 30   GLN   B CG  1 2 
ATOM   5205  C  CD  . GLN   B 1  30  ? 5.599   2.581   46.925  1    67.288  ? 30   GLN   B CD  1 2 
ATOM   5206  O  OE1 . GLN   B 1  30  ? 4.907   1.694   47.44   1    66.371  ? 30   GLN   B OE1 1 2 
ATOM   5207  N  NE2 . GLN   B 1  30  ? 6.88    2.748   47.229  1    68.61   ? 30   GLN   B NE2 1 2 
ATOM   5208  N  N   . VAL   B 1  31  ? 4.659   2.622   41.617  1    52.44   ? 31   VAL   B N   1 2 
ATOM   5209  C  CA  . VAL   B 1  31  ? 5.64    2.306   40.584  1    50.591  ? 31   VAL   B CA  1 2 
ATOM   5210  C  C   . VAL   B 1  31  ? 5.49    3.336   39.452  1    45.158  ? 31   VAL   B C   1 2 
ATOM   5211  O  O   . VAL   B 1  31  ? 6.468   3.94    39      1    40.719  ? 31   VAL   B O   1 2 
ATOM   5212  C  CB  . VAL   B 1  31  ? 5.59    0.849   40.057  1    51.033  ? 31   VAL   B CB  1 2 
ATOM   5213  C  CG1 . VAL   B 1  31  ? 6.579   0.617   38.926  1    48.287  ? 31   VAL   B CG1 1 2 
ATOM   5214  C  CG2 . VAL   B 1  31  ? 5.85    -0.191  41.161  1    51.713  ? 31   VAL   B CG2 1 2 
ATOM   5215  N  N   . LEU   B 1  32  ? 4.242   3.538   39.002  1    43.846  ? 32   LEU   B N   1 2 
ATOM   5216  C  CA  . LEU   B 1  32  ? 3.939   4.548   37.993  1    39.748  ? 32   LEU   B CA  1 2 
ATOM   5217  C  C   . LEU   B 1  32  ? 4.449   5.919   38.438  1    38.764  ? 32   LEU   B C   1 2 
ATOM   5218  O  O   . LEU   B 1  32  ? 5.057   6.641   37.657  1    39.291  ? 32   LEU   B O   1 2 
ATOM   5219  C  CB  . LEU   B 1  32  ? 2.425   4.549   37.787  1    40.15   ? 32   LEU   B CB  1 2 
ATOM   5220  C  CG  . LEU   B 1  32  ? 1.869   3.342   37.026  1    41.972  ? 32   LEU   B CG  1 2 
ATOM   5221  C  CD1 . LEU   B 1  32  ? 0.349   3.228   37.186  1    43.768  ? 32   LEU   B CD1 1 2 
ATOM   5222  C  CD2 . LEU   B 1  32  ? 2.285   3.369   35.563  1    41.024  ? 32   LEU   B CD2 1 2 
ATOM   5223  N  N   . PHE   B 1  33  ? 4.165   6.3     39.683  1    40.148  ? 33   PHE   B N   1 2 
ATOM   5224  C  CA  . PHE   B 1  33  ? 4.718   7.504   40.293  1    41.086  ? 33   PHE   B CA  1 2 
ATOM   5225  C  C   . PHE   B 1  33  ? 6.218   7.634   40.02   1    39.67   ? 33   PHE   B C   1 2 
ATOM   5226  O  O   . PHE   B 1  33  ? 6.651   8.683   39.605  1    37.379  ? 33   PHE   B O   1 2 
ATOM   5227  C  CB  . PHE   B 1  33  ? 4.445   7.752   41.795  1    44.123  ? 33   PHE   B CB  1 2 
ATOM   5228  C  CG  . PHE   B 1  33  ? 5.133   9.043   42.238  1    45.356  ? 33   PHE   B CG  1 2 
ATOM   5229  C  CD1 . PHE   B 1  33  ? 4.601   10.295  41.894  1    46.508  ? 33   PHE   B CD1 1 2 
ATOM   5230  C  CD2 . PHE   B 1  33  ? 6.361   9.02    42.901  1    47.405  ? 33   PHE   B CD2 1 2 
ATOM   5231  C  CE1 . PHE   B 1  33  ? 5.266   11.475  42.236  1    47.04   ? 33   PHE   B CE1 1 2 
ATOM   5232  C  CE2 . PHE   B 1  33  ? 7.003   10.2    43.271  1    49.292  ? 33   PHE   B CE2 1 2 
ATOM   5233  C  CZ  . PHE   B 1  33  ? 6.465   11.429  42.923  1    47.147  ? 33   PHE   B CZ  1 2 
ATOM   5234  N  N   . GLN   B 1  34  ? 7.038   6.616   40.313  1    44.416  ? 34   GLN   B N   1 2 
ATOM   5235  C  CA  . GLN   B 1  34  ? 8.498   6.75    40.226  1    44.679  ? 34   GLN   B CA  1 2 
ATOM   5236  C  C   . GLN   B 1  34  ? 9.001   6.831   38.759  1    42.616  ? 34   GLN   B C   1 2 
ATOM   5237  O  O   . GLN   B 1  34  ? 10.024  7.471   38.441  1    38.026  ? 34   GLN   B O   1 2 
ATOM   5238  C  CB  . GLN   B 1  34  ? 9.162   5.79    41.232  1    51.394  ? 34   GLN   B CB  1 2 
ATOM   5239  C  CG  . GLN   B 1  34  ? 9.15    4.312   40.843  1    58.509  ? 34   GLN   B CG  1 2 
ATOM   5240  C  CD  . GLN   B 1  34  ? 10.114  3.969   39.717  1    61.845  ? 34   GLN   B CD  1 2 
ATOM   5241  O  OE1 . GLN   B 1  34  ? 11.309  4.273   39.788  1    65.889  ? 34   GLN   B OE1 1 2 
ATOM   5242  N  NE2 . GLN   B 1  34  ? 9.61    3.362   38.645  1    61.983  ? 34   GLN   B NE2 1 2 
ATOM   5243  N  N   . SER   B 1  35  ? 8.291   6.175   37.825  1    44.152  ? 35   SER   B N   1 2 
ATOM   5244  C  CA  . SER   B 1  35  ? 8.569   6.389   36.405  1    41.79   ? 35   SER   B CA  1 2 
ATOM   5245  C  C   . SER   B 1  35  ? 8.207   7.832   36.049  1    38.525  ? 35   SER   B C   1 2 
ATOM   5246  O  O   . SER   B 1  35  ? 9.029   8.555   35.491  1    36.796  ? 35   SER   B O   1 2 
ATOM   5247  C  CB  . SER   B 1  35  ? 7.783   5.46    35.481  1    43.98   ? 35   SER   B CB  1 2 
ATOM   5248  O  OG  . SER   B 1  35  ? 8.038   4.098   35.787  1    52.534  ? 35   SER   B OG  1 2 
ATOM   5249  N  N   . VAL   B 1  36  ? 6.958   8.229   36.323  1    36.118  ? 36   VAL   B N   1 2 
ATOM   5250  C  CA  . VAL   B 1  36  ? 6.536   9.486   35.7    1    33.108  ? 36   VAL   B CA  1 2 
ATOM   5251  C  C   . VAL   B 1  36  ? 7.509   10.539  36.243  1    32.91   ? 36   VAL   B C   1 2 
ATOM   5252  O  O   . VAL   B 1  36  ? 8.077   11.327  35.512  1    32.278  ? 36   VAL   B O   1 2 
ATOM   5253  C  CB  . VAL   B 1  36  ? 5.069   9.875   35.922  1    33.365  ? 36   VAL   B CB  1 2 
ATOM   5254  C  CG1 . VAL   B 1  36  ? 4.786   11.276  35.38   1    32.022  ? 36   VAL   B CG1 1 2 
ATOM   5255  C  CG2 . VAL   B 1  36  ? 4.109   8.875   35.279  1    33.842  ? 36   VAL   B CG2 1 2 
ATOM   5256  N  N   . ALA   B 1  37  ? 7.808   10.447  37.538  1    34.714  ? 37   ALA   B N   1 2 
ATOM   5257  C  CA  . ALA   B 1  37  ? 8.725   11.355  38.229  1    35.975  ? 37   ALA   B CA  1 2 
ATOM   5258  C  C   . ALA   B 1  37  ? 10.091  11.481  37.535  1    35.056  ? 37   ALA   B C   1 2 
ATOM   5259  O  O   . ALA   B 1  37  ? 10.635  12.56   37.367  1    34.919  ? 37   ALA   B O   1 2 
ATOM   5260  C  CB  . ALA   B 1  37  ? 8.842   10.926  39.694  1    36.374  ? 37   ALA   B CB  1 2 
ATOM   5261  N  N   . ALA   B 1  38  ? 10.7    10.366  37.128  1    37.779  ? 38   ALA   B N   1 2 
ATOM   5262  C  CA  . ALA   B 1  38  ? 12.03   10.42   36.526  1    37.648  ? 38   ALA   B CA  1 2 
ATOM   5263  C  C   . ALA   B 1  38  ? 12.024  10.925  35.067  1    34.721  ? 38   ALA   B C   1 2 
ATOM   5264  O  O   . ALA   B 1  38  ? 12.953  11.608  34.616  1    33.495  ? 38   ALA   B O   1 2 
ATOM   5265  C  CB  . ALA   B 1  38  ? 12.677  9.031   36.664  1    40.304  ? 38   ALA   B CB  1 2 
ATOM   5266  N  N   . SER   B 1  39  ? 10.997  10.593  34.28   1    35.617  ? 39   SER   B N   1 2 
ATOM   5267  C  CA  . SER   B 1  39  ? 10.96   11.145  32.923  1    35.129  ? 39   SER   B CA  1 2 
ATOM   5268  C  C   . SER   B 1  39  ? 10.867  12.676  32.996  1    37.186  ? 39   SER   B C   1 2 
ATOM   5269  O  O   . SER   B 1  39  ? 11.474  13.395  32.185  1    33.177  ? 39   SER   B O   1 2 
ATOM   5270  C  CB  . SER   B 1  39  ? 9.81    10.605  32.155  1    36.134  ? 39   SER   B CB  1 2 
ATOM   5271  O  OG  . SER   B 1  39  ? 9.695   9.186   32.207  1    37.574  ? 39   SER   B OG  1 2 
ATOM   5272  N  N   . TRP   B 1  40  ? 10.169  13.157  34.051  1    36.896  ? 40   TRP   B N   1 2 
ATOM   5273  C  CA  . TRP   B 1  40  ? 9.971   14.593  34.238  1    36.289  ? 40   TRP   B CA  1 2 
ATOM   5274  C  C   . TRP   B 1  40  ? 11.306  15.296  34.42   1    35.954  ? 40   TRP   B C   1 2 
ATOM   5275  O  O   . TRP   B 1  40  ? 11.59   16.266  33.719  1    35.113  ? 40   TRP   B O   1 2 
ATOM   5276  C  CB  . TRP   B 1  40  ? 8.985   14.927  35.366  1    34.61   ? 40   TRP   B CB  1 2 
ATOM   5277  C  CG  . TRP   B 1  40  ? 8.966   16.405  35.642  1    33.433  ? 40   TRP   B CG  1 2 
ATOM   5278  C  CD1 . TRP   B 1  40  ? 9.773   17.108  36.482  1    34.933  ? 40   TRP   B CD1 1 2 
ATOM   5279  C  CD2 . TRP   B 1  40  ? 8.108   17.375  34.999  1    32.153  ? 40   TRP   B CD2 1 2 
ATOM   5280  N  NE1 . TRP   B 1  40  ? 9.463   18.443  36.413  1    34.689  ? 40   TRP   B NE1 1 2 
ATOM   5281  C  CE2 . TRP   B 1  40  ? 8.451   18.637  35.527  1    32.421  ? 40   TRP   B CE2 1 2 
ATOM   5282  C  CE3 . TRP   B 1  40  ? 7.078   17.289  34.06   1    28.245  ? 40   TRP   B CE3 1 2 
ATOM   5283  C  CZ2 . TRP   B 1  40  ? 7.792   19.8    35.133  1    32.778  ? 40   TRP   B CZ2 1 2 
ATOM   5284  C  CZ3 . TRP   B 1  40  ? 6.437   18.45   33.666  1    28.191  ? 40   TRP   B CZ3 1 2 
ATOM   5285  C  CH2 . TRP   B 1  40  ? 6.801   19.68   34.183  1    27.586  ? 40   TRP   B CH2 1 2 
ATOM   5286  N  N   . ALA   B 1  41  ? 12.117  14.792  35.365  1    39.965  ? 41   ALA   B N   1 2 
ATOM   5287  C  CA  . ALA   B 1  41  ? 13.452  15.299  35.654  1    38.742  ? 41   ALA   B CA  1 2 
ATOM   5288  C  C   . ALA   B 1  41  ? 14.295  15.423  34.39   1    38.641  ? 41   ALA   B C   1 2 
ATOM   5289  O  O   . ALA   B 1  41  ? 15.052  16.378  34.244  1    40.168  ? 41   ALA   B O   1 2 
ATOM   5290  C  CB  . ALA   B 1  41  ? 14.145  14.391  36.664  1    40.873  ? 41   ALA   B CB  1 2 
ATOM   5291  N  N   . HIS   B 1  42  ? 14.225  14.403  33.523  1    37.401  ? 42   HIS   B N   1 2 
ATOM   5292  C  CA  . HIS   B 1  42  ? 14.949  14.38   32.261  1    38.025  ? 42   HIS   B CA  1 2 
ATOM   5293  C  C   . HIS   B 1  42  ? 14.354  15.353  31.236  1    35.683  ? 42   HIS   B C   1 2 
ATOM   5294  O  O   . HIS   B 1  42  ? 15.077  16.152  30.636  1    32.821  ? 42   HIS   B O   1 2 
ATOM   5295  C  CB  . HIS   B 1  42  ? 14.884  12.954  31.699  1    41.464  ? 42   HIS   B CB  1 2 
ATOM   5296  C  CG  . HIS   B 1  42  ? 15.395  12.814  30.309  1    44.542  ? 42   HIS   B CG  1 2 
ATOM   5297  N  ND1 . HIS   B 1  42  ? 14.57   12.745  29.191  1    45.011  ? 42   HIS   B ND1 1 2 
ATOM   5298  C  CD2 . HIS   B 1  42  ? 16.66   12.707  29.868  1    45.146  ? 42   HIS   B CD2 1 2 
ATOM   5299  C  CE1 . HIS   B 1  42  ? 15.325  12.642  28.108  1    43.913  ? 42   HIS   B CE1 1 2 
ATOM   5300  N  NE2 . HIS   B 1  42  ? 16.588  12.584  28.506  1    45.922  ? 42   HIS   B NE2 1 2 
ATOM   5301  N  N   . ASP   B 1  43  ? 13.021  15.279  31.032  1    33.127  ? 43   ASP   B N   1 2 
ATOM   5302  C  CA  . ASP   B 1  43  ? 12.403  16.082  29.968  1    31.527  ? 43   ASP   B CA  1 2 
ATOM   5303  C  C   . ASP   B 1  43  ? 12.608  17.583  30.209  1    32.452  ? 43   ASP   B C   1 2 
ATOM   5304  O  O   . ASP   B 1  43  ? 12.621  18.357  29.252  1    31.611  ? 43   ASP   B O   1 2 
ATOM   5305  C  CB  . ASP   B 1  43  ? 10.98   15.621  29.651  1    31.684  ? 43   ASP   B CB  1 2 
ATOM   5306  C  CG  . ASP   B 1  43  ? 10.907  14.284  28.908  1    33.127  ? 43   ASP   B CG  1 2 
ATOM   5307  O  OD1 . ASP   B 1  43  ? 11.964  13.637  28.76   1    34.186  ? 43   ASP   B OD1 1 2 
ATOM   5308  O  OD2 . ASP   B 1  43  ? 9.809   13.845  28.594  1    36.263  ? 43   ASP   B OD2 1 2 
ATOM   5309  N  N   . THR   B 1  44  ? 12.784  18.006  31.485  1    32.365  ? 44   THR   B N   1 2 
ATOM   5310  C  CA  . THR   B 1  44  ? 12.913  19.432  31.756  1    33.398  ? 44   THR   B CA  1 2 
ATOM   5311  C  C   . THR   B 1  44  ? 14.377  19.762  32.024  1    38.194  ? 44   THR   B C   1 2 
ATOM   5312  O  O   . THR   B 1  44  ? 14.669  20.84   32.539  1    37.709  ? 44   THR   B O   1 2 
ATOM   5313  C  CB  . THR   B 1  44  ? 12.023  19.882  32.93   1    34.24   ? 44   THR   B CB  1 2 
ATOM   5314  O  OG1 . THR   B 1  44  ? 12.486  19.122  34.04   1    34.65   ? 44   THR   B OG1 1 2 
ATOM   5315  C  CG2 . THR   B 1  44  ? 10.536  19.601  32.749  1    31.539  ? 44   THR   B CG2 1 2 
ATOM   5316  N  N   . ASN   B 1  45  ? 15.28   18.814  31.707  1    37.543  ? 45   ASN   B N   1 2 
ATOM   5317  C  CA  . ASN   B 1  45  ? 16.676  18.914  32.083  1    40.162  ? 45   ASN   B CA  1 2 
ATOM   5318  C  C   . ASN   B 1  45  ? 17.428  17.709  31.502  1    41.361  ? 45   ASN   B C   1 2 
ATOM   5319  O  O   . ASN   B 1  45  ? 17.694  16.733  32.217  1    40.306  ? 45   ASN   B O   1 2 
ATOM   5320  C  CB  . ASN   B 1  45  ? 16.785  19.047  33.606  1    39.493  ? 45   ASN   B CB  1 2 
ATOM   5321  C  CG  . ASN   B 1  45  ? 18.18   19.36   34.1    1    40.631  ? 45   ASN   B CG  1 2 
ATOM   5322  O  OD1 . ASN   B 1  45  ? 19.034  19.828  33.342  1    41.371  ? 45   ASN   B OD1 1 2 
ATOM   5323  N  ND2 . ASN   B 1  45  ? 18.401  19.154  35.389  1    40.646  ? 45   ASN   B ND2 1 2 
ATOM   5324  N  N   . ILE   B 1  46  ? 17.661  17.748  30.174  1    41.863  ? 46   ILE   B N   1 2 
ATOM   5325  C  CA  . ILE   B 1  46  ? 18.239  16.635  29.429  1    40.961  ? 46   ILE   B CA  1 2 
ATOM   5326  C  C   . ILE   B 1  46  ? 19.751  16.524  29.696  1    42.686  ? 46   ILE   B C   1 2 
ATOM   5327  O  O   . ILE   B 1  46  ? 20.534  17.333  29.19   1    41.688  ? 46   ILE   B O   1 2 
ATOM   5328  C  CB  . ILE   B 1  46  ? 17.952  16.736  27.922  1    40.886  ? 46   ILE   B CB  1 2 
ATOM   5329  C  CG1 . ILE   B 1  46  ? 16.452  16.972  27.607  1    36.452  ? 46   ILE   B CG1 1 2 
ATOM   5330  C  CG2 . ILE   B 1  46  ? 18.484  15.486  27.217  1    43.004  ? 46   ILE   B CG2 1 2 
ATOM   5331  C  CD1 . ILE   B 1  46  ? 16.154  17.028  26.127  1    36.409  ? 46   ILE   B CD1 1 2 
ATOM   5332  N  N   . THR   B 1  47  ? 20.131  15.487  30.469  1    43.189  ? 47   THR   B N   1 2 
ATOM   5333  C  CA  . THR   B 1  47  ? 21.518  15.074  30.688  1    42.767  ? 47   THR   B CA  1 2 
ATOM   5334  C  C   . THR   B 1  47  ? 21.627  13.55   30.773  1    43.68   ? 47   THR   B C   1 2 
ATOM   5335  O  O   . THR   B 1  47  ? 20.666  12.822  31.096  1    41.177  ? 47   THR   B O   1 2 
ATOM   5336  C  CB  . THR   B 1  47  ? 22.054  15.696  31.983  1    45.327  ? 47   THR   B CB  1 2 
ATOM   5337  O  OG1 . THR   B 1  47  ? 21.549  14.961  33.102  1    47.339  ? 47   THR   B OG1 1 2 
ATOM   5338  C  CG2 . THR   B 1  47  ? 21.826  17.193  32.108  1    43.516  ? 47   THR   B CG2 1 2 
ATOM   5339  N  N   . ALA   B 1  48  ? 22.881  13.094  30.598  1    49.929  ? 48   ALA   B N   1 2 
ATOM   5340  C  CA  . ALA   B 1  48  ? 23.328  11.722  30.795  1    47.415  ? 48   ALA   B CA  1 2 
ATOM   5341  C  C   . ALA   B 1  48  ? 22.726  11.138  32.07   1    48.617  ? 48   ALA   B C   1 2 
ATOM   5342  O  O   . ALA   B 1  48  ? 22.107  10.059  32.015  1    48.367  ? 48   ALA   B O   1 2 
ATOM   5343  C  CB  . ALA   B 1  48  ? 24.831  11.675  30.797  1    52.758  ? 48   ALA   B CB  1 2 
ATOM   5344  N  N   . GLU   B 1  49  ? 22.826  11.899  33.178  1    48.05   ? 49   GLU   B N   1 2 
ATOM   5345  C  CA  . GLU   B 1  49  ? 22.42   11.441  34.496  1    50.07   ? 49   GLU   B CA  1 2 
ATOM   5346  C  C   . GLU   B 1  49  ? 20.919  11.205  34.561  1    47.418  ? 49   GLU   B C   1 2 
ATOM   5347  O  O   . GLU   B 1  49  ? 20.438  10.154  35.003  1    47.383  ? 49   GLU   B O   1 2 
ATOM   5348  C  CB  . GLU   B 1  49  ? 22.761  12.485  35.559  1    56.029  ? 49   GLU   B CB  1 2 
ATOM   5349  C  CG  . GLU   B 1  49  ? 22.797  11.895  36.961  1    65.102  ? 49   GLU   B CG  1 2 
ATOM   5350  C  CD  . GLU   B 1  49  ? 23.921  10.895  37.155  1    72.917  ? 49   GLU   B CD  1 2 
ATOM   5351  O  OE1 . GLU   B 1  49  ? 24.01   10.345  38.283  1    82.063  ? 49   GLU   B OE1 1 2 
ATOM   5352  O  OE2 . GLU   B 1  49  ? 24.707  10.675  36.198  1    72.061  ? 49   GLU   B OE2 1 2 
ATOM   5353  N  N   . ASN   B 1  50  ? 20.196  12.231  34.123  1    46.432  ? 50   ASN   B N   1 2 
ATOM   5354  C  CA  . ASN   B 1  50  ? 18.752  12.176  34.084  1    42.405  ? 50   ASN   B CA  1 2 
ATOM   5355  C  C   . ASN   B 1  50  ? 18.348  10.96   33.261  1    41.022  ? 50   ASN   B C   1 2 
ATOM   5356  O  O   . ASN   B 1  50  ? 17.506  10.18   33.714  1    42.908  ? 50   ASN   B O   1 2 
ATOM   5357  C  CB  . ASN   B 1  50  ? 18.166  13.57   33.864  1    41.696  ? 50   ASN   B CB  1 2 
ATOM   5358  C  CG  . ASN   B 1  50  ? 18.518  14.541  34.977  1    43.201  ? 50   ASN   B CG  1 2 
ATOM   5359  O  OD1 . ASN   B 1  50  ? 18.661  14.108  36.134  1    42.273  ? 50   ASN   B OD1 1 2 
ATOM   5360  N  ND2 . ASN   B 1  50  ? 18.697  15.824  34.64   1    41.215  ? 50   ASN   B ND2 1 2 
ATOM   5361  N  N   . ALA   B 1  51  ? 19.015  10.753  32.119  1    42.358  ? 51   ALA   B N   1 2 
ATOM   5362  C  CA  . ALA   B 1  51  ? 18.799  9.556   31.296  1    42.032  ? 51   ALA   B CA  1 2 
ATOM   5363  C  C   . ALA   B 1  51  ? 18.987  8.239   32.074  1    41.826  ? 51   ALA   B C   1 2 
ATOM   5364  O  O   . ALA   B 1  51  ? 18.096  7.345   32.129  1    38.698  ? 51   ALA   B O   1 2 
ATOM   5365  C  CB  . ALA   B 1  51  ? 19.613  9.646   30.013  1    44.683  ? 51   ALA   B CB  1 2 
ATOM   5366  N  N   . ARG   B 1  52  ? 20.121  8.157   32.79   1    46.221  ? 52   ARG   B N   1 2 
ATOM   5367  C  CA  . ARG   B 1  52  ? 20.43   6.984   33.595  1    44.19   ? 52   ARG   B CA  1 2 
ATOM   5368  C  C   . ARG   B 1  52  ? 19.274  6.671   34.553  1    45.25   ? 52   ARG   B C   1 2 
ATOM   5369  O  O   . ARG   B 1  52  ? 18.761  5.536   34.587  1    43.328  ? 52   ARG   B O   1 2 
ATOM   5370  C  CB  . ARG   B 1  52  ? 21.823  7.135   34.225  1    50.892  ? 52   ARG   B CB  1 2 
ATOM   5371  C  CG  . ARG   B 1  52  ? 22.695  5.888   34.234  1    53.118  ? 52   ARG   B CG  1 2 
ATOM   5372  C  CD  . ARG   B 1  52  ? 23.37   5.559   35.6    1    58.577  ? 52   ARG   B CD  1 2 
ATOM   5373  N  NE  . ARG   B 1  52  ? 23.54   6.673   36.549  1    59.283  ? 52   ARG   B NE  1 2 
ATOM   5374  C  CZ  . ARG   B 1  52  ? 22.838  6.9     37.682  1    60.696  ? 52   ARG   B CZ  1 2 
ATOM   5375  N  NH1 . ARG   B 1  52  ? 21.829  6.106   38.031  1    59.171  ? 52   ARG   B NH1 1 2 
ATOM   5376  N  NH2 . ARG   B 1  52  ? 23.139  7.928   38.466  1    60.534  ? 52   ARG   B NH2 1 2 
ATOM   5377  N  N   . ARG   B 1  53  ? 18.816  7.716   35.275  1    47.451  ? 53   ARG   B N   1 2 
ATOM   5378  C  CA  . ARG   B 1  53  ? 17.789  7.6     36.298  1    48.153  ? 53   ARG   B CA  1 2 
ATOM   5379  C  C   . ARG   B 1  53  ? 16.514  7.094   35.653  1    45.324  ? 53   ARG   B C   1 2 
ATOM   5380  O  O   . ARG   B 1  53  ? 15.851  6.17    36.144  1    44.722  ? 53   ARG   B O   1 2 
ATOM   5381  C  CB  . ARG   B 1  53  ? 17.549  8.915   37.051  1    52.226  ? 53   ARG   B CB  1 2 
ATOM   5382  C  CG  . ARG   B 1  53  ? 18.808  9.345   37.787  1    56.997  ? 53   ARG   B CG  1 2 
ATOM   5383  C  CD  . ARG   B 1  53  ? 18.503  10.303  38.928  1    60.347  ? 53   ARG   B CD  1 2 
ATOM   5384  N  NE  . ARG   B 1  53  ? 19.607  11.268  38.952  1    64.563  ? 53   ARG   B NE  1 2 
ATOM   5385  C  CZ  . ARG   B 1  53  ? 20.482  11.461  39.938  1    68.185  ? 53   ARG   B CZ  1 2 
ATOM   5386  N  NH1 . ARG   B 1  53  ? 20.422  10.753  41.057  1    68.563  ? 53   ARG   B NH1 1 2 
ATOM   5387  N  NH2 . ARG   B 1  53  ? 21.416  12.386  39.797  1    69.324  ? 53   ARG   B NH2 1 2 
ATOM   5388  N  N   . GLN   B 1  54  ? 16.224  7.692   34.499  1    45.664  ? 54   GLN   B N   1 2 
ATOM   5389  C  CA  . GLN   B 1  54  ? 15.03   7.373   33.754  1    46.046  ? 54   GLN   B CA  1 2 
ATOM   5390  C  C   . GLN   B 1  54  ? 15.027  5.869   33.422  1    43.125  ? 54   GLN   B C   1 2 
ATOM   5391  O  O   . GLN   B 1  54  ? 14.051  5.163   33.69   1    44.043  ? 54   GLN   B O   1 2 
ATOM   5392  C  CB  . GLN   B 1  54  ? 14.989  8.54    32.749  1    48.809  ? 54   GLN   B CB  1 2 
ATOM   5393  C  CG  . GLN   B 1  54  ? 13.757  8.606   31.859  1    53.081  ? 54   GLN   B CG  1 2 
ATOM   5394  C  CD  . GLN   B 1  54  ? 13.842  7.505   30.838  1    52.033  ? 54   GLN   B CD  1 2 
ATOM   5395  O  OE1 . GLN   B 1  54  ? 14.794  7.456   30.043  1    56.957  ? 54   GLN   B OE1 1 2 
ATOM   5396  N  NE2 . GLN   B 1  54  ? 12.935  6.554   30.978  1    46.656  ? 54   GLN   B NE2 1 2 
ATOM   5397  N  N   . GLU   B 1  55  ? 16.13   5.366   32.879  1    43.351  ? 55   GLU   B N   1 2 
ATOM   5398  C  CA  . GLU   B 1  55  ? 16.318  3.937   32.612  1    45.67   ? 55   GLU   B CA  1 2 
ATOM   5399  C  C   . GLU   B 1  55  ? 16.145  3.032   33.846  1    46.358  ? 55   GLU   B C   1 2 
ATOM   5400  O  O   . GLU   B 1  55  ? 15.488  1.971   33.739  1    43.35   ? 55   GLU   B O   1 2 
ATOM   5401  C  CB  . GLU   B 1  55  ? 17.649  3.788   31.879  1    47.428  ? 55   GLU   B CB  1 2 
ATOM   5402  C  CG  . GLU   B 1  55  ? 17.584  4.428   30.494  1    49.257  ? 55   GLU   B CG  1 2 
ATOM   5403  C  CD  . GLU   B 1  55  ? 18.868  4.847   29.785  1    50.093  ? 55   GLU   B CD  1 2 
ATOM   5404  O  OE1 . GLU   B 1  55  ? 19.815  4.064   29.747  1    55.276  ? 55   GLU   B OE1 1 2 
ATOM   5405  O  OE2 . GLU   B 1  55  ? 18.914  5.929   29.184  1    48.542  ? 55   GLU   B OE2 1 2 
ATOM   5406  N  N   . GLU   B 1  56  ? 16.72   3.437   35.01   1    45.893  ? 56   GLU   B N   1 2 
ATOM   5407  C  CA  . GLU   B 1  56  ? 16.548  2.705   36.253  1    46.001  ? 56   GLU   B CA  1 2 
ATOM   5408  C  C   . GLU   B 1  56  ? 15.067  2.473   36.541  1    45.952  ? 56   GLU   B C   1 2 
ATOM   5409  O  O   . GLU   B 1  56  ? 14.693  1.328   36.864  1    44.191  ? 56   GLU   B O   1 2 
ATOM   5410  C  CB  . GLU   B 1  56  ? 17.253  3.323   37.462  1    52.602  ? 56   GLU   B CB  1 2 
ATOM   5411  C  CG  . GLU   B 1  56  ? 18.651  2.764   37.72   1    57.257  ? 56   GLU   B CG  1 2 
ATOM   5412  C  CD  . GLU   B 1  56  ? 19.413  3.333   38.922  1    65.702  ? 56   GLU   B CD  1 2 
ATOM   5413  O  OE1 . GLU   B 1  56  ? 19.899  2.573   39.804  1    67.537  ? 56   GLU   B OE1 1 2 
ATOM   5414  O  OE2 . GLU   B 1  56  ? 19.527  4.579   38.99   1    68.135  ? 56   GLU   B OE2 1 2 
ATOM   5415  N  N   . ALA   B 1  57  ? 14.243  3.543   36.323  1    44.612  ? 57   ALA   B N   1 2 
ATOM   5416  C  CA  . ALA   B 1  57  ? 12.834  3.55    36.676  1    45.034  ? 57   ALA   B CA  1 2 
ATOM   5417  C  C   . ALA   B 1  57  ? 12.07   2.647   35.706  1    45.222  ? 57   ALA   B C   1 2 
ATOM   5418  O  O   . ALA   B 1  57  ? 11.114  1.941   36.08   1    46.771  ? 57   ALA   B O   1 2 
ATOM   5419  C  CB  . ALA   B 1  57  ? 12.288  4.978   36.651  1    42.798  ? 57   ALA   B CB  1 2 
ATOM   5420  N  N   . ALA   B 1  58  ? 12.511  2.692   34.448  1    44.931  ? 58   ALA   B N   1 2 
ATOM   5421  C  CA  . ALA   B 1  58  ? 11.866  1.952   33.382  1    42.684  ? 58   ALA   B CA  1 2 
ATOM   5422  C  C   . ALA   B 1  58  ? 12.016  0.447   33.65   1    43.656  ? 58   ALA   B C   1 2 
ATOM   5423  O  O   . ALA   B 1  58  ? 11.044  -0.314  33.591  1    45.57   ? 58   ALA   B O   1 2 
ATOM   5424  C  CB  . ALA   B 1  58  ? 12.405  2.41    32.036  1    41.941  ? 58   ALA   B CB  1 2 
ATOM   5425  N  N   . LEU   B 1  59  ? 13.209  0.037   34.055  1    45.372  ? 59   LEU   B N   1 2 
ATOM   5426  C  CA  . LEU   B 1  59  ? 13.499  -1.312  34.554  1    48.243  ? 59   LEU   B CA  1 2 
ATOM   5427  C  C   . LEU   B 1  59  ? 12.629  -1.783  35.734  1    49.05   ? 59   LEU   B C   1 2 
ATOM   5428  O  O   . LEU   B 1  59  ? 12.191  -2.949  35.775  1    47.538  ? 59   LEU   B O   1 2 
ATOM   5429  C  CB  . LEU   B 1  59  ? 14.974  -1.302  34.941  1    50.298  ? 59   LEU   B CB  1 2 
ATOM   5430  C  CG  . LEU   B 1  59  ? 15.982  -1.577  33.808  1    56.411  ? 59   LEU   B CG  1 2 
ATOM   5431  C  CD1 . LEU   B 1  59  ? 17.421  -1.629  34.334  1    54.992  ? 59   LEU   B CD1 1 2 
ATOM   5432  C  CD2 . LEU   B 1  59  ? 15.689  -2.835  32.957  1    56.279  ? 59   LEU   B CD2 1 2 
ATOM   5433  N  N   . LEU   B 1  60  ? 12.457  -0.921  36.754  1    47.751  ? 60   LEU   B N   1 2 
ATOM   5434  C  CA  . LEU   B 1  60  ? 11.629  -1.252  37.901  1    46.775  ? 60   LEU   B CA  1 2 
ATOM   5435  C  C   . LEU   B 1  60  ? 10.182  -1.498  37.456  1    46.932  ? 60   LEU   B C   1 2 
ATOM   5436  O  O   . LEU   B 1  60  ? 9.508   -2.399  37.991  1    47.537  ? 60   LEU   B O   1 2 
ATOM   5437  C  CB  . LEU   B 1  60  ? 11.718  -0.149  38.962  1    48.684  ? 60   LEU   B CB  1 2 
ATOM   5438  C  CG  . LEU   B 1  60  ? 12.996  -0.062  39.82   1    51.909  ? 60   LEU   B CG  1 2 
ATOM   5439  C  CD1 . LEU   B 1  60  ? 12.882  0.932   40.972  1    52.264  ? 60   LEU   B CD1 1 2 
ATOM   5440  C  CD2 . LEU   B 1  60  ? 13.55   -1.391  40.378  1    55.024  ? 60   LEU   B CD2 1 2 
ATOM   5441  N  N   . SER   B 1  61  ? 9.716   -0.698  36.463  1    44.466  ? 61   SER   B N   1 2 
ATOM   5442  C  CA  . SER   B 1  61  ? 8.367   -0.858  35.937  1    45.99   ? 61   SER   B CA  1 2 
ATOM   5443  C  C   . SER   B 1  61  ? 8.219   -2.228  35.289  1    46.835  ? 61   SER   B C   1 2 
ATOM   5444  O  O   . SER   B 1  61  ? 7.227   -2.94   35.513  1    50.899  ? 61   SER   B O   1 2 
ATOM   5445  C  CB  . SER   B 1  61  ? 7.97    0.228   34.936  1    43.211  ? 61   SER   B CB  1 2 
ATOM   5446  O  OG  . SER   B 1  61  ? 8.013   1.475   35.6    1    46.809  ? 61   SER   B OG  1 2 
ATOM   5447  N  N   . GLN   B 1  62  ? 9.201   -2.573  34.468  1    44.949  ? 62   GLN   B N   1 2 
ATOM   5448  C  CA  . GLN   B 1  62  ? 9.11    -3.856  33.779  1    48.119  ? 62   GLN   B CA  1 2 
ATOM   5449  C  C   . GLN   B 1  62  ? 9.075   -5.003  34.818  1    48.595  ? 62   GLN   B C   1 2 
ATOM   5450  O  O   . GLN   B 1  62  ? 8.336   -6.002  34.711  1    47.652  ? 62   GLN   B O   1 2 
ATOM   5451  C  CB  . GLN   B 1  62  ? 10.241  -3.869  32.737  1    48.305  ? 62   GLN   B CB  1 2 
ATOM   5452  C  CG  . GLN   B 1  62  ? 10.118  -2.827  31.617  1    49.711  ? 62   GLN   B CG  1 2 
ATOM   5453  C  CD  . GLN   B 1  62  ? 11.444  -2.425  30.988  1    48.521  ? 62   GLN   B CD  1 2 
ATOM   5454  O  OE1 . GLN   B 1  62  ? 12.508  -2.457  31.618  1    52.096  ? 62   GLN   B OE1 1 2 
ATOM   5455  N  NE2 . GLN   B 1  62  ? 11.391  -2.01   29.727  1    52.69   ? 62   GLN   B NE2 1 2 
ATOM   5456  N  N   . GLU   B 1  63  ? 9.871   -4.865  35.878  1    50.213  ? 63   GLU   B N   1 2 
ATOM   5457  C  CA  . GLU   B 1  63  ? 9.932   -5.934  36.875  1    51.289  ? 63   GLU   B CA  1 2 
ATOM   5458  C  C   . GLU   B 1  63  ? 8.551   -6.135  37.518  1    51.278  ? 63   GLU   B C   1 2 
ATOM   5459  O  O   . GLU   B 1  63  ? 8.086   -7.28   37.632  1    51.914  ? 63   GLU   B O   1 2 
ATOM   5460  C  CB  . GLU   B 1  63  ? 11.135  -5.75   37.798  1    53.76   ? 63   GLU   B CB  1 2 
ATOM   5461  C  CG  . GLU   B 1  63  ? 12.329  -5.12   37.072  1    57.031  ? 63   GLU   B CG  1 2 
ATOM   5462  C  CD  . GLU   B 1  63  ? 13.773  -5.279  37.562  1    64.421  ? 63   GLU   B CD  1 2 
ATOM   5463  O  OE1 . GLU   B 1  63  ? 14.016  -4.828  38.716  1    66.465  ? 63   GLU   B OE1 1 2 
ATOM   5464  O  OE2 . GLU   B 1  63  ? 14.652  -5.831  36.805  1    61.392  ? 63   GLU   B OE2 1 2 
ATOM   5465  N  N   . PHE   B 1  64  ? 7.919   -5.017  37.901  1    47.324  ? 64   PHE   B N   1 2 
ATOM   5466  C  CA  . PHE   B 1  64  ? 6.564   -4.976  38.41   1    49.341  ? 64   PHE   B CA  1 2 
ATOM   5467  C  C   . PHE   B 1  64  ? 5.62    -5.658  37.414  1    50.248  ? 64   PHE   B C   1 2 
ATOM   5468  O  O   . PHE   B 1  64  ? 4.873   -6.563  37.8    1    54.541  ? 64   PHE   B O   1 2 
ATOM   5469  C  CB  . PHE   B 1  64  ? 6.124   -3.522  38.705  1    48.237  ? 64   PHE   B CB  1 2 
ATOM   5470  C  CG  . PHE   B 1  64  ? 4.734   -3.374  39.331  1    48.131  ? 64   PHE   B CG  1 2 
ATOM   5471  C  CD1 . PHE   B 1  64  ? 4.545   -3.529  40.714  1    50.788  ? 64   PHE   B CD1 1 2 
ATOM   5472  C  CD2 . PHE   B 1  64  ? 3.605   -3.153  38.527  1    46.303  ? 64   PHE   B CD2 1 2 
ATOM   5473  C  CE1 . PHE   B 1  64  ? 3.263   -3.431  41.267  1    51.731  ? 64   PHE   B CE1 1 2 
ATOM   5474  C  CE2 . PHE   B 1  64  ? 2.324   -3.066  39.077  1    46.463  ? 64   PHE   B CE2 1 2 
ATOM   5475  C  CZ  . PHE   B 1  64  ? 2.154   -3.178  40.443  1    48.72   ? 64   PHE   B CZ  1 2 
ATOM   5476  N  N   . ALA   B 1  65  ? 5.645   -5.2    36.151  1    47.739  ? 65   ALA   B N   1 2 
ATOM   5477  C  CA  . ALA   B 1  65  ? 4.754   -5.698  35.11   1    48.382  ? 65   ALA   B CA  1 2 
ATOM   5478  C  C   . ALA   B 1  65  ? 4.973   -7.197  34.914  1    50.74   ? 65   ALA   B C   1 2 
ATOM   5479  O  O   . ALA   B 1  65  ? 4.001   -7.956  34.91   1    54.894  ? 65   ALA   B O   1 2 
ATOM   5480  C  CB  . ALA   B 1  65  ? 4.927   -4.917  33.82   1    46.428  ? 65   ALA   B CB  1 2 
ATOM   5481  N  N   . GLU   B 1  66  ? 6.239   -7.628  34.857  1    49.369  ? 66   GLU   B N   1 2 
ATOM   5482  C  CA  . GLU   B 1  66  ? 6.563   -9.044  34.76   1    52.98   ? 66   GLU   B CA  1 2 
ATOM   5483  C  C   . GLU   B 1  66  ? 5.877   -9.827  35.896  1    55.945  ? 66   GLU   B C   1 2 
ATOM   5484  O  O   . GLU   B 1  66  ? 5.073   -10.746 35.659  1    55.834  ? 66   GLU   B O   1 2 
ATOM   5485  C  CB  . GLU   B 1  66  ? 8.093   -9.135  34.755  1    55.729  ? 66   GLU   B CB  1 2 
ATOM   5486  C  CG  . GLU   B 1  66  ? 8.644   -10.485 34.286  1    63.53   ? 66   GLU   B CG  1 2 
ATOM   5487  C  CD  . GLU   B 1  66  ? 10.136  -10.788 34.454  1    67.139  ? 66   GLU   B CD  1 2 
ATOM   5488  O  OE1 . GLU   B 1  66  ? 10.609  -11.839 33.953  1    69.826  ? 66   GLU   B OE1 1 2 
ATOM   5489  O  OE2 . GLU   B 1  66  ? 10.848  -9.976  35.085  1    68.766  ? 66   GLU   B OE2 1 2 
ATOM   5490  N  N   . ALA   B 1  67  ? 6.201   -9.454  37.145  1    56.369  ? 67   ALA   B N   1 2 
ATOM   5491  C  CA  . ALA   B 1  67  ? 5.719   -10.155 38.337  1    55.789  ? 67   ALA   B CA  1 2 
ATOM   5492  C  C   . ALA   B 1  67  ? 4.186   -10.283 38.323  1    55.196  ? 67   ALA   B C   1 2 
ATOM   5493  O  O   . ALA   B 1  67  ? 3.644   -11.372 38.527  1    56.355  ? 67   ALA   B O   1 2 
ATOM   5494  C  CB  . ALA   B 1  67  ? 6.216   -9.451  39.567  1    55.471  ? 67   ALA   B CB  1 2 
ATOM   5495  N  N   . TRP   B 1  68  ? 3.485   -9.167  38.063  1    52.57   ? 68   TRP   B N   1 2 
ATOM   5496  C  CA  . TRP   B 1  68  ? 2.039   -9.109  38.174  1    53.105  ? 68   TRP   B CA  1 2 
ATOM   5497  C  C   . TRP   B 1  68  ? 1.333   -9.764  36.981  1    55.454  ? 68   TRP   B C   1 2 
ATOM   5498  O  O   . TRP   B 1  68  ? 0.328   -10.466 37.176  1    57.899  ? 68   TRP   B O   1 2 
ATOM   5499  C  CB  . TRP   B 1  68  ? 1.617   -7.652  38.403  1    51.554  ? 68   TRP   B CB  1 2 
ATOM   5500  C  CG  . TRP   B 1  68  ? 1.876   -7.269  39.824  1    53.26   ? 68   TRP   B CG  1 2 
ATOM   5501  C  CD1 . TRP   B 1  68  ? 3.029   -6.81   40.407  1    53.973  ? 68   TRP   B CD1 1 2 
ATOM   5502  C  CD2 . TRP   B 1  68  ? 0.921   -7.472  40.891  1    54.863  ? 68   TRP   B CD2 1 2 
ATOM   5503  N  NE1 . TRP   B 1  68  ? 2.836   -6.65   41.76   1    53.574  ? 68   TRP   B NE1 1 2 
ATOM   5504  C  CE2 . TRP   B 1  68  ? 1.561   -7.052  42.084  1    55.067  ? 68   TRP   B CE2 1 2 
ATOM   5505  C  CE3 . TRP   B 1  68  ? -0.405  -7.948  40.928  1    55.028  ? 68   TRP   B CE3 1 2 
ATOM   5506  C  CZ2 . TRP   B 1  68  ? 0.905   -7.104  43.316  1    56.109  ? 68   TRP   B CZ2 1 2 
ATOM   5507  C  CZ3 . TRP   B 1  68  ? -1.051  -8.002  42.147  1    56.807  ? 68   TRP   B CZ3 1 2 
ATOM   5508  C  CH2 . TRP   B 1  68  ? -0.396  -7.57   43.309  1    57.399  ? 68   TRP   B CH2 1 2 
ATOM   5509  N  N   . GLY   B 1  69  ? 1.887   -9.582  35.762  1    53.468  ? 69   GLY   B N   1 2 
ATOM   5510  C  CA  . GLY   B 1  69  ? 1.382   -10.257 34.575  1    56.027  ? 69   GLY   B CA  1 2 
ATOM   5511  C  C   . GLY   B 1  69  ? 1.555   -11.775 34.615  1    62.036  ? 69   GLY   B C   1 2 
ATOM   5512  O  O   . GLY   B 1  69  ? 0.648   -12.534 34.27   1    65.972  ? 69   GLY   B O   1 2 
ATOM   5513  N  N   . GLN   B 1  70  ? 2.73    -12.225 35.043  1    67.004  ? 70   GLN   B N   1 2 
ATOM   5514  C  CA  . GLN   B 1  70  ? 2.976   -13.652 35.204  1    72.051  ? 70   GLN   B CA  1 2 
ATOM   5515  C  C   . GLN   B 1  70  ? 2.024   -14.262 36.228  1    71.937  ? 70   GLN   B C   1 2 
ATOM   5516  O  O   . GLN   B 1  70  ? 1.613   -15.416 36.11   1    70.659  ? 70   GLN   B O   1 2 
ATOM   5517  C  CB  . GLN   B 1  70  ? 4.409   -13.87  35.682  1    78.422  ? 70   GLN   B CB  1 2 
ATOM   5518  C  CG  . GLN   B 1  70  ? 5.413   -13.215 34.738  1    82.73   ? 70   GLN   B CG  1 2 
ATOM   5519  C  CD  . GLN   B 1  70  ? 6.792   -13.831 34.784  1    89.732  ? 70   GLN   B CD  1 2 
ATOM   5520  O  OE1 . GLN   B 1  70  ? 7.166   -14.521 35.742  1    93.783  ? 70   GLN   B OE1 1 2 
ATOM   5521  N  NE2 . GLN   B 1  70  ? 7.554   -13.582 33.728  1    89.913  ? 70   GLN   B NE2 1 2 
ATOM   5522  N  N   . LYS   B 1  71  ? 1.689   -13.481 37.251  1    72.352  ? 71   LYS   B N   1 2 
ATOM   5523  C  CA  . LYS   B 1  71  ? 0.817   -13.993 38.291  1    71.907  ? 71   LYS   B CA  1 2 
ATOM   5524  C  C   . LYS   B 1  71  ? -0.605  -14.106 37.733  1    72.95   ? 71   LYS   B C   1 2 
ATOM   5525  O  O   . LYS   B 1  71  ? -1.297  -15.086 38.032  1    74.659  ? 71   LYS   B O   1 2 
ATOM   5526  C  CB  . LYS   B 1  71  ? 0.965   -13.14  39.553  1    72.703  ? 71   LYS   B CB  1 2 
ATOM   5527  C  CG  . LYS   B 1  71  ? 0.445   -13.798 40.824  1    79.389  ? 71   LYS   B CG  1 2 
ATOM   5528  C  CD  . LYS   B 1  71  ? 1.311   -14.902 41.427  1    81.215  ? 71   LYS   B CD  1 2 
ATOM   5529  C  CE  . LYS   B 1  71  ? 0.566   -15.509 42.56   1    85.135  ? 71   LYS   B CE  1 2 
ATOM   5530  N  NZ  . LYS   B 1  71  ? 1.45    -15.97  43.636  1    89.72   ? 71   LYS   B NZ  1 2 
ATOM   5531  N  N   . ALA   B 1  72  ? -0.999  -13.138 36.873  1    71.394  ? 72   ALA   B N   1 2 
ATOM   5532  C  CA  . ALA   B 1  72  ? -2.359  -13.094 36.348  1    71.814  ? 72   ALA   B CA  1 2 
ATOM   5533  C  C   . ALA   B 1  72  ? -2.584  -14.216 35.336  1    75.926  ? 72   ALA   B C   1 2 
ATOM   5534  O  O   . ALA   B 1  72  ? -3.686  -14.779 35.244  1    75.943  ? 72   ALA   B O   1 2 
ATOM   5535  C  CB  . ALA   B 1  72  ? -2.691  -11.742 35.77   1    66.961  ? 72   ALA   B CB  1 2 
ATOM   5536  N  N   . LYS   B 1  73  ? -1.51   -14.554 34.612  1    77.219  ? 73   LYS   B N   1 2 
ATOM   5537  C  CA  . LYS   B 1  73  ? -1.504  -15.74  33.77   1    79.286  ? 73   LYS   B CA  1 2 
ATOM   5538  C  C   . LYS   B 1  73  ? -1.719  -16.981 34.631  1    81.497  ? 73   LYS   B C   1 2 
ATOM   5539  O  O   . LYS   B 1  73  ? -2.658  -17.74  34.397  1    87.027  ? 73   LYS   B O   1 2 
ATOM   5540  C  CB  . LYS   B 1  73  ? -0.242  -15.763 32.908  1    81.594  ? 73   LYS   B CB  1 2 
ATOM   5541  C  CG  . LYS   B 1  73  ? -0.127  -14.565 31.962  1    80.576  ? 73   LYS   B CG  1 2 
ATOM   5542  C  CD  . LYS   B 1  73  ? 0.99    -14.811 30.96   1    79.726  ? 73   LYS   B CD  1 2 
ATOM   5543  C  CE  . LYS   B 1  73  ? 1.82    -13.596 30.792  1    79.055  ? 73   LYS   B CE  1 2 
ATOM   5544  N  NZ  . LYS   B 1  73  ? 3.182   -14.027 30.469  1    79.304  ? 73   LYS   B NZ  1 2 
ATOM   5545  N  N   . GLU   B 1  74  ? -0.866  -17.17  35.645  1    81.596  ? 74   GLU   B N   1 2 
ATOM   5546  C  CA  . GLU   B 1  74  ? -1.003  -18.297 36.554  1    83.268  ? 74   GLU   B CA  1 2 
ATOM   5547  C  C   . GLU   B 1  74  ? -2.445  -18.454 37.028  1    83.343  ? 74   GLU   B C   1 2 
ATOM   5548  O  O   . GLU   B 1  74  ? -3.004  -19.549 36.983  1    84.595  ? 74   GLU   B O   1 2 
ATOM   5549  C  CB  . GLU   B 1  74  ? -0.108  -18.19  37.786  1    87.717  ? 74   GLU   B CB  1 2 
ATOM   5550  C  CG  . GLU   B 1  74  ? 1.059   -19.171 37.772  1    93.736  ? 74   GLU   B CG  1 2 
ATOM   5551  C  CD  . GLU   B 1  74  ? 2.252   -18.423 38.327  1    96.976  ? 74   GLU   B CD  1 2 
ATOM   5552  O  OE1 . GLU   B 1  74  ? 2.215   -18.101 39.539  1    95.379  ? 74   GLU   B OE1 1 2 
ATOM   5553  O  OE2 . GLU   B 1  74  ? 3.171   -18.104 37.53   1    96.059  ? 74   GLU   B OE2 1 2 
ATOM   5554  N  N   . LEU   B 1  75  ? -3.032  -17.359 37.516  1    82.092  ? 75   LEU   B N   1 2 
ATOM   5555  C  CA  . LEU   B 1  75  ? -4.277  -17.46  38.251  1    82.167  ? 75   LEU   B CA  1 2 
ATOM   5556  C  C   . LEU   B 1  75  ? -5.473  -17.493 37.303  1    84.68   ? 75   LEU   B C   1 2 
ATOM   5557  O  O   . LEU   B 1  75  ? -6.361  -18.325 37.478  1    88.379  ? 75   LEU   B O   1 2 
ATOM   5558  C  CB  . LEU   B 1  75  ? -4.391  -16.335 39.272  1    78.792  ? 75   LEU   B CB  1 2 
ATOM   5559  C  CG  . LEU   B 1  75  ? -3.44   -16.392 40.471  1    79.451  ? 75   LEU   B CG  1 2 
ATOM   5560  C  CD1 . LEU   B 1  75  ? -3.701  -15.176 41.343  1    76.464  ? 75   LEU   B CD1 1 2 
ATOM   5561  C  CD2 . LEU   B 1  75  ? -3.595  -17.678 41.277  1    82.178  ? 75   LEU   B CD2 1 2 
ATOM   5562  N  N   . TYR   B 1  76  ? -5.478  -16.602 36.304  1    82.908  ? 76   TYR   B N   1 2 
ATOM   5563  C  CA  . TYR   B 1  76  ? -6.715  -16.21  35.646  1    85.861  ? 76   TYR   B CA  1 2 
ATOM   5564  C  C   . TYR   B 1  76  ? -6.734  -16.571 34.159  1    90.24   ? 76   TYR   B C   1 2 
ATOM   5565  O  O   . TYR   B 1  76  ? -7.811  -16.605 33.564  1    88.305  ? 76   TYR   B O   1 2 
ATOM   5566  C  CB  . TYR   B 1  76  ? -6.901  -14.718 35.952  1    83.686  ? 76   TYR   B CB  1 2 
ATOM   5567  C  CG  . TYR   B 1  76  ? -6.923  -14.469 37.455  1    80.501  ? 76   TYR   B CG  1 2 
ATOM   5568  C  CD1 . TYR   B 1  76  ? -7.789  -15.184 38.283  1    82.355  ? 76   TYR   B CD1 1 2 
ATOM   5569  C  CD2 . TYR   B 1  76  ? -6.018  -13.596 38.053  1    76.573  ? 76   TYR   B CD2 1 2 
ATOM   5570  C  CE1 . TYR   B 1  76  ? -7.793  -14.996 39.658  1    83.389  ? 76   TYR   B CE1 1 2 
ATOM   5571  C  CE2 . TYR   B 1  76  ? -6.019  -13.399 39.425  1    76.447  ? 76   TYR   B CE2 1 2 
ATOM   5572  C  CZ  . TYR   B 1  76  ? -6.905  -14.098 40.234  1    80.886  ? 76   TYR   B CZ  1 2 
ATOM   5573  O  OH  . TYR   B 1  76  ? -6.919  -13.925 41.594  1    79.661  ? 76   TYR   B OH  1 2 
ATOM   5574  N  N   . GLU   B 1  77  ? -5.558  -16.836 33.565  1    94.458  ? 77   GLU   B N   1 2 
ATOM   5575  C  CA  . GLU   B 1  77  ? -5.444  -17.096 32.133  1    98.016  ? 77   GLU   B CA  1 2 
ATOM   5576  C  C   . GLU   B 1  77  ? -6.536  -18.075 31.688  1    101.067 ? 77   GLU   B C   1 2 
ATOM   5577  O  O   . GLU   B 1  77  ? -7.188  -17.839 30.67   1    97.982  ? 77   GLU   B O   1 2 
ATOM   5578  C  CB  . GLU   B 1  77  ? -4.032  -17.517 31.712  1    100.554 ? 77   GLU   B CB  1 2 
ATOM   5579  C  CG  . GLU   B 1  77  ? -3.744  -17.348 30.221  1    100.867 ? 77   GLU   B CG  1 2 
ATOM   5580  C  CD  . GLU   B 1  77  ? -3.515  -15.926 29.728  1    103.666 ? 77   GLU   B CD  1 2 
ATOM   5581  O  OE1 . GLU   B 1  77  ? -2.41   -15.642 29.211  1    103.789 ? 77   GLU   B OE1 1 2 
ATOM   5582  O  OE2 . GLU   B 1  77  ? -4.441  -15.097 29.85   1    102.75  ? 77   GLU   B OE2 1 2 
ATOM   5583  N  N   . PRO   B 1  78  ? -6.796  -19.189 32.421  1    102.776 ? 78   PRO   B N   1 2 
ATOM   5584  C  CA  . PRO   B 1  78  ? -7.981  -20.014 32.161  1    105.69  ? 78   PRO   B CA  1 2 
ATOM   5585  C  C   . PRO   B 1  78  ? -9.318  -19.301 31.913  1    104.65  ? 78   PRO   B C   1 2 
ATOM   5586  O  O   . PRO   B 1  78  ? -9.919  -19.499 30.859  1    103.493 ? 78   PRO   B O   1 2 
ATOM   5587  C  CB  . PRO   B 1  78  ? -8.02   -20.965 33.388  1    104.302 ? 78   PRO   B CB  1 2 
ATOM   5588  C  CG  . PRO   B 1  78  ? -6.565  -21.122 33.78   1    102.462 ? 78   PRO   B CG  1 2 
ATOM   5589  C  CD  . PRO   B 1  78  ? -5.952  -19.756 33.491  1    105.58  ? 78   PRO   B CD  1 2 
ATOM   5590  N  N   . ILE   B 1  79  ? -9.744  -18.43  32.849  1    99.212  ? 79   ILE   B N   1 2 
ATOM   5591  C  CA  . ILE   B 1  79  ? -11.164 -18.2   33.111  1    93.592  ? 79   ILE   B CA  1 2 
ATOM   5592  C  C   . ILE   B 1  79  ? -11.622 -16.739 32.977  1    91.452  ? 79   ILE   B C   1 2 
ATOM   5593  O  O   . ILE   B 1  79  ? -12.821 -16.48  33.086  1    86.707  ? 79   ILE   B O   1 2 
ATOM   5594  C  CB  . ILE   B 1  79  ? -11.551 -18.803 34.477  1    94.247  ? 79   ILE   B CB  1 2 
ATOM   5595  C  CG1 . ILE   B 1  79  ? -10.602 -18.348 35.608  1    90.664  ? 79   ILE   B CG1 1 2 
ATOM   5596  C  CG2 . ILE   B 1  79  ? -11.649 -20.33  34.39   1    95.194  ? 79   ILE   B CG2 1 2 
ATOM   5597  C  CD1 . ILE   B 1  79  ? -10.947 -18.91  36.981  1    91.835  ? 79   ILE   B CD1 1 2 
ATOM   5598  N  N   . TRP   B 1  80  ? -10.704 -15.793 32.713  1    89.898  ? 80   TRP   B N   1 2 
ATOM   5599  C  CA  . TRP   B 1  80  ? -10.997 -14.374 32.908  1    95.826  ? 80   TRP   B CA  1 2 
ATOM   5600  C  C   . TRP   B 1  80  ? -11.939 -13.79  31.85   1    97.287  ? 80   TRP   B C   1 2 
ATOM   5601  O  O   . TRP   B 1  80  ? -12.647 -12.821 32.127  1    91.694  ? 80   TRP   B O   1 2 
ATOM   5602  C  CB  . TRP   B 1  80  ? -9.716  -13.534 33.045  1    96.006  ? 80   TRP   B CB  1 2 
ATOM   5603  C  CG  . TRP   B 1  80  ? -8.938  -13.314 31.772  1    96.447  ? 80   TRP   B CG  1 2 
ATOM   5604  C  CD1 . TRP   B 1  80  ? -7.856  -14.028 31.343  1    96.582  ? 80   TRP   B CD1 1 2 
ATOM   5605  C  CD2 . TRP   B 1  80  ? -9.159  -12.288 30.775  1    94.64   ? 80   TRP   B CD2 1 2 
ATOM   5606  N  NE1 . TRP   B 1  80  ? -7.388  -13.526 30.157  1    93.117  ? 80   TRP   B NE1 1 2 
ATOM   5607  C  CE2 . TRP   B 1  80  ? -8.166  -12.462 29.781  1    94.26   ? 80   TRP   B CE2 1 2 
ATOM   5608  C  CE3 . TRP   B 1  80  ? -10.091 -11.251 30.623  1    92.69   ? 80   TRP   B CE3 1 2 
ATOM   5609  C  CZ2 . TRP   B 1  80  ? -8.085  -11.639 28.656  1    92.75   ? 80   TRP   B CZ2 1 2 
ATOM   5610  C  CZ3 . TRP   B 1  80  ? -10.009 -10.438 29.512  1    93.603  ? 80   TRP   B CZ3 1 2 
ATOM   5611  C  CH2 . TRP   B 1  80  ? -9.019  -10.631 28.542  1    92.832  ? 80   TRP   B CH2 1 2 
ATOM   5612  N  N   . GLN   B 1  81  ? -11.937 -14.365 30.637  1    101.887 ? 81   GLN   B N   1 2 
ATOM   5613  C  CA  . GLN   B 1  81  ? -12.79  -13.878 29.56   1    98.731  ? 81   GLN   B CA  1 2 
ATOM   5614  C  C   . GLN   B 1  81  ? -14.266 -14.162 29.856  1    100.863 ? 81   GLN   B C   1 2 
ATOM   5615  O  O   . GLN   B 1  81  ? -15.138 -13.666 29.142  1    100.544 ? 81   GLN   B O   1 2 
ATOM   5616  C  CB  . GLN   B 1  81  ? -12.332 -14.345 28.175  1    95.423  ? 81   GLN   B CB  1 2 
ATOM   5617  C  CG  . GLN   B 1  81  ? -11.106 -13.6   27.651  1    95.205  ? 81   GLN   B CG  1 2 
ATOM   5618  C  CD  . GLN   B 1  81  ? -10.872 -13.723 26.158  1    92.239  ? 81   GLN   B CD  1 2 
ATOM   5619  O  OE1 . GLN   B 1  81  ? -10.455 -14.773 25.65   1    90.728  ? 81   GLN   B OE1 1 2 
ATOM   5620  N  NE2 . GLN   B 1  81  ? -11.11  -12.631 25.442  1    86.143  ? 81   GLN   B NE2 1 2 
ATOM   5621  N  N   . GLN   B 1  82  ? -14.538 -14.911 30.939  1    95.836  ? 82   GLN   B N   1 2 
ATOM   5622  C  CA  . GLN   B 1  82  ? -15.869 -15.43  31.214  1    95.582  ? 82   GLN   B CA  1 2 
ATOM   5623  C  C   . GLN   B 1  82  ? -16.427 -14.907 32.543  1    94.621  ? 82   GLN   B C   1 2 
ATOM   5624  O  O   . GLN   B 1  82  ? -17.442 -15.417 33.025  1    98.332  ? 82   GLN   B O   1 2 
ATOM   5625  C  CB  . GLN   B 1  82  ? -15.808 -16.954 31.074  1    99.347  ? 82   GLN   B CB  1 2 
ATOM   5626  C  CG  . GLN   B 1  82  ? -15.481 -17.423 29.656  1    97.164  ? 82   GLN   B CG  1 2 
ATOM   5627  C  CD  . GLN   B 1  82  ? -14.552 -18.619 29.592  1    96.752  ? 82   GLN   B CD  1 2 
ATOM   5628  O  OE1 . GLN   B 1  82  ? -14.81  -19.684 30.17   1    99.821  ? 82   GLN   B OE1 1 2 
ATOM   5629  N  NE2 . GLN   B 1  82  ? -13.453 -18.452 28.869  1    91.819  ? 82   GLN   B NE2 1 2 
ATOM   5630  N  N   . PHE   B 1  83  ? -15.782 -13.883 33.127  1    89.605  ? 83   PHE   B N   1 2 
ATOM   5631  C  CA  . PHE   B 1  83  ? -16.321 -13.192 34.296  1    88.059  ? 83   PHE   B CA  1 2 
ATOM   5632  C  C   . PHE   B 1  83  ? -17.471 -12.282 33.87   1    86.631  ? 83   PHE   B C   1 2 
ATOM   5633  O  O   . PHE   B 1  83  ? -17.327 -11.52  32.914  1    85.097  ? 83   PHE   B O   1 2 
ATOM   5634  C  CB  . PHE   B 1  83  ? -15.307 -12.271 34.983  1    85.781  ? 83   PHE   B CB  1 2 
ATOM   5635  C  CG  . PHE   B 1  83  ? -14.128 -12.96  35.65   1    85.667  ? 83   PHE   B CG  1 2 
ATOM   5636  C  CD1 . PHE   B 1  83  ? -14.242 -14.262 36.146  1    87.902  ? 83   PHE   B CD1 1 2 
ATOM   5637  C  CD2 . PHE   B 1  83  ? -12.912 -12.293 35.788  1    83.454  ? 83   PHE   B CD2 1 2 
ATOM   5638  C  CE1 . PHE   B 1  83  ? -13.162 -14.886 36.755  1    88.055  ? 83   PHE   B CE1 1 2 
ATOM   5639  C  CE2 . PHE   B 1  83  ? -11.831 -12.917 36.395  1    85.264  ? 83   PHE   B CE2 1 2 
ATOM   5640  C  CZ  . PHE   B 1  83  ? -11.96  -14.21  36.882  1    89.912  ? 83   PHE   B CZ  1 2 
ATOM   5641  N  N   . THR   B 1  84  ? -18.584 -12.331 34.616  1    88.244  ? 84   THR   B N   1 2 
ATOM   5642  C  CA  . THR   B 1  84  ? -19.778 -11.544 34.322  1    90.849  ? 84   THR   B CA  1 2 
ATOM   5643  C  C   . THR   B 1  84  ? -19.482 -10.036 34.367  1    89.052  ? 84   THR   B C   1 2 
ATOM   5644  O  O   . THR   B 1  84  ? -19.928 -9.293  33.493  1    89.013  ? 84   THR   B O   1 2 
ATOM   5645  C  CB  . THR   B 1  84  ? -20.946 -11.944 35.233  1    94.314  ? 84   THR   B CB  1 2 
ATOM   5646  O  OG1 . THR   B 1  84  ? -20.562 -11.541 36.544  1    95.394  ? 84   THR   B OG1 1 2 
ATOM   5647  C  CG2 . THR   B 1  84  ? -21.288 -13.425 35.194  1    91.611  ? 84   THR   B CG2 1 2 
ATOM   5648  N  N   . ASP   B 1  85  ? -18.724 -9.589  35.38   1    87.655  ? 85   ASP   B N   1 2 
ATOM   5649  C  CA  . ASP   B 1  85  ? -18.326 -8.195  35.558  1    85.275  ? 85   ASP   B CA  1 2 
ATOM   5650  C  C   . ASP   B 1  85  ? -17.437 -7.75   34.385  1    86.683  ? 85   ASP   B C   1 2 
ATOM   5651  O  O   . ASP   B 1  85  ? -16.304 -8.213  34.225  1    89.419  ? 85   ASP   B O   1 2 
ATOM   5652  C  CB  . ASP   B 1  85  ? -17.828 -7.979  36.986  1    81.717  ? 85   ASP   B CB  1 2 
ATOM   5653  C  CG  . ASP   B 1  85  ? -16.966 -6.76   37.309  1    79.621  ? 85   ASP   B CG  1 2 
ATOM   5654  O  OD1 . ASP   B 1  85  ? -16.808 -5.851  36.445  1    78.182  ? 85   ASP   B OD1 1 2 
ATOM   5655  O  OD2 . ASP   B 1  85  ? -16.42  -6.731  38.434  1    74.97   ? 85   ASP   B OD2 1 2 
ATOM   5656  N  N   . PRO   B 1  86  ? -17.91  -6.84   33.5    1    85.091  ? 86   PRO   B N   1 2 
ATOM   5657  C  CA  . PRO   B 1  86  ? -17.063 -6.347  32.408  1    79.958  ? 86   PRO   B CA  1 2 
ATOM   5658  C  C   . PRO   B 1  86  ? -15.898 -5.437  32.816  1    75.675  ? 86   PRO   B C   1 2 
ATOM   5659  O  O   . PRO   B 1  86  ? -14.89  -5.415  32.109  1    75.162  ? 86   PRO   B O   1 2 
ATOM   5660  C  CB  . PRO   B 1  86  ? -18.067 -5.656  31.453  1    78.976  ? 86   PRO   B CB  1 2 
ATOM   5661  C  CG  . PRO   B 1  86  ? -19.2   -5.217  32.365  1    80.802  ? 86   PRO   B CG  1 2 
ATOM   5662  C  CD  . PRO   B 1  86  ? -19.261 -6.244  33.494  1    83.318  ? 86   PRO   B CD  1 2 
ATOM   5663  N  N   . GLN   B 1  87  ? -16.04  -4.697  33.938  1    72.266  ? 87   GLN   B N   1 2 
ATOM   5664  C  CA  . GLN   B 1  87  ? -15.017 -3.784  34.453  1    68.678  ? 87   GLN   B CA  1 2 
ATOM   5665  C  C   . GLN   B 1  87  ? -13.746 -4.536  34.855  1    66.454  ? 87   GLN   B C   1 2 
ATOM   5666  O  O   . GLN   B 1  87  ? -12.646 -4.101  34.51   1    56.542  ? 87   GLN   B O   1 2 
ATOM   5667  C  CB  . GLN   B 1  87  ? -15.477 -2.779  35.514  1    70.442  ? 87   GLN   B CB  1 2 
ATOM   5668  C  CG  . GLN   B 1  87  ? -15.622 -1.352  34.991  1    70.443  ? 87   GLN   B CG  1 2 
ATOM   5669  C  CD  . GLN   B 1  87  ? -16.124 -0.352  36.016  1    73.002  ? 87   GLN   B CD  1 2 
ATOM   5670  O  OE1 . GLN   B 1  87  ? -15.503 -0.102  37.06   1    70.444  ? 87   GLN   B OE1 1 2 
ATOM   5671  N  NE2 . GLN   B 1  87  ? -17.263 0.253   35.711  1    76.015  ? 87   GLN   B NE2 1 2 
ATOM   5672  N  N   . LEU   B 1  88  ? -13.93  -5.666  35.561  1    71.209  ? 88   LEU   B N   1 2 
ATOM   5673  C  CA  . LEU   B 1  88  ? -12.891 -6.637  35.898  1    70.415  ? 88   LEU   B CA  1 2 
ATOM   5674  C  C   . LEU   B 1  88  ? -12.219 -7.241  34.659  1    64.441  ? 88   LEU   B C   1 2 
ATOM   5675  O  O   . LEU   B 1  88  ? -10.998 -7.362  34.614  1    58.729  ? 88   LEU   B O   1 2 
ATOM   5676  C  CB  . LEU   B 1  88  ? -13.499 -7.752  36.746  1    70.965  ? 88   LEU   B CB  1 2 
ATOM   5677  C  CG  . LEU   B 1  88  ? -13.006 -7.932  38.187  1    76.061  ? 88   LEU   B CG  1 2 
ATOM   5678  C  CD1 . LEU   B 1  88  ? -13.343 -9.387  38.553  1    74.054  ? 88   LEU   B CD1 1 2 
ATOM   5679  C  CD2 . LEU   B 1  88  ? -11.542 -7.594  38.525  1    70.815  ? 88   LEU   B CD2 1 2 
ATOM   5680  N  N   . ARG   B 1  89  ? -13.03  -7.703  33.701  1    66.081  ? 89   ARG   B N   1 2 
ATOM   5681  C  CA  . ARG   B 1  89  ? -12.538 -8.274  32.458  1    68.468  ? 89   ARG   B CA  1 2 
ATOM   5682  C  C   . ARG   B 1  89  ? -11.564 -7.32   31.754  1    67.214  ? 89   ARG   B C   1 2 
ATOM   5683  O  O   . ARG   B 1  89  ? -10.493 -7.741  31.306  1    63.539  ? 89   ARG   B O   1 2 
ATOM   5684  C  CB  . ARG   B 1  89  ? -13.739 -8.649  31.586  1    73.814  ? 89   ARG   B CB  1 2 
ATOM   5685  C  CG  . ARG   B 1  89  ? -14.36  -10.001 31.909  1    81.008  ? 89   ARG   B CG  1 2 
ATOM   5686  C  CD  . ARG   B 1  89  ? -15.038 -10.696 30.713  1    85.562  ? 89   ARG   B CD  1 2 
ATOM   5687  N  NE  . ARG   B 1  89  ? -16.351 -10.138 30.354  1    91.579  ? 89   ARG   B NE  1 2 
ATOM   5688  C  CZ  . ARG   B 1  89  ? -16.617 -9.084  29.577  1    88.974  ? 89   ARG   B CZ  1 2 
ATOM   5689  N  NH1 . ARG   B 1  89  ? -15.659 -8.499  28.876  1    93.309  ? 89   ARG   B NH1 1 2 
ATOM   5690  N  NH2 . ARG   B 1  89  ? -17.858 -8.643  29.471  1    86.77   ? 89   ARG   B NH2 1 2 
ATOM   5691  N  N   . ARG   B 1  90  ? -11.947 -6.038  31.645  1    66.061  ? 90   ARG   B N   1 2 
ATOM   5692  C  CA  . ARG   B 1  90  ? -11.067 -4.971  31.164  1    70.641  ? 90   ARG   B CA  1 2 
ATOM   5693  C  C   . ARG   B 1  90  ? -9.753  -4.937  31.961  1    68.971  ? 90   ARG   B C   1 2 
ATOM   5694  O  O   . ARG   B 1  90  ? -8.685  -4.994  31.343  1    63.878  ? 90   ARG   B O   1 2 
ATOM   5695  C  CB  . ARG   B 1  90  ? -11.723 -3.58   31.157  1    70.511  ? 90   ARG   B CB  1 2 
ATOM   5696  C  CG  . ARG   B 1  90  ? -12.77  -3.3    30.085  1    72.29   ? 90   ARG   B CG  1 2 
ATOM   5697  C  CD  . ARG   B 1  90  ? -13.156 -1.83   30.187  1    70.06   ? 90   ARG   B CD  1 2 
ATOM   5698  N  NE  . ARG   B 1  90  ? -13.187 -1.213  28.854  1    76.758  ? 90   ARG   B NE  1 2 
ATOM   5699  C  CZ  . ARG   B 1  90  ? -12.228 -0.471  28.274  1    75.94   ? 90   ARG   B CZ  1 2 
ATOM   5700  N  NH1 . ARG   B 1  90  ? -12.495 0.16    27.141  1    75.26   ? 90   ARG   B NH1 1 2 
ATOM   5701  N  NH2 . ARG   B 1  90  ? -11.02  -0.333  28.813  1    72.744  ? 90   ARG   B NH2 1 2 
ATOM   5702  N  N   . ILE   B 1  91  ? -9.828  -4.872  33.313  1    61.9    ? 91   ILE   B N   1 2 
ATOM   5703  C  CA  . ILE   B 1  91  ? -8.618  -4.726  34.104  1    59.042  ? 91   ILE   B CA  1 2 
ATOM   5704  C  C   . ILE   B 1  91  ? -7.727  -5.959  33.901  1    57.914  ? 91   ILE   B C   1 2 
ATOM   5705  O  O   . ILE   B 1  91  ? -6.538  -5.804  33.649  1    57.754  ? 91   ILE   B O   1 2 
ATOM   5706  C  CB  . ILE   B 1  91  ? -8.882  -4.416  35.595  1    62.906  ? 91   ILE   B CB  1 2 
ATOM   5707  C  CG1 . ILE   B 1  91  ? -9.807  -3.168  35.842  1    59.837  ? 91   ILE   B CG1 1 2 
ATOM   5708  C  CG2 . ILE   B 1  91  ? -7.541  -4.301  36.329  1    64.745  ? 91   ILE   B CG2 1 2 
ATOM   5709  C  CD1 . ILE   B 1  91  ? -10.778 -3.281  37.019  1    60.401  ? 91   ILE   B CD1 1 2 
ATOM   5710  N  N   . ILE   B 1  92  ? -8.276  -7.182  33.963  1    58.173  ? 92   ILE   B N   1 2 
ATOM   5711  C  CA  . ILE   B 1  92  ? -7.419  -8.371  33.96   1    63.214  ? 92   ILE   B CA  1 2 
ATOM   5712  C  C   . ILE   B 1  92  ? -6.736  -8.573  32.6    1    66.083  ? 92   ILE   B C   1 2 
ATOM   5713  O  O   . ILE   B 1  92  ? -5.542  -8.88   32.555  1    68.169  ? 92   ILE   B O   1 2 
ATOM   5714  C  CB  . ILE   B 1  92  ? -8.114  -9.652  34.477  1    68.037  ? 92   ILE   B CB  1 2 
ATOM   5715  C  CG1 . ILE   B 1  92  ? -8.517  -9.539  35.982  1    69.76   ? 92   ILE   B CG1 1 2 
ATOM   5716  C  CG2 . ILE   B 1  92  ? -7.284  -10.919 34.206  1    66.766  ? 92   ILE   B CG2 1 2 
ATOM   5717  C  CD1 . ILE   B 1  92  ? -7.389  -9.146  36.927  1    68.847  ? 92   ILE   B CD1 1 2 
ATOM   5718  N  N   . GLY   B 1  93  ? -7.491  -8.415  31.5    1    63.494  ? 93   GLY   B N   1 2 
ATOM   5719  C  CA  . GLY   B 1  93  ? -6.907  -8.416  30.163  1    64.497  ? 93   GLY   B CA  1 2 
ATOM   5720  C  C   . GLY   B 1  93  ? -5.702  -7.47   30.012  1    64.686  ? 93   GLY   B C   1 2 
ATOM   5721  O  O   . GLY   B 1  93  ? -4.713  -7.832  29.362  1    67.881  ? 93   GLY   B O   1 2 
ATOM   5722  N  N   . ALA   B 1  94  ? -5.789  -6.263  30.609  1    59.02   ? 94   ALA   B N   1 2 
ATOM   5723  C  CA  . ALA   B 1  94  ? -4.717  -5.267  30.596  1    57.357  ? 94   ALA   B CA  1 2 
ATOM   5724  C  C   . ALA   B 1  94  ? -3.505  -5.799  31.354  1    55.048  ? 94   ALA   B C   1 2 
ATOM   5725  O  O   . ALA   B 1  94  ? -2.397  -5.795  30.838  1    51.542  ? 94   ALA   B O   1 2 
ATOM   5726  C  CB  . ALA   B 1  94  ? -5.182  -3.923  31.137  1    52.693  ? 94   ALA   B CB  1 2 
ATOM   5727  N  N   . VAL   B 1  95  ? -3.761  -6.354  32.546  1    61.547  ? 95   VAL   B N   1 2 
ATOM   5728  C  CA  . VAL   B 1  95  ? -2.734  -6.84   33.454  1    57.262  ? 95   VAL   B CA  1 2 
ATOM   5729  C  C   . VAL   B 1  95  ? -1.849  -7.907  32.786  1    55.058  ? 95   VAL   B C   1 2 
ATOM   5730  O  O   . VAL   B 1  95  ? -0.632  -7.941  32.972  1    50.74   ? 95   VAL   B O   1 2 
ATOM   5731  C  CB  . VAL   B 1  95  ? -3.416  -7.356  34.735  1    60.032  ? 95   VAL   B CB  1 2 
ATOM   5732  C  CG1 . VAL   B 1  95  ? -2.354  -7.696  35.771  1    61.009  ? 95   VAL   B CG1 1 2 
ATOM   5733  C  CG2 . VAL   B 1  95  ? -4.385  -6.328  35.324  1    61.96   ? 95   VAL   B CG2 1 2 
ATOM   5734  N  N   . ARG   B 1  96  ? -2.487  -8.8    32.018  1    56.975  ? 96   ARG   B N   1 2 
ATOM   5735  C  CA  . ARG   B 1  96  ? -1.862  -9.95   31.398  1    58.362  ? 96   ARG   B CA  1 2 
ATOM   5736  C  C   . ARG   B 1  96  ? -1.174  -9.578  30.074  1    57.157  ? 96   ARG   B C   1 2 
ATOM   5737  O  O   . ARG   B 1  96  ? -0.713  -10.472 29.369  1    59.334  ? 96   ARG   B O   1 2 
ATOM   5738  C  CB  . ARG   B 1  96  ? -3.031  -10.942 31.315  1    64.785  ? 96   ARG   B CB  1 2 
ATOM   5739  C  CG  . ARG   B 1  96  ? -3.053  -12.187 30.439  1    73.028  ? 96   ARG   B CG  1 2 
ATOM   5740  C  CD  . ARG   B 1  96  ? -3.853  -12.011 29.127  1    75.021  ? 96   ARG   B CD  1 2 
ATOM   5741  N  NE  . ARG   B 1  96  ? -3.127  -11.303 28.064  1    74.2    ? 96   ARG   B NE  1 2 
ATOM   5742  C  CZ  . ARG   B 1  96  ? -2.197  -11.813 27.261  1    70.62   ? 96   ARG   B CZ  1 2 
ATOM   5743  N  NH1 . ARG   B 1  96  ? -1.416  -10.999 26.567  1    68.212  ? 96   ARG   B NH1 1 2 
ATOM   5744  N  NH2 . ARG   B 1  96  ? -2.004  -13.118 27.211  1    71.518  ? 96   ARG   B NH2 1 2 
ATOM   5745  N  N   . THR   B 1  97  ? -1.074  -8.275  29.747  1    55.49   ? 97   THR   B N   1 2 
ATOM   5746  C  CA  . THR   B 1  97  ? -0.296  -7.794  28.596  1    53.393  ? 97   THR   B CA  1 2 
ATOM   5747  C  C   . THR   B 1  97  ? 1.018   -7.187  29.097  1    49.457  ? 97   THR   B C   1 2 
ATOM   5748  O  O   . THR   B 1  97  ? 1.021   -6.109  29.666  1    48.705  ? 97   THR   B O   1 2 
ATOM   5749  C  CB  . THR   B 1  97  ? -1.112  -6.778  27.791  1    50.869  ? 97   THR   B CB  1 2 
ATOM   5750  O  OG1 . THR   B 1  97  ? -2.205  -7.509  27.251  1    54.819  ? 97   THR   B OG1 1 2 
ATOM   5751  C  CG2 . THR   B 1  97  ? -0.39   -6.223  26.575  1    50.488  ? 97   THR   B CG2 1 2 
ATOM   5752  N  N   . LEU   B 1  98  ? 2.138   -7.872  28.862  1    48.414  ? 98   LEU   B N   1 2 
ATOM   5753  C  CA  . LEU   B 1  98  ? 3.376   -7.51   29.534  1    48.97   ? 98   LEU   B CA  1 2 
ATOM   5754  C  C   . LEU   B 1  98  ? 4.203   -6.452  28.815  1    50.108  ? 98   LEU   B C   1 2 
ATOM   5755  O  O   . LEU   B 1  98  ? 5.001   -5.792  29.472  1    52.701  ? 98   LEU   B O   1 2 
ATOM   5756  C  CB  . LEU   B 1  98  ? 4.205   -8.759  29.809  1    51.892  ? 98   LEU   B CB  1 2 
ATOM   5757  C  CG  . LEU   B 1  98  ? 3.815   -9.55   31.064  1    53.243  ? 98   LEU   B CG  1 2 
ATOM   5758  C  CD1 . LEU   B 1  98  ? 2.369   -10.062 30.973  1    54.027  ? 98   LEU   B CD1 1 2 
ATOM   5759  C  CD2 . LEU   B 1  98  ? 4.811   -10.682 31.224  1    53.458  ? 98   LEU   B CD2 1 2 
ATOM   5760  N  N   . GLY   B 1  99  ? 4.077   -6.325  27.475  1    48.612  ? 99   GLY   B N   1 2 
ATOM   5761  C  CA  . GLY   B 1  99  ? 4.811   -5.286  26.763  1    43.195  ? 99   GLY   B CA  1 2 
ATOM   5762  C  C   . GLY   B 1  99  ? 6.304   -5.578  26.759  1    41.038  ? 99   GLY   B C   1 2 
ATOM   5763  O  O   . GLY   B 1  99  ? 6.705   -6.743  26.741  1    42.968  ? 99   GLY   B O   1 2 
ATOM   5764  N  N   . SER   B 1  100 ? 7.119   -4.532  26.884  1    38.425  ? 100  SER   B N   1 2 
ATOM   5765  C  CA  . SER   B 1  100 ? 8.567   -4.721  26.917  1    39.538  ? 100  SER   B CA  1 2 
ATOM   5766  C  C   . SER   B 1  100 ? 9.018   -5.556  28.115  1    46.139  ? 100  SER   B C   1 2 
ATOM   5767  O  O   . SER   B 1  100 ? 10.218  -5.844  28.256  1    49.089  ? 100  SER   B O   1 2 
ATOM   5768  C  CB  . SER   B 1  100 ? 9.307   -3.398  26.89   1    38.555  ? 100  SER   B CB  1 2 
ATOM   5769  O  OG  . SER   B 1  100 ? 9.158   -2.648  28.095  1    40.284  ? 100  SER   B OG  1 2 
ATOM   5770  N  N   . ALA   B 1  101 ? 8.067   -5.89   29.008  1    46.616  ? 101  ALA   B N   1 2 
ATOM   5771  C  CA  . ALA   B 1  101 ? 8.368   -6.742  30.156  1    49.105  ? 101  ALA   B CA  1 2 
ATOM   5772  C  C   . ALA   B 1  101 ? 8.606   -8.173  29.693  1    50.511  ? 101  ALA   B C   1 2 
ATOM   5773  O  O   . ALA   B 1  101 ? 9.11    -8.998  30.469  1    54.132  ? 101  ALA   B O   1 2 
ATOM   5774  C  CB  . ALA   B 1  101 ? 7.233   -6.709  31.169  1    48.913  ? 101  ALA   B CB  1 2 
ATOM   5775  N  N   . ASN   B 1  102 ? 8.152   -8.483  28.468  1    48.966  ? 102  ASN   B N   1 2 
ATOM   5776  C  CA  . ASN   B 1  102 ? 8.258   -9.835  27.952  1    49.703  ? 102  ASN   B CA  1 2 
ATOM   5777  C  C   . ASN   B 1  102 ? 9.687   -10.014 27.478  1    49.003  ? 102  ASN   B C   1 2 
ATOM   5778  O  O   . ASN   B 1  102 ? 10.07   -11.143 27.217  1    50.361  ? 102  ASN   B O   1 2 
ATOM   5779  C  CB  . ASN   B 1  102 ? 7.343   -10.121 26.763  1    50.629  ? 102  ASN   B CB  1 2 
ATOM   5780  C  CG  . ASN   B 1  102 ? 5.922   -10.409 27.192  1    52.878  ? 102  ASN   B CG  1 2 
ATOM   5781  O  OD1 . ASN   B 1  102 ? 5.655   -11.357 27.954  1    51.487  ? 102  ASN   B OD1 1 2 
ATOM   5782  N  ND2 . ASN   B 1  102 ? 5.005   -9.565  26.744  1    49.052  ? 102  ASN   B ND2 1 2 
ATOM   5783  N  N   . LEU   B 1  103 ? 10.46   -8.916  27.404  1    45.459  ? 103  LEU   B N   1 2 
ATOM   5784  C  CA  . LEU   B 1  103 ? 11.831  -9.035  26.911  1    46.872  ? 103  LEU   B CA  1 2 
ATOM   5785  C  C   . LEU   B 1  103 ? 12.686  -9.665  27.989  1    51.853  ? 103  LEU   B C   1 2 
ATOM   5786  O  O   . LEU   B 1  103 ? 12.401  -9.441  29.17   1    52.295  ? 103  LEU   B O   1 2 
ATOM   5787  C  CB  . LEU   B 1  103 ? 12.455  -7.695  26.548  1    45.767  ? 103  LEU   B CB  1 2 
ATOM   5788  C  CG  . LEU   B 1  103 ? 11.928  -7.051  25.253  1    45.674  ? 103  LEU   B CG  1 2 
ATOM   5789  C  CD1 . LEU   B 1  103 ? 12.161  -5.541  25.249  1    45.161  ? 103  LEU   B CD1 1 2 
ATOM   5790  C  CD2 . LEU   B 1  103 ? 12.564  -7.709  24.03   1    45.079  ? 103  LEU   B CD2 1 2 
ATOM   5791  N  N   . PRO   B 1  104 ? 13.792  -10.365 27.614  1    54.163  ? 104  PRO   B N   1 2 
ATOM   5792  C  CA  . PRO   B 1  104 ? 14.817  -10.751 28.585  1    56.793  ? 104  PRO   B CA  1 2 
ATOM   5793  C  C   . PRO   B 1  104 ? 15.47   -9.426  28.976  1    55.647  ? 104  PRO   B C   1 2 
ATOM   5794  O  O   . PRO   B 1  104 ? 15.197  -8.417  28.34   1    48.712  ? 104  PRO   B O   1 2 
ATOM   5795  C  CB  . PRO   B 1  104 ? 15.786  -11.701 27.838  1    57.318  ? 104  PRO   B CB  1 2 
ATOM   5796  C  CG  . PRO   B 1  104 ? 15.51   -11.42  26.359  1    55.815  ? 104  PRO   B CG  1 2 
ATOM   5797  C  CD  . PRO   B 1  104 ? 14.111  -10.814 26.241  1    53.317  ? 104  PRO   B CD  1 2 
ATOM   5798  N  N   . LEU   B 1  105 ? 16.352  -9.49   29.999  1    58.006  ? 105  LEU   B N   1 2 
ATOM   5799  C  CA  . LEU   B 1  105 ? 16.906  -8.374  30.754  1    57.471  ? 105  LEU   B CA  1 2 
ATOM   5800  C  C   . LEU   B 1  105 ? 17.839  -7.515  29.899  1    56.531  ? 105  LEU   B C   1 2 
ATOM   5801  O  O   . LEU   B 1  105 ? 17.701  -6.301  29.905  1    55.503  ? 105  LEU   B O   1 2 
ATOM   5802  C  CB  . LEU   B 1  105 ? 17.547  -8.803  32.084  1    62.228  ? 105  LEU   B CB  1 2 
ATOM   5803  C  CG  . LEU   B 1  105 ? 16.676  -9.656  33.023  1    64.848  ? 105  LEU   B CG  1 2 
ATOM   5804  C  CD1 . LEU   B 1  105 ? 17.43   -10.224 34.204  1    68.786  ? 105  LEU   B CD1 1 2 
ATOM   5805  C  CD2 . LEU   B 1  105 ? 15.466  -8.889  33.549  1    65.82   ? 105  LEU   B CD2 1 2 
ATOM   5806  N  N   . ALA   B 1  106 ? 18.769  -8.112  29.147  1    57.626  ? 106  ALA   B N   1 2 
ATOM   5807  C  CA  . ALA   B 1  106 ? 19.694  -7.306  28.356  1    56.121  ? 106  ALA   B CA  1 2 
ATOM   5808  C  C   . ALA   B 1  106 ? 18.959  -6.574  27.228  1    55.294  ? 106  ALA   B C   1 2 
ATOM   5809  O  O   . ALA   B 1  106 ? 19.419  -5.525  26.743  1    53.906  ? 106  ALA   B O   1 2 
ATOM   5810  C  CB  . ALA   B 1  106 ? 20.823  -8.152  27.813  1    55.543  ? 106  ALA   B CB  1 2 
ATOM   5811  N  N   . LYS   B 1  107 ? 17.837  -7.143  26.767  1    52.363  ? 107  LYS   B N   1 2 
ATOM   5812  C  CA  . LYS   B 1  107 ? 17.138  -6.473  25.676  1    50.27   ? 107  LYS   B CA  1 2 
ATOM   5813  C  C   . LYS   B 1  107 ? 16.276  -5.36   26.27   1    50.987  ? 107  LYS   B C   1 2 
ATOM   5814  O  O   . LYS   B 1  107 ? 16.015  -4.341  25.608  1    48.094  ? 107  LYS   B O   1 2 
ATOM   5815  C  CB  . LYS   B 1  107 ? 16.357  -7.47   24.821  1    49.674  ? 107  LYS   B CB  1 2 
ATOM   5816  C  CG  . LYS   B 1  107 ? 17.28   -8.289  23.921  1    50.515  ? 107  LYS   B CG  1 2 
ATOM   5817  C  CD  . LYS   B 1  107 ? 16.536  -9.44   23.264  1    55.822  ? 107  LYS   B CD  1 2 
ATOM   5818  C  CE  . LYS   B 1  107 ? 17.347  -10.319 22.337  1    60.301  ? 107  LYS   B CE  1 2 
ATOM   5819  N  NZ  . LYS   B 1  107 ? 16.505  -10.57  21.16   1    59.495  ? 107  LYS   B NZ  1 2 
ATOM   5820  N  N   . ARG   B 1  108 ? 15.833  -5.596  27.516  1    51.456  ? 108  ARG   B N   1 2 
ATOM   5821  C  CA  . ARG   B 1  108 ? 15.025  -4.652  28.273  1    52.109  ? 108  ARG   B CA  1 2 
ATOM   5822  C  C   . ARG   B 1  108 ? 15.832  -3.383  28.464  1    49.221  ? 108  ARG   B C   1 2 
ATOM   5823  O  O   . ARG   B 1  108 ? 15.289  -2.289  28.312  1    46.461  ? 108  ARG   B O   1 2 
ATOM   5824  C  CB  . ARG   B 1  108 ? 14.695  -5.116  29.694  1    53.617  ? 108  ARG   B CB  1 2 
ATOM   5825  C  CG  . ARG   B 1  108 ? 13.351  -5.815  29.762  1    55.556  ? 108  ARG   B CG  1 2 
ATOM   5826  C  CD  . ARG   B 1  108 ? 13.18   -6.167  31.207  1    58.533  ? 108  ARG   B CD  1 2 
ATOM   5827  N  NE  . ARG   B 1  108 ? 12.111  -7.156  31.359  1    61.017  ? 108  ARG   B NE  1 2 
ATOM   5828  C  CZ  . ARG   B 1  108 ? 11.932  -7.761  32.524  1    65.034  ? 108  ARG   B CZ  1 2 
ATOM   5829  N  NH1 . ARG   B 1  108 ? 12.616  -7.363  33.584  1    62.413  ? 108  ARG   B NH1 1 2 
ATOM   5830  N  NH2 . ARG   B 1  108 ? 11.054  -8.737  32.628  1    69.984  ? 108  ARG   B NH2 1 2 
ATOM   5831  N  N   . GLN   B 1  109 ? 17.104  -3.595  28.824  1    50.059  ? 109  GLN   B N   1 2 
ATOM   5832  C  CA  . GLN   B 1  109 ? 18.118  -2.567  28.952  1    51.016  ? 109  GLN   B CA  1 2 
ATOM   5833  C  C   . GLN   B 1  109 ? 18.104  -1.826  27.635  1    48.217  ? 109  GLN   B C   1 2 
ATOM   5834  O  O   . GLN   B 1  109 ? 17.537  -0.74   27.584  1    42.831  ? 109  GLN   B O   1 2 
ATOM   5835  C  CB  . GLN   B 1  109 ? 19.492  -3.139  29.316  1    58.561  ? 109  GLN   B CB  1 2 
ATOM   5836  C  CG  . GLN   B 1  109 ? 20.245  -2.359  30.396  1    60.936  ? 109  GLN   B CG  1 2 
ATOM   5837  C  CD  . GLN   B 1  109 ? 21.256  -3.194  31.164  1    65.184  ? 109  GLN   B CD  1 2 
ATOM   5838  O  OE1 . GLN   B 1  109 ? 22.3    -3.614  30.639  1    65.241  ? 109  GLN   B OE1 1 2 
ATOM   5839  N  NE2 . GLN   B 1  109 ? 20.952  -3.457  32.429  1    63.846  ? 109  GLN   B NE2 1 2 
ATOM   5840  N  N   . GLN   B 1  110 ? 18.553  -2.509  26.563  1    49.06   ? 110  GLN   B N   1 2 
ATOM   5841  C  CA  . GLN   B 1  110 ? 18.808  -1.914  25.254  1    45.859  ? 110  GLN   B CA  1 2 
ATOM   5842  C  C   . GLN   B 1  110 ? 17.637  -1.057  24.747  1    40.286  ? 110  GLN   B C   1 2 
ATOM   5843  O  O   . GLN   B 1  110 ? 17.857  -0.013  24.144  1    39.02   ? 110  GLN   B O   1 2 
ATOM   5844  C  CB  . GLN   B 1  110 ? 19.279  -2.924  24.203  1    48.231  ? 110  GLN   B CB  1 2 
ATOM   5845  C  CG  . GLN   B 1  110 ? 19.971  -2.242  23.025  1    52.592  ? 110  GLN   B CG  1 2 
ATOM   5846  C  CD  . GLN   B 1  110 ? 20.535  -3.186  21.981  1    58.962  ? 110  GLN   B CD  1 2 
ATOM   5847  O  OE1 . GLN   B 1  110 ? 21.177  -4.195  22.301  1    58.401  ? 110  GLN   B OE1 1 2 
ATOM   5848  N  NE2 . GLN   B 1  110 ? 20.319  -2.842  20.715  1    56.669  ? 110  GLN   B NE2 1 2 
ATOM   5849  N  N   . TYR   B 1  111 ? 16.401  -1.527  24.934  1    40.202  ? 111  TYR   B N   1 2 
ATOM   5850  C  CA  . TYR   B 1  111 ? 15.21   -0.807  24.526  1    38.592  ? 111  TYR   B CA  1 2 
ATOM   5851  C  C   . TYR   B 1  111 ? 15.064  0.487   25.323  1    38.646  ? 111  TYR   B C   1 2 
ATOM   5852  O  O   . TYR   B 1  111 ? 14.751  1.533   24.744  1    36.82   ? 111  TYR   B O   1 2 
ATOM   5853  C  CB  . TYR   B 1  111 ? 14.036  -1.712  24.874  1    39.125  ? 111  TYR   B CB  1 2 
ATOM   5854  C  CG  . TYR   B 1  111 ? 12.643  -1.17   24.613  1    42.007  ? 111  TYR   B CG  1 2 
ATOM   5855  C  CD1 . TYR   B 1  111 ? 12.019  -1.376  23.383  1    40.654  ? 111  TYR   B CD1 1 2 
ATOM   5856  C  CD2 . TYR   B 1  111 ? 11.93   -0.507  25.61   1    41.725  ? 111  TYR   B CD2 1 2 
ATOM   5857  C  CE1 . TYR   B 1  111 ? 10.73   -0.917  23.155  1    42.112  ? 111  TYR   B CE1 1 2 
ATOM   5858  C  CE2 . TYR   B 1  111 ? 10.634  -0.06   25.404  1    42.031  ? 111  TYR   B CE2 1 2 
ATOM   5859  C  CZ  . TYR   B 1  111 ? 10.043  -0.244  24.159  1    43.98   ? 111  TYR   B CZ  1 2 
ATOM   5860  O  OH  . TYR   B 1  111 ? 8.759   0.163   23.963  1    43.123  ? 111  TYR   B OH  1 2 
ATOM   5861  N  N   . ASN   B 1  112 ? 15.304  0.411   26.644  1    38.682  ? 112  ASN   B N   1 2 
ATOM   5862  C  CA  . ASN   B 1  112 ? 15.149  1.568   27.516  1    37.664  ? 112  ASN   B CA  1 2 
ATOM   5863  C  C   . ASN   B 1  112 ? 16.145  2.635   27.027  1    35.788  ? 112  ASN   B C   1 2 
ATOM   5864  O  O   . ASN   B 1  112 ? 15.781  3.799   26.887  1    35.99   ? 112  ASN   B O   1 2 
ATOM   5865  C  CB  . ASN   B 1  112 ? 15.143  1.231   29.016  1    38.232  ? 112  ASN   B CB  1 2 
ATOM   5866  C  CG  . ASN   B 1  112 ? 14.131  0.202   29.508  1    40.825  ? 112  ASN   B CG  1 2 
ATOM   5867  O  OD1 . ASN   B 1  112 ? 13.045  0.059   28.938  1    39.547  ? 112  ASN   B OD1 1 2 
ATOM   5868  N  ND2 . ASN   B 1  112 ? 14.401  -0.487  30.624  1    40.894  ? 112  ASN   B ND2 1 2 
ATOM   5869  N  N   . ALA   B 1  113 ? 17.349  2.237   26.604  1    35.919  ? 113  ALA   B N   1 2 
ATOM   5870  C  CA  . ALA   B 1  113 ? 18.398  3.165   26.139  1    35.574  ? 113  ALA   B CA  1 2 
ATOM   5871  C  C   . ALA   B 1  113 ? 18.14   3.777   24.749  1    36.003  ? 113  ALA   B C   1 2 
ATOM   5872  O  O   . ALA   B 1  113 ? 18.613  4.882   24.43   1    35.733  ? 113  ALA   B O   1 2 
ATOM   5873  C  CB  . ALA   B 1  113 ? 19.723  2.464   26.113  1    37.578  ? 113  ALA   B CB  1 2 
ATOM   5874  N  N   . LEU   B 1  114 ? 17.449  3.046   23.867  1    35.252  ? 114  LEU   B N   1 2 
ATOM   5875  C  CA  . LEU   B 1  114 ? 17.298  3.66    22.545  1    35.708  ? 114  LEU   B CA  1 2 
ATOM   5876  C  C   . LEU   B 1  114 ? 16.322  4.839   22.613  1    33.583  ? 114  LEU   B C   1 2 
ATOM   5877  O  O   . LEU   B 1  114 ? 16.538  5.859   21.958  1    31.663  ? 114  LEU   B O   1 2 
ATOM   5878  C  CB  . LEU   B 1  114 ? 16.903  2.66    21.472  1    35.367  ? 114  LEU   B CB  1 2 
ATOM   5879  C  CG  . LEU   B 1  114 ? 18.037  1.779   20.959  1    36.384  ? 114  LEU   B CG  1 2 
ATOM   5880  C  CD1 . LEU   B 1  114 ? 17.295  0.629   20.33   1    37.931  ? 114  LEU   B CD1 1 2 
ATOM   5881  C  CD2 . LEU   B 1  114 ? 18.844  2.576   19.955  1    34.96   ? 114  LEU   B CD2 1 2 
ATOM   5882  N  N   . LEU   B 1  115 ? 15.258  4.647   23.398  1    36.621  ? 115  LEU   B N   1 2 
ATOM   5883  C  CA  . LEU   B 1  115 ? 14.251  5.661   23.706  1    38.222  ? 115  LEU   B CA  1 2 
ATOM   5884  C  C   . LEU   B 1  115 ? 14.966  6.937   24.172  1    37.51   ? 115  LEU   B C   1 2 
ATOM   5885  O  O   . LEU   B 1  115 ? 14.625  8.052   23.77   1    33.412  ? 115  LEU   B O   1 2 
ATOM   5886  C  CB  . LEU   B 1  115 ? 13.249  5.15    24.75   1    37.015  ? 115  LEU   B CB  1 2 
ATOM   5887  C  CG  . LEU   B 1  115 ? 12.344  3.976   24.358  1    40.225  ? 115  LEU   B CG  1 2 
ATOM   5888  C  CD1 . LEU   B 1  115 ? 11.212  3.691   25.35   1    40.327  ? 115  LEU   B CD1 1 2 
ATOM   5889  C  CD2 . LEU   B 1  115 ? 11.766  4.115   22.959  1    41.607  ? 115  LEU   B CD2 1 2 
ATOM   5890  N  N   . SER   B 1  116 ? 16.008  6.768   25.007  1    35.313  ? 116  SER   B N   1 2 
ATOM   5891  C  CA  . SER   B 1  116 ? 16.677  7.9     25.611  1    32.885  ? 116  SER   B CA  1 2 
ATOM   5892  C  C   . SER   B 1  116 ? 17.542  8.627   24.577  1    32.53   ? 116  SER   B C   1 2 
ATOM   5893  O  O   . SER   B 1  116 ? 17.487  9.86    24.475  1    30.671  ? 116  SER   B O   1 2 
ATOM   5894  C  CB  . SER   B 1  116 ? 17.407  7.416   26.864  1    38.05   ? 116  SER   B CB  1 2 
ATOM   5895  O  OG  . SER   B 1  116 ? 18.365  8.359   27.288  1    38.698  ? 116  SER   B OG  1 2 
ATOM   5896  N  N   . GLN   B 1  117 ? 18.261  7.874   23.717  1    30.746  ? 117  GLN   B N   1 2 
ATOM   5897  C  CA  . GLN   B 1  117 ? 19.067  8.506   22.687  1    30.915  ? 117  GLN   B CA  1 2 
ATOM   5898  C  C   . GLN   B 1  117 ? 18.165  9.129   21.609  1    28.856  ? 117  GLN   B C   1 2 
ATOM   5899  O  O   . GLN   B 1  117 ? 18.475  10.219  21.156  1    28.649  ? 117  GLN   B O   1 2 
ATOM   5900  C  CB  . GLN   B 1  117 ? 20.17   7.659   22.045  1    34.538  ? 117  GLN   B CB  1 2 
ATOM   5901  C  CG  . GLN   B 1  117 ? 21.411  7.441   22.939  1    40.891  ? 117  GLN   B CG  1 2 
ATOM   5902  C  CD  . GLN   B 1  117 ? 22.367  6.4     22.361  1    49.457  ? 117  GLN   B CD  1 2 
ATOM   5903  O  OE1 . GLN   B 1  117 ? 22.208  5.94    21.215  1    53.252  ? 117  GLN   B OE1 1 2 
ATOM   5904  N  NE2 . GLN   B 1  117 ? 23.385  6       23.124  1    51.633  ? 117  GLN   B NE2 1 2 
ATOM   5905  N  N   . MET   B 1  118 ? 17.096  8.447   21.174  1    28.492  ? 118  MET   B N   1 2 
ATOM   5906  C  CA  . MET   B 1  118 ? 16.22   9.042   20.152  1    27.543  ? 118  MET   B CA  1 2 
ATOM   5907  C  C   . MET   B 1  118 ? 15.59   10.351  20.65   1    27.833  ? 118  MET   B C   1 2 
ATOM   5908  O  O   . MET   B 1  118 ? 15.531  11.326  19.908  1    30.32   ? 118  MET   B O   1 2 
ATOM   5909  C  CB  . MET   B 1  118 ? 15.097  8.096   19.737  1    26.007  ? 118  MET   B CB  1 2 
ATOM   5910  C  CG  . MET   B 1  118 ? 15.624  6.811   19.077  1    28.855  ? 118  MET   B CG  1 2 
ATOM   5911  S  SD  . MET   B 1  118 ? 14.31   5.966   18.174  1    29.647  ? 118  MET   B SD  1 2 
ATOM   5912  C  CE  . MET   B 1  118 ? 13.333  5.111   19.413  1    26.136  ? 118  MET   B CE  1 2 
ATOM   5913  N  N   . SER   B 1  119 ? 15.111  10.364  21.887  1    27.46   ? 119  SER   B N   1 2 
ATOM   5914  C  CA  . SER   B 1  119 ? 14.535  11.567  22.496  1    29.486  ? 119  SER   B CA  1 2 
ATOM   5915  C  C   . SER   B 1  119 ? 15.553  12.714  22.521  1    29.775  ? 119  SER   B C   1 2 
ATOM   5916  O  O   . SER   B 1  119 ? 15.236  13.87   22.203  1    26.07   ? 119  SER   B O   1 2 
ATOM   5917  C  CB  . SER   B 1  119 ? 14.03   11.226  23.889  1    32.262  ? 119  SER   B CB  1 2 
ATOM   5918  O  OG  . SER   B 1  119 ? 13.674  12.411  24.587  1    41.277  ? 119  SER   B OG  1 2 
ATOM   5919  N  N   . ARG   B 1  120 ? 16.802  12.393  22.916  1    29.266  ? 120  ARG   B N   1 2 
ATOM   5920  C  CA  . ARG   B 1  120 ? 17.874  13.372  23.007  1    31.189  ? 120  ARG   B CA  1 2 
ATOM   5921  C  C   . ARG   B 1  120 ? 18.178  13.929  21.621  1    30.915  ? 120  ARG   B C   1 2 
ATOM   5922  O  O   . ARG   B 1  120 ? 18.395  15.127  21.469  1    34.089  ? 120  ARG   B O   1 2 
ATOM   5923  C  CB  . ARG   B 1  120 ? 19.213  12.862  23.583  1    33.616  ? 120  ARG   B CB  1 2 
ATOM   5924  C  CG  . ARG   B 1  120 ? 20.307  13.925  23.507  1    38.147  ? 120  ARG   B CG  1 2 
ATOM   5925  C  CD  . ARG   B 1  120 ? 21.734  13.562  23.914  1    45.789  ? 120  ARG   B CD  1 2 
ATOM   5926  N  NE  . ARG   B 1  120 ? 22.098  12.314  23.221  1    48.868  ? 120  ARG   B NE  1 2 
ATOM   5927  C  CZ  . ARG   B 1  120 ? 22.399  12.153  21.925  1    53.294  ? 120  ARG   B CZ  1 2 
ATOM   5928  N  NH1 . ARG   B 1  120 ? 22.811  13.179  21.186  1    50.032  ? 120  ARG   B NH1 1 2 
ATOM   5929  N  NH2 . ARG   B 1  120 ? 22.376  10.931  21.397  1    56.621  ? 120  ARG   B NH2 1 2 
ATOM   5930  N  N   . ILE   B 1  121 ? 18.301  13.057  20.626  1    28.911  ? 121  ILE   B N   1 2 
ATOM   5931  C  CA  . ILE   B 1  121 ? 18.656  13.531  19.304  1    28.225  ? 121  ILE   B CA  1 2 
ATOM   5932  C  C   . ILE   B 1  121 ? 17.578  14.5    18.836  1    25.145  ? 121  ILE   B C   1 2 
ATOM   5933  O  O   . ILE   B 1  121 ? 17.909  15.516  18.259  1    26.766  ? 121  ILE   B O   1 2 
ATOM   5934  C  CB  . ILE   B 1  121 ? 18.848  12.373  18.297  1    30.227  ? 121  ILE   B CB  1 2 
ATOM   5935  C  CG1 . ILE   B 1  121 ? 20.101  11.528  18.611  1    34.448  ? 121  ILE   B CG1 1 2 
ATOM   5936  C  CG2 . ILE   B 1  121 ? 18.864  12.896  16.854  1    28.642  ? 121  ILE   B CG2 1 2 
ATOM   5937  C  CD1 . ILE   B 1  121 ? 20.142  10.218  17.859  1    36.027  ? 121  ILE   B CD1 1 2 
ATOM   5938  N  N   . TYR   B 1  122 ? 16.303  14.158  19.03   1    24.933  ? 122  TYR   B N   1 2 
ATOM   5939  C  CA  . TYR   B 1  122 ? 15.205  14.977  18.494  1    22.241  ? 122  TYR   B CA  1 2 
ATOM   5940  C  C   . TYR   B 1  122 ? 15.287  16.366  19.12   1    23.187  ? 122  TYR   B C   1 2 
ATOM   5941  O  O   . TYR   B 1  122 ? 15.268  17.395  18.434  1    23.467  ? 122  TYR   B O   1 2 
ATOM   5942  C  CB  . TYR   B 1  122 ? 13.827  14.341  18.698  1    20.974  ? 122  TYR   B CB  1 2 
ATOM   5943  C  CG  . TYR   B 1  122 ? 12.688  15.199  18.108  1    20.669  ? 122  TYR   B CG  1 2 
ATOM   5944  C  CD1 . TYR   B 1  122 ? 12.354  15.117  16.753  1    20.996  ? 122  TYR   B CD1 1 2 
ATOM   5945  C  CD2 . TYR   B 1  122 ? 12.025  16.168  18.871  1    20.185  ? 122  TYR   B CD2 1 2 
ATOM   5946  C  CE1 . TYR   B 1  122 ? 11.325  15.91   16.225  1    19.743  ? 122  TYR   B CE1 1 2 
ATOM   5947  C  CE2 . TYR   B 1  122 ? 11.05   17.014  18.344  1    19.977  ? 122  TYR   B CE2 1 2 
ATOM   5948  C  CZ  . TYR   B 1  122 ? 10.669  16.848  17.004  1    21.775  ? 122  TYR   B CZ  1 2 
ATOM   5949  O  OH  . TYR   B 1  122 ? 9.651   17.6    16.416  1    21.354  ? 122  TYR   B OH  1 2 
ATOM   5950  N  N   . SER   B 1  123 ? 15.36   16.385  20.446  1    25.499  ? 123  SER   B N   1 2 
ATOM   5951  C  CA  . SER   B 1  123 ? 15.106  17.594  21.214  1    28.243  ? 123  SER   B CA  1 2 
ATOM   5952  C  C   . SER   B 1  123 ? 16.353  18.45   21.373  1    31.852  ? 123  SER   B C   1 2 
ATOM   5953  O  O   . SER   B 1  123 ? 16.237  19.581  21.867  1    31.975  ? 123  SER   B O   1 2 
ATOM   5954  C  CB  . SER   B 1  123 ? 14.485  17.292  22.588  1    29.406  ? 123  SER   B CB  1 2 
ATOM   5955  O  OG  . SER   B 1  123 ? 13.112  16.971  22.431  1    29.066  ? 123  SER   B OG  1 2 
ATOM   5956  N  N   . THR   B 1  124 ? 17.522  17.936  20.965  1    31.7    ? 124  THR   B N   1 2 
ATOM   5957  C  CA  . THR   B 1  124 ? 18.711  18.782  20.96   1    34.8    ? 124  THR   B CA  1 2 
ATOM   5958  C  C   . THR   B 1  124 ? 19.241  19.115  19.555  1    35.543  ? 124  THR   B C   1 2 
ATOM   5959  O  O   . THR   B 1  124 ? 20.247  19.816  19.459  1    36.093  ? 124  THR   B O   1 2 
ATOM   5960  C  CB  . THR   B 1  124 ? 19.821  18.218  21.851  1    37.12   ? 124  THR   B CB  1 2 
ATOM   5961  O  OG1 . THR   B 1  124 ? 20.223  17.008  21.213  1    38.325  ? 124  THR   B OG1 1 2 
ATOM   5962  C  CG2 . THR   B 1  124 ? 19.394  17.972  23.286  1    35.032  ? 124  THR   B CG2 1 2 
ATOM   5963  N  N   . ALA   B 1  125 ? 18.579  18.68   18.463  1    33.405  ? 125  ALA   B N   1 2 
ATOM   5964  C  CA  . ALA   B 1  125 ? 19.083  18.942  17.121  1    32.723  ? 125  ALA   B CA  1 2 
ATOM   5965  C  C   . ALA   B 1  125 ? 18.969  20.423  16.783  1    33.424  ? 125  ALA   B C   1 2 
ATOM   5966  O  O   . ALA   B 1  125 ? 17.981  21.046  17.161  1    30.25   ? 125  ALA   B O   1 2 
ATOM   5967  C  CB  . ALA   B 1  125 ? 18.344  18.094  16.112  1    33.878  ? 125  ALA   B CB  1 2 
ATOM   5968  N  N   . LYS   B 1  126 ? 20.011  20.998  16.153  1    33.613  ? 126  LYS   B N   1 2 
ATOM   5969  C  CA  . LYS   B 1  126 ? 19.988  22.411  15.786  1    36.445  ? 126  LYS   B CA  1 2 
ATOM   5970  C  C   . LYS   B 1  126 ? 20.314  22.564  14.307  1    35.115  ? 126  LYS   B C   1 2 
ATOM   5971  O  O   . LYS   B 1  126 ? 20.873  21.658  13.713  1    40.293  ? 126  LYS   B O   1 2 
ATOM   5972  C  CB  . LYS   B 1  126 ? 20.993  23.231  16.607  1    41.79   ? 126  LYS   B CB  1 2 
ATOM   5973  C  CG  . LYS   B 1  126 ? 21.018  22.976  18.107  1    49.192  ? 126  LYS   B CG  1 2 
ATOM   5974  C  CD  . LYS   B 1  126 ? 20.341  24.06   18.948  1    54.906  ? 126  LYS   B CD  1 2 
ATOM   5975  C  CE  . LYS   B 1  126 ? 19.425  23.569  20.049  1    59.233  ? 126  LYS   B CE  1 2 
ATOM   5976  N  NZ  . LYS   B 1  126 ? 19.952  22.525  20.936  1    57.007  ? 126  LYS   B NZ  1 2 
ATOM   5977  N  N   . VAL   B 1  127 ? 19.969  23.712  13.727  1    33.288  ? 127  VAL   B N   1 2 
ATOM   5978  C  CA  . VAL   B 1  127 ? 20.339  24.054  12.367  1    36.169  ? 127  VAL   B CA  1 2 
ATOM   5979  C  C   . VAL   B 1  127 ? 21.367  25.189  12.436  1    41.055  ? 127  VAL   B C   1 2 
ATOM   5980  O  O   . VAL   B 1  127 ? 21.173  26.149  13.162  1    41.838  ? 127  VAL   B O   1 2 
ATOM   5981  C  CB  . VAL   B 1  127 ? 19.119  24.427  11.497  1    33.39   ? 127  VAL   B CB  1 2 
ATOM   5982  C  CG1 . VAL   B 1  127 ? 19.523  24.882  10.09   1    33.412  ? 127  VAL   B CG1 1 2 
ATOM   5983  C  CG2 . VAL   B 1  127 ? 18.109  23.293  11.453  1    34.094  ? 127  VAL   B CG2 1 2 
ATOM   5984  N  N   . CYS   B 1  128 ? 22.453  25.056  11.66   1    46.911  ? 128  CYS   B N   1 2 
ATOM   5985  C  CA  . CYS   B 1  128 ? 23.617  25.926  11.714  1    54.469  ? 128  CYS   B CA  1 2 
ATOM   5986  C  C   . CYS   B 1  128 ? 23.934  26.536  10.356  1    56.942  ? 128  CYS   B C   1 2 
ATOM   5987  O  O   . CYS   B 1  128 ? 23.802  25.87   9.333   1    58.427  ? 128  CYS   B O   1 2 
ATOM   5988  C  CB  . CYS   B 1  128 ? 24.879  25.084  11.859  1    61.177  ? 128  CYS   B CB  1 2 
ATOM   5989  S  SG  . CYS   B 1  128 ? 24.951  24.185  13.428  1    73.498  ? 128  CYS   B SG  1 2 
ATOM   5990  N  N   . LEU   B 1  129 ? 24.427  27.781  10.364  1    61.79   ? 129  LEU   B N   1 2 
ATOM   5991  C  CA  . LEU   B 1  129 ? 25.327  28.213  9.302   1    68.282  ? 129  LEU   B CA  1 2 
ATOM   5992  C  C   . LEU   B 1  129 ? 26.704  28.535  9.913   1    78.243  ? 129  LEU   B C   1 2 
ATOM   5993  O  O   . LEU   B 1  129 ? 27.46   27.564  10.161  1    83.061  ? 129  LEU   B O   1 2 
ATOM   5994  C  CB  . LEU   B 1  129 ? 24.785  29.366  8.459   1    65.899  ? 129  LEU   B CB  1 2 
ATOM   5995  C  CG  . LEU   B 1  129 ? 25.385  29.511  7.055   1    70.541  ? 129  LEU   B CG  1 2 
ATOM   5996  C  CD1 . LEU   B 1  129 ? 24.294  30.129  6.186   1    68.075  ? 129  LEU   B CD1 1 2 
ATOM   5997  C  CD2 . LEU   B 1  129 ? 26.704  30.324  6.971   1    69.831  ? 129  LEU   B CD2 1 2 
ATOM   5998  N  N   . CYS   B 1  136 ? 23.209  29.128  16.286  1    48.948  ? 136  CYS   B N   1 2 
ATOM   5999  C  CA  . CYS   B 1  136 ? 22.435  27.948  15.799  1    51.411  ? 136  CYS   B CA  1 2 
ATOM   6000  C  C   . CYS   B 1  136 ? 20.963  27.986  16.207  1    45.25   ? 136  CYS   B C   1 2 
ATOM   6001  O  O   . CYS   B 1  136 ? 20.63   28.256  17.354  1    47.472  ? 136  CYS   B O   1 2 
ATOM   6002  C  CB  . CYS   B 1  136 ? 23.063  26.648  16.271  1    53.474  ? 136  CYS   B CB  1 2 
ATOM   6003  S  SG  . CYS   B 1  136 ? 24.578  26.348  15.332  1    75.31   ? 136  CYS   B SG  1 2 
ATOM   6004  N  N   . TRP   B 1  137 ? 20.09   27.618  15.266  1    42.041  ? 137  TRP   B N   1 2 
ATOM   6005  C  CA  . TRP   B 1  137 ? 18.647  27.682  15.474  1    37.774  ? 137  TRP   B CA  1 2 
ATOM   6006  C  C   . TRP   B 1  137 ? 18.097  26.359  15.995  1    35.915  ? 137  TRP   B C   1 2 
ATOM   6007  O  O   . TRP   B 1  137 ? 18.357  25.319  15.419  1    34.076  ? 137  TRP   B O   1 2 
ATOM   6008  C  CB  . TRP   B 1  137 ? 17.968  28.001  14.147  1    37.657  ? 137  TRP   B CB  1 2 
ATOM   6009  C  CG  . TRP   B 1  137 ? 18.209  29.403  13.691  1    42.505  ? 137  TRP   B CG  1 2 
ATOM   6010  C  CD1 . TRP   B 1  137 ? 18.504  30.483  14.465  1    44.795  ? 137  TRP   B CD1 1 2 
ATOM   6011  C  CD2 . TRP   B 1  137 ? 18.115  29.877  12.339  1    45.044  ? 137  TRP   B CD2 1 2 
ATOM   6012  N  NE1 . TRP   B 1  137 ? 18.647  31.59   13.68   1    49.271  ? 137  TRP   B NE1 1 2 
ATOM   6013  C  CE2 . TRP   B 1  137 ? 18.399  31.257  12.376  1    46.612  ? 137  TRP   B CE2 1 2 
ATOM   6014  C  CE3 . TRP   B 1  137 ? 17.825  29.27   11.118  1    45.952  ? 137  TRP   B CE3 1 2 
ATOM   6015  C  CZ2 . TRP   B 1  137 ? 18.399  32.048  11.232  1    49.041  ? 137  TRP   B CZ2 1 2 
ATOM   6016  C  CZ3 . TRP   B 1  137 ? 17.819  30.05   9.984   1    47.566  ? 137  TRP   B CZ3 1 2 
ATOM   6017  C  CH2 . TRP   B 1  137 ? 18.093  31.419  10.046  1    49.765  ? 137  TRP   B CH2 1 2 
ATOM   6018  N  N   . SER   B 1  138 ? 17.242  26.425  17.014  1    33.183  ? 138  SER   B N   1 2 
ATOM   6019  C  CA  . SER   B 1  138 ? 16.533  25.267  17.535  1    32.641  ? 138  SER   B CA  1 2 
ATOM   6020  C  C   . SER   B 1  138 ? 15.131  25.218  16.907  1    28.296  ? 138  SER   B C   1 2 
ATOM   6021  O  O   . SER   B 1  138 ? 14.647  26.21   16.364  1    26.356  ? 138  SER   B O   1 2 
ATOM   6022  C  CB  . SER   B 1  138 ? 16.4    25.403  19.035  1    36.272  ? 138  SER   B CB  1 2 
ATOM   6023  O  OG  . SER   B 1  138 ? 15.594  26.546  19.316  1    42.089  ? 138  SER   B OG  1 2 
ATOM   6024  N  N   . LEU   B 1  139 ? 14.509  24.05   16.99   1    26.922  ? 139  LEU   B N   1 2 
ATOM   6025  C  CA  . LEU   B 1  139 ? 13.177  23.829  16.431  1    27.328  ? 139  LEU   B CA  1 2 
ATOM   6026  C  C   . LEU   B 1  139 ? 12.218  24.846  17.035  1    27.802  ? 139  LEU   B C   1 2 
ATOM   6027  O  O   . LEU   B 1  139 ? 11.493  25.54   16.324  1    30.411  ? 139  LEU   B O   1 2 
ATOM   6028  C  CB  . LEU   B 1  139 ? 12.724  22.4    16.706  1    25.111  ? 139  LEU   B CB  1 2 
ATOM   6029  C  CG  . LEU   B 1  139 ? 11.293  22.031  16.277  1    26.415  ? 139  LEU   B CG  1 2 
ATOM   6030  C  CD1 . LEU   B 1  139 ? 11.046  22.351  14.82   1    25.055  ? 139  LEU   B CD1 1 2 
ATOM   6031  C  CD2 . LEU   B 1  139 ? 11.044  20.531  16.578  1    22.212  ? 139  LEU   B CD2 1 2 
ATOM   6032  N  N   . ASP   B 1  140 ? 12.246  24.938  18.362  1    28.691  ? 140  ASP   B N   1 2 
ATOM   6033  C  CA  . ASP   B 1  140 ? 11.315  25.775  19.099  1    30.404  ? 140  ASP   B CA  1 2 
ATOM   6034  C  C   . ASP   B 1  140 ? 12.158  26.719  19.951  1    30.62   ? 140  ASP   B C   1 2 
ATOM   6035  O  O   . ASP   B 1  140 ? 12.851  26.229  20.825  1    30.977  ? 140  ASP   B O   1 2 
ATOM   6036  C  CB  . ASP   B 1  140 ? 10.385  24.879  19.919  1    31.905  ? 140  ASP   B CB  1 2 
ATOM   6037  C  CG  . ASP   B 1  140 ? 9.286   25.594  20.726  1    43.912  ? 140  ASP   B CG  1 2 
ATOM   6038  O  OD1 . ASP   B 1  140 ? 9.372   26.848  20.858  1    42.03   ? 140  ASP   B OD1 1 2 
ATOM   6039  O  OD2 . ASP   B 1  140 ? 8.336   24.912  21.249  1    40.197  ? 140  ASP   B OD2 1 2 
ATOM   6040  N  N   . PRO   B 1  141 ? 12.131  28.066  19.772  1    30.136  ? 141  PRO   B N   1 2 
ATOM   6041  C  CA  . PRO   B 1  141 ? 11.23   28.733  18.824  1    30.103  ? 141  PRO   B CA  1 2 
ATOM   6042  C  C   . PRO   B 1  141 ? 11.715  29.09   17.415  1    30.1    ? 141  PRO   B C   1 2 
ATOM   6043  O  O   . PRO   B 1  141 ? 10.925  29.555  16.592  1    29.657  ? 141  PRO   B O   1 2 
ATOM   6044  C  CB  . PRO   B 1  141 ? 10.923  30.002  19.672  1    30.685  ? 141  PRO   B CB  1 2 
ATOM   6045  C  CG  . PRO   B 1  141 ? 12.266  30.372  20.323  1    32.022  ? 141  PRO   B CG  1 2 
ATOM   6046  C  CD  . PRO   B 1  141 ? 12.908  29.027  20.575  1    32.273  ? 141  PRO   B CD  1 2 
ATOM   6047  N  N   . ASP   B 1  142 ? 13.013  28.878  17.128  1    28.145  ? 142  ASP   B N   1 2 
ATOM   6048  C  CA  . ASP   B 1  142 ? 13.62   29.553  15.991  1    27.808  ? 142  ASP   B CA  1 2 
ATOM   6049  C  C   . ASP   B 1  142 ? 13.067  29.059  14.653  1    27.188  ? 142  ASP   B C   1 2 
ATOM   6050  O  O   . ASP   B 1  142 ? 12.592  29.879  13.843  1    27.294  ? 142  ASP   B O   1 2 
ATOM   6051  C  CB  . ASP   B 1  142 ? 15.125  29.396  16.005  1    30.703  ? 142  ASP   B CB  1 2 
ATOM   6052  C  CG  . ASP   B 1  142 ? 15.754  29.898  17.287  1    34.931  ? 142  ASP   B CG  1 2 
ATOM   6053  O  OD1 . ASP   B 1  142 ? 15.294  30.981  17.736  1    35.783  ? 142  ASP   B OD1 1 2 
ATOM   6054  O  OD2 . ASP   B 1  142 ? 16.642  29.189  17.819  1    35.892  ? 142  ASP   B OD2 1 2 
ATOM   6055  N  N   . LEU   B 1  143 ? 13.19   27.746  14.414  1    24.755  ? 143  LEU   B N   1 2 
ATOM   6056  C  CA  . LEU   B 1  143 ? 12.634  27.159  13.198  1    25.788  ? 143  LEU   B CA  1 2 
ATOM   6057  C  C   . LEU   B 1  143 ? 11.091  27.269  13.136  1    23.702  ? 143  LEU   B C   1 2 
ATOM   6058  O  O   . LEU   B 1  143 ? 10.516  27.614  12.095  1    25.096  ? 143  LEU   B O   1 2 
ATOM   6059  C  CB  . LEU   B 1  143 ? 13.153  25.732  13.097  1    25.82   ? 143  LEU   B CB  1 2 
ATOM   6060  C  CG  . LEU   B 1  143 ? 14.691  25.622  13.035  1    27.376  ? 143  LEU   B CG  1 2 
ATOM   6061  C  CD1 . LEU   B 1  143 ? 15.137  24.157  13.14   1    27.486  ? 143  LEU   B CD1 1 2 
ATOM   6062  C  CD2 . LEU   B 1  143 ? 15.335  26.294  11.839  1    29.874  ? 143  LEU   B CD2 1 2 
ATOM   6063  N  N   . THR   B 1  144 ? 10.408  26.999  14.244  1    23.94   ? 144  THR   B N   1 2 
ATOM   6064  C  CA  . THR   B 1  144 ? 8.972   27.262  14.346  1    22.244  ? 144  THR   B CA  1 2 
ATOM   6065  C  C   . THR   B 1  144 ? 8.617   28.662  13.843  1    22.189  ? 144  THR   B C   1 2 
ATOM   6066  O  O   . THR   B 1  144 ? 7.726   28.812  13.03   1    21.661  ? 144  THR   B O   1 2 
ATOM   6067  C  CB  . THR   B 1  144 ? 8.44    27.042  15.773  1    22.752  ? 144  THR   B CB  1 2 
ATOM   6068  O  OG1 . THR   B 1  144 ? 8.801   25.678  15.987  1    21.577  ? 144  THR   B OG1 1 2 
ATOM   6069  C  CG2 . THR   B 1  144 ? 6.913   27.148  15.839  1    21.822  ? 144  THR   B CG2 1 2 
ATOM   6070  N  N   . ASN   B 1  145 ? 9.29    29.697  14.32   1    23.454  ? 145  ASN   B N   1 2 
ATOM   6071  C  CA  . ASN   B 1  145 ? 8.885   31.042  13.943  1    26.424  ? 145  ASN   B CA  1 2 
ATOM   6072  C  C   . ASN   B 1  145 ? 9.2     31.283  12.461  1    27.27   ? 145  ASN   B C   1 2 
ATOM   6073  O  O   . ASN   B 1  145 ? 8.427   31.944  11.756  1    29.878  ? 145  ASN   B O   1 2 
ATOM   6074  C  CB  . ASN   B 1  145 ? 9.504   32.103  14.859  1    31.277  ? 145  ASN   B CB  1 2 
ATOM   6075  C  CG  . ASN   B 1  145 ? 8.812   32.219  16.214  1    35.464  ? 145  ASN   B CG  1 2 
ATOM   6076  O  OD1 . ASN   B 1  145 ? 7.641   31.854  16.36   1    39.147  ? 145  ASN   B OD1 1 2 
ATOM   6077  N  ND2 . ASN   B 1  145 ? 9.481   32.759  17.228  1    33.359  ? 145  ASN   B ND2 1 2 
ATOM   6078  N  N   . ILE   B 1  146 ? 10.346  30.786  11.989  1    27.818  ? 146  ILE   B N   1 2 
ATOM   6079  C  CA  . ILE   B 1  146 ? 10.686  30.908  10.572  1    26.687  ? 146  ILE   B CA  1 2 
ATOM   6080  C  C   . ILE   B 1  146 ? 9.583   30.276  9.73    1    25.952  ? 146  ILE   B C   1 2 
ATOM   6081  O  O   . ILE   B 1  146 ? 9.103   30.92   8.805   1    26.989  ? 146  ILE   B O   1 2 
ATOM   6082  C  CB  . ILE   B 1  146 ? 12.086  30.373  10.205  1    26.617  ? 146  ILE   B CB  1 2 
ATOM   6083  C  CG1 . ILE   B 1  146 ? 13.181  31.164  10.855  1    28.435  ? 146  ILE   B CG1 1 2 
ATOM   6084  C  CG2 . ILE   B 1  146 ? 12.313  30.43   8.688   1    28.666  ? 146  ILE   B CG2 1 2 
ATOM   6085  C  CD1 . ILE   B 1  146 ? 14.541  30.546  10.62   1    29.385  ? 146  ILE   B CD1 1 2 
ATOM   6086  N  N   . LEU   B 1  147 ? 9.184   29.026  10.041  1    25.766  ? 147  LEU   B N   1 2 
ATOM   6087  C  CA  . LEU   B 1  147 ? 8.262   28.279  9.198   1    23.429  ? 147  LEU   B CA  1 2 
ATOM   6088  C  C   . LEU   B 1  147 ? 6.921   29.03   9.192   1    24.443  ? 147  LEU   B C   1 2 
ATOM   6089  O  O   . LEU   B 1  147 ? 6.232   28.996  8.17    1    23.342  ? 147  LEU   B O   1 2 
ATOM   6090  C  CB  . LEU   B 1  147 ? 8.11    26.81   9.632   1    21.46   ? 147  LEU   B CB  1 2 
ATOM   6091  C  CG  . LEU   B 1  147 ? 8.965   25.76   8.902   1    22.121  ? 147  LEU   B CG  1 2 
ATOM   6092  C  CD1 . LEU   B 1  147 ? 8.473   25.504  7.466   1    21.775  ? 147  LEU   B CD1 1 2 
ATOM   6093  C  CD2 . LEU   B 1  147 ? 10.453  26.186  8.823   1    23.228  ? 147  LEU   B CD2 1 2 
ATOM   6094  N  N   . ALA   B 1  148 ? 6.615   29.774  10.284  1    23.532  ? 148  ALA   B N   1 2 
ATOM   6095  C  CA  . ALA   B 1  148 ? 5.304   30.388  10.51   1    26.232  ? 148  ALA   B CA  1 2 
ATOM   6096  C  C   . ALA   B 1  148 ? 5.171   31.707  9.763   1    28.05   ? 148  ALA   B C   1 2 
ATOM   6097  O  O   . ALA   B 1  148 ? 4.106   31.991  9.246   1    28.559  ? 148  ALA   B O   1 2 
ATOM   6098  C  CB  . ALA   B 1  148 ? 4.985   30.592  11.979  1    24.153  ? 148  ALA   B CB  1 2 
ATOM   6099  N  N   . SER   B 1  149 ? 6.258   32.469  9.66    1    29.263  ? 149  SER   B N   1 2 
ATOM   6100  C  CA  . SER   B 1  149 ? 6.14    33.865  9.268   1    31.734  ? 149  SER   B CA  1 2 
ATOM   6101  C  C   . SER   B 1  149 ? 7.086   34.276  8.125   1    32.256  ? 149  SER   B C   1 2 
ATOM   6102  O  O   . SER   B 1  149 ? 6.876   35.323  7.51    1    34.807  ? 149  SER   B O   1 2 
ATOM   6103  C  CB  . SER   B 1  149 ? 6.354   34.717  10.474  1    35.23   ? 149  SER   B CB  1 2 
ATOM   6104  O  OG  . SER   B 1  149 ? 7.718   34.556  10.812  1    37.316  ? 149  SER   B OG  1 2 
ATOM   6105  N  N   . SER   B 1  150 ? 8.103   33.469  7.788   1    28.93   ? 150  SER   B N   1 2 
ATOM   6106  C  CA  . SER   B 1  150 ? 8.932   33.836  6.647   1    30.251  ? 150  SER   B CA  1 2 
ATOM   6107  C  C   . SER   B 1  150 ? 8.153   33.582  5.351   1    31.096  ? 150  SER   B C   1 2 
ATOM   6108  O  O   . SER   B 1  150 ? 7.504   32.543  5.201   1    30.627  ? 150  SER   B O   1 2 
ATOM   6109  C  CB  . SER   B 1  150 ? 10.264  33.127  6.67    1    29.55   ? 150  SER   B CB  1 2 
ATOM   6110  O  OG  . SER   B 1  150 ? 11.046  33.424  5.511   1    31.569  ? 150  SER   B OG  1 2 
ATOM   6111  N  N   . ARG   B 1  151 ? 8.209   34.537  4.405   1    31.93   ? 151  ARG   B N   1 2 
ATOM   6112  C  CA  . ARG   B 1  151 ? 7.58    34.344  3.107   1    33.001  ? 151  ARG   B CA  1 2 
ATOM   6113  C  C   . ARG   B 1  151 ? 8.646   34.305  2.009   1    36.762  ? 151  ARG   B C   1 2 
ATOM   6114  O  O   . ARG   B 1  151 ? 8.363   34.541  0.833   1    37.748  ? 151  ARG   B O   1 2 
ATOM   6115  C  CB  . ARG   B 1  151 ? 6.499   35.401  2.847   1    36.417  ? 151  ARG   B CB  1 2 
ATOM   6116  C  CG  . ARG   B 1  151 ? 5.338   35.401  3.836   1    34.675  ? 151  ARG   B CG  1 2 
ATOM   6117  C  CD  . ARG   B 1  151 ? 4.634   34.078  4.062   1    33.913  ? 151  ARG   B CD  1 2 
ATOM   6118  N  NE  . ARG   B 1  151 ? 3.401   34.334  4.822   1    36.576  ? 151  ARG   B NE  1 2 
ATOM   6119  C  CZ  . ARG   B 1  151 ? 3.026   33.623  5.883   1    39.184  ? 151  ARG   B CZ  1 2 
ATOM   6120  N  NH1 . ARG   B 1  151 ? 1.895   33.923  6.499   1    41.732  ? 151  ARG   B NH1 1 2 
ATOM   6121  N  NH2 . ARG   B 1  151 ? 3.716   32.559  6.288   1    37.241  ? 151  ARG   B NH2 1 2 
ATOM   6122  N  N   . SER   B 1  152 ? 9.882   34.021  2.418   1    35.036  ? 152  SER   B N   1 2 
ATOM   6123  C  CA  . SER   B 1  152 ? 11.006  33.903  1.52    1    35.303  ? 152  SER   B CA  1 2 
ATOM   6124  C  C   . SER   B 1  152 ? 11.24   32.421  1.244   1    32.401  ? 152  SER   B C   1 2 
ATOM   6125  O  O   . SER   B 1  152 ? 11.558  31.643  2.157   1    29.473  ? 152  SER   B O   1 2 
ATOM   6126  C  CB  . SER   B 1  152 ? 12.2    34.555  2.154   1    38.956  ? 152  SER   B CB  1 2 
ATOM   6127  O  OG  . SER   B 1  152 ? 13.356  33.776  1.927   1    38.753  ? 152  SER   B OG  1 2 
ATOM   6128  N  N   . TYR   B 1  153 ? 11.021  32.048  -0.023  1    30.757  ? 153  TYR   B N   1 2 
ATOM   6129  C  CA  . TYR   B 1  153 ? 11.094  30.655  -0.435  1    29.042  ? 153  TYR   B CA  1 2 
ATOM   6130  C  C   . TYR   B 1  153 ? 12.402  30.071  0.1     1    28.815  ? 153  TYR   B C   1 2 
ATOM   6131  O  O   . TYR   B 1  153 ? 12.393  28.99   0.68    1    27.429  ? 153  TYR   B O   1 2 
ATOM   6132  C  CB  . TYR   B 1  153 ? 10.958  30.564  -1.965  1    27.604  ? 153  TYR   B CB  1 2 
ATOM   6133  C  CG  . TYR   B 1  153 ? 10.918  29.113  -2.413  1    26.213  ? 153  TYR   B CG  1 2 
ATOM   6134  C  CD1 . TYR   B 1  153 ? 12.084  28.348  -2.496  1    25.828  ? 153  TYR   B CD1 1 2 
ATOM   6135  C  CD2 . TYR   B 1  153 ? 9.698   28.497  -2.693  1    24.063  ? 153  TYR   B CD2 1 2 
ATOM   6136  C  CE1 . TYR   B 1  153 ? 12.034  27.012  -2.905  1    25.217  ? 153  TYR   B CE1 1 2 
ATOM   6137  C  CE2 . TYR   B 1  153 ? 9.64    27.162  -3.058  1    23.97   ? 153  TYR   B CE2 1 2 
ATOM   6138  C  CZ  . TYR   B 1  153 ? 10.805  26.427  -3.204  1    24.429  ? 153  TYR   B CZ  1 2 
ATOM   6139  O  OH  . TYR   B 1  153 ? 10.651  25.093  -3.566  1    25.049  ? 153  TYR   B OH  1 2 
ATOM   6140  N  N   . ALA   B 1  154 ? 13.511  30.805  -0.065  1    30.513  ? 154  ALA   B N   1 2 
ATOM   6141  C  CA  . ALA   B 1  154 ? 14.847  30.257  0.16    1    30.808  ? 154  ALA   B CA  1 2 
ATOM   6142  C  C   . ALA   B 1  154 ? 15.119  30.049  1.644   1    30.172  ? 154  ALA   B C   1 2 
ATOM   6143  O  O   . ALA   B 1  154 ? 15.811  29.111  2.007   1    28.352  ? 154  ALA   B O   1 2 
ATOM   6144  C  CB  . ALA   B 1  154 ? 15.919  31.121  -0.479  1    31.949  ? 154  ALA   B CB  1 2 
ATOM   6145  N  N   . MET   B 1  155 ? 14.597  30.942  2.491   1    31.463  ? 155  MET   B N   1 2 
ATOM   6146  C  CA  . MET   B 1  155 ? 14.833  30.856  3.928   1    32.017  ? 155  MET   B CA  1 2 
ATOM   6147  C  C   . MET   B 1  155 ? 14.003  29.709  4.51    1    28.334  ? 155  MET   B C   1 2 
ATOM   6148  O  O   . MET   B 1  155 ? 14.468  28.996  5.41    1    27.918  ? 155  MET   B O   1 2 
ATOM   6149  C  CB  . MET   B 1  155 ? 14.457  32.169  4.618   1    34.917  ? 155  MET   B CB  1 2 
ATOM   6150  C  CG  . MET   B 1  155 ? 14.57   32.147  6.128   1    37.18   ? 155  MET   B CG  1 2 
ATOM   6151  S  SD  . MET   B 1  155 ? 16.288  32.044  6.677   1    45.815  ? 155  MET   B SD  1 2 
ATOM   6152  C  CE  . MET   B 1  155 ? 16.683  30.308  6.886   1    47.456  ? 155  MET   B CE  1 2 
ATOM   6153  N  N   . LEU   B 1  156 ? 12.769  29.55   4       1    27.213  ? 156  LEU   B N   1 2 
ATOM   6154  C  CA  . LEU   B 1  156 ? 11.852  28.492  4.461   1    24.703  ? 156  LEU   B CA  1 2 
ATOM   6155  C  C   . LEU   B 1  156 ? 12.491  27.151  4.097   1    24.042  ? 156  LEU   B C   1 2 
ATOM   6156  O  O   . LEU   B 1  156 ? 12.519  26.21   4.904   1    21.749  ? 156  LEU   B O   1 2 
ATOM   6157  C  CB  . LEU   B 1  156 ? 10.474  28.619  3.81    1    22.779  ? 156  LEU   B CB  1 2 
ATOM   6158  C  CG  . LEU   B 1  156 ? 9.671   29.865  4.179   1    23.133  ? 156  LEU   B CG  1 2 
ATOM   6159  C  CD1 . LEU   B 1  156 ? 8.482   29.997  3.226   1    23.595  ? 156  LEU   B CD1 1 2 
ATOM   6160  C  CD2 . LEU   B 1  156 ? 9.21    29.54   5.607   1    22.387  ? 156  LEU   B CD2 1 2 
ATOM   6161  N  N   . LEU   B 1  157 ? 13.105  27.131  2.889   1    24.874  ? 157  LEU   B N   1 2 
ATOM   6162  C  CA  . LEU   B 1  157 ? 13.752  25.933  2.379   1    25.06   ? 157  LEU   B CA  1 2 
ATOM   6163  C  C   . LEU   B 1  157 ? 14.89   25.56   3.313   1    25.281  ? 157  LEU   B C   1 2 
ATOM   6164  O  O   . LEU   B 1  157 ? 15.136  24.406  3.624   1    26.289  ? 157  LEU   B O   1 2 
ATOM   6165  C  CB  . LEU   B 1  157 ? 14.227  26.113  0.926   1    27.925  ? 157  LEU   B CB  1 2 
ATOM   6166  C  CG  . LEU   B 1  157 ? 14.873  24.888  0.248   1    28.207  ? 157  LEU   B CG  1 2 
ATOM   6167  C  CD1 . LEU   B 1  157 ? 14.019  23.654  0.458   1    27.866  ? 157  LEU   B CD1 1 2 
ATOM   6168  C  CD2 . LEU   B 1  157 ? 15.298  25.059  -1.231  1    29.83   ? 157  LEU   B CD2 1 2 
ATOM   6169  N  N   . PHE   B 1  158 ? 15.695  26.544  3.676   1    28.101  ? 158  PHE   B N   1 2 
ATOM   6170  C  CA  . PHE   B 1  158 ? 16.896  26.236  4.424   1    28.539  ? 158  PHE   B CA  1 2 
ATOM   6171  C  C   . PHE   B 1  158 ? 16.501  25.747  5.825   1    27.354  ? 158  PHE   B C   1 2 
ATOM   6172  O  O   . PHE   B 1  158 ? 17.117  24.88   6.412   1    27.911  ? 158  PHE   B O   1 2 
ATOM   6173  C  CB  . PHE   B 1  158 ? 17.61   27.588  4.418   1    32.719  ? 158  PHE   B CB  1 2 
ATOM   6174  C  CG  . PHE   B 1  158 ? 18.831  27.451  5.309   1    34.917  ? 158  PHE   B CG  1 2 
ATOM   6175  C  CD1 . PHE   B 1  158 ? 20.002  26.902  4.803   1    38.148  ? 158  PHE   B CD1 1 2 
ATOM   6176  C  CD2 . PHE   B 1  158 ? 18.78   27.828  6.653   1    36.661  ? 158  PHE   B CD2 1 2 
ATOM   6177  C  CE1 . PHE   B 1  158 ? 21.116  26.749  5.626   1    42.927  ? 158  PHE   B CE1 1 2 
ATOM   6178  C  CE2 . PHE   B 1  158 ? 19.875  27.638  7.487   1    40.302  ? 158  PHE   B CE2 1 2 
ATOM   6179  C  CZ  . PHE   B 1  158 ? 21.045  27.113  6.959   1    43.103  ? 158  PHE   B CZ  1 2 
ATOM   6180  N  N   . ALA   B 1  159 ? 15.428  26.293  6.381   1    25.07   ? 159  ALA   B N   1 2 
ATOM   6181  C  CA  . ALA   B 1  159 ? 14.931  25.783  7.664   1    24.413  ? 159  ALA   B CA  1 2 
ATOM   6182  C  C   . ALA   B 1  159 ? 14.407  24.331  7.576   1    23.353  ? 159  ALA   B C   1 2 
ATOM   6183  O  O   . ALA   B 1  159 ? 14.687  23.497  8.444   1    22.083  ? 159  ALA   B O   1 2 
ATOM   6184  C  CB  . ALA   B 1  159 ? 13.92   26.779  8.2     1    23.216  ? 159  ALA   B CB  1 2 
ATOM   6185  N  N   . TRP   B 1  160 ? 13.624  24.032  6.533   1    23.48   ? 160  TRP   B N   1 2 
ATOM   6186  C  CA  . TRP   B 1  160 ? 12.977  22.736  6.329   1    20.969  ? 160  TRP   B CA  1 2 
ATOM   6187  C  C   . TRP   B 1  160 ? 14.051  21.67   6.129   1    19.889  ? 160  TRP   B C   1 2 
ATOM   6188  O  O   . TRP   B 1  160 ? 14.074  20.653  6.77    1    18.481  ? 160  TRP   B O   1 2 
ATOM   6189  C  CB  . TRP   B 1  160 ? 11.994  22.824  5.149   1    20.06   ? 160  TRP   B CB  1 2 
ATOM   6190  C  CG  . TRP   B 1  160 ? 11.182  21.569  4.935   1    19.581  ? 160  TRP   B CG  1 2 
ATOM   6191  C  CD1 . TRP   B 1  160 ? 9.958   21.296  5.485   1    17.269  ? 160  TRP   B CD1 1 2 
ATOM   6192  C  CD2 . TRP   B 1  160 ? 11.618  20.355  4.29    1    19.304  ? 160  TRP   B CD2 1 2 
ATOM   6193  N  NE1 . TRP   B 1  160 ? 9.535   20.072  5.081   1    16.796  ? 160  TRP   B NE1 1 2 
ATOM   6194  C  CE2 . TRP   B 1  160 ? 10.547  19.45   4.385   1    18.625  ? 160  TRP   B CE2 1 2 
ATOM   6195  C  CE3 . TRP   B 1  160 ? 12.783  19.964  3.598   1    21.614  ? 160  TRP   B CE3 1 2 
ATOM   6196  C  CZ2 . TRP   B 1  160 ? 10.6    18.165  3.839   1    18.768  ? 160  TRP   B CZ2 1 2 
ATOM   6197  C  CZ3 . TRP   B 1  160 ? 12.838  18.679  3.061   1    22.15   ? 160  TRP   B CZ3 1 2 
ATOM   6198  C  CH2 . TRP   B 1  160 ? 11.753  17.793  3.174   1    20.461  ? 160  TRP   B CH2 1 2 
ATOM   6199  N  N   . GLU   B 1  161 ? 14.974  21.916  5.209   1    22.01   ? 161  GLU   B N   1 2 
ATOM   6200  C  CA  . GLU   B 1  161 ? 16.019  20.937  4.912   1    23.172  ? 161  GLU   B CA  1 2 
ATOM   6201  C  C   . GLU   B 1  161 ? 16.959  20.777  6.105   1    23.61   ? 161  GLU   B C   1 2 
ATOM   6202  O  O   . GLU   B 1  161 ? 17.276  19.659  6.539   1    24.273  ? 161  GLU   B O   1 2 
ATOM   6203  C  CB  . GLU   B 1  161 ? 16.816  21.45   3.72    1    25.046  ? 161  GLU   B CB  1 2 
ATOM   6204  C  CG  . GLU   B 1  161 ? 18.074  20.638  3.431   1    30.834  ? 161  GLU   B CG  1 2 
ATOM   6205  C  CD  . GLU   B 1  161 ? 18.807  21.128  2.179   1    34.132  ? 161  GLU   B CD  1 2 
ATOM   6206  O  OE1 . GLU   B 1  161 ? 19.138  22.331  2.045   1    37.538  ? 161  GLU   B OE1 1 2 
ATOM   6207  O  OE2 . GLU   B 1  161 ? 19.045  20.268  1.317   1    35.485  ? 161  GLU   B OE2 1 2 
ATOM   6208  N  N   . GLY   B 1  162 ? 17.407  21.903  6.641   1    23.965  ? 162  GLY   B N   1 2 
ATOM   6209  C  CA  . GLY   B 1  162 ? 18.29   21.823  7.795   1    24.016  ? 162  GLY   B CA  1 2 
ATOM   6210  C  C   . GLY   B 1  162 ? 17.645  20.976  8.887   1    23.724  ? 162  GLY   B C   1 2 
ATOM   6211  O  O   . GLY   B 1  162 ? 18.326  20.137  9.474   1    23.855  ? 162  GLY   B O   1 2 
ATOM   6212  N  N   . TRP   B 1  163 ? 16.339  21.206  9.175   1    21.74   ? 163  TRP   B N   1 2 
ATOM   6213  C  CA  . TRP   B 1  163 ? 15.72   20.475  10.282  1    20.496  ? 163  TRP   B CA  1 2 
ATOM   6214  C  C   . TRP   B 1  163 ? 15.63   18.967  9.981   1    19.957  ? 163  TRP   B C   1 2 
ATOM   6215  O  O   . TRP   B 1  163 ? 15.924  18.098  10.825  1    19.083  ? 163  TRP   B O   1 2 
ATOM   6216  C  CB  . TRP   B 1  163 ? 14.321  21.036  10.645  1    20.286  ? 163  TRP   B CB  1 2 
ATOM   6217  C  CG  . TRP   B 1  163 ? 13.684  20.17   11.699  1    20.377  ? 163  TRP   B CG  1 2 
ATOM   6218  C  CD1 . TRP   B 1  163 ? 12.652  19.285  11.553  1    20.554  ? 163  TRP   B CD1 1 2 
ATOM   6219  C  CD2 . TRP   B 1  163 ? 14.151  20.01   13.06   1    22.495  ? 163  TRP   B CD2 1 2 
ATOM   6220  N  NE1 . TRP   B 1  163 ? 12.422  18.634  12.737  1    22.025  ? 163  TRP   B NE1 1 2 
ATOM   6221  C  CE2 . TRP   B 1  163 ? 13.327  19.041  13.674  1    22.601  ? 163  TRP   B CE2 1 2 
ATOM   6222  C  CE3 . TRP   B 1  163 ? 15.173  20.61   13.812  1    24.242  ? 163  TRP   B CE3 1 2 
ATOM   6223  C  CZ2 . TRP   B 1  163 ? 13.484  18.635  14.999  1    23.169  ? 163  TRP   B CZ2 1 2 
ATOM   6224  C  CZ3 . TRP   B 1  163 ? 15.321  20.208  15.123  1    25.367  ? 163  TRP   B CZ3 1 2 
ATOM   6225  C  CH2 . TRP   B 1  163 ? 14.492  19.237  15.698  1    22.802  ? 163  TRP   B CH2 1 2 
ATOM   6226  N  N   . HIS   B 1  164 ? 15.103  18.657  8.799   1    18.121  ? 164  HIS   B N   1 2 
ATOM   6227  C  CA  . HIS   B 1  164 ? 14.887  17.271  8.423   1    18.029  ? 164  HIS   B CA  1 2 
ATOM   6228  C  C   . HIS   B 1  164 ? 16.232  16.536  8.387   1    18.885  ? 164  HIS   B C   1 2 
ATOM   6229  O  O   . HIS   B 1  164 ? 16.301  15.384  8.778   1    18.326  ? 164  HIS   B O   1 2 
ATOM   6230  C  CB  . HIS   B 1  164 ? 14.152  17.169  7.09    1    16.11   ? 164  HIS   B CB  1 2 
ATOM   6231  C  CG  . HIS   B 1  164 ? 12.698  17.418  7.343   1    16.212  ? 164  HIS   B CG  1 2 
ATOM   6232  N  ND1 . HIS   B 1  164 ? 12.09   18.662  7.474   1    15.991  ? 164  HIS   B ND1 1 2 
ATOM   6233  C  CD2 . HIS   B 1  164 ? 11.728  16.5    7.505   1    15.953  ? 164  HIS   B CD2 1 2 
ATOM   6234  C  CE1 . HIS   B 1  164 ? 10.786  18.493  7.723   1    15.251  ? 164  HIS   B CE1 1 2 
ATOM   6235  N  NE2 . HIS   B 1  164 ? 10.532  17.179  7.749   1    15.848  ? 164  HIS   B NE2 1 2 
ATOM   6236  N  N   . ASN   B 1  165 ? 17.249  17.195  7.861   1    20.953  ? 165  ASN   B N   1 2 
ATOM   6237  C  CA  . ASN   B 1  165 ? 18.571  16.566  7.863   1    24.822  ? 165  ASN   B CA  1 2 
ATOM   6238  C  C   . ASN   B 1  165 ? 19.116  16.368  9.29    1    27.354  ? 165  ASN   B C   1 2 
ATOM   6239  O  O   . ASN   B 1  165 ? 19.642  15.295  9.618   1    28.689  ? 165  ASN   B O   1 2 
ATOM   6240  C  CB  . ASN   B 1  165 ? 19.544  17.322  6.966   1    26.444  ? 165  ASN   B CB  1 2 
ATOM   6241  C  CG  . ASN   B 1  165 ? 19.219  17.24   5.491   1    26.499  ? 165  ASN   B CG  1 2 
ATOM   6242  O  OD1 . ASN   B 1  165 ? 18.421  16.403  5.034   1    26.452  ? 165  ASN   B OD1 1 2 
ATOM   6243  N  ND2 . ASN   B 1  165 ? 19.825  18.141  4.735   1    25.641  ? 165  ASN   B ND2 1 2 
ATOM   6244  N  N   . ALA   B 1  166 ? 19.042  17.409  10.149  1    27.066  ? 166  ALA   B N   1 2 
ATOM   6245  C  CA  . ALA   B 1  166 ? 19.663  17.354  11.469  1    25.807  ? 166  ALA   B CA  1 2 
ATOM   6246  C  C   . ALA   B 1  166 ? 18.966  16.342  12.371  1    25.191  ? 166  ALA   B C   1 2 
ATOM   6247  O  O   . ALA   B 1  166 ? 19.62   15.672  13.17   1    24.368  ? 166  ALA   B O   1 2 
ATOM   6248  C  CB  . ALA   B 1  166 ? 19.59   18.723  12.119  1    27.308  ? 166  ALA   B CB  1 2 
ATOM   6249  N  N   . ALA   B 1  167 ? 17.629  16.215  12.291  1    22.015  ? 167  ALA   B N   1 2 
ATOM   6250  C  CA  . ALA   B 1  167 ? 16.951  15.296  13.197  1    22.648  ? 167  ALA   B CA  1 2 
ATOM   6251  C  C   . ALA   B 1  167 ? 16.897  13.875  12.631  1    24.33   ? 167  ALA   B C   1 2 
ATOM   6252  O  O   . ALA   B 1  167 ? 17.119  12.918  13.369  1    27.295  ? 167  ALA   B O   1 2 
ATOM   6253  C  CB  . ALA   B 1  167 ? 15.515  15.768  13.511  1    22.45   ? 167  ALA   B CB  1 2 
ATOM   6254  N  N   . GLY   B 1  168 ? 16.534  13.734  11.344  1    23.639  ? 168  GLY   B N   1 2 
ATOM   6255  C  CA  . GLY   B 1  168 ? 16.172  12.46   10.73   1    22.561  ? 168  GLY   B CA  1 2 
ATOM   6256  C  C   . GLY   B 1  168 ? 17.41   11.58   10.517  1    23.705  ? 168  GLY   B C   1 2 
ATOM   6257  O  O   . GLY   B 1  168 ? 17.399  10.406  10.884  1    25.323  ? 168  GLY   B O   1 2 
ATOM   6258  N  N   . ILE   B 1  169 ? 18.448  12.119  9.882   1    24.473  ? 169  ILE   B N   1 2 
ATOM   6259  C  CA  . ILE   B 1  169 ? 19.606  11.294  9.502   1    27.643  ? 169  ILE   B CA  1 2 
ATOM   6260  C  C   . ILE   B 1  169 ? 20.136  10.44   10.675  1    28.304  ? 169  ILE   B C   1 2 
ATOM   6261  O  O   . ILE   B 1  169 ? 20.22   9.189   10.558  1    27.444  ? 169  ILE   B O   1 2 
ATOM   6262  C  CB  . ILE   B 1  169 ? 20.678  12.112  8.752   1    27.573  ? 169  ILE   B CB  1 2 
ATOM   6263  C  CG1 . ILE   B 1  169 ? 20.166  12.602  7.391   1    26.195  ? 169  ILE   B CG1 1 2 
ATOM   6264  C  CG2 . ILE   B 1  169 ? 22.027  11.361  8.66    1    28.23   ? 169  ILE   B CG2 1 2 
ATOM   6265  C  CD1 . ILE   B 1  169 ? 21.03   13.659  6.69    1    26.984  ? 169  ILE   B CD1 1 2 
ATOM   6266  N  N   . PRO   B 1  170 ? 20.543  11.052  11.831  1    27.122  ? 170  PRO   B N   1 2 
ATOM   6267  C  CA  . PRO   B 1  170 ? 21.069  10.286  12.967  1    27.586  ? 170  PRO   B CA  1 2 
ATOM   6268  C  C   . PRO   B 1  170 ? 20.106  9.347   13.695  1    26      ? 170  PRO   B C   1 2 
ATOM   6269  O  O   . PRO   B 1  170 ? 20.534  8.402   14.358  1    25.981  ? 170  PRO   B O   1 2 
ATOM   6270  C  CB  . PRO   B 1  170 ? 21.692  11.345  13.957  1    27.376  ? 170  PRO   B CB  1 2 
ATOM   6271  C  CG  . PRO   B 1  170 ? 21.18   12.657  13.448  1    26.226  ? 170  PRO   B CG  1 2 
ATOM   6272  C  CD  . PRO   B 1  170 ? 20.576  12.504  12.06   1    25.336  ? 170  PRO   B CD  1 2 
ATOM   6273  N  N   . LEU   B 1  171 ? 18.795  9.568   13.534  1    23.515  ? 171  LEU   B N   1 2 
ATOM   6274  C  CA  . LEU   B 1  171 ? 17.791  8.763   14.207  1    23.632  ? 171  LEU   B CA  1 2 
ATOM   6275  C  C   . LEU   B 1  171 ? 17.593  7.411   13.53   1    23.012  ? 171  LEU   B C   1 2 
ATOM   6276  O  O   . LEU   B 1  171 ? 17.263  6.449   14.203  1    23.935  ? 171  LEU   B O   1 2 
ATOM   6277  C  CB  . LEU   B 1  171 ? 16.435  9.494   14.225  1    23.356  ? 171  LEU   B CB  1 2 
ATOM   6278  C  CG  . LEU   B 1  171 ? 16.29   10.617  15.256  1    26.435  ? 171  LEU   B CG  1 2 
ATOM   6279  C  CD1 . LEU   B 1  171 ? 14.919  11.359  15.064  1    25.815  ? 171  LEU   B CD1 1 2 
ATOM   6280  C  CD2 . LEU   B 1  171 ? 16.39   9.938   16.608  1    25.196  ? 171  LEU   B CD2 1 2 
ATOM   6281  N  N   . LYS   B 1  172 ? 17.852  7.339   12.227  1    23.575  ? 172  LYS   B N   1 2 
ATOM   6282  C  CA  . LYS   B 1  172 ? 17.445  6.178   11.439  1    25.743  ? 172  LYS   B CA  1 2 
ATOM   6283  C  C   . LYS   B 1  172 ? 18.018  4.868   11.978  1    26.747  ? 172  LYS   B C   1 2 
ATOM   6284  O  O   . LYS   B 1  172 ? 17.28   3.889   12.155  1    25.67   ? 172  LYS   B O   1 2 
ATOM   6285  C  CB  . LYS   B 1  172 ? 17.868  6.274   9.968   1    26.235  ? 172  LYS   B CB  1 2 
ATOM   6286  C  CG  . LYS   B 1  172 ? 17.229  5.155   9.144   1    27.981  ? 172  LYS   B CG  1 2 
ATOM   6287  C  CD  . LYS   B 1  172 ? 17.6    5.201   7.666   1    32.089  ? 172  LYS   B CD  1 2 
ATOM   6288  C  CE  . LYS   B 1  172 ? 16.832  4.073   6.96    1    35.261  ? 172  LYS   B CE  1 2 
ATOM   6289  N  NZ  . LYS   B 1  172 ? 16.91   4.063   5.493   1    36.199  ? 172  LYS   B NZ  1 2 
ATOM   6290  N  N   . PRO   B 1  173 ? 19.358  4.782   12.222  1    28.726  ? 173  PRO   B N   1 2 
ATOM   6291  C  CA  . PRO   B 1  173 ? 19.936  3.562   12.792  1    30.211  ? 173  PRO   B CA  1 2 
ATOM   6292  C  C   . PRO   B 1  173 ? 19.308  3.114   14.107  1    30.317  ? 173  PRO   B C   1 2 
ATOM   6293  O  O   . PRO   B 1  173 ? 19.066  1.931   14.292  1    31.619  ? 173  PRO   B O   1 2 
ATOM   6294  C  CB  . PRO   B 1  173 ? 21.476  3.774   12.836  1    32.331  ? 173  PRO   B CB  1 2 
ATOM   6295  C  CG  . PRO   B 1  173 ? 21.631  5.269   12.598  1    33.068  ? 173  PRO   B CG  1 2 
ATOM   6296  C  CD  . PRO   B 1  173 ? 20.366  5.786   11.878  1    28.563  ? 173  PRO   B CD  1 2 
ATOM   6297  N  N   . LEU   B 1  174 ? 18.983  4.061   14.991  1    29.474  ? 174  LEU   B N   1 2 
ATOM   6298  C  CA  . LEU   B 1  174 ? 18.354  3.758   16.273  1    29.856  ? 174  LEU   B CA  1 2 
ATOM   6299  C  C   . LEU   B 1  174 ? 16.913  3.282   16.077  1    27.865  ? 174  LEU   B C   1 2 
ATOM   6300  O  O   . LEU   B 1  174 ? 16.44   2.339   16.725  1    28.967  ? 174  LEU   B O   1 2 
ATOM   6301  C  CB  . LEU   B 1  174 ? 18.386  5.06    17.095  1    30.736  ? 174  LEU   B CB  1 2 
ATOM   6302  C  CG  . LEU   B 1  174 ? 19.735  5.43    17.722  1    34.644  ? 174  LEU   B CG  1 2 
ATOM   6303  C  CD1 . LEU   B 1  174 ? 20.954  5.414   16.834  1    37.572  ? 174  LEU   B CD1 1 2 
ATOM   6304  C  CD2 . LEU   B 1  174 ? 19.64   6.728   18.512  1    36.968  ? 174  LEU   B CD2 1 2 
ATOM   6305  N  N   . TYR   B 1  175 ? 16.191  3.973   15.196  1    25.022  ? 175  TYR   B N   1 2 
ATOM   6306  C  CA  . TYR   B 1  175 ? 14.806  3.597   14.969  1    25.234  ? 175  TYR   B CA  1 2 
ATOM   6307  C  C   . TYR   B 1  175 ? 14.706  2.158   14.46   1    25.927  ? 175  TYR   B C   1 2 
ATOM   6308  O  O   . TYR   B 1  175 ? 13.787  1.449   14.833  1    26.115  ? 175  TYR   B O   1 2 
ATOM   6309  C  CB  . TYR   B 1  175 ? 14.091  4.628   14.066  1    24.061  ? 175  TYR   B CB  1 2 
ATOM   6310  C  CG  . TYR   B 1  175 ? 12.584  4.474   14.23   1    22.192  ? 175  TYR   B CG  1 2 
ATOM   6311  C  CD1 . TYR   B 1  175 ? 11.904  5.124   15.259  1    20.687  ? 175  TYR   B CD1 1 2 
ATOM   6312  C  CD2 . TYR   B 1  175 ? 11.849  3.678   13.346  1    21.768  ? 175  TYR   B CD2 1 2 
ATOM   6313  C  CE1 . TYR   B 1  175 ? 10.534  4.963   15.423  1    22.626  ? 175  TYR   B CE1 1 2 
ATOM   6314  C  CE2 . TYR   B 1  175 ? 10.465  3.55    13.483  1    22.827  ? 175  TYR   B CE2 1 2 
ATOM   6315  C  CZ  . TYR   B 1  175 ? 9.799   4.193   14.522  1    21.619  ? 175  TYR   B CZ  1 2 
ATOM   6316  O  OH  . TYR   B 1  175 ? 8.458   4.006   14.75   1    22.419  ? 175  TYR   B OH  1 2 
ATOM   6317  N  N   . GLU   B 1  176 ? 15.649  1.699   13.636  1    27.942  ? 176  GLU   B N   1 2 
ATOM   6318  C  CA  . GLU   B 1  176 ? 15.507  0.327   13.154  1    30.227  ? 176  GLU   B CA  1 2 
ATOM   6319  C  C   . GLU   B 1  176 ? 15.666  -0.671  14.312  1    32.382  ? 176  GLU   B C   1 2 
ATOM   6320  O  O   . GLU   B 1  176 ? 14.961  -1.681  14.398  1    30.603  ? 176  GLU   B O   1 2 
ATOM   6321  C  CB  . GLU   B 1  176 ? 16.587  -0.038  12.152  1    32.584  ? 176  GLU   B CB  1 2 
ATOM   6322  C  CG  . GLU   B 1  176 ? 16.825  0.998   11.064  1    36.477  ? 176  GLU   B CG  1 2 
ATOM   6323  C  CD  . GLU   B 1  176 ? 17.912  0.559   10.082  1    48.157  ? 176  GLU   B CD  1 2 
ATOM   6324  O  OE1 . GLU   B 1  176 ? 18.335  -0.644  10.111  1    47.908  ? 176  GLU   B OE1 1 2 
ATOM   6325  O  OE2 . GLU   B 1  176 ? 18.346  1.449   9.292   1    49.065  ? 176  GLU   B OE2 1 2 
ATOM   6326  N  N   . ASP   B 1  177 ? 16.588  -0.36   15.235  1    34.37   ? 177  ASP   B N   1 2 
ATOM   6327  C  CA  . ASP   B 1  177 ? 16.805  -1.227  16.391  1    34.598  ? 177  ASP   B CA  1 2 
ATOM   6328  C  C   . ASP   B 1  177 ? 15.584  -1.227  17.298  1    33.719  ? 177  ASP   B C   1 2 
ATOM   6329  O  O   . ASP   B 1  177 ? 15.159  -2.277  17.796  1    32.67   ? 177  ASP   B O   1 2 
ATOM   6330  C  CB  . ASP   B 1  177 ? 18.045  -0.774  17.124  1    39.102  ? 177  ASP   B CB  1 2 
ATOM   6331  C  CG  . ASP   B 1  177 ? 19.311  -1.095  16.352  1    43.812  ? 177  ASP   B CG  1 2 
ATOM   6332  O  OD1 . ASP   B 1  177 ? 19.214  -1.88   15.379  1    46.554  ? 177  ASP   B OD1 1 2 
ATOM   6333  O  OD2 . ASP   B 1  177 ? 20.352  -0.504  16.672  1    48.699  ? 177  ASP   B OD2 1 2 
ATOM   6334  N  N   . PHE   B 1  178 ? 15.003  -0.025  17.46   1    30.777  ? 178  PHE   B N   1 2 
ATOM   6335  C  CA  . PHE   B 1  178 ? 13.841  0.124   18.312  1    30.336  ? 178  PHE   B CA  1 2 
ATOM   6336  C  C   . PHE   B 1  178 ? 12.702  -0.741  17.778  1    29.553  ? 178  PHE   B C   1 2 
ATOM   6337  O  O   . PHE   B 1  178 ? 12.048  -1.465  18.539  1    29.646  ? 178  PHE   B O   1 2 
ATOM   6338  C  CB  . PHE   B 1  178 ? 13.491  1.605   18.545  1    29.822  ? 178  PHE   B CB  1 2 
ATOM   6339  C  CG  . PHE   B 1  178 ? 12.013  1.724   18.871  1    31.597  ? 178  PHE   B CG  1 2 
ATOM   6340  C  CD1 . PHE   B 1  178 ? 11.54   1.468   20.154  1    32.798  ? 178  PHE   B CD1 1 2 
ATOM   6341  C  CD2 . PHE   B 1  178 ? 11.099  2.009   17.854  1    34.624  ? 178  PHE   B CD2 1 2 
ATOM   6342  C  CE1 . PHE   B 1  178 ? 10.179  1.529   20.414  1    34.992  ? 178  PHE   B CE1 1 2 
ATOM   6343  C  CE2 . PHE   B 1  178 ? 9.733   2.048   18.106  1    35.759  ? 178  PHE   B CE2 1 2 
ATOM   6344  C  CZ  . PHE   B 1  178 ? 9.275   1.782   19.39   1    35.719  ? 178  PHE   B CZ  1 2 
ATOM   6345  N  N   . THR   B 1  179 ? 12.452  -0.654  16.457  1    26.099  ? 179  THR   B N   1 2 
ATOM   6346  C  CA  . THR   B 1  179 ? 11.325  -1.388  15.893  1    25.712  ? 179  THR   B CA  1 2 
ATOM   6347  C  C   . THR   B 1  179 ? 11.463  -2.881  16.19   1    25.719  ? 179  THR   B C   1 2 
ATOM   6348  O  O   . THR   B 1  179 ? 10.507  -3.539  16.576  1    25.699  ? 179  THR   B O   1 2 
ATOM   6349  C  CB  . THR   B 1  179 ? 11.193  -1.09   14.39   1    24.808  ? 179  THR   B CB  1 2 
ATOM   6350  O  OG1 . THR   B 1  179 ? 11.003  0.317   14.278  1    25.842  ? 179  THR   B OG1 1 2 
ATOM   6351  C  CG2 . THR   B 1  179 ? 10.143  -1.949  13.711  1    25.206  ? 179  THR   B CG2 1 2 
ATOM   6352  N  N   . ALA   B 1  180 ? 12.654  -3.417  15.933  1    27.349  ? 180  ALA   B N   1 2 
ATOM   6353  C  CA  . ALA   B 1  180 ? 12.904  -4.831  16.094  1    29.522  ? 180  ALA   B CA  1 2 
ATOM   6354  C  C   . ALA   B 1  180 ? 12.616  -5.276  17.541  1    31.084  ? 180  ALA   B C   1 2 
ATOM   6355  O  O   . ALA   B 1  180 ? 11.97   -6.312  17.755  1    31.186  ? 180  ALA   B O   1 2 
ATOM   6356  C  CB  . ALA   B 1  180 ? 14.35   -5.082  15.712  1    32.194  ? 180  ALA   B CB  1 2 
ATOM   6357  N  N   . LEU   B 1  181 ? 13.03   -4.47   18.548  1    32.399  ? 181  LEU   B N   1 2 
ATOM   6358  C  CA  . LEU   B 1  181 ? 12.862  -4.863  19.953  1    33.573  ? 181  LEU   B CA  1 2 
ATOM   6359  C  C   . LEU   B 1  181 ? 11.393  -4.786  20.337  1    34.322  ? 181  LEU   B C   1 2 
ATOM   6360  O  O   . LEU   B 1  181 ? 10.844  -5.672  20.991  1    34.832  ? 181  LEU   B O   1 2 
ATOM   6361  C  CB  . LEU   B 1  181 ? 13.698  -3.96   20.858  1    34.966  ? 181  LEU   B CB  1 2 
ATOM   6362  C  CG  . LEU   B 1  181 ? 15.212  -4.182  20.812  1    37.635  ? 181  LEU   B CG  1 2 
ATOM   6363  C  CD1 . LEU   B 1  181 ? 15.977  -3.088  21.5    1    39.781  ? 181  LEU   B CD1 1 2 
ATOM   6364  C  CD2 . LEU   B 1  181 ? 15.66   -5.53   21.357  1    39.307  ? 181  LEU   B CD2 1 2 
ATOM   6365  N  N   . SER   B 1  182 ? 10.741  -3.685  19.926  1    31.115  ? 182  SER   B N   1 2 
ATOM   6366  C  CA  . SER   B 1  182 ? 9.35    -3.506  20.268  1    30.682  ? 182  SER   B CA  1 2 
ATOM   6367  C  C   . SER   B 1  182 ? 8.517   -4.676  19.746  1    31.622  ? 182  SER   B C   1 2 
ATOM   6368  O  O   . SER   B 1  182 ? 7.643   -5.206  20.458  1    30.946  ? 182  SER   B O   1 2 
ATOM   6369  C  CB  . SER   B 1  182 ? 8.875   -2.128  19.788  1    30.549  ? 182  SER   B CB  1 2 
ATOM   6370  O  OG  . SER   B 1  182 ? 7.479   -1.983  19.987  1    30.825  ? 182  SER   B OG  1 2 
ATOM   6371  N  N   . ASN   B 1  183 ? 8.79    -5.086  18.487  1    30.51   ? 183  ASN   B N   1 2 
ATOM   6372  C  CA  . ASN   B 1  183 ? 8.041   -6.183  17.889  1    31.597  ? 183  ASN   B CA  1 2 
ATOM   6373  C  C   . ASN   B 1  183 ? 8.244   -7.486  18.671  1    34.137  ? 183  ASN   B C   1 2 
ATOM   6374  O  O   . ASN   B 1  183 ? 7.288   -8.25   18.861  1    34.983  ? 183  ASN   B O   1 2 
ATOM   6375  C  CB  . ASN   B 1  183 ? 8.409   -6.359  16.421  1    31.238  ? 183  ASN   B CB  1 2 
ATOM   6376  C  CG  . ASN   B 1  183 ? 7.625   -5.437  15.512  1    31.452  ? 183  ASN   B CG  1 2 
ATOM   6377  O  OD1 . ASN   B 1  183 ? 6.604   -4.855  15.924  1    32.847  ? 183  ASN   B OD1 1 2 
ATOM   6378  N  ND2 . ASN   B 1  183 ? 8.087   -5.289  14.274  1    31.311  ? 183  ASN   B ND2 1 2 
ATOM   6379  N  N   A GLU   B 1  184 ? 9.488   -7.772  19.051  0.58 35.638  ? 184  GLU   B N   1 2 
ATOM   6380  N  N   B GLU   B 1  184 ? 9.497   -7.682  19.123  0.42 35.771  ? 184  GLU   B N   1 2 
ATOM   6381  C  CA  A GLU   B 1  184 ? 9.803   -8.992  19.788  0.58 39.134  ? 184  GLU   B CA  1 2 
ATOM   6382  C  CA  B GLU   B 1  184 ? 10.016  -8.869  19.806  0.42 39.521  ? 184  GLU   B CA  1 2 
ATOM   6383  C  C   A GLU   B 1  184 ? 8.947   -9.022  21.055  0.58 40.767  ? 184  GLU   B C   1 2 
ATOM   6384  C  C   B GLU   B 1  184 ? 9.529   -8.935  21.255  0.42 41.24   ? 184  GLU   B C   1 2 
ATOM   6385  O  O   A GLU   B 1  184 ? 8.313   -10.031 21.383  0.58 40.415  ? 184  GLU   B O   1 2 
ATOM   6386  O  O   B GLU   B 1  184 ? 9.767   -9.919  21.945  0.42 43.312  ? 184  GLU   B O   1 2 
ATOM   6387  C  CB  A GLU   B 1  184 ? 11.288  -8.899  20.146  0.58 40.403  ? 184  GLU   B CB  1 2 
ATOM   6388  C  CB  B GLU   B 1  184 ? 11.542  -8.824  19.953  0.42 40.481  ? 184  GLU   B CB  1 2 
ATOM   6389  C  CG  A GLU   B 1  184 ? 11.832  -10.113 20.895  0.58 43.805  ? 184  GLU   B CG  1 2 
ATOM   6390  C  CG  B GLU   B 1  184 ? 12.331  -9.031  18.661  0.42 41.116  ? 184  GLU   B CG  1 2 
ATOM   6391  C  CD  A GLU   B 1  184 ? 13.328  -10.144 21.163  0.58 45.451  ? 184  GLU   B CD  1 2 
ATOM   6392  C  CD  B GLU   B 1  184 ? 13.836  -9.278  18.77   0.42 42.05   ? 184  GLU   B CD  1 2 
ATOM   6393  O  OE1 A GLU   B 1  184 ? 14.098  -9.411  20.505  0.58 44.109  ? 184  GLU   B OE1 1 2 
ATOM   6394  O  OE1 B GLU   B 1  184 ? 14.204  -10.435 19.073  0.42 44.257  ? 184  GLU   B OE1 1 2 
ATOM   6395  O  OE2 A GLU   B 1  184 ? 13.723  -10.923 22.066  0.58 48.956  ? 184  GLU   B OE2 1 2 
ATOM   6396  O  OE2 B GLU   B 1  184 ? 14.648  -8.34   18.548  0.42 40.683  ? 184  GLU   B OE2 1 2 
ATOM   6397  N  N   . ALA   B 1  185 ? 8.892   -7.854  21.718  1    40.802  ? 185  ALA   B N   1 2 
ATOM   6398  C  CA  . ALA   B 1  185 ? 8.265   -7.735  23.016  1    42.621  ? 185  ALA   B CA  1 2 
ATOM   6399  C  C   . ALA   B 1  185 ? 6.787   -8.088  22.868  1    43.746  ? 185  ALA   B C   1 2 
ATOM   6400  O  O   . ALA   B 1  185 ? 6.285   -8.934  23.609  1    45.887  ? 185  ALA   B O   1 2 
ATOM   6401  C  CB  . ALA   B 1  185 ? 8.478   -6.311  23.501  1    41.579  ? 185  ALA   B CB  1 2 
ATOM   6402  N  N   . TYR   B 1  186 ? 6.111   -7.496  21.868  1    40.047  ? 186  TYR   B N   1 2 
ATOM   6403  C  CA  . TYR   B 1  186 ? 4.662   -7.579  21.826  1    41.369  ? 186  TYR   B CA  1 2 
ATOM   6404  C  C   . TYR   B 1  186 ? 4.193   -8.917  21.253  1    43.866  ? 186  TYR   B C   1 2 
ATOM   6405  O  O   . TYR   B 1  186 ? 3.078   -9.357  21.561  1    44.589  ? 186  TYR   B O   1 2 
ATOM   6406  C  CB  . TYR   B 1  186 ? 3.966   -6.331  21.258  1    41.606  ? 186  TYR   B CB  1 2 
ATOM   6407  C  CG  . TYR   B 1  186 ? 4.001   -5.15   22.222  1    41.267  ? 186  TYR   B CG  1 2 
ATOM   6408  C  CD1 . TYR   B 1  186 ? 3.115   -5.079  23.302  1    44.807  ? 186  TYR   B CD1 1 2 
ATOM   6409  C  CD2 . TYR   B 1  186 ? 4.965   -4.158  22.105  1    39.829  ? 186  TYR   B CD2 1 2 
ATOM   6410  C  CE1 . TYR   B 1  186 ? 3.15    -4.021  24.203  1    44.013  ? 186  TYR   B CE1 1 2 
ATOM   6411  C  CE2 . TYR   B 1  186 ? 4.993   -3.088  22.979  1    41.447  ? 186  TYR   B CE2 1 2 
ATOM   6412  C  CZ  . TYR   B 1  186 ? 4.1     -3.03   24.04   1    43.484  ? 186  TYR   B CZ  1 2 
ATOM   6413  O  OH  . TYR   B 1  186 ? 4.169   -1.984  24.908  1    42.839  ? 186  TYR   B OH  1 2 
ATOM   6414  N  N   . LYS   B 1  187 ? 5.046   -9.57   20.449  1    45.122  ? 187  LYS   B N   1 2 
ATOM   6415  C  CA  . LYS   B 1  187 ? 4.708   -10.873 19.878  1    48.672  ? 187  LYS   B CA  1 2 
ATOM   6416  C  C   . LYS   B 1  187 ? 4.406   -11.891 20.984  1    49.664  ? 187  LYS   B C   1 2 
ATOM   6417  O  O   . LYS   B 1  187 ? 3.584   -12.795 20.814  1    50.519  ? 187  LYS   B O   1 2 
ATOM   6418  C  CB  . LYS   B 1  187 ? 5.774   -11.355 18.884  1    52.769  ? 187  LYS   B CB  1 2 
ATOM   6419  C  CG  . LYS   B 1  187 ? 5.543   -10.738 17.499  1    60.385  ? 187  LYS   B CG  1 2 
ATOM   6420  C  CD  . LYS   B 1  187 ? 6.492   -11.087 16.354  1    66.516  ? 187  LYS   B CD  1 2 
ATOM   6421  C  CE  . LYS   B 1  187 ? 6.505   -12.551 15.97   1    72.676  ? 187  LYS   B CE  1 2 
ATOM   6422  N  NZ  . LYS   B 1  187 ? 7.287   -12.773 14.743  1    73.092  ? 187  LYS   B NZ  1 2 
ATOM   6423  N  N   . GLN   B 1  188 ? 5.028   -11.695 22.144  1    48.9    ? 188  GLN   B N   1 2 
ATOM   6424  C  CA  . GLN   B 1  188 ? 4.822   -12.601 23.258  1    52.351  ? 188  GLN   B CA  1 2 
ATOM   6425  C  C   . GLN   B 1  188 ? 3.483   -12.385 23.968  1    54.005  ? 188  GLN   B C   1 2 
ATOM   6426  O  O   . GLN   B 1  188 ? 3.112   -13.193 24.808  1    57.178  ? 188  GLN   B O   1 2 
ATOM   6427  C  CB  . GLN   B 1  188 ? 6.117   -12.655 24.062  1    53.095  ? 188  GLN   B CB  1 2 
ATOM   6428  C  CG  . GLN   B 1  188 ? 7.288   -13.04  23.162  1    55.316  ? 188  GLN   B CG  1 2 
ATOM   6429  C  CD  . GLN   B 1  188 ? 8.619   -13.043 23.873  1    57.66   ? 188  GLN   B CD  1 2 
ATOM   6430  O  OE1 . GLN   B 1  188 ? 8.899   -13.932 24.679  1    61.421  ? 188  GLN   B OE1 1 2 
ATOM   6431  N  NE2 . GLN   B 1  188 ? 9.453   -12.058 23.575  1    57.394  ? 188  GLN   B NE2 1 2 
ATOM   6432  N  N   . ASP   B 1  189 ? 2.719   -11.352 23.597  1    50.482  ? 189  ASP   B N   1 2 
ATOM   6433  C  CA  . ASP   B 1  189 ? 1.392   -11.187 24.163  1    52.997  ? 189  ASP   B CA  1 2 
ATOM   6434  C  C   . ASP   B 1  189 ? 0.336   -11.645 23.167  1    54.446  ? 189  ASP   B C   1 2 
ATOM   6435  O  O   . ASP   B 1  189 ? -0.855  -11.527 23.446  1    57.568  ? 189  ASP   B O   1 2 
ATOM   6436  C  CB  . ASP   B 1  189 ? 1.173   -9.777  24.679  1    56.634  ? 189  ASP   B CB  1 2 
ATOM   6437  C  CG  . ASP   B 1  189 ? 2.372   -9.206  25.424  1    61.88   ? 189  ASP   B CG  1 2 
ATOM   6438  O  OD1 . ASP   B 1  189 ? 3.299   -9.998  25.705  1    65.065  ? 189  ASP   B OD1 1 2 
ATOM   6439  O  OD2 . ASP   B 1  189 ? 2.407   -7.97   25.665  1    59.246  ? 189  ASP   B OD2 1 2 
ATOM   6440  N  N   . GLY   B 1  190 ? 0.778   -12.168 22.013  1    52.134  ? 190  GLY   B N   1 2 
ATOM   6441  C  CA  . GLY   B 1  190 ? -0.149  -12.727 21.046  1    52.615  ? 190  GLY   B CA  1 2 
ATOM   6442  C  C   . GLY   B 1  190 ? -0.426  -11.766 19.893  1    50.667  ? 190  GLY   B C   1 2 
ATOM   6443  O  O   . GLY   B 1  190 ? -1.208  -12.085 18.99   1    51.128  ? 190  GLY   B O   1 2 
ATOM   6444  N  N   . PHE   B 1  191 ? 0.242   -10.603 19.91   1    50.011  ? 191  PHE   B N   1 2 
ATOM   6445  C  CA  . PHE   B 1  191 ? 0.108   -9.618  18.848  1    44.763  ? 191  PHE   B CA  1 2 
ATOM   6446  C  C   . PHE   B 1  191 ? 1.072   -9.909  17.704  1    45.951  ? 191  PHE   B C   1 2 
ATOM   6447  O  O   . PHE   B 1  191 ? 2.259   -10.13  17.936  1    47.405  ? 191  PHE   B O   1 2 
ATOM   6448  C  CB  . PHE   B 1  191 ? 0.446   -8.224  19.392  1    42.976  ? 191  PHE   B CB  1 2 
ATOM   6449  C  CG  . PHE   B 1  191 ? -0.571  -7.825  20.436  1    39.625  ? 191  PHE   B CG  1 2 
ATOM   6450  C  CD1 . PHE   B 1  191 ? -1.871  -7.512  20.061  1    38.3    ? 191  PHE   B CD1 1 2 
ATOM   6451  C  CD2 . PHE   B 1  191 ? -0.237  -7.827  21.786  1    42.915  ? 191  PHE   B CD2 1 2 
ATOM   6452  C  CE1 . PHE   B 1  191 ? -2.815  -7.158  21.012  1    39.385  ? 191  PHE   B CE1 1 2 
ATOM   6453  C  CE2 . PHE   B 1  191 ? -1.205  -7.516  22.747  1    43.894  ? 191  PHE   B CE2 1 2 
ATOM   6454  C  CZ  . PHE   B 1  191 ? -2.486  -7.163  22.351  1    42.511  ? 191  PHE   B CZ  1 2 
ATOM   6455  N  N   . THR   B 1  192 ? 0.563   -9.807  16.464  1    43.155  ? 192  THR   B N   1 2 
ATOM   6456  C  CA  . THR   B 1  192 ? 1.393   -10.012 15.286  1    42.158  ? 192  THR   B CA  1 2 
ATOM   6457  C  C   . THR   B 1  192 ? 2.552   -8.999  15.269  1    38.807  ? 192  THR   B C   1 2 
ATOM   6458  O  O   . THR   B 1  192 ? 3.693   -9.337  14.947  1    38.157  ? 192  THR   B O   1 2 
ATOM   6459  C  CB  . THR   B 1  192 ? 0.498   -10.025 14.043  1    46.609  ? 192  THR   B CB  1 2 
ATOM   6460  O  OG1 . THR   B 1  192 ? 1.438   -10.276 13.012  1    54.874  ? 192  THR   B OG1 1 2 
ATOM   6461  C  CG2 . THR   B 1  192 ? -0.249  -8.728  13.765  1    41.566  ? 192  THR   B CG2 1 2 
ATOM   6462  N  N   . ASP   B 1  193 ? 2.295   -7.759  15.731  1    35.61   ? 193  ASP   B N   1 2 
ATOM   6463  C  CA  . ASP   B 1  193 ? 3.338   -6.759  15.868  1    33.023  ? 193  ASP   B CA  1 2 
ATOM   6464  C  C   . ASP   B 1  193 ? 2.836   -5.602  16.736  1    30.795  ? 193  ASP   B C   1 2 
ATOM   6465  O  O   . ASP   B 1  193 ? 1.647   -5.512  17.05   1    32.081  ? 193  ASP   B O   1 2 
ATOM   6466  C  CB  . ASP   B 1  193 ? 3.804   -6.282  14.496  1    31.793  ? 193  ASP   B CB  1 2 
ATOM   6467  C  CG  . ASP   B 1  193 ? 2.708   -5.613  13.683  1    32.933  ? 193  ASP   B CG  1 2 
ATOM   6468  O  OD1 . ASP   B 1  193 ? 2.292   -4.483  14.095  1    32.649  ? 193  ASP   B OD1 1 2 
ATOM   6469  O  OD2 . ASP   B 1  193 ? 2.282   -6.194  12.632  1    33.669  ? 193  ASP   B OD2 1 2 
ATOM   6470  N  N   . THR   B 1  194 ? 3.746   -4.681  17.061  1    30.788  ? 194  THR   B N   1 2 
ATOM   6471  C  CA  . THR   B 1  194 ? 3.419   -3.539  17.923  1    31.218  ? 194  THR   B CA  1 2 
ATOM   6472  C  C   . THR   B 1  194 ? 2.215   -2.747  17.418  1    31.419  ? 194  THR   B C   1 2 
ATOM   6473  O  O   . THR   B 1  194 ? 1.478   -2.232  18.239  1    33.604  ? 194  THR   B O   1 2 
ATOM   6474  C  CB  . THR   B 1  194 ? 4.578   -2.573  18.038  1    29.11   ? 194  THR   B CB  1 2 
ATOM   6475  O  OG1 . THR   B 1  194 ? 5.632   -3.424  18.429  1    31.34   ? 194  THR   B OG1 1 2 
ATOM   6476  C  CG2 . THR   B 1  194 ? 4.37    -1.513  19.102  1    29.557  ? 194  THR   B CG2 1 2 
ATOM   6477  N  N   . GLY   B 1  195 ? 2.087   -2.553  16.093  1    29.693  ? 195  GLY   B N   1 2 
ATOM   6478  C  CA  . GLY   B 1  195 ? 1.004   -1.757  15.546  1    25.977  ? 195  GLY   B CA  1 2 
ATOM   6479  C  C   . GLY   B 1  195 ? -0.322  -2.395  15.915  1    28.491  ? 195  GLY   B C   1 2 
ATOM   6480  O  O   . GLY   B 1  195 ? -1.285  -1.694  16.231  1    27.245  ? 195  GLY   B O   1 2 
ATOM   6481  N  N   . ALA   B 1  196 ? -0.35   -3.738  15.963  1    27.399  ? 196  ALA   B N   1 2 
ATOM   6482  C  CA  . ALA   B 1  196 ? -1.597  -4.444  16.26   1    29.761  ? 196  ALA   B CA  1 2 
ATOM   6483  C  C   . ALA   B 1  196 ? -2.018  -4.197  17.709  1    29.645  ? 196  ALA   B C   1 2 
ATOM   6484  O  O   . ALA   B 1  196 ? -3.213  -4.15   18.025  1    32.823  ? 196  ALA   B O   1 2 
ATOM   6485  C  CB  . ALA   B 1  196 ? -1.49   -5.939  15.971  1    31.256  ? 196  ALA   B CB  1 2 
ATOM   6486  N  N   . TYR   B 1  197 ? -1.026  -4.075  18.577  1    29.185  ? 197  TYR   B N   1 2 
ATOM   6487  C  CA  . TYR   B 1  197 ? -1.262  -3.799  19.983  1    31.786  ? 197  TYR   B CA  1 2 
ATOM   6488  C  C   . TYR   B 1  197 ? -1.833  -2.375  20.105  1    31.018  ? 197  TYR   B C   1 2 
ATOM   6489  O  O   . TYR   B 1  197 ? -2.907  -2.154  20.677  1    29.808  ? 197  TYR   B O   1 2 
ATOM   6490  C  CB  . TYR   B 1  197 ? 0.094   -3.939  20.687  1    33.04   ? 197  TYR   B CB  1 2 
ATOM   6491  C  CG  . TYR   B 1  197 ? 0.022   -3.391  22.106  1    35.559  ? 197  TYR   B CG  1 2 
ATOM   6492  C  CD1 . TYR   B 1  197 ? -0.965  -3.827  22.992  1    37.657  ? 197  TYR   B CD1 1 2 
ATOM   6493  C  CD2 . TYR   B 1  197 ? 0.89    -2.39   22.542  1    35.387  ? 197  TYR   B CD2 1 2 
ATOM   6494  C  CE1 . TYR   B 1  197 ? -1.066  -3.315  24.278  1    39.907  ? 197  TYR   B CE1 1 2 
ATOM   6495  C  CE2 . TYR   B 1  197 ? 0.794   -1.867  23.828  1    39.661  ? 197  TYR   B CE2 1 2 
ATOM   6496  C  CZ  . TYR   B 1  197 ? -0.194  -2.325  24.687  1    40.966  ? 197  TYR   B CZ  1 2 
ATOM   6497  O  OH  . TYR   B 1  197 ? -0.3    -1.833  25.958  1    47.912  ? 197  TYR   B OH  1 2 
ATOM   6498  N  N   . TRP   B 1  198 ? -1.15   -1.414  19.463  1    30.364  ? 198  TRP   B N   1 2 
ATOM   6499  C  CA  . TRP   B 1  198 ? -1.559  -0.02   19.511  1    28.089  ? 198  TRP   B CA  1 2 
ATOM   6500  C  C   . TRP   B 1  198 ? -3.007  0.089   19.055  1    28.266  ? 198  TRP   B C   1 2 
ATOM   6501  O  O   . TRP   B 1  198 ? -3.796  0.772   19.686  1    29.455  ? 198  TRP   B O   1 2 
ATOM   6502  C  CB  . TRP   B 1  198 ? -0.617  0.841   18.652  1    27.797  ? 198  TRP   B CB  1 2 
ATOM   6503  C  CG  . TRP   B 1  198 ? 0.735   1.151   19.23   1    25.774  ? 198  TRP   B CG  1 2 
ATOM   6504  C  CD1 . TRP   B 1  198 ? 1.293   0.644   20.37   1    27.637  ? 198  TRP   B CD1 1 2 
ATOM   6505  C  CD2 . TRP   B 1  198 ? 1.712   2.061   18.663  1    25.043  ? 198  TRP   B CD2 1 2 
ATOM   6506  N  NE1 . TRP   B 1  198 ? 2.541   1.173   20.545  1    27.791  ? 198  TRP   B NE1 1 2 
ATOM   6507  C  CE2 . TRP   B 1  198 ? 2.822   2.054   19.528  1    25.216  ? 198  TRP   B CE2 1 2 
ATOM   6508  C  CE3 . TRP   B 1  198 ? 1.739   2.89    17.52   1    23.42   ? 198  TRP   B CE3 1 2 
ATOM   6509  C  CZ2 . TRP   B 1  198 ? 3.951   2.825   19.297  1    24.765  ? 198  TRP   B CZ2 1 2 
ATOM   6510  C  CZ3 . TRP   B 1  198 ? 2.858   3.665   17.29   1    22.963  ? 198  TRP   B CZ3 1 2 
ATOM   6511  C  CH2 . TRP   B 1  198 ? 3.949   3.638   18.175  1    24.546  ? 198  TRP   B CH2 1 2 
ATOM   6512  N  N   . ARG   B 1  199 ? -3.371  -0.619  17.978  1    27.764  ? 199  ARG   B N   1 2 
ATOM   6513  C  CA  . ARG   B 1  199 ? -4.717  -0.606  17.425  1    28.082  ? 199  ARG   B CA  1 2 
ATOM   6514  C  C   . ARG   B 1  199 ? -5.682  -1.307  18.397  1    32.334  ? 199  ARG   B C   1 2 
ATOM   6515  O  O   . ARG   B 1  199 ? -6.855  -0.952  18.452  1    31.699  ? 199  ARG   B O   1 2 
ATOM   6516  C  CB  . ARG   B 1  199 ? -4.843  -1.258  16.03   1    27.546  ? 199  ARG   B CB  1 2 
ATOM   6517  C  CG  . ARG   B 1  199 ? -4.111  -0.488  14.93   1    25.836  ? 199  ARG   B CG  1 2 
ATOM   6518  C  CD  . ARG   B 1  199 ? -4.469  -1.012  13.56   1    26.441  ? 199  ARG   B CD  1 2 
ATOM   6519  N  NE  . ARG   B 1  199 ? -3.895  -2.356  13.399  1    28.929  ? 199  ARG   B NE  1 2 
ATOM   6520  C  CZ  . ARG   B 1  199 ? -2.65   -2.742  13.084  1    29.413  ? 199  ARG   B CZ  1 2 
ATOM   6521  N  NH1 . ARG   B 1  199 ? -2.418  -4.044  12.969  1    30.013  ? 199  ARG   B NH1 1 2 
ATOM   6522  N  NH2 . ARG   B 1  199 ? -1.653  -1.874  12.884  1    24.6    ? 199  ARG   B NH2 1 2 
ATOM   6523  N  N   . SER   B 1  200 ? -5.19   -2.286  19.177  1    34.464  ? 200  SER   B N   1 2 
ATOM   6524  C  CA  . SER   B 1  200 ? -6.088  -2.979  20.1    1    38.855  ? 200  SER   B CA  1 2 
ATOM   6525  C  C   . SER   B 1  200 ? -6.812  -2.01   21.046  1    41.298  ? 200  SER   B C   1 2 
ATOM   6526  O  O   . SER   B 1  200 ? -7.942  -2.293  21.456  1    43.006  ? 200  SER   B O   1 2 
ATOM   6527  C  CB  . SER   B 1  200 ? -5.417  -4.102  20.84   1    37.903  ? 200  SER   B CB  1 2 
ATOM   6528  O  OG  . SER   B 1  200 ? -4.361  -3.64   21.677  1    37.736  ? 200  SER   B OG  1 2 
ATOM   6529  N  N   . TRP   B 1  201 ? -6.203  -0.84   21.311  1    40.546  ? 201  TRP   B N   1 2 
ATOM   6530  C  CA  . TRP   B 1  201 ? -6.693  0.142   22.277  1    42.182  ? 201  TRP   B CA  1 2 
ATOM   6531  C  C   . TRP   B 1  201 ? -8.071  0.676   21.917  1    42.012  ? 201  TRP   B C   1 2 
ATOM   6532  O  O   . TRP   B 1  201 ? -8.69   1.319   22.748  1    53.102  ? 201  TRP   B O   1 2 
ATOM   6533  C  CB  . TRP   B 1  201 ? -5.758  1.348   22.42   1    39.281  ? 201  TRP   B CB  1 2 
ATOM   6534  C  CG  . TRP   B 1  201 ? -4.406  1.026   22.975  1    36.418  ? 201  TRP   B CG  1 2 
ATOM   6535  C  CD1 . TRP   B 1  201 ? -4.057  -0.017  23.77   1    41.327  ? 201  TRP   B CD1 1 2 
ATOM   6536  C  CD2 . TRP   B 1  201 ? -3.201  1.758   22.704  1    37.758  ? 201  TRP   B CD2 1 2 
ATOM   6537  N  NE1 . TRP   B 1  201 ? -2.718  0.036   24.041  1    44.008  ? 201  TRP   B NE1 1 2 
ATOM   6538  C  CE2 . TRP   B 1  201 ? -2.164  1.111   23.393  1    39.492  ? 201  TRP   B CE2 1 2 
ATOM   6539  C  CE3 . TRP   B 1  201 ? -2.9    2.889   21.935  1    33.153  ? 201  TRP   B CE3 1 2 
ATOM   6540  C  CZ2 . TRP   B 1  201 ? -0.847  1.564   23.351  1    39.022  ? 201  TRP   B CZ2 1 2 
ATOM   6541  C  CZ3 . TRP   B 1  201 ? -1.596  3.327   21.892  1    34.811  ? 201  TRP   B CZ3 1 2 
ATOM   6542  C  CH2 . TRP   B 1  201 ? -0.581  2.68    22.596  1    35.936  ? 201  TRP   B CH2 1 2 
ATOM   6543  N  N   . TYR   B 1  202 ? -8.529  0.451   20.691  1    37.943  ? 202  TYR   B N   1 2 
ATOM   6544  C  CA  . TYR   B 1  202 ? -9.797  0.98    20.245  1    35.137  ? 202  TYR   B CA  1 2 
ATOM   6545  C  C   . TYR   B 1  202 ? -10.887 -0.083  20.332  1    39.639  ? 202  TYR   B C   1 2 
ATOM   6546  O  O   . TYR   B 1  202 ? -12.028 0.215   20.007  1    41.54   ? 202  TYR   B O   1 2 
ATOM   6547  C  CB  . TYR   B 1  202 ? -9.628  1.55    18.842  1    31.252  ? 202  TYR   B CB  1 2 
ATOM   6548  C  CG  . TYR   B 1  202 ? -8.792  2.818   18.934  1    28.117  ? 202  TYR   B CG  1 2 
ATOM   6549  C  CD1 . TYR   B 1  202 ? -9.414  4.042   19.153  1    27.478  ? 202  TYR   B CD1 1 2 
ATOM   6550  C  CD2 . TYR   B 1  202 ? -7.399  2.788   18.866  1    27.257  ? 202  TYR   B CD2 1 2 
ATOM   6551  C  CE1 . TYR   B 1  202 ? -8.682  5.209   19.255  1    25.835  ? 202  TYR   B CE1 1 2 
ATOM   6552  C  CE2 . TYR   B 1  202 ? -6.636  3.943   19.002  1    25.065  ? 202  TYR   B CE2 1 2 
ATOM   6553  C  CZ  . TYR   B 1  202 ? -7.295  5.164   19.162  1    26.286  ? 202  TYR   B CZ  1 2 
ATOM   6554  O  OH  . TYR   B 1  202 ? -6.66   6.36    19.329  1    23.865  ? 202  TYR   B OH  1 2 
ATOM   6555  N  N   . ASN   B 1  203 ? -10.52  -1.314  20.726  1    43.962  ? 203  ASN   B N   1 2 
ATOM   6556  C  CA  . ASN   B 1  203 ? -11.381 -2.497  20.678  1    46.578  ? 203  ASN   B CA  1 2 
ATOM   6557  C  C   . ASN   B 1  203 ? -12.436 -2.435  19.598  1    47.206  ? 203  ASN   B C   1 2 
ATOM   6558  O  O   . ASN   B 1  203 ? -13.624 -2.328  19.895  1    45.56   ? 203  ASN   B O   1 2 
ATOM   6559  C  CB  . ASN   B 1  203 ? -12.378 -2.564  21.814  1    48.27   ? 203  ASN   B CB  1 2 
ATOM   6560  C  CG  . ASN   B 1  203 ? -11.674 -3.117  23.012  1    51.477  ? 203  ASN   B CG  1 2 
ATOM   6561  O  OD1 . ASN   B 1  203 ? -10.901 -2.379  23.63   1    55.118  ? 203  ASN   B OD1 1 2 
ATOM   6562  N  ND2 . ASN   B 1  203 ? -11.903 -4.39   23.309  1    53.247  ? 203  ASN   B ND2 1 2 
ATOM   6563  N  N   . SER   B 1  204 ? -11.98  -2.524  18.355  1    48.289  ? 204  SER   B N   1 2 
ATOM   6564  C  CA  . SER   B 1  204 ? -12.913 -2.491  17.255  1    52.43   ? 204  SER   B CA  1 2 
ATOM   6565  C  C   . SER   B 1  204 ? -12.337 -3.395  16.179  1    56.565  ? 204  SER   B C   1 2 
ATOM   6566  O  O   . SER   B 1  204 ? -11.191 -3.197  15.761  1    55.452  ? 204  SER   B O   1 2 
ATOM   6567  C  CB  . SER   B 1  204 ? -13.144 -1.081  16.774  1    54.91   ? 204  SER   B CB  1 2 
ATOM   6568  O  OG  . SER   B 1  204 ? -14.189 -1.084  15.816  1    61.589  ? 204  SER   B OG  1 2 
ATOM   6569  N  N   . PRO   B 1  205 ? -13.084 -4.455  15.788  1    57.242  ? 205  PRO   B N   1 2 
ATOM   6570  C  CA  . PRO   B 1  205 ? -12.623 -5.382  14.754  1    55.906  ? 205  PRO   B CA  1 2 
ATOM   6571  C  C   . PRO   B 1  205 ? -12.474 -4.632  13.435  1    53.582  ? 205  PRO   B C   1 2 
ATOM   6572  O  O   . PRO   B 1  205 ? -11.518 -4.857  12.702  1    57.534  ? 205  PRO   B O   1 2 
ATOM   6573  C  CB  . PRO   B 1  205 ? -13.696 -6.502  14.706  1    55.133  ? 205  PRO   B CB  1 2 
ATOM   6574  C  CG  . PRO   B 1  205 ? -14.498 -6.295  15.982  1    57.701  ? 205  PRO   B CG  1 2 
ATOM   6575  C  CD  . PRO   B 1  205 ? -14.415 -4.811  16.317  1    58.431  ? 205  PRO   B CD  1 2 
ATOM   6576  N  N   . THR   B 1  206 ? -13.389 -3.701  13.145  1    49.417  ? 206  THR   B N   1 2 
ATOM   6577  C  CA  . THR   B 1  206 ? -13.326 -3.03   11.857  1    46.777  ? 206  THR   B CA  1 2 
ATOM   6578  C  C   . THR   B 1  206 ? -12.627 -1.65   11.936  1    43.417  ? 206  THR   B C   1 2 
ATOM   6579  O  O   . THR   B 1  206 ? -12.957 -0.763  11.149  1    41.255  ? 206  THR   B O   1 2 
ATOM   6580  C  CB  . THR   B 1  206 ? -14.757 -2.918  11.333  1    46.831  ? 206  THR   B CB  1 2 
ATOM   6581  O  OG1 . THR   B 1  206 ? -15.348 -2.285  12.462  1    46.964  ? 206  THR   B OG1 1 2 
ATOM   6582  C  CG2 . THR   B 1  206 ? -15.37  -4.256  10.96   1    50.185  ? 206  THR   B CG2 1 2 
ATOM   6583  N  N   . PHE   B 1  207 ? -11.666 -1.464  12.861  1    39.427  ? 207  PHE   B N   1 2 
ATOM   6584  C  CA  . PHE   B 1  207 ? -10.982 -0.185  13.091  1    39.083  ? 207  PHE   B CA  1 2 
ATOM   6585  C  C   . PHE   B 1  207 ? -10.422 0.432   11.798  1    36.104  ? 207  PHE   B C   1 2 
ATOM   6586  O  O   . PHE   B 1  207 ? -10.757 1.566   11.46   1    36.98   ? 207  PHE   B O   1 2 
ATOM   6587  C  CB  . PHE   B 1  207 ? -9.872  -0.249  14.147  1    34.498  ? 207  PHE   B CB  1 2 
ATOM   6588  C  CG  . PHE   B 1  207 ? -9.256  1.077   14.594  1    32.255  ? 207  PHE   B CG  1 2 
ATOM   6589  C  CD1 . PHE   B 1  207 ? -10.054 2.152   14.982  1    30.157  ? 207  PHE   B CD1 1 2 
ATOM   6590  C  CD2 . PHE   B 1  207 ? -7.869  1.258   14.605  1    31.695  ? 207  PHE   B CD2 1 2 
ATOM   6591  C  CE1 . PHE   B 1  207 ? -9.487  3.347   15.41   1    29.026  ? 207  PHE   B CE1 1 2 
ATOM   6592  C  CE2 . PHE   B 1  207 ? -7.303  2.451   15.05   1    30.862  ? 207  PHE   B CE2 1 2 
ATOM   6593  C  CZ  . PHE   B 1  207 ? -8.119  3.501   15.437  1    30.308  ? 207  PHE   B CZ  1 2 
ATOM   6594  N  N   . GLU   B 1  208 ? -9.567  -0.313  11.088  1    37.704  ? 208  GLU   B N   1 2 
ATOM   6595  C  CA  . GLU   B 1  208 ? -8.908  0.176   9.888   1    36.147  ? 208  GLU   B CA  1 2 
ATOM   6596  C  C   . GLU   B 1  208 ? -9.919  0.594   8.827   1    38.651  ? 208  GLU   B C   1 2 
ATOM   6597  O  O   . GLU   B 1  208 ? -9.836  1.713   8.332   1    37.637  ? 208  GLU   B O   1 2 
ATOM   6598  C  CB  . GLU   B 1  208 ? -7.785  -0.716  9.366   1    39.216  ? 208  GLU   B CB  1 2 
ATOM   6599  C  CG  . GLU   B 1  208 ? -6.571  -0.702  10.287  1    37.798  ? 208  GLU   B CG  1 2 
ATOM   6600  C  CD  . GLU   B 1  208 ? -5.341  -1.444  9.766   1    42.417  ? 208  GLU   B CD  1 2 
ATOM   6601  O  OE1 . GLU   B 1  208 ? -4.661  -0.916  8.85    1    42.384  ? 208  GLU   B OE1 1 2 
ATOM   6602  O  OE2 . GLU   B 1  208 ? -5.044  -2.553  10.272  1    43.71   ? 208  GLU   B OE2 1 2 
ATOM   6603  N  N   . ASP   B 1  209 ? -10.868 -0.29   8.508   1    37.239  ? 209  ASP   B N   1 2 
ATOM   6604  C  CA  . ASP   B 1  209 ? -11.964 -0.029  7.578   1    39.204  ? 209  ASP   B CA  1 2 
ATOM   6605  C  C   . ASP   B 1  209 ? -12.776 1.205   7.977   1    36.231  ? 209  ASP   B C   1 2 
ATOM   6606  O  O   . ASP   B 1  209 ? -13.079 2.036   7.132   1    36.563  ? 209  ASP   B O   1 2 
ATOM   6607  C  CB  . ASP   B 1  209 ? -12.856 -1.249  7.431   1    46.253  ? 209  ASP   B CB  1 2 
ATOM   6608  C  CG  . ASP   B 1  209 ? -12.152 -2.472  6.865   1    54.368  ? 209  ASP   B CG  1 2 
ATOM   6609  O  OD1 . ASP   B 1  209 ? -11.055 -2.286  6.292   1    60.7    ? 209  ASP   B OD1 1 2 
ATOM   6610  O  OD2 . ASP   B 1  209 ? -12.68  -3.601  7.027   1    61.733  ? 209  ASP   B OD2 1 2 
ATOM   6611  N  N   . ASP   B 1  210 ? -13.128 1.321   9.263   1    34.874  ? 210  ASP   B N   1 2 
ATOM   6612  C  CA  . ASP   B 1  210 ? -13.867 2.467   9.777   1    34.919  ? 210  ASP   B CA  1 2 
ATOM   6613  C  C   . ASP   B 1  210 ? -13.138 3.787   9.528   1    31.172  ? 210  ASP   B C   1 2 
ATOM   6614  O  O   . ASP   B 1  210 ? -13.763 4.736   9.053   1    30.582  ? 210  ASP   B O   1 2 
ATOM   6615  C  CB  . ASP   B 1  210 ? -14.183 2.318   11.253  1    36.522  ? 210  ASP   B CB  1 2 
ATOM   6616  C  CG  . ASP   B 1  210 ? -15.158 1.186   11.549  1    43.073  ? 210  ASP   B CG  1 2 
ATOM   6617  O  OD1 . ASP   B 1  210 ? -15.664 0.557   10.575  1    43.125  ? 210  ASP   B OD1 1 2 
ATOM   6618  O  OD2 . ASP   B 1  210 ? -15.407 0.941   12.75   1    48.445  ? 210  ASP   B OD2 1 2 
ATOM   6619  N  N   . LEU   B 1  211 ? -11.842 3.854   9.887   1    27.49   ? 211  LEU   B N   1 2 
ATOM   6620  C  CA  . LEU   B 1  211 ? -11.013 5.023   9.619   1    26.789  ? 211  LEU   B CA  1 2 
ATOM   6621  C  C   . LEU   B 1  211 ? -11.024 5.359   8.126   1    27.996  ? 211  LEU   B C   1 2 
ATOM   6622  O  O   . LEU   B 1  211 ? -11.089 6.524   7.726   1    25.839  ? 211  LEU   B O   1 2 
ATOM   6623  C  CB  . LEU   B 1  211 ? -9.585  4.682   10.049  1    27.555  ? 211  LEU   B CB  1 2 
ATOM   6624  C  CG  . LEU   B 1  211 ? -9.298  4.584   11.552  1    28.412  ? 211  LEU   B CG  1 2 
ATOM   6625  C  CD1 . LEU   B 1  211 ? -7.866  4.114   11.724  1    28.561  ? 211  LEU   B CD1 1 2 
ATOM   6626  C  CD2 . LEU   B 1  211 ? -9.516  5.873   12.318  1    26.454  ? 211  LEU   B CD2 1 2 
ATOM   6627  N  N   . GLU   B 1  212 ? -10.885 4.321   7.286   1    29.782  ? 212  GLU   B N   1 2 
ATOM   6628  C  CA  . GLU   B 1  212 ? -10.834 4.52    5.841   1    29.839  ? 212  GLU   B CA  1 2 
ATOM   6629  C  C   . GLU   B 1  212 ? -12.15  5.118   5.344   1    30.059  ? 212  GLU   B C   1 2 
ATOM   6630  O  O   . GLU   B 1  212 ? -12.156 5.97    4.472   1    30.29   ? 212  GLU   B O   1 2 
ATOM   6631  C  CB  . GLU   B 1  212 ? -10.485 3.18    5.193   1    32.818  ? 212  GLU   B CB  1 2 
ATOM   6632  C  CG  . GLU   B 1  212 ? -10.402 3.258   3.674   1    40.435  ? 212  GLU   B CG  1 2 
ATOM   6633  C  CD  . GLU   B 1  212 ? -10.01  1.909   3.072   1    55.909  ? 212  GLU   B CD  1 2 
ATOM   6634  O  OE1 . GLU   B 1  212 ? -8.8    1.565   3.103   1    61.04   ? 212  GLU   B OE1 1 2 
ATOM   6635  O  OE2 . GLU   B 1  212 ? -10.906 1.174   2.583   1    63.983  ? 212  GLU   B OE2 1 2 
ATOM   6636  N  N   . HIS   B 1  213 ? -13.285 4.643   5.876   1    31.82   ? 213  HIS   B N   1 2 
ATOM   6637  C  CA  . HIS   B 1  213 ? -14.584 5.161   5.468   1    34.874  ? 213  HIS   B CA  1 2 
ATOM   6638  C  C   . HIS   B 1  213 ? -14.737 6.602   5.93    1    32.145  ? 213  HIS   B C   1 2 
ATOM   6639  O  O   . HIS   B 1  213 ? -15.309 7.406   5.222   1    31.569  ? 213  HIS   B O   1 2 
ATOM   6640  C  CB  . HIS   B 1  213 ? -15.753 4.287   5.955   1    41.94   ? 213  HIS   B CB  1 2 
ATOM   6641  C  CG  . HIS   B 1  213 ? -15.841 2.942   5.296   1    52.295  ? 213  HIS   B CG  1 2 
ATOM   6642  N  ND1 . HIS   B 1  213 ? -16.535 1.884   5.857   1    59.846  ? 213  HIS   B ND1 1 2 
ATOM   6643  C  CD2 . HIS   B 1  213 ? -15.346 2.47    4.122   1    57.174  ? 213  HIS   B CD2 1 2 
ATOM   6644  C  CE1 . HIS   B 1  213 ? -16.45  0.819   5.053   1    57.86   ? 213  HIS   B CE1 1 2 
ATOM   6645  N  NE2 . HIS   B 1  213 ? -15.746 1.154   3.991   1    54.21   ? 213  HIS   B NE2 1 2 
ATOM   6646  N  N   . LEU   B 1  214 ? -14.233 6.911   7.128   1    29.798  ? 214  LEU   B N   1 2 
ATOM   6647  C  CA  . LEU   B 1  214 ? -14.204 8.287   7.591   1    30.109  ? 214  LEU   B CA  1 2 
ATOM   6648  C  C   . LEU   B 1  214 ? -13.401 9.152   6.626   1    26.562  ? 214  LEU   B C   1 2 
ATOM   6649  O  O   . LEU   B 1  214 ? -13.88  10.19   6.164   1    24.686  ? 214  LEU   B O   1 2 
ATOM   6650  C  CB  . LEU   B 1  214 ? -13.634 8.434   9.007   1    29.071  ? 214  LEU   B CB  1 2 
ATOM   6651  C  CG  . LEU   B 1  214 ? -14.582 8.005   10.126  1    33.683  ? 214  LEU   B CG  1 2 
ATOM   6652  C  CD1 . LEU   B 1  214 ? -13.788 8.172   11.41   1    32.766  ? 214  LEU   B CD1 1 2 
ATOM   6653  C  CD2 . LEU   B 1  214 ? -15.865 8.863   10.098  1    32.417  ? 214  LEU   B CD2 1 2 
ATOM   6654  N  N   . TYR   B 1  215 ? -12.132 8.781   6.401   1    24.022  ? 215  TYR   B N   1 2 
ATOM   6655  C  CA  . TYR   B 1  215 ? -11.323 9.564   5.476   1    23.562  ? 215  TYR   B CA  1 2 
ATOM   6656  C  C   . TYR   B 1  215 ? -12.039 9.816   4.131   1    25.599  ? 215  TYR   B C   1 2 
ATOM   6657  O  O   . TYR   B 1  215 ? -11.922 10.911  3.577   1    27.205  ? 215  TYR   B O   1 2 
ATOM   6658  C  CB  . TYR   B 1  215 ? -9.91   8.985   5.342   1    23.007  ? 215  TYR   B CB  1 2 
ATOM   6659  C  CG  . TYR   B 1  215 ? -9.055  10.076  4.722   1    25.559  ? 215  TYR   B CG  1 2 
ATOM   6660  C  CD1 . TYR   B 1  215 ? -8.672  11.173  5.502   1    27.709  ? 215  TYR   B CD1 1 2 
ATOM   6661  C  CD2 . TYR   B 1  215 ? -8.716  10.072  3.371   1    24.518  ? 215  TYR   B CD2 1 2 
ATOM   6662  C  CE1 . TYR   B 1  215 ? -7.945  12.223  4.966   1    32.899  ? 215  TYR   B CE1 1 2 
ATOM   6663  C  CE2 . TYR   B 1  215 ? -8.023  11.137  2.816   1    26.277  ? 215  TYR   B CE2 1 2 
ATOM   6664  C  CZ  . TYR   B 1  215 ? -7.618  12.205  3.62    1    28.489  ? 215  TYR   B CZ  1 2 
ATOM   6665  O  OH  . TYR   B 1  215 ? -6.968  13.305  3.13    1    29.791  ? 215  TYR   B OH  1 2 
ATOM   6666  N  N   . GLN   B 1  216 ? -12.693 8.8     3.536   1    25.873  ? 216  GLN   B N   1 2 
ATOM   6667  C  CA  . GLN   B 1  216 ? -13.307 9.01    2.228   1    29.658  ? 216  GLN   B CA  1 2 
ATOM   6668  C  C   . GLN   B 1  216 ? -14.359 10.125  2.248   1    29.906  ? 216  GLN   B C   1 2 
ATOM   6669  O  O   . GLN   B 1  216 ? -14.518 10.86   1.275   1    30.565  ? 216  GLN   B O   1 2 
ATOM   6670  C  CB  . GLN   B 1  216 ? -14.049 7.781   1.712   1    35.649  ? 216  GLN   B CB  1 2 
ATOM   6671  C  CG  . GLN   B 1  216 ? -13.143 6.586   1.451   1    45.587  ? 216  GLN   B CG  1 2 
ATOM   6672  C  CD  . GLN   B 1  216 ? -13.918 5.395   0.926   1    55.411  ? 216  GLN   B CD  1 2 
ATOM   6673  O  OE1 . GLN   B 1  216 ? -15.146 5.444   0.774   1    62.859  ? 216  GLN   B OE1 1 2 
ATOM   6674  N  NE2 . GLN   B 1  216 ? -13.211 4.307   0.653   1    53.479  ? 216  GLN   B NE2 1 2 
ATOM   6675  N  N   . GLN   B 1  217 ? -15.072 10.289  3.363   1    30.129  ? 217  GLN   B N   1 2 
ATOM   6676  C  CA  . GLN   B 1  217 ? -16.082 11.344  3.392   1    32.663  ? 217  GLN   B CA  1 2 
ATOM   6677  C  C   . GLN   B 1  217 ? -15.426 12.702  3.601   1    28.729  ? 217  GLN   B C   1 2 
ATOM   6678  O  O   . GLN   B 1  217 ? -15.999 13.729  3.245   1    28.237  ? 217  GLN   B O   1 2 
ATOM   6679  C  CB  . GLN   B 1  217 ? -17.097 11.269  4.524   1    35.479  ? 217  GLN   B CB  1 2 
ATOM   6680  C  CG  . GLN   B 1  217 ? -17.956 10.015  4.53    1    44.254  ? 217  GLN   B CG  1 2 
ATOM   6681  C  CD  . GLN   B 1  217 ? -18.769 9.967   5.807   1    51.234  ? 217  GLN   B CD  1 2 
ATOM   6682  O  OE1 . GLN   B 1  217 ? -19.813 10.627  5.936   1    53.217  ? 217  GLN   B OE1 1 2 
ATOM   6683  N  NE2 . GLN   B 1  217 ? -18.27  9.201   6.774   1    47.555  ? 217  GLN   B NE2 1 2 
ATOM   6684  N  N   . LEU   B 1  218 ? -14.227 12.704  4.209   1    26.711  ? 218  LEU   B N   1 2 
ATOM   6685  C  CA  . LEU   B 1  218 ? -13.559 13.954  4.514   1    24.106  ? 218  LEU   B CA  1 2 
ATOM   6686  C  C   . LEU   B 1  218 ? -12.68  14.406  3.336   1    23.178  ? 218  LEU   B C   1 2 
ATOM   6687  O  O   . LEU   B 1  218 ? -12.361 15.585  3.259   1    21.273  ? 218  LEU   B O   1 2 
ATOM   6688  C  CB  . LEU   B 1  218 ? -12.723 13.819  5.793   1    22.903  ? 218  LEU   B CB  1 2 
ATOM   6689  C  CG  . LEU   B 1  218 ? -13.428 13.352  7.068   1    24.663  ? 218  LEU   B CG  1 2 
ATOM   6690  C  CD1 . LEU   B 1  218 ? -12.402 12.937  8.13    1    24.772  ? 218  LEU   B CD1 1 2 
ATOM   6691  C  CD2 . LEU   B 1  218 ? -14.151 14.596  7.574   1    29.336  ? 218  LEU   B CD2 1 2 
ATOM   6692  N  N   . GLU   B 1  219 ? -12.197 13.48   2.468   1    24.521  ? 219  GLU   B N   1 2 
ATOM   6693  C  CA  . GLU   B 1  219 ? -11.221 13.836  1.423   1    23.447  ? 219  GLU   B CA  1 2 
ATOM   6694  C  C   . GLU   B 1  219 ? -11.631 15      0.5     1    25.559  ? 219  GLU   B C   1 2 
ATOM   6695  O  O   . GLU   B 1  219 ? -10.771 15.836  0.162   1    25.4    ? 219  GLU   B O   1 2 
ATOM   6696  C  CB  . GLU   B 1  219 ? -10.756 12.594  0.647   1    26.408  ? 219  GLU   B CB  1 2 
ATOM   6697  C  CG  . GLU   B 1  219 ? -9.654  12.892  -0.375  1    32.864  ? 219  GLU   B CG  1 2 
ATOM   6698  C  CD  . GLU   B 1  219 ? -9.164  11.697  -1.205  1    44.554  ? 219  GLU   B CD  1 2 
ATOM   6699  O  OE1 . GLU   B 1  219 ? -9.728  10.611  -0.985  1    44.891  ? 219  GLU   B OE1 1 2 
ATOM   6700  O  OE2 . GLU   B 1  219 ? -8.215  11.795  -2.048  1    56.624  ? 219  GLU   B OE2 1 2 
ATOM   6701  N  N   . PRO   B 1  220 ? -12.904 15.081  0.002   1    26.449  ? 220  PRO   B N   1 2 
ATOM   6702  C  CA  . PRO   B 1  220 ? -13.332 16.177  -0.872  1    26.636  ? 220  PRO   B CA  1 2 
ATOM   6703  C  C   . PRO   B 1  220 ? -13.081 17.528  -0.213  1    24.944  ? 220  PRO   B C   1 2 
ATOM   6704  O  O   . PRO   B 1  220 ? -12.656 18.441  -0.899  1    25.122  ? 220  PRO   B O   1 2 
ATOM   6705  C  CB  . PRO   B 1  220 ? -14.847 15.963  -1.224  1    28.397  ? 220  PRO   B CB  1 2 
ATOM   6706  C  CG  . PRO   B 1  220 ? -15.117 14.542  -0.748  1    30.582  ? 220  PRO   B CG  1 2 
ATOM   6707  C  CD  . PRO   B 1  220 ? -14     14.12   0.232   1    27.775  ? 220  PRO   B CD  1 2 
ATOM   6708  N  N   . LEU   B 1  221 ? -13.339 17.644  1.11    1    23.481  ? 221  LEU   B N   1 2 
ATOM   6709  C  CA  . LEU   B 1  221 ? -13.094 18.878  1.843   1    22.786  ? 221  LEU   B CA  1 2 
ATOM   6710  C  C   . LEU   B 1  221 ? -11.619 19.247  1.764   1    20.947  ? 221  LEU   B C   1 2 
ATOM   6711  O  O   . LEU   B 1  221 ? -11.286 20.404  1.515   1    21.523  ? 221  LEU   B O   1 2 
ATOM   6712  C  CB  . LEU   B 1  221 ? -13.481 18.785  3.322   1    23.331  ? 221  LEU   B CB  1 2 
ATOM   6713  C  CG  . LEU   B 1  221 ? -14.978 18.968  3.577   1    26.395  ? 221  LEU   B CG  1 2 
ATOM   6714  C  CD1 . LEU   B 1  221 ? -15.816 17.871  2.931   1    27.248  ? 221  LEU   B CD1 1 2 
ATOM   6715  C  CD2 . LEU   B 1  221 ? -15.182 19.089  5.113   1    24.591  ? 221  LEU   B CD2 1 2 
ATOM   6716  N  N   . TYR   B 1  222 ? -10.736 18.271  2.03    1    18.777  ? 222  TYR   B N   1 2 
ATOM   6717  C  CA  . TYR   B 1  222 ? -9.311  18.584  1.946   1    17.614  ? 222  TYR   B CA  1 2 
ATOM   6718  C  C   . TYR   B 1  222 ? -8.872  18.928  0.521   1    18.337  ? 222  TYR   B C   1 2 
ATOM   6719  O  O   . TYR   B 1  222 ? -8.059  19.843  0.29    1    17.934  ? 222  TYR   B O   1 2 
ATOM   6720  C  CB  . TYR   B 1  222 ? -8.497  17.362  2.378   1    16.808  ? 222  TYR   B CB  1 2 
ATOM   6721  C  CG  . TYR   B 1  222 ? -7.015  17.696  2.282   1    16.15   ? 222  TYR   B CG  1 2 
ATOM   6722  C  CD1 . TYR   B 1  222 ? -6.452  18.594  3.197   1    16.089  ? 222  TYR   B CD1 1 2 
ATOM   6723  C  CD2 . TYR   B 1  222 ? -6.185  17.121  1.316   1    16.572  ? 222  TYR   B CD2 1 2 
ATOM   6724  C  CE1 . TYR   B 1  222 ? -5.116  18.936  3.141   1    15.425  ? 222  TYR   B CE1 1 2 
ATOM   6725  C  CE2 . TYR   B 1  222 ? -4.825  17.438  1.274   1    16.226  ? 222  TYR   B CE2 1 2 
ATOM   6726  C  CZ  . TYR   B 1  222 ? -4.309  18.38   2.163   1    15.579  ? 222  TYR   B CZ  1 2 
ATOM   6727  O  OH  . TYR   B 1  222 ? -2.971  18.655  2.202   1    14.972  ? 222  TYR   B OH  1 2 
ATOM   6728  N  N   . LEU   B 1  223 ? -9.416  18.177  -0.459  1    19.049  ? 223  LEU   B N   1 2 
ATOM   6729  C  CA  . LEU   B 1  223 ? -8.975  18.427  -1.827  1    20.39   ? 223  LEU   B CA  1 2 
ATOM   6730  C  C   . LEU   B 1  223 ? -9.3    19.852  -2.244  1    21.975  ? 223  LEU   B C   1 2 
ATOM   6731  O  O   . LEU   B 1  223 ? -8.483  20.503  -2.897  1    20.802  ? 223  LEU   B O   1 2 
ATOM   6732  C  CB  . LEU   B 1  223 ? -9.572  17.403  -2.791  1    23.533  ? 223  LEU   B CB  1 2 
ATOM   6733  C  CG  . LEU   B 1  223 ? -9.039  15.983  -2.603  1    25.668  ? 223  LEU   B CG  1 2 
ATOM   6734  C  CD1 . LEU   B 1  223 ? -9.61   15.028  -3.64   1    27.465  ? 223  LEU   B CD1 1 2 
ATOM   6735  C  CD2 . LEU   B 1  223 ? -7.484  15.964  -2.497  1    24.399  ? 223  LEU   B CD2 1 2 
ATOM   6736  N  N   . ASN   B 1  224 ? -10.496 20.314  -1.831  1    22.406  ? 224  ASN   B N   1 2 
ATOM   6737  C  CA  . ASN   B 1  224 ? -10.917 21.657  -2.181  1    24.958  ? 224  ASN   B CA  1 2 
ATOM   6738  C  C   . ASN   B 1  224 ? -10.102 22.681  -1.421  1    23.024  ? 224  ASN   B C   1 2 
ATOM   6739  O  O   . ASN   B 1  224 ? -9.741  23.704  -1.982  1    24.603  ? 224  ASN   B O   1 2 
ATOM   6740  C  CB  . ASN   B 1  224 ? -12.408 21.838  -1.983  1    25.985  ? 224  ASN   B CB  1 2 
ATOM   6741  C  CG  . ASN   B 1  224 ? -13.115 21.407  -3.239  1    28.499  ? 224  ASN   B CG  1 2 
ATOM   6742  O  OD1 . ASN   B 1  224 ? -13.229 22.2    -4.186  1    29.985  ? 224  ASN   B OD1 1 2 
ATOM   6743  N  ND2 . ASN   B 1  224 ? -13.61  20.178  -3.242  1    27.726  ? 224  ASN   B ND2 1 2 
ATOM   6744  N  N   . LEU   B 1  225 ? -9.769  22.393  -0.166  1    21.727  ? 225  LEU   B N   1 2 
ATOM   6745  C  CA  . LEU   B 1  225 ? -8.999  23.386  0.553   1    20.089  ? 225  LEU   B CA  1 2 
ATOM   6746  C  C   . LEU   B 1  225 ? -7.604  23.492  -0.069  1    19.602  ? 225  LEU   B C   1 2 
ATOM   6747  O  O   . LEU   B 1  225 ? -7.041  24.573  -0.143  1    19.758  ? 225  LEU   B O   1 2 
ATOM   6748  C  CB  . LEU   B 1  225 ? -8.89   23      2.046   1    19.487  ? 225  LEU   B CB  1 2 
ATOM   6749  C  CG  . LEU   B 1  225 ? -7.935  23.869  2.854   1    18.623  ? 225  LEU   B CG  1 2 
ATOM   6750  C  CD1 . LEU   B 1  225 ? -8.684  25.222  3.068   1    19.538  ? 225  LEU   B CD1 1 2 
ATOM   6751  C  CD2 . LEU   B 1  225 ? -7.686  23.332  4.249   1    18.637  ? 225  LEU   B CD2 1 2 
ATOM   6752  N  N   . HIS   B 1  226 ? -6.973  22.335  -0.327  1    18.553  ? 226  HIS   B N   1 2 
ATOM   6753  C  CA  . HIS   B 1  226 ? -5.66   22.242  -0.962  1    18.934  ? 226  HIS   B CA  1 2 
ATOM   6754  C  C   . HIS   B 1  226 ? -5.581  23.039  -2.267  1    19.967  ? 226  HIS   B C   1 2 
ATOM   6755  O  O   . HIS   B 1  226 ? -4.615  23.733  -2.475  1    20.949  ? 226  HIS   B O   1 2 
ATOM   6756  C  CB  . HIS   B 1  226 ? -5.322  20.744  -1.166  1    17.329  ? 226  HIS   B CB  1 2 
ATOM   6757  C  CG  . HIS   B 1  226 ? -4.059  20.379  -1.843  1    16.93   ? 226  HIS   B CG  1 2 
ATOM   6758  N  ND1 . HIS   B 1  226 ? -3.88   20.518  -3.201  1    17.174  ? 226  HIS   B ND1 1 2 
ATOM   6759  C  CD2 . HIS   B 1  226 ? -2.886  19.888  -1.332  1    15.962  ? 226  HIS   B CD2 1 2 
ATOM   6760  C  CE1 . HIS   B 1  226 ? -2.636  20.128  -3.507  1    17.441  ? 226  HIS   B CE1 1 2 
ATOM   6761  N  NE2 . HIS   B 1  226 ? -2.041  19.728  -2.398  1    15.907  ? 226  HIS   B NE2 1 2 
ATOM   6762  N  N   . ALA   B 1  227 ? -6.525  22.843  -3.196  1    21.956  ? 227  ALA   B N   1 2 
ATOM   6763  C  CA  . ALA   B 1  227 ? -6.503  23.534  -4.482  1    22.811  ? 227  ALA   B CA  1 2 
ATOM   6764  C  C   . ALA   B 1  227 ? -6.613  25.054  -4.272  1    24.466  ? 227  ALA   B C   1 2 
ATOM   6765  O  O   . ALA   B 1  227 ? -5.876  25.823  -4.882  1    23.902  ? 227  ALA   B O   1 2 
ATOM   6766  C  CB  . ALA   B 1  227 ? -7.628  22.991  -5.34   1    23.215  ? 227  ALA   B CB  1 2 
ATOM   6767  N  N   . PHE   B 1  228 ? -7.498  25.467  -3.357  1    25.446  ? 228  PHE   B N   1 2 
ATOM   6768  C  CA  . PHE   B 1  228 ? -7.658  26.899  -3.04   1    26.946  ? 228  PHE   B CA  1 2 
ATOM   6769  C  C   . PHE   B 1  228 ? -6.373  27.491  -2.476  1    26.25   ? 228  PHE   B C   1 2 
ATOM   6770  O  O   . PHE   B 1  228 ? -5.933  28.549  -2.894  1    26.37   ? 228  PHE   B O   1 2 
ATOM   6771  C  CB  . PHE   B 1  228 ? -8.809  27.029  -2.044  1    29.152  ? 228  PHE   B CB  1 2 
ATOM   6772  C  CG  . PHE   B 1  228 ? -9.103  28.451  -1.565  1    32.645  ? 228  PHE   B CG  1 2 
ATOM   6773  C  CD1 . PHE   B 1  228 ? -9.843  29.327  -2.359  1    35.626  ? 228  PHE   B CD1 1 2 
ATOM   6774  C  CD2 . PHE   B 1  228 ? -8.673  28.877  -0.309  1    33.953  ? 228  PHE   B CD2 1 2 
ATOM   6775  C  CE1 . PHE   B 1  228 ? -10.126 30.614  -1.914  1    36.935  ? 228  PHE   B CE1 1 2 
ATOM   6776  C  CE2 . PHE   B 1  228 ? -8.967  30.171  0.127   1    36.658  ? 228  PHE   B CE2 1 2 
ATOM   6777  C  CZ  . PHE   B 1  228 ? -9.699  31.023  -0.672  1    35.809  ? 228  PHE   B CZ  1 2 
ATOM   6778  N  N   . VAL   B 1  229 ? -5.707  26.793  -1.54   1    24.487  ? 229  VAL   B N   1 2 
ATOM   6779  C  CA  . VAL   B 1  229 ? -4.453  27.271  -0.98   1    22.442  ? 229  VAL   B CA  1 2 
ATOM   6780  C  C   . VAL   B 1  229 ? -3.342  27.185  -2.014  1    22.688  ? 229  VAL   B C   1 2 
ATOM   6781  O  O   . VAL   B 1  229 ? -2.482  28.065  -2.09   1    23.216  ? 229  VAL   B O   1 2 
ATOM   6782  C  CB  . VAL   B 1  229 ? -4.101  26.468  0.3     1    21.664  ? 229  VAL   B CB  1 2 
ATOM   6783  C  CG1 . VAL   B 1  229 ? -2.684  26.735  0.785   1    20.947  ? 229  VAL   B CG1 1 2 
ATOM   6784  C  CG2 . VAL   B 1  229 ? -5.111  26.732  1.416   1    21.512  ? 229  VAL   B CG2 1 2 
ATOM   6785  N  N   . ARG   B 1  230 ? -3.291  26.091  -2.793  1    21.514  ? 230  ARG   B N   1 2 
ATOM   6786  C  CA  . ARG   B 1  230 ? -2.272  26.041  -3.845  1    20.885  ? 230  ARG   B CA  1 2 
ATOM   6787  C  C   . ARG   B 1  230 ? -2.346  27.279  -4.758  1    21.99   ? 230  ARG   B C   1 2 
ATOM   6788  O  O   . ARG   B 1  230 ? -1.335  27.824  -5.225  1    21.292  ? 230  ARG   B O   1 2 
ATOM   6789  C  CB  . ARG   B 1  230 ? -2.454  24.787  -4.715  1    20.197  ? 230  ARG   B CB  1 2 
ATOM   6790  C  CG  . ARG   B 1  230 ? -1.249  24.494  -5.609  1    20.546  ? 230  ARG   B CG  1 2 
ATOM   6791  C  CD  . ARG   B 1  230 ? -1.377  23.158  -6.427  1    19.672  ? 230  ARG   B CD  1 2 
ATOM   6792  N  NE  . ARG   B 1  230 ? -2.759  22.964  -6.925  1    19.992  ? 230  ARG   B NE  1 2 
ATOM   6793  C  CZ  . ARG   B 1  230 ? -3.263  21.746  -7.178  1    19.957  ? 230  ARG   B CZ  1 2 
ATOM   6794  N  NH1 . ARG   B 1  230 ? -2.443  20.68   -7.114  1    18.946  ? 230  ARG   B NH1 1 2 
ATOM   6795  N  NH2 . ARG   B 1  230 ? -4.557  21.6    -7.461  1    20.367  ? 230  ARG   B NH2 1 2 
ATOM   6796  N  N   . ARG   B 1  231 ? -3.584  27.664  -5.051  1    23.466  ? 231  ARG   B N   1 2 
ATOM   6797  C  CA  . ARG   B 1  231 ? -3.816  28.814  -5.923  1    26.638  ? 231  ARG   B CA  1 2 
ATOM   6798  C  C   . ARG   B 1  231 ? -3.21   30.061  -5.286  1    28.187  ? 231  ARG   B C   1 2 
ATOM   6799  O  O   . ARG   B 1  231 ? -2.583  30.87   -5.946  1    29.168  ? 231  ARG   B O   1 2 
ATOM   6800  C  CB  . ARG   B 1  231 ? -5.306  29.038  -6.196  1    28.076  ? 231  ARG   B CB  1 2 
ATOM   6801  C  CG  . ARG   B 1  231 ? -5.436  30.348  -6.965  1    31.987  ? 231  ARG   B CG  1 2 
ATOM   6802  C  CD  . ARG   B 1  231 ? -4.751  30.451  -8.321  1    35.046  ? 231  ARG   B CD  1 2 
ATOM   6803  N  NE  . ARG   B 1  231 ? -5.308  29.504  -9.294  1    36.717  ? 231  ARG   B NE  1 2 
ATOM   6804  C  CZ  . ARG   B 1  231 ? -5.025  29.451  -10.607 1    37.725  ? 231  ARG   B CZ  1 2 
ATOM   6805  N  NH1 . ARG   B 1  231 ? -4.238  30.371  -11.166 1    38.441  ? 231  ARG   B NH1 1 2 
ATOM   6806  N  NH2 . ARG   B 1  231 ? -5.497  28.441  -11.337 1    36.451  ? 231  ARG   B NH2 1 2 
ATOM   6807  N  N   . ALA   B 1  232 ? -3.435  30.23   -3.982  1    28.825  ? 232  ALA   B N   1 2 
ATOM   6808  C  CA  . ALA   B 1  232 ? -2.904  31.415  -3.305  1    30.37   ? 232  ALA   B CA  1 2 
ATOM   6809  C  C   . ALA   B 1  232 ? -1.378  31.396  -3.232  1    29.118  ? 232  ALA   B C   1 2 
ATOM   6810  O  O   . ALA   B 1  232 ? -0.723  32.424  -3.419  1    31.801  ? 232  ALA   B O   1 2 
ATOM   6811  C  CB  . ALA   B 1  232 ? -3.577  31.572  -1.936  1    30.916  ? 232  ALA   B CB  1 2 
ATOM   6812  N  N   . LEU   B 1  233 ? -0.756  30.213  -3.086  1    26.99   ? 233  LEU   B N   1 2 
ATOM   6813  C  CA  . LEU   B 1  233 ? 0.701   30.141  -3.032  1    26.105  ? 233  LEU   B CA  1 2 
ATOM   6814  C  C   . LEU   B 1  233 ? 1.292   30.402  -4.413  1    27.821  ? 233  LEU   B C   1 2 
ATOM   6815  O  O   . LEU   B 1  233 ? 2.427   30.852  -4.545  1    28.227  ? 233  LEU   B O   1 2 
ATOM   6816  C  CB  . LEU   B 1  233 ? 1.101   28.729  -2.583  1    25.917  ? 233  LEU   B CB  1 2 
ATOM   6817  C  CG  . LEU   B 1  233 ? 0.777   28.381  -1.123  1    25.245  ? 233  LEU   B CG  1 2 
ATOM   6818  C  CD1 . LEU   B 1  233 ? 0.998   26.885  -0.811  1    23.593  ? 233  LEU   B CD1 1 2 
ATOM   6819  C  CD2 . LEU   B 1  233 ? 1.752   29.23   -0.275  1    28.711  ? 233  LEU   B CD2 1 2 
ATOM   6820  N  N   . HIS   B 1  234 ? 0.572   29.987  -5.464  1    29.174  ? 234  HIS   B N   1 2 
ATOM   6821  C  CA  . HIS   B 1  234 ? 1.02    30.309  -6.815  1    30.323  ? 234  HIS   B CA  1 2 
ATOM   6822  C  C   . HIS   B 1  234 ? 1.019   31.832  -7.024  1    32.392  ? 234  HIS   B C   1 2 
ATOM   6823  O  O   . HIS   B 1  234 ? 1.93    32.368  -7.647  1    30.816  ? 234  HIS   B O   1 2 
ATOM   6824  C  CB  . HIS   B 1  234 ? 0.142   29.576  -7.839  1    31.298  ? 234  HIS   B CB  1 2 
ATOM   6825  C  CG  . HIS   B 1  234 ? 0.53    29.777  -9.27   1    36.251  ? 234  HIS   B CG  1 2 
ATOM   6826  N  ND1 . HIS   B 1  234 ? -0.152  30.664  -10.077 1    39.208  ? 234  HIS   B ND1 1 2 
ATOM   6827  C  CD2 . HIS   B 1  234 ? 1.504   29.242  -10.025 1    36.58   ? 234  HIS   B CD2 1 2 
ATOM   6828  C  CE1 . HIS   B 1  234 ? 0.38    30.646  -11.292 1    40.691  ? 234  HIS   B CE1 1 2 
ATOM   6829  N  NE2 . HIS   B 1  234 ? 1.389   29.793  -11.283 1    39.581  ? 234  HIS   B NE2 1 2 
ATOM   6830  N  N   . ARG   B 1  235 ? -0.055  32.511  -6.602  1    33.705  ? 235  ARG   B N   1 2 
ATOM   6831  C  CA  . ARG   B 1  235 ? -0.066  33.973  -6.701  1    36.925  ? 235  ARG   B CA  1 2 
ATOM   6832  C  C   . ARG   B 1  235 ? 1.191   34.559  -6.049  1    38.471  ? 235  ARG   B C   1 2 
ATOM   6833  O  O   . ARG   B 1  235 ? 1.831   35.428  -6.628  1    39.24   ? 235  ARG   B O   1 2 
ATOM   6834  C  CB  . ARG   B 1  235 ? -1.326  34.592  -6.091  1    39.166  ? 235  ARG   B CB  1 2 
ATOM   6835  C  CG  . ARG   B 1  235 ? -2.552  34.497  -6.988  1    44.517  ? 235  ARG   B CG  1 2 
ATOM   6836  C  CD  . ARG   B 1  235 ? -3.778  35.013  -6.243  1    50.447  ? 235  ARG   B CD  1 2 
ATOM   6837  N  NE  . ARG   B 1  235 ? -5.052  34.312  -6.452  1    56.802  ? 235  ARG   B NE  1 2 
ATOM   6838  C  CZ  . ARG   B 1  235 ? -5.782  34.144  -7.56   1    61.705  ? 235  ARG   B CZ  1 2 
ATOM   6839  N  NH1 . ARG   B 1  235 ? -6.961  33.55   -7.462  1    60.697  ? 235  ARG   B NH1 1 2 
ATOM   6840  N  NH2 . ARG   B 1  235 ? -5.378  34.588  -8.746  1    64.658  ? 235  ARG   B NH2 1 2 
ATOM   6841  N  N   . ARG   B 1  236 ? 1.562   34.055  -4.851  1    39.251  ? 236  ARG   B N   1 2 
ATOM   6842  C  CA  . ARG   B 1  236 ? 2.685   34.575  -4.078  1    40.314  ? 236  ARG   B CA  1 2 
ATOM   6843  C  C   . ARG   B 1  236 ? 4.001   34.122  -4.7    1    39.959  ? 236  ARG   B C   1 2 
ATOM   6844  O  O   . ARG   B 1  236 ? 4.915   34.912  -4.772  1    44.322  ? 236  ARG   B O   1 2 
ATOM   6845  C  CB  . ARG   B 1  236 ? 2.666   34.285  -2.566  1    38.78   ? 236  ARG   B CB  1 2 
ATOM   6846  C  CG  . ARG   B 1  236 ? 3.969   34.354  -1.761  1    40.115  ? 236  ARG   B CG  1 2 
ATOM   6847  C  CD  . ARG   B 1  236 ? 4.564   35.741  -1.433  1    47.598  ? 236  ARG   B CD  1 2 
ATOM   6848  N  NE  . ARG   B 1  236 ? 3.423   36.54   -0.973  1    50.684  ? 236  ARG   B NE  1 2 
ATOM   6849  C  CZ  . ARG   B 1  236 ? 3.191   37.084  0.236   1    58.508  ? 236  ARG   B CZ  1 2 
ATOM   6850  N  NH1 . ARG   B 1  236 ? 4.197   37.37   1.059   1    55.634  ? 236  ARG   B NH1 1 2 
ATOM   6851  N  NH2 . ARG   B 1  236 ? 1.944   37.41   0.59    1    54.158  ? 236  ARG   B NH2 1 2 
ATOM   6852  N  N   . TYR   B 1  237 ? 4.151   32.853  -5.097  1    38.892  ? 237  TYR   B N   1 2 
ATOM   6853  C  CA  . TYR   B 1  237 ? 5.515   32.391  -5.356  1    36.413  ? 237  TYR   B CA  1 2 
ATOM   6854  C  C   . TYR   B 1  237 ? 5.776   32.156  -6.845  1    39.108  ? 237  TYR   B C   1 2 
ATOM   6855  O  O   . TYR   B 1  237 ? 6.943   31.957  -7.199  1    39.462  ? 237  TYR   B O   1 2 
ATOM   6856  C  CB  . TYR   B 1  237 ? 5.965   31.097  -4.659  1    35.554  ? 237  TYR   B CB  1 2 
ATOM   6857  C  CG  . TYR   B 1  237 ? 6.003   31.229  -3.15   1    33.706  ? 237  TYR   B CG  1 2 
ATOM   6858  C  CD1 . TYR   B 1  237 ? 7.093   31.832  -2.524  1    33.9    ? 237  TYR   B CD1 1 2 
ATOM   6859  C  CD2 . TYR   B 1  237 ? 4.936   30.795  -2.37   1    30.982  ? 237  TYR   B CD2 1 2 
ATOM   6860  C  CE1 . TYR   B 1  237 ? 7.125   31.974  -1.151  1    32.917  ? 237  TYR   B CE1 1 2 
ATOM   6861  C  CE2 . TYR   B 1  237 ? 4.977   30.927  -0.992  1    30.418  ? 237  TYR   B CE2 1 2 
ATOM   6862  C  CZ  . TYR   B 1  237 ? 6.063   31.532  -0.382  1    31.729  ? 237  TYR   B CZ  1 2 
ATOM   6863  O  OH  . TYR   B 1  237 ? 6.118   31.702  0.993   1    31.816  ? 237  TYR   B OH  1 2 
ATOM   6864  N  N   . GLY   B 1  238 ? 4.72    32.11   -7.688  1    38.229  ? 238  GLY   B N   1 2 
ATOM   6865  C  CA  . GLY   B 1  238 ? 4.932   32.002  -9.136  1    39.283  ? 238  GLY   B CA  1 2 
ATOM   6866  C  C   . GLY   B 1  238 ? 4.949   30.568  -9.674  1    40.355  ? 238  GLY   B C   1 2 
ATOM   6867  O  O   . GLY   B 1  238 ? 5.046   29.62   -8.913  1    36.922  ? 238  GLY   B O   1 2 
ATOM   6868  N  N   . ASP   B 1  239 ? 4.881   30.406  -11.005 1    43.687  ? 239  ASP   B N   1 2 
ATOM   6869  C  CA  . ASP   B 1  239 ? 4.903   29.109  -11.68  1    42.71   ? 239  ASP   B CA  1 2 
ATOM   6870  C  C   . ASP   B 1  239 ? 6.225   28.375  -11.486 1    39.407  ? 239  ASP   B C   1 2 
ATOM   6871  O  O   . ASP   B 1  239 ? 6.339   27.189  -11.777 1    39.746  ? 239  ASP   B O   1 2 
ATOM   6872  C  CB  . ASP   B 1  239 ? 4.822   29.274  -13.194 1    49.263  ? 239  ASP   B CB  1 2 
ATOM   6873  C  CG  . ASP   B 1  239 ? 3.54    28.829  -13.893 1    56.107  ? 239  ASP   B CG  1 2 
ATOM   6874  O  OD1 . ASP   B 1  239 ? 2.608   28.37   -13.205 1    60.805  ? 239  ASP   B OD1 1 2 
ATOM   6875  O  OD2 . ASP   B 1  239 ? 3.484   28.915  -15.142 1    60.475  ? 239  ASP   B OD2 1 2 
ATOM   6876  N  N   . ARG   B 1  240 ? 7.288   29.072  -11.108 1    39.14   ? 240  ARG   B N   1 2 
ATOM   6877  C  CA  . ARG   B 1  240 ? 8.534   28.336  -10.985 1    39.702  ? 240  ARG   B CA  1 2 
ATOM   6878  C  C   . ARG   B 1  240 ? 8.447   27.35   -9.812  1    37.052  ? 240  ARG   B C   1 2 
ATOM   6879  O  O   . ARG   B 1  240 ? 8.998   26.246  -9.849  1    35.299  ? 240  ARG   B O   1 2 
ATOM   6880  C  CB  . ARG   B 1  240 ? 9.656   29.372  -10.857 1    47.27   ? 240  ARG   B CB  1 2 
ATOM   6881  C  CG  . ARG   B 1  240 ? 11.058  28.813  -10.655 1    53.148  ? 240  ARG   B CG  1 2 
ATOM   6882  C  CD  . ARG   B 1  240 ? 12.147  29.874  -10.4   1    62.519  ? 240  ARG   B CD  1 2 
ATOM   6883  N  NE  . ARG   B 1  240 ? 13.422  29.366  -9.852  1    68.041  ? 240  ARG   B NE  1 2 
ATOM   6884  C  CZ  . ARG   B 1  240 ? 14.314  28.475  -10.34  1    63.798  ? 240  ARG   B CZ  1 2 
ATOM   6885  N  NH1 . ARG   B 1  240 ? 14.151  27.887  -11.518 1    59.055  ? 240  ARG   B NH1 1 2 
ATOM   6886  N  NH2 . ARG   B 1  240 ? 15.392  28.193  -9.626  1    59.529  ? 240  ARG   B NH2 1 2 
ATOM   6887  N  N   . TYR   B 1  241 ? 7.744   27.756  -8.754  1    33.08   ? 241  TYR   B N   1 2 
ATOM   6888  C  CA  . TYR   B 1  241 ? 7.824   27      -7.509  1    31.578  ? 241  TYR   B CA  1 2 
ATOM   6889  C  C   . TYR   B 1  241 ? 6.51    26.319  -7.204  1    28.618  ? 241  TYR   B C   1 2 
ATOM   6890  O  O   . TYR   B 1  241 ? 6.446   25.5    -6.301  1    30.357  ? 241  TYR   B O   1 2 
ATOM   6891  C  CB  . TYR   B 1  241 ? 8.217   27.942  -6.366  1    32.361  ? 241  TYR   B CB  1 2 
ATOM   6892  C  CG  . TYR   B 1  241 ? 9.678   28.37   -6.424  1    34.263  ? 241  TYR   B CG  1 2 
ATOM   6893  C  CD1 . TYR   B 1  241 ? 10.7    27.432  -6.43   1    34.853  ? 241  TYR   B CD1 1 2 
ATOM   6894  C  CD2 . TYR   B 1  241 ? 10.024  29.713  -6.505  1    38.942  ? 241  TYR   B CD2 1 2 
ATOM   6895  C  CE1 . TYR   B 1  241 ? 12.025  27.825  -6.487  1    39.587  ? 241  TYR   B CE1 1 2 
ATOM   6896  C  CE2 . TYR   B 1  241 ? 11.347  30.13   -6.55   1    42.955  ? 241  TYR   B CE2 1 2 
ATOM   6897  C  CZ  . TYR   B 1  241 ? 12.349  29.176  -6.518  1    45.406  ? 241  TYR   B CZ  1 2 
ATOM   6898  O  OH  . TYR   B 1  241 ? 13.648  29.583  -6.571  1    50.04   ? 241  TYR   B OH  1 2 
ATOM   6899  N  N   . ILE   B 1  242 ? 5.444   26.743  -7.865  1    28.476  ? 242  ILE   B N   1 2 
ATOM   6900  C  CA  . ILE   B 1  242 ? 4.157   26.152  -7.577  1    28.191  ? 242  ILE   B CA  1 2 
ATOM   6901  C  C   . ILE   B 1  242 ? 3.614   25.615  -8.892  1    28.601  ? 242  ILE   B C   1 2 
ATOM   6902  O  O   . ILE   B 1  242 ? 3.568   26.345  -9.891  1    30.641  ? 242  ILE   B O   1 2 
ATOM   6903  C  CB  . ILE   B 1  242 ? 3.202   27.157  -6.908  1    30.071  ? 242  ILE   B CB  1 2 
ATOM   6904  C  CG1 . ILE   B 1  242 ? 3.765   27.785  -5.575  1    28.695  ? 242  ILE   B CG1 1 2 
ATOM   6905  C  CG2 . ILE   B 1  242 ? 1.818   26.543  -6.727  1    28.769  ? 242  ILE   B CG2 1 2 
ATOM   6906  C  CD1 . ILE   B 1  242 ? 3.87    26.82   -4.394  1    28.164  ? 242  ILE   B CD1 1 2 
ATOM   6907  N  N   . ASN   B 1  243 ? 3.276   24.329  -8.878  1    25.444  ? 243  ASN   B N   1 2 
ATOM   6908  C  CA  . ASN   B 1  243 ? 2.653   23.644  -9.999  1    25.392  ? 243  ASN   B CA  1 2 
ATOM   6909  C  C   . ASN   B 1  243 ? 1.153   23.553  -9.705  1    24.349  ? 243  ASN   B C   1 2 
ATOM   6910  O  O   . ASN   B 1  243 ? 0.724   22.852  -8.777  1    23.942  ? 243  ASN   B O   1 2 
ATOM   6911  C  CB  . ASN   B 1  243 ? 3.312   22.276  -10.216 1    25.597  ? 243  ASN   B CB  1 2 
ATOM   6912  C  CG  . ASN   B 1  243 ? 2.797   21.552  -11.444 1    26.22   ? 243  ASN   B CG  1 2 
ATOM   6913  O  OD1 . ASN   B 1  243 ? 1.764   21.911  -11.983 1    26.415  ? 243  ASN   B OD1 1 2 
ATOM   6914  N  ND2 . ASN   B 1  243 ? 3.47    20.499  -11.882 1    27.717  ? 243  ASN   B ND2 1 2 
ATOM   6915  N  N   . LEU   B 1  244 ? 0.347   24.26   -10.5   1    24.94   ? 244  LEU   B N   1 2 
ATOM   6916  C  CA  . LEU   B 1  244 ? -1.088  24.246  -10.321 1    25.291  ? 244  LEU   B CA  1 2 
ATOM   6917  C  C   . LEU   B 1  244 ? -1.719  22.875  -10.499 1    24.906  ? 244  LEU   B C   1 2 
ATOM   6918  O  O   . LEU   B 1  244 ? -2.855  22.698  -10.072 1    24.871  ? 244  LEU   B O   1 2 
ATOM   6919  C  CB  . LEU   B 1  244 ? -1.732  25.272  -11.231 1    27.694  ? 244  LEU   B CB  1 2 
ATOM   6920  C  CG  . LEU   B 1  244 ? -1.491  26.709  -10.746 1    28.755  ? 244  LEU   B CG  1 2 
ATOM   6921  C  CD1 . LEU   B 1  244 ? -1.832  27.739  -11.862 1    30.028  ? 244  LEU   B CD1 1 2 
ATOM   6922  C  CD2 . LEU   B 1  244 ? -2.144  27.013  -9.415  1    27.702  ? 244  LEU   B CD2 1 2 
ATOM   6923  N  N   . ARG   B 1  245 ? -0.967  21.904  -11.043 1    25.024  ? 245  ARG   B N   1 2 
ATOM   6924  C  CA  . ARG   B 1  245 ? -1.514  20.555  -11.129 1    25.349  ? 245  ARG   B CA  1 2 
ATOM   6925  C  C   . ARG   B 1  245 ? -0.67   19.544  -10.356 1    23.79   ? 245  ARG   B C   1 2 
ATOM   6926  O  O   . ARG   B 1  245 ? -0.792  18.348  -10.622 1    24.792  ? 245  ARG   B O   1 2 
ATOM   6927  C  CB  . ARG   B 1  245 ? -1.605  20.195  -12.627 1    27.768  ? 245  ARG   B CB  1 2 
ATOM   6928  C  CG  . ARG   B 1  245 ? -2.748  20.975  -13.292 1    33.965  ? 245  ARG   B CG  1 2 
ATOM   6929  C  CD  . ARG   B 1  245 ? -2.875  20.771  -14.804 1    41.77   ? 245  ARG   B CD  1 2 
ATOM   6930  N  NE  . ARG   B 1  245 ? -1.583  21.029  -15.449 1    46.424  ? 245  ARG   B NE  1 2 
ATOM   6931  C  CZ  . ARG   B 1  245 ? -1.199  20.72   -16.699 1    55.811  ? 245  ARG   B CZ  1 2 
ATOM   6932  N  NH1 . ARG   B 1  245 ? -2.05   20.193  -17.573 1    51.385  ? 245  ARG   B NH1 1 2 
ATOM   6933  N  NH2 . ARG   B 1  245 ? 0.068   20.906  -17.057 1    55.917  ? 245  ARG   B NH2 1 2 
ATOM   6934  N  N   . GLY   B 1  246 ? 0.244   20.011  -9.517  1    21.26   ? 246  GLY   B N   1 2 
ATOM   6935  C  CA  . GLY   B 1  246 ? 1.18    19.129  -8.85   1    20.762  ? 246  GLY   B CA  1 2 
ATOM   6936  C  C   . GLY   B 1  246 ? 1.138   19.275  -7.329  1    19.487  ? 246  GLY   B C   1 2 
ATOM   6937  O  O   . GLY   B 1  246 ? 0.398   20.089  -6.783  1    18.835  ? 246  GLY   B O   1 2 
ATOM   6938  N  N   . PRO   B 1  247 ? 1.923   18.487  -6.555  1    19.652  ? 247  PRO   B N   1 2 
ATOM   6939  C  CA  . PRO   B 1  247 ? 1.895   18.638  -5.085  1    18.577  ? 247  PRO   B CA  1 2 
ATOM   6940  C  C   . PRO   B 1  247 ? 2.484   19.982  -4.657  1    18.108  ? 247  PRO   B C   1 2 
ATOM   6941  O  O   . PRO   B 1  247 ? 3.332   20.507  -5.355  1    19.362  ? 247  PRO   B O   1 2 
ATOM   6942  C  CB  . PRO   B 1  247 ? 2.797   17.519  -4.598  1    18.238  ? 247  PRO   B CB  1 2 
ATOM   6943  C  CG  . PRO   B 1  247 ? 2.795   16.552  -5.704  1    19.731  ? 247  PRO   B CG  1 2 
ATOM   6944  C  CD  . PRO   B 1  247 ? 2.826   17.422  -6.991  1    19.382  ? 247  PRO   B CD  1 2 
ATOM   6945  N  N   . ILE   B 1  248 ? 2.098   20.475  -3.485  1    17.801  ? 248  ILE   B N   1 2 
ATOM   6946  C  CA  . ILE   B 1  248 ? 2.598   21.746  -2.954  1    18.039  ? 248  ILE   B CA  1 2 
ATOM   6947  C  C   . ILE   B 1  248 ? 3.946   21.432  -2.284  1    18.453  ? 248  ILE   B C   1 2 
ATOM   6948  O  O   . ILE   B 1  248 ? 4.023   20.456  -1.541  1    18.452  ? 248  ILE   B O   1 2 
ATOM   6949  C  CB  . ILE   B 1  248 ? 1.607   22.278  -1.922  1    16.57   ? 248  ILE   B CB  1 2 
ATOM   6950  C  CG1 . ILE   B 1  248 ? 0.218   22.594  -2.547  1    17.061  ? 248  ILE   B CG1 1 2 
ATOM   6951  C  CG2 . ILE   B 1  248 ? 2.156   23.506  -1.17   1    17.263  ? 248  ILE   B CG2 1 2 
ATOM   6952  C  CD1 . ILE   B 1  248 ? -0.83   22.874  -1.472  1    16.174  ? 248  ILE   B CD1 1 2 
ATOM   6953  N  N   . PRO   B 1  249 ? 5.036   22.206  -2.52   1    19.563  ? 249  PRO   B N   1 2 
ATOM   6954  C  CA  . PRO   B 1  249 ? 6.302   22.042  -1.782  1    19.206  ? 249  PRO   B CA  1 2 
ATOM   6955  C  C   . PRO   B 1  249 ? 6.089   22.111  -0.257  1    17.747  ? 249  PRO   B C   1 2 
ATOM   6956  O  O   . PRO   B 1  249 ? 5.357   22.98   0.21    1    18.167  ? 249  PRO   B O   1 2 
ATOM   6957  C  CB  . PRO   B 1  249 ? 7.168   23.178  -2.326  1    19.525  ? 249  PRO   B CB  1 2 
ATOM   6958  C  CG  . PRO   B 1  249 ? 6.675   23.324  -3.754  1    20.286  ? 249  PRO   B CG  1 2 
ATOM   6959  C  CD  . PRO   B 1  249 ? 5.147   23.277  -3.531  1    20.175  ? 249  PRO   B CD  1 2 
ATOM   6960  N  N   . ALA   B 1  250 ? 6.68    21.149  0.488   1    16.539  ? 250  ALA   B N   1 2 
ATOM   6961  C  CA  . ALA   B 1  250 ? 6.264   20.778  1.844   1    16.349  ? 250  ALA   B CA  1 2 
ATOM   6962  C  C   . ALA   B 1  250 ? 6.619   21.865  2.878   1    16.824  ? 250  ALA   B C   1 2 
ATOM   6963  O  O   . ALA   B 1  250 ? 6.198   21.755  4.049   1    18.355  ? 250  ALA   B O   1 2 
ATOM   6964  C  CB  . ALA   B 1  250 ? 6.907   19.444  2.23    1    15.287  ? 250  ALA   B CB  1 2 
ATOM   6965  N  N   . HIS   B 1  251 ? 7.328   22.918  2.459   1    17.014  ? 251  HIS   B N   1 2 
ATOM   6966  C  CA  . HIS   B 1  251 ? 7.859   23.929  3.382   1    17.682  ? 251  HIS   B CA  1 2 
ATOM   6967  C  C   . HIS   B 1  251 ? 7.044   25.23   3.353   1    17.506  ? 251  HIS   B C   1 2 
ATOM   6968  O  O   . HIS   B 1  251 ? 7.366   26.145  4.085   1    18.318  ? 251  HIS   B O   1 2 
ATOM   6969  C  CB  . HIS   B 1  251 ? 9.347   24.218  3.127   1    18.742  ? 251  HIS   B CB  1 2 
ATOM   6970  C  CG  . HIS   B 1  251 ? 9.665   24.832  1.793   1    20.193  ? 251  HIS   B CG  1 2 
ATOM   6971  N  ND1 . HIS   B 1  251 ? 9.169   24.315  0.608   1    20.649  ? 251  HIS   B ND1 1 2 
ATOM   6972  C  CD2 . HIS   B 1  251 ? 10.379  25.891  1.446   1    22.1    ? 251  HIS   B CD2 1 2 
ATOM   6973  C  CE1 . HIS   B 1  251 ? 9.612   25.022  -0.415  1    22.506  ? 251  HIS   B CE1 1 2 
ATOM   6974  N  NE2 . HIS   B 1  251 ? 10.397  25.963  0.064   1    24.398  ? 251  HIS   B NE2 1 2 
ATOM   6975  N  N   . LEU   B 1  252 ? 5.973   25.307  2.568   1    17.483  ? 252  LEU   B N   1 2 
ATOM   6976  C  CA  . LEU   B 1  252 ? 5.327   26.594  2.268   1    17.659  ? 252  LEU   B CA  1 2 
ATOM   6977  C  C   . LEU   B 1  252 ? 3.994   26.778  2.994   1    17.914  ? 252  LEU   B C   1 2 
ATOM   6978  O  O   . LEU   B 1  252 ? 3.304   27.771  2.764   1    18.916  ? 252  LEU   B O   1 2 
ATOM   6979  C  CB  . LEU   B 1  252 ? 5.108   26.618  0.75    1    18.611  ? 252  LEU   B CB  1 2 
ATOM   6980  C  CG  . LEU   B 1  252 ? 6.372   26.688  -0.132  1    19.397  ? 252  LEU   B CG  1 2 
ATOM   6981  C  CD1 . LEU   B 1  252 ? 5.976   26.863  -1.625  1    20.17   ? 252  LEU   B CD1 1 2 
ATOM   6982  C  CD2 . LEU   B 1  252 ? 7.252   27.85   0.293   1    20.159  ? 252  LEU   B CD2 1 2 
ATOM   6983  N  N   . LEU   B 1  253 ? 3.644   25.883  3.927   1    18.99   ? 253  LEU   B N   1 2 
ATOM   6984  C  CA  . LEU   B 1  253 ? 2.285   25.851  4.455   1    18.552  ? 253  LEU   B CA  1 2 
ATOM   6985  C  C   . LEU   B 1  253 ? 2.248   26.312  5.924   1    19.366  ? 253  LEU   B C   1 2 
ATOM   6986  O  O   . LEU   B 1  253 ? 1.213   26.235  6.595   1    19.748  ? 253  LEU   B O   1 2 
ATOM   6987  C  CB  . LEU   B 1  253 ? 1.698   24.465  4.23    1    18.89   ? 253  LEU   B CB  1 2 
ATOM   6988  C  CG  . LEU   B 1  253 ? 1.432   24.133  2.748   1    19.811  ? 253  LEU   B CG  1 2 
ATOM   6989  C  CD1 . LEU   B 1  253 ? 1.434   22.628  2.52    1    17.935  ? 253  LEU   B CD1 1 2 
ATOM   6990  C  CD2 . LEU   B 1  253 ? 0.083   24.751  2.268   1    19.943  ? 253  LEU   B CD2 1 2 
ATOM   6991  N  N   . GLY   B 1  254 ? 3.375   26.782  6.43    1    17.872  ? 254  GLY   B N   1 2 
ATOM   6992  C  CA  . GLY   B 1  254 ? 3.372   27.575  7.651   1    19.428  ? 254  GLY   B CA  1 2 
ATOM   6993  C  C   . GLY   B 1  254 ? 3.819   26.775  8.871   1    19.157  ? 254  GLY   B C   1 2 
ATOM   6994  O  O   . GLY   B 1  254 ? 3.872   27.302  9.973   1    20.804  ? 254  GLY   B O   1 2 
ATOM   6995  N  N   . ASP   B 1  255 ? 4.199   25.531  8.638   1    18.043  ? 255  ASP   B N   1 2 
ATOM   6996  C  CA  . ASP   B 1  255 ? 4.464   24.585  9.704   1    19.071  ? 255  ASP   B CA  1 2 
ATOM   6997  C  C   . ASP   B 1  255 ? 5.525   23.604  9.192   1    17.908  ? 255  ASP   B C   1 2 
ATOM   6998  O  O   . ASP   B 1  255 ? 5.511   23.226  8.015   1    17.865  ? 255  ASP   B O   1 2 
ATOM   6999  C  CB  . ASP   B 1  255 ? 3.139   23.902  10.013  1    20.968  ? 255  ASP   B CB  1 2 
ATOM   7000  C  CG  . ASP   B 1  255 ? 3.19    22.715  10.949  1    24.195  ? 255  ASP   B CG  1 2 
ATOM   7001  O  OD1 . ASP   B 1  255 ? 3.419   21.569  10.484  1    22.686  ? 255  ASP   B OD1 1 2 
ATOM   7002  O  OD2 . ASP   B 1  255 ? 2.906   22.958  12.135  1    29.766  ? 255  ASP   B OD2 1 2 
ATOM   7003  N  N   . MET   B 1  256 ? 6.436   23.173  10.07   1    16.805  ? 256  MET   B N   1 2 
ATOM   7004  C  CA  . MET   B 1  256 ? 7.538   22.281  9.668   1    16.899  ? 256  MET   B CA  1 2 
ATOM   7005  C  C   . MET   B 1  256 ? 7.027   20.998  8.991   1    17.061  ? 256  MET   B C   1 2 
ATOM   7006  O  O   . MET   B 1  256 ? 7.742   20.428  8.146   1    18.858  ? 256  MET   B O   1 2 
ATOM   7007  C  CB  . MET   B 1  256 ? 8.391   21.931  10.888  1    18.409  ? 256  MET   B CB  1 2 
ATOM   7008  C  CG  . MET   B 1  256 ? 9.633   21.076  10.585  1    21.171  ? 256  MET   B CG  1 2 
ATOM   7009  S  SD  . MET   B 1  256 ? 10.738  21.924  9.416   1    19.8    ? 256  MET   B SD  1 2 
ATOM   7010  C  CE  . MET   B 1  256 ? 11.556  22.976  10.635  1    21.421  ? 256  MET   B CE  1 2 
ATOM   7011  N  N   . TRP   B 1  257 ? 5.839   20.524  9.385   1    14.958  ? 257  TRP   B N   1 2 
ATOM   7012  C  CA  . TRP   B 1  257 ? 5.337   19.233  8.913   1    15.685  ? 257  TRP   B CA  1 2 
ATOM   7013  C  C   . TRP   B 1  257 ? 4.189   19.43   7.934   1    14.356  ? 257  TRP   B C   1 2 
ATOM   7014  O  O   . TRP   B 1  257 ? 3.607   18.452  7.496   1    14.764  ? 257  TRP   B O   1 2 
ATOM   7015  C  CB  . TRP   B 1  257 ? 4.923   18.29   10.068  1    15.717  ? 257  TRP   B CB  1 2 
ATOM   7016  C  CG  . TRP   B 1  257 ? 6.099   18.092  10.972  1    15.663  ? 257  TRP   B CG  1 2 
ATOM   7017  C  CD1 . TRP   B 1  257 ? 7.181   17.284  10.781  1    17.486  ? 257  TRP   B CD1 1 2 
ATOM   7018  C  CD2 . TRP   B 1  257 ? 6.396   18.928  12.096  1    16.588  ? 257  TRP   B CD2 1 2 
ATOM   7019  N  NE1 . TRP   B 1  257 ? 8.111   17.511  11.763  1    17.464  ? 257  TRP   B NE1 1 2 
ATOM   7020  C  CE2 . TRP   B 1  257 ? 7.659   18.509  12.578  1    16.969  ? 257  TRP   B CE2 1 2 
ATOM   7021  C  CE3 . TRP   B 1  257 ? 5.701   19.948  12.759  1    16.979  ? 257  TRP   B CE3 1 2 
ATOM   7022  C  CZ2 . TRP   B 1  257 ? 8.239   19.118  13.671  1    18.053  ? 257  TRP   B CZ2 1 2 
ATOM   7023  C  CZ3 . TRP   B 1  257 ? 6.28    20.564  13.85   1    19.668  ? 257  TRP   B CZ3 1 2 
ATOM   7024  C  CH2 . TRP   B 1  257 ? 7.552   20.148  14.27   1    18.573  ? 257  TRP   B CH2 1 2 
ATOM   7025  N  N   . ALA   B 1  258 ? 3.855   20.691  7.676   1    14.436  ? 258  ALA   B N   1 2 
ATOM   7026  C  CA  . ALA   B 1  258 ? 2.709   21.019  6.834   1    16.563  ? 258  ALA   B CA  1 2 
ATOM   7027  C  C   . ALA   B 1  258 ? 1.438   20.449  7.462   1    15.831  ? 258  ALA   B C   1 2 
ATOM   7028  O  O   . ALA   B 1  258 ? 0.481   20.161  6.755   1    16.965  ? 258  ALA   B O   1 2 
ATOM   7029  C  CB  . ALA   B 1  258 ? 2.891   20.604  5.354   1    15.227  ? 258  ALA   B CB  1 2 
ATOM   7030  N  N   . GLN   B 1  259 ? 1.387   20.346  8.783   1    15.108  ? 259  GLN   B N   1 2 
ATOM   7031  C  CA  . GLN   B 1  259 ? 0.286   19.569  9.334   1    16.932  ? 259  GLN   B CA  1 2 
ATOM   7032  C  C   . GLN   B 1  259 ? -0.891  20.472  9.706   1    19.946  ? 259  GLN   B C   1 2 
ATOM   7033  O  O   . GLN   B 1  259 ? -2.018  20.012  9.822   1    24.77   ? 259  GLN   B O   1 2 
ATOM   7034  C  CB  . GLN   B 1  259 ? 0.774   18.822  10.563  1    17.236  ? 259  GLN   B CB  1 2 
ATOM   7035  C  CG  . GLN   B 1  259 ? 1.042   19.746  11.744  1    20.918  ? 259  GLN   B CG  1 2 
ATOM   7036  C  CD  . GLN   B 1  259 ? 1.532   18.956  12.939  1    27.143  ? 259  GLN   B CD  1 2 
ATOM   7037  O  OE1 . GLN   B 1  259 ? 2.539   18.247  12.842  1    25.342  ? 259  GLN   B OE1 1 2 
ATOM   7038  N  NE2 . GLN   B 1  259 ? 0.83    19.057  14.068  1    28.577  ? 259  GLN   B NE2 1 2 
ATOM   7039  N  N   . SER   B 1  260 ? -0.622  21.737  9.942   1    19.472  ? 260  SER   B N   1 2 
ATOM   7040  C  CA  . SER   B 1  260 ? -1.743  22.648  9.989   1    24.549  ? 260  SER   B CA  1 2 
ATOM   7041  C  C   . SER   B 1  260 ? -1.297  23.961  9.356   1    22.904  ? 260  SER   B C   1 2 
ATOM   7042  O  O   . SER   B 1  260 ? -0.105  24.283  9.413   1    22.561  ? 260  SER   B O   1 2 
ATOM   7043  C  CB  . SER   B 1  260 ? -2.321  22.817  11.364  1    30.53   ? 260  SER   B CB  1 2 
ATOM   7044  O  OG  . SER   B 1  260 ? -1.366  23.474  12.163  1    28.704  ? 260  SER   B OG  1 2 
ATOM   7045  N  N   . TRP   B 1  261 ? -2.254  24.635  8.715   1    17.767  ? 261  TRP   B N   1 2 
ATOM   7046  C  CA  . TRP   B 1  261 ? -1.879  25.691  7.782   1    18.152  ? 261  TRP   B CA  1 2 
ATOM   7047  C  C   . TRP   B 1  261 ? -2.334  27.05   8.314   1    18.114  ? 261  TRP   B C   1 2 
ATOM   7048  O  O   . TRP   B 1  261 ? -2.412  28.007  7.551   1    18.495  ? 261  TRP   B O   1 2 
ATOM   7049  C  CB  . TRP   B 1  261 ? -2.506  25.432  6.394   1    16.702  ? 261  TRP   B CB  1 2 
ATOM   7050  C  CG  . TRP   B 1  261 ? -2.126  24.121  5.786   1    16.102  ? 261  TRP   B CG  1 2 
ATOM   7051  C  CD1 . TRP   B 1  261 ? -1.198  23.195  6.188   1    15.889  ? 261  TRP   B CD1 1 2 
ATOM   7052  C  CD2 . TRP   B 1  261 ? -2.648  23.621  4.541   1    17.128  ? 261  TRP   B CD2 1 2 
ATOM   7053  N  NE1 . TRP   B 1  261 ? -1.155  22.126  5.305   1    15.227  ? 261  TRP   B NE1 1 2 
ATOM   7054  C  CE2 . TRP   B 1  261 ? -2.017  22.383  4.278   1    16.166  ? 261  TRP   B CE2 1 2 
ATOM   7055  C  CE3 . TRP   B 1  261 ? -3.61   24.119  3.644   1    18.54   ? 261  TRP   B CE3 1 2 
ATOM   7056  C  CZ2 . TRP   B 1  261 ? -2.292  21.624  3.137   1    16.905  ? 261  TRP   B CZ2 1 2 
ATOM   7057  C  CZ3 . TRP   B 1  261 ? -3.914  23.356  2.525   1    20.226  ? 261  TRP   B CZ3 1 2 
ATOM   7058  C  CH2 . TRP   B 1  261 ? -3.241  22.144  2.271   1    18.029  ? 261  TRP   B CH2 1 2 
ATOM   7059  N  N   . GLU   B 1  262 ? -2.708  27.138  9.594   1    17.911  ? 262  GLU   B N   1 2 
ATOM   7060  C  CA  . GLU   B 1  262 ? -3.258  28.434  10.028  1    19.861  ? 262  GLU   B CA  1 2 
ATOM   7061  C  C   . GLU   B 1  262 ? -2.264  29.592  9.867   1    19.866  ? 262  GLU   B C   1 2 
ATOM   7062  O  O   . GLU   B 1  262 ? -2.659  30.755  9.733   1    19.764  ? 262  GLU   B O   1 2 
ATOM   7063  C  CB  . GLU   B 1  262 ? -3.67   28.443  11.502  1    23.35   ? 262  GLU   B CB  1 2 
ATOM   7064  C  CG  . GLU   B 1  262 ? -2.515  28.112  12.441  1    30.048  ? 262  GLU   B CG  1 2 
ATOM   7065  C  CD  . GLU   B 1  262 ? -2.165  26.612  12.649  1    39.965  ? 262  GLU   B CD  1 2 
ATOM   7066  O  OE1 . GLU   B 1  262 ? -2.554  25.592  11.894  1    31.082  ? 262  GLU   B OE1 1 2 
ATOM   7067  O  OE2 . GLU   B 1  262 ? -1.42   26.478  13.673  1    40.138  ? 262  GLU   B OE2 1 2 
ATOM   7068  N  N   . ASN   B 1  263 ? -0.954  29.309  9.916   1    18.843  ? 263  ASN   B N   1 2 
ATOM   7069  C  CA  . ASN   B 1  263 ? 0.004   30.393  9.803   1    22.781  ? 263  ASN   B CA  1 2 
ATOM   7070  C  C   . ASN   B 1  263 ? 0.031   31.066  8.439   1    24.381  ? 263  ASN   B C   1 2 
ATOM   7071  O  O   . ASN   B 1  263 ? 0.589   32.154  8.348   1    24.588  ? 263  ASN   B O   1 2 
ATOM   7072  C  CB  . ASN   B 1  263 ? 1.435   30      10.145  1    23.52   ? 263  ASN   B CB  1 2 
ATOM   7073  C  CG  . ASN   B 1  263 ? 1.516   29.663  11.605  1    26.516  ? 263  ASN   B CG  1 2 
ATOM   7074  O  OD1 . ASN   B 1  263 ? 1.898   28.547  11.982  1    29.642  ? 263  ASN   B OD1 1 2 
ATOM   7075  N  ND2 . ASN   B 1  263 ? 1.152   30.621  12.431  1    22.852  ? 263  ASN   B ND2 1 2 
ATOM   7076  N  N   . ILE   B 1  264 ? -0.593  30.482  7.396   1    23.324  ? 264  ILE   B N   1 2 
ATOM   7077  C  CA  . ILE   B 1  264 ? -0.61   31.21   6.133   1    23.95   ? 264  ILE   B CA  1 2 
ATOM   7078  C  C   . ILE   B 1  264 ? -1.983  31.797  5.884   1    25.541  ? 264  ILE   B C   1 2 
ATOM   7079  O  O   . ILE   B 1  264 ? -2.263  32.186  4.749   1    26.84   ? 264  ILE   B O   1 2 
ATOM   7080  C  CB  . ILE   B 1  264 ? -0.182  30.306  4.954   1    26.202  ? 264  ILE   B CB  1 2 
ATOM   7081  C  CG1 . ILE   B 1  264 ? -1.054  29.088  4.803   1    24.358  ? 264  ILE   B CG1 1 2 
ATOM   7082  C  CG2 . ILE   B 1  264 ? 1.291   29.938  5.049   1    25.208  ? 264  ILE   B CG2 1 2 
ATOM   7083  C  CD1 . ILE   B 1  264 ? -0.76   28.305  3.536   1    28.843  ? 264  ILE   B CD1 1 2 
ATOM   7084  N  N   . TYR   B 1  265 ? -2.826  31.887  6.927   1    23.243  ? 265  TYR   B N   1 2 
ATOM   7085  C  CA  . TYR   B 1  265 ? -4.148  32.521  6.804   1    24.727  ? 265  TYR   B CA  1 2 
ATOM   7086  C  C   . TYR   B 1  265 ? -4.06   33.902  6.135   1    26.552  ? 265  TYR   B C   1 2 
ATOM   7087  O  O   . TYR   B 1  265 ? -4.894  34.27   5.276   1    27.296  ? 265  TYR   B O   1 2 
ATOM   7088  C  CB  . TYR   B 1  265 ? -4.795  32.575  8.2     1    23.954  ? 265  TYR   B CB  1 2 
ATOM   7089  C  CG  . TYR   B 1  265 ? -6.108  33.344  8.184   1    26.145  ? 265  TYR   B CG  1 2 
ATOM   7090  C  CD1 . TYR   B 1  265 ? -7.265  32.795  7.64    1    25.316  ? 265  TYR   B CD1 1 2 
ATOM   7091  C  CD2 . TYR   B 1  265 ? -6.195  34.6    8.769   1    29.111  ? 265  TYR   B CD2 1 2 
ATOM   7092  C  CE1 . TYR   B 1  265 ? -8.469  33.48   7.642   1    27.029  ? 265  TYR   B CE1 1 2 
ATOM   7093  C  CE2 . TYR   B 1  265 ? -7.396  35.309  8.772   1    29.793  ? 265  TYR   B CE2 1 2 
ATOM   7094  C  CZ  . TYR   B 1  265 ? -8.531  34.737  8.221   1    29.274  ? 265  TYR   B CZ  1 2 
ATOM   7095  O  OH  . TYR   B 1  265 ? -9.703  35.428  8.207   1    33.671  ? 265  TYR   B OH  1 2 
ATOM   7096  N  N   . ASP   B 1  266 ? -3.098  34.712  6.554   1    27.389  ? 266  ASP   B N   1 2 
ATOM   7097  C  CA  . ASP   B 1  266 ? -3.012  36.059  6.004   1    33.609  ? 266  ASP   B CA  1 2 
ATOM   7098  C  C   . ASP   B 1  266 ? -2.858  36.033  4.463   1    36.01   ? 266  ASP   B C   1 2 
ATOM   7099  O  O   . ASP   B 1  266 ? -3.245  36.98   3.768   1    33.429  ? 266  ASP   B O   1 2 
ATOM   7100  C  CB  . ASP   B 1  266 ? -1.952  36.876  6.738   1    38.099  ? 266  ASP   B CB  1 2 
ATOM   7101  C  CG  . ASP   B 1  266 ? -0.517  36.357  6.656   1    44.25   ? 266  ASP   B CG  1 2 
ATOM   7102  O  OD1 . ASP   B 1  266 ? -0.316  35.203  6.187   1    46.157  ? 266  ASP   B OD1 1 2 
ATOM   7103  O  OD2 . ASP   B 1  266 ? 0.415   37.091  7.06    1    47.475  ? 266  ASP   B OD2 1 2 
ATOM   7104  N  N   . MET   B 1  267 ? -2.333  34.937  3.903   1    33.523  ? 267  MET   B N   1 2 
ATOM   7105  C  CA  . MET   B 1  267 ? -2.108  34.896  2.47    1    35.619  ? 267  MET   B CA  1 2 
ATOM   7106  C  C   . MET   B 1  267 ? -3.326  34.39   1.727   1    36.55   ? 267  MET   B C   1 2 
ATOM   7107  O  O   . MET   B 1  267 ? -3.38   34.533  0.5     1    40.02   ? 267  MET   B O   1 2 
ATOM   7108  C  CB  . MET   B 1  267 ? -0.958  33.978  2.078   1    38.005  ? 267  MET   B CB  1 2 
ATOM   7109  C  CG  . MET   B 1  267 ? 0.397   34.623  2.186   1    44.743  ? 267  MET   B CG  1 2 
ATOM   7110  S  SD  . MET   B 1  267 ? 1.522   33.492  1.331   1    61.574  ? 267  MET   B SD  1 2 
ATOM   7111  C  CE  . MET   B 1  267 ? 1.72    32.133  2.483   1    42.713  ? 267  MET   B CE  1 2 
ATOM   7112  N  N   . VAL   B 1  268 ? -4.284  33.782  2.431   1    32.302  ? 268  VAL   B N   1 2 
ATOM   7113  C  CA  . VAL   B 1  268 ? -5.361  33.114  1.703   1    33.25   ? 268  VAL   B CA  1 2 
ATOM   7114  C  C   . VAL   B 1  268 ? -6.735  33.628  2.115   1    36.041  ? 268  VAL   B C   1 2 
ATOM   7115  O  O   . VAL   B 1  268 ? -7.748  33.166  1.577   1    35.909  ? 268  VAL   B O   1 2 
ATOM   7116  C  CB  . VAL   B 1  268 ? -5.312  31.575  1.76    1    32.876  ? 268  VAL   B CB  1 2 
ATOM   7117  C  CG1 . VAL   B 1  268 ? -3.887  31.067  1.534   1    32.573  ? 268  VAL   B CG1 1 2 
ATOM   7118  C  CG2 . VAL   B 1  268 ? -5.846  31.011  3.077   1    32.236  ? 268  VAL   B CG2 1 2 
ATOM   7119  N  N   . VAL   B 1  269 ? -6.758  34.546  3.082   1    35.706  ? 269  VAL   B N   1 2 
ATOM   7120  C  CA  . VAL   B 1  269 ? -8.011  35.022  3.657   1    40.617  ? 269  VAL   B CA  1 2 
ATOM   7121  C  C   . VAL   B 1  269 ? -9.009  35.447  2.57    1    41.337  ? 269  VAL   B C   1 2 
ATOM   7122  O  O   . VAL   B 1  269 ? -8.714  36.308  1.757   1    43.141  ? 269  VAL   B O   1 2 
ATOM   7123  C  CB  . VAL   B 1  269 ? -7.761  36.102  4.736   1    39.017  ? 269  VAL   B CB  1 2 
ATOM   7124  C  CG1 . VAL   B 1  269 ? -6.664  37.07   4.352   1    42.813  ? 269  VAL   B CG1 1 2 
ATOM   7125  C  CG2 . VAL   B 1  269 ? -9.027  36.845  5.126   1    45.062  ? 269  VAL   B CG2 1 2 
ATOM   7126  N  N   . PRO   B 1  270 ? -10.215 34.835  2.517   1    42.592  ? 270  PRO   B N   1 2 
ATOM   7127  C  CA  . PRO   B 1  270 ? -11.194 35.056  1.451   1    43.283  ? 270  PRO   B CA  1 2 
ATOM   7128  C  C   . PRO   B 1  270 ? -11.784 36.432  1.199   1    48.807  ? 270  PRO   B C   1 2 
ATOM   7129  O  O   . PRO   B 1  270 ? -12.081 36.703  0.044   1    48.569  ? 270  PRO   B O   1 2 
ATOM   7130  C  CB  . PRO   B 1  270 ? -12.327 34.048  1.747   1    44.085  ? 270  PRO   B CB  1 2 
ATOM   7131  C  CG  . PRO   B 1  270 ? -11.635 32.953  2.577   1    42.551  ? 270  PRO   B CG  1 2 
ATOM   7132  C  CD  . PRO   B 1  270 ? -10.659 33.76   3.424   1    44.234  ? 270  PRO   B CD  1 2 
ATOM   7133  N  N   . PHE   B 1  271 ? -12.075 37.204  2.278   1    46.7    ? 271  PHE   B N   1 2 
ATOM   7134  C  CA  . PHE   B 1  271 ? -12.528 38.588  2.235   1    45.937  ? 271  PHE   B CA  1 2 
ATOM   7135  C  C   . PHE   B 1  271 ? -11.572 39.415  3.098   1    47.459  ? 271  PHE   B C   1 2 
ATOM   7136  O  O   . PHE   B 1  271 ? -11.86  39.683  4.269   1    44.634  ? 271  PHE   B O   1 2 
ATOM   7137  C  CB  . PHE   B 1  271 ? -13.978 38.543  2.711   1    44.962  ? 271  PHE   B CB  1 2 
ATOM   7138  C  CG  . PHE   B 1  271 ? -14.866 37.674  1.83    1    45.689  ? 271  PHE   B CG  1 2 
ATOM   7139  C  CD1 . PHE   B 1  271 ? -15.37  38.164  0.624   1    47.419  ? 271  PHE   B CD1 1 2 
ATOM   7140  C  CD2 . PHE   B 1  271 ? -15.234 36.382  2.217   1    43.181  ? 271  PHE   B CD2 1 2 
ATOM   7141  C  CE1 . PHE   B 1  271 ? -16.18  37.366  -0.195  1    48.606  ? 271  PHE   B CE1 1 2 
ATOM   7142  C  CE2 . PHE   B 1  271 ? -16.054 35.59   1.399   1    43.814  ? 271  PHE   B CE2 1 2 
ATOM   7143  C  CZ  . PHE   B 1  271 ? -16.525 36.078  0.186   1    44.262  ? 271  PHE   B CZ  1 2 
ATOM   7144  N  N   . PRO   B 1  272 ? -10.373 39.752  2.553   1    53.022  ? 272  PRO   B N   1 2 
ATOM   7145  C  CA  . PRO   B 1  272 ? -9.22   40.287  3.324   1    55.37   ? 272  PRO   B CA  1 2 
ATOM   7146  C  C   . PRO   B 1  272 ? -9.073  41.526  4.212   1    61.893  ? 272  PRO   B C   1 2 
ATOM   7147  O  O   . PRO   B 1  272 ? -8.141  41.616  5.015   1    62.555  ? 272  PRO   B O   1 2 
ATOM   7148  C  CB  . PRO   B 1  272 ? -8.098  40.279  2.269   1    54.881  ? 272  PRO   B CB  1 2 
ATOM   7149  C  CG  . PRO   B 1  272 ? -8.841  40.394  0.959   1    58.187  ? 272  PRO   B CG  1 2 
ATOM   7150  C  CD  . PRO   B 1  272 ? -10.021 39.455  1.147   1    54.686  ? 272  PRO   B CD  1 2 
ATOM   7151  N  N   . ASP   B 1  273 ? -9.959  42.499  4.03    1    65.558  ? 273  ASP   B N   1 2 
ATOM   7152  C  CA  . ASP   B 1  273 ? -9.926  43.796  4.691   1    70.476  ? 273  ASP   B CA  1 2 
ATOM   7153  C  C   . ASP   B 1  273 ? -10.664 43.784  6.033   1    71.296  ? 273  ASP   B C   1 2 
ATOM   7154  O  O   . ASP   B 1  273 ? -10.56  44.762  6.783   1    70.436  ? 273  ASP   B O   1 2 
ATOM   7155  C  CB  . ASP   B 1  273 ? -10.806 44.726  3.88    1    76.261  ? 273  ASP   B CB  1 2 
ATOM   7156  C  CG  . ASP   B 1  273 ? -12.133 44.05   3.572   1    76.466  ? 273  ASP   B CG  1 2 
ATOM   7157  O  OD1 . ASP   B 1  273 ? -12.094 42.911  3.03    1    79.058  ? 273  ASP   B OD1 1 2 
ATOM   7158  O  OD2 . ASP   B 1  273 ? -13.177 44.594  3.979   1    77.349  ? 273  ASP   B OD2 1 2 
ATOM   7159  N  N   . LYS   B 1  274 ? -11.463 42.725  6.29    1    62.193  ? 274  LYS   B N   1 2 
ATOM   7160  C  CA  . LYS   B 1  274 ? -12.343 42.626  7.443   1    55.668  ? 274  LYS   B CA  1 2 
ATOM   7161  C  C   . LYS   B 1  274 ? -11.463 42.507  8.672   1    56.436  ? 274  LYS   B C   1 2 
ATOM   7162  O  O   . LYS   B 1  274 ? -10.254 42.409  8.525   1    62.121  ? 274  LYS   B O   1 2 
ATOM   7163  C  CB  . LYS   B 1  274 ? -13.206 41.369  7.37    1    52.204  ? 274  LYS   B CB  1 2 
ATOM   7164  C  CG  . LYS   B 1  274 ? -14.185 41.247  6.241   1    56.029  ? 274  LYS   B CG  1 2 
ATOM   7165  C  CD  . LYS   B 1  274 ? -15.466 42.005  6.537   1    61.408  ? 274  LYS   B CD  1 2 
ATOM   7166  C  CE  . LYS   B 1  274 ? -16.596 41.178  6.043   1    63.041  ? 274  LYS   B CE  1 2 
ATOM   7167  N  NZ  . LYS   B 1  274 ? -17.864 41.672  6.584   1    68.102  ? 274  LYS   B NZ  1 2 
ATOM   7168  N  N   . PRO   B 1  275 ? -12.004 42.473  9.912   1    57.771  ? 275  PRO   B N   1 2 
ATOM   7169  C  CA  . PRO   B 1  275 ? -11.15  42.378  11.102  1    55.999  ? 275  PRO   B CA  1 2 
ATOM   7170  C  C   . PRO   B 1  275 ? -10.257 41.145  10.986  1    52.036  ? 275  PRO   B C   1 2 
ATOM   7171  O  O   . PRO   B 1  275 ? -10.681 40.112  10.469  1    49.208  ? 275  PRO   B O   1 2 
ATOM   7172  C  CB  . PRO   B 1  275 ? -12.137 42.276  12.283  1    57.913  ? 275  PRO   B CB  1 2 
ATOM   7173  C  CG  . PRO   B 1  275 ? -13.435 42.841  11.715  1    62.856  ? 275  PRO   B CG  1 2 
ATOM   7174  C  CD  . PRO   B 1  275 ? -13.443 42.498  10.229  1    61.072  ? 275  PRO   B CD  1 2 
ATOM   7175  N  N   . ASN   B 1  276 ? -9.013  41.294  11.445  1    47.971  ? 276  ASN   B N   1 2 
ATOM   7176  C  CA  . ASN   B 1  276 ? -8.027  40.234  11.457  1    48.103  ? 276  ASN   B CA  1 2 
ATOM   7177  C  C   . ASN   B 1  276 ? -8.424  39.2    12.521  1    44.846  ? 276  ASN   B C   1 2 
ATOM   7178  O  O   . ASN   B 1  276 ? -8.371  39.493  13.716  1    42.504  ? 276  ASN   B O   1 2 
ATOM   7179  C  CB  . ASN   B 1  276 ? -6.654  40.867  11.669  1    49.075  ? 276  ASN   B CB  1 2 
ATOM   7180  C  CG  . ASN   B 1  276 ? -5.534  39.855  11.677  1    51.059  ? 276  ASN   B CG  1 2 
ATOM   7181  O  OD1 . ASN   B 1  276 ? -5.712  38.726  11.207  1    49.713  ? 276  ASN   B OD1 1 2 
ATOM   7182  N  ND2 . ASN   B 1  276 ? -4.375  40.242  12.197  1    54.25   ? 276  ASN   B ND2 1 2 
ATOM   7183  N  N   . LEU   B 1  277 ? -8.82   37.995  12.08   1    41.729  ? 277  LEU   B N   1 2 
ATOM   7184  C  CA  . LEU   B 1  277 ? -9.296  36.946  12.981  1    40.961  ? 277  LEU   B CA  1 2 
ATOM   7185  C  C   . LEU   B 1  277 ? -8.13   36.239  13.656  1    40.135  ? 277  LEU   B C   1 2 
ATOM   7186  O  O   . LEU   B 1  277 ? -8.348  35.369  14.498  1    44.989  ? 277  LEU   B O   1 2 
ATOM   7187  C  CB  . LEU   B 1  277 ? -10.2   35.914  12.305  1    38.891  ? 277  LEU   B CB  1 2 
ATOM   7188  C  CG  . LEU   B 1  277 ? -11.574 36.416  11.855  1    44.36   ? 277  LEU   B CG  1 2 
ATOM   7189  C  CD1 . LEU   B 1  277 ? -12.287 35.299  11.117  1    41.288  ? 277  LEU   B CD1 1 2 
ATOM   7190  C  CD2 . LEU   B 1  277 ? -12.425 36.987  12.995  1    42.352  ? 277  LEU   B CD2 1 2 
ATOM   7191  N  N   . ASP   B 1  278 ? -6.902  36.544  13.24   1    39.61   ? 278  ASP   B N   1 2 
ATOM   7192  C  CA  . ASP   B 1  278 ? -5.756  36.055  13.988  1    39.698  ? 278  ASP   B CA  1 2 
ATOM   7193  C  C   . ASP   B 1  278 ? -5.396  37.155  14.977  1    39.138  ? 278  ASP   B C   1 2 
ATOM   7194  O  O   . ASP   B 1  278 ? -4.971  38.224  14.54   1    43.064  ? 278  ASP   B O   1 2 
ATOM   7195  C  CB  . ASP   B 1  278 ? -4.591  35.596  13.104  1    44.373  ? 278  ASP   B CB  1 2 
ATOM   7196  C  CG  . ASP   B 1  278 ? -3.215  35.476  13.775  1    52.129  ? 278  ASP   B CG  1 2 
ATOM   7197  O  OD1 . ASP   B 1  278 ? -3.132  35.384  15.039  1    49.424  ? 278  ASP   B OD1 1 2 
ATOM   7198  O  OD2 . ASP   B 1  278 ? -2.206  35.541  13.046  1    55.927  ? 278  ASP   B OD2 1 2 
ATOM   7199  N  N   . VAL   B 1  279 ? -5.581  36.867  16.282  1    33.69   ? 279  VAL   B N   1 2 
ATOM   7200  C  CA  . VAL   B 1  279 ? -5.528  37.857  17.349  1    30.597  ? 279  VAL   B CA  1 2 
ATOM   7201  C  C   . VAL   B 1  279 ? -4.117  37.928  17.936  1    28.412  ? 279  VAL   B C   1 2 
ATOM   7202  O  O   . VAL   B 1  279 ? -3.852  38.58   18.943  1    28.15   ? 279  VAL   B O   1 2 
ATOM   7203  C  CB  . VAL   B 1  279 ? -6.633  37.576  18.395  1    31.204  ? 279  VAL   B CB  1 2 
ATOM   7204  C  CG1 . VAL   B 1  279 ? -8.019  37.567  17.76   1    33.964  ? 279  VAL   B CG1 1 2 
ATOM   7205  C  CG2 . VAL   B 1  279 ? -6.431  36.33   19.238  1    28.197  ? 279  VAL   B CG2 1 2 
ATOM   7206  N  N   . THR   B 1  280 ? -3.176  37.226  17.312  1    28.814  ? 280  THR   B N   1 2 
ATOM   7207  C  CA  . THR   B 1  280 ? -1.826  37.227  17.837  1    28.519  ? 280  THR   B CA  1 2 
ATOM   7208  C  C   . THR   B 1  280 ? -1.358  38.649  18.07   1    29.94   ? 280  THR   B C   1 2 
ATOM   7209  O  O   . THR   B 1  280 ? -0.886  38.968  19.152  1    29.53   ? 280  THR   B O   1 2 
ATOM   7210  C  CB  . THR   B 1  280 ? -0.855  36.486  16.914  1    30.256  ? 280  THR   B CB  1 2 
ATOM   7211  O  OG1 . THR   B 1  280 ? -1.166  35.1    16.899  1    30.15   ? 280  THR   B OG1 1 2 
ATOM   7212  C  CG2 . THR   B 1  280 ? 0.568   36.657  17.401  1    30.382  ? 280  THR   B CG2 1 2 
ATOM   7213  N  N   . SER   B 1  281 ? -1.432  39.51   17.036  1    32.639  ? 281  SER   B N   1 2 
ATOM   7214  C  CA  . SER   B 1  281 ? -0.797  40.816  17.224  1    36.987  ? 281  SER   B CA  1 2 
ATOM   7215  C  C   . SER   B 1  281 ? -1.45   41.628  18.352  1    37.085  ? 281  SER   B C   1 2 
ATOM   7216  O  O   . SER   B 1  281 ? -0.747  42.393  19.019  1    36.416  ? 281  SER   B O   1 2 
ATOM   7217  C  CB  . SER   B 1  281 ? -0.662  41.618  15.934  1    40.673  ? 281  SER   B CB  1 2 
ATOM   7218  O  OG  . SER   B 1  281 ? -1.956  41.906  15.435  1    43.76   ? 281  SER   B OG  1 2 
ATOM   7219  N  N   . THR   B 1  282 ? -2.776  41.453  18.569  1    34.801  ? 282  THR   B N   1 2 
ATOM   7220  C  CA  . THR   B 1  282 ? -3.472  42.038  19.721  1    33.772  ? 282  THR   B CA  1 2 
ATOM   7221  C  C   . THR   B 1  282 ? -2.942  41.453  21.052  1    31.383  ? 282  THR   B C   1 2 
ATOM   7222  O  O   . THR   B 1  282 ? -2.768  42.171  22.013  1    31.999  ? 282  THR   B O   1 2 
ATOM   7223  C  CB  . THR   B 1  282 ? -4.989  41.855  19.567  1    34.127  ? 282  THR   B CB  1 2 
ATOM   7224  O  OG1 . THR   B 1  282 ? -5.487  42.374  18.326  1    36.679  ? 282  THR   B OG1 1 2 
ATOM   7225  C  CG2 . THR   B 1  282 ? -5.772  42.436  20.738  1    32.979  ? 282  THR   B CG2 1 2 
ATOM   7226  N  N   . MET   B 1  283 ? -2.723  40.126  21.163  1    30.74   ? 283  MET   B N   1 2 
ATOM   7227  C  CA  . MET   B 1  283 ? -2.175  39.529  22.381  1    28.917  ? 283  MET   B CA  1 2 
ATOM   7228  C  C   . MET   B 1  283 ? -0.827  40.165  22.729  1    31.015  ? 283  MET   B C   1 2 
ATOM   7229  O  O   . MET   B 1  283 ? -0.55   40.447  23.872  1    32.064  ? 283  MET   B O   1 2 
ATOM   7230  C  CB  . MET   B 1  283 ? -1.938  38.02   22.199  1    27.685  ? 283  MET   B CB  1 2 
ATOM   7231  C  CG  . MET   B 1  283 ? -3.209  37.223  21.978  1    27      ? 283  MET   B CG  1 2 
ATOM   7232  S  SD  . MET   B 1  283 ? -2.966  35.454  21.699  1    28.106  ? 283  MET   B SD  1 2 
ATOM   7233  C  CE  . MET   B 1  283 ? -2.468  34.908  23.345  1    26.072  ? 283  MET   B CE  1 2 
ATOM   7234  N  N   . LEU   B 1  284 ? 0.039   40.364  21.724  1    33.07   ? 284  LEU   B N   1 2 
ATOM   7235  C  CA  . LEU   B 1  284 ? 1.33    40.994  21.964  1    35.361  ? 284  LEU   B CA  1 2 
ATOM   7236  C  C   . LEU   B 1  284 ? 1.073   42.46   22.246  1    35.581  ? 284  LEU   B C   1 2 
ATOM   7237  O  O   . LEU   B 1  284 ? 1.686   43.003  23.133  1    35.094  ? 284  LEU   B O   1 2 
ATOM   7238  C  CB  . LEU   B 1  284 ? 2.171   40.844  20.697  1    37.99   ? 284  LEU   B CB  1 2 
ATOM   7239  C  CG  . LEU   B 1  284 ? 2.59    39.402  20.406  1    37.875  ? 284  LEU   B CG  1 2 
ATOM   7240  C  CD1 . LEU   B 1  284 ? 2.937   39.154  18.937  1    37.961  ? 284  LEU   B CD1 1 2 
ATOM   7241  C  CD2 . LEU   B 1  284 ? 3.704   39.037  21.409  1    36.254  ? 284  LEU   B CD2 1 2 
ATOM   7242  N  N   . GLN   B 1  285 ? 0.168   43.097  21.481  1    36.984  ? 285  GLN   B N   1 2 
ATOM   7243  C  CA  . GLN   B 1  285 ? -0.071  44.528  21.705  1    39.963  ? 285  GLN   B CA  1 2 
ATOM   7244  C  C   . GLN   B 1  285 ? -0.435  44.729  23.18   1    39.476  ? 285  GLN   B C   1 2 
ATOM   7245  O  O   . GLN   B 1  285 ? 0.048   45.66   23.792  1    40.752  ? 285  GLN   B O   1 2 
ATOM   7246  C  CB  . GLN   B 1  285 ? -0.989  45.182  20.654  1    42.083  ? 285  GLN   B CB  1 2 
ATOM   7247  C  CG  . GLN   B 1  285 ? -1.42   46.631  20.918  1    51.138  ? 285  GLN   B CG  1 2 
ATOM   7248  C  CD  . GLN   B 1  285 ? -2.788  46.76   21.568  1    56.753  ? 285  GLN   B CD  1 2 
ATOM   7249  O  OE1 . GLN   B 1  285 ? -2.945  47.346  22.648  1    62.527  ? 285  GLN   B OE1 1 2 
ATOM   7250  N  NE2 . GLN   B 1  285 ? -3.806  46.212  20.915  1    58.048  ? 285  GLN   B NE2 1 2 
ATOM   7251  N  N   . GLN   B 1  286 ? -1.246  43.821  23.753  1    38.649  ? 286  GLN   B N   1 2 
ATOM   7252  C  CA  . GLN   B 1  286 ? -1.776  43.938  25.114  1    38.669  ? 286  GLN   B CA  1 2 
ATOM   7253  C  C   . GLN   B 1  286 ? -0.808  43.389  26.164  1    37.278  ? 286  GLN   B C   1 2 
ATOM   7254  O  O   . GLN   B 1  286 ? -1.071  43.539  27.36   1    36.912  ? 286  GLN   B O   1 2 
ATOM   7255  C  CB  . GLN   B 1  286 ? -3.123  43.225  25.331  1    37.79   ? 286  GLN   B CB  1 2 
ATOM   7256  C  CG  . GLN   B 1  286 ? -4.293  43.819  24.543  1    39.992  ? 286  GLN   B CG  1 2 
ATOM   7257  C  CD  . GLN   B 1  286 ? -5.599  43.045  24.672  1    39.886  ? 286  GLN   B CD  1 2 
ATOM   7258  O  OE1 . GLN   B 1  286 ? -5.664  41.941  25.225  1    37.576  ? 286  GLN   B OE1 1 2 
ATOM   7259  N  NE2 . GLN   B 1  286 ? -6.671  43.608  24.137  1    39.451  ? 286  GLN   B NE2 1 2 
ATOM   7260  N  N   . GLY   B 1  287 ? 0.281   42.71   25.759  1    35.247  ? 287  GLY   B N   1 2 
ATOM   7261  C  CA  . GLY   B 1  287 ? 1.203   42.221  26.779  1    34.791  ? 287  GLY   B CA  1 2 
ATOM   7262  C  C   . GLY   B 1  287 ? 0.829   40.875  27.416  1    33.091  ? 287  GLY   B C   1 2 
ATOM   7263  O  O   . GLY   B 1  287 ? 1.231   40.589  28.538  1    32.629  ? 287  GLY   B O   1 2 
ATOM   7264  N  N   . TRP   B 1  288 ? 0.146   39.978  26.692  1    30.558  ? 288  TRP   B N   1 2 
ATOM   7265  C  CA  . TRP   B 1  288 ? -0.112  38.674  27.286  1    29.787  ? 288  TRP   B CA  1 2 
ATOM   7266  C  C   . TRP   B 1  288 ? 1.212   37.926  27.522  1    29.589  ? 288  TRP   B C   1 2 
ATOM   7267  O  O   . TRP   B 1  288 ? 2.164   38.082  26.758  1    28.783  ? 288  TRP   B O   1 2 
ATOM   7268  C  CB  . TRP   B 1  288 ? -1.002  37.853  26.329  1    28.8    ? 288  TRP   B CB  1 2 
ATOM   7269  C  CG  . TRP   B 1  288 ? -2.454  38.298  26.292  1    28.255  ? 288  TRP   B CG  1 2 
ATOM   7270  C  CD1 . TRP   B 1  288 ? -2.965  39.53   26.01   1    29.802  ? 288  TRP   B CD1 1 2 
ATOM   7271  C  CD2 . TRP   B 1  288 ? -3.588  37.44   26.525  1    27.202  ? 288  TRP   B CD2 1 2 
ATOM   7272  N  NE1 . TRP   B 1  288 ? -4.342  39.499  26.048  1    29.593  ? 288  TRP   B NE1 1 2 
ATOM   7273  C  CE2 . TRP   B 1  288 ? -4.75   38.23   26.359  1    27.818  ? 288  TRP   B CE2 1 2 
ATOM   7274  C  CE3 . TRP   B 1  288 ? -3.722  36.08   26.843  1    25.946  ? 288  TRP   B CE3 1 2 
ATOM   7275  C  CZ2 . TRP   B 1  288 ? -6.029  37.708  26.531  1    26.947  ? 288  TRP   B CZ2 1 2 
ATOM   7276  C  CZ3 . TRP   B 1  288 ? -4.987  35.564  27.003  1    26.289  ? 288  TRP   B CZ3 1 2 
ATOM   7277  C  CH2 . TRP   B 1  288 ? -6.119  36.378  26.871  1    25.713  ? 288  TRP   B CH2 1 2 
ATOM   7278  N  N   . GLN   B 1  289 ? 1.249   37.091  28.555  1    28.238  ? 289  GLN   B N   1 2 
ATOM   7279  C  CA  . GLN   B 1  289 ? 2.362   36.2    28.804  1    30.375  ? 289  GLN   B CA  1 2 
ATOM   7280  C  C   . GLN   B 1  289 ? 1.837   34.795  29.023  1    28.439  ? 289  GLN   B C   1 2 
ATOM   7281  O  O   . GLN   B 1  289 ? 0.623   34.602  29.104  1    28.171  ? 289  GLN   B O   1 2 
ATOM   7282  C  CB  . GLN   B 1  289 ? 3.11    36.586  30.076  1    33.103  ? 289  GLN   B CB  1 2 
ATOM   7283  C  CG  . GLN   B 1  289 ? 3.821   37.927  29.925  1    41.35   ? 289  GLN   B CG  1 2 
ATOM   7284  C  CD  . GLN   B 1  289 ? 4.898   37.923  28.861  1    44.861  ? 289  GLN   B CD  1 2 
ATOM   7285  O  OE1 . GLN   B 1  289 ? 5.306   36.884  28.314  1    48.691  ? 289  GLN   B OE1 1 2 
ATOM   7286  N  NE2 . GLN   B 1  289 ? 5.406   39.112  28.587  1    51.375  ? 289  GLN   B NE2 1 2 
ATOM   7287  N  N   . ALA   B 1  290 ? 2.761   33.838  29.133  1    25.774  ? 290  ALA   B N   1 2 
ATOM   7288  C  CA  . ALA   B 1  290 ? 2.38    32.453  29.316  1    26.464  ? 290  ALA   B CA  1 2 
ATOM   7289  C  C   . ALA   B 1  290 ? 1.395   32.336  30.468  1    27.319  ? 290  ALA   B C   1 2 
ATOM   7290  O  O   . ALA   B 1  290 ? 0.432   31.594  30.372  1    24.638  ? 290  ALA   B O   1 2 
ATOM   7291  C  CB  . ALA   B 1  290 ? 3.577   31.536  29.514  1    25.47   ? 290  ALA   B CB  1 2 
ATOM   7292  N  N   . THR   B 1  291 ? 1.651   33.082  31.547  1    28.243  ? 291  THR   B N   1 2 
ATOM   7293  C  CA  . THR   B 1  291 ? 0.839   32.903  32.721  1    31.236  ? 291  THR   B CA  1 2 
ATOM   7294  C  C   . THR   B 1  291 ? -0.618  33.336  32.449  1    29.743  ? 291  THR   B C   1 2 
ATOM   7295  O  O   . THR   B 1  291 ? -1.539  32.642  32.884  1    29.257  ? 291  THR   B O   1 2 
ATOM   7296  C  CB  . THR   B 1  291 ? 1.553   33.643  33.859  1    34.448  ? 291  THR   B CB  1 2 
ATOM   7297  O  OG1 . THR   B 1  291 ? 0.872   33.134  34.985  1    39.603  ? 291  THR   B OG1 1 2 
ATOM   7298  C  CG2 . THR   B 1  291 ? 1.344   35.138  33.82   1    34.972  ? 291  THR   B CG2 1 2 
ATOM   7299  N  N   . HIS   B 1  292 ? -0.837  34.422  31.688  1    28.765  ? 292  HIS   B N   1 2 
ATOM   7300  C  CA  . HIS   B 1  292 ? -2.197  34.862  31.394  1    28.559  ? 292  HIS   B CA  1 2 
ATOM   7301  C  C   . HIS   B 1  292 ? -2.935  33.803  30.58   1    26.22   ? 292  HIS   B C   1 2 
ATOM   7302  O  O   . HIS   B 1  292 ? -4.124  33.526  30.802  1    25.218  ? 292  HIS   B O   1 2 
ATOM   7303  C  CB  . HIS   B 1  292 ? -2.241  36.141  30.551  1    32.385  ? 292  HIS   B CB  1 2 
ATOM   7304  C  CG  . HIS   B 1  292 ? -1.573  37.299  31.203  1    38.942  ? 292  HIS   B CG  1 2 
ATOM   7305  N  ND1 . HIS   B 1  292 ? -0.246  37.599  30.959  1    40.008  ? 292  HIS   B ND1 1 2 
ATOM   7306  C  CD2 . HIS   B 1  292 ? -2.007  38.191  32.132  1    40.23   ? 292  HIS   B CD2 1 2 
ATOM   7307  C  CE1 . HIS   B 1  292 ? 0.087   38.674  31.663  1    41.583  ? 292  HIS   B CE1 1 2 
ATOM   7308  N  NE2 . HIS   B 1  292 ? -0.961  39.04   32.398  1    42.374  ? 292  HIS   B NE2 1 2 
ATOM   7309  N  N   . MET   B 1  293 ? -2.204  33.195  29.649  1    23.543  ? 293  MET   B N   1 2 
ATOM   7310  C  CA  . MET   B 1  293 ? -2.794  32.239  28.724  1    22.059  ? 293  MET   B CA  1 2 
ATOM   7311  C  C   . MET   B 1  293 ? -3.347  31.048  29.515  1    21.645  ? 293  MET   B C   1 2 
ATOM   7312  O  O   . MET   B 1  293 ? -4.46   30.597  29.241  1    20.603  ? 293  MET   B O   1 2 
ATOM   7313  C  CB  . MET   B 1  293 ? -1.714  31.765  27.739  1    22.037  ? 293  MET   B CB  1 2 
ATOM   7314  C  CG  . MET   B 1  293 ? -1.416  32.908  26.739  1    22.93   ? 293  MET   B CG  1 2 
ATOM   7315  S  SD  . MET   B 1  293 ? 0.108   32.648  25.805  1    26.197  ? 293  MET   B SD  1 2 
ATOM   7316  C  CE  . MET   B 1  293 ? -0.454  31.369  24.664  1    19.418  ? 293  MET   B CE  1 2 
ATOM   7317  N  N   . PHE   B 1  294 ? -2.518  30.493  30.422  1    20.57   ? 294  PHE   B N   1 2 
ATOM   7318  C  CA  . PHE   B 1  294 ? -2.94   29.393  31.279  1    20.373  ? 294  PHE   B CA  1 2 
ATOM   7319  C  C   . PHE   B 1  294 ? -4.143  29.8    32.173  1    20.168  ? 294  PHE   B C   1 2 
ATOM   7320  O  O   . PHE   B 1  294 ? -5.014  28.963  32.417  1    19.677  ? 294  PHE   B O   1 2 
ATOM   7321  C  CB  . PHE   B 1  294 ? -1.742  28.816  32.048  1    20.726  ? 294  PHE   B CB  1 2 
ATOM   7322  C  CG  . PHE   B 1  294 ? -0.888  27.9    31.19   1    20.563  ? 294  PHE   B CG  1 2 
ATOM   7323  C  CD1 . PHE   B 1  294 ? 0.134   28.422  30.395  1    21.657  ? 294  PHE   B CD1 1 2 
ATOM   7324  C  CD2 . PHE   B 1  294 ? -1.108  26.521  31.193  1    20.477  ? 294  PHE   B CD2 1 2 
ATOM   7325  C  CE1 . PHE   B 1  294 ? 0.889   27.577  29.583  1    20.482  ? 294  PHE   B CE1 1 2 
ATOM   7326  C  CE2 . PHE   B 1  294 ? -0.384  25.681  30.353  1    20.332  ? 294  PHE   B CE2 1 2 
ATOM   7327  C  CZ  . PHE   B 1  294 ? 0.601   26.225  29.538  1    20.748  ? 294  PHE   B CZ  1 2 
ATOM   7328  N  N   . ARG   B 1  295 ? -4.143  31.01   32.759  1    20.755  ? 295  ARG   B N   1 2 
ATOM   7329  C  CA  . ARG   B 1  295 ? -5.233  31.385  33.675  1    21.715  ? 295  ARG   B CA  1 2 
ATOM   7330  C  C   . ARG   B 1  295 ? -6.522  31.567  32.88   1    21.939  ? 295  ARG   B C   1 2 
ATOM   7331  O  O   . ARG   B 1  295 ? -7.639  31.333  33.36   1    21.897  ? 295  ARG   B O   1 2 
ATOM   7332  C  CB  . ARG   B 1  295 ? -4.995  32.69   34.46   1    22.506  ? 295  ARG   B CB  1 2 
ATOM   7333  C  CG  . ARG   B 1  295 ? -3.846  32.473  35.447  1    22.963  ? 295  ARG   B CG  1 2 
ATOM   7334  C  CD  . ARG   B 1  295 ? -4.295  31.498  36.536  1    23.64   ? 295  ARG   B CD  1 2 
ATOM   7335  N  NE  . ARG   B 1  295 ? -3.395  31.403  37.698  1    23.843  ? 295  ARG   B NE  1 2 
ATOM   7336  C  CZ  . ARG   B 1  295 ? -3.703  30.777  38.833  1    25.409  ? 295  ARG   B CZ  1 2 
ATOM   7337  N  NH1 . ARG   B 1  295 ? -4.948  30.315  39.086  1    25.428  ? 295  ARG   B NH1 1 2 
ATOM   7338  N  NH2 . ARG   B 1  295 ? -2.757  30.736  39.765  1    26.198  ? 295  ARG   B NH2 1 2 
ATOM   7339  N  N   . VAL   B 1  296 ? -6.358  32.058  31.66   1    22.09   ? 296  VAL   B N   1 2 
ATOM   7340  C  CA  . VAL   B 1  296 ? -7.544  32.276  30.852  1    23.033  ? 296  VAL   B CA  1 2 
ATOM   7341  C  C   . VAL   B 1  296 ? -8.131  30.93   30.438  1    21.777  ? 296  VAL   B C   1 2 
ATOM   7342  O  O   . VAL   B 1  296 ? -9.349  30.742  30.484  1    22.711  ? 296  VAL   B O   1 2 
ATOM   7343  C  CB  . VAL   B 1  296 ? -7.209  33.194  29.668  1    23.974  ? 296  VAL   B CB  1 2 
ATOM   7344  C  CG1 . VAL   B 1  296 ? -8.119  32.956  28.479  1    25.296  ? 296  VAL   B CG1 1 2 
ATOM   7345  C  CG2 . VAL   B 1  296 ? -7.057  34.639  30.099  1    24.547  ? 296  VAL   B CG2 1 2 
ATOM   7346  N  N   . ALA   B 1  297 ? -7.279  29.96   30.113  1    20.835  ? 297  ALA   B N   1 2 
ATOM   7347  C  CA  . ALA   B 1  297 ? -7.75   28.619  29.821  1    20.051  ? 297  ALA   B CA  1 2 
ATOM   7348  C  C   . ALA   B 1  297 ? -8.448  28.012  31.044  1    20.501  ? 297  ALA   B C   1 2 
ATOM   7349  O  O   . ALA   B 1  297 ? -9.546  27.472  30.96   1    20.772  ? 297  ALA   B O   1 2 
ATOM   7350  C  CB  . ALA   B 1  297 ? -6.615  27.741  29.357  1    19.24   ? 297  ALA   B CB  1 2 
ATOM   7351  N  N   . GLU   B 1  298 ? -7.843  28.16   32.222  1    20.809  ? 298  GLU   B N   1 2 
ATOM   7352  C  CA  . GLU   B 1  298 ? -8.424  27.572  33.406  1    21.809  ? 298  GLU   B CA  1 2 
ATOM   7353  C  C   . GLU   B 1  298 ? -9.846  28.103  33.653  1    22.796  ? 298  GLU   B C   1 2 
ATOM   7354  O  O   . GLU   B 1  298 ? -10.755 27.36   34.065  1    22.824  ? 298  GLU   B O   1 2 
ATOM   7355  C  CB  . GLU   B 1  298 ? -7.501  28.026  34.531  1    23.032  ? 298  GLU   B CB  1 2 
ATOM   7356  C  CG  . GLU   B 1  298 ? -7.91   27.447  35.886  1    26.209  ? 298  GLU   B CG  1 2 
ATOM   7357  C  CD  . GLU   B 1  298 ? -7.14   28.017  37.082  1    29.963  ? 298  GLU   B CD  1 2 
ATOM   7358  O  OE1 . GLU   B 1  298 ? -6.93   29.266  37.273  1    29.96   ? 298  GLU   B OE1 1 2 
ATOM   7359  O  OE2 . GLU   B 1  298 ? -6.831  27.142  37.936  1    34.106  ? 298  GLU   B OE2 1 2 
ATOM   7360  N  N   . GLU   B 1  299 ? -10.014 29.422  33.493  1    22.519  ? 299  GLU   B N   1 2 
ATOM   7361  C  CA  . GLU   B 1  299 ? -11.28  30.022  33.812  1    23.852  ? 299  GLU   B CA  1 2 
ATOM   7362  C  C   . GLU   B 1  299 ? -12.392 29.477  32.899  1    23.893  ? 299  GLU   B C   1 2 
ATOM   7363  O  O   . GLU   B 1  299 ? -13.588 29.471  33.287  1    24.092  ? 299  GLU   B O   1 2 
ATOM   7364  C  CB  . GLU   B 1  299 ? -11.099 31.539  33.804  1    25.305  ? 299  GLU   B CB  1 2 
ATOM   7365  C  CG  . GLU   B 1  299 ? -12.22  32.295  34.542  1    28.237  ? 299  GLU   B CG  1 2 
ATOM   7366  C  CD  . GLU   B 1  299 ? -13.507 32.449  33.713  1    31.336  ? 299  GLU   B CD  1 2 
ATOM   7367  O  OE1 . GLU   B 1  299 ? -13.4   32.64   32.465  1    32.284  ? 299  GLU   B OE1 1 2 
ATOM   7368  O  OE2 . GLU   B 1  299 ? -14.626 32.375  34.304  1    32.782  ? 299  GLU   B OE2 1 2 
ATOM   7369  N  N   . PHE   B 1  300 ? -12.026 29.148  31.657  1    22.924  ? 300  PHE   B N   1 2 
ATOM   7370  C  CA  . PHE   B 1  300 ? -12.994 28.484  30.786  1    24.28   ? 300  PHE   B CA  1 2 
ATOM   7371  C  C   . PHE   B 1  300 ? -13.475 27.207  31.482  1    24.134  ? 300  PHE   B C   1 2 
ATOM   7372  O  O   . PHE   B 1  300 ? -14.669 26.99   31.63   1    24.261  ? 300  PHE   B O   1 2 
ATOM   7373  C  CB  . PHE   B 1  300 ? -12.458 28.262  29.363  1    24.315  ? 300  PHE   B CB  1 2 
ATOM   7374  C  CG  . PHE   B 1  300 ? -13.551 28.038  28.324  1    26.08   ? 300  PHE   B CG  1 2 
ATOM   7375  C  CD1 . PHE   B 1  300 ? -14.342 26.888  28.352  1    28.815  ? 300  PHE   B CD1 1 2 
ATOM   7376  C  CD2 . PHE   B 1  300 ? -13.897 29.035  27.411  1    26.22   ? 300  PHE   B CD2 1 2 
ATOM   7377  C  CE1 . PHE   B 1  300 ? -15.378 26.694  27.413  1    30.152  ? 300  PHE   B CE1 1 2 
ATOM   7378  C  CE2 . PHE   B 1  300 ? -14.912 28.831  26.461  1    26.344  ? 300  PHE   B CE2 1 2 
ATOM   7379  C  CZ  . PHE   B 1  300 ? -15.668 27.678  26.477  1    27.189  ? 300  PHE   B CZ  1 2 
ATOM   7380  N  N   . PHE   B 1  301 ? -12.517 26.384  31.942  1    24.604  ? 301  PHE   B N   1 2 
ATOM   7381  C  CA  . PHE   B 1  301 ? -12.796 25.15   32.658  1    26.14   ? 301  PHE   B CA  1 2 
ATOM   7382  C  C   . PHE   B 1  301 ? -13.719 25.398  33.853  1    27.423  ? 301  PHE   B C   1 2 
ATOM   7383  O  O   . PHE   B 1  301 ? -14.726 24.698  33.976  1    27.872  ? 301  PHE   B O   1 2 
ATOM   7384  C  CB  . PHE   B 1  301 ? -11.531 24.359  33.006  1    26.434  ? 301  PHE   B CB  1 2 
ATOM   7385  C  CG  . PHE   B 1  301 ? -10.911 23.619  31.831  1    26.859  ? 301  PHE   B CG  1 2 
ATOM   7386  C  CD1 . PHE   B 1  301 ? -11.334 22.325  31.506  1    27.702  ? 301  PHE   B CD1 1 2 
ATOM   7387  C  CD2 . PHE   B 1  301 ? -9.943  24.21   31.03   1    26.656  ? 301  PHE   B CD2 1 2 
ATOM   7388  C  CE1 . PHE   B 1  301 ? -10.764 21.626  30.449  1    26.434  ? 301  PHE   B CE1 1 2 
ATOM   7389  C  CE2 . PHE   B 1  301 ? -9.38   23.51   29.952  1    28.413  ? 301  PHE   B CE2 1 2 
ATOM   7390  C  CZ  . PHE   B 1  301 ? -9.812  22.225  29.642  1    26.794  ? 301  PHE   B CZ  1 2 
ATOM   7391  N  N   . THR   B 1  302 ? -13.357 26.367  34.732  1    27.122  ? 302  THR   B N   1 2 
ATOM   7392  C  CA  . THR   B 1  302 ? -14.102 26.627  35.94   1    28.504  ? 302  THR   B CA  1 2 
ATOM   7393  C  C   . THR   B 1  302 ? -15.443 27.243  35.581  1    28.527  ? 302  THR   B C   1 2 
ATOM   7394  O  O   . THR   B 1  302 ? -16.359 27.123  36.372  1    29.707  ? 302  THR   B O   1 2 
ATOM   7395  C  CB  . THR   B 1  302 ? -13.321 27.501  36.924  1    29.865  ? 302  THR   B CB  1 2 
ATOM   7396  O  OG1 . THR   B 1  302 ? -13.023 28.751  36.294  1    28.001  ? 302  THR   B OG1 1 2 
ATOM   7397  C  CG2 . THR   B 1  302 ? -12.004 26.84   37.297  1    29.799  ? 302  THR   B CG2 1 2 
ATOM   7398  N  N   . SER   B 1  303 ? -15.571 27.854  34.391  1    27.85   ? 303  SER   B N   1 2 
ATOM   7399  C  CA  . SER   B 1  303 ? -16.853 28.454  34.032  1    29.098  ? 303  SER   B CA  1 2 
ATOM   7400  C  C   . SER   B 1  303 ? -17.9   27.356  33.797  1    29.937  ? 303  SER   B C   1 2 
ATOM   7401  O  O   . SER   B 1  303 ? -19.097 27.598  33.96   1    31.676  ? 303  SER   B O   1 2 
ATOM   7402  C  CB  . SER   B 1  303 ? -16.762 29.348  32.813  1    28.457  ? 303  SER   B CB  1 2 
ATOM   7403  O  OG  . SER   B 1  303 ? -16.828 28.538  31.645  1    30.01   ? 303  SER   B OG  1 2 
ATOM   7404  N  N   . LEU   B 1  304 ? -17.434 26.148  33.471  1    28.599  ? 304  LEU   B N   1 2 
ATOM   7405  C  CA  . LEU   B 1  304 ? -18.223 24.948  33.205  1    29.902  ? 304  LEU   B CA  1 2 
ATOM   7406  C  C   . LEU   B 1  304 ? -18.446 24.158  34.493  1    32.325  ? 304  LEU   B C   1 2 
ATOM   7407  O  O   . LEU   B 1  304 ? -19.04  23.075  34.441  1    33.457  ? 304  LEU   B O   1 2 
ATOM   7408  C  CB  . LEU   B 1  304 ? -17.513 24.032  32.193  1    27.254  ? 304  LEU   B CB  1 2 
ATOM   7409  C  CG  . LEU   B 1  304 ? -17.244 24.645  30.813  1    26.539  ? 304  LEU   B CG  1 2 
ATOM   7410  C  CD1 . LEU   B 1  304 ? -16.644 23.605  29.911  1    26.368  ? 304  LEU   B CD1 1 2 
ATOM   7411  C  CD2 . LEU   B 1  304 ? -18.531 25.097  30.169  1    27.285  ? 304  LEU   B CD2 1 2 
ATOM   7412  N  N   . GLU   B 1  305 ? -17.9   24.655  35.61   1    33.565  ? 305  GLU   B N   1 2 
ATOM   7413  C  CA  . GLU   B 1  305 ? -17.916 23.972  36.897  1    36.129  ? 305  GLU   B CA  1 2 
ATOM   7414  C  C   . GLU   B 1  305 ? -17.068 22.707  36.847  1    35.996  ? 305  GLU   B C   1 2 
ATOM   7415  O  O   . GLU   B 1  305 ? -17.25  21.803  37.646  1    38.376  ? 305  GLU   B O   1 2 
ATOM   7416  C  CB  . GLU   B 1  305 ? -19.33  23.765  37.439  1    41.113  ? 305  GLU   B CB  1 2 
ATOM   7417  C  CG  . GLU   B 1  305 ? -20.077 25.089  37.521  1    49.179  ? 305  GLU   B CG  1 2 
ATOM   7418  C  CD  . GLU   B 1  305 ? -21.042 25.216  38.681  1    60.614  ? 305  GLU   B CD  1 2 
ATOM   7419  O  OE1 . GLU   B 1  305 ? -22.283 25.176  38.46   1    65.608  ? 305  GLU   B OE1 1 2 
ATOM   7420  O  OE2 . GLU   B 1  305 ? -20.53  25.382  39.817  1    70.123  ? 305  GLU   B OE2 1 2 
ATOM   7421  N  N   . LEU   B 1  306 ? -16.084 22.675  35.949  1    34.382  ? 306  LEU   B N   1 2 
ATOM   7422  C  CA  . LEU   B 1  306 ? -15.01  21.704  36.077  1    33.503  ? 306  LEU   B CA  1 2 
ATOM   7423  C  C   . LEU   B 1  306 ? -13.987 22.253  37.069  1    33.124  ? 306  LEU   B C   1 2 
ATOM   7424  O  O   . LEU   B 1  306 ? -14.195 23.322  37.638  1    34.122  ? 306  LEU   B O   1 2 
ATOM   7425  C  CB  . LEU   B 1  306 ? -14.451 21.433  34.68   1    31.47   ? 306  LEU   B CB  1 2 
ATOM   7426  C  CG  . LEU   B 1  306 ? -15.447 20.869  33.663  1    32.943  ? 306  LEU   B CG  1 2 
ATOM   7427  C  CD1 . LEU   B 1  306 ? -14.742 20.74   32.336  1    30.991  ? 306  LEU   B CD1 1 2 
ATOM   7428  C  CD2 . LEU   B 1  306 ? -15.976 19.512  34.061  1    35.477  ? 306  LEU   B CD2 1 2 
ATOM   7429  N  N   . SER   B 1  307 ? -12.918 21.507  37.315  1    32.392  ? 307  SER   B N   1 2 
ATOM   7430  C  CA  . SER   B 1  307 ? -11.997 21.825  38.391  1    34.932  ? 307  SER   B CA  1 2 
ATOM   7431  C  C   . SER   B 1  307 ? -10.96  22.857  37.959  1    31.649  ? 307  SER   B C   1 2 
ATOM   7432  O  O   . SER   B 1  307 ? -10.487 22.841  36.816  1    29.897  ? 307  SER   B O   1 2 
ATOM   7433  C  CB  . SER   B 1  307 ? -11.322 20.595  38.893  1    36.704  ? 307  SER   B CB  1 2 
ATOM   7434  O  OG  . SER   B 1  307 ? -12.356 19.712  39.289  1    44.179  ? 307  SER   B OG  1 2 
ATOM   7435  N  N   . PRO   B 1  308 ? -10.586 23.758  38.898  1    31.433  ? 308  PRO   B N   1 2 
ATOM   7436  C  CA  . PRO   B 1  308 ? -9.421  24.623  38.707  1    30.557  ? 308  PRO   B CA  1 2 
ATOM   7437  C  C   . PRO   B 1  308 ? -8.16   23.763  38.722  1    29.146  ? 308  PRO   B C   1 2 
ATOM   7438  O  O   . PRO   B 1  308 ? -8.202  22.6    39.127  1    29.734  ? 308  PRO   B O   1 2 
ATOM   7439  C  CB  . PRO   B 1  308 ? -9.49   25.618  39.902  1    30.547  ? 308  PRO   B CB  1 2 
ATOM   7440  C  CG  . PRO   B 1  308 ? -10.261 24.857  40.969  1    33.249  ? 308  PRO   B CG  1 2 
ATOM   7441  C  CD  . PRO   B 1  308 ? -11.238 23.937  40.218  1    32.318  ? 308  PRO   B CD  1 2 
ATOM   7442  N  N   . MET   B 1  309 ? -7.049  24.325  38.24   1    27.591  ? 309  MET   B N   1 2 
ATOM   7443  C  CA  . MET   B 1  309 ? -5.753  23.684  38.407  1    27.801  ? 309  MET   B CA  1 2 
ATOM   7444  C  C   . MET   B 1  309 ? -5.359  23.768  39.881  1    28.903  ? 309  MET   B C   1 2 
ATOM   7445  O  O   . MET   B 1  309 ? -5.57   24.809  40.528  1    29.466  ? 309  MET   B O   1 2 
ATOM   7446  C  CB  . MET   B 1  309 ? -4.694  24.361  37.522  1    26.926  ? 309  MET   B CB  1 2 
ATOM   7447  C  CG  . MET   B 1  309 ? -5.032  24.399  36.03   1    26.233  ? 309  MET   B CG  1 2 
ATOM   7448  S  SD  . MET   B 1  309 ? -5.055  22.726  35.329  1    28.048  ? 309  MET   B SD  1 2 
ATOM   7449  C  CE  . MET   B 1  309 ? -6.851  22.577  35.495  1    27.541  ? 309  MET   B CE  1 2 
ATOM   7450  N  N   . PRO   B 1  310 ? -4.891  22.65   40.502  1    29.647  ? 310  PRO   B N   1 2 
ATOM   7451  C  CA  . PRO   B 1  310 ? -4.483  22.67   41.921  1    29.928  ? 310  PRO   B CA  1 2 
ATOM   7452  C  C   . PRO   B 1  310 ? -3.175  23.438  42.15   1    29.287  ? 310  PRO   B C   1 2 
ATOM   7453  O  O   . PRO   B 1  310 ? -2.45   23.684  41.188  1    28.434  ? 310  PRO   B O   1 2 
ATOM   7454  C  CB  . PRO   B 1  310 ? -4.353  21.159  42.232  1    30.514  ? 310  PRO   B CB  1 2 
ATOM   7455  C  CG  . PRO   B 1  310 ? -3.986  20.525  40.902  1    29.136  ? 310  PRO   B CG  1 2 
ATOM   7456  C  CD  . PRO   B 1  310 ? -4.713  21.339  39.837  1    28.792  ? 310  PRO   B CD  1 2 
ATOM   7457  N  N   . PRO   B 1  311 ? -2.821  23.835  43.402  1    30.082  ? 311  PRO   B N   1 2 
ATOM   7458  C  CA  . PRO   B 1  311 ? -1.543  24.503  43.701  1    30.203  ? 311  PRO   B CA  1 2 
ATOM   7459  C  C   . PRO   B 1  311 ? -0.308  23.793  43.144  1    29.647  ? 311  PRO   B C   1 2 
ATOM   7460  O  O   . PRO   B 1  311 ? 0.577   24.431  42.565  1    29.195  ? 311  PRO   B O   1 2 
ATOM   7461  C  CB  . PRO   B 1  311 ? -1.5    24.506  45.26   1    31.661  ? 311  PRO   B CB  1 2 
ATOM   7462  C  CG  . PRO   B 1  311 ? -2.947  24.489  45.657  1    32.478  ? 311  PRO   B CG  1 2 
ATOM   7463  C  CD  . PRO   B 1  311 ? -3.632  23.604  44.604  1    30.886  ? 311  PRO   B CD  1 2 
ATOM   7464  N  N   . GLU   B 1  312 ? -0.28   22.463  43.284  1    30.424  ? 312  GLU   B N   1 2 
ATOM   7465  C  CA  . GLU   B 1  312 ? 0.817   21.636  42.781  1    31.369  ? 312  GLU   B CA  1 2 
ATOM   7466  C  C   . GLU   B 1  312 ? 1.032   21.852  41.285  1    29.389  ? 312  GLU   B C   1 2 
ATOM   7467  O  O   . GLU   B 1  312 ? 2.181   21.775  40.838  1    28.74   ? 312  GLU   B O   1 2 
ATOM   7468  C  CB  . GLU   B 1  312 ? 0.545   20.146  43.003  1    33.929  ? 312  GLU   B CB  1 2 
ATOM   7469  C  CG  . GLU   B 1  312 ? 0.388   19.807  44.495  1    38.354  ? 312  GLU   B CG  1 2 
ATOM   7470  C  CD  . GLU   B 1  312 ? -0.894  20.093  45.293  1    41.812  ? 312  GLU   B CD  1 2 
ATOM   7471  O  OE1 . GLU   B 1  312 ? -1.931  20.552  44.765  1    41.276  ? 312  GLU   B OE1 1 2 
ATOM   7472  O  OE2 . GLU   B 1  312 ? -0.878  19.834  46.509  1    45.789  ? 312  GLU   B OE2 1 2 
ATOM   7473  N  N   . PHE   B 1  313 ? -0.054  22.137  40.521  1    27.106  ? 313  PHE   B N   1 2 
ATOM   7474  C  CA  . PHE   B 1  313 ? 0.069   22.411  39.085  1    25.98   ? 313  PHE   B CA  1 2 
ATOM   7475  C  C   . PHE   B 1  313 ? 0.855   23.703  38.855  1    26.377  ? 313  PHE   B C   1 2 
ATOM   7476  O  O   . PHE   B 1  313 ? 1.773   23.718  38.025  1    26.082  ? 313  PHE   B O   1 2 
ATOM   7477  C  CB  . PHE   B 1  313 ? -1.281  22.451  38.34   1    24.891  ? 313  PHE   B CB  1 2 
ATOM   7478  C  CG  . PHE   B 1  313 ? -1.186  22.972  36.908  1    23.912  ? 313  PHE   B CG  1 2 
ATOM   7479  C  CD1 . PHE   B 1  313 ? -1.248  24.351  36.652  1    23.507  ? 313  PHE   B CD1 1 2 
ATOM   7480  C  CD2 . PHE   B 1  313 ? -1.02   22.081  35.851  1    22.776  ? 313  PHE   B CD2 1 2 
ATOM   7481  C  CE1 . PHE   B 1  313 ? -1.153  24.831  35.362  1    22.765  ? 313  PHE   B CE1 1 2 
ATOM   7482  C  CE2 . PHE   B 1  313 ? -0.932  22.552  34.547  1    22.365  ? 313  PHE   B CE2 1 2 
ATOM   7483  C  CZ  . PHE   B 1  313 ? -0.981  23.929  34.299  1    22.713  ? 313  PHE   B CZ  1 2 
ATOM   7484  N  N   . TRP   B 1  314 ? 0.503   24.799  39.577  1    27.53   ? 314  TRP   B N   1 2 
ATOM   7485  C  CA  . TRP   B 1  314 ? 1.153   26.086  39.353  1    28.343  ? 314  TRP   B CA  1 2 
ATOM   7486  C  C   . TRP   B 1  314 ? 2.588   26.038  39.861  1    30.001  ? 314  TRP   B C   1 2 
ATOM   7487  O  O   . TRP   B 1  314 ? 3.492   26.641  39.287  1    29.163  ? 314  TRP   B O   1 2 
ATOM   7488  C  CB  . TRP   B 1  314 ? 0.371   27.255  39.99   1    28.479  ? 314  TRP   B CB  1 2 
ATOM   7489  C  CG  . TRP   B 1  314 ? -1.008  27.361  39.386  1    27.055  ? 314  TRP   B CG  1 2 
ATOM   7490  C  CD1 . TRP   B 1  314 ? -2.166  26.938  39.959  1    27.527  ? 314  TRP   B CD1 1 2 
ATOM   7491  C  CD2 . TRP   B 1  314 ? -1.363  27.808  38.05   1    26.08   ? 314  TRP   B CD2 1 2 
ATOM   7492  N  NE1 . TRP   B 1  314 ? -3.209  27.092  39.091  1    26.8    ? 314  TRP   B NE1 1 2 
ATOM   7493  C  CE2 . TRP   B 1  314 ? -2.756  27.616  37.911  1    25.7    ? 314  TRP   B CE2 1 2 
ATOM   7494  C  CE3 . TRP   B 1  314 ? -0.647  28.352  36.974  1    25.451  ? 314  TRP   B CE3 1 2 
ATOM   7495  C  CZ2 . TRP   B 1  314 ? -3.448  27.969  36.759  1    24.925  ? 314  TRP   B CZ2 1 2 
ATOM   7496  C  CZ3 . TRP   B 1  314 ? -1.33   28.694  35.815  1    25.074  ? 314  TRP   B CZ3 1 2 
ATOM   7497  C  CH2 . TRP   B 1  314 ? -2.712  28.497  35.709  1    24.276  ? 314  TRP   B CH2 1 2 
ATOM   7498  N  N   . GLU   B 1  315 ? 2.765   25.335  40.975  1    32.224  ? 315  GLU   B N   1 2 
ATOM   7499  C  CA  . GLU   B 1  315 ? 4.069   25.278  41.609  1    36.229  ? 315  GLU   B CA  1 2 
ATOM   7500  C  C   . GLU   B 1  315 ? 5.049   24.483  40.75   1    35.509  ? 315  GLU   B C   1 2 
ATOM   7501  O  O   . GLU   B 1  315 ? 6.224   24.805  40.706  1    38.476  ? 315  GLU   B O   1 2 
ATOM   7502  C  CB  . GLU   B 1  315 ? 3.953   24.659  43.003  1    40.675  ? 315  GLU   B CB  1 2 
ATOM   7503  C  CG  . GLU   B 1  315 ? 3.322   25.607  44.021  1    49.197  ? 315  GLU   B CG  1 2 
ATOM   7504  C  CD  . GLU   B 1  315 ? 3.708   27.086  43.908  1    55.173  ? 315  GLU   B CD  1 2 
ATOM   7505  O  OE1 . GLU   B 1  315 ? 4.917   27.38   44.099  1    57.888  ? 315  GLU   B OE1 1 2 
ATOM   7506  O  OE2 . GLU   B 1  315 ? 2.822   27.942  43.593  1    56.774  ? 315  GLU   B OE2 1 2 
ATOM   7507  N  N   . GLY   B 1  316 ? 4.566   23.481  40.017  1    33.5    ? 316  GLY   B N   1 2 
ATOM   7508  C  CA  . GLY   B 1  316 ? 5.487   22.486  39.507  1    33.185  ? 316  GLY   B CA  1 2 
ATOM   7509  C  C   . GLY   B 1  316 ? 5.606   22.492  37.983  1    32.035  ? 316  GLY   B C   1 2 
ATOM   7510  O  O   . GLY   B 1  316 ? 6.498   21.846  37.455  1    30.342  ? 316  GLY   B O   1 2 
ATOM   7511  N  N   . SER   B 1  317 ? 4.71    23.204  37.285  1    30.11   ? 317  SER   B N   1 2 
ATOM   7512  C  CA  . SER   B 1  317 ? 4.703   23.121  35.834  1    28.804  ? 317  SER   B CA  1 2 
ATOM   7513  C  C   . SER   B 1  317 ? 5.853   23.959  35.258  1    28.531  ? 317  SER   B C   1 2 
ATOM   7514  O  O   . SER   B 1  317 ? 6.313   24.884  35.888  1    28.083  ? 317  SER   B O   1 2 
ATOM   7515  C  CB  . SER   B 1  317 ? 3.388   23.602  35.261  1    27.709  ? 317  SER   B CB  1 2 
ATOM   7516  O  OG  . SER   B 1  317 ? 2.325   22.733  35.583  1    29.813  ? 317  SER   B OG  1 2 
ATOM   7517  N  N   . MET   B 1  318 ? 6.268   23.676  34.01   1    27.532  ? 318  MET   B N   1 2 
ATOM   7518  C  CA  . MET   B 1  318 ? 7.194   24.537  33.293  1    28.953  ? 318  MET   B CA  1 2 
ATOM   7519  C  C   . MET   B 1  318 ? 6.426   25.169  32.129  1    28.211  ? 318  MET   B C   1 2 
ATOM   7520  O  O   . MET   B 1  318 ? 6.094   24.47   31.155  1    25.564  ? 318  MET   B O   1 2 
ATOM   7521  C  CB  . MET   B 1  318 ? 8.361   23.693  32.755  1    30.442  ? 318  MET   B CB  1 2 
ATOM   7522  C  CG  . MET   B 1  318 ? 9.467   24.487  32.12   1    34.538  ? 318  MET   B CG  1 2 
ATOM   7523  S  SD  . MET   B 1  318 ? 10.488  23.4    31.085  1    40.431  ? 318  MET   B SD  1 2 
ATOM   7524  C  CE  . MET   B 1  318 ? 9.781   23.505  29.429  1    39.086  ? 318  MET   B CE  1 2 
ATOM   7525  N  N   . LEU   B 1  319 ? 6.146   26.483  32.237  1    28.947  ? 319  LEU   B N   1 2 
ATOM   7526  C  CA  . LEU   B 1  319 ? 5.194   27.142  31.341  1    29.02   ? 319  LEU   B CA  1 2 
ATOM   7527  C  C   . LEU   B 1  319 ? 5.949   28.018  30.333  1    30.055  ? 319  LEU   B C   1 2 
ATOM   7528  O  O   . LEU   B 1  319 ? 5.348   28.588  29.447  1    29.935  ? 319  LEU   B O   1 2 
ATOM   7529  C  CB  . LEU   B 1  319 ? 4.099   27.927  32.088  1    29.605  ? 319  LEU   B CB  1 2 
ATOM   7530  C  CG  . LEU   B 1  319 ? 3.33    27.215  33.214  1    29.04   ? 319  LEU   B CG  1 2 
ATOM   7531  C  CD1 . LEU   B 1  319 ? 2.387   28.178  33.947  1    33.539  ? 319  LEU   B CD1 1 2 
ATOM   7532  C  CD2 . LEU   B 1  319 ? 2.563   26.068  32.697  1    28.09   ? 319  LEU   B CD2 1 2 
ATOM   7533  N  N   . GLU   B 1  320 ? 7.275   28.128  30.464  1    31.358  ? 320  GLU   B N   1 2 
ATOM   7534  C  CA  . GLU   B 1  320 ? 8.104   28.895  29.545  1    34.241  ? 320  GLU   B CA  1 2 
ATOM   7535  C  C   . GLU   B 1  320 ? 9.422   28.128  29.319  1    34.531  ? 320  GLU   B C   1 2 
ATOM   7536  O  O   . GLU   B 1  320 ? 9.869   27.376  30.196  1    30.869  ? 320  GLU   B O   1 2 
ATOM   7537  C  CB  . GLU   B 1  320 ? 8.504   30.176  30.284  1    39.487  ? 320  GLU   B CB  1 2 
ATOM   7538  C  CG  . GLU   B 1  320 ? 7.615   31.387  30.032  1    44.3    ? 320  GLU   B CG  1 2 
ATOM   7539  C  CD  . GLU   B 1  320 ? 7.867   32.565  30.981  1    51.251  ? 320  GLU   B CD  1 2 
ATOM   7540  O  OE1 . GLU   B 1  320 ? 8.919   32.657  31.694  1    51.84   ? 320  GLU   B OE1 1 2 
ATOM   7541  O  OE2 . GLU   B 1  320 ? 6.938   33.411  31.031  1    49.3    ? 320  GLU   B OE2 1 2 
ATOM   7542  N  N   . LYS   B 1  321 ? 10.052  28.315  28.148  1    34.103  ? 321  LYS   B N   1 2 
ATOM   7543  C  CA  . LYS   B 1  321 ? 11.376  27.733  27.945  1    34.384  ? 321  LYS   B CA  1 2 
ATOM   7544  C  C   . LYS   B 1  321 ? 12.391  28.345  28.926  1    36.128  ? 321  LYS   B C   1 2 
ATOM   7545  O  O   . LYS   B 1  321 ? 12.535  29.565  29.003  1    37.853  ? 321  LYS   B O   1 2 
ATOM   7546  C  CB  . LYS   B 1  321 ? 11.808  27.926  26.497  1    36.713  ? 321  LYS   B CB  1 2 
ATOM   7547  C  CG  . LYS   B 1  321 ? 13.166  27.257  26.23   1    39.268  ? 321  LYS   B CG  1 2 
ATOM   7548  C  CD  . LYS   B 1  321 ? 13.445  27.137  24.737  1    45.169  ? 321  LYS   B CD  1 2 
ATOM   7549  C  CE  . LYS   B 1  321 ? 14.702  26.369  24.424  1    44.237  ? 321  LYS   B CE  1 2 
ATOM   7550  N  NZ  . LYS   B 1  321 ? 14.896  26.346  22.972  1    47.14   ? 321  LYS   B NZ  1 2 
ATOM   7551  N  N   . PRO   B 1  322 ? 13.107  27.534  29.738  1    36.598  ? 322  PRO   B N   1 2 
ATOM   7552  C  CA  . PRO   B 1  322 ? 14.037  28.066  30.747  1    42.682  ? 322  PRO   B CA  1 2 
ATOM   7553  C  C   . PRO   B 1  322 ? 15.165  28.862  30.108  1    45.683  ? 322  PRO   B C   1 2 
ATOM   7554  O  O   . PRO   B 1  322 ? 15.684  28.474  29.065  1    49.252  ? 322  PRO   B O   1 2 
ATOM   7555  C  CB  . PRO   B 1  322 ? 14.59   26.872  31.524  1    42.67   ? 322  PRO   B CB  1 2 
ATOM   7556  C  CG  . PRO   B 1  322 ? 13.965  25.652  30.897  1    38.277  ? 322  PRO   B CG  1 2 
ATOM   7557  C  CD  . PRO   B 1  322 ? 12.997  26.072  29.793  1    35.137  ? 322  PRO   B CD  1 2 
ATOM   7558  N  N   . ALA   B 1  323 ? 15.495  29.982  30.734  1    48.261  ? 323  ALA   B N   1 2 
ATOM   7559  C  CA  . ALA   B 1  323 ? 16.424  30.965  30.192  1    58.603  ? 323  ALA   B CA  1 2 
ATOM   7560  C  C   . ALA   B 1  323 ? 17.881  30.681  30.604  1    63.115  ? 323  ALA   B C   1 2 
ATOM   7561  O  O   . ALA   B 1  323 ? 18.776  31.479  30.32   1    60.81   ? 323  ALA   B O   1 2 
ATOM   7562  C  CB  . ALA   B 1  323 ? 15.976  32.363  30.616  1    55.626  ? 323  ALA   B CB  1 2 
ATOM   7563  N  N   . ASP   B 1  324 ? 18.135  29.521  31.229  1    70.05   ? 324  ASP   B N   1 2 
ATOM   7564  C  CA  . ASP   B 1  324 ? 19.388  29.294  31.938  1    76.14   ? 324  ASP   B CA  1 2 
ATOM   7565  C  C   . ASP   B 1  324 ? 20.304  28.347  31.168  1    81.152  ? 324  ASP   B C   1 2 
ATOM   7566  O  O   . ASP   B 1  324 ? 21.088  27.632  31.788  1    87.653  ? 324  ASP   B O   1 2 
ATOM   7567  C  CB  . ASP   B 1  324 ? 19.14   28.783  33.351  1    78.369  ? 324  ASP   B CB  1 2 
ATOM   7568  C  CG  . ASP   B 1  324 ? 18.181  27.605  33.459  1    83.044  ? 324  ASP   B CG  1 2 
ATOM   7569  O  OD1 . ASP   B 1  324 ? 17.887  26.973  32.412  1    78.328  ? 324  ASP   B OD1 1 2 
ATOM   7570  O  OD2 . ASP   B 1  324 ? 17.705  27.349  34.584  1    87.069  ? 324  ASP   B OD2 1 2 
ATOM   7571  N  N   . GLY   B 1  325 ? 20.218  28.371  29.83   1    82.167  ? 325  GLY   B N   1 2 
ATOM   7572  C  CA  . GLY   B 1  325 ? 20.975  27.466  28.977  1    81.554  ? 325  GLY   B CA  1 2 
ATOM   7573  C  C   . GLY   B 1  325 ? 20.801  26.012  29.416  1    76.364  ? 325  GLY   B C   1 2 
ATOM   7574  O  O   . GLY   B 1  325 ? 21.747  25.359  29.852  1    76.614  ? 325  GLY   B O   1 2 
ATOM   7575  N  N   . ARG   B 1  326 ? 19.568  25.519  29.333  1    63.551  ? 326  ARG   B N   1 2 
ATOM   7576  C  CA  . ARG   B 1  326 ? 19.309  24.152  29.743  1    57.646  ? 326  ARG   B CA  1 2 
ATOM   7577  C  C   . ARG   B 1  326 ? 18.494  23.5    28.628  1    54.156  ? 326  ARG   B C   1 2 
ATOM   7578  O  O   . ARG   B 1  326 ? 17.528  24.082  28.141  1    55.043  ? 326  ARG   B O   1 2 
ATOM   7579  C  CB  . ARG   B 1  326 ? 18.744  24.139  31.173  1    54.454  ? 326  ARG   B CB  1 2 
ATOM   7580  C  CG  . ARG   B 1  326 ? 18.102  22.815  31.554  1    53.302  ? 326  ARG   B CG  1 2 
ATOM   7581  C  CD  . ARG   B 1  326 ? 17.224  22.766  32.799  1    55.784  ? 326  ARG   B CD  1 2 
ATOM   7582  N  NE  . ARG   B 1  326 ? 16.616  24.028  33.236  1    58.55   ? 326  ARG   B NE  1 2 
ATOM   7583  C  CZ  . ARG   B 1  326 ? 15.516  24.183  33.969  1    56.112  ? 326  ARG   B CZ  1 2 
ATOM   7584  N  NH1 . ARG   B 1  326 ? 14.636  23.209  34.096  1    53.581  ? 326  ARG   B NH1 1 2 
ATOM   7585  N  NH2 . ARG   B 1  326 ? 15.245  25.359  34.498  1    56.02   ? 326  ARG   B NH2 1 2 
ATOM   7586  N  N   . GLU   B 1  327 ? 18.923  22.323  28.184  1    49.646  ? 327  GLU   B N   1 2 
ATOM   7587  C  CA  . GLU   B 1  327 ? 18.236  21.614  27.125  1    48.268  ? 327  GLU   B CA  1 2 
ATOM   7588  C  C   . GLU   B 1  327 ? 16.946  21.051  27.708  1    45.5    ? 327  GLU   B C   1 2 
ATOM   7589  O  O   . GLU   B 1  327 ? 16.964  20.473  28.801  1    45.302  ? 327  GLU   B O   1 2 
ATOM   7590  C  CB  . GLU   B 1  327 ? 19.189  20.568  26.54   1    51.749  ? 327  GLU   B CB  1 2 
ATOM   7591  C  CG  . GLU   B 1  327 ? 20.405  21.159  25.822  1    59.489  ? 327  GLU   B CG  1 2 
ATOM   7592  C  CD  . GLU   B 1  327 ? 20.279  21.522  24.34   1    69.376  ? 327  GLU   B CD  1 2 
ATOM   7593  O  OE1 . GLU   B 1  327 ? 21.344  21.76   23.721  1    70.968  ? 327  GLU   B OE1 1 2 
ATOM   7594  O  OE2 . GLU   B 1  327 ? 19.152  21.585  23.781  1    70.25   ? 327  GLU   B OE2 1 2 
ATOM   7595  N  N   . VAL   B 1  328 ? 15.823  21.312  27.019  1    37.166  ? 328  VAL   B N   1 2 
ATOM   7596  C  CA  . VAL   B 1  328 ? 14.537  20.776  27.426  1    35.296  ? 328  VAL   B CA  1 2 
ATOM   7597  C  C   . VAL   B 1  328 ? 13.885  20.188  26.184  1    30.986  ? 328  VAL   B C   1 2 
ATOM   7598  O  O   . VAL   B 1  328 ? 14.252  20.6    25.105  1    30.05   ? 328  VAL   B O   1 2 
ATOM   7599  C  CB  . VAL   B 1  328 ? 13.59   21.819  28.052  1    37.512  ? 328  VAL   B CB  1 2 
ATOM   7600  C  CG1 . VAL   B 1  328 ? 14.101  22.289  29.403  1    38.597  ? 328  VAL   B CG1 1 2 
ATOM   7601  C  CG2 . VAL   B 1  328 ? 13.351  23.005  27.119  1    41.265  ? 328  VAL   B CG2 1 2 
ATOM   7602  N  N   . VAL   B 1  329 ? 13.003  19.197  26.38   1    29.896  ? 329  VAL   B N   1 2 
ATOM   7603  C  CA  . VAL   B 1  329 ? 12.027  18.754  25.395  1    30.083  ? 329  VAL   B CA  1 2 
ATOM   7604  C  C   . VAL   B 1  329 ? 10.984  19.866  25.304  1    31.597  ? 329  VAL   B C   1 2 
ATOM   7605  O  O   . VAL   B 1  329 ? 10.216  20.07   26.253  1    30.273  ? 329  VAL   B O   1 2 
ATOM   7606  C  CB  . VAL   B 1  329 ? 11.31   17.445  25.769  1    27.928  ? 329  VAL   B CB  1 2 
ATOM   7607  C  CG1 . VAL   B 1  329 ? 10.299  17.052  24.696  1    25.581  ? 329  VAL   B CG1 1 2 
ATOM   7608  C  CG2 . VAL   B 1  329 ? 12.264  16.292  26.05   1    27.825  ? 329  VAL   B CG2 1 2 
ATOM   7609  N  N   . CYS   B 1  330 ? 10.978  20.555  24.162  1    31.083  ? 330  CYS   B N   1 2 
ATOM   7610  C  CA  . CYS   B 1  330 ? 10.094  21.689  23.989  1    34.477  ? 330  CYS   B CA  1 2 
ATOM   7611  C  C   . CYS   B 1  330 ? 8.659   21.254  23.72   1    33.04   ? 330  CYS   B C   1 2 
ATOM   7612  O  O   . CYS   B 1  330 ? 7.727   21.944  24.127  1    35.007  ? 330  CYS   B O   1 2 
ATOM   7613  C  CB  . CYS   B 1  330 ? 10.671  22.685  23      1    38.692  ? 330  CYS   B CB  1 2 
ATOM   7614  S  SG  . CYS   B 1  330 ? 11.708  23.906  23.858  1    52.14   ? 330  CYS   B SG  1 2 
ATOM   7615  N  N   . HIS   B 1  331 ? 8.495   20.118  23.052  1    28.109  ? 331  HIS   B N   1 2 
ATOM   7616  C  CA  . HIS   B 1  331 ? 7.184   19.715  22.573  1    24.204  ? 331  HIS   B CA  1 2 
ATOM   7617  C  C   . HIS   B 1  331 ? 6.223   19.737  23.751  1    22.87   ? 331  HIS   B C   1 2 
ATOM   7618  O  O   . HIS   B 1  331 ? 6.549   19.183  24.8    1    22.539  ? 331  HIS   B O   1 2 
ATOM   7619  C  CB  . HIS   B 1  331 ? 7.272   18.293  21.994  1    23.852  ? 331  HIS   B CB  1 2 
ATOM   7620  C  CG  . HIS   B 1  331 ? 6.02    17.936  21.32   1    25.353  ? 331  HIS   B CG  1 2 
ATOM   7621  N  ND1 . HIS   B 1  331 ? 5.727   18.191  19.989  1    31.204  ? 331  HIS   B ND1 1 2 
ATOM   7622  C  CD2 . HIS   B 1  331 ? 4.94    17.386  21.868  1    26.399  ? 331  HIS   B CD2 1 2 
ATOM   7623  C  CE1 . HIS   B 1  331 ? 4.478   17.829  19.781  1    29.966  ? 331  HIS   B CE1 1 2 
ATOM   7624  N  NE2 . HIS   B 1  331 ? 4.013   17.303  20.909  1    27.043  ? 331  HIS   B NE2 1 2 
ATOM   7625  N  N   . ALA   B 1  332 ? 5.062   20.419  23.618  1    19.592  ? 332  ALA   B N   1 2 
ATOM   7626  C  CA  . ALA   B 1  332 ? 4.164   20.633  24.768  1    19.866  ? 332  ALA   B CA  1 2 
ATOM   7627  C  C   . ALA   B 1  332 ? 3.6     19.293  25.249  1    20.057  ? 332  ALA   B C   1 2 
ATOM   7628  O  O   . ALA   B 1  332 ? 3.219   18.44   24.439  1    19.677  ? 332  ALA   B O   1 2 
ATOM   7629  C  CB  . ALA   B 1  332 ? 3.006   21.626  24.424  1    19.588  ? 332  ALA   B CB  1 2 
ATOM   7630  N  N   . SER   B 1  333 ? 3.456   19.129  26.575  1    19.993  ? 333  SER   B N   1 2 
ATOM   7631  C  CA  . SER   B 1  333 ? 2.914   17.88   27.088  1    20.918  ? 333  SER   B CA  1 2 
ATOM   7632  C  C   . SER   B 1  333 ? 2.346   18.023  28.514  1    20.101  ? 333  SER   B C   1 2 
ATOM   7633  O  O   . SER   B 1  333 ? 2.602   18.998  29.224  1    19.334  ? 333  SER   B O   1 2 
ATOM   7634  C  CB  . SER   B 1  333 ? 3.954   16.739  26.988  1    22.618  ? 333  SER   B CB  1 2 
ATOM   7635  O  OG  . SER   B 1  333 ? 5.067   17.035  27.797  1    23.735  ? 333  SER   B OG  1 2 
ATOM   7636  N  N   . ALA   B 1  334 ? 1.456   17.106  28.85   1    20.293  ? 334  ALA   B N   1 2 
ATOM   7637  C  CA  . ALA   B 1  334 ? 0.702   17.133  30.111  1    22.33   ? 334  ALA   B CA  1 2 
ATOM   7638  C  C   . ALA   B 1  334 ? 0.999   15.829  30.844  1    24.074  ? 334  ALA   B C   1 2 
ATOM   7639  O  O   . ALA   B 1  334 ? 0.954   14.8    30.222  1    23.087  ? 334  ALA   B O   1 2 
ATOM   7640  C  CB  . ALA   B 1  334 ? -0.793  17.248  29.883  1    19.668  ? 334  ALA   B CB  1 2 
ATOM   7641  N  N   . TRP   B 1  335 ? 1.158   15.896  32.172  1    26.001  ? 335  TRP   B N   1 2 
ATOM   7642  C  CA  . TRP   B 1  335 ? 1.802   14.864  32.98   1    28.179  ? 335  TRP   B CA  1 2 
ATOM   7643  C  C   . TRP   B 1  335 ? 0.936   14.508  34.182  1    29.893  ? 335  TRP   B C   1 2 
ATOM   7644  O  O   . TRP   B 1  335 ? 0.577   15.389  34.975  1    29.141  ? 335  TRP   B O   1 2 
ATOM   7645  C  CB  . TRP   B 1  335 ? 3.141   15.405  33.473  1    29.436  ? 335  TRP   B CB  1 2 
ATOM   7646  C  CG  . TRP   B 1  335 ? 4.136   15.623  32.369  1    32.676  ? 335  TRP   B CG  1 2 
ATOM   7647  C  CD1 . TRP   B 1  335 ? 4.12    16.555  31.358  1    32.193  ? 335  TRP   B CD1 1 2 
ATOM   7648  C  CD2 . TRP   B 1  335 ? 5.345   14.856  32.2    1    32.801  ? 335  TRP   B CD2 1 2 
ATOM   7649  N  NE1 . TRP   B 1  335 ? 5.226   16.393  30.56   1    33.101  ? 335  TRP   B NE1 1 2 
ATOM   7650  C  CE2 . TRP   B 1  335 ? 5.997   15.373  31.057  1    31.186  ? 335  TRP   B CE2 1 2 
ATOM   7651  C  CE3 . TRP   B 1  335 ? 5.933   13.806  32.929  1    33.567  ? 335  TRP   B CE3 1 2 
ATOM   7652  C  CZ2 . TRP   B 1  335 ? 7.22    14.873  30.627  1    32.112  ? 335  TRP   B CZ2 1 2 
ATOM   7653  C  CZ3 . TRP   B 1  335 ? 7.131   13.307  32.48   1    32.631  ? 335  TRP   B CZ3 1 2 
ATOM   7654  C  CH2 . TRP   B 1  335 ? 7.751   13.824  31.347  1    32.156  ? 335  TRP   B CH2 1 2 
ATOM   7655  N  N   . ASP   B 1  336 ? 0.556   13.22   34.273  1    31.091  ? 336  ASP   B N   1 2 
ATOM   7656  C  CA  . ASP   B 1  336 ? -0.125  12.636  35.427  1    31.515  ? 336  ASP   B CA  1 2 
ATOM   7657  C  C   . ASP   B 1  336 ? 0.886   11.784  36.19   1    34.438  ? 336  ASP   B C   1 2 
ATOM   7658  O  O   . ASP   B 1  336 ? 1.451   10.849  35.62   1    33.308  ? 336  ASP   B O   1 2 
ATOM   7659  C  CB  . ASP   B 1  336 ? -1.302  11.762  35.009  1    32.506  ? 336  ASP   B CB  1 2 
ATOM   7660  C  CG  . ASP   B 1  336 ? -2.18   11.205  36.132  1    34.645  ? 336  ASP   B CG  1 2 
ATOM   7661  O  OD1 . ASP   B 1  336 ? -1.787  11.298  37.306  1    34.059  ? 336  ASP   B OD1 1 2 
ATOM   7662  O  OD2 . ASP   B 1  336 ? -3.286  10.713  35.817  1    40.072  ? 336  ASP   B OD2 1 2 
ATOM   7663  N  N   . PHE   B 1  337 ? 1.131   12.119  37.47   1    34.437  ? 337  PHE   B N   1 2 
ATOM   7664  C  CA  . PHE   B 1  337 ? 2.155   11.395  38.213  1    36.46   ? 337  PHE   B CA  1 2 
ATOM   7665  C  C   . PHE   B 1  337 ? 1.547   10.222  38.988  1    36.727  ? 337  PHE   B C   1 2 
ATOM   7666  O  O   . PHE   B 1  337 ? 2.261   9.577   39.717  1    40.28   ? 337  PHE   B O   1 2 
ATOM   7667  C  CB  . PHE   B 1  337 ? 2.924   12.342  39.145  1    36.423  ? 337  PHE   B CB  1 2 
ATOM   7668  C  CG  . PHE   B 1  337 ? 3.921   13.277  38.481  1    33.847  ? 337  PHE   B CG  1 2 
ATOM   7669  C  CD1 . PHE   B 1  337 ? 3.491   14.337  37.674  1    32.184  ? 337  PHE   B CD1 1 2 
ATOM   7670  C  CD2 . PHE   B 1  337 ? 5.284   13.144  38.698  1    33.871  ? 337  PHE   B CD2 1 2 
ATOM   7671  C  CE1 . PHE   B 1  337 ? 4.407   15.196  37.091  1    30.925  ? 337  PHE   B CE1 1 2 
ATOM   7672  C  CE2 . PHE   B 1  337 ? 6.195   14.015  38.098  1    32.795  ? 337  PHE   B CE2 1 2 
ATOM   7673  C  CZ  . PHE   B 1  337 ? 5.76    15.044  37.294  1    31.202  ? 337  PHE   B CZ  1 2 
ATOM   7674  N  N   . TYR   B 1  338 ? 0.254   9.915   38.823  1    38.899  ? 338  TYR   B N   1 2 
ATOM   7675  C  CA  . TYR   B 1  338 ? -0.405  8.786   39.488  1    44.835  ? 338  TYR   B CA  1 2 
ATOM   7676  C  C   . TYR   B 1  338 ? -0.177  8.842   41.016  1    48.634  ? 338  TYR   B C   1 2 
ATOM   7677  O  O   . TYR   B 1  338 ? 0.248   7.848   41.601  1    47.838  ? 338  TYR   B O   1 2 
ATOM   7678  C  CB  . TYR   B 1  338 ? -0.027  7.411   38.882  1    45.065  ? 338  TYR   B CB  1 2 
ATOM   7679  C  CG  . TYR   B 1  338 ? -0.158  7.329   37.364  1    44.016  ? 338  TYR   B CG  1 2 
ATOM   7680  C  CD1 . TYR   B 1  338 ? -1.384  7.042   36.774  1    45.354  ? 338  TYR   B CD1 1 2 
ATOM   7681  C  CD2 . TYR   B 1  338 ? 0.913   7.591   36.524  1    45.407  ? 338  TYR   B CD2 1 2 
ATOM   7682  C  CE1 . TYR   B 1  338 ? -1.558  7.05    35.401  1    47.082  ? 338  TYR   B CE1 1 2 
ATOM   7683  C  CE2 . TYR   B 1  338 ? 0.763   7.581   35.145  1    44.319  ? 338  TYR   B CE2 1 2 
ATOM   7684  C  CZ  . TYR   B 1  338 ? -0.474  7.3     34.586  1    45.472  ? 338  TYR   B CZ  1 2 
ATOM   7685  O  OH  . TYR   B 1  338 ? -0.69   7.241   33.236  1    48.667  ? 338  TYR   B OH  1 2 
ATOM   7686  N  N   . ASN   B 1  339 ? -0.413  10.014  41.641  1    51.656  ? 339  ASN   B N   1 2 
ATOM   7687  C  CA  . ASN   B 1  339 ? -0.413  10.249  43.082  1    51.172  ? 339  ASN   B CA  1 2 
ATOM   7688  C  C   . ASN   B 1  339 ? -1.778  10.774  43.516  1    52.415  ? 339  ASN   B C   1 2 
ATOM   7689  O  O   . ASN   B 1  339 ? -2.022  10.966  44.712  1    48.482  ? 339  ASN   B O   1 2 
ATOM   7690  C  CB  . ASN   B 1  339 ? 0.189   11.614  43.418  1    56.206  ? 339  ASN   B CB  1 2 
ATOM   7691  C  CG  . ASN   B 1  339 ? 1.693   11.638  43.436  1    56.445  ? 339  ASN   B CG  1 2 
ATOM   7692  O  OD1 . ASN   B 1  339 ? 2.322   10.575  43.422  1    56.281  ? 339  ASN   B OD1 1 2 
ATOM   7693  N  ND2 . ASN   B 1  339 ? 2.28    12.825  43.443  1    51.405  ? 339  ASN   B ND2 1 2 
ATOM   7694  N  N   . ARG   B 1  340 ? -2.607  11.171  42.543  1    48.298  ? 340  ARG   B N   1 2 
ATOM   7695  C  CA  . ARG   B 1  340 ? -3.83   11.918  42.815  1    51.737  ? 340  ARG   B CA  1 2 
ATOM   7696  C  C   . ARG   B 1  340 ? -3.528  13.361  43.27   1    50.976  ? 340  ARG   B C   1 2 
ATOM   7697  O  O   . ARG   B 1  340 ? -4.462  14.09   43.592  1    55.244  ? 340  ARG   B O   1 2 
ATOM   7698  C  CB  . ARG   B 1  340 ? -4.76   11.167  43.787  1    53.732  ? 340  ARG   B CB  1 2 
ATOM   7699  C  CG  . ARG   B 1  340 ? -5.033  9.698   43.49   1    57.262  ? 340  ARG   B CG  1 2 
ATOM   7700  C  CD  . ARG   B 1  340 ? -6.2    9.075   44.251  1    59.562  ? 340  ARG   B CD  1 2 
ATOM   7701  N  NE  . ARG   B 1  340 ? -6.126  9.228   45.713  1    72.868  ? 340  ARG   B NE  1 2 
ATOM   7702  C  CZ  . ARG   B 1  340 ? -5.181  8.775   46.559  1    72.883  ? 340  ARG   B CZ  1 2 
ATOM   7703  N  NH1 . ARG   B 1  340 ? -4.127  8.084   46.134  1    73.836  ? 340  ARG   B NH1 1 2 
ATOM   7704  N  NH2 . ARG   B 1  340 ? -5.3    9.032   47.846  1    75.49   ? 340  ARG   B NH2 1 2 
ATOM   7705  N  N   . LYS   B 1  341 ? -2.246  13.777  43.257  1    48.073  ? 341  LYS   B N   1 2 
ATOM   7706  C  CA  . LYS   B 1  341 ? -1.772  15.051  43.782  1    49.493  ? 341  LYS   B CA  1 2 
ATOM   7707  C  C   . LYS   B 1  341 ? -1.003  15.858  42.73   1    46.545  ? 341  LYS   B C   1 2 
ATOM   7708  O  O   . LYS   B 1  341 ? -1.244  17.054  42.579  1    44.471  ? 341  LYS   B O   1 2 
ATOM   7709  C  CB  . LYS   B 1  341 ? -0.779  14.879  44.941  1    54.229  ? 341  LYS   B CB  1 2 
ATOM   7710  C  CG  . LYS   B 1  341 ? -1.324  14.501  46.319  1    61.428  ? 341  LYS   B CG  1 2 
ATOM   7711  C  CD  . LYS   B 1  341 ? -0.166  14.104  47.242  1    67.481  ? 341  LYS   B CD  1 2 
ATOM   7712  C  CE  . LYS   B 1  341 ? -0.376  14.208  48.736  1    68.566  ? 341  LYS   B CE  1 2 
ATOM   7713  N  NZ  . LYS   B 1  341 ? -0.546  12.933  49.436  1    68.315  ? 341  LYS   B NZ  1 2 
ATOM   7714  N  N   . ASP   B 1  342 ? -0.025  15.236  42.057  1    42.136  ? 342  ASP   B N   1 2 
ATOM   7715  C  CA  . ASP   B 1  342 ? 0.812   15.989  41.135  1    40.562  ? 342  ASP   B CA  1 2 
ATOM   7716  C  C   . ASP   B 1  342 ? 0.352   15.853  39.677  1    37.131  ? 342  ASP   B C   1 2 
ATOM   7717  O  O   . ASP   B 1  342 ? 0.282   14.746  39.132  1    35.151  ? 342  ASP   B O   1 2 
ATOM   7718  C  CB  . ASP   B 1  342 ? 2.289   15.707  41.306  1    41.649  ? 342  ASP   B CB  1 2 
ATOM   7719  C  CG  . ASP   B 1  342 ? 2.838   16.143  42.648  1    47.115  ? 342  ASP   B CG  1 2 
ATOM   7720  O  OD1 . ASP   B 1  342 ? 2.75    15.33   43.595  1    46.044  ? 342  ASP   B OD1 1 2 
ATOM   7721  O  OD2 . ASP   B 1  342 ? 3.287   17.31   42.721  1    48.737  ? 342  ASP   B OD2 1 2 
ATOM   7722  N  N   . PHE   B 1  343 ? 0.125   17.018  39.048  1    33.882  ? 343  PHE   B N   1 2 
ATOM   7723  C  CA  . PHE   B 1  343 ? -0.295  17.154  37.658  1    31.97   ? 343  PHE   B CA  1 2 
ATOM   7724  C  C   . PHE   B 1  343 ? 0.358   18.407  37.083  1    29.843  ? 343  PHE   B C   1 2 
ATOM   7725  O  O   . PHE   B 1  343 ? 0.383   19.439  37.754  1    28.59   ? 343  PHE   B O   1 2 
ATOM   7726  C  CB  . PHE   B 1  343 ? -1.797  17.405  37.631  1    33.01   ? 343  PHE   B CB  1 2 
ATOM   7727  C  CG  . PHE   B 1  343 ? -2.597  16.382  38.414  1    34.268  ? 343  PHE   B CG  1 2 
ATOM   7728  C  CD1 . PHE   B 1  343 ? -2.92   15.147  37.855  1    33.78   ? 343  PHE   B CD1 1 2 
ATOM   7729  C  CD2 . PHE   B 1  343 ? -3.02   16.649  39.715  1    36.984  ? 343  PHE   B CD2 1 2 
ATOM   7730  C  CE1 . PHE   B 1  343 ? -3.649  14.199  38.566  1    35.354  ? 343  PHE   B CE1 1 2 
ATOM   7731  C  CE2 . PHE   B 1  343 ? -3.749  15.698  40.431  1    37.592  ? 343  PHE   B CE2 1 2 
ATOM   7732  C  CZ  . PHE   B 1  343 ? -4.065  14.475  39.853  1    36.267  ? 343  PHE   B CZ  1 2 
ATOM   7733  N  N   . ARG   B 1  344 ? 0.968   18.308  35.889  1    27.236  ? 344  ARG   B N   1 2 
ATOM   7734  C  CA  . ARG   B 1  344 ? 1.801   19.403  35.446  1    25.337  ? 344  ARG   B CA  1 2 
ATOM   7735  C  C   . ARG   B 1  344 ? 1.785   19.489  33.931  1    24.445  ? 344  ARG   B C   1 2 
ATOM   7736  O  O   . ARG   B 1  344 ? 1.481   18.511  33.259  1    24.39   ? 344  ARG   B O   1 2 
ATOM   7737  C  CB  . ARG   B 1  344 ? 3.271   19.186  35.799  1    26.481  ? 344  ARG   B CB  1 2 
ATOM   7738  C  CG  . ARG   B 1  344 ? 3.566   19.132  37.291  1    27.599  ? 344  ARG   B CG  1 2 
ATOM   7739  C  CD  . ARG   B 1  344 ? 5.035   18.838  37.498  1    28.695  ? 344  ARG   B CD  1 2 
ATOM   7740  N  NE  . ARG   B 1  344 ? 5.226   18.779  38.961  1    30.753  ? 344  ARG   B NE  1 2 
ATOM   7741  C  CZ  . ARG   B 1  344 ? 6.381   18.574  39.571  1    32.706  ? 344  ARG   B CZ  1 2 
ATOM   7742  N  NH1 . ARG   B 1  344 ? 7.427   18.345  38.806  1    32.413  ? 344  ARG   B NH1 1 2 
ATOM   7743  N  NH2 . ARG   B 1  344 ? 6.468   18.537  40.912  1    32.703  ? 344  ARG   B NH2 1 2 
ATOM   7744  N  N   . ILE   B 1  345 ? 2.134   20.667  33.425  1    24.389  ? 345  ILE   B N   1 2 
ATOM   7745  C  CA  . ILE   B 1  345 ? 2.306   20.848  31.991  1    22.463  ? 345  ILE   B CA  1 2 
ATOM   7746  C  C   . ILE   B 1  345 ? 3.743   21.319  31.79   1    22.831  ? 345  ILE   B C   1 2 
ATOM   7747  O  O   . ILE   B 1  345 ? 4.249   22.058  32.612  1    23.033  ? 345  ILE   B O   1 2 
ATOM   7748  C  CB  . ILE   B 1  345 ? 1.295   21.865  31.434  1    20.973  ? 345  ILE   B CB  1 2 
ATOM   7749  C  CG1 . ILE   B 1  345 ? -0.096  21.195  31.258  1    20.545  ? 345  ILE   B CG1 1 2 
ATOM   7750  C  CG2 . ILE   B 1  345 ? 1.791   22.478  30.102  1    19.511  ? 345  ILE   B CG2 1 2 
ATOM   7751  C  CD1 . ILE   B 1  345 ? -1.218  22.185  30.959  1    18.98   ? 345  ILE   B CD1 1 2 
ATOM   7752  N  N   . LYS   B 1  346 ? 4.371   20.85   30.712  1    22.506  ? 346  LYS   B N   1 2 
ATOM   7753  C  CA  . LYS   B 1  346 ? 5.68    21.314  30.306  1    24.679  ? 346  LYS   B CA  1 2 
ATOM   7754  C  C   . LYS   B 1  346 ? 5.476   21.897  28.912  1    23.147  ? 346  LYS   B C   1 2 
ATOM   7755  O  O   . LYS   B 1  346 ? 5.246   21.124  27.981  1    23.346  ? 346  LYS   B O   1 2 
ATOM   7756  C  CB  . LYS   B 1  346 ? 6.676   20.125  30.342  1    25.019  ? 346  LYS   B CB  1 2 
ATOM   7757  C  CG  . LYS   B 1  346 ? 7.997   20.438  29.701  1    25.886  ? 346  LYS   B CG  1 2 
ATOM   7758  C  CD  . LYS   B 1  346 ? 8.806   19.161  29.449  1    26.567  ? 346  LYS   B CD  1 2 
ATOM   7759  C  CE  . LYS   B 1  346 ? 8.244   18.273  28.353  1    28.169  ? 346  LYS   B CE  1 2 
ATOM   7760  N  NZ  . LYS   B 1  346 ? 8.033   19.145  27.197  1    27.119  ? 346  LYS   B NZ  1 2 
ATOM   7761  N  N   . GLN   B 1  347 ? 5.528   23.232  28.783  1    22.326  ? 347  GLN   B N   1 2 
ATOM   7762  C  CA  . GLN   B 1  347 ? 5.259   23.857  27.48   1    23.279  ? 347  GLN   B CA  1 2 
ATOM   7763  C  C   . GLN   B 1  347 ? 6.229   25.009  27.31   1    24.916  ? 347  GLN   B C   1 2 
ATOM   7764  O  O   . GLN   B 1  347 ? 6.413   25.79   28.264  1    25.164  ? 347  GLN   B O   1 2 
ATOM   7765  C  CB  . GLN   B 1  347 ? 3.774   24.247  27.31   1    21.573  ? 347  GLN   B CB  1 2 
ATOM   7766  C  CG  . GLN   B 1  347 ? 3.484   24.946  25.984  1    21.877  ? 347  GLN   B CG  1 2 
ATOM   7767  C  CD  . GLN   B 1  347 ? 2.003   25.183  25.769  1    22.806  ? 347  GLN   B CD  1 2 
ATOM   7768  O  OE1 . GLN   B 1  347 ? 1.152   24.619  26.472  1    21.394  ? 347  GLN   B OE1 1 2 
ATOM   7769  N  NE2 . GLN   B 1  347 ? 1.703   25.981  24.757  1    22.724  ? 347  GLN   B NE2 1 2 
ATOM   7770  N  N   . CYS   B 1  348 ? 6.885   25.087  26.132  1    23.25   ? 348  CYS   B N   1 2 
ATOM   7771  C  CA  . CYS   B 1  348 ? 7.738   26.239  25.864  1    25.035  ? 348  CYS   B CA  1 2 
ATOM   7772  C  C   . CYS   B 1  348 ? 6.888   27.348  25.261  1    25.245  ? 348  CYS   B C   1 2 
ATOM   7773  O  O   . CYS   B 1  348 ? 7.013   27.704  24.075  1    24.115  ? 348  CYS   B O   1 2 
ATOM   7774  C  CB  . CYS   B 1  348 ? 8.928   25.895  24.973  1    26.619  ? 348  CYS   B CB  1 2 
ATOM   7775  S  SG  . CYS   B 1  348 ? 10.029  24.764  25.882  1    30.18   ? 348  CYS   B SG  1 2 
ATOM   7776  N  N   . THR   B 1  349 ? 5.965   27.844  26.084  1    25.469  ? 349  THR   B N   1 2 
ATOM   7777  C  CA  . THR   B 1  349 ? 4.82    28.609  25.583  1    25.684  ? 349  THR   B CA  1 2 
ATOM   7778  C  C   . THR   B 1  349 ? 5.321   29.879  24.909  1    24.241  ? 349  THR   B C   1 2 
ATOM   7779  O  O   . THR   B 1  349 ? 6.032   30.619  25.544  1    25.282  ? 349  THR   B O   1 2 
ATOM   7780  C  CB  . THR   B 1  349 ? 3.918   29.059  26.745  1    25.396  ? 349  THR   B CB  1 2 
ATOM   7781  O  OG1 . THR   B 1  349 ? 3.654   27.879  27.493  1    24.204  ? 349  THR   B OG1 1 2 
ATOM   7782  C  CG2 . THR   B 1  349 ? 2.628   29.711  26.258  1    26.202  ? 349  THR   B CG2 1 2 
ATOM   7783  N  N   . ARG   B 1  350 ? 4.818   30.151  23.695  1    23.207  ? 350  ARG   B N   1 2 
ATOM   7784  C  CA  . ARG   B 1  350 ? 4.937   31.423  23.005  1    25.489  ? 350  ARG   B CA  1 2 
ATOM   7785  C  C   . ARG   B 1  350 ? 3.598   32.181  22.992  1    24.273  ? 350  ARG   B C   1 2 
ATOM   7786  O  O   . ARG   B 1  350 ? 2.558   31.582  23.064  1    22.838  ? 350  ARG   B O   1 2 
ATOM   7787  C  CB  . ARG   B 1  350 ? 5.359   31.097  21.564  1    23.731  ? 350  ARG   B CB  1 2 
ATOM   7788  C  CG  . ARG   B 1  350 ? 6.825   30.674  21.566  1    27.467  ? 350  ARG   B CG  1 2 
ATOM   7789  C  CD  . ARG   B 1  350 ? 7.334   30.173  20.199  1    28.063  ? 350  ARG   B CD  1 2 
ATOM   7790  N  NE  . ARG   B 1  350 ? 6.712   28.927  19.716  1    30.549  ? 350  ARG   B NE  1 2 
ATOM   7791  C  CZ  . ARG   B 1  350 ? 5.673   28.908  18.891  1    28.447  ? 350  ARG   B CZ  1 2 
ATOM   7792  N  NH1 . ARG   B 1  350 ? 5.265   30.028  18.308  1    33.069  ? 350  ARG   B NH1 1 2 
ATOM   7793  N  NH2 . ARG   B 1  350 ? 4.998   27.807  18.694  1    26.963  ? 350  ARG   B NH2 1 2 
ATOM   7794  N  N   . VAL   B 1  351 ? 3.627   33.509  22.843  1    26.158  ? 351  VAL   B N   1 2 
ATOM   7795  C  CA  . VAL   B 1  351 ? 2.404   34.299  22.81   1    26.919  ? 351  VAL   B CA  1 2 
ATOM   7796  C  C   . VAL   B 1  351 ? 1.867   34.413  21.38   1    26.816  ? 351  VAL   B C   1 2 
ATOM   7797  O  O   . VAL   B 1  351 ? 2.16    35.366  20.654  1    26.298  ? 351  VAL   B O   1 2 
ATOM   7798  C  CB  . VAL   B 1  351 ? 2.645   35.665  23.455  1    29.518  ? 351  VAL   B CB  1 2 
ATOM   7799  C  CG1 . VAL   B 1  351 ? 1.366   36.509  23.43   1    30.27   ? 351  VAL   B CG1 1 2 
ATOM   7800  C  CG2 . VAL   B 1  351 ? 3.159   35.53   24.899  1    28.674  ? 351  VAL   B CG2 1 2 
ATOM   7801  N  N   . THR   B 1  352 ? 1.038   33.444  20.988  1    24.722  ? 352  THR   B N   1 2 
ATOM   7802  C  CA  . THR   B 1  352 ? 0.391   33.422  19.684  1    24.691  ? 352  THR   B CA  1 2 
ATOM   7803  C  C   . THR   B 1  352 ? -1.011  32.856  19.877  1    23.301  ? 352  THR   B C   1 2 
ATOM   7804  O  O   . THR   B 1  352 ? -1.264  32.176  20.877  1    23.983  ? 352  THR   B O   1 2 
ATOM   7805  C  CB  . THR   B 1  352 ? 1.186   32.647  18.614  1    25.683  ? 352  THR   B CB  1 2 
ATOM   7806  O  OG1 . THR   B 1  352 ? 1.101   31.281  19.013  1    24.134  ? 352  THR   B OG1 1 2 
ATOM   7807  C  CG2 . THR   B 1  352 ? 2.646   33.048  18.441  1    24.384  ? 352  THR   B CG2 1 2 
ATOM   7808  N  N   . MET   B 1  353 ? -1.928  33.14   18.937  1    23.53   ? 353  MET   B N   1 2 
ATOM   7809  C  CA  . MET   B 1  353 ? -3.251  32.536  18.961  1    25.666  ? 353  MET   B CA  1 2 
ATOM   7810  C  C   . MET   B 1  353 ? -3.182  30.987  18.877  1    25.274  ? 353  MET   B C   1 2 
ATOM   7811  O  O   . MET   B 1  353 ? -3.912  30.293  19.58   1    25.043  ? 353  MET   B O   1 2 
ATOM   7812  C  CB  . MET   B 1  353 ? -4.151  33.125  17.867  1    27.996  ? 353  MET   B CB  1 2 
ATOM   7813  C  CG  . MET   B 1  353 ? -5.601  32.622  17.948  1    31.571  ? 353  MET   B CG  1 2 
ATOM   7814  S  SD  . MET   B 1  353 ? -6.557  33.327  16.574  1    35.864  ? 353  MET   B SD  1 2 
ATOM   7815  C  CE  . MET   B 1  353 ? -8.212  32.837  17.108  1    37.234  ? 353  MET   B CE  1 2 
ATOM   7816  N  N   . ASP   B 1  354 ? -2.257  30.404  18.097  1    25.852  ? 354  ASP   B N   1 2 
ATOM   7817  C  CA  . ASP   B 1  354 ? -2.189  28.935  17.999  1    27.241  ? 354  ASP   B CA  1 2 
ATOM   7818  C  C   . ASP   B 1  354 ? -1.676  28.294  19.306  1    24.066  ? 354  ASP   B C   1 2 
ATOM   7819  O  O   . ASP   B 1  354 ? -2.079  27.199  19.677  1    21.739  ? 354  ASP   B O   1 2 
ATOM   7820  C  CB  . ASP   B 1  354 ? -1.386  28.446  16.801  1    34.906  ? 354  ASP   B CB  1 2 
ATOM   7821  C  CG  . ASP   B 1  354 ? 0.131   28.671  16.884  1    52.848  ? 354  ASP   B CG  1 2 
ATOM   7822  O  OD1 . ASP   B 1  354 ? 0.589   29.825  16.609  1    50.838  ? 354  ASP   B OD1 1 2 
ATOM   7823  O  OD2 . ASP   B 1  354 ? 0.875   27.7    17.249  1    53.256  ? 354  ASP   B OD2 1 2 
ATOM   7824  N  N   . GLN   B 1  355 ? -0.771  28.976  20.006  1    22.795  ? 355  GLN   B N   1 2 
ATOM   7825  C  CA  . GLN   B 1  355 ? -0.31   28.512  21.301  1    21.93   ? 355  GLN   B CA  1 2 
ATOM   7826  C  C   . GLN   B 1  355 ? -1.432  28.564  22.331  1    20.597  ? 355  GLN   B C   1 2 
ATOM   7827  O  O   . GLN   B 1  355 ? -1.469  27.737  23.23   1    19.954  ? 355  GLN   B O   1 2 
ATOM   7828  C  CB  . GLN   B 1  355 ? 0.906   29.345  21.711  1    22.124  ? 355  GLN   B CB  1 2 
ATOM   7829  C  CG  . GLN   B 1  355 ? 2.155   28.866  20.968  1    23.517  ? 355  GLN   B CG  1 2 
ATOM   7830  C  CD  . GLN   B 1  355 ? 2.81    27.709  21.689  1    22.851  ? 355  GLN   B CD  1 2 
ATOM   7831  O  OE1 . GLN   B 1  355 ? 3.372   27.885  22.77   1    22.809  ? 355  GLN   B OE1 1 2 
ATOM   7832  N  NE2 . GLN   B 1  355 ? 2.588   26.511  21.175  1    20.547  ? 355  GLN   B NE2 1 2 
ATOM   7833  N  N   . LEU   B 1  356 ? -2.302  29.6    22.264  1    21.969  ? 356  LEU   B N   1 2 
ATOM   7834  C  CA  . LEU   B 1  356 ? -3.459  29.65   23.139  1    20.77   ? 356  LEU   B CA  1 2 
ATOM   7835  C  C   . LEU   B 1  356 ? -4.32   28.389  22.99   1    19.609  ? 356  LEU   B C   1 2 
ATOM   7836  O  O   . LEU   B 1  356 ? -4.765  27.785  23.994  1    19.712  ? 356  LEU   B O   1 2 
ATOM   7837  C  CB  . LEU   B 1  356 ? -4.261  30.942  22.953  1    21.856  ? 356  LEU   B CB  1 2 
ATOM   7838  C  CG  . LEU   B 1  356 ? -5.434  31.105  23.914  1    22.954  ? 356  LEU   B CG  1 2 
ATOM   7839  C  CD1 . LEU   B 1  356 ? -4.982  31.097  25.383  1    24.258  ? 356  LEU   B CD1 1 2 
ATOM   7840  C  CD2 . LEU   B 1  356 ? -6.017  32.475  23.504  1    24.755  ? 356  LEU   B CD2 1 2 
ATOM   7841  N  N   A SER   B 1  357 ? -4.556  27.979  21.745  0.75 18.405  ? 357  SER   B N   1 2 
ATOM   7842  N  N   B SER   B 1  357 ? -4.495  27.954  21.734  0.25 18.775  ? 357  SER   B N   1 2 
ATOM   7843  C  CA  A SER   B 1  357 ? -5.15   26.687  21.471  0.75 19.111  ? 357  SER   B CA  1 2 
ATOM   7844  C  CA  B SER   B 1  357 ? -5.123  26.681  21.423  0.25 18.567  ? 357  SER   B CA  1 2 
ATOM   7845  C  C   A SER   B 1  357 ? -4.352  25.514  22.053  0.75 17.703  ? 357  SER   B C   1 2 
ATOM   7846  C  C   B SER   B 1  357 ? -4.354  25.519  22.05   0.25 17.68   ? 357  SER   B C   1 2 
ATOM   7847  O  O   A SER   B 1  357 ? -4.94   24.615  22.647  0.75 18.033  ? 357  SER   B O   1 2 
ATOM   7848  O  O   B SER   B 1  357 ? -4.963  24.637  22.651  0.25 17.795  ? 357  SER   B O   1 2 
ATOM   7849  C  CB  A SER   B 1  357 ? -5.384  26.522  19.949  0.75 19.97   ? 357  SER   B CB  1 2 
ATOM   7850  C  CB  B SER   B 1  357 ? -5.27   26.459  19.922  0.25 18.522  ? 357  SER   B CB  1 2 
ATOM   7851  O  OG  A SER   B 1  357 ? -6.448  27.421  19.618  0.75 20.751  ? 357  SER   B OG  1 2 
ATOM   7852  O  OG  B SER   B 1  357 ? -6.411  25.644  19.682  0.25 18.933  ? 357  SER   B OG  1 2 
ATOM   7853  N  N   . THR   B 1  358 ? -3.023  25.511  21.885  1    16.979  ? 358  THR   B N   1 2 
ATOM   7854  C  CA  . THR   B 1  358 ? -2.226  24.445  22.465  1    17.386  ? 358  THR   B CA  1 2 
ATOM   7855  C  C   . THR   B 1  358 ? -2.425  24.418  23.989  1    16.76   ? 358  THR   B C   1 2 
ATOM   7856  O  O   . THR   B 1  358 ? -2.409  23.366  24.596  1    16.387  ? 358  THR   B O   1 2 
ATOM   7857  C  CB  . THR   B 1  358 ? -0.733  24.587  22.137  1    20.477  ? 358  THR   B CB  1 2 
ATOM   7858  O  OG1 . THR   B 1  358 ? -0.701  24.373  20.726  1    19.47   ? 358  THR   B OG1 1 2 
ATOM   7859  C  CG2 . THR   B 1  358 ? 0.072   23.419  22.708  1    21.944  ? 358  THR   B CG2 1 2 
ATOM   7860  N  N   . VAL   B 1  359 ? -2.413  25.579  24.636  1    16.163  ? 359  VAL   B N   1 2 
ATOM   7861  C  CA  . VAL   B 1  359 ? -2.614  25.601  26.083  1    17.426  ? 359  VAL   B CA  1 2 
ATOM   7862  C  C   . VAL   B 1  359 ? -3.935  24.94   26.491  1    17.279  ? 359  VAL   B C   1 2 
ATOM   7863  O  O   . VAL   B 1  359 ? -3.962  24.144  27.429  1    17.157  ? 359  VAL   B O   1 2 
ATOM   7864  C  CB  . VAL   B 1  359 ? -2.529  27.069  26.537  1    17.188  ? 359  VAL   B CB  1 2 
ATOM   7865  C  CG1 . VAL   B 1  359 ? -3.026  27.259  27.969  1    18.564  ? 359  VAL   B CG1 1 2 
ATOM   7866  C  CG2 . VAL   B 1  359 ? -1.044  27.511  26.481  1    18.238  ? 359  VAL   B CG2 1 2 
ATOM   7867  N  N   . HIS   B 1  360 ? -5.008  25.211  25.729  1    16.2    ? 360  HIS   B N   1 2 
ATOM   7868  C  CA  . HIS   B 1  360 ? -6.287  24.561  25.985  1    17.68   ? 360  HIS   B CA  1 2 
ATOM   7869  C  C   . HIS   B 1  360 ? -6.188  23.056  25.753  1    17.144  ? 360  HIS   B C   1 2 
ATOM   7870  O  O   . HIS   B 1  360 ? -6.675  22.281  26.56   1    17.681  ? 360  HIS   B O   1 2 
ATOM   7871  C  CB  . HIS   B 1  360 ? -7.406  25.124  25.095  1    17.015  ? 360  HIS   B CB  1 2 
ATOM   7872  C  CG  . HIS   B 1  360 ? -7.907  26.441  25.591  1    17.692  ? 360  HIS   B CG  1 2 
ATOM   7873  N  ND1 . HIS   B 1  360 ? -7.193  27.597  25.388  1    18.058  ? 360  HIS   B ND1 1 2 
ATOM   7874  C  CD2 . HIS   B 1  360 ? -8.978  26.781  26.355  1    18.572  ? 360  HIS   B CD2 1 2 
ATOM   7875  C  CE1 . HIS   B 1  360 ? -7.838  28.608  25.923  1    18.748  ? 360  HIS   B CE1 1 2 
ATOM   7876  N  NE2 . HIS   B 1  360 ? -8.929  28.133  26.53   1    18.839  ? 360  HIS   B NE2 1 2 
ATOM   7877  N  N   . HIS   B 1  361 ? -5.483  22.654  24.699  1    18.32   ? 361  HIS   B N   1 2 
ATOM   7878  C  CA  . HIS   B 1  361 ? -5.326  21.222  24.41   1    17.643  ? 361  HIS   B CA  1 2 
ATOM   7879  C  C   . HIS   B 1  361 ? -4.652  20.553  25.613  1    17.763  ? 361  HIS   B C   1 2 
ATOM   7880  O  O   . HIS   B 1  361 ? -5.156  19.526  26.108  1    18.362  ? 361  HIS   B O   1 2 
ATOM   7881  C  CB  . HIS   B 1  361 ? -4.476  21.022  23.145  1    17.742  ? 361  HIS   B CB  1 2 
ATOM   7882  C  CG  . HIS   B 1  361 ? -4.134  19.577  22.874  1    16.552  ? 361  HIS   B CG  1 2 
ATOM   7883  N  ND1 . HIS   B 1  361 ? -4.902  18.778  22.055  1    17.382  ? 361  HIS   B ND1 1 2 
ATOM   7884  C  CD2 . HIS   B 1  361 ? -3.138  18.798  23.332  1    17.399  ? 361  HIS   B CD2 1 2 
ATOM   7885  C  CE1 . HIS   B 1  361 ? -4.415  17.528  22.041  1    17.7    ? 361  HIS   B CE1 1 2 
ATOM   7886  N  NE2 . HIS   B 1  361 ? -3.347  17.517  22.847  1    18.234  ? 361  HIS   B NE2 1 2 
ATOM   7887  N  N   . GLU   B 1  362 ? -3.549  21.153  26.102  1    17.934  ? 362  GLU   B N   1 2 
ATOM   7888  C  CA  . GLU   B 1  362 ? -2.802  20.541  27.202  1    19.408  ? 362  GLU   B CA  1 2 
ATOM   7889  C  C   . GLU   B 1  362 ? -3.641  20.519  28.484  1    20.04   ? 362  GLU   B C   1 2 
ATOM   7890  O  O   . GLU   B 1  362 ? -3.593  19.55   29.246  1    20.076  ? 362  GLU   B O   1 2 
ATOM   7891  C  CB  . GLU   B 1  362 ? -1.419  21.135  27.506  1    20.99   ? 362  GLU   B CB  1 2 
ATOM   7892  C  CG  . GLU   B 1  362 ? -0.474  21.086  26.304  1    22.402  ? 362  GLU   B CG  1 2 
ATOM   7893  C  CD  . GLU   B 1  362 ? -0.241  19.691  25.718  1    24.243  ? 362  GLU   B CD  1 2 
ATOM   7894  O  OE1 . GLU   B 1  362 ? -0.136  18.762  26.514  1    24.444  ? 362  GLU   B OE1 1 2 
ATOM   7895  O  OE2 . GLU   B 1  362 ? -0.149  19.507  24.509  1    24.608  ? 362  GLU   B OE2 1 2 
ATOM   7896  N  N   . MET   B 1  363 ? -4.347  21.626  28.768  1    18.469  ? 363  MET   B N   1 2 
ATOM   7897  C  CA  . MET   B 1  363 ? -5.132  21.687  29.992  1    20.073  ? 363  MET   B CA  1 2 
ATOM   7898  C  C   . MET   B 1  363 ? -6.31   20.708  29.938  1    19.648  ? 363  MET   B C   1 2 
ATOM   7899  O  O   . MET   B 1  363 ? -6.794  20.3    30.998  1    19.955  ? 363  MET   B O   1 2 
ATOM   7900  C  CB  . MET   B 1  363 ? -5.623  23.133  30.229  1    20.735  ? 363  MET   B CB  1 2 
ATOM   7901  C  CG  . MET   B 1  363 ? -6.308  23.353  31.588  1    24.524  ? 363  MET   B CG  1 2 
ATOM   7902  S  SD  . MET   B 1  363 ? -6.405  25.094  32.102  1    26.576  ? 363  MET   B SD  1 2 
ATOM   7903  C  CE  . MET   B 1  363 ? -4.631  25.426  32.207  1    27.341  ? 363  MET   B CE  1 2 
ATOM   7904  N  N   . GLY   B 1  364 ? -6.774  20.361  28.713  1    19.284  ? 364  GLY   B N   1 2 
ATOM   7905  C  CA  . GLY   B 1  364 ? -7.771  19.323  28.487  1    19.795  ? 364  GLY   B CA  1 2 
ATOM   7906  C  C   . GLY   B 1  364 ? -7.266  18.014  29.111  1    22.033  ? 364  GLY   B C   1 2 
ATOM   7907  O  O   . GLY   B 1  364 ? -8.019  17.313  29.777  1    22.032  ? 364  GLY   B O   1 2 
ATOM   7908  N  N   . HIS   B 1  365 ? -5.97   17.709  28.917  1    20.372  ? 365  HIS   B N   1 2 
ATOM   7909  C  CA  . HIS   B 1  365 ? -5.408  16.466  29.449  1    21.228  ? 365  HIS   B CA  1 2 
ATOM   7910  C  C   . HIS   B 1  365 ? -5.4    16.534  30.966  1    22.227  ? 365  HIS   B C   1 2 
ATOM   7911  O  O   . HIS   B 1  365 ? -5.741  15.553  31.637  1    23.084  ? 365  HIS   B O   1 2 
ATOM   7912  C  CB  . HIS   B 1  365 ? -3.962  16.199  28.972  1    20.436  ? 365  HIS   B CB  1 2 
ATOM   7913  C  CG  . HIS   B 1  365 ? -3.783  15.854  27.508  1    21.191  ? 365  HIS   B CG  1 2 
ATOM   7914  N  ND1 . HIS   B 1  365 ? -4.514  14.848  26.913  1    23.172  ? 365  HIS   B ND1 1 2 
ATOM   7915  C  CD2 . HIS   B 1  365 ? -2.985  16.355  26.521  1    20.113  ? 365  HIS   B CD2 1 2 
ATOM   7916  C  CE1 . HIS   B 1  365 ? -4.168  14.745  25.629  1    22.842  ? 365  HIS   B CE1 1 2 
ATOM   7917  N  NE2 . HIS   B 1  365 ? -3.216  15.601  25.399  1    21.016  ? 365  HIS   B NE2 1 2 
ATOM   7918  N  N   . ILE   B 1  366 ? -5      17.69   31.498  1    21.709  ? 366  ILE   B N   1 2 
ATOM   7919  C  CA  . ILE   B 1  366 ? -4.968  17.833  32.95   1    22.083  ? 366  ILE   B CA  1 2 
ATOM   7920  C  C   . ILE   B 1  366 ? -6.355  17.661  33.557  1    24.294  ? 366  ILE   B C   1 2 
ATOM   7921  O  O   . ILE   B 1  366 ? -6.51   16.985  34.607  1    25.277  ? 366  ILE   B O   1 2 
ATOM   7922  C  CB  . ILE   B 1  366 ? -4.364  19.187  33.365  1    22.515  ? 366  ILE   B CB  1 2 
ATOM   7923  C  CG1 . ILE   B 1  366 ? -2.918  19.379  32.878  1    21.851  ? 366  ILE   B CG1 1 2 
ATOM   7924  C  CG2 . ILE   B 1  366 ? -4.464  19.31   34.892  1    22.427  ? 366  ILE   B CG2 1 2 
ATOM   7925  C  CD1 . ILE   B 1  366 ? -1.927  18.422  33.576  1    23.422  ? 366  ILE   B CD1 1 2 
ATOM   7926  N  N   . GLN   B 1  367 ? -7.355  18.348  32.992  1    23.151  ? 367  GLN   B N   1 2 
ATOM   7927  C  CA  . GLN   B 1  367 ? -8.703  18.184  33.508  1    25.527  ? 367  GLN   B CA  1 2 
ATOM   7928  C  C   . GLN   B 1  367 ? -9.094  16.701  33.598  1    27.756  ? 367  GLN   B C   1 2 
ATOM   7929  O  O   . GLN   B 1  367 ? -9.693  16.236  34.595  1    28.233  ? 367  GLN   B O   1 2 
ATOM   7930  C  CB  . GLN   B 1  367 ? -9.649  18.993  32.624  1    24.861  ? 367  GLN   B CB  1 2 
ATOM   7931  C  CG  . GLN   B 1  367 ? -11.023 19.217  33.26   1    25.341  ? 367  GLN   B CG  1 2 
ATOM   7932  C  CD  . GLN   B 1  367 ? -11.007 19.903  34.614  1    27.783  ? 367  GLN   B CD  1 2 
ATOM   7933  O  OE1 . GLN   B 1  367 ? -11.612 19.4    35.564  1    28.908  ? 367  GLN   B OE1 1 2 
ATOM   7934  N  NE2 . GLN   B 1  367 ? -10.379 21.067  34.747  1    26.143  ? 367  GLN   B NE2 1 2 
ATOM   7935  N  N   . TYR   B 1  368 ? -8.84   15.94   32.515  1    27.789  ? 368  TYR   B N   1 2 
ATOM   7936  C  CA  . TYR   B 1  368 ? -9.137  14.511  32.501  1    28.153  ? 368  TYR   B CA  1 2 
ATOM   7937  C  C   . TYR   B 1  368 ? -8.517  13.878  33.752  1    29.544  ? 368  TYR   B C   1 2 
ATOM   7938  O  O   . TYR   B 1  368 ? -9.207  13.189  34.517  1    31.367  ? 368  TYR   B O   1 2 
ATOM   7939  C  CB  . TYR   B 1  368 ? -8.562  13.857  31.227  1    27.599  ? 368  TYR   B CB  1 2 
ATOM   7940  C  CG  . TYR   B 1  368 ? -9.475  12.872  30.517  1    28.522  ? 368  TYR   B CG  1 2 
ATOM   7941  C  CD1 . TYR   B 1  368 ? -10.29  11.982  31.218  1    31.461  ? 368  TYR   B CD1 1 2 
ATOM   7942  C  CD2 . TYR   B 1  368 ? -9.524  12.838  29.131  1    27.912  ? 368  TYR   B CD2 1 2 
ATOM   7943  C  CE1 . TYR   B 1  368 ? -11.144 11.104  30.558  1    32.311  ? 368  TYR   B CE1 1 2 
ATOM   7944  C  CE2 . TYR   B 1  368 ? -10.332 11.938  28.464  1    28.53   ? 368  TYR   B CE2 1 2 
ATOM   7945  C  CZ  . TYR   B 1  368 ? -11.146 11.06   29.174  1    30.879  ? 368  TYR   B CZ  1 2 
ATOM   7946  O  OH  . TYR   B 1  368 ? -11.955 10.196  28.465  1    30.484  ? 368  TYR   B OH  1 2 
ATOM   7947  N  N   . TYR   B 1  369 ? -7.226  14.145  33.961  1    28.11   ? 369  TYR   B N   1 2 
ATOM   7948  C  CA  . TYR   B 1  369 ? -6.478  13.506  35.019  1    30.785  ? 369  TYR   B CA  1 2 
ATOM   7949  C  C   . TYR   B 1  369 ? -7.035  13.891  36.389  1    33.619  ? 369  TYR   B C   1 2 
ATOM   7950  O  O   . TYR   B 1  369 ? -6.837  13.125  37.329  1    35.263  ? 369  TYR   B O   1 2 
ATOM   7951  C  CB  . TYR   B 1  369 ? -5.02   13.926  35.124  1    29.405  ? 369  TYR   B CB  1 2 
ATOM   7952  C  CG  . TYR   B 1  369 ? -4.11   13.821  33.905  1    27.906  ? 369  TYR   B CG  1 2 
ATOM   7953  C  CD1 . TYR   B 1  369 ? -4.268  12.815  32.955  1    27.13   ? 369  TYR   B CD1 1 2 
ATOM   7954  C  CD2 . TYR   B 1  369 ? -3.051  14.717  33.757  1    26.769  ? 369  TYR   B CD2 1 2 
ATOM   7955  C  CE1 . TYR   B 1  369 ? -3.419  12.733  31.868  1    26.735  ? 369  TYR   B CE1 1 2 
ATOM   7956  C  CE2 . TYR   B 1  369 ? -2.166  14.612  32.695  1    26.497  ? 369  TYR   B CE2 1 2 
ATOM   7957  C  CZ  . TYR   B 1  369 ? -2.353  13.603  31.763  1    25.842  ? 369  TYR   B CZ  1 2 
ATOM   7958  O  OH  . TYR   B 1  369 ? -1.538  13.463  30.688  1    26.815  ? 369  TYR   B OH  1 2 
ATOM   7959  N  N   . LEU   B 1  370 ? -7.621  15.098  36.507  1    32.618  ? 370  LEU   B N   1 2 
ATOM   7960  C  CA  . LEU   B 1  370 ? -8.219  15.55   37.754  1    35.007  ? 370  LEU   B CA  1 2 
ATOM   7961  C  C   . LEU   B 1  370 ? -9.552  14.834  37.947  1    35.569  ? 370  LEU   B C   1 2 
ATOM   7962  O  O   . LEU   B 1  370 ? -9.971  14.549  39.062  1    36.803  ? 370  LEU   B O   1 2 
ATOM   7963  C  CB  . LEU   B 1  370 ? -8.39   17.074  37.807  1    33.741  ? 370  LEU   B CB  1 2 
ATOM   7964  C  CG  . LEU   B 1  370 ? -7.135  17.943  37.637  1    32.203  ? 370  LEU   B CG  1 2 
ATOM   7965  C  CD1 . LEU   B 1  370 ? -7.573  19.395  37.471  1    30.984  ? 370  LEU   B CD1 1 2 
ATOM   7966  C  CD2 . LEU   B 1  370 ? -6.18   17.83   38.813  1    35.177  ? 370  LEU   B CD2 1 2 
ATOM   7967  N  N   . GLN   B 1  371 ? -10.231 14.547  36.855  1    34.689  ? 371  GLN   B N   1 2 
ATOM   7968  C  CA  . GLN   B 1  371 ? -11.556 13.961  36.955  1    36.854  ? 371  GLN   B CA  1 2 
ATOM   7969  C  C   . GLN   B 1  371 ? -11.484 12.461  37.258  1    38.891  ? 371  GLN   B C   1 2 
ATOM   7970  O  O   . GLN   B 1  371 ? -12.431 11.963  37.853  1    37.279  ? 371  GLN   B O   1 2 
ATOM   7971  C  CB  . GLN   B 1  371 ? -12.479 14.288  35.782  1    35.529  ? 371  GLN   B CB  1 2 
ATOM   7972  C  CG  . GLN   B 1  371 ? -12.888 15.759  35.66   1    35.758  ? 371  GLN   B CG  1 2 
ATOM   7973  C  CD  . GLN   B 1  371 ? -13.69  16.346  36.806  1    38.896  ? 371  GLN   B CD  1 2 
ATOM   7974  O  OE1 . GLN   B 1  371 ? -14.525 15.687  37.449  1    39.696  ? 371  GLN   B OE1 1 2 
ATOM   7975  N  NE2 . GLN   B 1  371 ? -13.418 17.613  37.096  1    39.629  ? 371  GLN   B NE2 1 2 
ATOM   7976  N  N   . TYR   B 1  372 ? -10.378 11.761  36.914  1    35.903  ? 372  TYR   B N   1 2 
ATOM   7977  C  CA  . TYR   B 1  372 ? -10.357 10.317  37.166  1    38.115  ? 372  TYR   B CA  1 2 
ATOM   7978  C  C   . TYR   B 1  372 ? -9.305  9.907   38.212  1    38.992  ? 372  TYR   B C   1 2 
ATOM   7979  O  O   . TYR   B 1  372 ? -8.935  8.727   38.329  1    40.91   ? 372  TYR   B O   1 2 
ATOM   7980  C  CB  . TYR   B 1  372 ? -10.342 9.605   35.804  1    34.308  ? 372  TYR   B CB  1 2 
ATOM   7981  C  CG  . TYR   B 1  372 ? -9.112  9.747   34.895  1    32.396  ? 372  TYR   B CG  1 2 
ATOM   7982  C  CD1 . TYR   B 1  372 ? -7.833  9.907   35.408  1    31.283  ? 372  TYR   B CD1 1 2 
ATOM   7983  C  CD2 . TYR   B 1  372 ? -9.254  9.677   33.505  1    31.175  ? 372  TYR   B CD2 1 2 
ATOM   7984  C  CE1 . TYR   B 1  372 ? -6.739  10.035  34.56   1    31.979  ? 372  TYR   B CE1 1 2 
ATOM   7985  C  CE2 . TYR   B 1  372 ? -8.165  9.803   32.65   1    30.166  ? 372  TYR   B CE2 1 2 
ATOM   7986  C  CZ  . TYR   B 1  372 ? -6.909  9.971   33.188  1    30.078  ? 372  TYR   B CZ  1 2 
ATOM   7987  O  OH  . TYR   B 1  372 ? -5.832  10.044  32.368  1    30.782  ? 372  TYR   B OH  1 2 
ATOM   7988  N  N   . LYS   B 1  373 ? -8.801  10.873  38.99   1    38.672  ? 373  LYS   B N   1 2 
ATOM   7989  C  CA  . LYS   B 1  373 ? -7.676  10.608  39.862  1    40.105  ? 373  LYS   B CA  1 2 
ATOM   7990  C  C   . LYS   B 1  373 ? -8.089  9.65    40.998  1    42.626  ? 373  LYS   B C   1 2 
ATOM   7991  O  O   . LYS   B 1  373 ? -7.216  9.093   41.64   1    44.055  ? 373  LYS   B O   1 2 
ATOM   7992  C  CB  . LYS   B 1  373 ? -7.125  11.907  40.462  1    40.039  ? 373  LYS   B CB  1 2 
ATOM   7993  C  CG  . LYS   B 1  373 ? -7.84   12.486  41.696  1    42.553  ? 373  LYS   B CG  1 2 
ATOM   7994  C  CD  . LYS   B 1  373 ? -8.008  13.994  41.505  1    43.435  ? 373  LYS   B CD  1 2 
ATOM   7995  C  CE  . LYS   B 1  373 ? -7.788  14.95   42.605  1    43.847  ? 373  LYS   B CE  1 2 
ATOM   7996  N  NZ  . LYS   B 1  373 ? -8.748  14.617  43.634  1    46.838  ? 373  LYS   B NZ  1 2 
ATOM   7997  N  N   . ASP   B 1  374 ? -9.389  9.443   41.228  1    43.533  ? 374  ASP   B N   1 2 
ATOM   7998  C  CA  . ASP   B 1  374 ? -9.777  8.563   42.333  1    49.034  ? 374  ASP   B CA  1 2 
ATOM   7999  C  C   . ASP   B 1  374 ? -10.049 7.152   41.818  1    49.651  ? 374  ASP   B C   1 2 
ATOM   8000  O  O   . ASP   B 1  374 ? -10.724 6.368   42.473  1    50.381  ? 374  ASP   B O   1 2 
ATOM   8001  C  CB  . ASP   B 1  374 ? -10.948 9.101   43.134  1    49.787  ? 374  ASP   B CB  1 2 
ATOM   8002  C  CG  . ASP   B 1  374 ? -10.687 10.433  43.827  1    54.618  ? 374  ASP   B CG  1 2 
ATOM   8003  O  OD1 . ASP   B 1  374 ? -9.638  10.549  44.519  1    54.084  ? 374  ASP   B OD1 1 2 
ATOM   8004  O  OD2 . ASP   B 1  374 ? -11.529 11.35   43.649  1    58.186  ? 374  ASP   B OD2 1 2 
ATOM   8005  N  N   . LEU   B 1  375 ? -9.489  6.826   40.656  1    47.406  ? 375  LEU   B N   1 2 
ATOM   8006  C  CA  . LEU   B 1  375 ? -9.729  5.528   40.053  1    47.703  ? 375  LEU   B CA  1 2 
ATOM   8007  C  C   . LEU   B 1  375 ? -8.537  4.62    40.31   1    50.533  ? 375  LEU   B C   1 2 
ATOM   8008  O  O   . LEU   B 1  375 ? -7.411  5.083   40.55   1    47.456  ? 375  LEU   B O   1 2 
ATOM   8009  C  CB  . LEU   B 1  375 ? -10.058 5.531   38.563  1    46.407  ? 375  LEU   B CB  1 2 
ATOM   8010  C  CG  . LEU   B 1  375 ? -11.39  6.137   38.131  1    45.579  ? 375  LEU   B CG  1 2 
ATOM   8011  C  CD1 . LEU   B 1  375 ? -11.747 5.662   36.721  1    43.147  ? 375  LEU   B CD1 1 2 
ATOM   8012  C  CD2 . LEU   B 1  375 ? -12.488 5.915   39.131  1    45.679  ? 375  LEU   B CD2 1 2 
ATOM   8013  N  N   . PRO   B 1  376 ? -8.801  3.294   40.322  1    55.3    ? 376  PRO   B N   1 2 
ATOM   8014  C  CA  . PRO   B 1  376 ? -7.76   2.283   40.151  1    58.364  ? 376  PRO   B CA  1 2 
ATOM   8015  C  C   . PRO   B 1  376 ? -6.956  2.626   38.906  1    56.522  ? 376  PRO   B C   1 2 
ATOM   8016  O  O   . PRO   B 1  376 ? -7.509  2.734   37.813  1    57.97   ? 376  PRO   B O   1 2 
ATOM   8017  C  CB  . PRO   B 1  376 ? -8.606  0.995   39.988  1    62.455  ? 376  PRO   B CB  1 2 
ATOM   8018  C  CG  . PRO   B 1  376 ? -9.999  1.483   39.639  1    62.784  ? 376  PRO   B CG  1 2 
ATOM   8019  C  CD  . PRO   B 1  376 ? -10.132 2.703   40.537  1    60.802  ? 376  PRO   B CD  1 2 
ATOM   8020  N  N   . VAL   B 1  377 ? -5.655  2.824   39.106  1    55.023  ? 377  VAL   B N   1 2 
ATOM   8021  C  CA  . VAL   B 1  377 ? -4.715  3.272   38.091  1    58.905  ? 377  VAL   B CA  1 2 
ATOM   8022  C  C   . VAL   B 1  377 ? -5.116  2.854   36.67   1    58.341  ? 377  VAL   B C   1 2 
ATOM   8023  O  O   . VAL   B 1  377 ? -5.25   3.691   35.796  1    54.861  ? 377  VAL   B O   1 2 
ATOM   8024  C  CB  . VAL   B 1  377 ? -3.289  2.824   38.458  1    60.36   ? 377  VAL   B CB  1 2 
ATOM   8025  C  CG1 . VAL   B 1  377 ? -2.684  3.713   39.528  1    60.762  ? 377  VAL   B CG1 1 2 
ATOM   8026  C  CG2 . VAL   B 1  377 ? -3.23   1.374   38.925  1    65.672  ? 377  VAL   B CG2 1 2 
ATOM   8027  N  N   . SER   B 1  378 ? -5.335  1.563   36.441  1    60.918  ? 378  SER   B N   1 2 
ATOM   8028  C  CA  . SER   B 1  378 ? -5.558  1.027   35.112  1    60.997  ? 378  SER   B CA  1 2 
ATOM   8029  C  C   . SER   B 1  378 ? -6.843  1.575   34.488  1    58.817  ? 378  SER   B C   1 2 
ATOM   8030  O  O   . SER   B 1  378 ? -7.099  1.348   33.308  1    61.439  ? 378  SER   B O   1 2 
ATOM   8031  C  CB  . SER   B 1  378 ? -5.573  -0.492  35.157  1    65.789  ? 378  SER   B CB  1 2 
ATOM   8032  O  OG  . SER   B 1  378 ? -4.39   -0.986  35.774  1    66.827  ? 378  SER   B OG  1 2 
ATOM   8033  N  N   . LEU   B 1  379 ? -7.653  2.299   35.262  1    52.356  ? 379  LEU   B N   1 2 
ATOM   8034  C  CA  . LEU   B 1  379 ? -8.787  2.955   34.643  1    50.786  ? 379  LEU   B CA  1 2 
ATOM   8035  C  C   . LEU   B 1  379 ? -8.495  4.444   34.364  1    44.479  ? 379  LEU   B C   1 2 
ATOM   8036  O  O   . LEU   B 1  379 ? -9.367  5.148   33.862  1    44.501  ? 379  LEU   B O   1 2 
ATOM   8037  C  CB  . LEU   B 1  379 ? -10.045 2.737   35.488  1    57.588  ? 379  LEU   B CB  1 2 
ATOM   8038  C  CG  . LEU   B 1  379 ? -10.467 1.288   35.774  1    59.185  ? 379  LEU   B CG  1 2 
ATOM   8039  C  CD1 . LEU   B 1  379 ? -11.822 1.294   36.44   1    58.941  ? 379  LEU   B CD1 1 2 
ATOM   8040  C  CD2 . LEU   B 1  379 ? -10.526 0.485   34.486  1    57.967  ? 379  LEU   B CD2 1 2 
ATOM   8041  N  N   . ARG   B 1  380 ? -7.286  4.915   34.695  1    39.154  ? 380  ARG   B N   1 2 
ATOM   8042  C  CA  . ARG   B 1  380 ? -6.922  6.323   34.592  1    39.242  ? 380  ARG   B CA  1 2 
ATOM   8043  C  C   . ARG   B 1  380 ? -6.28   6.592   33.236  1    34.175  ? 380  ARG   B C   1 2 
ATOM   8044  O  O   . ARG   B 1  380 ? -5.109  6.939   33.132  1    32.63   ? 380  ARG   B O   1 2 
ATOM   8045  C  CB  . ARG   B 1  380 ? -5.922  6.8     35.646  1    39.224  ? 380  ARG   B CB  1 2 
ATOM   8046  C  CG  . ARG   B 1  380 ? -6.451  6.779   37.077  1    40.01   ? 380  ARG   B CG  1 2 
ATOM   8047  C  CD  . ARG   B 1  380 ? -5.298  7.237   37.96   1    41.22   ? 380  ARG   B CD  1 2 
ATOM   8048  N  NE  . ARG   B 1  380 ? -5.606  6.794   39.324  1    46.725  ? 380  ARG   B NE  1 2 
ATOM   8049  C  CZ  . ARG   B 1  380 ? -4.87   6.833   40.402  1    47.458  ? 380  ARG   B CZ  1 2 
ATOM   8050  N  NH1 . ARG   B 1  380 ? -3.711  7.458   40.427  1    44.951  ? 380  ARG   B NH1 1 2 
ATOM   8051  N  NH2 . ARG   B 1  380 ? -5.329  6.204   41.477  1    51.083  ? 380  ARG   B NH2 1 2 
ATOM   8052  N  N   . ARG   B 1  381 ? -7.065  6.343   32.203  1    36.98   ? 381  ARG   B N   1 2 
ATOM   8053  C  CA  . ARG   B 1  381 ? -6.659  6.586   30.829  1    35.978  ? 381  ARG   B CA  1 2 
ATOM   8054  C  C   . ARG   B 1  381 ? -7.913  7.183   30.246  1    33.78   ? 381  ARG   B C   1 2 
ATOM   8055  O  O   . ARG   B 1  381 ? -8.9    7.109   30.942  1    34.406  ? 381  ARG   B O   1 2 
ATOM   8056  C  CB  . ARG   B 1  381 ? -6.483  5.214   30.162  1    38.994  ? 381  ARG   B CB  1 2 
ATOM   8057  C  CG  . ARG   B 1  381 ? -5.044  4.74    30.202  1    45.832  ? 381  ARG   B CG  1 2 
ATOM   8058  C  CD  . ARG   B 1  381 ? -4.934  3.265   29.811  1    57.435  ? 381  ARG   B CD  1 2 
ATOM   8059  N  NE  . ARG   B 1  381 ? -4.383  2.533   30.959  1    66.981  ? 381  ARG   B NE  1 2 
ATOM   8060  C  CZ  . ARG   B 1  381 ? -3.083  2.228   31.103  1    75.253  ? 381  ARG   B CZ  1 2 
ATOM   8061  N  NH1 . ARG   B 1  381 ? -2.247  2.344   30.077  1    70.98   ? 381  ARG   B NH1 1 2 
ATOM   8062  N  NH2 . ARG   B 1  381 ? -2.628  1.785   32.271  1    76.05   ? 381  ARG   B NH2 1 2 
ATOM   8063  N  N   . GLY   B 1  382 ? -7.898  7.691   28.992  1    33.297  ? 382  GLY   B N   1 2 
ATOM   8064  C  CA  . GLY   B 1  382 ? -9.152  8.11    28.394  1    30.227  ? 382  GLY   B CA  1 2 
ATOM   8065  C  C   . GLY   B 1  382 ? -9.921  6.854   27.981  1    33.553  ? 382  GLY   B C   1 2 
ATOM   8066  O  O   . GLY   B 1  382 ? -9.337  5.775   28      1    36.696  ? 382  GLY   B O   1 2 
ATOM   8067  N  N   . ALA   B 1  383 ? -11.201 7.002   27.633  1    32.624  ? 383  ALA   B N   1 2 
ATOM   8068  C  CA  . ALA   B 1  383 ? -12.05  5.909   27.183  1    36.642  ? 383  ALA   B CA  1 2 
ATOM   8069  C  C   . ALA   B 1  383 ? -11.441 5.244   25.932  1    36.896  ? 383  ALA   B C   1 2 
ATOM   8070  O  O   . ALA   B 1  383 ? -11.562 4.041   25.738  1    36.069  ? 383  ALA   B O   1 2 
ATOM   8071  C  CB  . ALA   B 1  383 ? -13.433 6.443   26.914  1    34.597  ? 383  ALA   B CB  1 2 
ATOM   8072  N  N   . ASN   B 1  384 ? -10.811 6.052   25.071  1    33.111  ? 384  ASN   B N   1 2 
ATOM   8073  C  CA  . ASN   B 1  384 ? -9.789  5.634   24.133  1    32.614  ? 384  ASN   B CA  1 2 
ATOM   8074  C  C   . ASN   B 1  384 ? -8.799  6.803   24.029  1    30.813  ? 384  ASN   B C   1 2 
ATOM   8075  O  O   . ASN   B 1  384 ? -9.091  7.886   24.527  1    28.892  ? 384  ASN   B O   1 2 
ATOM   8076  C  CB  . ASN   B 1  384 ? -10.395 5.095   22.833  1    31.121  ? 384  ASN   B CB  1 2 
ATOM   8077  C  CG  . ASN   B 1  384 ? -11.002 6.123   21.909  1    30.166  ? 384  ASN   B CG  1 2 
ATOM   8078  O  OD1 . ASN   B 1  384 ? -10.484 7.24    21.746  1    29.644  ? 384  ASN   B OD1 1 2 
ATOM   8079  N  ND2 . ASN   B 1  384 ? -12.092 5.756   21.268  1    30.264  ? 384  ASN   B ND2 1 2 
ATOM   8080  N  N   . PRO   B 1  385 ? -7.586  6.643   23.435  1    28.109  ? 385  PRO   B N   1 2 
ATOM   8081  C  CA  . PRO   B 1  385 ? -6.625  7.741   23.392  1    25.979  ? 385  PRO   B CA  1 2 
ATOM   8082  C  C   . PRO   B 1  385 ? -7.12   8.99    22.656  1    23.841  ? 385  PRO   B C   1 2 
ATOM   8083  O  O   . PRO   B 1  385 ? -6.722  10.07   23.03   1    22.493  ? 385  PRO   B O   1 2 
ATOM   8084  C  CB  . PRO   B 1  385 ? -5.455  7.071   22.628  1    24.672  ? 385  PRO   B CB  1 2 
ATOM   8085  C  CG  . PRO   B 1  385 ? -5.576  5.612   23.115  1    25.733  ? 385  PRO   B CG  1 2 
ATOM   8086  C  CD  . PRO   B 1  385 ? -7.054  5.386   22.849  1    27.562  ? 385  PRO   B CD  1 2 
ATOM   8087  N  N   . GLY   B 1  386 ? -8.003  8.804   21.667  1    23.179  ? 386  GLY   B N   1 2 
ATOM   8088  C  CA  . GLY   B 1  386 ? -8.668  9.853   20.91   1    23.539  ? 386  GLY   B CA  1 2 
ATOM   8089  C  C   . GLY   B 1  386 ? -9.492  10.78   21.804  1    25.656  ? 386  GLY   B C   1 2 
ATOM   8090  O  O   . GLY   B 1  386 ? -9.618  11.986  21.539  1    23.345  ? 386  GLY   B O   1 2 
ATOM   8091  N  N   . PHE   B 1  387 ? -10.085 10.203  22.859  1    26.562  ? 387  PHE   B N   1 2 
ATOM   8092  C  CA  . PHE   B 1  387 ? -10.891 10.97   23.795  1    25.419  ? 387  PHE   B CA  1 2 
ATOM   8093  C  C   . PHE   B 1  387 ? -9.987  11.946  24.516  1    23.361  ? 387  PHE   B C   1 2 
ATOM   8094  O  O   . PHE   B 1  387 ? -10.334 13.126  24.653  1    22.911  ? 387  PHE   B O   1 2 
ATOM   8095  C  CB  . PHE   B 1  387 ? -11.62  10.139  24.875  1    27.093  ? 387  PHE   B CB  1 2 
ATOM   8096  C  CG  . PHE   B 1  387 ? -12.952 9.567   24.416  1    29.564  ? 387  PHE   B CG  1 2 
ATOM   8097  C  CD1 . PHE   B 1  387 ? -13.032 8.741   23.294  1    29.524  ? 387  PHE   B CD1 1 2 
ATOM   8098  C  CD2 . PHE   B 1  387 ? -14.142 9.914   25.062  1    31.629  ? 387  PHE   B CD2 1 2 
ATOM   8099  C  CE1 . PHE   B 1  387 ? -14.253 8.235   22.852  1    31.271  ? 387  PHE   B CE1 1 2 
ATOM   8100  C  CE2 . PHE   B 1  387 ? -15.375 9.388   24.634  1    35.284  ? 387  PHE   B CE2 1 2 
ATOM   8101  C  CZ  . PHE   B 1  387 ? -15.428 8.556   23.522  1    34.431  ? 387  PHE   B CZ  1 2 
ATOM   8102  N  N   . HIS   B 1  388 ? -8.809  11.457  24.907  1    22.566  ? 388  HIS   B N   1 2 
ATOM   8103  C  CA  . HIS   B 1  388 ? -7.9    12.277  25.676  1    22.82   ? 388  HIS   B CA  1 2 
ATOM   8104  C  C   . HIS   B 1  388 ? -7.485  13.483  24.835  1    22.74   ? 388  HIS   B C   1 2 
ATOM   8105  O  O   . HIS   B 1  388 ? -7.418  14.597  25.351  1    21.748  ? 388  HIS   B O   1 2 
ATOM   8106  C  CB  . HIS   B 1  388 ? -6.758  11.397  26.175  1    24.439  ? 388  HIS   B CB  1 2 
ATOM   8107  C  CG  . HIS   B 1  388 ? -6.427  11.632  27.612  1    24.822  ? 388  HIS   B CG  1 2 
ATOM   8108  N  ND1 . HIS   B 1  388 ? -6.158  12.875  28.169  1    24.165  ? 388  HIS   B ND1 1 2 
ATOM   8109  C  CD2 . HIS   B 1  388 ? -6.396  10.728  28.64   1    26.02   ? 388  HIS   B CD2 1 2 
ATOM   8110  C  CE1 . HIS   B 1  388 ? -5.923  12.717  29.469  1    27.051  ? 388  HIS   B CE1 1 2 
ATOM   8111  N  NE2 . HIS   B 1  388 ? -6.113  11.431  29.784  1    27.28   ? 388  HIS   B NE2 1 2 
ATOM   8112  N  N   . GLU   B 1  389 ? -7.298  13.287  23.521  1    22.127  ? 389  GLU   B N   1 2 
ATOM   8113  C  CA  . GLU   B 1  389 ? -6.79   14.349  22.66   1    21.07   ? 389  GLU   B CA  1 2 
ATOM   8114  C  C   . GLU   B 1  389 ? -7.895  15.349  22.314  1    20.982  ? 389  GLU   B C   1 2 
ATOM   8115  O  O   . GLU   B 1  389 ? -7.604  16.444  21.833  1    22.628  ? 389  GLU   B O   1 2 
ATOM   8116  C  CB  . GLU   B 1  389 ? -6.246  13.783  21.351  1    20.518  ? 389  GLU   B CB  1 2 
ATOM   8117  C  CG  . GLU   B 1  389 ? -5.087  12.831  21.626  1    20.199  ? 389  GLU   B CG  1 2 
ATOM   8118  C  CD  . GLU   B 1  389 ? -3.981  13.441  22.479  1    20.826  ? 389  GLU   B CD  1 2 
ATOM   8119  O  OE1 . GLU   B 1  389 ? -3.266  12.648  23.191  1    22.348  ? 389  GLU   B OE1 1 2 
ATOM   8120  O  OE2 . GLU   B 1  389 ? -3.772  14.703  22.457  1    20.072  ? 389  GLU   B OE2 1 2 
ATOM   8121  N  N   . ALA   B 1  390 ? -9.157  14.987  22.546  1    20.034  ? 390  ALA   B N   1 2 
ATOM   8122  C  CA  . ALA   B 1  390 ? -10.222 15.824  22.028  1    20.952  ? 390  ALA   B CA  1 2 
ATOM   8123  C  C   . ALA   B 1  390 ? -10.705 16.852  23.063  1    23.018  ? 390  ALA   B C   1 2 
ATOM   8124  O  O   . ALA   B 1  390 ? -11.422 17.797  22.726  1    25.115  ? 390  ALA   B O   1 2 
ATOM   8125  C  CB  . ALA   B 1  390 ? -11.324 14.908  21.58   1    20.719  ? 390  ALA   B CB  1 2 
ATOM   8126  N  N   . ILE   B 1  391 ? -10.395 16.639  24.349  1    23.513  ? 391  ILE   B N   1 2 
ATOM   8127  C  CA  . ILE   B 1  391 ? -11.109 17.366  25.41   1    24.014  ? 391  ILE   B CA  1 2 
ATOM   8128  C  C   . ILE   B 1  391 ? -10.815 18.865  25.303  1    22.958  ? 391  ILE   B C   1 2 
ATOM   8129  O  O   . ILE   B 1  391 ? -11.737 19.688  25.293  1    21.998  ? 391  ILE   B O   1 2 
ATOM   8130  C  CB  . ILE   B 1  391 ? -10.799 16.824  26.826  1    24.18   ? 391  ILE   B CB  1 2 
ATOM   8131  C  CG1 . ILE   B 1  391 ? -11.191 15.344  26.932  1    25.985  ? 391  ILE   B CG1 1 2 
ATOM   8132  C  CG2 . ILE   B 1  391 ? -11.497 17.664  27.923  1    25.263  ? 391  ILE   B CG2 1 2 
ATOM   8133  C  CD1 . ILE   B 1  391 ? -12.621 15.015  26.516  1    25.905  ? 391  ILE   B CD1 1 2 
ATOM   8134  N  N   . GLY   B 1  392 ? -9.517  19.224  25.274  1    20.19   ? 392  GLY   B N   1 2 
ATOM   8135  C  CA  . GLY   B 1  392 ? -9.214  20.645  25.305  1    19.314  ? 392  GLY   B CA  1 2 
ATOM   8136  C  C   . GLY   B 1  392 ? -9.5    21.276  23.944  1    19.836  ? 392  GLY   B C   1 2 
ATOM   8137  O  O   . GLY   B 1  392 ? -9.788  22.476  23.862  1    18.775  ? 392  GLY   B O   1 2 
ATOM   8138  N  N   . ASP   B 1  393 ? -9.425  20.456  22.873  1    18.972  ? 393  ASP   B N   1 2 
ATOM   8139  C  CA  . ASP   B 1  393 ? -9.726  20.955  21.537  1    20.181  ? 393  ASP   B CA  1 2 
ATOM   8140  C  C   . ASP   B 1  393 ? -11.191 21.378  21.478  1    19.989  ? 393  ASP   B C   1 2 
ATOM   8141  O  O   . ASP   B 1  393 ? -11.53  22.368  20.831  1    20.97   ? 393  ASP   B O   1 2 
ATOM   8142  C  CB  . ASP   B 1  393 ? -9.428  19.981  20.401  1    21.471  ? 393  ASP   B CB  1 2 
ATOM   8143  C  CG  . ASP   B 1  393 ? -7.95   19.844  19.994  1    25.916  ? 393  ASP   B CG  1 2 
ATOM   8144  O  OD1 . ASP   B 1  393 ? -7.017  20.142  20.829  1    24.353  ? 393  ASP   B OD1 1 2 
ATOM   8145  O  OD2 . ASP   B 1  393 ? -7.727  19.447  18.832  1    27.205  ? 393  ASP   B OD2 1 2 
ATOM   8146  N  N   . VAL   B 1  394 ? -12.046 20.647  22.187  1    20.284  ? 394  VAL   B N   1 2 
ATOM   8147  C  CA  . VAL   B 1  394 ? -13.464 20.995  22.203  1    21.505  ? 394  VAL   B CA  1 2 
ATOM   8148  C  C   . VAL   B 1  394 ? -13.649 22.394  22.774  1    22.716  ? 394  VAL   B C   1 2 
ATOM   8149  O  O   . VAL   B 1  394 ? -14.363 23.209  22.178  1    22.627  ? 394  VAL   B O   1 2 
ATOM   8150  C  CB  . VAL   B 1  394 ? -14.267 19.925  22.965  1    23.901  ? 394  VAL   B CB  1 2 
ATOM   8151  C  CG1 . VAL   B 1  394 ? -15.725 20.309  23.184  1    26.079  ? 394  VAL   B CG1 1 2 
ATOM   8152  C  CG2 . VAL   B 1  394 ? -14.223 18.633  22.156  1    25.422  ? 394  VAL   B CG2 1 2 
ATOM   8153  N  N   . LEU   B 1  395 ? -13.027 22.668  23.945  1    21.864  ? 395  LEU   B N   1 2 
ATOM   8154  C  CA  . LEU   B 1  395 ? -13.195 23.988  24.538  1    23.099  ? 395  LEU   B CA  1 2 
ATOM   8155  C  C   . LEU   B 1  395 ? -12.625 25.028  23.576  1    22.491  ? 395  LEU   B C   1 2 
ATOM   8156  O  O   . LEU   B 1  395 ? -13.205 26.11   23.434  1    23.212  ? 395  LEU   B O   1 2 
ATOM   8157  C  CB  . LEU   B 1  395 ? -12.504 24.065  25.907  1    24.941  ? 395  LEU   B CB  1 2 
ATOM   8158  C  CG  . LEU   B 1  395 ? -13.336 23.606  27.123  1    28.151  ? 395  LEU   B CG  1 2 
ATOM   8159  C  CD1 . LEU   B 1  395 ? -13.476 22.126  27.206  1    27.777  ? 395  LEU   B CD1 1 2 
ATOM   8160  C  CD2 . LEU   B 1  395 ? -12.616 24.092  28.382  1    28.316  ? 395  LEU   B CD2 1 2 
ATOM   8161  N  N   . ALA   B 1  396 ? -11.457 24.713  22.96   1    20.502  ? 396  ALA   B N   1 2 
ATOM   8162  C  CA  . ALA   B 1  396 ? -10.837 25.673  22.053  1    21.07   ? 396  ALA   B CA  1 2 
ATOM   8163  C  C   . ALA   B 1  396 ? -11.754 26.036  20.874  1    21.057  ? 396  ALA   B C   1 2 
ATOM   8164  O  O   . ALA   B 1  396 ? -11.648 27.132  20.344  1    22.274  ? 396  ALA   B O   1 2 
ATOM   8165  C  CB  . ALA   B 1  396 ? -9.521  25.206  21.501  1    17.919  ? 396  ALA   B CB  1 2 
ATOM   8166  N  N   . LEU   B 1  397 ? -12.611 25.129  20.422  1    22.002  ? 397  LEU   B N   1 2 
ATOM   8167  C  CA  . LEU   B 1  397 ? -13.57  25.513  19.38   1    23.247  ? 397  LEU   B CA  1 2 
ATOM   8168  C  C   . LEU   B 1  397 ? -14.483 26.656  19.847  1    24.994  ? 397  LEU   B C   1 2 
ATOM   8169  O  O   . LEU   B 1  397 ? -14.881 27.491  19.052  1    27.163  ? 397  LEU   B O   1 2 
ATOM   8170  C  CB  . LEU   B 1  397 ? -14.395 24.308  18.947  1    25.221  ? 397  LEU   B CB  1 2 
ATOM   8171  C  CG  . LEU   B 1  397 ? -13.625 23.215  18.213  1    24.553  ? 397  LEU   B CG  1 2 
ATOM   8172  C  CD1 . LEU   B 1  397 ? -14.541 22.03   17.979  1    25.841  ? 397  LEU   B CD1 1 2 
ATOM   8173  C  CD2 . LEU   B 1  397 ? -13.217 23.802  16.89   1    26.405  ? 397  LEU   B CD2 1 2 
ATOM   8174  N  N   . SER   B 1  398 ? -14.891 26.663  21.119  1    23.703  ? 398  SER   B N   1 2 
ATOM   8175  C  CA  . SER   B 1  398 ? -15.701 27.77   21.614  1    24.355  ? 398  SER   B CA  1 2 
ATOM   8176  C  C   . SER   B 1  398 ? -14.816 29.004  21.755  1    23.239  ? 398  SER   B C   1 2 
ATOM   8177  O  O   . SER   B 1  398 ? -15.239 30.09   21.412  1    24.431  ? 398  SER   B O   1 2 
ATOM   8178  C  CB  . SER   B 1  398 ? -16.351 27.429  22.936  1    25.613  ? 398  SER   B CB  1 2 
ATOM   8179  O  OG  . SER   B 1  398 ? -17.468 26.563  22.809  1    27.347  ? 398  SER   B OG  1 2 
ATOM   8180  N  N   . VAL   B 1  399 ? -13.594 28.84   22.289  1    21.764  ? 399  VAL   B N   1 2 
ATOM   8181  C  CA  . VAL   B 1  399 ? -12.727 29.985  22.555  1    22.957  ? 399  VAL   B CA  1 2 
ATOM   8182  C  C   . VAL   B 1  399 ? -12.427 30.744  21.259  1    22.609  ? 399  VAL   B C   1 2 
ATOM   8183  O  O   . VAL   B 1  399 ? -12.336 31.964  21.266  1    22.793  ? 399  VAL   B O   1 2 
ATOM   8184  C  CB  . VAL   B 1  399 ? -11.441 29.56   23.318  1    22.729  ? 399  VAL   B CB  1 2 
ATOM   8185  C  CG1 . VAL   B 1  399 ? -10.387 30.648  23.328  1    24.123  ? 399  VAL   B CG1 1 2 
ATOM   8186  C  CG2 . VAL   B 1  399 ? -11.76  29.127  24.761  1    21.838  ? 399  VAL   B CG2 1 2 
ATOM   8187  N  N   . SER   B 1  400 ? -12.227 30.039  20.144  1    22.906  ? 400  SER   B N   1 2 
ATOM   8188  C  CA  . SER   B 1  400 ? -11.749 30.702  18.933  1    23.871  ? 400  SER   B CA  1 2 
ATOM   8189  C  C   . SER   B 1  400 ? -12.87  31.483  18.202  1    25.981  ? 400  SER   B C   1 2 
ATOM   8190  O  O   . SER   B 1  400 ? -12.598 32.252  17.257  1    27.827  ? 400  SER   B O   1 2 
ATOM   8191  C  CB  . SER   B 1  400 ? -11.086 29.681  18.042  1    26.091  ? 400  SER   B CB  1 2 
ATOM   8192  O  OG  . SER   B 1  400 ? -12.125 28.937  17.423  1    28.391  ? 400  SER   B OG  1 2 
ATOM   8193  N  N   . THR   B 1  401 ? -14.129 31.293  18.611  1    24.393  ? 401  THR   B N   1 2 
ATOM   8194  C  CA  . THR   B 1  401 ? -15.223 32.022  17.971  1    27.153  ? 401  THR   B CA  1 2 
ATOM   8195  C  C   . THR   B 1  401 ? -15.006 33.522  18.118  1    29.499  ? 401  THR   B C   1 2 
ATOM   8196  O  O   . THR   B 1  401 ? -14.615 34.015  19.195  1    29.994  ? 401  THR   B O   1 2 
ATOM   8197  C  CB  . THR   B 1  401 ? -16.635 31.657  18.464  1    26.543  ? 401  THR   B CB  1 2 
ATOM   8198  O  OG1 . THR   B 1  401 ? -16.794 31.863  19.881  1    26.584  ? 401  THR   B OG1 1 2 
ATOM   8199  C  CG2 . THR   B 1  401 ? -16.961 30.215  18.159  1    26.321  ? 401  THR   B CG2 1 2 
ATOM   8200  N  N   . PRO   B 1  402 ? -15.322 34.297  17.05   1    30.46   ? 402  PRO   B N   1 2 
ATOM   8201  C  CA  . PRO   B 1  402 ? -15.216 35.756  17.118  1    30.24   ? 402  PRO   B CA  1 2 
ATOM   8202  C  C   . PRO   B 1  402 ? -15.937 36.34   18.328  1    31.462  ? 402  PRO   B C   1 2 
ATOM   8203  O  O   . PRO   B 1  402 ? -15.454 37.297  18.934  1    32.014  ? 402  PRO   B O   1 2 
ATOM   8204  C  CB  . PRO   B 1  402 ? -15.823 36.193  15.787  1    31.697  ? 402  PRO   B CB  1 2 
ATOM   8205  C  CG  . PRO   B 1  402 ? -15.529 35.04   14.864  1    30.475  ? 402  PRO   B CG  1 2 
ATOM   8206  C  CD  . PRO   B 1  402 ? -15.65  33.783  15.71   1    28.491  ? 402  PRO   B CD  1 2 
ATOM   8207  N  N   . GLU   B 1  403 ? -17.103 35.775  18.673  1    31.909  ? 403  GLU   B N   1 2 
ATOM   8208  C  CA  . GLU   B 1  403 ? -17.888 36.329  19.76   1    34.356  ? 403  GLU   B CA  1 2 
ATOM   8209  C  C   . GLU   B 1  403 ? -17.19  36.11   21.109  1    30.66   ? 403  GLU   B C   1 2 
ATOM   8210  O  O   . GLU   B 1  403 ? -17.269 36.933  22.028  1    29.828  ? 403  GLU   B O   1 2 
ATOM   8211  C  CB  . GLU   B 1  403 ? -19.306 35.765  19.765  1    39.782  ? 403  GLU   B CB  1 2 
ATOM   8212  C  CG  . GLU   B 1  403 ? -20.202 36.612  20.666  1    54.875  ? 403  GLU   B CG  1 2 
ATOM   8213  C  CD  . GLU   B 1  403 ? -21.727 36.511  20.71   1    70.747  ? 403  GLU   B CD  1 2 
ATOM   8214  O  OE1 . GLU   B 1  403 ? -22.347 37.332  21.442  1    73.08   ? 403  GLU   B OE1 1 2 
ATOM   8215  O  OE2 . GLU   B 1  403 ? -22.307 35.634  20.022  1    80.006  ? 403  GLU   B OE2 1 2 
ATOM   8216  N  N   . HIS   B 1  404 ? -16.545 34.955  21.254  1    28.128  ? 404  HIS   B N   1 2 
ATOM   8217  C  CA  . HIS   B 1  404 ? -15.838 34.682  22.496  1    26.846  ? 404  HIS   B CA  1 2 
ATOM   8218  C  C   . HIS   B 1  404 ? -14.591 35.564  22.557  1    26.308  ? 404  HIS   B C   1 2 
ATOM   8219  O  O   . HIS   B 1  404 ? -14.246 36.062  23.619  1    25.662  ? 404  HIS   B O   1 2 
ATOM   8220  C  CB  . HIS   B 1  404 ? -15.4   33.215  22.574  1    24.869  ? 404  HIS   B CB  1 2 
ATOM   8221  C  CG  . HIS   B 1  404 ? -14.892 32.948  23.953  1    25.335  ? 404  HIS   B CG  1 2 
ATOM   8222  N  ND1 . HIS   B 1  404 ? -15.772 32.743  24.993  1    26.932  ? 404  HIS   B ND1 1 2 
ATOM   8223  C  CD2 . HIS   B 1  404 ? -13.65  32.93   24.492  1    24.03   ? 404  HIS   B CD2 1 2 
ATOM   8224  C  CE1 . HIS   B 1  404 ? -15.075 32.606  26.125  1    27.169  ? 404  HIS   B CE1 1 2 
ATOM   8225  N  NE2 . HIS   B 1  404 ? -13.788 32.68   25.828  1    25.037  ? 404  HIS   B NE2 1 2 
ATOM   8226  N  N   . LEU   B 1  405 ? -13.864 35.652  21.431  1    25.406  ? 405  LEU   B N   1 2 
ATOM   8227  C  CA  . LEU   B 1  405 ? -12.671 36.475  21.364  1    25.814  ? 405  LEU   B CA  1 2 
ATOM   8228  C  C   . LEU   B 1  405 ? -13.05  37.888  21.794  1    27.656  ? 405  LEU   B C   1 2 
ATOM   8229  O  O   . LEU   B 1  405 ? -12.333 38.546  22.553  1    27.152  ? 405  LEU   B O   1 2 
ATOM   8230  C  CB  . LEU   B 1  405 ? -12.058 36.456  19.965  1    25.58   ? 405  LEU   B CB  1 2 
ATOM   8231  C  CG  . LEU   B 1  405 ? -11.437 35.129  19.54   1    25.954  ? 405  LEU   B CG  1 2 
ATOM   8232  C  CD1 . LEU   B 1  405 ? -11.089 35.101  18.056  1    25.007  ? 405  LEU   B CD1 1 2 
ATOM   8233  C  CD2 . LEU   B 1  405 ? -10.185 34.815  20.392  1    25.117  ? 405  LEU   B CD2 1 2 
ATOM   8234  N  N   . HIS   B 1  406 ? -14.216 38.353  21.325  1    28.736  ? 406  HIS   B N   1 2 
ATOM   8235  C  CA  . HIS   B 1  406 ? -14.676 39.669  21.77   1    30.646  ? 406  HIS   B CA  1 2 
ATOM   8236  C  C   . HIS   B 1  406 ? -14.923 39.699  23.282  1    31.167  ? 406  HIS   B C   1 2 
ATOM   8237  O  O   . HIS   B 1  406 ? -14.626 40.685  23.967  1    30.775  ? 406  HIS   B O   1 2 
ATOM   8238  C  CB  . HIS   B 1  406 ? -15.899 40.077  20.947  1    32.902  ? 406  HIS   B CB  1 2 
ATOM   8239  C  CG  . HIS   B 1  406 ? -16.504 41.346  21.451  1    35.455  ? 406  HIS   B CG  1 2 
ATOM   8240  N  ND1 . HIS   B 1  406 ? -15.915 42.571  21.22   1    37.451  ? 406  HIS   B ND1 1 2 
ATOM   8241  C  CD2 . HIS   B 1  406 ? -17.619 41.595  22.178  1    38.392  ? 406  HIS   B CD2 1 2 
ATOM   8242  C  CE1 . HIS   B 1  406 ? -16.67  43.544  21.771  1    40.237  ? 406  HIS   B CE1 1 2 
ATOM   8243  N  NE2 . HIS   B 1  406 ? -17.714 42.974  22.352  1    39.956  ? 406  HIS   B NE2 1 2 
ATOM   8244  N  N   . LYS   B 1  407 ? -15.445 38.6    23.837  1    32.272  ? 407  LYS   B N   1 2 
ATOM   8245  C  CA  . LYS   B 1  407 ? -15.723 38.591  25.272  1    34.635  ? 407  LYS   B CA  1 2 
ATOM   8246  C  C   . LYS   B 1  407 ? -14.442 38.724  26.103  1    34.53   ? 407  LYS   B C   1 2 
ATOM   8247  O  O   . LYS   B 1  407 ? -14.509 39.265  27.211  1    36.565  ? 407  LYS   B O   1 2 
ATOM   8248  C  CB  . LYS   B 1  407 ? -16.487 37.364  25.785  1    38.369  ? 407  LYS   B CB  1 2 
ATOM   8249  C  CG  . LYS   B 1  407 ? -17.982 37.399  25.586  1    45.877  ? 407  LYS   B CG  1 2 
ATOM   8250  C  CD  . LYS   B 1  407 ? -18.678 36.044  25.665  1    49.584  ? 407  LYS   B CD  1 2 
ATOM   8251  C  CE  . LYS   B 1  407 ? -20.129 36.346  25.384  1    56.235  ? 407  LYS   B CE  1 2 
ATOM   8252  N  NZ  . LYS   B 1  407 ? -20.995 35.17   25.267  1    61.379  ? 407  LYS   B NZ  1 2 
ATOM   8253  N  N   . ILE   B 1  408 ? -13.305 38.198  25.62   1    32.085  ? 408  ILE   B N   1 2 
ATOM   8254  C  CA  . ILE   B 1  408 ? -12.058 38.225  26.386  1    31.327  ? 408  ILE   B CA  1 2 
ATOM   8255  C  C   . ILE   B 1  408 ? -11.126 39.33   25.876  1    31.81   ? 408  ILE   B C   1 2 
ATOM   8256  O  O   . ILE   B 1  408 ? -9.927  39.263  26.087  1    32.118  ? 408  ILE   B O   1 2 
ATOM   8257  C  CB  . ILE   B 1  408 ? -11.394 36.826  26.436  1    28.918  ? 408  ILE   B CB  1 2 
ATOM   8258  C  CG1 . ILE   B 1  408 ? -11.008 36.268  25.019  1    27.01   ? 408  ILE   B CG1 1 2 
ATOM   8259  C  CG2 . ILE   B 1  408 ? -12.351 35.89   27.176  1    28.816  ? 408  ILE   B CG2 1 2 
ATOM   8260  C  CD1 . ILE   B 1  408 ? -10.112 35.038  25.001  1    27.286  ? 408  ILE   B CD1 1 2 
ATOM   8261  N  N   . GLY   B 1  409 ? -11.671 40.292  25.128  1    32.104  ? 409  GLY   B N   1 2 
ATOM   8262  C  CA  . GLY   B 1  409 ? -11.026 41.554  24.79   1    32.775  ? 409  GLY   B CA  1 2 
ATOM   8263  C  C   . GLY   B 1  409 ? -9.936  41.43   23.722  1    33.21   ? 409  GLY   B C   1 2 
ATOM   8264  O  O   . GLY   B 1  409 ? -9.126  42.336  23.609  1    36.166  ? 409  GLY   B O   1 2 
ATOM   8265  N  N   . LEU   B 1  410 ? -9.944  40.367  22.915  1    31.168  ? 410  LEU   B N   1 2 
ATOM   8266  C  CA  . LEU   B 1  410 ? -8.967  40.162  21.849  1    29.693  ? 410  LEU   B CA  1 2 
ATOM   8267  C  C   . LEU   B 1  410 ? -9.511  40.551  20.467  1    31.226  ? 410  LEU   B C   1 2 
ATOM   8268  O  O   . LEU   B 1  410 ? -8.82   40.353  19.477  1    30.723  ? 410  LEU   B O   1 2 
ATOM   8269  C  CB  . LEU   B 1  410 ? -8.5    38.705  21.809  1    26.467  ? 410  LEU   B CB  1 2 
ATOM   8270  C  CG  . LEU   B 1  410 ? -7.73   38.188  23.033  1    26.806  ? 410  LEU   B CG  1 2 
ATOM   8271  C  CD1 . LEU   B 1  410 ? -7.465  36.676  22.903  1    24.237  ? 410  LEU   B CD1 1 2 
ATOM   8272  C  CD2 . LEU   B 1  410 ? -6.421  38.972  23.175  1    25.741  ? 410  LEU   B CD2 1 2 
ATOM   8273  N  N   . LEU   B 1  411 ? -10.756 41.007  20.351  1    33.583  ? 411  LEU   B N   1 2 
ATOM   8274  C  CA  . LEU   B 1  411 ? -11.269 41.333  19.025  1    37      ? 411  LEU   B CA  1 2 
ATOM   8275  C  C   . LEU   B 1  411 ? -12.42  42.32   19.17   1    41.393  ? 411  LEU   B C   1 2 
ATOM   8276  O  O   . LEU   B 1  411 ? -13.25  42.167  20.063  1    42.033  ? 411  LEU   B O   1 2 
ATOM   8277  C  CB  . LEU   B 1  411 ? -11.762 40.042  18.371  1    36.403  ? 411  LEU   B CB  1 2 
ATOM   8278  C  CG  . LEU   B 1  411 ? -12.117 40.093  16.877  1    38.848  ? 411  LEU   B CG  1 2 
ATOM   8279  C  CD1 . LEU   B 1  411 ? -10.899 40.264  15.951  1    38.102  ? 411  LEU   B CD1 1 2 
ATOM   8280  C  CD2 . LEU   B 1  411 ? -12.88  38.821  16.509  1    36.21   ? 411  LEU   B CD2 1 2 
ATOM   8281  N  N   . ASP   B 1  412 ? -12.5   43.314  18.286  1    52.857  ? 412  ASP   B N   1 2 
ATOM   8282  C  CA  . ASP   B 1  412 ? -13.67  44.194  18.312  1    61.045  ? 412  ASP   B CA  1 2 
ATOM   8283  C  C   . ASP   B 1  412 ? -14.805 43.591  17.485  1    66.697  ? 412  ASP   B C   1 2 
ATOM   8284  O  O   . ASP   B 1  412 ? -14.555 43.048  16.402  1    69.602  ? 412  ASP   B O   1 2 
ATOM   8285  C  CB  . ASP   B 1  412 ? -13.269 45.654  18.261  1    68.155  ? 412  ASP   B CB  1 2 
ATOM   8286  C  CG  . ASP   B 1  412 ? -12.512 46.041  19.52   1    79.45   ? 412  ASP   B CG  1 2 
ATOM   8287  O  OD1 . ASP   B 1  412 ? -13.039 45.759  20.626  1    81.724  ? 412  ASP   B OD1 1 2 
ATOM   8288  O  OD2 . ASP   B 1  412 ? -11.377 46.554  19.395  1    87.925  ? 412  ASP   B OD2 1 2 
ATOM   8289  N  N   . ARG   B 1  413 ? -16.03  43.646  18.048  1    63.708  ? 413  ARG   B N   1 2 
ATOM   8290  C  CA  . ARG   B 1  413 ? -17.152 42.794  17.659  1    60.596  ? 413  ARG   B CA  1 2 
ATOM   8291  C  C   . ARG   B 1  413 ? -17.27  42.729  16.134  1    56.949  ? 413  ARG   B C   1 2 
ATOM   8292  O  O   . ARG   B 1  413 ? -17.125 43.745  15.472  1    53.902  ? 413  ARG   B O   1 2 
ATOM   8293  C  CB  . ARG   B 1  413 ? -18.438 43.251  18.36   1    63.05   ? 413  ARG   B CB  1 2 
ATOM   8294  C  CG  . ARG   B 1  413 ? -19.729 42.811  17.677  1    70.554  ? 413  ARG   B CG  1 2 
ATOM   8295  C  CD  . ARG   B 1  413 ? -20.301 41.442  18.037  1    72.574  ? 413  ARG   B CD  1 2 
ATOM   8296  N  NE  . ARG   B 1  413 ? -20.806 41.339  19.415  1    80.192  ? 413  ARG   B NE  1 2 
ATOM   8297  C  CZ  . ARG   B 1  413 ? -21.659 42.177  20.02   1    83.683  ? 413  ARG   B CZ  1 2 
ATOM   8298  N  NH1 . ARG   B 1  413 ? -22.066 41.948  21.257  1    83.818  ? 413  ARG   B NH1 1 2 
ATOM   8299  N  NH2 . ARG   B 1  413 ? -22.111 43.246  19.39   1    85.824  ? 413  ARG   B NH2 1 2 
ATOM   8300  N  N   . VAL   B 1  414 ? -17.487 41.534  15.565  1    55.399  ? 414  VAL   B N   1 2 
ATOM   8301  C  CA  . VAL   B 1  414 ? -17.561 41.439  14.11   1    57.278  ? 414  VAL   B CA  1 2 
ATOM   8302  C  C   . VAL   B 1  414 ? -19.025 41.534  13.702  1    58.371  ? 414  VAL   B C   1 2 
ATOM   8303  O  O   . VAL   B 1  414 ? -19.919 41.218  14.492  1    59.172  ? 414  VAL   B O   1 2 
ATOM   8304  C  CB  . VAL   B 1  414 ? -16.892 40.214  13.438  1    58.302  ? 414  VAL   B CB  1 2 
ATOM   8305  C  CG1 . VAL   B 1  414 ? -15.426 40.073  13.841  1    51.994  ? 414  VAL   B CG1 1 2 
ATOM   8306  C  CG2 . VAL   B 1  414 ? -17.671 38.916  13.662  1    58.208  ? 414  VAL   B CG2 1 2 
ATOM   8307  N  N   . THR   B 1  415 ? -19.272 41.961  12.461  1    59.267  ? 415  THR   B N   1 2 
ATOM   8308  C  CA  . THR   B 1  415 ? -20.656 41.904  12.03   1    64.017  ? 415  THR   B CA  1 2 
ATOM   8309  C  C   . THR   B 1  415 ? -20.946 40.473  11.578  1    57.724  ? 415  THR   B C   1 2 
ATOM   8310  O  O   . THR   B 1  415 ? -20.156 39.882  10.868  1    59.591  ? 415  THR   B O   1 2 
ATOM   8311  C  CB  . THR   B 1  415 ? -21.101 43.025  11.072  1    68.603  ? 415  THR   B CB  1 2 
ATOM   8312  O  OG1 . THR   B 1  415 ? -20.957 42.688  9.692   1    71.602  ? 415  THR   B OG1 1 2 
ATOM   8313  C  CG2 . THR   B 1  415 ? -20.485 44.375  11.403  1    67.116  ? 415  THR   B CG2 1 2 
ATOM   8314  N  N   . ASN   B 1  416 ? -22.05  39.912  12.078  1    56.242  ? 416  ASN   B N   1 2 
ATOM   8315  C  CA  . ASN   B 1  416 ? -22.564 38.599  11.738  1    52.8    ? 416  ASN   B CA  1 2 
ATOM   8316  C  C   . ASN   B 1  416 ? -23.064 38.604  10.286  1    55.021  ? 416  ASN   B C   1 2 
ATOM   8317  O  O   . ASN   B 1  416 ? -24.256 38.505  10.026  1    54.096  ? 416  ASN   B O   1 2 
ATOM   8318  C  CB  . ASN   B 1  416 ? -23.682 38.258  12.717  1    53.582  ? 416  ASN   B CB  1 2 
ATOM   8319  C  CG  . ASN   B 1  416 ? -24.117 36.813  12.676  1    54.784  ? 416  ASN   B CG  1 2 
ATOM   8320  O  OD1 . ASN   B 1  416 ? -23.346 35.933  12.26   1    55.286  ? 416  ASN   B OD1 1 2 
ATOM   8321  N  ND2 . ASN   B 1  416 ? -25.34  36.555  13.125  1    56.279  ? 416  ASN   B ND2 1 2 
ATOM   8322  N  N   . ASP   B 1  417 ? -22.148 38.688  9.316   1    54.256  ? 417  ASP   B N   1 2 
ATOM   8323  C  CA  . ASP   B 1  417 ? -22.54  38.576  7.918   1    53.773  ? 417  ASP   B CA  1 2 
ATOM   8324  C  C   . ASP   B 1  417 ? -21.886 37.346  7.28    1    53.427  ? 417  ASP   B C   1 2 
ATOM   8325  O  O   . ASP   B 1  417 ? -20.974 36.738  7.846   1    49.125  ? 417  ASP   B O   1 2 
ATOM   8326  C  CB  . ASP   B 1  417 ? -22.272 39.885  7.204   1    55.091  ? 417  ASP   B CB  1 2 
ATOM   8327  C  CG  . ASP   B 1  417 ? -20.812 40.256  6.983   1    57.658  ? 417  ASP   B CG  1 2 
ATOM   8328  O  OD1 . ASP   B 1  417 ? -19.892 39.514  7.434   1    53.118  ? 417  ASP   B OD1 1 2 
ATOM   8329  O  OD2 . ASP   B 1  417 ? -20.598 41.283  6.321   1    58.6    ? 417  ASP   B OD2 1 2 
ATOM   8330  N  N   . THR   B 1  418 ? -22.352 36.987  6.079   1    52.936  ? 418  THR   B N   1 2 
ATOM   8331  C  CA  . THR   B 1  418 ? -21.883 35.768  5.421   1    51.701  ? 418  THR   B CA  1 2 
ATOM   8332  C  C   . THR   B 1  418 ? -20.381 35.801  5.11    1    46.208  ? 418  THR   B C   1 2 
ATOM   8333  O  O   . THR   B 1  418 ? -19.736 34.741  5.182   1    42.453  ? 418  THR   B O   1 2 
ATOM   8334  C  CB  . THR   B 1  418 ? -22.77  35.427  4.219   1    55.015  ? 418  THR   B CB  1 2 
ATOM   8335  O  OG1 . THR   B 1  418 ? -22.404 36.434  3.281   1    58.873  ? 418  THR   B OG1 1 2 
ATOM   8336  C  CG2 . THR   B 1  418 ? -24.256 35.479  4.552   1    50.768  ? 418  THR   B CG2 1 2 
ATOM   8337  N  N   . GLU   B 1  419 ? -19.808 36.993  4.836   1    44.039  ? 419  GLU   B N   1 2 
ATOM   8338  C  CA  . GLU   B 1  419 ? -18.364 37.098  4.59    1    44.693  ? 419  GLU   B CA  1 2 
ATOM   8339  C  C   . GLU   B 1  419 ? -17.5   36.82   5.829   1    43.227  ? 419  GLU   B C   1 2 
ATOM   8340  O  O   . GLU   B 1  419 ? -16.428 36.199  5.72    1    40.397  ? 419  GLU   B O   1 2 
ATOM   8341  C  CB  . GLU   B 1  419 ? -17.92  38.454  4.049   1    47.853  ? 419  GLU   B CB  1 2 
ATOM   8342  C  CG  . GLU   B 1  419 ? -18.539 38.77   2.684   1    56.994  ? 419  GLU   B CG  1 2 
ATOM   8343  C  CD  . GLU   B 1  419 ? -18.266 40.177  2.18    1    62.537  ? 419  GLU   B CD  1 2 
ATOM   8344  O  OE1 . GLU   B 1  419 ? -17.437 40.896  2.787   1    66.181  ? 419  GLU   B OE1 1 2 
ATOM   8345  O  OE2 . GLU   B 1  419 ? -18.887 40.551  1.16    1    70.606  ? 419  GLU   B OE2 1 2 
ATOM   8346  N  N   . SER   B 1  420 ? -17.914 37.348  6.999   1    44.113  ? 420  SER   B N   1 2 
ATOM   8347  C  CA  . SER   B 1  420 ? -17.21  37.046  8.241   1    41.994  ? 420  SER   B CA  1 2 
ATOM   8348  C  C   . SER   B 1  420 ? -17.315 35.554  8.544   1    37.647  ? 420  SER   B C   1 2 
ATOM   8349  O  O   . SER   B 1  420 ? -16.34  34.957  8.985   1    37.017  ? 420  SER   B O   1 2 
ATOM   8350  C  CB  . SER   B 1  420 ? -17.751 37.859  9.397   1    43.614  ? 420  SER   B CB  1 2 
ATOM   8351  O  OG  . SER   B 1  420 ? -17.793 39.239  9.069   1    46.284  ? 420  SER   B OG  1 2 
ATOM   8352  N  N   . ASP   B 1  421 ? -18.512 34.969  8.344   1    40.136  ? 421  ASP   B N   1 2 
ATOM   8353  C  CA  . ASP   B 1  421 ? -18.682 33.523  8.469   1    42.142  ? 421  ASP   B CA  1 2 
ATOM   8354  C  C   . ASP   B 1  421 ? -17.608 32.828  7.639   1    38.707  ? 421  ASP   B C   1 2 
ATOM   8355  O  O   . ASP   B 1  421 ? -16.823 32.024  8.168   1    37.425  ? 421  ASP   B O   1 2 
ATOM   8356  C  CB  . ASP   B 1  421 ? -20.075 33.009  8.114   1    50.338  ? 421  ASP   B CB  1 2 
ATOM   8357  C  CG  . ASP   B 1  421 ? -21.003 32.644  9.271   1    61.713  ? 421  ASP   B CG  1 2 
ATOM   8358  O  OD1 . ASP   B 1  421 ? -20.477 32.301  10.367  1    65.563  ? 421  ASP   B OD1 1 2 
ATOM   8359  O  OD2 . ASP   B 1  421 ? -22.253 32.752  9.088   1    65.188  ? 421  ASP   B OD2 1 2 
ATOM   8360  N  N   . ILE   B 1  422 ? -17.543 33.174  6.35    1    37.789  ? 422  ILE   B N   1 2 
ATOM   8361  C  CA  . ILE   B 1  422 ? -16.625 32.472  5.464   1    36.591  ? 422  ILE   B CA  1 2 
ATOM   8362  C  C   . ILE   B 1  422 ? -15.176 32.618  5.947   1    33.194  ? 422  ILE   B C   1 2 
ATOM   8363  O  O   . ILE   B 1  422 ? -14.433 31.622  5.946   1    30.429  ? 422  ILE   B O   1 2 
ATOM   8364  C  CB  . ILE   B 1  422 ? -16.793 32.839  3.977   1    37.965  ? 422  ILE   B CB  1 2 
ATOM   8365  C  CG1 . ILE   B 1  422 ? -18.166 32.466  3.424   1    42.205  ? 422  ILE   B CG1 1 2 
ATOM   8366  C  CG2 . ILE   B 1  422 ? -15.696 32.174  3.163   1    37.327  ? 422  ILE   B CG2 1 2 
ATOM   8367  C  CD1 . ILE   B 1  422 ? -18.66  31.081  3.803   1    41.538  ? 422  ILE   B CD1 1 2 
ATOM   8368  N  N   . ASN   B 1  423 ? -14.758 33.841  6.323   1    32.444  ? 423  ASN   B N   1 2 
ATOM   8369  C  CA  . ASN   B 1  423 ? -13.384 34.073  6.757   1    31.35   ? 423  ASN   B CA  1 2 
ATOM   8370  C  C   . ASN   B 1  423 ? -13.039 33.225  7.987   1    29.488  ? 423  ASN   B C   1 2 
ATOM   8371  O  O   . ASN   B 1  423 ? -11.938 32.645  8.083   1    28.476  ? 423  ASN   B O   1 2 
ATOM   8372  C  CB  . ASN   B 1  423 ? -13.114 35.497  7.212   1    33.705  ? 423  ASN   B CB  1 2 
ATOM   8373  C  CG  . ASN   B 1  423 ? -12.697 36.445  6.113   1    34.993  ? 423  ASN   B CG  1 2 
ATOM   8374  O  OD1 . ASN   B 1  423 ? -12.549 36.035  4.953   1    33.96   ? 423  ASN   B OD1 1 2 
ATOM   8375  N  ND2 . ASN   B 1  423 ? -12.477 37.704  6.479   1    35.299  ? 423  ASN   B ND2 1 2 
ATOM   8376  N  N   . TYR   B 1  424 ? -13.989 33.129  8.921   1    29.746  ? 424  TYR   B N   1 2 
ATOM   8377  C  CA  . TYR   B 1  424 ? -13.763 32.379  10.157  1    28.915  ? 424  TYR   B CA  1 2 
ATOM   8378  C  C   . TYR   B 1  424 ? -13.658 30.887  9.828   1    26.407  ? 424  TYR   B C   1 2 
ATOM   8379  O  O   . TYR   B 1  424 ? -12.737 30.186  10.301  1    25.39   ? 424  TYR   B O   1 2 
ATOM   8380  C  CB  . TYR   B 1  424 ? -14.784 32.699  11.261  1    29.014  ? 424  TYR   B CB  1 2 
ATOM   8381  C  CG  . TYR   B 1  424 ? -14.673 31.763  12.46   1    27.515  ? 424  TYR   B CG  1 2 
ATOM   8382  C  CD1 . TYR   B 1  424 ? -13.576 31.818  13.305  1    27.46   ? 424  TYR   B CD1 1 2 
ATOM   8383  C  CD2 . TYR   B 1  424 ? -15.652 30.82   12.746  1    28.041  ? 424  TYR   B CD2 1 2 
ATOM   8384  C  CE1 . TYR   B 1  424 ? -13.462 30.979  14.409  1    27.479  ? 424  TYR   B CE1 1 2 
ATOM   8385  C  CE2 . TYR   B 1  424 ? -15.569 30.003  13.869  1    28.436  ? 424  TYR   B CE2 1 2 
ATOM   8386  C  CZ  . TYR   B 1  424 ? -14.446 30.05   14.683  1    28.167  ? 424  TYR   B CZ  1 2 
ATOM   8387  O  OH  . TYR   B 1  424 ? -14.313 29.22   15.775  1    26.307  ? 424  TYR   B OH  1 2 
ATOM   8388  N  N   . LEU   B 1  425 ? -14.588 30.4    9.008   1    27.026  ? 425  LEU   B N   1 2 
ATOM   8389  C  CA  . LEU   B 1  425 ? -14.634 28.973  8.707   1    26.505  ? 425  LEU   B CA  1 2 
ATOM   8390  C  C   . LEU   B 1  425 ? -13.389 28.538  7.949   1    25.96   ? 425  LEU   B C   1 2 
ATOM   8391  O  O   . LEU   B 1  425 ? -12.912 27.397  8.065   1    23.734  ? 425  LEU   B O   1 2 
ATOM   8392  C  CB  . LEU   B 1  425 ? -15.93  28.553  8.018   1    28.365  ? 425  LEU   B CB  1 2 
ATOM   8393  C  CG  . LEU   B 1  425 ? -17.132 28.463  8.964   1    30.034  ? 425  LEU   B CG  1 2 
ATOM   8394  C  CD1 . LEU   B 1  425 ? -18.444 28.296  8.246   1    32.651  ? 425  LEU   B CD1 1 2 
ATOM   8395  C  CD2 . LEU   B 1  425 ? -16.976 27.468  10.079  1    28.781  ? 425  LEU   B CD2 1 2 
ATOM   8396  N  N   . LEU   B 1  426 ? -12.841 29.474  7.184   1    26.036  ? 426  LEU   B N   1 2 
ATOM   8397  C  CA  . LEU   B 1  426 ? -11.67  29.149  6.389   1    25.308  ? 426  LEU   B CA  1 2 
ATOM   8398  C  C   . LEU   B 1  426 ? -10.473 29.079  7.333   1    23.565  ? 426  LEU   B C   1 2 
ATOM   8399  O  O   . LEU   B 1  426 ? -9.639  28.199  7.212   1    21.517  ? 426  LEU   B O   1 2 
ATOM   8400  C  CB  . LEU   B 1  426 ? -11.513 30.229  5.324   1    26.797  ? 426  LEU   B CB  1 2 
ATOM   8401  C  CG  . LEU   B 1  426 ? -10.448 30.003  4.249   1    27.211  ? 426  LEU   B CG  1 2 
ATOM   8402  C  CD1 . LEU   B 1  426 ? -9.127  30.363  4.903   1    26.397  ? 426  LEU   B CD1 1 2 
ATOM   8403  C  CD2 . LEU   B 1  426 ? -10.39  28.582  3.626   1    25.994  ? 426  LEU   B CD2 1 2 
ATOM   8404  N  N   . LYS   B 1  427 ? -10.356 30.017  8.258   1    23.032  ? 427  LYS   B N   1 2 
ATOM   8405  C  CA  . LYS   B 1  427 ? -9.274  29.919  9.233   1    23.033  ? 427  LYS   B CA  1 2 
ATOM   8406  C  C   . LYS   B 1  427 ? -9.341  28.582  9.983   1    20.733  ? 427  LYS   B C   1 2 
ATOM   8407  O  O   . LYS   B 1  427 ? -8.313  27.937  10.192  1    19.444  ? 427  LYS   B O   1 2 
ATOM   8408  C  CB  . LYS   B 1  427 ? -9.274  31.158  10.145  1    24.596  ? 427  LYS   B CB  1 2 
ATOM   8409  C  CG  . LYS   B 1  427 ? -8.051  31.245  11.086  1    25.548  ? 427  LYS   B CG  1 2 
ATOM   8410  C  CD  . LYS   B 1  427 ? -8.155  32.48   11.978  1    28.664  ? 427  LYS   B CD  1 2 
ATOM   8411  C  CE  . LYS   B 1  427 ? -6.86   32.693  12.656  1    30.927  ? 427  LYS   B CE  1 2 
ATOM   8412  N  NZ  . LYS   B 1  427 ? -6.652  31.508  13.494  1    35.977  ? 427  LYS   B NZ  1 2 
ATOM   8413  N  N   . MET   B 1  428 ? -10.556 28.173  10.375  1    20.32   ? 428  MET   B N   1 2 
ATOM   8414  C  CA  . MET   B 1  428 ? -10.779 26.93   11.118  1    21.183  ? 428  MET   B CA  1 2 
ATOM   8415  C  C   . MET   B 1  428 ? -10.457 25.741  10.213  1    21.44   ? 428  MET   B C   1 2 
ATOM   8416  O  O   . MET   B 1  428 ? -9.925  24.723  10.663  1    20.739  ? 428  MET   B O   1 2 
ATOM   8417  C  CB  . MET   B 1  428 ? -12.21  26.891  11.694  1    22.099  ? 428  MET   B CB  1 2 
ATOM   8418  C  CG  . MET   B 1  428 ? -12.465 27.932  12.82   1    25.427  ? 428  MET   B CG  1 2 
ATOM   8419  S  SD  . MET   B 1  428 ? -11.221 27.881  14.143  1    27.837  ? 428  MET   B SD  1 2 
ATOM   8420  C  CE  . MET   B 1  428 ? -11.249 26.138  14.585  1    22.955  ? 428  MET   B CE  1 2 
ATOM   8421  N  N   . ALA   B 1  429 ? -10.7   25.882  8.896   1    20.091  ? 429  ALA   B N   1 2 
ATOM   8422  C  CA  . ALA   B 1  429 ? -10.363 24.793  7.992   1    18.911  ? 429  ALA   B CA  1 2 
ATOM   8423  C  C   . ALA   B 1  429 ? -8.834  24.618  7.905   1    18.664  ? 429  ALA   B C   1 2 
ATOM   8424  O  O   . ALA   B 1  429 ? -8.372  23.477  7.827   1    17.971  ? 429  ALA   B O   1 2 
ATOM   8425  C  CB  . ALA   B 1  429 ? -10.92  25.058  6.63    1    19.953  ? 429  ALA   B CB  1 2 
ATOM   8426  N  N   . LEU   B 1  430 ? -8.065  25.727  7.871   1    18.488  ? 430  LEU   B N   1 2 
ATOM   8427  C  CA  . LEU   B 1  430 ? -6.605  25.666  7.781   1    19.732  ? 430  LEU   B CA  1 2 
ATOM   8428  C  C   . LEU   B 1  430 ? -6.02   24.901  8.968   1    20.014  ? 430  LEU   B C   1 2 
ATOM   8429  O  O   . LEU   B 1  430 ? -4.971  24.227  8.872   1    18.355  ? 430  LEU   B O   1 2 
ATOM   8430  C  CB  . LEU   B 1  430 ? -6.065  27.1    7.731   1    20.459  ? 430  LEU   B CB  1 2 
ATOM   8431  C  CG  . LEU   B 1  430 ? -6.344  27.908  6.445   1    22.225  ? 430  LEU   B CG  1 2 
ATOM   8432  C  CD1 . LEU   B 1  430 ? -5.837  29.356  6.56    1    22.794  ? 430  LEU   B CD1 1 2 
ATOM   8433  C  CD2 . LEU   B 1  430 ? -5.73   27.209  5.224   1    22.412  ? 430  LEU   B CD2 1 2 
ATOM   8434  N  N   . GLU   B 1  431 ? -6.712  25.008  10.108  1    20.515  ? 431  GLU   B N   1 2 
ATOM   8435  C  CA  . GLU   B 1  431 ? -6.255  24.325  11.311  1    22.577  ? 431  GLU   B CA  1 2 
ATOM   8436  C  C   . GLU   B 1  431 ? -6.731  22.866  11.399  1    21.03   ? 431  GLU   B C   1 2 
ATOM   8437  O  O   . GLU   B 1  431 ? -5.95   21.983  11.72   1    20.535  ? 431  GLU   B O   1 2 
ATOM   8438  C  CB  . GLU   B 1  431 ? -6.655  25.231  12.482  1    24.112  ? 431  GLU   B CB  1 2 
ATOM   8439  C  CG  . GLU   B 1  431 ? -6.254  24.561  13.783  1    30.021  ? 431  GLU   B CG  1 2 
ATOM   8440  C  CD  . GLU   B 1  431 ? -6.816  25.394  14.924  1    37.087  ? 431  GLU   B CD  1 2 
ATOM   8441  O  OE1 . GLU   B 1  431 ? -6.857  24.787  16.016  1    33.535  ? 431  GLU   B OE1 1 2 
ATOM   8442  O  OE2 . GLU   B 1  431 ? -7.24   26.575  14.721  1    36.423  ? 431  GLU   B OE2 1 2 
ATOM   8443  N  N   . LYS   B 1  432 ? -7.999  22.588  11.07   1    18.055  ? 432  LYS   B N   1 2 
ATOM   8444  C  CA  . LYS   B 1  432 ? -8.656  21.328  11.353  1    17.83   ? 432  LYS   B CA  1 2 
ATOM   8445  C  C   . LYS   B 1  432 ? -8.703  20.421  10.114  1    18.976  ? 432  LYS   B C   1 2 
ATOM   8446  O  O   . LYS   B 1  432 ? -8.345  19.248  10.248  1    20.966  ? 432  LYS   B O   1 2 
ATOM   8447  C  CB  . LYS   B 1  432 ? -10.095 21.55   11.858  1    18.683  ? 432  LYS   B CB  1 2 
ATOM   8448  C  CG  . LYS   B 1  432 ? -10.17  22.425  13.136  1    20.489  ? 432  LYS   B CG  1 2 
ATOM   8449  C  CD  . LYS   B 1  432 ? -9.489  21.788  14.361  1    20.514  ? 432  LYS   B CD  1 2 
ATOM   8450  C  CE  . LYS   B 1  432 ? -9.566  22.641  15.679  1    20.846  ? 432  LYS   B CE  1 2 
ATOM   8451  N  NZ  . LYS   B 1  432 ? -8.933  21.795  16.731  1    21.461  ? 432  LYS   B NZ  1 2 
ATOM   8452  N  N   A ILE   B 1  433 ? -9.12   20.948  8.948   0.52 17.298  ? 433  ILE   B N   1 2 
ATOM   8453  N  N   B ILE   B 1  433 ? -9.131  20.966  8.956   0.48 17.569  ? 433  ILE   B N   1 2 
ATOM   8454  C  CA  A ILE   B 1  433 ? -9.213  20.095  7.765   0.52 16.561  ? 433  ILE   B CA  1 2 
ATOM   8455  C  CA  B ILE   B 1  433 ? -9.22   20.183  7.725   0.48 17.047  ? 433  ILE   B CA  1 2 
ATOM   8456  C  C   A ILE   B 1  433 ? -7.815  19.808  7.205   0.52 16.083  ? 433  ILE   B C   1 2 
ATOM   8457  C  C   B ILE   B 1  433 ? -7.82   19.819  7.238   0.48 16.32   ? 433  ILE   B C   1 2 
ATOM   8458  O  O   A ILE   B 1  433 ? -7.571  18.688  6.745   0.52 16.024  ? 433  ILE   B O   1 2 
ATOM   8459  O  O   B ILE   B 1  433 ? -7.587  18.671  6.853   0.48 16.297  ? 433  ILE   B O   1 2 
ATOM   8460  C  CB  A ILE   B 1  433 ? -10.144 20.697  6.7     0.52 16.861  ? 433  ILE   B CB  1 2 
ATOM   8461  C  CB  B ILE   B 1  433 ? -9.979  20.942  6.623   0.48 17.474  ? 433  ILE   B CB  1 2 
ATOM   8462  C  CG1 A ILE   B 1  433 ? -11.556 20.912  7.283   0.52 16.755  ? 433  ILE   B CG1 1 2 
ATOM   8463  C  CG1 B ILE   B 1  433 ? -11.399 21.225  7.088   0.48 17.959  ? 433  ILE   B CG1 1 2 
ATOM   8464  C  CG2 A ILE   B 1  433 ? -10.168 19.822  5.436   0.52 16.786  ? 433  ILE   B CG2 1 2 
ATOM   8465  C  CG2 B ILE   B 1  433 ? -9.97   20.123  5.323   0.48 17.491  ? 433  ILE   B CG2 1 2 
ATOM   8466  C  CD1 A ILE   B 1  433 ? -12.549 21.562  6.34    0.52 17.275  ? 433  ILE   B CD1 1 2 
ATOM   8467  C  CD1 B ILE   B 1  433 ? -12.092 19.976  7.583   0.48 18.244  ? 433  ILE   B CD1 1 2 
ATOM   8468  N  N   . ALA   B 1  434 ? -6.921  20.804  7.199   1    15.177  ? 434  ALA   B N   1 2 
ATOM   8469  C  CA  . ALA   B 1  434 ? -5.589  20.561  6.656   1    16.604  ? 434  ALA   B CA  1 2 
ATOM   8470  C  C   . ALA   B 1  434 ? -4.865  19.443  7.425   1    16.272  ? 434  ALA   B C   1 2 
ATOM   8471  O  O   . ALA   B 1  434 ? -4.103  18.703  6.82    1    17.373  ? 434  ALA   B O   1 2 
ATOM   8472  C  CB  . ALA   B 1  434 ? -4.749  21.823  6.591   1    17.066  ? 434  ALA   B CB  1 2 
ATOM   8473  N  N   . PHE   B 1  435 ? -5.171  19.269  8.717   1    14.834  ? 435  PHE   B N   1 2 
ATOM   8474  C  CA  . PHE   B 1  435 ? -4.552  18.298  9.586   1    14.376  ? 435  PHE   B CA  1 2 
ATOM   8475  C  C   . PHE   B 1  435 ? -4.967  16.876  9.256   1    15.349  ? 435  PHE   B C   1 2 
ATOM   8476  O  O   . PHE   B 1  435 ? -4.173  15.934  9.382   1    15.506  ? 435  PHE   B O   1 2 
ATOM   8477  C  CB  . PHE   B 1  435 ? -4.891  18.564  11.054  1    15.384  ? 435  PHE   B CB  1 2 
ATOM   8478  C  CG  . PHE   B 1  435 ? -4.201  17.51   11.919  1    14.932  ? 435  PHE   B CG  1 2 
ATOM   8479  C  CD1 . PHE   B 1  435 ? -2.828  17.645  12.2    1    14.997  ? 435  PHE   B CD1 1 2 
ATOM   8480  C  CD2 . PHE   B 1  435 ? -4.912  16.451  12.45   1    15.231  ? 435  PHE   B CD2 1 2 
ATOM   8481  C  CE1 . PHE   B 1  435 ? -2.18   16.705  13.036  1    15.869  ? 435  PHE   B CE1 1 2 
ATOM   8482  C  CE2 . PHE   B 1  435 ? -4.301  15.511  13.293  1    15.909  ? 435  PHE   B CE2 1 2 
ATOM   8483  C  CZ  . PHE   B 1  435 ? -2.909  15.633  13.565  1    14.629  ? 435  PHE   B CZ  1 2 
ATOM   8484  N  N   . LEU   B 1  436 ? -6.201  16.72   8.76    1    16.205  ? 436  LEU   B N   1 2 
ATOM   8485  C  CA  . LEU   B 1  436 ? -6.719  15.373  8.643   1    17.194  ? 436  LEU   B CA  1 2 
ATOM   8486  C  C   . LEU   B 1  436 ? -5.812  14.395  7.888   1    15.934  ? 436  LEU   B C   1 2 
ATOM   8487  O  O   . LEU   B 1  436 ? -5.608  13.285  8.395   1    14.54   ? 436  LEU   B O   1 2 
ATOM   8488  C  CB  . LEU   B 1  436 ? -8.109  15.431  8.028   1    17.79   ? 436  LEU   B CB  1 2 
ATOM   8489  C  CG  . LEU   B 1  436 ? -9.162  16.083  8.934   1    17.473  ? 436  LEU   B CG  1 2 
ATOM   8490  C  CD1 . LEU   B 1  436 ? -10.431 16.244  8.085   1    18.886  ? 436  LEU   B CD1 1 2 
ATOM   8491  C  CD2 . LEU   B 1  436 ? -9.408  15.348  10.273  1    17.863  ? 436  LEU   B CD2 1 2 
ATOM   8492  N  N   . PRO   B 1  437 ? -5.349  14.67   6.638   1    15.613  ? 437  PRO   B N   1 2 
ATOM   8493  C  CA  . PRO   B 1  437 ? -4.549  13.676  5.937   1    15.375  ? 437  PRO   B CA  1 2 
ATOM   8494  C  C   . PRO   B 1  437 ? -3.297  13.362  6.76    1    14.858  ? 437  PRO   B C   1 2 
ATOM   8495  O  O   . PRO   B 1  437 ? -2.803  12.247  6.755   1    16.233  ? 437  PRO   B O   1 2 
ATOM   8496  C  CB  . PRO   B 1  437 ? -4.235  14.286  4.559   1    16.524  ? 437  PRO   B CB  1 2 
ATOM   8497  C  CG  . PRO   B 1  437 ? -4.524  15.777  4.724   1    16.489  ? 437  PRO   B CG  1 2 
ATOM   8498  C  CD  . PRO   B 1  437 ? -5.625  15.854  5.797   1    16.462  ? 437  PRO   B CD  1 2 
ATOM   8499  N  N   . PHE   B 1  438 ? -2.754  14.304  7.49    1    13.368  ? 438  PHE   B N   1 2 
ATOM   8500  C  CA  . PHE   B 1  438 ? -1.47   13.986  8.123   1    13.426  ? 438  PHE   B CA  1 2 
ATOM   8501  C  C   . PHE   B 1  438 ? -1.747  13.157  9.375   1    14.231  ? 438  PHE   B C   1 2 
ATOM   8502  O  O   . PHE   B 1  438 ? -1.06   12.172  9.639   1    14.824  ? 438  PHE   B O   1 2 
ATOM   8503  C  CB  . PHE   B 1  438 ? -0.868  15.288  8.648   1    12.576  ? 438  PHE   B CB  1 2 
ATOM   8504  C  CG  . PHE   B 1  438 ? 0.476   15.083  9.341   1    14.716  ? 438  PHE   B CG  1 2 
ATOM   8505  C  CD1 . PHE   B 1  438 ? 1.602   14.774  8.579   1    16.298  ? 438  PHE   B CD1 1 2 
ATOM   8506  C  CD2 . PHE   B 1  438 ? 0.608   15.25   10.724  1    14.692  ? 438  PHE   B CD2 1 2 
ATOM   8507  C  CE1 . PHE   B 1  438 ? 2.872   14.621  9.191   1    16.774  ? 438  PHE   B CE1 1 2 
ATOM   8508  C  CE2 . PHE   B 1  438 ? 1.874   15.103  11.313  1    16.806  ? 438  PHE   B CE2 1 2 
ATOM   8509  C  CZ  . PHE   B 1  438 ? 2.982   14.787  10.556  1    15.963  ? 438  PHE   B CZ  1 2 
ATOM   8510  N  N   . GLY   B 1  439 ? -2.832  13.537  10.084  1    14.164  ? 439  GLY   B N   1 2 
ATOM   8511  C  CA  . GLY   B 1  439 ? -3.331  12.736  11.194  1    14.115  ? 439  GLY   B CA  1 2 
ATOM   8512  C  C   . GLY   B 1  439 ? -3.544  11.282  10.788  1    16.211  ? 439  GLY   B C   1 2 
ATOM   8513  O  O   . GLY   B 1  439 ? -3.307  10.389  11.594  1    15.765  ? 439  GLY   B O   1 2 
ATOM   8514  N  N   . TYR   B 1  440 ? -4.099  11.048  9.586   1    15.068  ? 440  TYR   B N   1 2 
ATOM   8515  C  CA  . TYR   B 1  440 ? -4.342  9.683   9.128   1    15.893  ? 440  TYR   B CA  1 2 
ATOM   8516  C  C   . TYR   B 1  440 ? -3.04   8.981   8.712   1    16.752  ? 440  TYR   B C   1 2 
ATOM   8517  O  O   . TYR   B 1  440 ? -2.89   7.785   9.005   1    18.773  ? 440  TYR   B O   1 2 
ATOM   8518  C  CB  . TYR   B 1  440 ? -5.314  9.802   7.952   1    17.21   ? 440  TYR   B CB  1 2 
ATOM   8519  C  CG  . TYR   B 1  440 ? -5.901  8.489   7.467   1    19.998  ? 440  TYR   B CG  1 2 
ATOM   8520  C  CD1 . TYR   B 1  440 ? -6.138  7.425   8.338   1    24.455  ? 440  TYR   B CD1 1 2 
ATOM   8521  C  CD2 . TYR   B 1  440 ? -6.23   8.31    6.142   1    22.909  ? 440  TYR   B CD2 1 2 
ATOM   8522  C  CE1 . TYR   B 1  440 ? -6.712  6.236   7.915   1    25.034  ? 440  TYR   B CE1 1 2 
ATOM   8523  C  CE2 . TYR   B 1  440 ? -6.832  7.134   5.696   1    24.281  ? 440  TYR   B CE2 1 2 
ATOM   8524  C  CZ  . TYR   B 1  440 ? -7.049  6.092   6.583   1    24.567  ? 440  TYR   B CZ  1 2 
ATOM   8525  O  OH  . TYR   B 1  440 ? -7.567  4.919   6.126   1    25.482  ? 440  TYR   B OH  1 2 
ATOM   8526  N  N   . LEU   B 1  441 ? -2.089  9.682   8.041   1    15.396  ? 441  LEU   B N   1 2 
ATOM   8527  C  CA  . LEU   B 1  441 ? -1.038  8.925   7.34    1    14.672  ? 441  LEU   B CA  1 2 
ATOM   8528  C  C   . LEU   B 1  441 ? 0.111   8.483   8.257   1    15.031  ? 441  LEU   B C   1 2 
ATOM   8529  O  O   . LEU   B 1  441 ? 0.85    7.528   7.964   1    14.291  ? 441  LEU   B O   1 2 
ATOM   8530  C  CB  . LEU   B 1  441 ? -0.512  9.815   6.201   1    15.018  ? 441  LEU   B CB  1 2 
ATOM   8531  C  CG  . LEU   B 1  441 ? 0.383   11.014  6.537   1    14.774  ? 441  LEU   B CG  1 2 
ATOM   8532  C  CD1 . LEU   B 1  441 ? 1.851   10.573  6.739   1    15.273  ? 441  LEU   B CD1 1 2 
ATOM   8533  C  CD2 . LEU   B 1  441 ? 0.29    12      5.342   1    14.246  ? 441  LEU   B CD2 1 2 
ATOM   8534  N  N   . VAL   B 1  442 ? 0.357   9.224   9.341   1    13.776  ? 442  VAL   B N   1 2 
ATOM   8535  C  CA  . VAL   B 1  442 ? 1.524   8.946   10.177  1    14.654  ? 442  VAL   B CA  1 2 
ATOM   8536  C  C   . VAL   B 1  442 ? 1.531   7.505   10.672  1    14.884  ? 442  VAL   B C   1 2 
ATOM   8537  O  O   . VAL   B 1  442 ? 2.56    6.817   10.607  1    16.838  ? 442  VAL   B O   1 2 
ATOM   8538  C  CB  . VAL   B 1  442 ? 1.686   9.936   11.356  1    14.692  ? 442  VAL   B CB  1 2 
ATOM   8539  C  CG1 . VAL   B 1  442 ? 2.84    9.506   12.273  1    15.099  ? 442  VAL   B CG1 1 2 
ATOM   8540  C  CG2 . VAL   B 1  442 ? 1.905   11.376  10.876  1    13.726  ? 442  VAL   B CG2 1 2 
ATOM   8541  N  N   . ASP   B 1  443 ? 0.4     7.052   11.249  1    14.76   ? 443  ASP   B N   1 2 
ATOM   8542  C  CA  . ASP   B 1  443 ? 0.375   5.701   11.75   1    15.792  ? 443  ASP   B CA  1 2 
ATOM   8543  C  C   . ASP   B 1  443 ? 0.171   4.721   10.597  1    16.089  ? 443  ASP   B C   1 2 
ATOM   8544  O  O   . ASP   B 1  443 ? 0.635   3.596   10.715  1    17.905  ? 443  ASP   B O   1 2 
ATOM   8545  C  CB  . ASP   B 1  443 ? -0.557  5.517   12.958  1    18.027  ? 443  ASP   B CB  1 2 
ATOM   8546  C  CG  . ASP   B 1  443 ? 0.077   5.868   14.31   1    18.876  ? 443  ASP   B CG  1 2 
ATOM   8547  O  OD1 . ASP   B 1  443 ? 1.283   6.263   14.346  1    19.155  ? 443  ASP   B OD1 1 2 
ATOM   8548  O  OD2 . ASP   B 1  443 ? -0.625  5.716   15.341  1    19.882  ? 443  ASP   B OD2 1 2 
ATOM   8549  N  N   . GLN   B 1  444 ? -0.342  5.14    9.434   1    15.858  ? 444  GLN   B N   1 2 
ATOM   8550  C  CA  . GLN   B 1  444 ? -0.234  4.221   8.277   1    16.601  ? 444  GLN   B CA  1 2 
ATOM   8551  C  C   . GLN   B 1  444 ? 1.241   3.915   7.964   1    16.966  ? 444  GLN   B C   1 2 
ATOM   8552  O  O   . GLN   B 1  444 ? 1.62    2.761   7.783   1    18.242  ? 444  GLN   B O   1 2 
ATOM   8553  C  CB  . GLN   B 1  444 ? -0.941  4.805   7.07    1    18.134  ? 444  GLN   B CB  1 2 
ATOM   8554  C  CG  . GLN   B 1  444 ? -2.455  4.725   7.251   1    24.064  ? 444  GLN   B CG  1 2 
ATOM   8555  C  CD  . GLN   B 1  444 ? -3.153  4.911   5.934   1    31.475  ? 444  GLN   B CD  1 2 
ATOM   8556  O  OE1 . GLN   B 1  444 ? -3.03   4.086   5.009   1    35.685  ? 444  GLN   B OE1 1 2 
ATOM   8557  N  NE2 . GLN   B 1  444 ? -3.832  6.048   5.828   1    30.545  ? 444  GLN   B NE2 1 2 
ATOM   8558  N  N   . TRP   B 1  445 ? 2.095   4.924   8.004   1    15.923  ? 445  TRP   B N   1 2 
ATOM   8559  C  CA  . TRP   B 1  445 ? 3.515   4.661   7.833   1    16.017  ? 445  TRP   B CA  1 2 
ATOM   8560  C  C   . TRP   B 1  445 ? 4.028   3.717   8.932   1    16.912  ? 445  TRP   B C   1 2 
ATOM   8561  O  O   . TRP   B 1  445 ? 4.661   2.657   8.688   1    16.849  ? 445  TRP   B O   1 2 
ATOM   8562  C  CB  . TRP   B 1  445 ? 4.268   5.991   7.783   1    15.457  ? 445  TRP   B CB  1 2 
ATOM   8563  C  CG  . TRP   B 1  445 ? 5.761   5.768   7.598   1    17.401  ? 445  TRP   B CG  1 2 
ATOM   8564  C  CD1 . TRP   B 1  445 ? 6.404   5.471   6.429   1    17.578  ? 445  TRP   B CD1 1 2 
ATOM   8565  C  CD2 . TRP   B 1  445 ? 6.771   5.723   8.628   1    17.543  ? 445  TRP   B CD2 1 2 
ATOM   8566  N  NE1 . TRP   B 1  445 ? 7.755   5.291   6.652   1    17.781  ? 445  TRP   B NE1 1 2 
ATOM   8567  C  CE2 . TRP   B 1  445 ? 8.009   5.46    7.989   1    18.139  ? 445  TRP   B CE2 1 2 
ATOM   8568  C  CE3 . TRP   B 1  445 ? 6.747   5.913   10.015  1    18.347  ? 445  TRP   B CE3 1 2 
ATOM   8569  C  CZ2 . TRP   B 1  445 ? 9.206   5.298   8.686   1    18.263  ? 445  TRP   B CZ2 1 2 
ATOM   8570  C  CZ3 . TRP   B 1  445 ? 7.943   5.779   10.704  1    18.1    ? 445  TRP   B CZ3 1 2 
ATOM   8571  C  CH2 . TRP   B 1  445 ? 9.143   5.469   10.057  1    19.058  ? 445  TRP   B CH2 1 2 
ATOM   8572  N  N   . ARG   B 1  446 ? 3.726   4.075   10.198  1    17.123  ? 446  ARG   B N   1 2 
ATOM   8573  C  CA  . ARG   B 1  446 ? 4.332   3.32    11.277  1    18.75   ? 446  ARG   B CA  1 2 
ATOM   8574  C  C   . ARG   B 1  446 ? 3.736   1.924   11.398  1    18.847  ? 446  ARG   B C   1 2 
ATOM   8575  O  O   . ARG   B 1  446 ? 4.471   1.001   11.733  1    19.666  ? 446  ARG   B O   1 2 
ATOM   8576  C  CB  . ARG   B 1  446 ? 4.303   4.165   12.562  1    18.532  ? 446  ARG   B CB  1 2 
ATOM   8577  C  CG  . ARG   B 1  446 ? 4.943   3.691   13.845  1    21.52   ? 446  ARG   B CG  1 2 
ATOM   8578  C  CD  . ARG   B 1  446 ? 5.274   4.969   14.593  1    19.612  ? 446  ARG   B CD  1 2 
ATOM   8579  N  NE  . ARG   B 1  446 ? 4.12    5.831   14.858  1    17.785  ? 446  ARG   B NE  1 2 
ATOM   8580  C  CZ  . ARG   B 1  446 ? 4.173   6.781   15.8    1    19.141  ? 446  ARG   B CZ  1 2 
ATOM   8581  N  NH1 . ARG   B 1  446 ? 5.264   6.887   16.56   1    16.752  ? 446  ARG   B NH1 1 2 
ATOM   8582  N  NH2 . ARG   B 1  446 ? 3.144   7.615   15.957  1    17.7    ? 446  ARG   B NH2 1 2 
ATOM   8583  N  N   . TRP   B 1  447 ? 2.424   1.738   11.115  1    19.418  ? 447  TRP   B N   1 2 
ATOM   8584  C  CA  . TRP   B 1  447 ? 1.916   0.369   11.054  1    20.108  ? 447  TRP   B CA  1 2 
ATOM   8585  C  C   . TRP   B 1  447 ? 2.642   -0.47   9.992   1    20.438  ? 447  TRP   B C   1 2 
ATOM   8586  O  O   . TRP   B 1  447 ? 2.773   -1.679  10.198  1    21.959  ? 447  TRP   B O   1 2 
ATOM   8587  C  CB  . TRP   B 1  447 ? 0.405   0.276   10.794  1    20.978  ? 447  TRP   B CB  1 2 
ATOM   8588  C  CG  . TRP   B 1  447 ? -0.433  0.917   11.851  1    19.931  ? 447  TRP   B CG  1 2 
ATOM   8589  C  CD1 . TRP   B 1  447 ? -0.072  1.165   13.132  1    20.329  ? 447  TRP   B CD1 1 2 
ATOM   8590  C  CD2 . TRP   B 1  447 ? -1.759  1.455   11.681  1    20.736  ? 447  TRP   B CD2 1 2 
ATOM   8591  N  NE1 . TRP   B 1  447 ? -1.097  1.793   13.791  1    20.174  ? 447  TRP   B NE1 1 2 
ATOM   8592  C  CE2 . TRP   B 1  447 ? -2.138  1.997   12.929  1    20.751  ? 447  TRP   B CE2 1 2 
ATOM   8593  C  CE3 . TRP   B 1  447 ? -2.635  1.563   10.593  1    21.833  ? 447  TRP   B CE3 1 2 
ATOM   8594  C  CZ2 . TRP   B 1  447 ? -3.367  2.625   13.133  1    20.92   ? 447  TRP   B CZ2 1 2 
ATOM   8595  C  CZ3 . TRP   B 1  447 ? -3.866  2.182   10.789  1    23.6    ? 447  TRP   B CZ3 1 2 
ATOM   8596  C  CH2 . TRP   B 1  447 ? -4.205  2.718   12.041  1    22.261  ? 447  TRP   B CH2 1 2 
ATOM   8597  N  N   . GLY   B 1  448 ? 3.009   0.103   8.83    1    19.768  ? 448  GLY   B N   1 2 
ATOM   8598  C  CA  . GLY   B 1  448 ? 3.703   -0.691  7.809   1    18.754  ? 448  GLY   B CA  1 2 
ATOM   8599  C  C   . GLY   B 1  448 ? 5.143   -0.989  8.26    1    19.254  ? 448  GLY   B C   1 2 
ATOM   8600  O  O   . GLY   B 1  448 ? 5.737   -1.994  7.892   1    20.695  ? 448  GLY   B O   1 2 
ATOM   8601  N  N   . VAL   B 1  449 ? 5.748   -0.079  9.028   1    18.424  ? 449  VAL   B N   1 2 
ATOM   8602  C  CA  . VAL   B 1  449 ? 7.078   -0.36   9.53    1    19.628  ? 449  VAL   B CA  1 2 
ATOM   8603  C  C   . VAL   B 1  449 ? 6.988   -1.522  10.532  1    21.173  ? 449  VAL   B C   1 2 
ATOM   8604  O  O   . VAL   B 1  449 ? 7.722   -2.499  10.455  1    23.991  ? 449  VAL   B O   1 2 
ATOM   8605  C  CB  . VAL   B 1  449 ? 7.755   0.899   10.131  1    18.222  ? 449  VAL   B CB  1 2 
ATOM   8606  C  CG1 . VAL   B 1  449 ? 9.01    0.522   10.938  1    19.254  ? 449  VAL   B CG1 1 2 
ATOM   8607  C  CG2 . VAL   B 1  449 ? 8.055   1.969   9.064   1    17.938  ? 449  VAL   B CG2 1 2 
ATOM   8608  N  N   . PHE   B 1  450 ? 6.112   -1.416  11.529  1    21.983  ? 450  PHE   B N   1 2 
ATOM   8609  C  CA  . PHE   B 1  450 ? 6.027   -2.499  12.506  1    23.507  ? 450  PHE   B CA  1 2 
ATOM   8610  C  C   . PHE   B 1  450 ? 5.646   -3.843  11.87   1    24.716  ? 450  PHE   B C   1 2 
ATOM   8611  O  O   . PHE   B 1  450 ? 6.101   -4.89   12.347  1    27.621  ? 450  PHE   B O   1 2 
ATOM   8612  C  CB  . PHE   B 1  450 ? 4.927   -2.218  13.529  1    23.657  ? 450  PHE   B CB  1 2 
ATOM   8613  C  CG  . PHE   B 1  450 ? 5.338   -1.219  14.599  1    24.873  ? 450  PHE   B CG  1 2 
ATOM   8614  C  CD1 . PHE   B 1  450 ? 6.502   -1.42   15.353  1    27.082  ? 450  PHE   B CD1 1 2 
ATOM   8615  C  CD2 . PHE   B 1  450 ? 4.525   -0.118  14.885  1    23.819  ? 450  PHE   B CD2 1 2 
ATOM   8616  C  CE1 . PHE   B 1  450 ? 6.863   -0.491  16.343  1    27.613  ? 450  PHE   B CE1 1 2 
ATOM   8617  C  CE2 . PHE   B 1  450 ? 4.861   0.773   15.909  1    25.292  ? 450  PHE   B CE2 1 2 
ATOM   8618  C  CZ  . PHE   B 1  450 ? 6.044   0.599   16.618  1    26.632  ? 450  PHE   B CZ  1 2 
ATOM   8619  N  N   . SER   B 1  451 ? 4.796   -3.849  10.831  1    23.361  ? 451  SER   B N   1 2 
ATOM   8620  C  CA  . SER   B 1  451 ? 4.419   -5.104  10.198  1    24.958  ? 451  SER   B CA  1 2 
ATOM   8621  C  C   . SER   B 1  451 ? 5.521   -5.717  9.328   1    26.493  ? 451  SER   B C   1 2 
ATOM   8622  O  O   . SER   B 1  451 ? 5.418   -6.889  8.946   1    26.93   ? 451  SER   B O   1 2 
ATOM   8623  C  CB  . SER   B 1  451 ? 3.151   -4.972  9.419   1    26.421  ? 451  SER   B CB  1 2 
ATOM   8624  O  OG  . SER   B 1  451 ? 3.375   -4.268  8.192   1    25.576  ? 451  SER   B OG  1 2 
ATOM   8625  N  N   . GLY   B 1  452 ? 6.593   -4.968  9.035   1    27.2    ? 452  GLY   B N   1 2 
ATOM   8626  C  CA  . GLY   B 1  452 ? 7.611   -5.437  8.093   1    28.128  ? 452  GLY   B CA  1 2 
ATOM   8627  C  C   . GLY   B 1  452 ? 7.305   -5.083  6.624   1    28.2    ? 452  GLY   B C   1 2 
ATOM   8628  O  O   . GLY   B 1  452 ? 8.146   -5.28   5.752   1    27.362  ? 452  GLY   B O   1 2 
ATOM   8629  N  N   . ARG   B 1  453 ? 6.142   -4.479  6.339   1    26.662  ? 453  ARG   B N   1 2 
ATOM   8630  C  CA  . ARG   B 1  453 ? 5.823   -4.134  4.957   1    28.715  ? 453  ARG   B CA  1 2 
ATOM   8631  C  C   . ARG   B 1  453 ? 6.782   -3.049  4.48    1    25.473  ? 453  ARG   B C   1 2 
ATOM   8632  O  O   . ARG   B 1  453 ? 6.987   -2.952  3.279   1    24.738  ? 453  ARG   B O   1 2 
ATOM   8633  C  CB  . ARG   B 1  453 ? 4.381   -3.657  4.739   1    31.498  ? 453  ARG   B CB  1 2 
ATOM   8634  C  CG  . ARG   B 1  453 ? 3.419   -4.833  4.87    1    42.947  ? 453  ARG   B CG  1 2 
ATOM   8635  C  CD  . ARG   B 1  453 ? 2.001   -4.505  4.366   1    59.357  ? 453  ARG   B CD  1 2 
ATOM   8636  N  NE  . ARG   B 1  453 ? 1.066   -5.642  4.287   1    72.058  ? 453  ARG   B NE  1 2 
ATOM   8637  C  CZ  . ARG   B 1  453 ? -0.276  -5.604  4.168   1    70.423  ? 453  ARG   B CZ  1 2 
ATOM   8638  N  NH1 . ARG   B 1  453 ? -0.938  -4.457  4.16    1    65.277  ? 453  ARG   B NH1 1 2 
ATOM   8639  N  NH2 . ARG   B 1  453 ? -0.966  -6.728  4.084   1    69.077  ? 453  ARG   B NH2 1 2 
ATOM   8640  N  N   . THR   B 1  454 ? 7.257   -2.195  5.414   1    23.316  ? 454  THR   B N   1 2 
ATOM   8641  C  CA  . THR   B 1  454 ? 8.213   -1.129  5.165   1    20.682  ? 454  THR   B CA  1 2 
ATOM   8642  C  C   . THR   B 1  454 ? 9.518   -1.431  5.916   1    21.213  ? 454  THR   B C   1 2 
ATOM   8643  O  O   . THR   B 1  454 ? 9.707   -0.992  7.064   1    19.616  ? 454  THR   B O   1 2 
ATOM   8644  C  CB  . THR   B 1  454 ? 7.627   0.23    5.567   1    20.707  ? 454  THR   B CB  1 2 
ATOM   8645  O  OG1 . THR   B 1  454 ? 6.428   0.404   4.8     1    18.621  ? 454  THR   B OG1 1 2 
ATOM   8646  C  CG2 . THR   B 1  454 ? 8.584   1.395   5.321   1    20.075  ? 454  THR   B CG2 1 2 
ATOM   8647  N  N   . PRO   B 1  455 ? 10.483  -2.09   5.244   1    21.492  ? 455  PRO   B N   1 2 
ATOM   8648  C  CA  . PRO   B 1  455 ? 11.803  -2.345  5.834   1    21.862  ? 455  PRO   B CA  1 2 
ATOM   8649  C  C   . PRO   B 1  455 ? 12.611  -1.046  5.824   1    21.259  ? 455  PRO   B C   1 2 
ATOM   8650  O  O   . PRO   B 1  455 ? 12.241  -0.076  5.156   1    19.781  ? 455  PRO   B O   1 2 
ATOM   8651  C  CB  . PRO   B 1  455 ? 12.411  -3.42   4.903   1    22.774  ? 455  PRO   B CB  1 2 
ATOM   8652  C  CG  . PRO   B 1  455 ? 11.776  -3.136  3.565   1    22.768  ? 455  PRO   B CG  1 2 
ATOM   8653  C  CD  . PRO   B 1  455 ? 10.361  -2.658  3.878   1    21.064  ? 455  PRO   B CD  1 2 
ATOM   8654  N  N   . PRO   B 1  456 ? 13.745  -0.957  6.574   1    22.375  ? 456  PRO   B N   1 2 
ATOM   8655  C  CA  . PRO   B 1  456 ? 14.598  0.243   6.551   1    21.449  ? 456  PRO   B CA  1 2 
ATOM   8656  C  C   . PRO   B 1  456 ? 14.944  0.792   5.162   1    20.884  ? 456  PRO   B C   1 2 
ATOM   8657  O  O   . PRO   B 1  456 ? 15.004  2.004   4.944   1    19.938  ? 456  PRO   B O   1 2 
ATOM   8658  C  CB  . PRO   B 1  456 ? 15.888  -0.289  7.273   1    24.268  ? 456  PRO   B CB  1 2 
ATOM   8659  C  CG  . PRO   B 1  456 ? 15.349  -1.311  8.251   1    24.876  ? 456  PRO   B CG  1 2 
ATOM   8660  C  CD  . PRO   B 1  456 ? 14.258  -2.044  7.449   1    24.108  ? 456  PRO   B CD  1 2 
ATOM   8661  N  N   . SER   B 1  457 ? 15.034  -0.11   4.173   1    20.872  ? 457  SER   B N   1 2 
ATOM   8662  C  CA  . SER   B 1  457 ? 15.424  0.261   2.817   1    21.769  ? 457  SER   B CA  1 2 
ATOM   8663  C  C   . SER   B 1  457 ? 14.289  1.034   2.117   1    20.482  ? 457  SER   B C   1 2 
ATOM   8664  O  O   . SER   B 1  457 ? 14.505  1.679   1.073   1    20.908  ? 457  SER   B O   1 2 
ATOM   8665  C  CB  . SER   B 1  457 ? 15.848  -1.017  2.029   1    23.881  ? 457  SER   B CB  1 2 
ATOM   8666  O  OG  . SER   B 1  457 ? 14.635  -1.71   1.713   1    24.662  ? 457  SER   B OG  1 2 
ATOM   8667  N  N   . ARG   B 1  458 ? 13.099  1.096   2.753   1    18.816  ? 458  ARG   B N   1 2 
ATOM   8668  C  CA  . ARG   B 1  458 ? 12.023  1.882   2.164   1    18.225  ? 458  ARG   B CA  1 2 
ATOM   8669  C  C   . ARG   B 1  458 ? 11.391  2.882   3.133   1    17.58   ? 458  ARG   B C   1 2 
ATOM   8670  O  O   . ARG   B 1  458 ? 10.26   3.305   2.885   1    17.558  ? 458  ARG   B O   1 2 
ATOM   8671  C  CB  . ARG   B 1  458 ? 10.904  0.958   1.646   1    17.973  ? 458  ARG   B CB  1 2 
ATOM   8672  C  CG  . ARG   B 1  458 ? 11.37   0.257   0.364   1    19.917  ? 458  ARG   B CG  1 2 
ATOM   8673  C  CD  . ARG   B 1  458 ? 10.056  -0.403  -0.25   1    20.317  ? 458  ARG   B CD  1 2 
ATOM   8674  N  NE  . ARG   B 1  458 ? 9.579   -1.616  0.449   1    21.715  ? 458  ARG   B NE  1 2 
ATOM   8675  C  CZ  . ARG   B 1  458 ? 10.032  -2.857  0.424   1    23.574  ? 458  ARG   B CZ  1 2 
ATOM   8676  N  NH1 . ARG   B 1  458 ? 11.107  -3.175  -0.279  1    23.693  ? 458  ARG   B NH1 1 2 
ATOM   8677  N  NH2 . ARG   B 1  458 ? 9.37    -3.815  1.08    1    24.689  ? 458  ARG   B NH2 1 2 
ATOM   8678  N  N   . TYR   B 1  459 ? 12.014  3.141   4.295   1    17.347  ? 459  TYR   B N   1 2 
ATOM   8679  C  CA  . TYR   B 1  459 ? 11.398  4.086   5.228   1    16.508  ? 459  TYR   B CA  1 2 
ATOM   8680  C  C   . TYR   B 1  459 ? 11.067  5.431   4.586   1    15.722  ? 459  TYR   B C   1 2 
ATOM   8681  O  O   . TYR   B 1  459 ? 9.977   5.943   4.835   1    14.974  ? 459  TYR   B O   1 2 
ATOM   8682  C  CB  . TYR   B 1  459 ? 12.384  4.508   6.318   1    17.639  ? 459  TYR   B CB  1 2 
ATOM   8683  C  CG  . TYR   B 1  459 ? 12.485  3.596   7.524   1    18.787  ? 459  TYR   B CG  1 2 
ATOM   8684  C  CD1 . TYR   B 1  459 ? 11.842  2.373   7.564   1    19.176  ? 459  TYR   B CD1 1 2 
ATOM   8685  C  CD2 . TYR   B 1  459 ? 13.386  3.918   8.547   1    21.704  ? 459  TYR   B CD2 1 2 
ATOM   8686  C  CE1 . TYR   B 1  459 ? 12.016  1.509   8.644   1    21.635  ? 459  TYR   B CE1 1 2 
ATOM   8687  C  CE2 . TYR   B 1  459 ? 13.562  3.084   9.644   1    21.523  ? 459  TYR   B CE2 1 2 
ATOM   8688  C  CZ  . TYR   B 1  459 ? 12.857  1.892   9.687   1    21.94   ? 459  TYR   B CZ  1 2 
ATOM   8689  O  OH  . TYR   B 1  459 ? 13.078  1.029   10.72   1    26.524  ? 459  TYR   B OH  1 2 
ATOM   8690  N  N   . ASN   B 1  460 ? 12      6.052   3.823   1    15.537  ? 460  ASN   B N   1 2 
ATOM   8691  C  CA  . ASN   B 1  460 ? 11.702  7.371   3.269   1    14.8    ? 460  ASN   B CA  1 2 
ATOM   8692  C  C   . ASN   B 1  460 ? 10.819  7.282   2.024   1    15.012  ? 460  ASN   B C   1 2 
ATOM   8693  O  O   . ASN   B 1  460 ? 9.959   8.159   1.806   1    14.064  ? 460  ASN   B O   1 2 
ATOM   8694  C  CB  . ASN   B 1  460 ? 12.979  8.149   2.973   1    15.691  ? 460  ASN   B CB  1 2 
ATOM   8695  C  CG  . ASN   B 1  460 ? 12.912  9.585   3.47    1    16.355  ? 460  ASN   B CG  1 2 
ATOM   8696  O  OD1 . ASN   B 1  460 ? 12.474  9.845   4.608   1    18.674  ? 460  ASN   B OD1 1 2 
ATOM   8697  N  ND2 . ASN   B 1  460 ? 13.221  10.542  2.601   1    16.013  ? 460  ASN   B ND2 1 2 
ATOM   8698  N  N   . PHE   B 1  461 ? 11.105  6.298   1.148   1    14.841  ? 461  PHE   B N   1 2 
ATOM   8699  C  CA  . PHE   B 1  461 ? 10.246  6.032   -0.015  1    15.371  ? 461  PHE   B CA  1 2 
ATOM   8700  C  C   . PHE   B 1  461 ? 8.757   5.92    0.415   1    15.242  ? 461  PHE   B C   1 2 
ATOM   8701  O  O   . PHE   B 1  461 ? 7.877   6.553   -0.195  1    15.033  ? 461  PHE   B O   1 2 
ATOM   8702  C  CB  . PHE   B 1  461 ? 10.806  4.814   -0.772  1    17.082  ? 461  PHE   B CB  1 2 
ATOM   8703  C  CG  . PHE   B 1  461 ? 9.997   4.22    -1.934  1    16.953  ? 461  PHE   B CG  1 2 
ATOM   8704  C  CD1 . PHE   B 1  461 ? 9.88    4.889   -3.149  1    17.381  ? 461  PHE   B CD1 1 2 
ATOM   8705  C  CD2 . PHE   B 1  461 ? 9.419   2.966   -1.809  1    17.691  ? 461  PHE   B CD2 1 2 
ATOM   8706  C  CE1 . PHE   B 1  461 ? 9.12    4.368   -4.213  1    17.286  ? 461  PHE   B CE1 1 2 
ATOM   8707  C  CE2 . PHE   B 1  461 ? 8.736   2.387   -2.901  1    18.155  ? 461  PHE   B CE2 1 2 
ATOM   8708  C  CZ  . PHE   B 1  461 ? 8.614   3.1     -4.097  1    18.153  ? 461  PHE   B CZ  1 2 
ATOM   8709  N  N   . ASP   B 1  462 ? 8.443   5.086   1.409   1    15.02   ? 462  ASP   B N   1 2 
ATOM   8710  C  CA  . ASP   B 1  462 ? 7.052   4.901   1.862   1    15.062  ? 462  ASP   B CA  1 2 
ATOM   8711  C  C   . ASP   B 1  462 ? 6.479   6.105   2.611   1    14.392  ? 462  ASP   B C   1 2 
ATOM   8712  O  O   . ASP   B 1  462 ? 5.283   6.361   2.52    1    13.101  ? 462  ASP   B O   1 2 
ATOM   8713  C  CB  . ASP   B 1  462 ? 6.873   3.639   2.688   1    16.887  ? 462  ASP   B CB  1 2 
ATOM   8714  C  CG  . ASP   B 1  462 ? 6.875   2.38    1.834   1    21.26   ? 462  ASP   B CG  1 2 
ATOM   8715  O  OD1 . ASP   B 1  462 ? 6.975   2.506   0.609   1    22.584  ? 462  ASP   B OD1 1 2 
ATOM   8716  O  OD2 . ASP   B 1  462 ? 6.862   1.274   2.381   1    23.79   ? 462  ASP   B OD2 1 2 
ATOM   8717  N  N   . TRP   B 1  463 ? 7.332   6.818   3.344   1    13.798  ? 463  TRP   B N   1 2 
ATOM   8718  C  CA  . TRP   B 1  463 ? 6.917   8.083   3.947   1    13.687  ? 463  TRP   B CA  1 2 
ATOM   8719  C  C   . TRP   B 1  463 ? 6.425   9.088   2.896   1    13.243  ? 463  TRP   B C   1 2 
ATOM   8720  O  O   . TRP   B 1  463 ? 5.257   9.534   2.938   1    12.414  ? 463  TRP   B O   1 2 
ATOM   8721  C  CB  . TRP   B 1  463 ? 8.044   8.644   4.827   1    14.129  ? 463  TRP   B CB  1 2 
ATOM   8722  C  CG  . TRP   B 1  463 ? 7.766   10.012  5.419   1    14.368  ? 463  TRP   B CG  1 2 
ATOM   8723  C  CD1 . TRP   B 1  463 ? 8.31    11.188  5.005   1    15.314  ? 463  TRP   B CD1 1 2 
ATOM   8724  C  CD2 . TRP   B 1  463 ? 6.939   10.307  6.555   1    15.28   ? 463  TRP   B CD2 1 2 
ATOM   8725  N  NE1 . TRP   B 1  463 ? 7.88    12.223  5.802   1    15.277  ? 463  TRP   B NE1 1 2 
ATOM   8726  C  CE2 . TRP   B 1  463 ? 7.066   11.689  6.79    1    15.385  ? 463  TRP   B CE2 1 2 
ATOM   8727  C  CE3 . TRP   B 1  463 ? 6.125   9.527   7.409   1    17.068  ? 463  TRP   B CE3 1 2 
ATOM   8728  C  CZ2 . TRP   B 1  463 ? 6.373   12.296  7.842   1    16.894  ? 463  TRP   B CZ2 1 2 
ATOM   8729  C  CZ3 . TRP   B 1  463 ? 5.473   10.126  8.464   1    16.282  ? 463  TRP   B CZ3 1 2 
ATOM   8730  C  CH2 . TRP   B 1  463 ? 5.619   11.496  8.686   1    16.055  ? 463  TRP   B CH2 1 2 
ATOM   8731  N  N   . TRP   B 1  464 ? 7.269   9.333   1.897   1    13.192  ? 464  TRP   B N   1 2 
ATOM   8732  C  CA  . TRP   B 1  464 ? 6.892   10.318  0.906   1    13.142  ? 464  TRP   B CA  1 2 
ATOM   8733  C  C   . TRP   B 1  464 ? 5.755   9.834   0.013   1    12.513  ? 464  TRP   B C   1 2 
ATOM   8734  O  O   . TRP   B 1  464 ? 5       10.677  -0.456  1    12.094  ? 464  TRP   B O   1 2 
ATOM   8735  C  CB  . TRP   B 1  464 ? 8.113   10.833  0.108   1    13.899  ? 464  TRP   B CB  1 2 
ATOM   8736  C  CG  . TRP   B 1  464 ? 8.849   11.802  0.994   1    14.645  ? 464  TRP   B CG  1 2 
ATOM   8737  C  CD1 . TRP   B 1  464 ? 10.047  11.64   1.627   1    15.34   ? 464  TRP   B CD1 1 2 
ATOM   8738  C  CD2 . TRP   B 1  464 ? 8.356   13.104  1.354   1    14.764  ? 464  TRP   B CD2 1 2 
ATOM   8739  N  NE1 . TRP   B 1  464 ? 10.308  12.744  2.396   1    15.806  ? 464  TRP   B NE1 1 2 
ATOM   8740  C  CE2 . TRP   B 1  464 ? 9.308   13.664  2.236   1    16.024  ? 464  TRP   B CE2 1 2 
ATOM   8741  C  CE3 . TRP   B 1  464 ? 7.204   13.834  0.99    1    16.129  ? 464  TRP   B CE3 1 2 
ATOM   8742  C  CZ2 . TRP   B 1  464 ? 9.148   14.94   2.795   1    15.862  ? 464  TRP   B CZ2 1 2 
ATOM   8743  C  CZ3 . TRP   B 1  464 ? 7.047   15.105  1.543   1    16.197  ? 464  TRP   B CZ3 1 2 
ATOM   8744  C  CH2 . TRP   B 1  464 ? 7.992   15.621  2.44    1    16.279  ? 464  TRP   B CH2 1 2 
ATOM   8745  N  N   . TYR   B 1  465 ? 5.681   8.527   -0.27   1    13.208  ? 465  TYR   B N   1 2 
ATOM   8746  C  CA  . TYR   B 1  465 ? 4.515   7.944   -0.951  1    13.593  ? 465  TYR   B CA  1 2 
ATOM   8747  C  C   . TYR   B 1  465 ? 3.241   8.421   -0.222  1    13.443  ? 465  TYR   B C   1 2 
ATOM   8748  O  O   . TYR   B 1  465 ? 2.296   8.954   -0.848  1    13.082  ? 465  TYR   B O   1 2 
ATOM   8749  C  CB  . TYR   B 1  465 ? 4.536   6.396   -1.009  1    14.532  ? 465  TYR   B CB  1 2 
ATOM   8750  C  CG  . TYR   B 1  465 ? 3.225   5.84    -1.526  1    15.366  ? 465  TYR   B CG  1 2 
ATOM   8751  C  CD1 . TYR   B 1  465 ? 2.982   5.754   -2.905  1    16.144  ? 465  TYR   B CD1 1 2 
ATOM   8752  C  CD2 . TYR   B 1  465 ? 2.216   5.474   -0.642  1    16.057  ? 465  TYR   B CD2 1 2 
ATOM   8753  C  CE1 . TYR   B 1  465 ? 1.775   5.277   -3.39   1    17.573  ? 465  TYR   B CE1 1 2 
ATOM   8754  C  CE2 . TYR   B 1  465 ? 0.996   5.023   -1.11   1    18.322  ? 465  TYR   B CE2 1 2 
ATOM   8755  C  CZ  . TYR   B 1  465 ? 0.783   4.912   -2.481  1    18.439  ? 465  TYR   B CZ  1 2 
ATOM   8756  O  OH  . TYR   B 1  465 ? -0.438  4.533   -2.954  1    19.793  ? 465  TYR   B OH  1 2 
ATOM   8757  N  N   . LEU   B 1  466 ? 3.227   8.272   1.115   1    13.047  ? 466  LEU   B N   1 2 
ATOM   8758  C  CA  . LEU   B 1  466 ? 2.04    8.556   1.918   1    13.623  ? 466  LEU   B CA  1 2 
ATOM   8759  C  C   . LEU   B 1  466 ? 1.83    10.072  1.996   1    13.04   ? 466  LEU   B C   1 2 
ATOM   8760  O  O   . LEU   B 1  466 ? 0.702   10.551  1.932   1    12.071  ? 466  LEU   B O   1 2 
ATOM   8761  C  CB  . LEU   B 1  466 ? 2.172   7.924   3.318   1    13.442  ? 466  LEU   B CB  1 2 
ATOM   8762  C  CG  . LEU   B 1  466 ? 2.003   6.397   3.309   1    15.557  ? 466  LEU   B CG  1 2 
ATOM   8763  C  CD1 . LEU   B 1  466 ? 2.347   5.82    4.703   1    16.702  ? 466  LEU   B CD1 1 2 
ATOM   8764  C  CD2 . LEU   B 1  466 ? 0.577   6.011   2.949   1    15.645  ? 466  LEU   B CD2 1 2 
ATOM   8765  N  N   . ARG   B 1  467 ? 2.925   10.83   2.174   1    14.13   ? 467  ARG   B N   1 2 
ATOM   8766  C  CA  . ARG   B 1  467 ? 2.788   12.286  2.193   1    14.815  ? 467  ARG   B CA  1 2 
ATOM   8767  C  C   . ARG   B 1  467 ? 2.156   12.815  0.895   1    16.235  ? 467  ARG   B C   1 2 
ATOM   8768  O  O   . ARG   B 1  467 ? 1.271   13.7    0.926   1    16.286  ? 467  ARG   B O   1 2 
ATOM   8769  C  CB  . ARG   B 1  467 ? 4.102   12.986  2.516   1    15.536  ? 467  ARG   B CB  1 2 
ATOM   8770  C  CG  . ARG   B 1  467 ? 4.65    12.511  3.866   1    15.76   ? 467  ARG   B CG  1 2 
ATOM   8771  C  CD  . ARG   B 1  467 ? 4.341   13.455  4.957   1    16.446  ? 467  ARG   B CD  1 2 
ATOM   8772  N  NE  . ARG   B 1  467 ? 5.255   14.593  4.892   1    16.842  ? 467  ARG   B NE  1 2 
ATOM   8773  C  CZ  . ARG   B 1  467 ? 5.209   15.749  5.596   1    17.648  ? 467  ARG   B CZ  1 2 
ATOM   8774  N  NH1 . ARG   B 1  467 ? 4.084   16.16   6.157   1    15.477  ? 467  ARG   B NH1 1 2 
ATOM   8775  N  NH2 . ARG   B 1  467 ? 6.265   16.544  5.619   1    17.128  ? 467  ARG   B NH2 1 2 
ATOM   8776  N  N   . THR   B 1  468 ? 2.664   12.359  -0.239  1    15.216  ? 468  THR   B N   1 2 
ATOM   8777  C  CA  . THR   B 1  468 ? 2.084   12.773  -1.513  1    15.612  ? 468  THR   B CA  1 2 
ATOM   8778  C  C   . THR   B 1  468 ? 0.653   12.231  -1.65   1    15.463  ? 468  THR   B C   1 2 
ATOM   8779  O  O   . THR   B 1  468 ? -0.235  13.009  -2.013  1    15.029  ? 468  THR   B O   1 2 
ATOM   8780  C  CB  . THR   B 1  468 ? 3.021   12.416  -2.685  1    17.046  ? 468  THR   B CB  1 2 
ATOM   8781  O  OG1 . THR   B 1  468 ? 4.335   12.951  -2.401  1    17.633  ? 468  THR   B OG1 1 2 
ATOM   8782  C  CG2 . THR   B 1  468 ? 2.455   12.806  -4.037  1    17.698  ? 468  THR   B CG2 1 2 
ATOM   8783  N  N   . LYS   B 1  469 ? 0.427   10.916  -1.406  1    14.516  ? 469  LYS   B N   1 2 
ATOM   8784  C  CA  . LYS   B 1  469 ? -0.886  10.291  -1.558  1    15.836  ? 469  LYS   B CA  1 2 
ATOM   8785  C  C   . LYS   B 1  469 ? -1.95   11.118  -0.82   1    15.608  ? 469  LYS   B C   1 2 
ATOM   8786  O  O   . LYS   B 1  469 ? -3.009  11.399  -1.378  1    16.031  ? 469  LYS   B O   1 2 
ATOM   8787  C  CB  . LYS   B 1  469 ? -0.931  8.856   -1.009  1    16.852  ? 469  LYS   B CB  1 2 
ATOM   8788  C  CG  . LYS   B 1  469 ? -2.295  8.169   -1.054  1    18.552  ? 469  LYS   B CG  1 2 
ATOM   8789  C  CD  . LYS   B 1  469 ? -2.321  6.699   -0.667  1    18.319  ? 469  LYS   B CD  1 2 
ATOM   8790  C  CE  . LYS   B 1  469 ? -3.755  6.256   -0.714  1    21.527  ? 469  LYS   B CE  1 2 
ATOM   8791  N  NZ  . LYS   B 1  469 ? -3.841  4.866   -0.283  1    24.143  ? 469  LYS   B NZ  1 2 
ATOM   8792  N  N   . TYR   B 1  470 ? -1.684  11.445  0.455   1    14.071  ? 470  TYR   B N   1 2 
ATOM   8793  C  CA  . TYR   B 1  470 ? -2.732  11.957  1.344   1    15.479  ? 470  TYR   B CA  1 2 
ATOM   8794  C  C   . TYR   B 1  470 ? -2.687  13.484  1.412   1    15.221  ? 470  TYR   B C   1 2 
ATOM   8795  O  O   . TYR   B 1  470 ? -3.727  14.121  1.244   1    16.609  ? 470  TYR   B O   1 2 
ATOM   8796  C  CB  . TYR   B 1  470 ? -2.576  11.384  2.777   1    14.426  ? 470  TYR   B CB  1 2 
ATOM   8797  C  CG  . TYR   B 1  470 ? -3.157  9.988   2.8     1    15.398  ? 470  TYR   B CG  1 2 
ATOM   8798  C  CD1 . TYR   B 1  470 ? -4.542  9.78    2.726   1    15.558  ? 470  TYR   B CD1 1 2 
ATOM   8799  C  CD2 . TYR   B 1  470 ? -2.334  8.854   2.885   1    15.538  ? 470  TYR   B CD2 1 2 
ATOM   8800  C  CE1 . TYR   B 1  470 ? -5.075  8.501   2.691   1    16.923  ? 470  TYR   B CE1 1 2 
ATOM   8801  C  CE2 . TYR   B 1  470 ? -2.868  7.563   2.87    1    17.472  ? 470  TYR   B CE2 1 2 
ATOM   8802  C  CZ  . TYR   B 1  470 ? -4.248  7.398   2.787   1    17.927  ? 470  TYR   B CZ  1 2 
ATOM   8803  O  OH  . TYR   B 1  470 ? -4.794  6.165   2.764   1    18.865  ? 470  TYR   B OH  1 2 
ATOM   8804  N  N   . GLN   B 1  471 ? -1.494  14.076  1.602   1    14.306  ? 471  GLN   B N   1 2 
ATOM   8805  C  CA  . GLN   B 1  471 ? -1.426  15.52   1.823   1    13.773  ? 471  GLN   B CA  1 2 
ATOM   8806  C  C   . GLN   B 1  471 ? -1.191  16.252  0.499   1    14.308  ? 471  GLN   B C   1 2 
ATOM   8807  O  O   . GLN   B 1  471 ? -1.455  17.431  0.44    1    16.62   ? 471  GLN   B O   1 2 
ATOM   8808  C  CB  . GLN   B 1  471 ? -0.31   15.99   2.762   1    13.241  ? 471  GLN   B CB  1 2 
ATOM   8809  C  CG  . GLN   B 1  471 ? -0.546  15.591  4.206   1    12.848  ? 471  GLN   B CG  1 2 
ATOM   8810  C  CD  . GLN   B 1  471 ? 0.582   16.074  5.083   1    13.095  ? 471  GLN   B CD  1 2 
ATOM   8811  O  OE1 . GLN   B 1  471 ? 1.59    15.333  5.213   1    12.993  ? 471  GLN   B OE1 1 2 
ATOM   8812  N  NE2 . GLN   B 1  471 ? 0.473   17.314  5.61    1    11.147  ? 471  GLN   B NE2 1 2 
ATOM   8813  N  N   . GLY   B 1  472 ? -0.714  15.596  -0.55   1    14.45   ? 472  GLY   B N   1 2 
ATOM   8814  C  CA  . GLY   B 1  472 ? -0.512  16.311  -1.824  1    15.099  ? 472  GLY   B CA  1 2 
ATOM   8815  C  C   . GLY   B 1  472 ? 0.604   17.361  -1.706  1    16.028  ? 472  GLY   B C   1 2 
ATOM   8816  O  O   . GLY   B 1  472 ? 0.502   18.492  -2.214  1    15.496  ? 472  GLY   B O   1 2 
ATOM   8817  N  N   . ILE   B 1  473 ? 1.715   16.947  -1.045  1    16.06   ? 473  ILE   B N   1 2 
ATOM   8818  C  CA  . ILE   B 1  473 ? 2.887   17.773  -0.843  1    16.249  ? 473  ILE   B CA  1 2 
ATOM   8819  C  C   . ILE   B 1  473 ? 4.094   17.009  -1.389  1    17.355  ? 473  ILE   B C   1 2 
ATOM   8820  O  O   . ILE   B 1  473 ? 4.053   15.775  -1.506  1    17.955  ? 473  ILE   B O   1 2 
ATOM   8821  C  CB  . ILE   B 1  473 ? 3.11    18.171  0.63    1    16.352  ? 473  ILE   B CB  1 2 
ATOM   8822  C  CG1 . ILE   B 1  473 ? 3.258   16.977  1.565   1    16.758  ? 473  ILE   B CG1 1 2 
ATOM   8823  C  CG2 . ILE   B 1  473 ? 2.004   19.114  1.135   1    18.129  ? 473  ILE   B CG2 1 2 
ATOM   8824  C  CD1 . ILE   B 1  473 ? 3.526   17.464  3.003   1    15.52   ? 473  ILE   B CD1 1 2 
ATOM   8825  N  N   . CYS   B 1  474 ? 5.188   17.714  -1.616  1    18.212  ? 474  CYS   B N   1 2 
ATOM   8826  C  CA  . CYS   B 1  474 ? 6.384   17.025  -2.112  1    17.857  ? 474  CYS   B CA  1 2 
ATOM   8827  C  C   . CYS   B 1  474 ? 7.573   17.625  -1.417  1    17.834  ? 474  CYS   B C   1 2 
ATOM   8828  O  O   . CYS   B 1  474 ? 7.514   18.784  -0.992  1    18.385  ? 474  CYS   B O   1 2 
ATOM   8829  C  CB  . CYS   B 1  474 ? 6.541   17.162  -3.631  1    19.54   ? 474  CYS   B CB  1 2 
ATOM   8830  S  SG  . CYS   B 1  474 ? 6.502   18.894  -4.169  1    20.491  ? 474  CYS   B SG  1 2 
ATOM   8831  N  N   . PRO   B 1  475 ? 8.709   16.891  -1.294  1    18.86   ? 475  PRO   B N   1 2 
ATOM   8832  C  CA  . PRO   B 1  475 ? 9.84    17.438  -0.567  1    18.754  ? 475  PRO   B CA  1 2 
ATOM   8833  C  C   . PRO   B 1  475 ? 10.405  18.501  -1.51   1    20.767  ? 475  PRO   B C   1 2 
ATOM   8834  O  O   . PRO   B 1  475 ? 10.448  18.313  -2.718  1    20.85   ? 475  PRO   B O   1 2 
ATOM   8835  C  CB  . PRO   B 1  475 ? 10.797  16.249  -0.34   1    19.052  ? 475  PRO   B CB  1 2 
ATOM   8836  C  CG  . PRO   B 1  475 ? 10.418  15.275  -1.422  1    19.608  ? 475  PRO   B CG  1 2 
ATOM   8837  C  CD  . PRO   B 1  475 ? 8.929   15.495  -1.73   1    18.11   ? 475  PRO   B CD  1 2 
ATOM   8838  N  N   . PRO   B 1  476 ? 10.832  19.67   -0.976  1    20.527  ? 476  PRO   B N   1 2 
ATOM   8839  C  CA  . PRO   B 1  476 ? 11.334  20.749  -1.822  1    21.928  ? 476  PRO   B CA  1 2 
ATOM   8840  C  C   . PRO   B 1  476 ? 12.792  20.519  -2.181  1    23.815  ? 476  PRO   B C   1 2 
ATOM   8841  O  O   . PRO   B 1  476 ? 13.346  21.3    -2.935  1    26.596  ? 476  PRO   B O   1 2 
ATOM   8842  C  CB  . PRO   B 1  476 ? 11.189  21.979  -0.93   1    21.071  ? 476  PRO   B CB  1 2 
ATOM   8843  C  CG  . PRO   B 1  476 ? 11.388  21.41   0.511   1    20.881  ? 476  PRO   B CG  1 2 
ATOM   8844  C  CD  . PRO   B 1  476 ? 10.778  20.012  0.455   1    19.897  ? 476  PRO   B CD  1 2 
ATOM   8845  N  N   . VAL   B 1  477 ? 13.423  19.492  -1.611  1    24.039  ? 477  VAL   B N   1 2 
ATOM   8846  C  CA  . VAL   B 1  477 ? 14.746  19.102  -2.103  1    24.582  ? 477  VAL   B CA  1 2 
ATOM   8847  C  C   . VAL   B 1  477 ? 14.723  17.582  -2.282  1    24.606  ? 477  VAL   B C   1 2 
ATOM   8848  O  O   . VAL   B 1  477 ? 13.894  16.875  -1.666  1    21.884  ? 477  VAL   B O   1 2 
ATOM   8849  C  CB  . VAL   B 1  477 ? 15.916  19.524  -1.196  1    27.478  ? 477  VAL   B CB  1 2 
ATOM   8850  C  CG1 . VAL   B 1  477 ? 16.229  21.029  -1.249  1    28.03   ? 477  VAL   B CG1 1 2 
ATOM   8851  C  CG2 . VAL   B 1  477 ? 15.719  19.021  0.236   1    26.34   ? 477  VAL   B CG2 1 2 
ATOM   8852  N  N   . THR   B 1  478 ? 15.622  17.075  -3.132  1    23.194  ? 478  THR   B N   1 2 
ATOM   8853  C  CA  . THR   B 1  478 ? 15.725  15.636  -3.343  1    24.005  ? 478  THR   B CA  1 2 
ATOM   8854  C  C   . THR   B 1  478 ? 15.971  14.924  -2.003  1    22.398  ? 478  THR   B C   1 2 
ATOM   8855  O  O   . THR   B 1  478 ? 16.723  15.418  -1.171  1    21.84   ? 478  THR   B O   1 2 
ATOM   8856  C  CB  . THR   B 1  478 ? 16.874  15.379  -4.33   1    27.84   ? 478  THR   B CB  1 2 
ATOM   8857  O  OG1 . THR   B 1  478 ? 16.35   15.998  -5.505  1    28.102  ? 478  THR   B OG1 1 2 
ATOM   8858  C  CG2 . THR   B 1  478 ? 17.003  13.893  -4.64   1    29.918  ? 478  THR   B CG2 1 2 
ATOM   8859  N  N   . ARG   B 1  479 ? 15.286  13.791  -1.767  1    21.425  ? 479  ARG   B N   1 2 
ATOM   8860  C  CA  . ARG   B 1  479 ? 15.537  12.951  -0.596  1    20.387  ? 479  ARG   B CA  1 2 
ATOM   8861  C  C   . ARG   B 1  479 ? 15.951  11.559  -1.078  1    20.37   ? 479  ARG   B C   1 2 
ATOM   8862  O  O   . ARG   B 1  479 ? 15.553  11.17   -2.169  1    20.417  ? 479  ARG   B O   1 2 
ATOM   8863  C  CB  . ARG   B 1  479 ? 14.247  12.783  0.23    1    18.679  ? 479  ARG   B CB  1 2 
ATOM   8864  C  CG  . ARG   B 1  479 ? 13.51   14.111  0.398   1    18.574  ? 479  ARG   B CG  1 2 
ATOM   8865  C  CD  . ARG   B 1  479 ? 14.38   15.173  1.096   1    18.689  ? 479  ARG   B CD  1 2 
ATOM   8866  N  NE  . ARG   B 1  479 ? 14.684  14.823  2.483   1    18.329  ? 479  ARG   B NE  1 2 
ATOM   8867  C  CZ  . ARG   B 1  479 ? 15.746  15.352  3.173   1    20.274  ? 479  ARG   B CZ  1 2 
ATOM   8868  N  NH1 . ARG   B 1  479 ? 15.799  15.27   4.501   1    18.953  ? 479  ARG   B NH1 1 2 
ATOM   8869  N  NH2 . ARG   B 1  479 ? 16.707  16.043  2.542   1    20.543  ? 479  ARG   B NH2 1 2 
ATOM   8870  N  N   . ASN   B 1  480 ? 16.736  10.812  -0.294  1    19.759  ? 480  ASN   B N   1 2 
ATOM   8871  C  CA  . ASN   B 1  480 ? 16.963  9.414   -0.607  1    19.965  ? 480  ASN   B CA  1 2 
ATOM   8872  C  C   . ASN   B 1  480 ? 16.904  8.634   0.697   1    20      ? 480  ASN   B C   1 2 
ATOM   8873  O  O   . ASN   B 1  480 ? 16.471  9.16    1.711   1    19.002  ? 480  ASN   B O   1 2 
ATOM   8874  C  CB  . ASN   B 1  480 ? 18.271  9.245   -1.389  1    23.215  ? 480  ASN   B CB  1 2 
ATOM   8875  C  CG  . ASN   B 1  480 ? 19.445  9.784   -0.605  1    25.321  ? 480  ASN   B CG  1 2 
ATOM   8876  O  OD1 . ASN   B 1  480 ? 19.554  9.586   0.613   1    23.405  ? 480  ASN   B OD1 1 2 
ATOM   8877  N  ND2 . ASN   B 1  480 ? 20.334  10.449  -1.319  1    30.013  ? 480  ASN   B ND2 1 2 
ATOM   8878  N  N   . GLU   B 1  481 ? 17.317  7.368   0.689   1    21.503  ? 481  GLU   B N   1 2 
ATOM   8879  C  CA  . GLU   B 1  481 ? 17.143  6.572   1.907   1    23.364  ? 481  GLU   B CA  1 2 
ATOM   8880  C  C   . GLU   B 1  481 ? 18.164  6.872   3.015   1    25.692  ? 481  GLU   B C   1 2 
ATOM   8881  O  O   . GLU   B 1  481 ? 18.025  6.289   4.103   1    26.638  ? 481  GLU   B O   1 2 
ATOM   8882  C  CB  . GLU   B 1  481 ? 17.127  5.072   1.568   1    25.09   ? 481  GLU   B CB  1 2 
ATOM   8883  C  CG  . GLU   B 1  481 ? 15.829  4.59    0.915   1    24.636  ? 481  GLU   B CG  1 2 
ATOM   8884  C  CD  . GLU   B 1  481 ? 14.545  4.82    1.756   1    22.659  ? 481  GLU   B CD  1 2 
ATOM   8885  O  OE1 . GLU   B 1  481 ? 14.488  5.156   3.002   1    22.454  ? 481  GLU   B OE1 1 2 
ATOM   8886  O  OE2 . GLU   B 1  481 ? 13.536  4.707   1.078   1    20.629  ? 481  GLU   B OE2 1 2 
ATOM   8887  N  N   . THR   B 1  482 ? 19.186  7.735   2.784   1    25.71   ? 482  THR   B N   1 2 
ATOM   8888  C  CA  . THR   B 1  482 ? 19.97   8.204   3.938   1    26.995  ? 482  THR   B CA  1 2 
ATOM   8889  C  C   . THR   B 1  482 ? 19.104  9.108   4.814   1    26.994  ? 482  THR   B C   1 2 
ATOM   8890  O  O   . THR   B 1  482 ? 19.283  9.202   6.022   1    27.215  ? 482  THR   B O   1 2 
ATOM   8891  C  CB  . THR   B 1  482 ? 21.234  8.949   3.521   1    29.163  ? 482  THR   B CB  1 2 
ATOM   8892  O  OG1 . THR   B 1  482 ? 21.927  7.949   2.776   1    27.413  ? 482  THR   B OG1 1 2 
ATOM   8893  C  CG2 . THR   B 1  482 ? 22.052  9.429   4.705   1    30.234  ? 482  THR   B CG2 1 2 
ATOM   8894  N  N   . HIS   B 1  483 ? 18.15   9.783   4.188   1    23.621  ? 483  HIS   B N   1 2 
ATOM   8895  C  CA  . HIS   B 1  483 ? 17.231  10.64   4.928   1    23.403  ? 483  HIS   B CA  1 2 
ATOM   8896  C  C   . HIS   B 1  483 ? 16.156  9.782   5.609   1    22.249  ? 483  HIS   B C   1 2 
ATOM   8897  O  O   . HIS   B 1  483 ? 15.807  8.707   5.116   1    22.527  ? 483  HIS   B O   1 2 
ATOM   8898  C  CB  . HIS   B 1  483 ? 16.592  11.67   3.989   1    21.56   ? 483  HIS   B CB  1 2 
ATOM   8899  C  CG  . HIS   B 1  483 ? 17.631  12.44   3.242   1    22.501  ? 483  HIS   B CG  1 2 
ATOM   8900  N  ND1 . HIS   B 1  483 ? 17.796  12.338  1.876   1    22.489  ? 483  HIS   B ND1 1 2 
ATOM   8901  C  CD2 . HIS   B 1  483 ? 18.545  13.33   3.68    1    23.028  ? 483  HIS   B CD2 1 2 
ATOM   8902  C  CE1 . HIS   B 1  483 ? 18.764  13.163  1.494   1    23.445  ? 483  HIS   B CE1 1 2 
ATOM   8903  N  NE2 . HIS   B 1  483 ? 19.237  13.784  2.585   1    23.323  ? 483  HIS   B NE2 1 2 
ATOM   8904  N  N   . PHE   B 1  484 ? 15.69   10.255  6.781   1    20.147  ? 484  PHE   B N   1 2 
ATOM   8905  C  CA  . PHE   B 1  484 ? 14.636  9.602   7.525   1    18.697  ? 484  PHE   B CA  1 2 
ATOM   8906  C  C   . PHE   B 1  484 ? 13.683  10.703  7.985   1    17.512  ? 484  PHE   B C   1 2 
ATOM   8907  O  O   . PHE   B 1  484 ? 13.745  11.151  9.151   1    18.263  ? 484  PHE   B O   1 2 
ATOM   8908  C  CB  . PHE   B 1  484 ? 15.345  8.936   8.701   1    20.375  ? 484  PHE   B CB  1 2 
ATOM   8909  C  CG  . PHE   B 1  484 ? 14.376  8.223   9.643   1    20.231  ? 484  PHE   B CG  1 2 
ATOM   8910  C  CD1 . PHE   B 1  484 ? 13.269  7.545   9.15    1    19.403  ? 484  PHE   B CD1 1 2 
ATOM   8911  C  CD2 . PHE   B 1  484 ? 14.576  8.237   11.014  1    20.315  ? 484  PHE   B CD2 1 2 
ATOM   8912  C  CE1 . PHE   B 1  484 ? 12.377  6.902   9.987   1    20.073  ? 484  PHE   B CE1 1 2 
ATOM   8913  C  CE2 . PHE   B 1  484 ? 13.674  7.598   11.866  1    19.947  ? 484  PHE   B CE2 1 2 
ATOM   8914  C  CZ  . PHE   B 1  484 ? 12.582  6.92    11.365  1    20.407  ? 484  PHE   B CZ  1 2 
ATOM   8915  N  N   . ASP   B 1  485 ? 12.833  11.132  7.051   1    17.121  ? 485  ASP   B N   1 2 
ATOM   8916  C  CA  . ASP   B 1  485 ? 12.001  12.322  7.225   1    17.152  ? 485  ASP   B CA  1 2 
ATOM   8917  C  C   . ASP   B 1  485 ? 10.918  12.096  8.281   1    18.321  ? 485  ASP   B C   1 2 
ATOM   8918  O  O   . ASP   B 1  485 ? 10.527  13.025  8.972   1    18.078  ? 485  ASP   B O   1 2 
ATOM   8919  C  CB  . ASP   B 1  485 ? 11.536  12.907  5.899   1    16.855  ? 485  ASP   B CB  1 2 
ATOM   8920  C  CG  . ASP   B 1  485 ? 12.734  13.41   5.091   1    17.274  ? 485  ASP   B CG  1 2 
ATOM   8921  O  OD1 . ASP   B 1  485 ? 13.695  13.893  5.707   1    17.408  ? 485  ASP   B OD1 1 2 
ATOM   8922  O  OD2 . ASP   B 1  485 ? 12.678  13.345  3.874   1    17.874  ? 485  ASP   B OD2 1 2 
ATOM   8923  N  N   . ALA   B 1  486 ? 10.417  10.876  8.396   1    18.988  ? 486  ALA   B N   1 2 
ATOM   8924  C  CA  . ALA   B 1  486 ? 9.472   10.559  9.465   1    18.03   ? 486  ALA   B CA  1 2 
ATOM   8925  C  C   . ALA   B 1  486 ? 10.134  10.817  10.829  1    18.462  ? 486  ALA   B C   1 2 
ATOM   8926  O  O   . ALA   B 1  486 ? 9.45    11.171  11.771  1    16.199  ? 486  ALA   B O   1 2 
ATOM   8927  C  CB  . ALA   B 1  486 ? 9.089   9.092   9.402   1    17.779  ? 486  ALA   B CB  1 2 
ATOM   8928  N  N   . GLY   B 1  487 ? 11.462  10.594  10.958  1    17.181  ? 487  GLY   B N   1 2 
ATOM   8929  C  CA  . GLY   B 1  487 ? 12.128  10.784  12.252  1    16.962  ? 487  GLY   B CA  1 2 
ATOM   8930  C  C   . GLY   B 1  487 ? 12.248  12.249  12.656  1    17.818  ? 487  GLY   B C   1 2 
ATOM   8931  O  O   . GLY   B 1  487 ? 12.456  12.545  13.838  1    19.818  ? 487  GLY   B O   1 2 
ATOM   8932  N  N   . ALA   B 1  488 ? 11.919  13.171  11.739  1    16.481  ? 488  ALA   B N   1 2 
ATOM   8933  C  CA  . ALA   B 1  488 ? 11.945  14.585  12.071  1    17.216  ? 488  ALA   B CA  1 2 
ATOM   8934  C  C   . ALA   B 1  488 ? 10.597  15.1    12.624  1    16.157  ? 488  ALA   B C   1 2 
ATOM   8935  O  O   . ALA   B 1  488 ? 10.442  16.297  12.829  1    16.525  ? 488  ALA   B O   1 2 
ATOM   8936  C  CB  . ALA   B 1  488 ? 12.444  15.394  10.878  1    18.354  ? 488  ALA   B CB  1 2 
ATOM   8937  N  N   . LYS   B 1  489 ? 9.659   14.198  12.929  1    16.397  ? 489  LYS   B N   1 2 
ATOM   8938  C  CA  . LYS   B 1  489 ? 8.427   14.587  13.618  1    16.982  ? 489  LYS   B CA  1 2 
ATOM   8939  C  C   . LYS   B 1  489 ? 8.479   14.002  15.033  1    17.353  ? 489  LYS   B C   1 2 
ATOM   8940  O  O   . LYS   B 1  489 ? 8.66    12.798  15.181  1    17.996  ? 489  LYS   B O   1 2 
ATOM   8941  C  CB  . LYS   B 1  489 ? 7.254   13.993  12.805  1    15.77   ? 489  LYS   B CB  1 2 
ATOM   8942  C  CG  . LYS   B 1  489 ? 5.876   13.943  13.5    1    16.83   ? 489  LYS   B CG  1 2 
ATOM   8943  C  CD  . LYS   B 1  489 ? 5.357   15.384  13.642  1    17.742  ? 489  LYS   B CD  1 2 
ATOM   8944  C  CE  . LYS   B 1  489 ? 4.027   15.465  14.392  1    20.486  ? 489  LYS   B CE  1 2 
ATOM   8945  N  NZ  . LYS   B 1  489 ? 3.818   16.883  14.741  1    21.04   ? 489  LYS   B NZ  1 2 
ATOM   8946  N  N   . PHE   B 1  490 ? 8.262   14.829  16.062  1    17.191  ? 490  PHE   B N   1 2 
ATOM   8947  C  CA  . PHE   B 1  490 ? 8.381   14.425  17.485  1    18.055  ? 490  PHE   B CA  1 2 
ATOM   8948  C  C   . PHE   B 1  490 ? 7.928   12.997  17.835  1    18.081  ? 490  PHE   B C   1 2 
ATOM   8949  O  O   . PHE   B 1  490 ? 8.656   12.209  18.46   1    17.893  ? 490  PHE   B O   1 2 
ATOM   8950  C  CB  . PHE   B 1  490 ? 7.633   15.449  18.335  1    18.882  ? 490  PHE   B CB  1 2 
ATOM   8951  C  CG  . PHE   B 1  490 ? 7.58    15.061  19.81   1    20.538  ? 490  PHE   B CG  1 2 
ATOM   8952  C  CD1 . PHE   B 1  490 ? 6.53    14.29   20.313  1    20.481  ? 490  PHE   B CD1 1 2 
ATOM   8953  C  CD2 . PHE   B 1  490 ? 8.599   15.437  20.666  1    20.977  ? 490  PHE   B CD2 1 2 
ATOM   8954  C  CE1 . PHE   B 1  490 ? 6.497   13.933  21.66   1    22.475  ? 490  PHE   B CE1 1 2 
ATOM   8955  C  CE2 . PHE   B 1  490 ? 8.58    15.07   22.023  1    23.434  ? 490  PHE   B CE2 1 2 
ATOM   8956  C  CZ  . PHE   B 1  490 ? 7.519   14.331  22.52   1    22.359  ? 490  PHE   B CZ  1 2 
ATOM   8957  N  N   . HIS   B 1  491 ? 6.704   12.632  17.453  1    16.057  ? 491  HIS   B N   1 2 
ATOM   8958  C  CA  . HIS   B 1  491 ? 6.051   11.455  17.984  1    16.361  ? 491  HIS   B CA  1 2 
ATOM   8959  C  C   . HIS   B 1  491 ? 6.698   10.147  17.507  1    16.878  ? 491  HIS   B C   1 2 
ATOM   8960  O  O   . HIS   B 1  491 ? 6.477   9.107   18.114  1    17.548  ? 491  HIS   B O   1 2 
ATOM   8961  C  CB  . HIS   B 1  491 ? 4.625   11.406  17.422  1    16.068  ? 491  HIS   B CB  1 2 
ATOM   8962  C  CG  . HIS   B 1  491 ? 3.825   12.524  17.98   1    14.875  ? 491  HIS   B CG  1 2 
ATOM   8963  N  ND1 . HIS   B 1  491 ? 4.074   13.786  17.54   1    14.957  ? 491  HIS   B ND1 1 2 
ATOM   8964  C  CD2 . HIS   B 1  491 ? 2.852   12.611  18.893  1    15.017  ? 491  HIS   B CD2 1 2 
ATOM   8965  C  CE1 . HIS   B 1  491 ? 3.259   14.628  18.151  1    15.284  ? 491  HIS   B CE1 1 2 
ATOM   8966  N  NE2 . HIS   B 1  491 ? 2.495   13.932  18.964  1    15.224  ? 491  HIS   B NE2 1 2 
ATOM   8967  N  N   . VAL   B 1  492 ? 7.488   10.196  16.426  1    16.658  ? 492  VAL   B N   1 2 
ATOM   8968  C  CA  . VAL   B 1  492 ? 8.172   9.015   15.919  1    17.572  ? 492  VAL   B CA  1 2 
ATOM   8969  C  C   . VAL   B 1  492 ? 9.323   8.649   16.863  1    19.101  ? 492  VAL   B C   1 2 
ATOM   8970  O  O   . VAL   B 1  492 ? 9.28    7.584   17.495  1    20.387  ? 492  VAL   B O   1 2 
ATOM   8971  C  CB  . VAL   B 1  492 ? 8.552   9.183   14.426  1    17.347  ? 492  VAL   B CB  1 2 
ATOM   8972  C  CG1 . VAL   B 1  492 ? 9.398   8.025   13.885  1    17.241  ? 492  VAL   B CG1 1 2 
ATOM   8973  C  CG2 . VAL   B 1  492 ? 7.269   9.323   13.601  1    15.62   ? 492  VAL   B CG2 1 2 
ATOM   8974  N  N   . PRO   B 1  493 ? 10.403  9.453   17.011  1    19.914  ? 493  PRO   B N   1 2 
ATOM   8975  C  CA  . PRO   B 1  493 ? 11.456  9.12    17.977  1    21.92   ? 493  PRO   B CA  1 2 
ATOM   8976  C  C   . PRO   B 1  493 ? 10.923  8.955   19.413  1    23.6    ? 493  PRO   B C   1 2 
ATOM   8977  O  O   . PRO   B 1  493 ? 11.512  8.223   20.203  1    25.532  ? 493  PRO   B O   1 2 
ATOM   8978  C  CB  . PRO   B 1  493 ? 12.502  10.27   17.83   1    20.371  ? 493  PRO   B CB  1 2 
ATOM   8979  C  CG  . PRO   B 1  493 ? 11.655  11.4    17.22   1    18.665  ? 493  PRO   B CG  1 2 
ATOM   8980  C  CD  . PRO   B 1  493 ? 10.741  10.658  16.256  1    18.099  ? 493  PRO   B CD  1 2 
ATOM   8981  N  N   . ASN   B 1  494 ? 9.797   9.617   19.738  1    23.455  ? 494  ASN   B N   1 2 
ATOM   8982  C  CA  . ASN   B 1  494 ? 9.255   9.672   21.095  1    23.689  ? 494  ASN   B CA  1 2 
ATOM   8983  C  C   . ASN   B 1  494 ? 8.206   8.578   21.252  1    24.913  ? 494  ASN   B C   1 2 
ATOM   8984  O  O   . ASN   B 1  494 ? 7.489   8.517   22.246  1    25.147  ? 494  ASN   B O   1 2 
ATOM   8985  C  CB  . ASN   B 1  494 ? 8.843   11.107  21.478  1    26.224  ? 494  ASN   B CB  1 2 
ATOM   8986  C  CG  . ASN   B 1  494 ? 10.065  11.996  21.696  1    29.511  ? 494  ASN   B CG  1 2 
ATOM   8987  O  OD1 . ASN   B 1  494 ? 10.669  11.945  22.781  1    33.869  ? 494  ASN   B OD1 1 2 
ATOM   8988  N  ND2 . ASN   B 1  494 ? 10.505  12.777  20.703  1    25.838  ? 494  ASN   B ND2 1 2 
ATOM   8989  N  N   . VAL   B 1  495 ? 8.07    7.72    20.225  1    23.602  ? 495  VAL   B N   1 2 
ATOM   8990  C  CA  . VAL   B 1  495 ? 7.2     6.566   20.228  1    23.998  ? 495  VAL   B CA  1 2 
ATOM   8991  C  C   . VAL   B 1  495 ? 5.836   6.91    20.824  1    27.602  ? 495  VAL   B C   1 2 
ATOM   8992  O  O   . VAL   B 1  495 ? 5.341   6.198   21.712  1    27.287  ? 495  VAL   B O   1 2 
ATOM   8993  C  CB  . VAL   B 1  495 ? 7.854   5.394   20.978  1    27.969  ? 495  VAL   B CB  1 2 
ATOM   8994  C  CG1 . VAL   B 1  495 ? 7.087   4.117   20.676  1    29.666  ? 495  VAL   B CG1 1 2 
ATOM   8995  C  CG2 . VAL   B 1  495 ? 9.325   5.253   20.573  1    27.392  ? 495  VAL   B CG2 1 2 
ATOM   8996  N  N   . THR   B 1  496 ? 5.205   7.981   20.334  1    22.916  ? 496  THR   B N   1 2 
ATOM   8997  C  CA  . THR   B 1  496 ? 3.85    8.255   20.793  1    23.447  ? 496  THR   B CA  1 2 
ATOM   8998  C  C   . THR   B 1  496 ? 2.951   7.967   19.6    1    20.653  ? 496  THR   B C   1 2 
ATOM   8999  O  O   . THR   B 1  496 ? 3.159   8.569   18.545  1    22.093  ? 496  THR   B O   1 2 
ATOM   9000  C  CB  . THR   B 1  496 ? 3.714   9.727   21.208  1    24.418  ? 496  THR   B CB  1 2 
ATOM   9001  O  OG1 . THR   B 1  496 ? 4.75    9.984   22.161  1    28.71   ? 496  THR   B OG1 1 2 
ATOM   9002  C  CG2 . THR   B 1  496 ? 2.329   10.113  21.717  1    22.886  ? 496  THR   B CG2 1 2 
ATOM   9003  N  N   . PRO   B 1  497 ? 1.938   7.089   19.714  1    20.661  ? 497  PRO   B N   1 2 
ATOM   9004  C  CA  . PRO   B 1  497 ? 1.035   6.801   18.588  1    20.868  ? 497  PRO   B CA  1 2 
ATOM   9005  C  C   . PRO   B 1  497 ? 0.341   8.08    18.127  1    18.923  ? 497  PRO   B C   1 2 
ATOM   9006  O  O   . PRO   B 1  497 ? 0.186   9.03    18.923  1    18.365  ? 497  PRO   B O   1 2 
ATOM   9007  C  CB  . PRO   B 1  497 ? 0.012   5.805   19.133  1    21.078  ? 497  PRO   B CB  1 2 
ATOM   9008  C  CG  . PRO   B 1  497 ? 0.72    5.219   20.362  1    22.047  ? 497  PRO   B CG  1 2 
ATOM   9009  C  CD  . PRO   B 1  497 ? 1.58    6.336   20.944  1    22.568  ? 497  PRO   B CD  1 2 
ATOM   9010  N  N   . TYR   B 1  498 ? -0.073  8.056   16.857  1    17.056  ? 498  TYR   B N   1 2 
ATOM   9011  C  CA  . TYR   B 1  498 ? -0.581  9.251   16.206  1    16.155  ? 498  TYR   B CA  1 2 
ATOM   9012  C  C   . TYR   B 1  498 ? -2.057  9.151   15.824  1    16.356  ? 498  TYR   B C   1 2 
ATOM   9013  O  O   . TYR   B 1  498 ? -2.696  10.175  15.604  1    17.263  ? 498  TYR   B O   1 2 
ATOM   9014  C  CB  . TYR   B 1  498 ? 0.283   9.564   14.972  1    14.319  ? 498  TYR   B CB  1 2 
ATOM   9015  C  CG  . TYR   B 1  498 ? 0.35    11.061  14.769  1    13.849  ? 498  TYR   B CG  1 2 
ATOM   9016  C  CD1 . TYR   B 1  498 ? 1.102   11.83   15.677  1    13.697  ? 498  TYR   B CD1 1 2 
ATOM   9017  C  CD2 . TYR   B 1  498 ? -0.437  11.707  13.81   1    13.36   ? 498  TYR   B CD2 1 2 
ATOM   9018  C  CE1 . TYR   B 1  498 ? 1.186   13.209  15.543  1    13.979  ? 498  TYR   B CE1 1 2 
ATOM   9019  C  CE2 . TYR   B 1  498 ? -0.338  13.088  13.659  1    13.327  ? 498  TYR   B CE2 1 2 
ATOM   9020  C  CZ  . TYR   B 1  498 ? 0.437   13.836  14.548  1    14.108  ? 498  TYR   B CZ  1 2 
ATOM   9021  O  OH  . TYR   B 1  498 ? 0.569   15.2    14.423  1    14.076  ? 498  TYR   B OH  1 2 
ATOM   9022  N  N   . ILE   B 1  499 ? -2.587  7.94    15.618  1    16.767  ? 499  ILE   B N   1 2 
ATOM   9023  C  CA  . ILE   B 1  499 ? -3.927  7.788   15.06   1    16.344  ? 499  ILE   B CA  1 2 
ATOM   9024  C  C   . ILE   B 1  499 ? -4.98   8.452   15.991  1    18.274  ? 499  ILE   B C   1 2 
ATOM   9025  O  O   . ILE   B 1  499 ? -6.027  8.914   15.524  1    16.821  ? 499  ILE   B O   1 2 
ATOM   9026  C  CB  . ILE   B 1  499 ? -4.279  6.334   14.719  1    17.065  ? 499  ILE   B CB  1 2 
ATOM   9027  C  CG1 . ILE   B 1  499 ? -5.539  6.235   13.818  1    17.184  ? 499  ILE   B CG1 1 2 
ATOM   9028  C  CG2 . ILE   B 1  499 ? -4.488  5.55    16.022  1    17.216  ? 499  ILE   B CG2 1 2 
ATOM   9029  C  CD1 . ILE   B 1  499 ? -5.352  6.842   12.422  1    16.96   ? 499  ILE   B CD1 1 2 
ATOM   9030  N  N   . ARG   B 1  500 ? -4.636  8.586   17.289  1    17.456  ? 500  ARG   B N   1 2 
ATOM   9031  C  CA  . ARG   B 1  500 ? -5.456  9.278   18.273  1    17.721  ? 500  ARG   B CA  1 2 
ATOM   9032  C  C   . ARG   B 1  500 ? -5.785  10.697  17.806  1    17.107  ? 500  ARG   B C   1 2 
ATOM   9033  O  O   . ARG   B 1  500 ? -6.861  11.176  18.153  1    17.057  ? 500  ARG   B O   1 2 
ATOM   9034  C  CB  . ARG   B 1  500 ? -4.727  9.31    19.615  1    17.87   ? 500  ARG   B CB  1 2 
ATOM   9035  C  CG  . ARG   B 1  500 ? -3.331  9.913   19.439  1    19.106  ? 500  ARG   B CG  1 2 
ATOM   9036  C  CD  . ARG   B 1  500 ? -2.485  9.905   20.734  1    20.597  ? 500  ARG   B CD  1 2 
ATOM   9037  N  NE  . ARG   B 1  500 ? -2.394  8.516   21.206  1    20.705  ? 500  ARG   B NE  1 2 
ATOM   9038  C  CZ  . ARG   B 1  500 ? -1.725  8.133   22.298  1    24.083  ? 500  ARG   B CZ  1 2 
ATOM   9039  N  NH1 . ARG   B 1  500 ? -1.116  9.051   23.061  1    21.601  ? 500  ARG   B NH1 1 2 
ATOM   9040  N  NH2 . ARG   B 1  500 ? -1.65   6.813   22.566  1    23.367  ? 500  ARG   B NH2 1 2 
ATOM   9041  N  N   . TYR   B 1  501 ? -4.88   11.35   17.046  1    15.663  ? 501  TYR   B N   1 2 
ATOM   9042  C  CA  . TYR   B 1  501 ? -5.177  12.73   16.663  1    16.414  ? 501  TYR   B CA  1 2 
ATOM   9043  C  C   . TYR   B 1  501 ? -6.157  12.77   15.505  1    16.468  ? 501  TYR   B C   1 2 
ATOM   9044  O  O   . TYR   B 1  501 ? -7.01   13.641  15.446  1    16.599  ? 501  TYR   B O   1 2 
ATOM   9045  C  CB  . TYR   B 1  501 ? -3.93   13.489  16.223  1    16.124  ? 501  TYR   B CB  1 2 
ATOM   9046  C  CG  . TYR   B 1  501 ? -2.97   13.544  17.411  1    17.255  ? 501  TYR   B CG  1 2 
ATOM   9047  C  CD1 . TYR   B 1  501 ? -3.251  14.295  18.554  1    17.664  ? 501  TYR   B CD1 1 2 
ATOM   9048  C  CD2 . TYR   B 1  501 ? -1.778  12.853  17.366  1    15.725  ? 501  TYR   B CD2 1 2 
ATOM   9049  C  CE1 . TYR   B 1  501 ? -2.359  14.346  19.618  1    16.756  ? 501  TYR   B CE1 1 2 
ATOM   9050  C  CE2 . TYR   B 1  501 ? -0.902  12.857  18.432  1    16.161  ? 501  TYR   B CE2 1 2 
ATOM   9051  C  CZ  . TYR   B 1  501 ? -1.182  13.628  19.539  1    17.552  ? 501  TYR   B CZ  1 2 
ATOM   9052  O  OH  . TYR   B 1  501 ? -0.193  13.612  20.479  1    18.394  ? 501  TYR   B OH  1 2 
ATOM   9053  N  N   . PHE   B 1  502 ? -6.037  11.844  14.556  1    16.549  ? 502  PHE   B N   1 2 
ATOM   9054  C  CA  . PHE   B 1  502 ? -7.099  11.756  13.552  1    17.291  ? 502  PHE   B CA  1 2 
ATOM   9055  C  C   . PHE   B 1  502 ? -8.472  11.456  14.2    1    18.796  ? 502  PHE   B C   1 2 
ATOM   9056  O  O   . PHE   B 1  502 ? -9.464  12.07   13.864  1    19.102  ? 502  PHE   B O   1 2 
ATOM   9057  C  CB  . PHE   B 1  502 ? -6.744  10.652  12.54   1    18.22   ? 502  PHE   B CB  1 2 
ATOM   9058  C  CG  . PHE   B 1  502 ? -7.793  10.531  11.429  1    20.062  ? 502  PHE   B CG  1 2 
ATOM   9059  C  CD1 . PHE   B 1  502 ? -7.841  11.474  10.393  1    19.531  ? 502  PHE   B CD1 1 2 
ATOM   9060  C  CD2 . PHE   B 1  502 ? -8.774  9.547   11.476  1    21.181  ? 502  PHE   B CD2 1 2 
ATOM   9061  C  CE1 . PHE   B 1  502 ? -8.787  11.335  9.363   1    21.687  ? 502  PHE   B CE1 1 2 
ATOM   9062  C  CE2 . PHE   B 1  502 ? -9.717  9.419   10.468  1    23.224  ? 502  PHE   B CE2 1 2 
ATOM   9063  C  CZ  . PHE   B 1  502 ? -9.751  10.355  9.44    1    23.199  ? 502  PHE   B CZ  1 2 
ATOM   9064  N  N   . VAL   B 1  503 ? -8.541  10.501  15.128  1    18.677  ? 503  VAL   B N   1 2 
ATOM   9065  C  CA  . VAL   B 1  503 ? -9.783  10.209  15.853  1    20.316  ? 503  VAL   B CA  1 2 
ATOM   9066  C  C   . VAL   B 1  503 ? -10.335 11.464  16.56   1    20.204  ? 503  VAL   B C   1 2 
ATOM   9067  O  O   . VAL   B 1  503 ? -11.536 11.746  16.446  1    21.407  ? 503  VAL   B O   1 2 
ATOM   9068  C  CB  . VAL   B 1  503 ? -9.576  9.028   16.822  1    20.232  ? 503  VAL   B CB  1 2 
ATOM   9069  C  CG1 . VAL   B 1  503 ? -10.77  8.792   17.747  1    21.517  ? 503  VAL   B CG1 1 2 
ATOM   9070  C  CG2 . VAL   B 1  503 ? -9.288  7.76    16.01   1    20.449  ? 503  VAL   B CG2 1 2 
ATOM   9071  N  N   A SER   B 1  504 ? -9.472  12.198  17.273  0.56 19.521  ? 504  SER   B N   1 2 
ATOM   9072  N  N   B SER   B 1  504 ? -9.438  12.211  17.212  0.44 19.011  ? 504  SER   B N   1 2 
ATOM   9073  C  CA  A SER   B 1  504 ? -9.857  13.414  17.996  0.56 19.818  ? 504  SER   B CA  1 2 
ATOM   9074  C  CA  B SER   B 1  504 ? -9.782  13.376  18.023  0.44 18.888  ? 504  SER   B CA  1 2 
ATOM   9075  C  C   A SER   B 1  504 ? -10.476 14.44   17.062  0.56 20.045  ? 504  SER   B C   1 2 
ATOM   9076  C  C   B SER   B 1  504 ? -10.255 14.556  17.18   0.44 19.424  ? 504  SER   B C   1 2 
ATOM   9077  O  O   A SER   B 1  504 ? -11.489 15.066  17.385  0.56 19.46   ? 504  SER   B O   1 2 
ATOM   9078  O  O   B SER   B 1  504 ? -11.045 15.366  17.665  0.44 19.74   ? 504  SER   B O   1 2 
ATOM   9079  C  CB  A SER   B 1  504 ? -8.694  14.05   18.67   0.56 20.164  ? 504  SER   B CB  1 2 
ATOM   9080  C  CB  B SER   B 1  504 ? -8.659  13.751  18.952  0.44 18.128  ? 504  SER   B CB  1 2 
ATOM   9081  O  OG  A SER   B 1  504 ? -9.061  15.331  19.176  0.56 23.63   ? 504  SER   B OG  1 2 
ATOM   9082  O  OG  B SER   B 1  504 ? -7.546  14.326  18.284  0.44 16.972  ? 504  SER   B OG  1 2 
ATOM   9083  N  N   . PHE   B 1  505 ? -9.832  14.617  15.905  1    19.297  ? 505  PHE   B N   1 2 
ATOM   9084  C  CA  . PHE   B 1  505 ? -10.194 15.715  15.033  1    21.01   ? 505  PHE   B CA  1 2 
ATOM   9085  C  C   . PHE   B 1  505 ? -11.619 15.486  14.543  1    22.733  ? 505  PHE   B C   1 2 
ATOM   9086  O  O   . PHE   B 1  505 ? -12.362 16.459  14.426  1    25.757  ? 505  PHE   B O   1 2 
ATOM   9087  C  CB  . PHE   B 1  505 ? -9.162  16.052  13.955  1    19.721  ? 505  PHE   B CB  1 2 
ATOM   9088  C  CG  . PHE   B 1  505 ? -8.103  17.044  14.381  1    22.235  ? 505  PHE   B CG  1 2 
ATOM   9089  C  CD1 . PHE   B 1  505 ? -7.343  16.819  15.51   1    19.343  ? 505  PHE   B CD1 1 2 
ATOM   9090  C  CD2 . PHE   B 1  505 ? -7.839  18.179  13.61   1    23.224  ? 505  PHE   B CD2 1 2 
ATOM   9091  C  CE1 . PHE   B 1  505 ? -6.319  17.679  15.846  1    23.727  ? 505  PHE   B CE1 1 2 
ATOM   9092  C  CE2 . PHE   B 1  505 ? -6.798  19.049  13.947  1    23.293  ? 505  PHE   B CE2 1 2 
ATOM   9093  C  CZ  . PHE   B 1  505 ? -6.025  18.805  15.074  1    26.27   ? 505  PHE   B CZ  1 2 
ATOM   9094  N  N   . VAL   B 1  506 ? -12.003 14.213  14.373  1    22.256  ? 506  VAL   B N   1 2 
ATOM   9095  C  CA  . VAL   B 1  506 ? -13.393 13.893  14.078  1    25.158  ? 506  VAL   B CA  1 2 
ATOM   9096  C  C   . VAL   B 1  506 ? -14.228 13.93   15.369  1    26.116  ? 506  VAL   B C   1 2 
ATOM   9097  O  O   . VAL   B 1  506 ? -15.342 14.47   15.396  1    28.695  ? 506  VAL   B O   1 2 
ATOM   9098  C  CB  . VAL   B 1  506 ? -13.512 12.497  13.42   1    26.274  ? 506  VAL   B CB  1 2 
ATOM   9099  C  CG1 . VAL   B 1  506 ? -14.983 12.079  13.237  1    27.924  ? 506  VAL   B CG1 1 2 
ATOM   9100  C  CG2 . VAL   B 1  506 ? -12.711 12.441  12.118  1    25.483  ? 506  VAL   B CG2 1 2 
ATOM   9101  N  N   . LEU   B 1  507 ? -13.711 13.326  16.435  1    25.738  ? 507  LEU   B N   1 2 
ATOM   9102  C  CA  . LEU   B 1  507 ? -14.468 13.213  17.67   1    27.627  ? 507  LEU   B CA  1 2 
ATOM   9103  C  C   . LEU   B 1  507 ? -14.801 14.588  18.275  1    26.759  ? 507  LEU   B C   1 2 
ATOM   9104  O  O   . LEU   B 1  507 ? -15.915 14.766  18.783  1    27.974  ? 507  LEU   B O   1 2 
ATOM   9105  C  CB  . LEU   B 1  507 ? -13.65  12.315  18.592  1    31.06   ? 507  LEU   B CB  1 2 
ATOM   9106  C  CG  . LEU   B 1  507 ? -14.285 11.822  19.893  1    33.303  ? 507  LEU   B CG  1 2 
ATOM   9107  C  CD1 . LEU   B 1  507 ? -15.254 10.65   19.668  1    34.73   ? 507  LEU   B CD1 1 2 
ATOM   9108  C  CD2 . LEU   B 1  507 ? -13.122 11.33   20.772  1    34.434  ? 507  LEU   B CD2 1 2 
ATOM   9109  N  N   . GLN   B 1  508 ? -13.916 15.579  18.157  1    22.951  ? 508  GLN   B N   1 2 
ATOM   9110  C  CA  . GLN   B 1  508 ? -14.157 16.891  18.792  1    23.588  ? 508  GLN   B CA  1 2 
ATOM   9111  C  C   . GLN   B 1  508 ? -15.409 17.591  18.256  1    24.671  ? 508  GLN   B C   1 2 
ATOM   9112  O  O   . GLN   B 1  508 ? -16.089 18.308  19.003  1    23.303  ? 508  GLN   B O   1 2 
ATOM   9113  C  CB  . GLN   B 1  508 ? -12.896 17.767  18.763  1    21.189  ? 508  GLN   B CB  1 2 
ATOM   9114  C  CG  . GLN   B 1  508 ? -12.518 18.318  17.397  1    19.729  ? 508  GLN   B CG  1 2 
ATOM   9115  C  CD  . GLN   B 1  508 ? -11.142 18.975  17.459  1    20.981  ? 508  GLN   B CD  1 2 
ATOM   9116  O  OE1 . GLN   B 1  508 ? -11     20.173  17.231  1    22.327  ? 508  GLN   B OE1 1 2 
ATOM   9117  N  NE2 . GLN   B 1  508 ? -10.116 18.229  17.844  1    21.035  ? 508  GLN   B NE2 1 2 
ATOM   9118  N  N   . PHE   B 1  509 ? -15.738 17.332  16.977  1    24.727  ? 509  PHE   B N   1 2 
ATOM   9119  C  CA  . PHE   B 1  509 ? -16.948 17.91   16.402  1    26.175  ? 509  PHE   B CA  1 2 
ATOM   9120  C  C   . PHE   B 1  509 ? -18.204 17.215  16.911  1    26.83   ? 509  PHE   B C   1 2 
ATOM   9121  O  O   . PHE   B 1  509 ? -19.208 17.886  17.096  1    27.886  ? 509  PHE   B O   1 2 
ATOM   9122  C  CB  . PHE   B 1  509 ? -16.9   17.964  14.873  1    24.762  ? 509  PHE   B CB  1 2 
ATOM   9123  C  CG  . PHE   B 1  509 ? -15.86  18.981  14.462  1    24.263  ? 509  PHE   B CG  1 2 
ATOM   9124  C  CD1 . PHE   B 1  509 ? -16.192 20.342  14.394  1    24.735  ? 509  PHE   B CD1 1 2 
ATOM   9125  C  CD2 . PHE   B 1  509 ? -14.527 18.597  14.257  1    21.18   ? 509  PHE   B CD2 1 2 
ATOM   9126  C  CE1 . PHE   B 1  509 ? -15.231 21.288  14.027  1    22.594  ? 509  PHE   B CE1 1 2 
ATOM   9127  C  CE2 . PHE   B 1  509 ? -13.59  19.537  13.894  1    20.941  ? 509  PHE   B CE2 1 2 
ATOM   9128  C  CZ  . PHE   B 1  509 ? -13.939 20.88   13.783  1    21.822  ? 509  PHE   B CZ  1 2 
ATOM   9129  N  N   . GLN   B 1  510 ? -18.114 15.909  17.195  1    28.469  ? 510  GLN   B N   1 2 
ATOM   9130  C  CA  . GLN   B 1  510 ? -19.226 15.167  17.763  1    30.793  ? 510  GLN   B CA  1 2 
ATOM   9131  C  C   . GLN   B 1  510 ? -19.501 15.68   19.177  1    31.808  ? 510  GLN   B C   1 2 
ATOM   9132  O  O   . GLN   B 1  510 ? -20.658 15.812  19.583  1    29.756  ? 510  GLN   B O   1 2 
ATOM   9133  C  CB  . GLN   B 1  510 ? -19.019 13.649  17.833  1    30.309  ? 510  GLN   B CB  1 2 
ATOM   9134  C  CG  . GLN   B 1  510 ? -18.871 12.984  16.465  1    31.712  ? 510  GLN   B CG  1 2 
ATOM   9135  C  CD  . GLN   B 1  510 ? -18.658 11.485  16.519  1    32.274  ? 510  GLN   B CD  1 2 
ATOM   9136  O  OE1 . GLN   B 1  510 ? -17.555 10.963  16.269  1    32.228  ? 510  GLN   B OE1 1 2 
ATOM   9137  N  NE2 . GLN   B 1  510 ? -19.738 10.776  16.803  1    33.288  ? 510  GLN   B NE2 1 2 
ATOM   9138  N  N   . PHE   B 1  511 ? -18.422 15.852  19.941  1    31.451  ? 511  PHE   B N   1 2 
ATOM   9139  C  CA  . PHE   B 1  511 ? -18.519 16.361  21.303  1    31.721  ? 511  PHE   B CA  1 2 
ATOM   9140  C  C   . PHE   B 1  511 ? -19.092 17.776  21.302  1    30.571  ? 511  PHE   B C   1 2 
ATOM   9141  O  O   . PHE   B 1  511 ? -19.968 18.094  22.117  1    31.552  ? 511  PHE   B O   1 2 
ATOM   9142  C  CB  . PHE   B 1  511 ? -17.116 16.407  21.891  1    30.152  ? 511  PHE   B CB  1 2 
ATOM   9143  C  CG  . PHE   B 1  511 ? -16.552 15.09   22.393  1    33.105  ? 511  PHE   B CG  1 2 
ATOM   9144  C  CD1 . PHE   B 1  511 ? -17.251 13.907  22.225  1    34.871  ? 511  PHE   B CD1 1 2 
ATOM   9145  C  CD2 . PHE   B 1  511 ? -15.275 15.042  22.958  1    33.575  ? 511  PHE   B CD2 1 2 
ATOM   9146  C  CE1 . PHE   B 1  511 ? -16.701 12.713  22.626  1    34.688  ? 511  PHE   B CE1 1 2 
ATOM   9147  C  CE2 . PHE   B 1  511 ? -14.745 13.847  23.404  1    33.676  ? 511  PHE   B CE2 1 2 
ATOM   9148  C  CZ  . PHE   B 1  511 ? -15.47  12.684  23.234  1    34.61   ? 511  PHE   B CZ  1 2 
ATOM   9149  N  N   . HIS   B 1  512 ? -18.593 18.612  20.386  1    27.136  ? 512  HIS   B N   1 2 
ATOM   9150  C  CA  . HIS   B 1  512 ? -18.98  20.007  20.299  1    27.708  ? 512  HIS   B CA  1 2 
ATOM   9151  C  C   . HIS   B 1  512 ? -20.486 20.108  20.029  1    29.866  ? 512  HIS   B C   1 2 
ATOM   9152  O  O   . HIS   B 1  512 ? -21.196 20.89   20.678  1    29.139  ? 512  HIS   B O   1 2 
ATOM   9153  C  CB  . HIS   B 1  512 ? -18.143 20.673  19.201  1    25.635  ? 512  HIS   B CB  1 2 
ATOM   9154  C  CG  . HIS   B 1  512 ? -18.383 22.132  19.02   1    25.895  ? 512  HIS   B CG  1 2 
ATOM   9155  N  ND1 . HIS   B 1  512 ? -18.177 23.076  20.009  1    26.16   ? 512  HIS   B ND1 1 2 
ATOM   9156  C  CD2 . HIS   B 1  512 ? -18.893 22.802  17.977  1    27.015  ? 512  HIS   B CD2 1 2 
ATOM   9157  C  CE1 . HIS   B 1  512 ? -18.464 24.276  19.536  1    26.202  ? 512  HIS   B CE1 1 2 
ATOM   9158  N  NE2 . HIS   B 1  512 ? -18.91  24.135  18.301  1    26.448  ? 512  HIS   B NE2 1 2 
ATOM   9159  N  N   . GLU   B 1  513 ? -20.988 19.33   19.049  1    31.106  ? 513  GLU   B N   1 2 
ATOM   9160  C  CA  . GLU   B 1  513 ? -22.426 19.37   18.754  1    32.643  ? 513  GLU   B CA  1 2 
ATOM   9161  C  C   . GLU   B 1  513 ? -23.21  18.842  19.956  1    31.99   ? 513  GLU   B C   1 2 
ATOM   9162  O  O   . GLU   B 1  513 ? -24.271 19.359  20.31   1    34.561  ? 513  GLU   B O   1 2 
ATOM   9163  C  CB  . GLU   B 1  513 ? -22.735 18.624  17.444  1    35.608  ? 513  GLU   B CB  1 2 
ATOM   9164  C  CG  . GLU   B 1  513 ? -24.222 18.498  17.089  1    40.942  ? 513  GLU   B CG  1 2 
ATOM   9165  C  CD  . GLU   B 1  513 ? -24.396 17.718  15.778  1    46.718  ? 513  GLU   B CD  1 2 
ATOM   9166  O  OE1 . GLU   B 1  513 ? -24.286 16.479  15.821  1    46.666  ? 513  GLU   B OE1 1 2 
ATOM   9167  O  OE2 . GLU   B 1  513 ? -24.584 18.311  14.692  1    50.663  ? 513  GLU   B OE2 1 2 
ATOM   9168  N  N   . ALA   B 1  514 ? -22.754 17.759  20.579  1    31.081  ? 514  ALA   B N   1 2 
ATOM   9169  C  CA  . ALA   B 1  514 ? -23.484 17.296  21.753  1    32.904  ? 514  ALA   B CA  1 2 
ATOM   9170  C  C   . ALA   B 1  514 ? -23.485 18.361  22.86   1    34.007  ? 514  ALA   B C   1 2 
ATOM   9171  O  O   . ALA   B 1  514 ? -24.466 18.472  23.585  1    35.606  ? 514  ALA   B O   1 2 
ATOM   9172  C  CB  . ALA   B 1  514 ? -22.925 15.999  22.28   1    33.244  ? 514  ALA   B CB  1 2 
ATOM   9173  N  N   . LEU   B 1  515 ? -22.36  19.071  23.04   1    32.952  ? 515  LEU   B N   1 2 
ATOM   9174  C  CA  . LEU   B 1  515 ? -22.209 20.027  24.131  1    33.575  ? 515  LEU   B CA  1 2 
ATOM   9175  C  C   . LEU   B 1  515 ? -23.091 21.25   23.912  1    33.575  ? 515  LEU   B C   1 2 
ATOM   9176  O  O   . LEU   B 1  515 ? -23.785 21.682  24.851  1    34.079  ? 515  LEU   B O   1 2 
ATOM   9177  C  CB  . LEU   B 1  515 ? -20.757 20.367  24.456  1    30.928  ? 515  LEU   B CB  1 2 
ATOM   9178  C  CG  . LEU   B 1  515 ? -19.979 19.239  25.146  1    31.936  ? 515  LEU   B CG  1 2 
ATOM   9179  C  CD1 . LEU   B 1  515 ? -18.523 19.569  25.461  1    31.486  ? 515  LEU   B CD1 1 2 
ATOM   9180  C  CD2 . LEU   B 1  515 ? -20.671 18.763  26.432  1    36.595  ? 515  LEU   B CD2 1 2 
ATOM   9181  N  N   . CYS   B 1  516 ? -23.087 21.749  22.667  1    33.731  ? 516  CYS   B N   1 2 
ATOM   9182  C  CA  . CYS   B 1  516 ? -23.861 22.907  22.26   1    36.817  ? 516  CYS   B CA  1 2 
ATOM   9183  C  C   . CYS   B 1  516 ? -25.35  22.611  22.355  1    40.73   ? 516  CYS   B C   1 2 
ATOM   9184  O  O   . CYS   B 1  516 ? -26.141 23.523  22.621  1    43.646  ? 516  CYS   B O   1 2 
ATOM   9185  C  CB  . CYS   B 1  516 ? -23.52  23.339  20.844  1    39.746  ? 516  CYS   B CB  1 2 
ATOM   9186  S  SG  . CYS   B 1  516 ? -21.79  23.908  20.792  1    43.394  ? 516  CYS   B SG  1 2 
ATOM   9187  N  N   . LYS   B 1  517 ? -25.712 21.333  22.222  1    40.632  ? 517  LYS   B N   1 2 
ATOM   9188  C  CA  . LYS   B 1  517 ? -27.11  20.958  22.438  1    44.372  ? 517  LYS   B CA  1 2 
ATOM   9189  C  C   . LYS   B 1  517 ? -27.449 20.951  23.936  1    44.328  ? 517  LYS   B C   1 2 
ATOM   9190  O  O   . LYS   B 1  517 ? -28.488 21.45   24.348  1    47.164  ? 517  LYS   B O   1 2 
ATOM   9191  C  CB  . LYS   B 1  517 ? -27.449 19.679  21.652  1    46.04   ? 517  LYS   B CB  1 2 
ATOM   9192  C  CG  . LYS   B 1  517 ? -28.942 19.372  21.658  1    50.181  ? 517  LYS   B CG  1 2 
ATOM   9193  C  CD  . LYS   B 1  517 ? -29.416 18.311  20.672  1    54.502  ? 517  LYS   B CD  1 2 
ATOM   9194  C  CE  . LYS   B 1  517 ? -30.867 18.055  21.06   1    58.411  ? 517  LYS   B CE  1 2 
ATOM   9195  N  NZ  . LYS   B 1  517 ? -31.46  17.034  20.199  1    62.807  ? 517  LYS   B NZ  1 2 
ATOM   9196  N  N   . GLU   B 1  518 ? -26.598 20.348  24.763  1    42.477  ? 518  GLU   B N   1 2 
ATOM   9197  C  CA  . GLU   B 1  518 ? -26.833 20.322  26.188  1    44.373  ? 518  GLU   B CA  1 2 
ATOM   9198  C  C   . GLU   B 1  518 ? -26.879 21.76   26.694  1    46.338  ? 518  GLU   B C   1 2 
ATOM   9199  O  O   . GLU   B 1  518 ? -27.704 22.059  27.547  1    47.363  ? 518  GLU   B O   1 2 
ATOM   9200  C  CB  . GLU   B 1  518 ? -25.88  19.297  26.807  1    46.116  ? 518  GLU   B CB  1 2 
ATOM   9201  C  CG  . GLU   B 1  518 ? -25.892 19.203  28.332  1    48.085  ? 518  GLU   B CG  1 2 
ATOM   9202  C  CD  . GLU   B 1  518 ? -26.944 18.3    28.989  1    53.92   ? 518  GLU   B CD  1 2 
ATOM   9203  O  OE1 . GLU   B 1  518 ? -26.994 18.311  30.267  1    48.66   ? 518  GLU   B OE1 1 2 
ATOM   9204  O  OE2 . GLU   B 1  518 ? -27.683 17.591  28.239  1    54.349  ? 518  GLU   B OE2 1 2 
ATOM   9205  N  N   . ALA   B 1  519 ? -26.075 22.662  26.106  1    45.84   ? 519  ALA   B N   1 2 
ATOM   9206  C  CA  . ALA   B 1  519 ? -26.044 24.074  26.483  1    44.472  ? 519  ALA   B CA  1 2 
ATOM   9207  C  C   . ALA   B 1  519 ? -27.359 24.801  26.185  1    46.249  ? 519  ALA   B C   1 2 
ATOM   9208  O  O   . ALA   B 1  519 ? -27.625 25.871  26.735  1    49.237  ? 519  ALA   B O   1 2 
ATOM   9209  C  CB  . ALA   B 1  519 ? -24.856 24.777  25.847  1    39.552  ? 519  ALA   B CB  1 2 
ATOM   9210  N  N   . GLY   B 1  520 ? -28.182 24.252  25.292  1    46.154  ? 520  GLY   B N   1 2 
ATOM   9211  C  CA  . GLY   B 1  520 ? -29.42  24.906  24.912  1    47.204  ? 520  GLY   B CA  1 2 
ATOM   9212  C  C   . GLY   B 1  520 ? -29.202 25.927  23.798  1    46.65   ? 520  GLY   B C   1 2 
ATOM   9213  O  O   . GLY   B 1  520 ? -30.108 26.691  23.494  1    46.631  ? 520  GLY   B O   1 2 
ATOM   9214  N  N   . TYR   B 1  521 ? -28.014 25.926  23.177  1    42.684  ? 521  TYR   B N   1 2 
ATOM   9215  C  CA  . TYR   B 1  521 ? -27.691 26.844  22.089  1    43.496  ? 521  TYR   B CA  1 2 
ATOM   9216  C  C   . TYR   B 1  521 ? -28.417 26.434  20.806  1    47.717  ? 521  TYR   B C   1 2 
ATOM   9217  O  O   . TYR   B 1  521 ? -28.621 25.251  20.563  1    46.544  ? 521  TYR   B O   1 2 
ATOM   9218  C  CB  . TYR   B 1  521 ? -26.185 26.762  21.793  1    40.838  ? 521  TYR   B CB  1 2 
ATOM   9219  C  CG  . TYR   B 1  521 ? -25.754 27.626  20.616  1    39.468  ? 521  TYR   B CG  1 2 
ATOM   9220  C  CD1 . TYR   B 1  521 ? -25.756 29.019  20.68   1    42.017  ? 521  TYR   B CD1 1 2 
ATOM   9221  C  CD2 . TYR   B 1  521 ? -25.421 27.029  19.41   1    41.185  ? 521  TYR   B CD2 1 2 
ATOM   9222  C  CE1 . TYR   B 1  521 ? -25.411 29.782  19.572  1    43.221  ? 521  TYR   B CE1 1 2 
ATOM   9223  C  CE2 . TYR   B 1  521 ? -25.058 27.772  18.302  1    40.727  ? 521  TYR   B CE2 1 2 
ATOM   9224  C  CZ  . TYR   B 1  521 ? -25.029 29.149  18.393  1    42.223  ? 521  TYR   B CZ  1 2 
ATOM   9225  O  OH  . TYR   B 1  521 ? -24.635 29.776  17.245  1    43.183  ? 521  TYR   B OH  1 2 
ATOM   9226  N  N   . GLU   B 1  522 ? -28.727 27.408  19.939  1    52.877  ? 522  GLU   B N   1 2 
ATOM   9227  C  CA  . GLU   B 1  522 ? -29.667 27.14   18.858  1    56.049  ? 522  GLU   B CA  1 2 
ATOM   9228  C  C   . GLU   B 1  522 ? -29.263 27.752  17.515  1    55.809  ? 522  GLU   B C   1 2 
ATOM   9229  O  O   . GLU   B 1  522 ? -29.968 27.583  16.531  1    61.049  ? 522  GLU   B O   1 2 
ATOM   9230  C  CB  . GLU   B 1  522 ? -31.068 27.628  19.213  1    62.932  ? 522  GLU   B CB  1 2 
ATOM   9231  C  CG  . GLU   B 1  522 ? -31.88  26.611  20.01   1    67.782  ? 522  GLU   B CG  1 2 
ATOM   9232  C  CD  . GLU   B 1  522 ? -33.367 26.866  19.811  1    78.115  ? 522  GLU   B CD  1 2 
ATOM   9233  O  OE1 . GLU   B 1  522 ? -34.002 27.408  20.757  1    79.646  ? 522  GLU   B OE1 1 2 
ATOM   9234  O  OE2 . GLU   B 1  522 ? -33.884 26.538  18.704  1    79.646  ? 522  GLU   B OE2 1 2 
ATOM   9235  N  N   . GLY   B 1  523 ? -28.125 28.442  17.438  1    55.532  ? 523  GLY   B N   1 2 
ATOM   9236  C  CA  . GLY   B 1  523 ? -27.707 29.008  16.164  1    48.68   ? 523  GLY   B CA  1 2 
ATOM   9237  C  C   . GLY   B 1  523 ? -26.848 28.038  15.347  1    44.684  ? 523  GLY   B C   1 2 
ATOM   9238  O  O   . GLY   B 1  523 ? -26.768 26.835  15.622  1    43.005  ? 523  GLY   B O   1 2 
ATOM   9239  N  N   . PRO   B 1  524 ? -26.126 28.548  14.334  1    40.744  ? 524  PRO   B N   1 2 
ATOM   9240  C  CA  . PRO   B 1  524 ? -25.195 27.711  13.585  1    40.599  ? 524  PRO   B CA  1 2 
ATOM   9241  C  C   . PRO   B 1  524 ? -24.151 27.082  14.516  1    39.451  ? 524  PRO   B C   1 2 
ATOM   9242  O  O   . PRO   B 1  524 ? -23.625 27.735  15.425  1    38.957  ? 524  PRO   B O   1 2 
ATOM   9243  C  CB  . PRO   B 1  524 ? -24.565 28.633  12.52   1    40.61   ? 524  PRO   B CB  1 2 
ATOM   9244  C  CG  . PRO   B 1  524 ? -25.358 29.915  12.601  1    42.49   ? 524  PRO   B CG  1 2 
ATOM   9245  C  CD  . PRO   B 1  524 ? -26.129 29.951  13.911  1    41.629  ? 524  PRO   B CD  1 2 
ATOM   9246  N  N   . LEU   B 1  525 ? -23.918 25.783  14.315  1    36.947  ? 525  LEU   B N   1 2 
ATOM   9247  C  CA  . LEU   B 1  525 ? -22.908 25.023  15.041  1    39.055  ? 525  LEU   B CA  1 2 
ATOM   9248  C  C   . LEU   B 1  525 ? -21.595 25.8    15.201  1    37.413  ? 525  LEU   B C   1 2 
ATOM   9249  O  O   . LEU   B 1  525 ? -20.987 25.792  16.291  1    37.981  ? 525  LEU   B O   1 2 
ATOM   9250  C  CB  . LEU   B 1  525 ? -22.683 23.637  14.428  1    39.261  ? 525  LEU   B CB  1 2 
ATOM   9251  C  CG  . LEU   B 1  525 ? -21.956 22.623  15.322  1    41.071  ? 525  LEU   B CG  1 2 
ATOM   9252  C  CD1 . LEU   B 1  525 ? -22.514 22.525  16.744  1    41.726  ? 525  LEU   B CD1 1 2 
ATOM   9253  C  CD2 . LEU   B 1  525 ? -21.974 21.242  14.665  1    42.052  ? 525  LEU   B CD2 1 2 
ATOM   9254  N  N   . HIS   B 1  526 ? -21.14  26.485  14.146  1    34.686  ? 526  HIS   B N   1 2 
ATOM   9255  C  CA  . HIS   B 1  526 ? -19.787 27.032  14.229  1    33.034  ? 526  HIS   B CA  1 2 
ATOM   9256  C  C   . HIS   B 1  526 ? -19.73  28.379  14.96   1    32.534  ? 526  HIS   B C   1 2 
ATOM   9257  O  O   . HIS   B 1  526 ? -18.7   29.077  14.94   1    30.11   ? 526  HIS   B O   1 2 
ATOM   9258  C  CB  . HIS   B 1  526 ? -19.189 27.224  12.843  1    32.593  ? 526  HIS   B CB  1 2 
ATOM   9259  C  CG  . HIS   B 1  526 ? -20.001 28.16   12.032  1    35.731  ? 526  HIS   B CG  1 2 
ATOM   9260  N  ND1 . HIS   B 1  526 ? -21.167 27.771  11.408  1    38.216  ? 526  HIS   B ND1 1 2 
ATOM   9261  C  CD2 . HIS   B 1  526 ? -19.776 29.423  11.695  1    36.426  ? 526  HIS   B CD2 1 2 
ATOM   9262  C  CE1 . HIS   B 1  526 ? -21.671 28.819  10.766  1    39.218  ? 526  HIS   B CE1 1 2 
ATOM   9263  N  NE2 . HIS   B 1  526 ? -20.827 29.828  10.919  1    39.338  ? 526  HIS   B NE2 1 2 
ATOM   9264  N  N   . GLN   B 1  527 ? -20.866 28.773  15.535  1    32.891  ? 527  GLN   B N   1 2 
ATOM   9265  C  CA  . GLN   B 1  527 ? -20.982 30.055  16.223  1    34.272  ? 527  GLN   B CA  1 2 
ATOM   9266  C  C   . GLN   B 1  527 ? -21.296 29.786  17.702  1    33.69   ? 527  GLN   B C   1 2 
ATOM   9267  O  O   . GLN   B 1  527 ? -21.495 30.71   18.478  1    36.318  ? 527  GLN   B O   1 2 
ATOM   9268  C  CB  . GLN   B 1  527 ? -21.963 31.022  15.547  1    38.089  ? 527  GLN   B CB  1 2 
ATOM   9269  C  CG  . GLN   B 1  527 ? -21.414 31.749  14.315  1    39.455  ? 527  GLN   B CG  1 2 
ATOM   9270  C  CD  . GLN   B 1  527 ? -22.393 32.727  13.676  1    44.21   ? 527  GLN   B CD  1 2 
ATOM   9271  O  OE1 . GLN   B 1  527 ? -23.573 32.8    14.023  1    45.082  ? 527  GLN   B OE1 1 2 
ATOM   9272  N  NE2 . GLN   B 1  527 ? -21.928 33.506  12.709  1    47.044  ? 527  GLN   B NE2 1 2 
ATOM   9273  N  N   . CYS   B 1  528 ? -21.391 28.51   18.089  1    31.568  ? 528  CYS   B N   1 2 
ATOM   9274  C  CA  . CYS   B 1  528 ? -21.661 28.136  19.465  1    32.924  ? 528  CYS   B CA  1 2 
ATOM   9275  C  C   . CYS   B 1  528 ? -20.451 28.402  20.377  1    30.767  ? 528  CYS   B C   1 2 
ATOM   9276  O  O   . CYS   B 1  528 ? -19.317 28.016  20.039  1    29.338  ? 528  CYS   B O   1 2 
ATOM   9277  C  CB  . CYS   B 1  528 ? -22.026 26.662  19.503  1    36.708  ? 528  CYS   B CB  1 2 
ATOM   9278  S  SG  . CYS   B 1  528 ? -21.949 25.935  21.161  1    46.567  ? 528  CYS   B SG  1 2 
ATOM   9279  N  N   . ASP   B 1  529 ? -20.749 28.946  21.567  1    29.566  ? 529  ASP   B N   1 2 
ATOM   9280  C  CA  . ASP   B 1  529 ? -19.792 29.126  22.651  1    28.658  ? 529  ASP   B CA  1 2 
ATOM   9281  C  C   . ASP   B 1  529 ? -20.403 28.512  23.915  1    28.388  ? 529  ASP   B C   1 2 
ATOM   9282  O  O   . ASP   B 1  529 ? -21.457 28.974  24.354  1    29.097  ? 529  ASP   B O   1 2 
ATOM   9283  C  CB  . ASP   B 1  529 ? -19.539 30.614  22.9    1    29.037  ? 529  ASP   B CB  1 2 
ATOM   9284  C  CG  . ASP   B 1  529 ? -18.441 30.964  23.907  1    28.283  ? 529  ASP   B CG  1 2 
ATOM   9285  O  OD1 . ASP   B 1  529 ? -17.726 30.053  24.331  1    28.312  ? 529  ASP   B OD1 1 2 
ATOM   9286  O  OD2 . ASP   B 1  529 ? -18.313 32.143  24.302  1    28.563  ? 529  ASP   B OD2 1 2 
ATOM   9287  N  N   . ILE   B 1  530 ? -19.78  27.46   24.46   1    26.587  ? 530  ILE   B N   1 2 
ATOM   9288  C  CA  . ILE   B 1  530 ? -20.322 26.742  25.605  1    28.452  ? 530  ILE   B CA  1 2 
ATOM   9289  C  C   . ILE   B 1  530 ? -19.874 27.384  26.91   1    27.829  ? 530  ILE   B C   1 2 
ATOM   9290  O  O   . ILE   B 1  530 ? -20.249 26.888  27.975  1    28.77   ? 530  ILE   B O   1 2 
ATOM   9291  C  CB  . ILE   B 1  530 ? -19.999 25.24   25.609  1    28.443  ? 530  ILE   B CB  1 2 
ATOM   9292  C  CG1 . ILE   B 1  530 ? -18.484 24.976  25.695  1    27.595  ? 530  ILE   B CG1 1 2 
ATOM   9293  C  CG2 . ILE   B 1  530 ? -20.612 24.573  24.362  1    29.671  ? 530  ILE   B CG2 1 2 
ATOM   9294  C  CD1 . ILE   B 1  530 ? -18.134 23.555  26.08   1    28.539  ? 530  ILE   B CD1 1 2 
ATOM   9295  N  N   . TYR   B 1  531 ? -19.037 28.421  26.822  1    26.647  ? 531  TYR   B N   1 2 
ATOM   9296  C  CA  . TYR   B 1  531 ? -18.602 29.156  28.01   1    26.422  ? 531  TYR   B CA  1 2 
ATOM   9297  C  C   . TYR   B 1  531 ? -19.76  29.371  28.977  1    28.046  ? 531  TYR   B C   1 2 
ATOM   9298  O  O   . TYR   B 1  531 ? -20.812 29.892  28.613  1    29.505  ? 531  TYR   B O   1 2 
ATOM   9299  C  CB  . TYR   B 1  531 ? -18.101 30.541  27.594  1    26.539  ? 531  TYR   B CB  1 2 
ATOM   9300  C  CG  . TYR   B 1  531 ? -17.429 31.403  28.656  1    26.444  ? 531  TYR   B CG  1 2 
ATOM   9301  C  CD1 . TYR   B 1  531 ? -16.375 30.907  29.433  1    26.092  ? 531  TYR   B CD1 1 2 
ATOM   9302  C  CD2 . TYR   B 1  531 ? -17.818 32.731  28.83   1    27.409  ? 531  TYR   B CD2 1 2 
ATOM   9303  C  CE1 . TYR   B 1  531 ? -15.732 31.703  30.363  1    26.28   ? 531  TYR   B CE1 1 2 
ATOM   9304  C  CE2 . TYR   B 1  531 ? -17.221 33.522  29.808  1    28.679  ? 531  TYR   B CE2 1 2 
ATOM   9305  C  CZ  . TYR   B 1  531 ? -16.129 33.015  30.518  1    27.695  ? 531  TYR   B CZ  1 2 
ATOM   9306  O  OH  . TYR   B 1  531 ? -15.538 33.783  31.481  1    28.381  ? 531  TYR   B OH  1 2 
ATOM   9307  N  N   . ARG   B 1  532 ? -19.514 29.05   30.252  1    28.175  ? 532  ARG   B N   1 2 
ATOM   9308  C  CA  . ARG   B 1  532 ? -20.459 29.324  31.332  1    29.762  ? 532  ARG   B CA  1 2 
ATOM   9309  C  C   . ARG   B 1  532 ? -21.68  28.406  31.335  1    31.481  ? 532  ARG   B C   1 2 
ATOM   9310  O  O   . ARG   B 1  532 ? -22.595 28.644  32.131  1    32.55   ? 532  ARG   B O   1 2 
ATOM   9311  C  CB  . ARG   B 1  532 ? -20.914 30.793  31.341  1    30.63   ? 532  ARG   B CB  1 2 
ATOM   9312  C  CG  . ARG   B 1  532 ? -19.835 31.639  32      1    29.878  ? 532  ARG   B CG  1 2 
ATOM   9313  C  CD  . ARG   B 1  532 ? -20.226 33.086  31.986  1    31.585  ? 532  ARG   B CD  1 2 
ATOM   9314  N  NE  . ARG   B 1  532 ? -19.202 33.876  32.678  1    31.947  ? 532  ARG   B NE  1 2 
ATOM   9315  C  CZ  . ARG   B 1  532 ? -19.017 35.187  32.56   1    32.619  ? 532  ARG   B CZ  1 2 
ATOM   9316  N  NH1 . ARG   B 1  532 ? -19.83  35.934  31.827  1    32.302  ? 532  ARG   B NH1 1 2 
ATOM   9317  N  NH2 . ARG   B 1  532 ? -17.989 35.725  33.184  1    32.341  ? 532  ARG   B NH2 1 2 
ATOM   9318  N  N   . SER   B 1  533 ? -21.728 27.372  30.471  1    32.93   ? 533  SER   B N   1 2 
ATOM   9319  C  CA  . SER   B 1  533 ? -22.81  26.383  30.511  1    34.419  ? 533  SER   B CA  1 2 
ATOM   9320  C  C   . SER   B 1  533 ? -22.484 25.281  31.524  1    34.832  ? 533  SER   B C   1 2 
ATOM   9321  O  O   . SER   B 1  533 ? -21.602 24.443  31.277  1    34.074  ? 533  SER   B O   1 2 
ATOM   9322  C  CB  . SER   B 1  533 ? -23.148 25.82   29.111  1    36.114  ? 533  SER   B CB  1 2 
ATOM   9323  O  OG  . SER   B 1  533 ? -24.167 24.822  29.182  1    36.902  ? 533  SER   B OG  1 2 
ATOM   9324  N  N   . THR   B 1  534 ? -23.154 25.337  32.688  1    36.578  ? 534  THR   B N   1 2 
ATOM   9325  C  CA  . THR   B 1  534 ? -23.066 24.309  33.72   1    39.356  ? 534  THR   B CA  1 2 
ATOM   9326  C  C   . THR   B 1  534 ? -23.6   22.96   33.213  1    39.985  ? 534  THR   B C   1 2 
ATOM   9327  O  O   . THR   B 1  534 ? -23.035 21.935  33.559  1    40.758  ? 534  THR   B O   1 2 
ATOM   9328  C  CB  . THR   B 1  534 ? -23.61  24.723  35.1    1    43.6    ? 534  THR   B CB  1 2 
ATOM   9329  O  OG1 . THR   B 1  534 ? -25.008 24.969  35.062  1    43.357  ? 534  THR   B OG1 1 2 
ATOM   9330  C  CG2 . THR   B 1  534 ? -22.995 26.001  35.642  1    44.8    ? 534  THR   B CG2 1 2 
ATOM   9331  N  N   . LYS   B 1  535 ? -24.62  22.951  32.346  1    42.111  ? 535  LYS   B N   1 2 
ATOM   9332  C  CA  . LYS   B 1  535 ? -25.168 21.722  31.774  1    44.135  ? 535  LYS   B CA  1 2 
ATOM   9333  C  C   . LYS   B 1  535 ? -24.161 21.032  30.838  1    41.848  ? 535  LYS   B C   1 2 
ATOM   9334  O  O   . LYS   B 1  535 ? -23.878 19.833  30.973  1    43.247  ? 535  LYS   B O   1 2 
ATOM   9335  C  CB  . LYS   B 1  535 ? -26.477 22.009  31.033  1    47.107  ? 535  LYS   B CB  1 2 
ATOM   9336  C  CG  . LYS   B 1  535 ? -27.628 22.51   31.925  1    50.718  ? 535  LYS   B CG  1 2 
ATOM   9337  C  CD  . LYS   B 1  535 ? -29.056 22.218  31.477  1    56.051  ? 535  LYS   B CD  1 2 
ATOM   9338  C  CE  . LYS   B 1  535 ? -29.43  22.498  30.034  1    61.58   ? 535  LYS   B CE  1 2 
ATOM   9339  N  NZ  . LYS   B 1  535 ? -29.173 23.867  29.555  1    61.033  ? 535  LYS   B NZ  1 2 
ATOM   9340  N  N   . ALA   B 1  536 ? -23.584 21.787  29.895  1    37.702  ? 536  ALA   B N   1 2 
ATOM   9341  C  CA  . ALA   B 1  536 ? -22.539 21.203  29.059  1    36.725  ? 536  ALA   B CA  1 2 
ATOM   9342  C  C   . ALA   B 1  536 ? -21.379 20.71   29.926  1    36.113  ? 536  ALA   B C   1 2 
ATOM   9343  O  O   . ALA   B 1  536 ? -20.921 19.589  29.776  1    37.406  ? 536  ALA   B O   1 2 
ATOM   9344  C  CB  . ALA   B 1  536 ? -22.109 22.194  28.016  1    36.281  ? 536  ALA   B CB  1 2 
ATOM   9345  N  N   . GLY   B 1  537 ? -20.986 21.493  30.936  1    35.911  ? 537  GLY   B N   1 2 
ATOM   9346  C  CA  . GLY   B 1  537 ? -19.982 21.073  31.901  1    33.458  ? 537  GLY   B CA  1 2 
ATOM   9347  C  C   . GLY   B 1  537 ? -20.33  19.734  32.549  1    35.38   ? 537  GLY   B C   1 2 
ATOM   9348  O  O   . GLY   B 1  537 ? -19.454 18.883  32.651  1    35.955  ? 537  GLY   B O   1 2 
ATOM   9349  N  N   . ALA   B 1  538 ? -21.602 19.568  32.986  1    36.855  ? 538  ALA   B N   1 2 
ATOM   9350  C  CA  . ALA   B 1  538 ? -22.115 18.368  33.646  1    38.918  ? 538  ALA   B CA  1 2 
ATOM   9351  C  C   . ALA   B 1  538 ? -21.93  17.149  32.736  1    38.56   ? 538  ALA   B C   1 2 
ATOM   9352  O  O   . ALA   B 1  538 ? -21.37  16.13   33.151  1    38.357  ? 538  ALA   B O   1 2 
ATOM   9353  C  CB  . ALA   B 1  538 ? -23.585 18.56   34.034  1    40.036  ? 538  ALA   B CB  1 2 
ATOM   9354  N  N   . LYS   B 1  539 ? -22.359 17.279  31.478  1    38.821  ? 539  LYS   B N   1 2 
ATOM   9355  C  CA  . LYS   B 1  539 ? -22.193 16.212  30.501  1    39.586  ? 539  LYS   B CA  1 2 
ATOM   9356  C  C   . LYS   B 1  539 ? -20.714 15.865  30.241  1    40.998  ? 539  LYS   B C   1 2 
ATOM   9357  O  O   . LYS   B 1  539 ? -20.335 14.686  30.176  1    41.266  ? 539  LYS   B O   1 2 
ATOM   9358  C  CB  . LYS   B 1  539 ? -22.885 16.677  29.219  1    40.04   ? 539  LYS   B CB  1 2 
ATOM   9359  C  CG  . LYS   B 1  539 ? -22.613 15.728  28.056  1    40.204  ? 539  LYS   B CG  1 2 
ATOM   9360  C  CD  . LYS   B 1  539 ? -23.654 15.9    26.956  1    42.797  ? 539  LYS   B CD  1 2 
ATOM   9361  C  CE  . LYS   B 1  539 ? -24.961 15.29   27.368  1    45.845  ? 539  LYS   B CE  1 2 
ATOM   9362  N  NZ  . LYS   B 1  539 ? -24.798 13.846  27.583  1    44.754  ? 539  LYS   B NZ  1 2 
ATOM   9363  N  N   . LEU   B 1  540 ? -19.859 16.883  30.051  1    39.532  ? 540  LEU   B N   1 2 
ATOM   9364  C  CA  . LEU   B 1  540 ? -18.439 16.628  29.875  1    37.277  ? 540  LEU   B CA  1 2 
ATOM   9365  C  C   . LEU   B 1  540 ? -17.89  15.924  31.112  1    38.924  ? 540  LEU   B C   1 2 
ATOM   9366  O  O   . LEU   B 1  540 ? -17.119 14.973  30.99   1    39.853  ? 540  LEU   B O   1 2 
ATOM   9367  C  CB  . LEU   B 1  540 ? -17.687 17.899  29.492  1    35.539  ? 540  LEU   B CB  1 2 
ATOM   9368  C  CG  . LEU   B 1  540 ? -16.233 17.764  29.024  1    35.445  ? 540  LEU   B CG  1 2 
ATOM   9369  C  CD1 . LEU   B 1  540 ? -16.114 16.853  27.799  1    34.669  ? 540  LEU   B CD1 1 2 
ATOM   9370  C  CD2 . LEU   B 1  540 ? -15.783 19.17   28.637  1    32.964  ? 540  LEU   B CD2 1 2 
ATOM   9371  N  N   . ARG   B 1  541 ? -18.331 16.344  32.312  1    41.003  ? 541  ARG   B N   1 2 
ATOM   9372  C  CA  . ARG   B 1  541 ? -17.799 15.772  33.539  1    41.611  ? 541  ARG   B CA  1 2 
ATOM   9373  C  C   . ARG   B 1  541 ? -17.983 14.253  33.565  1    41.478  ? 541  ARG   B C   1 2 
ATOM   9374  O  O   . ARG   B 1  541 ? -17.064 13.544  33.982  1    43.679  ? 541  ARG   B O   1 2 
ATOM   9375  C  CB  . ARG   B 1  541 ? -18.307 16.471  34.806  1    45.985  ? 541  ARG   B CB  1 2 
ATOM   9376  C  CG  . ARG   B 1  541 ? -17.431 16.186  36.019  1    51.605  ? 541  ARG   B CG  1 2 
ATOM   9377  C  CD  . ARG   B 1  541 ? -17.45  17.272  37.1    1    53.49   ? 541  ARG   B CD  1 2 
ATOM   9378  N  NE  . ARG   B 1  541 ? -18.771 17.326  37.725  1    58.346  ? 541  ARG   B NE  1 2 
ATOM   9379  C  CZ  . ARG   B 1  541 ? -19.695 18.281  37.612  1    54.171  ? 541  ARG   B CZ  1 2 
ATOM   9380  N  NH1 . ARG   B 1  541 ? -19.394 19.468  37.111  1    46.952  ? 541  ARG   B NH1 1 2 
ATOM   9381  N  NH2 . ARG   B 1  541 ? -20.924 18.026  38.056  1    53.358  ? 541  ARG   B NH2 1 2 
ATOM   9382  N  N   . LYS   B 1  542 ? -19.131 13.764  33.071  1    43.546  ? 542  LYS   B N   1 2 
ATOM   9383  C  CA  . LYS   B 1  542 ? -19.483 12.342  33.144  1    47.409  ? 542  LYS   B CA  1 2 
ATOM   9384  C  C   . LYS   B 1  542 ? -18.51  11.528  32.278  1    45.749  ? 542  LYS   B C   1 2 
ATOM   9385  O  O   . LYS   B 1  542 ? -17.968 10.504  32.71   1    44.312  ? 542  LYS   B O   1 2 
ATOM   9386  C  CB  . LYS   B 1  542 ? -20.982 12.134  32.875  1    49.747  ? 542  LYS   B CB  1 2 
ATOM   9387  C  CG  . LYS   B 1  542 ? -21.53  10.705  32.991  1    56.019  ? 542  LYS   B CG  1 2 
ATOM   9388  C  CD  . LYS   B 1  542 ? -23.053 10.595  32.897  1    60.068  ? 542  LYS   B CD  1 2 
ATOM   9389  C  CE  . LYS   B 1  542 ? -23.656 11.663  33.764  1    63.403  ? 542  LYS   B CE  1 2 
ATOM   9390  N  NZ  . LYS   B 1  542 ? -25.067 11.461  34.105  1    71.47   ? 542  LYS   B NZ  1 2 
ATOM   9391  N  N   . VAL   B 1  543 ? -18.199 12.063  31.088  1    42.878  ? 543  VAL   B N   1 2 
ATOM   9392  C  CA  . VAL   B 1  543 ? -17.147 11.493  30.271  1    38.871  ? 543  VAL   B CA  1 2 
ATOM   9393  C  C   . VAL   B 1  543 ? -15.836 11.398  31.05   1    36.637  ? 543  VAL   B C   1 2 
ATOM   9394  O  O   . VAL   B 1  543 ? -15.193 10.341  31.051  1    37.383  ? 543  VAL   B O   1 2 
ATOM   9395  C  CB  . VAL   B 1  543 ? -17.015 12.222  28.918  1    35.268  ? 543  VAL   B CB  1 2 
ATOM   9396  C  CG1 . VAL   B 1  543 ? -15.832 11.682  28.132  1    33.907  ? 543  VAL   B CG1 1 2 
ATOM   9397  C  CG2 . VAL   B 1  543 ? -18.297 12.043  28.136  1    34.329  ? 543  VAL   B CG2 1 2 
ATOM   9398  N  N   . LEU   B 1  544 ? -15.394 12.492  31.677  1    35.072  ? 544  LEU   B N   1 2 
ATOM   9399  C  CA  . LEU   B 1  544 ? -14.032 12.519  32.193  1    34.082  ? 544  LEU   B CA  1 2 
ATOM   9400  C  C   . LEU   B 1  544 ? -13.846 11.608  33.408  1    37.75   ? 544  LEU   B C   1 2 
ATOM   9401  O  O   . LEU   B 1  544 ? -12.749 11.095  33.642  1    35.021  ? 544  LEU   B O   1 2 
ATOM   9402  C  CB  . LEU   B 1  544 ? -13.597 13.942  32.52   1    34.141  ? 544  LEU   B CB  1 2 
ATOM   9403  C  CG  . LEU   B 1  544 ? -13.701 14.957  31.381  1    35.392  ? 544  LEU   B CG  1 2 
ATOM   9404  C  CD1 . LEU   B 1  544 ? -12.986 16.22   31.825  1    37.225  ? 544  LEU   B CD1 1 2 
ATOM   9405  C  CD2 . LEU   B 1  544 ? -12.996 14.383  30.144  1    33.555  ? 544  LEU   B CD2 1 2 
ATOM   9406  N  N   . ARG   B 1  545 ? -14.895 11.477  34.232  1    40.522  ? 545  ARG   B N   1 2 
ATOM   9407  C  CA  . ARG   B 1  545 ? -14.784 10.688  35.45   1    46.759  ? 545  ARG   B CA  1 2 
ATOM   9408  C  C   . ARG   B 1  545 ? -14.742 9.183   35.16   1    48.431  ? 545  ARG   B C   1 2 
ATOM   9409  O  O   . ARG   B 1  545 ? -14.21  8.415   35.962  1    49.007  ? 545  ARG   B O   1 2 
ATOM   9410  C  CB  . ARG   B 1  545 ? -15.98  11.001  36.352  1    49.704  ? 545  ARG   B CB  1 2 
ATOM   9411  C  CG  . ARG   B 1  545 ? -16.08  12.473  36.73   1    52.882  ? 545  ARG   B CG  1 2 
ATOM   9412  C  CD  . ARG   B 1  545 ? -17.266 12.668  37.678  1    60.012  ? 545  ARG   B CD  1 2 
ATOM   9413  N  NE  . ARG   B 1  545 ? -16.964 12.211  39.039  1    64.305  ? 545  ARG   B NE  1 2 
ATOM   9414  C  CZ  . ARG   B 1  545 ? -16.057 12.755  39.848  1    65.429  ? 545  ARG   B CZ  1 2 
ATOM   9415  N  NH1 . ARG   B 1  545 ? -15.355 13.818  39.466  1    62.203  ? 545  ARG   B NH1 1 2 
ATOM   9416  N  NH2 . ARG   B 1  545 ? -15.862 12.222  41.041  1    68.029  ? 545  ARG   B NH2 1 2 
ATOM   9417  N  N   . ALA   B 1  546 ? -15.334 8.779   34.026  1    49.873  ? 546  ALA   B N   1 2 
ATOM   9418  C  CA  . ALA   B 1  546 ? -15.439 7.389   33.605  1    48.841  ? 546  ALA   B CA  1 2 
ATOM   9419  C  C   . ALA   B 1  546 ? -14.064 6.794   33.294  1    51.135  ? 546  ALA   B C   1 2 
ATOM   9420  O  O   . ALA   B 1  546 ? -13.92  5.572   33.305  1    54.417  ? 546  ALA   B O   1 2 
ATOM   9421  C  CB  . ALA   B 1  546 ? -16.388 7.261   32.432  1    47.105  ? 546  ALA   B CB  1 2 
ATOM   9422  N  N   . GLY   B 1  547 ? -13.052 7.633   32.986  1    46.762  ? 547  GLY   B N   1 2 
ATOM   9423  C  CA  . GLY   B 1  547 ? -11.757 7.117   32.569  1    41.314  ? 547  GLY   B CA  1 2 
ATOM   9424  C  C   . GLY   B 1  547 ? -11.963 6.04    31.502  1    38.41   ? 547  GLY   B C   1 2 
ATOM   9425  O  O   . GLY   B 1  547 ? -12.772 6.231   30.599  1    36.034  ? 547  GLY   B O   1 2 
ATOM   9426  N  N   . SER   B 1  548 ? -11.284 4.894   31.669  1    41.42   ? 548  SER   B N   1 2 
ATOM   9427  C  CA  . SER   B 1  548 ? -11.456 3.732   30.796  1    42.512  ? 548  SER   B CA  1 2 
ATOM   9428  C  C   . SER   B 1  548 ? -12.144 2.577   31.528  1    47.02   ? 548  SER   B C   1 2 
ATOM   9429  O  O   . SER   B 1  548 ? -11.858 1.409   31.25   1    45.222  ? 548  SER   B O   1 2 
ATOM   9430  C  CB  . SER   B 1  548 ? -10.144 3.255   30.271  1    42.487  ? 548  SER   B CB  1 2 
ATOM   9431  O  OG  . SER   B 1  548 ? -9.265  3.054   31.37   1    44.756  ? 548  SER   B OG  1 2 
ATOM   9432  N  N   . SER   B 1  549 ? -13.074 2.911   32.424  1    47.27   ? 549  SER   B N   1 2 
ATOM   9433  C  CA  . SER   B 1  549 ? -13.809 1.897   33.161  1    54.316  ? 549  SER   B CA  1 2 
ATOM   9434  C  C   . SER   B 1  549 ? -14.777 1.21    32.207  1    55.165  ? 549  SER   B C   1 2 
ATOM   9435  O  O   . SER   B 1  549 ? -15.01  0.015   32.309  1    62.846  ? 549  SER   B O   1 2 
ATOM   9436  C  CB  . SER   B 1  549 ? -14.563 2.509   34.312  1    54.229  ? 549  SER   B CB  1 2 
ATOM   9437  O  OG  . SER   B 1  549 ? -15.718 3.177   33.811  1    54.532  ? 549  SER   B OG  1 2 
ATOM   9438  N  N   . ARG   B 1  550 ? -15.339 1.996   31.289  1    50.219  ? 550  ARG   B N   1 2 
ATOM   9439  C  CA  . ARG   B 1  550 ? -16.37  1.537   30.385  1    51.512  ? 550  ARG   B CA  1 2 
ATOM   9440  C  C   . ARG   B 1  550 ? -15.874 1.537   28.938  1    50.253  ? 550  ARG   B C   1 2 
ATOM   9441  O  O   . ARG   B 1  550 ? -14.897 2.227   28.625  1    49.204  ? 550  ARG   B O   1 2 
ATOM   9442  C  CB  . ARG   B 1  550 ? -17.557 2.47    30.598  1    54.326  ? 550  ARG   B CB  1 2 
ATOM   9443  C  CG  . ARG   B 1  550 ? -18.295 2.051   31.859  1    64.034  ? 550  ARG   B CG  1 2 
ATOM   9444  C  CD  . ARG   B 1  550 ? -19.766 2.445   31.911  1    63.844  ? 550  ARG   B CD  1 2 
ATOM   9445  N  NE  . ARG   B 1  550 ? -19.977 3.83    31.473  1    57.147  ? 550  ARG   B NE  1 2 
ATOM   9446  C  CZ  . ARG   B 1  550 ? -20.953 4.199   30.654  1    55.993  ? 550  ARG   B CZ  1 2 
ATOM   9447  N  NH1 . ARG   B 1  550 ? -21.835 3.318   30.194  1    56.52   ? 550  ARG   B NH1 1 2 
ATOM   9448  N  NH2 . ARG   B 1  550 ? -21.056 5.47    30.331  1    53.539  ? 550  ARG   B NH2 1 2 
ATOM   9449  N  N   . PRO   B 1  551 ? -16.498 0.73    28.037  1    50.721  ? 551  PRO   B N   1 2 
ATOM   9450  C  CA  . PRO   B 1  551 ? -16.224 0.805   26.593  1    46.752  ? 551  PRO   B CA  1 2 
ATOM   9451  C  C   . PRO   B 1  551 ? -16.539 2.178   25.998  1    45.058  ? 551  PRO   B C   1 2 
ATOM   9452  O  O   . PRO   B 1  551 ? -17.637 2.727   26.216  1    43.989  ? 551  PRO   B O   1 2 
ATOM   9453  C  CB  . PRO   B 1  551 ? -17.105 -0.275  25.961  1    47.828  ? 551  PRO   B CB  1 2 
ATOM   9454  C  CG  . PRO   B 1  551 ? -17.47  -1.201  27.115  1    49.788  ? 551  PRO   B CG  1 2 
ATOM   9455  C  CD  . PRO   B 1  551 ? -17.426 -0.368  28.384  1    51.417  ? 551  PRO   B CD  1 2 
ATOM   9456  N  N   . TRP   B 1  552 ? -15.586 2.691   25.188  1    41.08   ? 552  TRP   B N   1 2 
ATOM   9457  C  CA  . TRP   B 1  552 ? -15.668 4.046   24.679  1    36.12   ? 552  TRP   B CA  1 2 
ATOM   9458  C  C   . TRP   B 1  552 ? -16.924 4.161   23.826  1    36.163  ? 552  TRP   B C   1 2 
ATOM   9459  O  O   . TRP   B 1  552 ? -17.514 5.232   23.703  1    37.455  ? 552  TRP   B O   1 2 
ATOM   9460  C  CB  . TRP   B 1  552 ? -14.377 4.445   23.929  1    35.589  ? 552  TRP   B CB  1 2 
ATOM   9461  C  CG  . TRP   B 1  552 ? -14.102 3.69    22.652  1    35.549  ? 552  TRP   B CG  1 2 
ATOM   9462  C  CD1 . TRP   B 1  552 ? -13.251 2.631   22.502  1    35.782  ? 552  TRP   B CD1 1 2 
ATOM   9463  C  CD2 . TRP   B 1  552 ? -14.685 3.937   21.347  1    35.233  ? 552  TRP   B CD2 1 2 
ATOM   9464  N  NE1 . TRP   B 1  552 ? -13.245 2.227   21.189  1    36.961  ? 552  TRP   B NE1 1 2 
ATOM   9465  C  CE2 . TRP   B 1  552 ? -14.121 2.989   20.459  1    35.55   ? 552  TRP   B CE2 1 2 
ATOM   9466  C  CE3 . TRP   B 1  552 ? -15.599 4.867   20.841  1    33.994  ? 552  TRP   B CE3 1 2 
ATOM   9467  C  CZ2 . TRP   B 1  552 ? -14.439 2.946   19.099  1    36.795  ? 552  TRP   B CZ2 1 2 
ATOM   9468  C  CZ3 . TRP   B 1  552 ? -15.924 4.818   19.5    1    36.585  ? 552  TRP   B CZ3 1 2 
ATOM   9469  C  CH2 . TRP   B 1  552 ? -15.354 3.868   18.64   1    36.614  ? 552  TRP   B CH2 1 2 
ATOM   9470  N  N   . GLN   B 1  553 ? -17.345 3.041   23.24   1    36.328  ? 553  GLN   B N   1 2 
ATOM   9471  C  CA  . GLN   B 1  553 ? -18.555 3.017   22.425  1    39.652  ? 553  GLN   B CA  1 2 
ATOM   9472  C  C   . GLN   B 1  553 ? -19.798 3.362   23.257  1    43.358  ? 553  GLN   B C   1 2 
ATOM   9473  O  O   . GLN   B 1  553 ? -20.755 3.958   22.753  1    43.246  ? 553  GLN   B O   1 2 
ATOM   9474  C  CB  . GLN   B 1  553 ? -18.804 1.668   21.733  1    40.929  ? 553  GLN   B CB  1 2 
ATOM   9475  C  CG  . GLN   B 1  553 ? -17.824 1.347   20.603  1    40.461  ? 553  GLN   B CG  1 2 
ATOM   9476  C  CD  . GLN   B 1  553 ? -16.611 0.561   21.05   1    40.824  ? 553  GLN   B CD  1 2 
ATOM   9477  O  OE1 . GLN   B 1  553 ? -16.286 0.462   22.243  1    43.868  ? 553  GLN   B OE1 1 2 
ATOM   9478  N  NE2 . GLN   B 1  553 ? -15.932 -0.041  20.089  1    42.299  ? 553  GLN   B NE2 1 2 
ATOM   9479  N  N   . GLU   B 1  554 ? -19.779 2.971   24.534  1    45.961  ? 554  GLU   B N   1 2 
ATOM   9480  C  CA  . GLU   B 1  554 ? -20.914 3.196   25.403  1    49.726  ? 554  GLU   B CA  1 2 
ATOM   9481  C  C   . GLU   B 1  554 ? -20.788 4.595   25.998  1    48.111  ? 554  GLU   B C   1 2 
ATOM   9482  O  O   . GLU   B 1  554 ? -21.775 5.332   26.069  1    48.845  ? 554  GLU   B O   1 2 
ATOM   9483  C  CB  . GLU   B 1  554 ? -20.902 2.155   26.522  1    56.367  ? 554  GLU   B CB  1 2 
ATOM   9484  C  CG  . GLU   B 1  554 ? -21.326 0.763   26.065  1    62.871  ? 554  GLU   B CG  1 2 
ATOM   9485  C  CD  . GLU   B 1  554 ? -20.97  -0.241  27.143  1    70.396  ? 554  GLU   B CD  1 2 
ATOM   9486  O  OE1 . GLU   B 1  554 ? -20.589 0.208   28.249  1    76.12   ? 554  GLU   B OE1 1 2 
ATOM   9487  O  OE2 . GLU   B 1  554 ? -21.053 -1.465  26.89   1    73.19   ? 554  GLU   B OE2 1 2 
ATOM   9488  N  N   . VAL   B 1  555 ? -19.568 4.93    26.431  1    45.455  ? 555  VAL   B N   1 2 
ATOM   9489  C  CA  . VAL   B 1  555 ? -19.277 6.286   26.868  1    45.63   ? 555  VAL   B CA  1 2 
ATOM   9490  C  C   . VAL   B 1  555 ? -19.767 7.246   25.779  1    43.867  ? 555  VAL   B C   1 2 
ATOM   9491  O  O   . VAL   B 1  555 ? -20.455 8.207   26.087  1    40.113  ? 555  VAL   B O   1 2 
ATOM   9492  C  CB  . VAL   B 1  555 ? -17.808 6.502   27.307  1    46.56   ? 555  VAL   B CB  1 2 
ATOM   9493  C  CG1 . VAL   B 1  555 ? -17.467 7.958   27.626  1    44.565  ? 555  VAL   B CG1 1 2 
ATOM   9494  C  CG2 . VAL   B 1  555 ? -17.444 5.632   28.514  1    48.948  ? 555  VAL   B CG2 1 2 
ATOM   9495  N  N   . LEU   B 1  556 ? -19.467 6.956   24.494  1    45.206  ? 556  LEU   B N   1 2 
ATOM   9496  C  CA  . LEU   B 1  556 ? -19.807 7.834   23.38   1    40.915  ? 556  LEU   B CA  1 2 
ATOM   9497  C  C   . LEU   B 1  556 ? -21.315 7.992   23.23   1    44.904  ? 556  LEU   B C   1 2 
ATOM   9498  O  O   . LEU   B 1  556 ? -21.799 9.109   23.062  1    42.965  ? 556  LEU   B O   1 2 
ATOM   9499  C  CB  . LEU   B 1  556 ? -19.153 7.415   22.066  1    41.616  ? 556  LEU   B CB  1 2 
ATOM   9500  C  CG  . LEU   B 1  556 ? -19.221 8.387   20.88   1    41.179  ? 556  LEU   B CG  1 2 
ATOM   9501  C  CD1 . LEU   B 1  556 ? -18.571 9.756   21.077  1    39.74   ? 556  LEU   B CD1 1 2 
ATOM   9502  C  CD2 . LEU   B 1  556 ? -18.571 7.694   19.686  1    39.508  ? 556  LEU   B CD2 1 2 
ATOM   9503  N  N   . LYS   B 1  557 ? -22.06  6.877   23.242  1    49.064  ? 557  LYS   B N   1 2 
ATOM   9504  C  CA  . LYS   B 1  557 ? -23.515 6.9     23.091  1    52.321  ? 557  LYS   B CA  1 2 
ATOM   9505  C  C   . LYS   B 1  557 ? -24.155 7.748   24.193  1    52.517  ? 557  LYS   B C   1 2 
ATOM   9506  O  O   . LYS   B 1  557 ? -25.031 8.565   23.911  1    55.458  ? 557  LYS   B O   1 2 
ATOM   9507  C  CB  . LYS   B 1  557 ? -24.075 5.473   23.156  1    56.422  ? 557  LYS   B CB  1 2 
ATOM   9508  C  CG  . LYS   B 1  557 ? -25.573 5.256   23.014  1    58.163  ? 557  LYS   B CG  1 2 
ATOM   9509  C  CD  . LYS   B 1  557 ? -25.923 4.63    21.668  1    58.158  ? 557  LYS   B CD  1 2 
ATOM   9510  C  CE  . LYS   B 1  557 ? -27.341 4.167   21.515  1    62.42   ? 557  LYS   B CE  1 2 
ATOM   9511  N  NZ  . LYS   B 1  557 ? -28.213 5.291   21.152  1    60.725  ? 557  LYS   B NZ  1 2 
ATOM   9512  N  N   . ASP   B 1  558 ? -23.71  7.567   25.441  1    51.911  ? 558  ASP   B N   1 2 
ATOM   9513  C  CA  . ASP   B 1  558 ? -24.298 8.312   26.546  1    54.944  ? 558  ASP   B CA  1 2 
ATOM   9514  C  C   . ASP   B 1  558 ? -24.115 9.791   26.257  1    55.018  ? 558  ASP   B C   1 2 
ATOM   9515  O  O   . ASP   B 1  558 ? -25.028 10.581  26.472  1    51.906  ? 558  ASP   B O   1 2 
ATOM   9516  C  CB  . ASP   B 1  558 ? -23.663 7.966   27.886  1    57.228  ? 558  ASP   B CB  1 2 
ATOM   9517  C  CG  . ASP   B 1  558 ? -24.16  6.666   28.511  1    63.301  ? 558  ASP   B CG  1 2 
ATOM   9518  O  OD1 . ASP   B 1  558 ? -25.245 6.197   28.1    1    66.804  ? 558  ASP   B OD1 1 2 
ATOM   9519  O  OD2 . ASP   B 1  558 ? -23.441 6.105   29.371  1    62.557  ? 558  ASP   B OD2 1 2 
ATOM   9520  N  N   . MET   B 1  559 ? -22.934 10.122  25.703  1    51.256  ? 559  MET   B N   1 2 
ATOM   9521  C  CA  . MET   B 1  559 ? -22.542 11.505  25.525  1    48.217  ? 559  MET   B CA  1 2 
ATOM   9522  C  C   . MET   B 1  559 ? -23.255 12.101  24.313  1    46.822  ? 559  MET   B C   1 2 
ATOM   9523  O  O   . MET   B 1  559 ? -23.92  13.118  24.447  1    48.877  ? 559  MET   B O   1 2 
ATOM   9524  C  CB  . MET   B 1  559 ? -21.017 11.678  25.498  1    48.646  ? 559  MET   B CB  1 2 
ATOM   9525  C  CG  . MET   B 1  559 ? -20.571 13.049  26.003  1    51.487  ? 559  MET   B CG  1 2 
ATOM   9526  S  SD  . MET   B 1  559 ? -19.326 13.631  24.838  1    55.14   ? 559  MET   B SD  1 2 
ATOM   9527  C  CE  . MET   B 1  559 ? -18.639 15.207  25.386  1    48.024  ? 559  MET   B CE  1 2 
ATOM   9528  N  N   . VAL   B 1  560 ? -23.162 11.463  23.136  1    44.389  ? 560  VAL   B N   1 2 
ATOM   9529  C  CA  . VAL   B 1  560 ? -23.588 12.153  21.933  1    42.209  ? 560  VAL   B CA  1 2 
ATOM   9530  C  C   . VAL   B 1  560 ? -24.81  11.51   21.295  1    45.985  ? 560  VAL   B C   1 2 
ATOM   9531  O  O   . VAL   B 1  560 ? -25.329 12.1    20.357  1    43.529  ? 560  VAL   B O   1 2 
ATOM   9532  C  CB  . VAL   B 1  560 ? -22.478 12.322  20.879  1    40.735  ? 560  VAL   B CB  1 2 
ATOM   9533  C  CG1 . VAL   B 1  560 ? -21.208 12.844  21.528  1    35.651  ? 560  VAL   B CG1 1 2 
ATOM   9534  C  CG2 . VAL   B 1  560 ? -22.215 11.03   20.071  1    38.226  ? 560  VAL   B CG2 1 2 
ATOM   9535  N  N   . GLY   B 1  561 ? -25.219 10.315  21.759  1    51.969  ? 561  GLY   B N   1 2 
ATOM   9536  C  CA  . GLY   B 1  561 ? -26.407 9.645   21.233  1    57.234  ? 561  GLY   B CA  1 2 
ATOM   9537  C  C   . GLY   B 1  561 ? -26.1   8.6     20.15   1    58.256  ? 561  GLY   B C   1 2 
ATOM   9538  O  O   . GLY   B 1  561 ? -26.993 7.942   19.622  1    57.682  ? 561  GLY   B O   1 2 
ATOM   9539  N  N   . LEU   B 1  562 ? -24.817 8.434   19.82   1    58.827  ? 562  LEU   B N   1 2 
ATOM   9540  C  CA  . LEU   B 1  562 ? -24.402 7.495   18.791  1    56.622  ? 562  LEU   B CA  1 2 
ATOM   9541  C  C   . LEU   B 1  562 ? -23.226 6.694   19.334  1    51.635  ? 562  LEU   B C   1 2 
ATOM   9542  O  O   . LEU   B 1  562 ? -22.494 7.157   20.204  1    51.834  ? 562  LEU   B O   1 2 
ATOM   9543  C  CB  . LEU   B 1  562 ? -23.997 8.347   17.59   1    60.517  ? 562  LEU   B CB  1 2 
ATOM   9544  C  CG  . LEU   B 1  562 ? -23.89  7.651   16.229  1    61.816  ? 562  LEU   B CG  1 2 
ATOM   9545  C  CD1 . LEU   B 1  562 ? -25.195 7.728   15.429  1    61.499  ? 562  LEU   B CD1 1 2 
ATOM   9546  C  CD2 . LEU   B 1  562 ? -22.719 8.25    15.468  1    56.707  ? 562  LEU   B CD2 1 2 
ATOM   9547  N  N   . ASP   B 1  563 ? -23.028 5.489   18.808  1    48.921  ? 563  ASP   B N   1 2 
ATOM   9548  C  CA  . ASP   B 1  563 ? -22.045 4.587   19.386  1    48.775  ? 563  ASP   B CA  1 2 
ATOM   9549  C  C   . ASP   B 1  563 ? -20.801 4.494   18.5    1    46.636  ? 563  ASP   B C   1 2 
ATOM   9550  O  O   . ASP   B 1  563 ? -19.934 3.659   18.775  1    48.176  ? 563  ASP   B O   1 2 
ATOM   9551  C  CB  . ASP   B 1  563 ? -22.644 3.222   19.704  1    56.607  ? 563  ASP   B CB  1 2 
ATOM   9552  C  CG  . ASP   B 1  563 ? -23.155 2.368   18.539  1    61.92   ? 563  ASP   B CG  1 2 
ATOM   9553  O  OD1 . ASP   B 1  563 ? -22.893 2.706   17.353  1    60.734  ? 563  ASP   B OD1 1 2 
ATOM   9554  O  OD2 . ASP   B 1  563 ? -23.839 1.357   18.823  1    66.25   ? 563  ASP   B OD2 1 2 
ATOM   9555  N  N   . ALA   B 1  564 ? -20.703 5.344   17.465  1    43.682  ? 564  ALA   B N   1 2 
ATOM   9556  C  CA  . ALA   B 1  564 ? -19.524 5.296   16.599  1    41.201  ? 564  ALA   B CA  1 2 
ATOM   9557  C  C   . ALA   B 1  564 ? -19.007 6.692   16.236  1    40.255  ? 564  ALA   B C   1 2 
ATOM   9558  O  O   . ALA   B 1  564 ? -19.78  7.658   16.195  1    37.974  ? 564  ALA   B O   1 2 
ATOM   9559  C  CB  . ALA   B 1  564 ? -19.828 4.473   15.348  1    38.992  ? 564  ALA   B CB  1 2 
ATOM   9560  N  N   . LEU   B 1  565 ? -17.697 6.759   15.915  1    37.904  ? 565  LEU   B N   1 2 
ATOM   9561  C  CA  . LEU   B 1  565 ? -17.09  7.89    15.218  1    37.75   ? 565  LEU   B CA  1 2 
ATOM   9562  C  C   . LEU   B 1  565 ? -17.93  8.227   14.004  1    38.38   ? 565  LEU   B C   1 2 
ATOM   9563  O  O   . LEU   B 1  565 ? -18.369 7.316   13.305  1    42.527  ? 565  LEU   B O   1 2 
ATOM   9564  C  CB  . LEU   B 1  565 ? -15.691 7.592   14.694  1    36.016  ? 565  LEU   B CB  1 2 
ATOM   9565  C  CG  . LEU   B 1  565 ? -14.602 7.371   15.737  1    39.01   ? 565  LEU   B CG  1 2 
ATOM   9566  C  CD1 . LEU   B 1  565 ? -13.292 7.633   14.965  1    36.671  ? 565  LEU   B CD1 1 2 
ATOM   9567  C  CD2 . LEU   B 1  565 ? -14.808 8.39    16.833  1    37.463  ? 565  LEU   B CD2 1 2 
ATOM   9568  N  N   . ASP   B 1  566 ? -18.077 9.523   13.726  1    35.206  ? 566  ASP   B N   1 2 
ATOM   9569  C  CA  . ASP   B 1  566 ? -18.99  9.987   12.687  1    36.113  ? 566  ASP   B CA  1 2 
ATOM   9570  C  C   . ASP   B 1  566 ? -18.52  11.351  12.181  1    34.729  ? 566  ASP   B C   1 2 
ATOM   9571  O  O   . ASP   B 1  566 ? -18.232 12.257  12.975  1    34.006  ? 566  ASP   B O   1 2 
ATOM   9572  C  CB  . ASP   B 1  566 ? -20.417 10.114  13.224  1    39.952  ? 566  ASP   B CB  1 2 
ATOM   9573  C  CG  . ASP   B 1  566 ? -21.484 10.643  12.267  1    45.746  ? 566  ASP   B CG  1 2 
ATOM   9574  O  OD1 . ASP   B 1  566 ? -21.209 10.751  11.047  1    51.522  ? 566  ASP   B OD1 1 2 
ATOM   9575  O  OD2 . ASP   B 1  566 ? -22.625 10.928  12.729  1    50.274  ? 566  ASP   B OD2 1 2 
ATOM   9576  N  N   . ALA   B 1  567 ? -18.504 11.505  10.853  1    33.048  ? 567  ALA   B N   1 2 
ATOM   9577  C  CA  . ALA   B 1  567 ? -18.03  12.727  10.224  1    33.306  ? 567  ALA   B CA  1 2 
ATOM   9578  C  C   . ALA   B 1  567 ? -19.124 13.79   10.054  1    32.447  ? 567  ALA   B C   1 2 
ATOM   9579  O  O   . ALA   B 1  567 ? -18.785 14.897  9.648   1    31.779  ? 567  ALA   B O   1 2 
ATOM   9580  C  CB  . ALA   B 1  567 ? -17.374 12.41   8.875   1    33.868  ? 567  ALA   B CB  1 2 
ATOM   9581  N  N   . GLN   B 1  568 ? -20.407 13.483  10.339  1    32.967  ? 568  GLN   B N   1 2 
ATOM   9582  C  CA  . GLN   B 1  568 ? -21.461 14.425  9.989   1    35.697  ? 568  GLN   B CA  1 2 
ATOM   9583  C  C   . GLN   B 1  568 ? -21.322 15.711  10.797  1    31.556  ? 568  GLN   B C   1 2 
ATOM   9584  O  O   . GLN   B 1  568 ? -21.419 16.814  10.251  1    32.462  ? 568  GLN   B O   1 2 
ATOM   9585  C  CB  . GLN   B 1  568 ? -22.911 13.935  10.118  1    40.638  ? 568  GLN   B CB  1 2 
ATOM   9586  C  CG  . GLN   B 1  568 ? -23.397 13.141  8.914   1    49.924  ? 568  GLN   B CG  1 2 
ATOM   9587  C  CD  . GLN   B 1  568 ? -23.257 13.908  7.616   1    54.306  ? 568  GLN   B CD  1 2 
ATOM   9588  O  OE1 . GLN   B 1  568 ? -23.749 15.032  7.468   1    57.889  ? 568  GLN   B OE1 1 2 
ATOM   9589  N  NE2 . GLN   B 1  568 ? -22.525 13.321  6.68    1    55.28   ? 568  GLN   B NE2 1 2 
ATOM   9590  N  N   . PRO   B 1  569 ? -21.055 15.641  12.112  1    30.951  ? 569  PRO   B N   1 2 
ATOM   9591  C  CA  . PRO   B 1  569 ? -20.833 16.872  12.883  1    29.88   ? 569  PRO   B CA  1 2 
ATOM   9592  C  C   . PRO   B 1  569 ? -19.761 17.762  12.262  1    27.26   ? 569  PRO   B C   1 2 
ATOM   9593  O  O   . PRO   B 1  569 ? -19.971 18.948  12.014  1    28.403  ? 569  PRO   B O   1 2 
ATOM   9594  C  CB  . PRO   B 1  569 ? -20.496 16.353  14.288  1    30.782  ? 569  PRO   B CB  1 2 
ATOM   9595  C  CG  . PRO   B 1  569 ? -21.208 14.989  14.317  1    31.57   ? 569  PRO   B CG  1 2 
ATOM   9596  C  CD  . PRO   B 1  569 ? -20.886 14.421  12.919  1    31.311  ? 569  PRO   B CD  1 2 
ATOM   9597  N  N   . LEU   B 1  570 ? -18.609 17.188  11.92   1    25.646  ? 570  LEU   B N   1 2 
ATOM   9598  C  CA  . LEU   B 1  570 ? -17.573 17.991  11.325  1    24.025  ? 570  LEU   B CA  1 2 
ATOM   9599  C  C   . LEU   B 1  570 ? -18.06  18.58   10.014  1    25.662  ? 570  LEU   B C   1 2 
ATOM   9600  O  O   . LEU   B 1  570 ? -17.81  19.748  9.696   1    25.888  ? 570  LEU   B O   1 2 
ATOM   9601  C  CB  . LEU   B 1  570 ? -16.31  17.139  11.116  1    22.213  ? 570  LEU   B CB  1 2 
ATOM   9602  C  CG  . LEU   B 1  570 ? -15.093 17.901  10.589  1    21.627  ? 570  LEU   B CG  1 2 
ATOM   9603  C  CD1 . LEU   B 1  570 ? -13.828 17.131  10.991  1    19.337  ? 570  LEU   B CD1 1 2 
ATOM   9604  C  CD2 . LEU   B 1  570 ? -15.186 17.962  9.057   1    22.103  ? 570  LEU   B CD2 1 2 
ATOM   9605  N  N   . LEU   B 1  571 ? -18.667 17.73   9.185   1    25.934  ? 571  LEU   B N   1 2 
ATOM   9606  C  CA  . LEU   B 1  571 ? -19.164 18.221  7.907   1    28.324  ? 571  LEU   B CA  1 2 
ATOM   9607  C  C   . LEU   B 1  571 ? -20.165 19.367  8.104   1    29.402  ? 571  LEU   B C   1 2 
ATOM   9608  O  O   . LEU   B 1  571 ? -20.159 20.36   7.371   1    28.249  ? 571  LEU   B O   1 2 
ATOM   9609  C  CB  . LEU   B 1  571 ? -19.794 17.035  7.169   1    31.408  ? 571  LEU   B CB  1 2 
ATOM   9610  C  CG  . LEU   B 1  571 ? -18.769 16.014  6.631   1    34.334  ? 571  LEU   B CG  1 2 
ATOM   9611  C  CD1 . LEU   B 1  571 ? -19.462 14.831  5.945   1    38.041  ? 571  LEU   B CD1 1 2 
ATOM   9612  C  CD2 . LEU   B 1  571 ? -17.812 16.718  5.691   1    31.903  ? 571  LEU   B CD2 1 2 
ATOM   9613  N  N   . LYS   B 1  572 ? -21.001 19.241  9.131   1    30.494  ? 572  LYS   B N   1 2 
ATOM   9614  C  CA  . LYS   B 1  572 ? -22.059 20.224  9.322   1    33.598  ? 572  LYS   B CA  1 2 
ATOM   9615  C  C   . LYS   B 1  572 ? -21.446 21.531  9.845   1    32.418  ? 572  LYS   B C   1 2 
ATOM   9616  O  O   . LYS   B 1  572 ? -21.833 22.619  9.442   1    31.298  ? 572  LYS   B O   1 2 
ATOM   9617  C  CB  . LYS   B 1  572 ? -23.025 19.548  10.292  1    38.752  ? 572  LYS   B CB  1 2 
ATOM   9618  C  CG  . LYS   B 1  572 ? -24.205 20.426  10.641  1    48.425  ? 572  LYS   B CG  1 2 
ATOM   9619  C  CD  . LYS   B 1  572 ? -24.887 19.993  11.932  1    53.704  ? 572  LYS   B CD  1 2 
ATOM   9620  C  CE  . LYS   B 1  572 ? -26.007 20.932  12.283  1    54.613  ? 572  LYS   B CE  1 2 
ATOM   9621  N  NZ  . LYS   B 1  572 ? -26.674 20.457  13.494  1    61.209  ? 572  LYS   B NZ  1 2 
ATOM   9622  N  N   . TYR   B 1  573 ? -20.399 21.426  10.685  1    30.451  ? 573  TYR   B N   1 2 
ATOM   9623  C  CA  . TYR   B 1  573 ? -19.685 22.606  11.158  1    27.914  ? 573  TYR   B CA  1 2 
ATOM   9624  C  C   . TYR   B 1  573 ? -19.166 23.425  9.978   1    27.128  ? 573  TYR   B C   1 2 
ATOM   9625  O  O   . TYR   B 1  573 ? -19.29  24.648  9.988   1    26.555  ? 573  TYR   B O   1 2 
ATOM   9626  C  CB  . TYR   B 1  573 ? -18.564 22.152  12.108  1    25.618  ? 573  TYR   B CB  1 2 
ATOM   9627  C  CG  . TYR   B 1  573 ? -17.732 23.283  12.701  1    24.706  ? 573  TYR   B CG  1 2 
ATOM   9628  C  CD1 . TYR   B 1  573 ? -16.727 23.89   11.942  1    24.036  ? 573  TYR   B CD1 1 2 
ATOM   9629  C  CD2 . TYR   B 1  573 ? -17.908 23.697  14.023  1    24.75   ? 573  TYR   B CD2 1 2 
ATOM   9630  C  CE1 . TYR   B 1  573 ? -15.93  24.888  12.476  1    23.422  ? 573  TYR   B CE1 1 2 
ATOM   9631  C  CE2 . TYR   B 1  573 ? -17.132 24.709  14.573  1    24.602  ? 573  TYR   B CE2 1 2 
ATOM   9632  C  CZ  . TYR   B 1  573 ? -16.143 25.295  13.79   1    25.02   ? 573  TYR   B CZ  1 2 
ATOM   9633  O  OH  . TYR   B 1  573 ? -15.323 26.269  14.263  1    25.226  ? 573  TYR   B OH  1 2 
ATOM   9634  N  N   . PHE   B 1  574 ? -18.565 22.758  8.974   1    25.821  ? 574  PHE   B N   1 2 
ATOM   9635  C  CA  . PHE   B 1  574 ? -17.846 23.459  7.917   1    26.369  ? 574  PHE   B CA  1 2 
ATOM   9636  C  C   . PHE   B 1  574 ? -18.689 23.668  6.646   1    29.437  ? 574  PHE   B C   1 2 
ATOM   9637  O  O   . PHE   B 1  574 ? -18.248 24.371  5.739   1    28.007  ? 574  PHE   B O   1 2 
ATOM   9638  C  CB  . PHE   B 1  574 ? -16.573 22.697  7.47    1    26.194  ? 574  PHE   B CB  1 2 
ATOM   9639  C  CG  . PHE   B 1  574 ? -15.425 22.887  8.446   1    23.153  ? 574  PHE   B CG  1 2 
ATOM   9640  C  CD1 . PHE   B 1  574 ? -14.725 24.088  8.502   1    23.474  ? 574  PHE   B CD1 1 2 
ATOM   9641  C  CD2 . PHE   B 1  574 ? -15.045 21.855  9.284   1    22.507  ? 574  PHE   B CD2 1 2 
ATOM   9642  C  CE1 . PHE   B 1  574 ? -13.649 24.26   9.378   1    23.33   ? 574  PHE   B CE1 1 2 
ATOM   9643  C  CE2 . PHE   B 1  574 ? -14.016 22.04   10.193  1    22.794  ? 574  PHE   B CE2 1 2 
ATOM   9644  C  CZ  . PHE   B 1  574 ? -13.324 23.229  10.243  1    22.308  ? 574  PHE   B CZ  1 2 
ATOM   9645  N  N   . GLN   B 1  575 ? -19.92  23.12   6.634   1    32.928  ? 575  GLN   B N   1 2 
ATOM   9646  C  CA  . GLN   B 1  575 ? -20.859 23.124  5.504   1    36.895  ? 575  GLN   B CA  1 2 
ATOM   9647  C  C   . GLN   B 1  575 ? -20.752 24.38   4.639   1    36.865  ? 575  GLN   B C   1 2 
ATOM   9648  O  O   . GLN   B 1  575 ? -20.682 24.259  3.424   1    36.656  ? 575  GLN   B O   1 2 
ATOM   9649  C  CB  . GLN   B 1  575 ? -22.269 22.878  6.043   1    43.632  ? 575  GLN   B CB  1 2 
ATOM   9650  C  CG  . GLN   B 1  575 ? -23.351 22.709  4.983   1    51.235  ? 575  GLN   B CG  1 2 
ATOM   9651  C  CD  . GLN   B 1  575 ? -24.729 22.64   5.604   1    64.65   ? 575  GLN   B CD  1 2 
ATOM   9652  O  OE1 . GLN   B 1  575 ? -25.166 23.573  6.292   1    71.387  ? 575  GLN   B OE1 1 2 
ATOM   9653  N  NE2 . GLN   B 1  575 ? -25.423 21.528  5.382   1    66.307  ? 575  GLN   B NE2 1 2 
ATOM   9654  N  N   . LEU   B 1  576 ? -20.728 25.585  5.236   1    37.463  ? 576  LEU   B N   1 2 
ATOM   9655  C  CA  . LEU   B 1  576 ? -20.755 26.826  4.462   1    37.209  ? 576  LEU   B CA  1 2 
ATOM   9656  C  C   . LEU   B 1  576 ? -19.486 27.08   3.667   1    37.72   ? 576  LEU   B C   1 2 
ATOM   9657  O  O   . LEU   B 1  576 ? -19.58  27.665  2.57    1    37.756  ? 576  LEU   B O   1 2 
ATOM   9658  C  CB  . LEU   B 1  576 ? -20.994 28.079  5.29    1    39.948  ? 576  LEU   B CB  1 2 
ATOM   9659  C  CG  . LEU   B 1  576 ? -22.417 28.292  5.806   1    42.196  ? 576  LEU   B CG  1 2 
ATOM   9660  C  CD1 . LEU   B 1  576 ? -22.256 29.511  6.736   1    41.088  ? 576  LEU   B CD1 1 2 
ATOM   9661  C  CD2 . LEU   B 1  576 ? -23.393 28.511  4.651   1    43.478  ? 576  LEU   B CD2 1 2 
ATOM   9662  N  N   . VAL   B 1  577 ? -18.327 26.842  4.317   1    33.472  ? 577  VAL   B N   1 2 
ATOM   9663  C  CA  . VAL   B 1  577 ? -17.031 27.043  3.687   1    31.409  ? 577  VAL   B CA  1 2 
ATOM   9664  C  C   . VAL   B 1  577 ? -16.792 25.892  2.696   1    29.822  ? 577  VAL   B C   1 2 
ATOM   9665  O  O   . VAL   B 1  577 ? -16.108 26.071  1.698   1    28.766  ? 577  VAL   B O   1 2 
ATOM   9666  C  CB  . VAL   B 1  577 ? -15.806 27.295  4.609   1    29.362  ? 577  VAL   B CB  1 2 
ATOM   9667  C  CG1 . VAL   B 1  577 ? -15.181 26.004  5.189   1    27.084  ? 577  VAL   B CG1 1 2 
ATOM   9668  C  CG2 . VAL   B 1  577 ? -14.705 28.092  3.922   1    27.99   ? 577  VAL   B CG2 1 2 
ATOM   9669  N  N   . THR   B 1  578 ? -17.335 24.711  2.986   1    29.372  ? 578  THR   B N   1 2 
ATOM   9670  C  CA  . THR   B 1  578 ? -17.162 23.583  2.084   1    32.229  ? 578  THR   B CA  1 2 
ATOM   9671  C  C   . THR   B 1  578 ? -17.782 23.977  0.75    1    36.874  ? 578  THR   B C   1 2 
ATOM   9672  O  O   . THR   B 1  578 ? -17.171 23.819  -0.314  1    38.684  ? 578  THR   B O   1 2 
ATOM   9673  C  CB  . THR   B 1  578 ? -17.884 22.372  2.657   1    32.612  ? 578  THR   B CB  1 2 
ATOM   9674  O  OG1 . THR   B 1  578 ? -17.072 21.986  3.753   1    32.082  ? 578  THR   B OG1 1 2 
ATOM   9675  C  CG2 . THR   B 1  578 ? -17.917 21.175  1.722   1    32.132  ? 578  THR   B CG2 1 2 
ATOM   9676  N  N   . GLN   B 1  579 ? -19.01  24.499  0.854   1    37.239  ? 579  GLN   B N   1 2 
ATOM   9677  C  CA  . GLN   B 1  579 ? -19.84  24.857  -0.283  1    43.315  ? 579  GLN   B CA  1 2 
ATOM   9678  C  C   . GLN   B 1  579 ? -19.128 25.986  -1.02   1    40.68   ? 579  GLN   B C   1 2 
ATOM   9679  O  O   . GLN   B 1  579 ? -19.01  25.939  -2.245  1    44.831  ? 579  GLN   B O   1 2 
ATOM   9680  C  CB  . GLN   B 1  579 ? -21.251 25.17   0.236   1    47.033  ? 579  GLN   B CB  1 2 
ATOM   9681  C  CG  . GLN   B 1  579 ? -22.229 25.676  -0.817  1    61.491  ? 579  GLN   B CG  1 2 
ATOM   9682  C  CD  . GLN   B 1  579 ? -22.445 24.745  -1.996  1    73.994  ? 579  GLN   B CD  1 2 
ATOM   9683  O  OE1 . GLN   B 1  579 ? -22.648 23.531  -1.839  1    75.217  ? 579  GLN   B OE1 1 2 
ATOM   9684  N  NE2 . GLN   B 1  579 ? -22.413 25.315  -3.198  1    78.216  ? 579  GLN   B NE2 1 2 
ATOM   9685  N  N   . TRP   B 1  580 ? -18.598 26.951  -0.267  1    36.074  ? 580  TRP   B N   1 2 
ATOM   9686  C  CA  . TRP   B 1  580 ? -17.951 28.123  -0.843  1    36.206  ? 580  TRP   B CA  1 2 
ATOM   9687  C  C   . TRP   B 1  580 ? -16.706 27.712  -1.62   1    35.989  ? 580  TRP   B C   1 2 
ATOM   9688  O  O   . TRP   B 1  580 ? -16.568 28.108  -2.761  1    38.538  ? 580  TRP   B O   1 2 
ATOM   9689  C  CB  . TRP   B 1  580 ? -17.632 29.221  0.201   1    36.311  ? 580  TRP   B CB  1 2 
ATOM   9690  C  CG  . TRP   B 1  580 ? -17.141 30.544  -0.353  1    36.087  ? 580  TRP   B CG  1 2 
ATOM   9691  C  CD1 . TRP   B 1  580 ? -17.909 31.586  -0.815  1    38.025  ? 580  TRP   B CD1 1 2 
ATOM   9692  C  CD2 . TRP   B 1  580 ? -15.778 31.011  -0.414  1    34.996  ? 580  TRP   B CD2 1 2 
ATOM   9693  N  NE1 . TRP   B 1  580 ? -17.116 32.629  -1.228  1    37.676  ? 580  TRP   B NE1 1 2 
ATOM   9694  C  CE2 . TRP   B 1  580 ? -15.801 32.302  -0.988  1    37.915  ? 580  TRP   B CE2 1 2 
ATOM   9695  C  CE3 . TRP   B 1  580 ? -14.541 30.438  -0.094  1    35.011  ? 580  TRP   B CE3 1 2 
ATOM   9696  C  CZ2 . TRP   B 1  580 ? -14.639 33.039  -1.205  1    38.705  ? 580  TRP   B CZ2 1 2 
ATOM   9697  C  CZ3 . TRP   B 1  580 ? -13.391 31.169  -0.301  1    36.3    ? 580  TRP   B CZ3 1 2 
ATOM   9698  C  CH2 . TRP   B 1  580 ? -13.446 32.467  -0.812  1    38.308  ? 580  TRP   B CH2 1 2 
ATOM   9699  N  N   . LEU   B 1  581 ? -15.835 26.887  -1.007  1    32.318  ? 581  LEU   B N   1 2 
ATOM   9700  C  CA  . LEU   B 1  581 ? -14.539 26.593  -1.576  1    32.214  ? 581  LEU   B CA  1 2 
ATOM   9701  C  C   . LEU   B 1  581 ? -14.72  25.894  -2.917  1    34.772  ? 581  LEU   B C   1 2 
ATOM   9702  O  O   . LEU   B 1  581 ? -13.933 26.162  -3.825  1    32.693  ? 581  LEU   B O   1 2 
ATOM   9703  C  CB  . LEU   B 1  581 ? -13.706 25.693  -0.647  1    28.957  ? 581  LEU   B CB  1 2 
ATOM   9704  C  CG  . LEU   B 1  581 ? -13.104 26.385  0.575   1    28.692  ? 581  LEU   B CG  1 2 
ATOM   9705  C  CD1 . LEU   B 1  581 ? -12.583 25.356  1.578   1    25.415  ? 581  LEU   B CD1 1 2 
ATOM   9706  C  CD2 . LEU   B 1  581 ? -11.977 27.262  0.061   1    28.396  ? 581  LEU   B CD2 1 2 
ATOM   9707  N  N   . GLN   B 1  582 ? -15.694 24.957  -2.969  1    37.281  ? 582  GLN   B N   1 2 
ATOM   9708  C  CA  . GLN   B 1  582 ? -16.087 24.24   -4.175  1    43.013  ? 582  GLN   B CA  1 2 
ATOM   9709  C  C   . GLN   B 1  582 ? -16.402 25.177  -5.335  1    46.597  ? 582  GLN   B C   1 2 
ATOM   9710  O  O   . GLN   B 1  582 ? -16.006 24.889  -6.471  1    45.312  ? 582  GLN   B O   1 2 
ATOM   9711  C  CB  . GLN   B 1  582 ? -17.374 23.458  -3.969  1    47.225  ? 582  GLN   B CB  1 2 
ATOM   9712  C  CG  . GLN   B 1  582 ? -17.112 22.025  -3.547  1    52.159  ? 582  GLN   B CG  1 2 
ATOM   9713  C  CD  . GLN   B 1  582 ? -18.367 21.197  -3.612  1    65.915  ? 582  GLN   B CD  1 2 
ATOM   9714  O  OE1 . GLN   B 1  582 ? -19.292 21.377  -2.807  1    73.048  ? 582  GLN   B OE1 1 2 
ATOM   9715  N  NE2 . GLN   B 1  582 ? -18.415 20.302  -4.592  1    67.506  ? 582  GLN   B NE2 1 2 
ATOM   9716  N  N   . GLU   B 1  583 ? -17.136 26.264  -5.028  1    47.642  ? 583  GLU   B N   1 2 
ATOM   9717  C  CA  . GLU   B 1  583 ? -17.512 27.296  -5.975  1    47.815  ? 583  GLU   B CA  1 2 
ATOM   9718  C  C   . GLU   B 1  583 ? -16.276 28.051  -6.441  1    45.18   ? 583  GLU   B C   1 2 
ATOM   9719  O  O   . GLU   B 1  583 ? -16.107 28.193  -7.639  1    47.517  ? 583  GLU   B O   1 2 
ATOM   9720  C  CB  . GLU   B 1  583 ? -18.41  28.371  -5.372  1    55.881  ? 583  GLU   B CB  1 2 
ATOM   9721  C  CG  . GLU   B 1  583 ? -19.852 27.929  -5.147  1    63.548  ? 583  GLU   B CG  1 2 
ATOM   9722  C  CD  . GLU   B 1  583 ? -20.671 28.866  -4.262  1    66.607  ? 583  GLU   B CD  1 2 
ATOM   9723  O  OE1 . GLU   B 1  583 ? -20.22  29.951  -3.784  1    64.646  ? 583  GLU   B OE1 1 2 
ATOM   9724  O  OE2 . GLU   B 1  583 ? -21.822 28.44   -4.039  1    70.53   ? 583  GLU   B OE2 1 2 
ATOM   9725  N  N   . GLN   B 1  584 ? -15.427 28.532  -5.523  1    42.053  ? 584  GLN   B N   1 2 
ATOM   9726  C  CA  . GLN   B 1  584 ? -14.252 29.29   -5.934  1    44.592  ? 584  GLN   B CA  1 2 
ATOM   9727  C  C   . GLN   B 1  584 ? -13.335 28.494  -6.879  1    48.288  ? 584  GLN   B C   1 2 
ATOM   9728  O  O   . GLN   B 1  584 ? -12.761 29.056  -7.833  1    44.766  ? 584  GLN   B O   1 2 
ATOM   9729  C  CB  . GLN   B 1  584 ? -13.344 29.677  -4.768  1    47.035  ? 584  GLN   B CB  1 2 
ATOM   9730  C  CG  . GLN   B 1  584 ? -14.006 30.613  -3.777  1    51.584  ? 584  GLN   B CG  1 2 
ATOM   9731  C  CD  . GLN   B 1  584 ? -14.495 31.88   -4.445  1    56.945  ? 584  GLN   B CD  1 2 
ATOM   9732  O  OE1 . GLN   B 1  584 ? -13.698 32.779  -4.751  1    57.796  ? 584  GLN   B OE1 1 2 
ATOM   9733  N  NE2 . GLN   B 1  584 ? -15.802 31.944  -4.688  1    57.075  ? 584  GLN   B NE2 1 2 
ATOM   9734  N  N   . ASN   B 1  585 ? -13.126 27.199  -6.566  1    40.947  ? 585  ASN   B N   1 2 
ATOM   9735  C  CA  . ASN   B 1  585 ? -12.135 26.465  -7.334  1    39.53   ? 585  ASN   B CA  1 2 
ATOM   9736  C  C   . ASN   B 1  585 ? -12.554 26.353  -8.8    1    41.701  ? 585  ASN   B C   1 2 
ATOM   9737  O  O   . ASN   B 1  585 ? -11.704 26.566  -9.668  1    39.674  ? 585  ASN   B O   1 2 
ATOM   9738  C  CB  . ASN   B 1  585 ? -11.876 25.099  -6.728  1    34.188  ? 585  ASN   B CB  1 2 
ATOM   9739  C  CG  . ASN   B 1  585 ? -11.147 25.234  -5.421  1    30.481  ? 585  ASN   B CG  1 2 
ATOM   9740  O  OD1 . ASN   B 1  585 ? -10.305 26.128  -5.275  1    30.235  ? 585  ASN   B OD1 1 2 
ATOM   9741  N  ND2 . ASN   B 1  585 ? -11.357 24.271  -4.533  1    28.992  ? 585  ASN   B ND2 1 2 
ATOM   9742  N  N   . GLN   B 1  586 ? -13.826 25.973  -9.03   1    41.95   ? 586  GLN   B N   1 2 
ATOM   9743  C  CA  . GLN   B 1  586 ? -14.498 26.003  -10.337 1    49.727  ? 586  GLN   B CA  1 2 
ATOM   9744  C  C   . GLN   B 1  586 ? -14.264 27.303  -11.11  1    50.038  ? 586  GLN   B C   1 2 
ATOM   9745  O  O   . GLN   B 1  586 ? -13.901 27.244  -12.28  1    50.979  ? 586  GLN   B O   1 2 
ATOM   9746  C  CB  . GLN   B 1  586 ? -15.983 25.65   -10.262 1    50.649  ? 586  GLN   B CB  1 2 
ATOM   9747  C  CG  . GLN   B 1  586 ? -16.179 24.289  -9.597  1    55.445  ? 586  GLN   B CG  1 2 
ATOM   9748  C  CD  . GLN   B 1  586 ? -17.618 23.83   -9.463  1    63.632  ? 586  GLN   B CD  1 2 
ATOM   9749  O  OE1 . GLN   B 1  586 ? -18.176 23.752  -8.355  1    64.159  ? 586  GLN   B OE1 1 2 
ATOM   9750  N  NE2 . GLN   B 1  586 ? -18.224 23.49   -10.596 1    62.43   ? 586  GLN   B NE2 1 2 
ATOM   9751  N  N   . GLN   B 1  587 ? -14.449 28.462  -10.472 1    50.063  ? 587  GLN   B N   1 2 
ATOM   9752  C  CA  . GLN   B 1  587 ? -14.298 29.743  -11.153 1    56.914  ? 587  GLN   B CA  1 2 
ATOM   9753  C  C   . GLN   B 1  587 ? -12.859 29.991  -11.583 1    54.043  ? 587  GLN   B C   1 2 
ATOM   9754  O  O   . GLN   B 1  587 ? -12.628 30.655  -12.586 1    54.829  ? 587  GLN   B O   1 2 
ATOM   9755  C  CB  . GLN   B 1  587 ? -14.668 30.948  -10.294 1    63.271  ? 587  GLN   B CB  1 2 
ATOM   9756  C  CG  . GLN   B 1  587 ? -16.105 31.383  -10.536 1    75.749  ? 587  GLN   B CG  1 2 
ATOM   9757  C  CD  . GLN   B 1  587 ? -16.818 31.759  -9.258  1    85.097  ? 587  GLN   B CD  1 2 
ATOM   9758  O  OE1 . GLN   B 1  587 ? -16.649 32.86   -8.719  1    91.422  ? 587  GLN   B OE1 1 2 
ATOM   9759  N  NE2 . GLN   B 1  587 ? -17.637 30.836  -8.77   1    85.621  ? 587  GLN   B NE2 1 2 
ATOM   9760  N  N   . ASN   B 1  588 ? -11.887 29.503  -10.808 1    48.984  ? 588  ASN   B N   1 2 
ATOM   9761  C  CA  . ASN   B 1  588 ? -10.511 29.631  -11.258 1    48.022  ? 588  ASN   B CA  1 2 
ATOM   9762  C  C   . ASN   B 1  588 ? -10.146 28.418  -12.113 1    45.557  ? 588  ASN   B C   1 2 
ATOM   9763  O  O   . ASN   B 1  588 ? -8.974  28.261  -12.456 1    46.693  ? 588  ASN   B O   1 2 
ATOM   9764  C  CB  . ASN   B 1  588 ? -9.517  29.819  -10.113 1    46.567  ? 588  ASN   B CB  1 2 
ATOM   9765  C  CG  . ASN   B 1  588 ? -9.897  30.977  -9.23   1    50.278  ? 588  ASN   B CG  1 2 
ATOM   9766  O  OD1 . ASN   B 1  588 ? -10.332 32.019  -9.731  1    52.257  ? 588  ASN   B OD1 1 2 
ATOM   9767  N  ND2 . ASN   B 1  588 ? -9.796  30.796  -7.918  1    51.997  ? 588  ASN   B ND2 1 2 
ATOM   9768  N  N   . GLY   B 1  589 ? -11.154 27.575  -12.401 1    42.578  ? 589  GLY   B N   1 2 
ATOM   9769  C  CA  . GLY   B 1  589 ? -11.007 26.32   -13.121 1    44.206  ? 589  GLY   B CA  1 2 
ATOM   9770  C  C   . GLY   B 1  589 ? -9.897  25.433  -12.548 1    43.413  ? 589  GLY   B C   1 2 
ATOM   9771  O  O   . GLY   B 1  589 ? -9.073  24.917  -13.293 1    43.953  ? 589  GLY   B O   1 2 
ATOM   9772  N  N   . GLU   B 1  590 ? -9.89   25.221  -11.228 1    38.974  ? 590  GLU   B N   1 2 
ATOM   9773  C  CA  . GLU   B 1  590 ? -8.812  24.452  -10.622 1    37.323  ? 590  GLU   B CA  1 2 
ATOM   9774  C  C   . GLU   B 1  590 ? -8.917  22.979  -10.985 1    36.97   ? 590  GLU   B C   1 2 
ATOM   9775  O  O   . GLU   B 1  590 ? -10     22.47   -11.29  1    38.662  ? 590  GLU   B O   1 2 
ATOM   9776  C  CB  . GLU   B 1  590 ? -8.808  24.498  -9.097  1    34.258  ? 590  GLU   B CB  1 2 
ATOM   9777  C  CG  . GLU   B 1  590 ? -8.792  25.929  -8.593  1    34.71   ? 590  GLU   B CG  1 2 
ATOM   9778  C  CD  . GLU   B 1  590 ? -7.464  26.639  -8.768  1    36.592  ? 590  GLU   B CD  1 2 
ATOM   9779  O  OE1 . GLU   B 1  590 ? -6.519  26.059  -9.351  1    34.352  ? 590  GLU   B OE1 1 2 
ATOM   9780  O  OE2 . GLU   B 1  590 ? -7.398  27.81   -8.318  1    38.394  ? 590  GLU   B OE2 1 2 
ATOM   9781  N  N   . VAL   B 1  591 ? -7.748  22.333  -10.966 1    34.87   ? 591  VAL   B N   1 2 
ATOM   9782  C  CA  . VAL   B 1  591 ? -7.666  20.884  -10.95  1    34.999  ? 591  VAL   B CA  1 2 
ATOM   9783  C  C   . VAL   B 1  591 ? -7.587  20.482  -9.483  1    32.573  ? 591  VAL   B C   1 2 
ATOM   9784  O  O   . VAL   B 1  591 ? -6.739  20.982  -8.727  1    33.656  ? 591  VAL   B O   1 2 
ATOM   9785  C  CB  . VAL   B 1  591 ? -6.51   20.364  -11.846 1    37.747  ? 591  VAL   B CB  1 2 
ATOM   9786  C  CG1 . VAL   B 1  591 ? -6.065  18.944  -11.501 1    35.734  ? 591  VAL   B CG1 1 2 
ATOM   9787  C  CG2 . VAL   B 1  591 ? -6.849  20.476  -13.333 1    39.354  ? 591  VAL   B CG2 1 2 
ATOM   9788  N  N   . LEU   B 1  592 ? -8.578  19.692  -9.052  1    30.522  ? 592  LEU   B N   1 2 
ATOM   9789  C  CA  . LEU   B 1  592 ? -8.585  19.106  -7.729  1    30.521  ? 592  LEU   B CA  1 2 
ATOM   9790  C  C   . LEU   B 1  592 ? -7.612  17.928  -7.727  1    28.873  ? 592  LEU   B C   1 2 
ATOM   9791  O  O   . LEU   B 1  592 ? -7.641  17.106  -8.636  1    29.662  ? 592  LEU   B O   1 2 
ATOM   9792  C  CB  . LEU   B 1  592 ? -9.973  18.66   -7.278  1    31.425  ? 592  LEU   B CB  1 2 
ATOM   9793  C  CG  . LEU   B 1  592 ? -11.018 19.77   -7.338  1    34.45   ? 592  LEU   B CG  1 2 
ATOM   9794  C  CD1 . LEU   B 1  592 ? -12.334 19.27   -6.758  1    36.749  ? 592  LEU   B CD1 1 2 
ATOM   9795  C  CD2 . LEU   B 1  592 ? -10.416 20.927  -6.545  1    31.535  ? 592  LEU   B CD2 1 2 
ATOM   9796  N  N   . GLY   B 1  593 ? -6.744  17.867  -6.732  1    25.473  ? 593  GLY   B N   1 2 
ATOM   9797  C  CA  . GLY   B 1  593 ? -5.749  16.801  -6.727  1    25.1    ? 593  GLY   B CA  1 2 
ATOM   9798  C  C   . GLY   B 1  593 ? -4.456  17.271  -7.394  1    23.513  ? 593  GLY   B C   1 2 
ATOM   9799  O  O   . GLY   B 1  593 ? -4.265  18.458  -7.689  1    23.24   ? 593  GLY   B O   1 2 
ATOM   9800  N  N   . TRP   B 1  594 ? -3.551  16.324  -7.573  1    21.664  ? 594  TRP   B N   1 2 
ATOM   9801  C  CA  . TRP   B 1  594 ? -2.203  16.618  -8.028  1    20.335  ? 594  TRP   B CA  1 2 
ATOM   9802  C  C   . TRP   B 1  594 ? -1.777  15.548  -9.033  1    21.206  ? 594  TRP   B C   1 2 
ATOM   9803  O  O   . TRP   B 1  594 ? -0.866  14.753  -8.757  1    21.192  ? 594  TRP   B O   1 2 
ATOM   9804  C  CB  . TRP   B 1  594 ? -1.269  16.748  -6.811  1    19.448  ? 594  TRP   B CB  1 2 
ATOM   9805  C  CG  . TRP   B 1  594 ? -1.556  15.766  -5.697  1    18.234  ? 594  TRP   B CG  1 2 
ATOM   9806  C  CD1 . TRP   B 1  594 ? -0.996  14.528  -5.57   1    17.747  ? 594  TRP   B CD1 1 2 
ATOM   9807  C  CD2 . TRP   B 1  594 ? -2.527  15.901  -4.631  1    18.078  ? 594  TRP   B CD2 1 2 
ATOM   9808  N  NE1 . TRP   B 1  594 ? -1.523  13.89   -4.48   1    17.426  ? 594  TRP   B NE1 1 2 
ATOM   9809  C  CE2 . TRP   B 1  594 ? -2.476  14.694  -3.893  1    17.301  ? 594  TRP   B CE2 1 2 
ATOM   9810  C  CE3 . TRP   B 1  594 ? -3.419  16.924  -4.216  1    18.967  ? 594  TRP   B CE3 1 2 
ATOM   9811  C  CZ2 . TRP   B 1  594 ? -3.26   14.482  -2.757  1    16.316  ? 594  TRP   B CZ2 1 2 
ATOM   9812  C  CZ3 . TRP   B 1  594 ? -4.188  16.727  -3.083  1    18.36   ? 594  TRP   B CZ3 1 2 
ATOM   9813  C  CH2 . TRP   B 1  594 ? -4.141  15.501  -2.397  1    17.467  ? 594  TRP   B CH2 1 2 
ATOM   9814  N  N   . PRO   B 1  595 ? -2.387  15.566  -10.237 1    21.682  ? 595  PRO   B N   1 2 
ATOM   9815  C  CA  . PRO   B 1  595 ? -2.106  14.588  -11.302 1    22.396  ? 595  PRO   B CA  1 2 
ATOM   9816  C  C   . PRO   B 1  595 ? -0.637  14.541  -11.748 1    23.595  ? 595  PRO   B C   1 2 
ATOM   9817  O  O   . PRO   B 1  595 ? -0.165  13.491  -12.218 1    23.027  ? 595  PRO   B O   1 2 
ATOM   9818  C  CB  . PRO   B 1  595 ? -3.083  14.919  -12.419 1    23.233  ? 595  PRO   B CB  1 2 
ATOM   9819  C  CG  . PRO   B 1  595 ? -3.393  16.39   -12.179 1    23.748  ? 595  PRO   B CG  1 2 
ATOM   9820  C  CD  . PRO   B 1  595 ? -3.427  16.533  -10.634 1    21.547  ? 595  PRO   B CD  1 2 
ATOM   9821  N  N   . GLU   B 1  596 ? 0.088   15.661  -11.538 1    22.638  ? 596  GLU   B N   1 2 
ATOM   9822  C  CA  . GLU   B 1  596 ? 1.511   15.717  -11.862 1    23.597  ? 596  GLU   B CA  1 2 
ATOM   9823  C  C   . GLU   B 1  596 ? 2.346   15.245  -10.665 1    21.788  ? 596  GLU   B C   1 2 
ATOM   9824  O  O   . GLU   B 1  596 ? 3.104   16.014  -10.054 1    21.156  ? 596  GLU   B O   1 2 
ATOM   9825  C  CB  . GLU   B 1  596 ? 1.969   17.051  -12.47  1    25.408  ? 596  GLU   B CB  1 2 
ATOM   9826  C  CG  . GLU   B 1  596 ? 1.285   17.395  -13.778 1    28.681  ? 596  GLU   B CG  1 2 
ATOM   9827  C  CD  . GLU   B 1  596 ? 1.821   18.588  -14.584 1    32.365  ? 596  GLU   B CD  1 2 
ATOM   9828  O  OE1 . GLU   B 1  596 ? 2.873   19.146  -14.217 1    32.041  ? 596  GLU   B OE1 1 2 
ATOM   9829  O  OE2 . GLU   B 1  596 ? 1.165   19      -15.582 1    34.636  ? 596  GLU   B OE2 1 2 
ATOM   9830  N  N   . TYR   B 1  597 ? 2.231   13.935  -10.36  1    20.409  ? 597  TYR   B N   1 2 
ATOM   9831  C  CA  . TYR   B 1  597 ? 2.527   13.462  -9.03   1    19.92   ? 597  TYR   B CA  1 2 
ATOM   9832  C  C   . TYR   B 1  597 ? 4.049   13.348  -8.887  1    20.228  ? 597  TYR   B C   1 2 
ATOM   9833  O  O   . TYR   B 1  597 ? 4.529   13.141  -7.776  1    21.162  ? 597  TYR   B O   1 2 
ATOM   9834  C  CB  . TYR   B 1  597 ? 1.931   12.085  -8.638  1    18.702  ? 597  TYR   B CB  1 2 
ATOM   9835  C  CG  . TYR   B 1  597 ? 2.293   11.052  -9.685  1    18.187  ? 597  TYR   B CG  1 2 
ATOM   9836  C  CD1 . TYR   B 1  597 ? 3.493   10.368  -9.626  1    17.844  ? 597  TYR   B CD1 1 2 
ATOM   9837  C  CD2 . TYR   B 1  597 ? 1.427   10.816  -10.764 1    18.926  ? 597  TYR   B CD2 1 2 
ATOM   9838  C  CE1 . TYR   B 1  597 ? 3.848   9.482   -10.636 1    18.243  ? 597  TYR   B CE1 1 2 
ATOM   9839  C  CE2 . TYR   B 1  597 ? 1.775   9.933   -11.779 1    19.85   ? 597  TYR   B CE2 1 2 
ATOM   9840  C  CZ  . TYR   B 1  597 ? 2.997   9.283   -11.715 1    19.2    ? 597  TYR   B CZ  1 2 
ATOM   9841  O  OH  . TYR   B 1  597 ? 3.302   8.431   -12.746 1    19.732  ? 597  TYR   B OH  1 2 
ATOM   9842  N  N   . GLN   B 1  598 ? 4.77    13.38   -10.008 1    22.742  ? 598  GLN   B N   1 2 
ATOM   9843  C  CA  . GLN   B 1  598 ? 6.227   13.232  -10.008 1    24.828  ? 598  GLN   B CA  1 2 
ATOM   9844  C  C   . GLN   B 1  598 ? 6.909   14.603  -9.844  1    24.901  ? 598  GLN   B C   1 2 
ATOM   9845  O  O   . GLN   B 1  598 ? 8.123   14.684  -9.624  1    25.33   ? 598  GLN   B O   1 2 
ATOM   9846  C  CB  . GLN   B 1  598 ? 6.519   12.517  -11.328 1    27.175  ? 598  GLN   B CB  1 2 
ATOM   9847  C  CG  . GLN   B 1  598 ? 7.661   11.517  -11.282 1    32.799  ? 598  GLN   B CG  1 2 
ATOM   9848  C  CD  . GLN   B 1  598 ? 8.196   11.139  -12.654 1    32.308  ? 598  GLN   B CD  1 2 
ATOM   9849  O  OE1 . GLN   B 1  598 ? 7.525   10.495  -13.46  1    31.123  ? 598  GLN   B OE1 1 2 
ATOM   9850  N  NE2 . GLN   B 1  598 ? 9.443   11.518  -12.926 1    35.489  ? 598  GLN   B NE2 1 2 
ATOM   9851  N  N   . TRP   B 1  599 ? 6.122   15.688  -9.825  1    24.058  ? 599  TRP   B N   1 2 
ATOM   9852  C  CA  . TRP   B 1  599 ? 6.681   17.034  -9.852  1    25.06   ? 599  TRP   B CA  1 2 
ATOM   9853  C  C   . TRP   B 1  599 ? 7.349   17.411  -8.525  1    24.088  ? 599  TRP   B C   1 2 
ATOM   9854  O  O   . TRP   B 1  599 ? 6.786   17.234  -7.44   1    23.811  ? 599  TRP   B O   1 2 
ATOM   9855  C  CB  . TRP   B 1  599 ? 5.61    18.042  -10.273 1    25.68   ? 599  TRP   B CB  1 2 
ATOM   9856  C  CG  . TRP   B 1  599 ? 6.154   19.435  -10.368 1    27.569  ? 599  TRP   B CG  1 2 
ATOM   9857  C  CD1 . TRP   B 1  599 ? 6.764   20.018  -11.446 1    27.591  ? 599  TRP   B CD1 1 2 
ATOM   9858  C  CD2 . TRP   B 1  599 ? 6.204   20.391  -9.282  1    25.864  ? 599  TRP   B CD2 1 2 
ATOM   9859  N  NE1 . TRP   B 1  599 ? 7.172   21.28   -11.094 1    28.081  ? 599  TRP   B NE1 1 2 
ATOM   9860  C  CE2 . TRP   B 1  599 ? 6.849   21.539  -9.789  1    27.731  ? 599  TRP   B CE2 1 2 
ATOM   9861  C  CE3 . TRP   B 1  599 ? 5.75    20.39   -7.964  1    26.102  ? 599  TRP   B CE3 1 2 
ATOM   9862  C  CZ2 . TRP   B 1  599 ? 7.054   22.676  -9.003  1    29.307  ? 599  TRP   B CZ2 1 2 
ATOM   9863  C  CZ3 . TRP   B 1  599 ? 5.955   21.503  -7.176  1    26.873  ? 599  TRP   B CZ3 1 2 
ATOM   9864  C  CH2 . TRP   B 1  599 ? 6.586   22.642  -7.693  1    29.037  ? 599  TRP   B CH2 1 2 
ATOM   9865  N  N   . HIS   B 1  600 ? 8.591   17.917  -8.615  1    25.631  ? 600  HIS   B N   1 2 
ATOM   9866  C  CA  . HIS   B 1  600 ? 9.271   18.602  -7.507  1    24.463  ? 600  HIS   B CA  1 2 
ATOM   9867  C  C   . HIS   B 1  600 ? 9.682   20.005  -7.949  1    24.478  ? 600  HIS   B C   1 2 
ATOM   9868  O  O   . HIS   B 1  600 ? 10.016  20.212  -9.117  1    24.025  ? 600  HIS   B O   1 2 
ATOM   9869  C  CB  . HIS   B 1  600 ? 10.525  17.809  -7.1    1    25.245  ? 600  HIS   B CB  1 2 
ATOM   9870  C  CG  . HIS   B 1  600 ? 10.135  16.493  -6.478  1    26.689  ? 600  HIS   B CG  1 2 
ATOM   9871  N  ND1 . HIS   B 1  600 ? 9.819   15.379  -7.249  1    28.109  ? 600  HIS   B ND1 1 2 
ATOM   9872  C  CD2 . HIS   B 1  600 ? 9.97    16.115  -5.199  1    25.599  ? 600  HIS   B CD2 1 2 
ATOM   9873  C  CE1 . HIS   B 1  600 ? 9.439   14.383  -6.462  1    26.954  ? 600  HIS   B CE1 1 2 
ATOM   9874  N  NE2 . HIS   B 1  600 ? 9.542   14.799  -5.213  1    27.439  ? 600  HIS   B NE2 1 2 
ATOM   9875  N  N   . PRO   B 1  601 ? 9.705   21.008  -7.043  1    23.696  ? 601  PRO   B N   1 2 
ATOM   9876  C  CA  . PRO   B 1  601 ? 10.174  22.346  -7.396  1    24.758  ? 601  PRO   B CA  1 2 
ATOM   9877  C  C   . PRO   B 1  601 ? 11.674  22.325  -7.683  1    25.522  ? 601  PRO   B C   1 2 
ATOM   9878  O  O   . PRO   B 1  601 ? 12.381  21.488  -7.183  1    24.995  ? 601  PRO   B O   1 2 
ATOM   9879  C  CB  . PRO   B 1  601 ? 9.88    23.145  -6.098  1    23.655  ? 601  PRO   B CB  1 2 
ATOM   9880  C  CG  . PRO   B 1  601 ? 9.964   22.12   -4.979  1    23.11   ? 601  PRO   B CG  1 2 
ATOM   9881  C  CD  . PRO   B 1  601 ? 9.362   20.882  -5.606  1    22.413  ? 601  PRO   B CD  1 2 
ATOM   9882  N  N   . PRO   B 1  602 ? 12.217  23.27   -8.469  1    28.651  ? 602  PRO   B N   1 2 
ATOM   9883  C  CA  . PRO   B 1  602 ? 13.669  23.364  -8.635  1    30.62   ? 602  PRO   B CA  1 2 
ATOM   9884  C  C   . PRO   B 1  602 ? 14.266  24.036  -7.399  1    30.609  ? 602  PRO   B C   1 2 
ATOM   9885  O  O   . PRO   B 1  602 ? 13.517  24.526  -6.574  1    30.055  ? 602  PRO   B O   1 2 
ATOM   9886  C  CB  . PRO   B 1  602 ? 13.709  24.212  -9.912  1    32.514  ? 602  PRO   B CB  1 2 
ATOM   9887  C  CG  . PRO   B 1  602 ? 12.582  25.199  -9.725  1    32.523  ? 602  PRO   B CG  1 2 
ATOM   9888  C  CD  . PRO   B 1  602 ? 11.449  24.311  -9.178  1    30.068  ? 602  PRO   B CD  1 2 
ATOM   9889  N  N   . LEU   B 1  603 ? 15.598  24.005  -7.225  1    32.414  ? 603  LEU   B N   1 2 
ATOM   9890  C  CA  . LEU   B 1  603 ? 16.323  24.753  -6.193  1    34.749  ? 603  LEU   B CA  1 2 
ATOM   9891  C  C   . LEU   B 1  603 ? 16.342  26.243  -6.527  1    36.972  ? 603  LEU   B C   1 2 
ATOM   9892  O  O   . LEU   B 1  603 ? 16.481  26.619  -7.689  1    38.61   ? 603  LEU   B O   1 2 
ATOM   9893  C  CB  . LEU   B 1  603 ? 17.777  24.281  -6.041  1    36.954  ? 603  LEU   B CB  1 2 
ATOM   9894  C  CG  . LEU   B 1  603 ? 17.94   22.839  -5.554  1    38.51   ? 603  LEU   B CG  1 2 
ATOM   9895  C  CD1 . LEU   B 1  603 ? 19.334  22.34   -5.84   1    41.521  ? 603  LEU   B CD1 1 2 
ATOM   9896  C  CD2 . LEU   B 1  603 ? 17.559  22.703  -4.055  1    38.613  ? 603  LEU   B CD2 1 2 
ATOM   9897  N  N   . PRO   B 1  604 ? 16.265  27.154  -5.529  1    37.301  ? 604  PRO   B N   1 2 
ATOM   9898  C  CA  . PRO   B 1  604 ? 16.498  28.577  -5.787  1    39.67   ? 604  PRO   B CA  1 2 
ATOM   9899  C  C   . PRO   B 1  604 ? 17.925  28.818  -6.291  1    43.915  ? 604  PRO   B C   1 2 
ATOM   9900  O  O   . PRO   B 1  604 ? 18.815  27.98   -6.121  1    40.4    ? 604  PRO   B O   1 2 
ATOM   9901  C  CB  . PRO   B 1  604 ? 16.231  29.277  -4.449  1    39.058  ? 604  PRO   B CB  1 2 
ATOM   9902  C  CG  . PRO   B 1  604 ? 15.505  28.253  -3.604  1    36.395  ? 604  PRO   B CG  1 2 
ATOM   9903  C  CD  . PRO   B 1  604 ? 15.939  26.869  -4.12   1    36.264  ? 604  PRO   B CD  1 2 
ATOM   9904  N  N   . ASP   B 1  605 ? 18.131  29.96   -6.956  1    52.146  ? 605  ASP   B N   1 2 
ATOM   9905  C  CA  . ASP   B 1  605 ? 19.405  30.204  -7.62   1    64.457  ? 605  ASP   B CA  1 2 
ATOM   9906  C  C   . ASP   B 1  605 ? 20.534  30.268  -6.592  1    62.829  ? 605  ASP   B C   1 2 
ATOM   9907  O  O   . ASP   B 1  605 ? 20.408  30.985  -5.595  1    61.52   ? 605  ASP   B O   1 2 
ATOM   9908  C  CB  . ASP   B 1  605 ? 19.318  31.32   -8.651  1    72.469  ? 605  ASP   B CB  1 2 
ATOM   9909  C  CG  . ASP   B 1  605 ? 18.828  30.877  -10.026 1    79.472  ? 605  ASP   B CG  1 2 
ATOM   9910  O  OD1 . ASP   B 1  605 ? 19.463  29.97   -10.619 1    83.568  ? 605  ASP   B OD1 1 2 
ATOM   9911  O  OD2 . ASP   B 1  605 ? 17.82   31.444  -10.502 1    82.685  ? 605  ASP   B OD2 1 2 
ATOM   9912  N  N   . ASN   B 1  606 ? 21.59   29.469  -6.846  1    61.125  ? 606  ASN   B N   1 2 
ATOM   9913  C  CA  . ASN   B 1  606 ? 22.747  29.294  -5.972  1    66.698  ? 606  ASN   B CA  1 2 
ATOM   9914  C  C   . ASN   B 1  606 ? 22.294  29.104  -4.526  1    67.866  ? 606  ASN   B C   1 2 
ATOM   9915  O  O   . ASN   B 1  606 ? 22.526  29.976  -3.683  1    69.075  ? 606  ASN   B O   1 2 
ATOM   9916  C  CB  . ASN   B 1  606 ? 23.682  30.505  -5.925  1    70.511  ? 606  ASN   B CB  1 2 
ATOM   9917  C  CG  . ASN   B 1  606 ? 24.357  30.845  -7.229  1    69.424  ? 606  ASN   B CG  1 2 
ATOM   9918  O  OD1 . ASN   B 1  606 ? 24.873  29.968  -7.929  1    68.418  ? 606  ASN   B OD1 1 2 
ATOM   9919  N  ND2 . ASN   B 1  606 ? 24.38   32.125  -7.557  1    72.345  ? 606  ASN   B ND2 1 2 
ATOM   9920  N  N   . TYR   B 1  607 ? 21.63   27.971  -4.262  1    66.159  ? 607  TYR   B N   1 2 
ATOM   9921  C  CA  . TYR   B 1  607 ? 21.298  27.568  -2.907  1    59.837  ? 607  TYR   B CA  1 2 
ATOM   9922  C  C   . TYR   B 1  607 ? 22.418  26.67   -2.381  1    57.287  ? 607  TYR   B C   1 2 
ATOM   9923  O  O   . TYR   B 1  607 ? 22.883  25.781  -3.091  1    60.241  ? 607  TYR   B O   1 2 
ATOM   9924  C  CB  . TYR   B 1  607 ? 19.886  26.965  -2.945  1    58.224  ? 607  TYR   B CB  1 2 
ATOM   9925  C  CG  . TYR   B 1  607 ? 19.4    26.367  -1.625  1    51.779  ? 607  TYR   B CG  1 2 
ATOM   9926  C  CD1 . TYR   B 1  607 ? 18.759  27.154  -0.663  1    48.736  ? 607  TYR   B CD1 1 2 
ATOM   9927  C  CD2 . TYR   B 1  607 ? 19.617  25.019  -1.343  1    44.942  ? 607  TYR   B CD2 1 2 
ATOM   9928  C  CE1 . TYR   B 1  607 ? 18.338  26.619  0.549   1    47.64   ? 607  TYR   B CE1 1 2 
ATOM   9929  C  CE2 . TYR   B 1  607 ? 19.222  24.477  -0.138  1    46.195  ? 607  TYR   B CE2 1 2 
ATOM   9930  C  CZ  . TYR   B 1  607 ? 18.567  25.274  0.798   1    45.73   ? 607  TYR   B CZ  1 2 
ATOM   9931  O  OH  . TYR   B 1  607 ? 18.157  24.708  1.959   1    44.664  ? 607  TYR   B OH  1 2 
ATOM   9932  N  N   . PRO   B 1  608 ? 22.886  26.838  -1.123  1    56.424  ? 608  PRO   B N   1 2 
ATOM   9933  C  CA  . PRO   B 1  608 ? 22.337  27.834  -0.197  1    58.217  ? 608  PRO   B CA  1 2 
ATOM   9934  C  C   . PRO   B 1  608 ? 23.149  29.075  0.167   1    61.047  ? 608  PRO   B C   1 2 
ATOM   9935  O  O   . PRO   B 1  608 ? 23.676  29.133  1.266   1    64.649  ? 608  PRO   B O   1 2 
ATOM   9936  C  CB  . PRO   B 1  608 ? 22.301  26.852  0.985   1    56.561  ? 608  PRO   B CB  1 2 
ATOM   9937  C  CG  . PRO   B 1  608 ? 23.699  26.237  0.98    1    56.541  ? 608  PRO   B CG  1 2 
ATOM   9938  C  CD  . PRO   B 1  608 ? 23.921  25.987  -0.503  1    56.702  ? 608  PRO   B CD  1 2 
ATOM   9939  N  N   . GLU   B 1  609 ? 23.222  30.075  -0.723  1    69.191  ? 609  GLU   B N   1 2 
ATOM   9940  C  CA  . GLU   B 1  609 ? 24.031  31.267  -0.475  1    72.838  ? 609  GLU   B CA  1 2 
ATOM   9941  C  C   . GLU   B 1  609 ? 23.32   32.524  -1.006  1    67.715  ? 609  GLU   B C   1 2 
ATOM   9942  O  O   . GLU   B 1  609 ? 22.411  33.009  -0.298  1    66.737  ? 609  GLU   B O   1 2 
ATOM   9943  C  CB  . GLU   B 1  609 ? 25.391  31.157  -1.165  1    77.048  ? 609  GLU   B CB  1 2 
ATOM   9944  C  CG  . GLU   B 1  609 ? 26.05   29.788  -1.019  1    78.375  ? 609  GLU   B CG  1 2 
ATOM   9945  C  CD  . GLU   B 1  609 ? 26.742  29.402  -2.314  1    83.772  ? 609  GLU   B CD  1 2 
ATOM   9946  O  OE1 . GLU   B 1  609 ? 27.754  30.046  -2.687  1    91.211  ? 609  GLU   B OE1 1 2 
ATOM   9947  O  OE2 . GLU   B 1  609 ? 26.238  28.467  -2.975  1    83.713  ? 609  GLU   B OE2 1 2 
HETATM 9948  C  C1  . NAG   C 2  .   ? -25.973 35.248  13.187  1    60.322  ? 1    NAG   C C1  1 2 
HETATM 9949  C  C2  . NAG   C 2  .   ? -26.647 34.88   14.509  1    63.199  ? 1    NAG   C C2  1 2 
HETATM 9950  C  C3  . NAG   C 2  .   ? -27.239 33.482  14.34   1    64.318  ? 1    NAG   C C3  1 2 
HETATM 9951  C  C4  . NAG   C 2  .   ? -28.303 33.493  13.246  1    67.507  ? 1    NAG   C C4  1 2 
HETATM 9952  C  C5  . NAG   C 2  .   ? -27.654 33.917  11.928  1    64.311  ? 1    NAG   C C5  1 2 
HETATM 9953  C  C6  . NAG   C 2  .   ? -28.691 34.227  10.86   1    69.069  ? 1    NAG   C C6  1 2 
HETATM 9954  C  C7  . NAG   C 2  .   ? -24.889 35.73   16.124  1    69.876  ? 1    NAG   C C7  1 2 
HETATM 9955  C  C8  . NAG   C 2  .   ? -23.645 35.085  16.676  1    63.594  ? 1    NAG   C C8  1 2 
HETATM 9956  N  N2  . NAG   C 2  .   ? -25.87  34.898  15.74   1    67.512  ? 1    NAG   C N2  1 2 
HETATM 9957  O  O3  . NAG   C 2  .   ? -27.73  32.977  15.574  1    64.838  ? 1    NAG   C O3  1 2 
HETATM 9958  O  O4  . NAG   C 2  .   ? -28.938 32.204  13.095  1    71.248  ? 1    NAG   C O4  1 2 
HETATM 9959  O  O5  . NAG   C 2  .   ? -26.895 35.14   12.095  1    61.706  ? 1    NAG   C O5  1 2 
HETATM 9960  O  O6  . NAG   C 2  .   ? -28.366 33.65   9.595   1    68.838  ? 1    NAG   C O6  1 2 
HETATM 9961  O  O7  . NAG   C 2  .   ? -25.014 36.953  16.044  1    72.473  ? 1    NAG   C O7  1 2 
HETATM 9962  C  C1  . NAG   C 2  .   ? -30.28  32.063  13.457  1    75.854  ? 2    NAG   C C1  1 2 
HETATM 9963  C  C2  . NAG   C 2  .   ? -30.775 30.663  13.087  1    78.607  ? 2    NAG   C C2  1 2 
HETATM 9964  C  C3  . NAG   C 2  .   ? -32.158 30.413  13.695  1    81.551  ? 2    NAG   C C3  1 2 
HETATM 9965  C  C4  . NAG   C 2  .   ? -32.203 30.714  15.188  1    83.177  ? 2    NAG   C C4  1 2 
HETATM 9966  C  C5  . NAG   C 2  .   ? -31.659 32.117  15.471  1    84.63   ? 2    NAG   C C5  1 2 
HETATM 9967  C  C6  . NAG   C 2  .   ? -31.494 32.424  16.953  1    84.249  ? 2    NAG   C C6  1 2 
HETATM 9968  C  C7  . NAG   C 2  .   ? -30.01  29.793  10.836  1    81.787  ? 2    NAG   C C7  1 2 
HETATM 9969  C  C8  . NAG   C 2  .   ? -30.505 29.573  9.436   1    84.039  ? 2    NAG   C C8  1 2 
HETATM 9970  N  N2  . NAG   C 2  .   ? -30.851 30.452  11.651  1    83.046  ? 2    NAG   C N2  1 2 
HETATM 9971  O  O3  . NAG   C 2  .   ? -32.571 29.074  13.472  1    79.894  ? 2    NAG   C O3  1 2 
HETATM 9972  O  O4  . NAG   C 2  .   ? -33.564 30.617  15.608  1    81.142  ? 2    NAG   C O4  1 2 
HETATM 9973  O  O5  . NAG   C 2  .   ? -30.358 32.289  14.867  1    78.147  ? 2    NAG   C O5  1 2 
HETATM 9974  O  O6  . NAG   C 2  .   ? -30.664 31.466  17.634  1    79.288  ? 2    NAG   C O6  1 2 
HETATM 9975  O  O7  . NAG   C 2  .   ? -28.908 29.39   11.202  1    74.768  ? 2    NAG   C O7  1 2 
HETATM 9976  C  C1  . NAG   D 3  .   ? 21.527  10.979  -0.744  0.96 34.38   ? 1    NAG   D C1  1 2 
HETATM 9977  C  C2  . NAG   D 3  .   ? 22.746  10.502  -1.516  0.96 34.502  ? 1    NAG   D C2  1 2 
HETATM 9978  C  C3  . NAG   D 3  .   ? 23.97   11.082  -0.821  0.96 38.149  ? 1    NAG   D C3  1 2 
HETATM 9979  C  C4  . NAG   D 3  .   ? 23.898  12.602  -0.768  0.96 40.606  ? 1    NAG   D C4  1 2 
HETATM 9980  C  C5  . NAG   D 3  .   ? 22.664  12.975  0.048   0.96 41.276  ? 1    NAG   D C5  1 2 
HETATM 9981  C  C6  . NAG   D 3  .   ? 22.43   14.468  0.135   0.96 45.57   ? 1    NAG   D C6  1 2 
HETATM 9982  C  C7  . NAG   D 3  .   ? 22.939  8.185   -0.713  0.96 33.165  ? 1    NAG   D C7  1 2 
HETATM 9983  C  C8  . NAG   D 3  .   ? 23.014  6.729   -1.071  0.96 33.354  ? 1    NAG   D C8  1 2 
HETATM 9984  N  N2  . NAG   D 3  .   ? 22.958  9.077   -1.715  0.96 33.702  ? 1    NAG   D N2  1 2 
HETATM 9985  O  O3  . NAG   D 3  .   ? 25.077  10.644  -1.558  0.96 35.888  ? 1    NAG   D O3  1 2 
HETATM 9986  O  O4  . NAG   D 3  .   ? 25.069  13.069  -0.108  0.96 44.28   ? 1    NAG   D O4  1 2 
HETATM 9987  O  O5  . NAG   D 3  .   ? 21.501  12.408  -0.61   0.96 36.235  ? 1    NAG   D O5  1 2 
HETATM 9988  O  O6  . NAG   D 3  .   ? 22.762  15.076  -1.13   0.96 55.404  ? 1    NAG   D O6  1 2 
HETATM 9989  O  O7  . NAG   D 3  .   ? 22.837  8.548   0.452   0.96 35.338  ? 1    NAG   D O7  1 2 
HETATM 9990  C  C1  . FUC   D 3  .   ? 21.718  15.744  -1.79   0.98 66.005  ? 2    FUC   D C1  1 2 
HETATM 9991  C  C2  . FUC   D 3  .   ? 22.367  16.72   -2.772  0.98 77.581  ? 2    FUC   D C2  1 2 
HETATM 9992  C  C3  . FUC   D 3  .   ? 21.677  16.68   -4.139  0.98 80.884  ? 2    FUC   D C3  1 2 
HETATM 9993  C  C4  . FUC   D 3  .   ? 21.721  15.27   -4.741  0.98 75.076  ? 2    FUC   D C4  1 2 
HETATM 9994  C  C5  . FUC   D 3  .   ? 21.521  14.222  -3.643  0.98 69.887  ? 2    FUC   D C5  1 2 
HETATM 9995  C  C6  . FUC   D 3  .   ? 20.708  13.008  -4.037  0.98 72.66   ? 2    FUC   D C6  1 2 
HETATM 9996  O  O2  . FUC   D 3  .   ? 23.761  16.443  -2.905  0.98 81.498  ? 2    FUC   D O2  1 2 
HETATM 9997  O  O3  . FUC   D 3  .   ? 20.325  17.129  -3.982  0.98 70.722  ? 2    FUC   D O3  1 2 
HETATM 9998  O  O4  . FUC   D 3  .   ? 20.722  15.158  -5.745  0.98 69.254  ? 2    FUC   D O4  1 2 
HETATM 9999  O  O5  . FUC   D 3  .   ? 20.874  14.829  -2.498  0.98 68.237  ? 2    FUC   D O5  1 2 
HETATM 10000 C  C1  . NAG   E 4  .   ? 29.152  -32.105 -15.471 1    26.983  ? 1    NAG   E C1  1 ? 
HETATM 10001 C  C2  . NAG   E 4  .   ? 28.218  -33.296 -15.701 1    33.922  ? 1    NAG   E C2  1 ? 
HETATM 10002 C  C3  . NAG   E 4  .   ? 27.511  -33.643 -14.394 1    33.661  ? 1    NAG   E C3  1 ? 
HETATM 10003 C  C4  . NAG   E 4  .   ? 28.496  -33.828 -13.258 1    28.048  ? 1    NAG   E C4  1 ? 
HETATM 10004 C  C5  . NAG   E 4  .   ? 29.34   -32.572 -13.092 1    30.873  ? 1    NAG   E C5  1 ? 
HETATM 10005 C  C6  . NAG   E 4  .   ? 30.459  -32.737 -12.085 1    32.311  ? 1    NAG   E C6  1 ? 
HETATM 10006 C  C7  . NAG   E 4  .   ? 27.048  -33.132 -17.85  1    38.149  ? 1    NAG   E C7  1 ? 
HETATM 10007 C  C8  . NAG   E 4  .   ? 25.941  -32.449 -18.616 1    38.318  ? 1    NAG   E C8  1 ? 
HETATM 10008 N  N2  . NAG   E 4  .   ? 27.168  -32.812 -16.571 1    35.51   ? 1    NAG   E N2  1 ? 
HETATM 10009 O  O3  . NAG   E 4  .   ? 26.724  -34.808 -14.533 1    36.985  ? 1    NAG   E O3  1 ? 
HETATM 10010 O  O4  . NAG   E 4  .   ? 27.753  -33.995 -12.066 1    35.275  ? 1    NAG   E O4  1 ? 
HETATM 10011 O  O5  . NAG   E 4  .   ? 29.992  -32.374 -14.357 1    27.013  ? 1    NAG   E O5  1 ? 
HETATM 10012 O  O6  . NAG   E 4  .   ? 30.953  -34.12  -12.234 1    32.685  ? 1    NAG   E O6  1 ? 
HETATM 10013 O  O7  . NAG   E 4  .   ? 27.801  -33.949 -18.351 1    39.196  ? 1    NAG   E O7  1 ? 
HETATM 10014 C  C1  . NAG   E 4  .   ? 27.912  -35.205 -11.402 1    38.197  ? 2    NAG   E C1  1 ? 
HETATM 10015 C  C2  . NAG   E 4  .   ? 27.393  -35.108 -9.981  1    39.964  ? 2    NAG   E C2  1 ? 
HETATM 10016 C  C3  . NAG   E 4  .   ? 27.515  -36.482 -9.328  1    45.703  ? 2    NAG   E C3  1 ? 
HETATM 10017 C  C4  . NAG   E 4  .   ? 26.907  -37.572 -10.202 1    47.695  ? 2    NAG   E C4  1 ? 
HETATM 10018 C  C5  . NAG   E 4  .   ? 27.526  -37.528 -11.597 1    50.662  ? 2    NAG   E C5  1 ? 
HETATM 10019 C  C6  . NAG   E 4  .   ? 27.005  -38.54  -12.607 1    59.173  ? 2    NAG   E C6  1 ? 
HETATM 10020 C  C7  . NAG   E 4  .   ? 27.292  -32.965 -8.765  1    57.444  ? 2    NAG   E C7  1 ? 
HETATM 10021 C  C8  . NAG   E 4  .   ? 28.098  -31.753 -8.403  1    53.097  ? 2    NAG   E C8  1 ? 
HETATM 10022 N  N2  . NAG   E 4  .   ? 27.973  -34.044 -9.182  1    44.54   ? 2    NAG   E N2  1 ? 
HETATM 10023 O  O3  . NAG   E 4  .   ? 26.808  -36.384 -8.113  1    47.477  ? 2    NAG   E O3  1 ? 
HETATM 10024 O  O4  . NAG   E 4  .   ? 27.117  -38.812 -9.539  1    59.796  ? 2    NAG   E O4  1 ? 
HETATM 10025 O  O5  . NAG   E 4  .   ? 27.23   -36.223 -12.129 1    44.521  ? 2    NAG   E O5  1 ? 
HETATM 10026 O  O6  . NAG   E 4  .   ? 25.588  -38.575 -12.641 1    56.007  ? 2    NAG   E O6  1 ? 
HETATM 10027 O  O7  . NAG   E 4  .   ? 26.066  -32.963 -8.673  1    67.724  ? 2    NAG   E O7  1 ? 
HETATM 10028 C  C1  . BMA   E 4  .   ? 26.017  -39.513 -9.037  1    62.886  ? 3    BMA   E C1  1 ? 
HETATM 10029 C  C2  . BMA   E 4  .   ? 26.36   -40.995 -9.164  1    67.063  ? 3    BMA   E C2  1 ? 
HETATM 10030 C  C3  . BMA   E 4  .   ? 25.265  -41.889 -8.534  1    68.812  ? 3    BMA   E C3  1 ? 
HETATM 10031 C  C4  . BMA   E 4  .   ? 24.902  -41.44  -7.112  1    69.17   ? 3    BMA   E C4  1 ? 
HETATM 10032 C  C5  . BMA   E 4  .   ? 24.614  -39.904 -7.071  1    68.725  ? 3    BMA   E C5  1 ? 
HETATM 10033 C  C6  . BMA   E 4  .   ? 24.422  -39.338 -5.675  1    61.763  ? 3    BMA   E C6  1 ? 
HETATM 10034 O  O2  . BMA   E 4  .   ? 27.693  -41.217 -8.699  1    59.089  ? 3    BMA   E O2  1 ? 
HETATM 10035 O  O3  . BMA   E 4  .   ? 25.618  -43.276 -8.587  1    63.65   ? 3    BMA   E O3  1 ? 
HETATM 10036 O  O4  . BMA   E 4  .   ? 23.75   -42.173 -6.666  1    61.427  ? 3    BMA   E O4  1 ? 
HETATM 10037 O  O5  . BMA   E 4  .   ? 25.719  -39.163 -7.681  1    68.308  ? 3    BMA   E O5  1 ? 
HETATM 10038 O  O6  . BMA   E 4  .   ? 23.918  -37.999 -5.691  1    50.364  ? 3    BMA   E O6  1 ? 
HETATM 10039 C  C1  . FUC   E 4  .   ? 31.702  -34.644 -11.154 1    43.623  ? 4    FUC   E C1  1 ? 
HETATM 10040 C  C2  . FUC   E 4  .   ? 32.415  -35.901 -11.664 1    44.733  ? 4    FUC   E C2  1 ? 
HETATM 10041 C  C3  . FUC   E 4  .   ? 33.459  -35.533 -12.714 1    47.855  ? 4    FUC   E C3  1 ? 
HETATM 10042 C  C4  . FUC   E 4  .   ? 34.418  -34.445 -12.211 1    49.746  ? 4    FUC   E C4  1 ? 
HETATM 10043 C  C5  . FUC   E 4  .   ? 33.61   -33.251 -11.701 1    37.901  ? 4    FUC   E C5  1 ? 
HETATM 10044 C  C6  . FUC   E 4  .   ? 34.417  -32.155 -11.053 1    41.31   ? 4    FUC   E C6  1 ? 
HETATM 10045 O  O2  . FUC   E 4  .   ? 31.456  -36.838 -12.172 1    54.396  ? 4    FUC   E O2  1 ? 
HETATM 10046 O  O3  . FUC   E 4  .   ? 34.181  -36.718 -13.027 1    59.784  ? 4    FUC   E O3  1 ? 
HETATM 10047 O  O4  . FUC   E 4  .   ? 35.195  -35.01  -11.126 1    52.26   ? 4    FUC   E O4  1 ? 
HETATM 10048 O  O5  . FUC   E 4  .   ? 32.669  -33.69  -10.687 1    37.943  ? 4    FUC   E O5  1 ? 
HETATM 10049 C  C1  . NAG   F 5  .   ? -11.459 -10.653 -42.57  1    42.42   ? 701  NAG   A C1  1 1 
HETATM 10050 C  C2  . NAG   F 5  .   ? -11.484 -11.678 -43.693 1    42.533  ? 701  NAG   A C2  1 1 
HETATM 10051 C  C3  . NAG   F 5  .   ? -12.36  -11.183 -44.847 1    44.476  ? 701  NAG   A C3  1 1 
HETATM 10052 C  C4  . NAG   F 5  .   ? -13.766 -10.868 -44.36  1    45.971  ? 701  NAG   A C4  1 1 
HETATM 10053 C  C5  . NAG   F 5  .   ? -13.644 -9.799  -43.268 1    47.654  ? 701  NAG   A C5  1 1 
HETATM 10054 C  C6  . NAG   F 5  .   ? -14.97  -9.454  -42.627 1    47.903  ? 701  NAG   A C6  1 1 
HETATM 10055 C  C7  . NAG   F 5  .   ? -9.577  -13.168 -44.076 1    47.453  ? 701  NAG   A C7  1 1 
HETATM 10056 C  C8  . NAG   F 5  .   ? -8.401  -13.446 -44.964 1    47.108  ? 701  NAG   A C8  1 1 
HETATM 10057 N  N2  . NAG   F 5  .   ? -10.165 -11.975 -44.219 1    46.661  ? 701  NAG   A N2  1 1 
HETATM 10058 O  O3  . NAG   F 5  .   ? -12.396 -12.264 -45.75  1    44.605  ? 701  NAG   A O3  1 1 
HETATM 10059 O  O4  . NAG   F 5  .   ? -14.605 -10.528 -45.475 1    52.375  ? 701  NAG   A O4  1 1 
HETATM 10060 O  O5  . NAG   F 5  .   ? -12.79  -10.293 -42.193 1    44.491  ? 701  NAG   A O5  1 1 
HETATM 10061 O  O6  . NAG   F 5  .   ? -14.778 -8.522  -41.552 1    44.51   ? 701  NAG   A O6  1 1 
HETATM 10062 O  O7  . NAG   F 5  .   ? -10.008 -14.005 -43.292 1    48.307  ? 701  NAG   A O7  1 1 
HETATM 10063 C  C1  . NAG   G 5  .   ? 1.136   15.197  -18.449 1    30.982  ? 702  NAG   A C1  1 1 
HETATM 10064 C  C2  . NAG   G 5  .   ? 0.419   16.541  -18.322 1    32.766  ? 702  NAG   A C2  1 1 
HETATM 10065 C  C3  . NAG   G 5  .   ? 0.156   17.186  -19.695 1    36.763  ? 702  NAG   A C3  1 1 
HETATM 10066 C  C4  . NAG   G 5  .   ? 1.276   17.019  -20.714 1    37.336  ? 702  NAG   A C4  1 1 
HETATM 10067 C  C5  . NAG   G 5  .   ? 1.837   15.606  -20.764 1    35.005  ? 702  NAG   A C5  1 1 
HETATM 10068 C  C6  . NAG   G 5  .   ? 3.082   15.592  -21.66  1    35.29   ? 702  NAG   A C6  1 1 
HETATM 10069 C  C7  . NAG   G 5  .   ? -1.612  16.765  -17.074 1    40.831  ? 702  NAG   A C7  1 1 
HETATM 10070 C  C8  . NAG   G 5  .   ? -2.918  16.184  -16.627 1    45.839  ? 702  NAG   A C8  1 1 
HETATM 10071 N  N2  . NAG   G 5  .   ? -0.937  16.117  -18     1    37.575  ? 702  NAG   A N2  1 1 
HETATM 10072 O  O3  . NAG   G 5  .   ? -0.237  18.558  -19.604 1    34.548  ? 702  NAG   A O3  1 1 
HETATM 10073 O  O4  . NAG   G 5  .   ? 0.7     17.326  -21.981 1    40.937  ? 702  NAG   A O4  1 1 
HETATM 10074 O  O5  . NAG   G 5  .   ? 2.176   15.145  -19.429 1    33.288  ? 702  NAG   A O5  1 1 
HETATM 10075 O  O6  . NAG   G 5  .   ? 4.299   15.057  -21.09  1    35.936  ? 702  NAG   A O6  1 1 
HETATM 10076 O  O7  . NAG   G 5  .   ? -1.148  17.785  -16.594 1    50.685  ? 702  NAG   A O7  1 1 
HETATM 10077 ZN ZN  . ZN    H 6  .   ? 0.461   -19.095 -21.046 1    17.802  ? 703  ZN    A ZN  1 1 
HETATM 10078 CL CL  . CL    I 7  .   ? -4.617  -16.293 -12.061 1    17.592  ? 704  CL    A CL  1 1 
HETATM 10079 O  O01 . A1IJX J 8  .   ? 1.615   -13.392 -21.904 1    25.077  ? 705  A1IJX A O01 1 ? 
HETATM 10080 C  C02 . A1IJX J 8  .   ? 2.231   -14.425 -22.015 1    28.76   ? 705  A1IJX A C02 1 ? 
HETATM 10081 C  C03 . A1IJX J 8  .   ? 1.996   -15.402 -23.184 1    33.052  ? 705  A1IJX A C03 1 ? 
HETATM 10082 N  N04 . A1IJX J 8  .   ? 0.641   -15.212 -23.798 1    35.084  ? 705  A1IJX A N04 1 ? 
HETATM 10083 C  C05 . A1IJX J 8  .   ? -0.483  -15.784 -23.025 1    26.75   ? 705  A1IJX A C05 1 ? 
HETATM 10084 C  C06 . A1IJX J 8  .   ? -1.845  -15.796 -23.781 1    25.546  ? 705  A1IJX A C06 1 ? 
HETATM 10085 C  C07 . A1IJX J 8  .   ? -2.451  -14.309 -23.807 1    25.031  ? 705  A1IJX A C07 1 ? 
HETATM 10086 C  C08 . A1IJX J 8  .   ? -3.069  -14.224 -22.329 1    21.577  ? 705  A1IJX A C08 1 ? 
HETATM 10087 C  C09 . A1IJX J 8  .   ? -3.55   -15.531 -21.986 1    24.379  ? 705  A1IJX A C09 1 ? 
HETATM 10088 N  N10 . A1IJX J 8  .   ? -2.834  -16.452 -23.133 1    24.538  ? 705  A1IJX A N10 1 ? 
HETATM 10089 C  C11 . A1IJX J 8  .   ? -3.307  -17.774 -23.487 1    27.549  ? 705  A1IJX A C11 1 ? 
HETATM 10090 C  C12 . A1IJX J 8  .   ? -4.448  -18.457 -22.708 1    31.273  ? 705  A1IJX A C12 1 ? 
HETATM 10091 N  N13 . A1IJX J 8  .   ? -5.327  -19.071 -23.675 1    29.336  ? 705  A1IJX A N13 1 ? 
HETATM 10092 C  C14 . A1IJX J 8  .   ? -3.745  -19.524 -21.823 1    30.152  ? 705  A1IJX A C14 1 ? 
HETATM 10093 C  C15 . A1IJX J 8  .   ? -4.505  -19.909 -20.54  1    39.962  ? 705  A1IJX A C15 1 ? 
HETATM 10094 C  C16 . A1IJX J 8  .   ? -5.557  -21.014 -20.821 1    47.229  ? 705  A1IJX A C16 1 ? 
HETATM 10095 O  O17 . A1IJX J 8  .   ? -6.178  -21.549 -19.836 1    50.379  ? 705  A1IJX A O17 1 ? 
HETATM 10096 O  O18 . A1IJX J 8  .   ? -5.817  -21.357 -22.035 1    54.638  ? 705  A1IJX A O18 1 ? 
HETATM 10097 O  O19 . A1IJX J 8  .   ? -2.745  -18.35  -24.375 1    28.188  ? 705  A1IJX A O19 1 ? 
HETATM 10098 C  C20 . A1IJX J 8  .   ? -0.208  -17.177 -22.541 1    31.158  ? 705  A1IJX A C20 1 ? 
HETATM 10099 O  O21 . A1IJX J 8  .   ? -0.096  -18.148 -23.368 1    26.151  ? 705  A1IJX A O21 1 ? 
HETATM 10100 O  O22 . A1IJX J 8  .   ? -0.162  -17.221 -21.244 1    23.731  ? 705  A1IJX A O22 1 ? 
HETATM 10101 C  C23 . A1IJX J 8  .   ? 2.966   -15.064 -24.291 1    25.72   ? 705  A1IJX A C23 1 ? 
HETATM 10102 N  N24 . A1IJX J 8  .   ? 3.25    -14.713 -20.989 1    27.604  ? 705  A1IJX A N24 1 ? 
HETATM 10103 C  C25 . A1IJX J 8  .   ? 4.26    -16.002 -20.922 1    25.96   ? 705  A1IJX A C25 1 ? 
HETATM 10104 C  C26 . A1IJX J 8  .   ? 4.896   -15.935 -19.664 1    22.221  ? 705  A1IJX A C26 1 ? 
HETATM 10105 C  C27 . A1IJX J 8  .   ? 4.945   -14.366 -19.309 1    22.491  ? 705  A1IJX A C27 1 ? 
HETATM 10106 C  C28 . A1IJX J 8  .   ? 3.597   -13.858 -19.959 1    23.281  ? 705  A1IJX A C28 1 ? 
HETATM 10107 C  C29 . A1IJX J 8  .   ? 3.969   -12.519 -20.553 1    19.391  ? 705  A1IJX A C29 1 ? 
HETATM 10108 O  O30 . A1IJX J 8  .   ? 3.717   -11.392 -19.951 1    18.925  ? 705  A1IJX A O30 1 ? 
HETATM 10109 O  O31 . A1IJX J 8  .   ? 4.506   -12.508 -21.693 1    22.546  ? 705  A1IJX A O31 1 ? 
HETATM 10110 C  C1  . PGE   K 9  .   ? 0.601   36.008  38.811  1    62.179  ? 701  PGE   B C1  1 2 
HETATM 10111 O  O1  . PGE   K 9  .   ? 0.073   37.322  38.618  1    60.05   ? 701  PGE   B O1  1 2 
HETATM 10112 C  C2  . PGE   K 9  .   ? -0.464  34.997  39.153  1    59.77   ? 701  PGE   B C2  1 2 
HETATM 10113 O  O2  . PGE   K 9  .   ? -1.458  35.558  40.015  1    51.165  ? 701  PGE   B O2  1 2 
HETATM 10114 C  C3  . PGE   K 9  .   ? -2.346  34.558  40.507  1    48.879  ? 701  PGE   B C3  1 2 
HETATM 10115 C  C4  . PGE   K 9  .   ? -3.768  35.011  40.457  1    48.423  ? 701  PGE   B C4  1 2 
HETATM 10116 O  O4  . PGE   K 9  .   ? -6.128  35.254  37.218  1    52.393  ? 701  PGE   B O4  1 2 
HETATM 10117 C  C6  . PGE   K 9  .   ? -4.828  35.742  37.002  1    51.98   ? 701  PGE   B C6  1 2 
HETATM 10118 C  C5  . PGE   K 9  .   ? -4.112  35.914  38.302  1    55.198  ? 701  PGE   B C5  1 2 
HETATM 10119 O  O3  . PGE   K 9  .   ? -4.363  34.818  39.181  1    47.478  ? 701  PGE   B O3  1 2 
HETATM 10120 O  O22 . P33   L 10 .   ? -1.952  39.054  36.243  1    55.041  ? 702  P33   B O22 1 2 
HETATM 10121 C  C21 . P33   L 10 .   ? -0.845  39.722  35.656  1    50.259  ? 702  P33   B C21 1 2 
HETATM 10122 C  C20 . P33   L 10 .   ? -1.22   41.098  35.208  1    53.213  ? 702  P33   B C20 1 2 
HETATM 10123 O  O19 . P33   L 10 .   ? -0.161  41.682  34.451  1    54.97   ? 702  P33   B O19 1 2 
HETATM 10124 C  C18 . P33   L 10 .   ? -0.61   42.523  33.388  1    50.016  ? 702  P33   B C18 1 2 
HETATM 10125 C  C17 . P33   L 10 .   ? -0.518  41.778  32.097  1    47.964  ? 702  P33   B C17 1 2 
HETATM 10126 O  O16 . P33   L 10 .   ? -1.264  42.44   31.091  1    50.482  ? 702  P33   B O16 1 2 
HETATM 10127 C  C15 . P33   L 10 .   ? -1.748  41.587  30.054  1    51.674  ? 702  P33   B C15 1 2 
HETATM 10128 C  C14 . P33   L 10 .   ? -3.026  40.885  30.446  1    53.698  ? 702  P33   B C14 1 2 
HETATM 10129 O  O13 . P33   L 10 .   ? -3.954  40.842  29.363  1    52.975  ? 702  P33   B O13 1 2 
HETATM 10130 C  C12 . P33   L 10 .   ? -5.251  40.366  29.729  1    53.631  ? 702  P33   B C12 1 2 
HETATM 10131 C  C11 . P33   L 10 .   ? -5.194  38.922  30.184  1    56.576  ? 702  P33   B C11 1 2 
HETATM 10132 O  O10 . P33   L 10 .   ? -6.299  38.621  31.035  1    65.908  ? 702  P33   B O10 1 2 
HETATM 10133 C  C9  . P33   L 10 .   ? -7.558  39.112  30.561  1    66.691  ? 702  P33   B C9  1 2 
HETATM 10134 C  C8  . P33   L 10 .   ? -8.396  37.98   29.986  1    66.363  ? 702  P33   B C8  1 2 
HETATM 10135 O  O7  . P33   L 10 .   ? -9.798  38.266  29.972  1    64.216  ? 702  P33   B O7  1 2 
HETATM 10136 C  C6  . P33   L 10 .   ? -10.52  37.733  31.089  1    59.057  ? 702  P33   B C6  1 2 
HETATM 10137 C  C5  . P33   L 10 .   ? -10.613 36.224  31.057  1    55.403  ? 702  P33   B C5  1 2 
HETATM 10138 O  O4  . P33   L 10 .   ? -10.892 35.725  32.367  1    56.94   ? 702  P33   B O4  1 2 
HETATM 10139 C  C3  . P33   L 10 .   ? -9.818  35.035  33.012  1    48.289  ? 702  P33   B C3  1 2 
HETATM 10140 C  C2  . P33   L 10 .   ? -8.919  35.981  33.748  1    53.683  ? 702  P33   B C2  1 2 
HETATM 10141 O  O1  . P33   L 10 .   ? -7.922  35.323  34.528  1    51.889  ? 702  P33   B O1  1 2 
HETATM 10142 O  O1  . PG4   M 11 .   ? 1.909   -0.75   4.79    1    59.24   ? 703  PG4   B O1  1 2 
HETATM 10143 C  C1  . PG4   M 11 .   ? 2.03    0.681   4.753   1    60.143  ? 703  PG4   B C1  1 2 
HETATM 10144 C  C2  . PG4   M 11 .   ? 1.617   1.251   3.422   1    72.657  ? 703  PG4   B C2  1 2 
HETATM 10145 O  O2  . PG4   M 11 .   ? 2.525   2.257   2.968   1    65.815  ? 703  PG4   B O2  1 2 
HETATM 10146 C  C3  . PG4   M 11 .   ? 2.674   2.3     1.542   1    59.077  ? 703  PG4   B C3  1 2 
HETATM 10147 C  C4  . PG4   M 11 .   ? 1.427   1.881   0.774   1    59.078  ? 703  PG4   B C4  1 2 
HETATM 10148 O  O3  . PG4   M 11 .   ? 1.781   1.575   -0.577  1    50.584  ? 703  PG4   B O3  1 2 
HETATM 10149 C  C5  . PG4   M 11 .   ? 0.696   1.668   -1.498  1    45.941  ? 703  PG4   B C5  1 2 
HETATM 10150 C  C6  . PG4   M 11 .   ? 0.718   0.494   -2.435  1    48.156  ? 703  PG4   B C6  1 2 
HETATM 10151 O  O4  . PG4   M 11 .   ? 0.319   0.837   -3.767  1    51.516  ? 703  PG4   B O4  1 2 
HETATM 10152 C  C7  . PG4   M 11 .   ? -0.99   0.386   -4.131  1    49.513  ? 703  PG4   B C7  1 2 
HETATM 10153 C  C8  . PG4   M 11 .   ? -1.09   -1.109  -4.174  1    48.471  ? 703  PG4   B C8  1 2 
HETATM 10154 O  O5  . PG4   M 11 .   ? -2.393  -1.574  -3.814  1    54.777  ? 703  PG4   B O5  1 2 
HETATM 10155 ZN ZN  . ZN    N 6  .   ? -2.551  15.85   23.526  1    19.804  ? 704  ZN    B ZN  1 2 
HETATM 10156 CL CL  . CL    O 7  .   ? -3.563  5.915   19.665  1    25.061  ? 705  CL    B CL  1 2 
HETATM 10157 O  O01 . A1IJX P 8  .   ? 1.607   16.647  19.869  1    37.621  ? 706  A1IJX B O01 1 ? 
HETATM 10158 C  C02 . A1IJX P 8  .   ? 0.727   17.403  20.115  1    40.573  ? 706  A1IJX B C02 1 ? 
HETATM 10159 C  C03 . A1IJX P 8  .   ? 0.784   18.072  21.535  1    48.172  ? 706  A1IJX B C03 1 ? 
HETATM 10160 N  N04 . A1IJX P 8  .   ? 1.648   17.314  22.494  1    43.24   ? 706  A1IJX B N04 1 ? 
HETATM 10161 C  C05 . A1IJX P 8  .   ? 1.251   15.91   22.811  1    33.979  ? 706  A1IJX B C05 1 ? 
HETATM 10162 C  C06 . A1IJX P 8  .   ? 2.076   15.391  24.032  1    34.719  ? 706  A1IJX B C06 1 ? 
HETATM 10163 C  C07 . A1IJX P 8  .   ? 3.495   14.812  23.497  1    36.669  ? 706  A1IJX B C07 1 ? 
HETATM 10164 C  C08 . A1IJX P 8  .   ? 3.12    13.33   23.102  1    36.238  ? 706  A1IJX B C08 1 ? 
HETATM 10165 C  C09 . A1IJX P 8  .   ? 2.105   12.942  24.021  1    37.621  ? 706  A1IJX B C09 1 ? 
HETATM 10166 N  N10 . A1IJX P 8  .   ? 1.602   14.34   24.757  1    43.73   ? 706  A1IJX B N10 1 ? 
HETATM 10167 C  C11 . A1IJX P 8  .   ? 0.853   14.393  26.096  1    49.076  ? 706  A1IJX B C11 1 ? 
HETATM 10168 C  C12 . A1IJX P 8  .   ? 0.388   13.051  26.785  1    48.578  ? 706  A1IJX B C12 1 ? 
HETATM 10169 N  N13 . A1IJX P 8  .   ? 0.345   13.218  28.213  1    50.032  ? 706  A1IJX B N13 1 ? 
HETATM 10170 C  C14 . A1IJX P 8  .   ? -1.069  12.793  26.343  1    43.747  ? 706  A1IJX B C14 1 ? 
HETATM 10171 C  C15 . A1IJX P 8  .   ? -1.524  11.33   26.499  1    48.501  ? 706  A1IJX B C15 1 ? 
HETATM 10172 C  C16 . A1IJX P 8  .   ? -2.031  11.081  27.931  1    50.995  ? 706  A1IJX B C16 1 ? 
HETATM 10173 O  O17 . A1IJX P 8  .   ? -2.507  9.969   28.239  1    52.811  ? 706  A1IJX B O17 1 ? 
HETATM 10174 O  O18 . A1IJX P 8  .   ? -1.968  11.987  28.801  1    62.347  ? 706  A1IJX B O18 1 ? 
HETATM 10175 O  O19 . A1IJX P 8  .   ? 0.517   15.476  26.603  1    43.673  ? 706  A1IJX B O19 1 ? 
HETATM 10176 C  C20 . A1IJX P 8  .   ? -0.165  15.966  23.273  1    30.188  ? 706  A1IJX B C20 1 ? 
HETATM 10177 O  O21 . A1IJX P 8  .   ? -0.563  16.743  24.218  1    28.429  ? 706  A1IJX B O21 1 ? 
HETATM 10178 O  O22 . A1IJX P 8  .   ? -0.865  15.187  22.633  1    26.294  ? 706  A1IJX B O22 1 ? 
HETATM 10179 C  C23 . A1IJX P 8  .   ? 1.354   19.473  21.452  1    39.868  ? 706  A1IJX B C23 1 ? 
HETATM 10180 N  N24 . A1IJX P 8  .   ? -0.372  17.661  19.1    1    40.19   ? 706  A1IJX B N24 1 ? 
HETATM 10181 C  C25 . A1IJX P 8  .   ? -1.658  18.671  19.308  1    37.735  ? 706  A1IJX B C25 1 ? 
HETATM 10182 C  C26 . A1IJX P 8  .   ? -2.598  18.262  18.342  1    34.831  ? 706  A1IJX B C26 1 ? 
HETATM 10183 C  C27 . A1IJX P 8  .   ? -1.745  17.803  17.097  1    28.444  ? 706  A1IJX B C27 1 ? 
HETATM 10184 C  C28 . A1IJX P 8  .   ? -0.473  17.13   17.795  1    29.472  ? 706  A1IJX B C28 1 ? 
HETATM 10185 C  C29 . A1IJX P 8  .   ? 0.82    17.462  17.109  1    23.542  ? 706  A1IJX B C29 1 ? 
HETATM 10186 O  O30 . A1IJX P 8  .   ? 1.478   16.689  16.291  1    22.069  ? 706  A1IJX B O30 1 ? 
HETATM 10187 O  O31 . A1IJX P 8  .   ? 1.298   18.547  17.379  1    24.686  ? 706  A1IJX B O31 1 ? 
HETATM 10188 O  O   . HOH   Q 12 .   ? 10.075  -17.015 -23.936 1    42.249  ? 801  HOH   A O   1 1 
HETATM 10189 O  O   . HOH   Q 12 .   ? -24.863 0.87    -19.776 1    44.837  ? 802  HOH   A O   1 1 
HETATM 10190 O  O   . HOH   Q 12 .   ? 11.956  -5.93   0.553   1    38.013  ? 803  HOH   A O   1 1 
HETATM 10191 O  O   . HOH   Q 12 .   ? 9.385   -14.357 -27.064 1    31.882  ? 804  HOH   A O   1 1 
HETATM 10192 O  O   . HOH   Q 12 .   ? 29.531  -25.889 -12.031 1    25.581  ? 805  HOH   A O   1 1 
HETATM 10193 O  O   . HOH   Q 12 .   ? 10.86   -5.23   -3.024  1    31.533  ? 806  HOH   A O   1 1 
HETATM 10194 O  O   . HOH   Q 12 .   ? -28.501 -29.203 -23.041 1    36.878  ? 807  HOH   A O   1 1 
HETATM 10195 O  O   . HOH   Q 12 .   ? -13.323 -4.751  -2.107  1    30.493  ? 808  HOH   A O   1 1 
HETATM 10196 O  O   . HOH   Q 12 .   ? -14.442 5.08    -11.468 1    38.098  ? 809  HOH   A O   1 1 
HETATM 10197 O  O   . HOH   Q 12 .   ? -1.625  -20.417 -0.669  1    41.126  ? 810  HOH   A O   1 1 
HETATM 10198 O  O   . HOH   Q 12 .   ? 17.57   -25.841 -17.288 1    24.006  ? 811  HOH   A O   1 1 
HETATM 10199 O  O   . HOH   Q 12 .   ? -11.44  -28.157 -37.859 1    44.752  ? 812  HOH   A O   1 1 
HETATM 10200 O  O   . HOH   Q 12 .   ? 6.024   -14.079 -22.861 1    33.535  ? 813  HOH   A O   1 1 
HETATM 10201 O  O   . HOH   Q 12 .   ? -14.967 -11.031 -18.856 1    35.091  ? 814  HOH   A O   1 1 
HETATM 10202 O  O   . HOH   Q 12 .   ? 3.248   -13.681 -31.26  1    30.621  ? 815  HOH   A O   1 1 
HETATM 10203 O  O   . HOH   Q 12 .   ? 37.126  -22.91  -17.832 1    38.003  ? 816  HOH   A O   1 1 
HETATM 10204 O  O   . HOH   Q 12 .   ? -28.493 -11.931 -14.774 1    42.65   ? 817  HOH   A O   1 1 
HETATM 10205 O  O   . HOH   Q 12 .   ? 9.781   13.116  -24.139 1    39.759  ? 818  HOH   A O   1 1 
HETATM 10206 O  O   . HOH   Q 12 .   ? -4.435  1.556   1.563   1    42.124  ? 819  HOH   A O   1 1 
HETATM 10207 O  O   . HOH   Q 12 .   ? 13.735  -10.909 1.703   1    36.507  ? 820  HOH   A O   1 1 
HETATM 10208 O  O   . HOH   Q 12 .   ? -3.044  -0.726  -6.761  1    19.517  ? 821  HOH   A O   1 1 
HETATM 10209 O  O   . HOH   Q 12 .   ? 0.792   -10.358 -10.086 1    19.582  ? 822  HOH   A O   1 1 
HETATM 10210 O  O   . HOH   Q 12 .   ? 16.502  -16.703 -0.028  1    34.474  ? 823  HOH   A O   1 1 
HETATM 10211 O  O   . HOH   Q 12 .   ? 6.228   -42.308 -14.235 1    29.038  ? 824  HOH   A O   1 1 
HETATM 10212 O  O   . HOH   Q 12 .   ? -3.778  4.446   -3.664  1    26.593  ? 825  HOH   A O   1 1 
HETATM 10213 O  O   . HOH   Q 12 .   ? -5.263  -6.714  -27.85  1    21.722  ? 826  HOH   A O   1 1 
HETATM 10214 O  O   . HOH   Q 12 .   ? -22.908 1.551   -16.797 1    34.934  ? 827  HOH   A O   1 1 
HETATM 10215 O  O   . HOH   Q 12 .   ? -18.128 -10.698 -22.759 1    35.375  ? 828  HOH   A O   1 1 
HETATM 10216 O  O   . HOH   Q 12 .   ? -10.205 6.525   -25.301 1    30.228  ? 829  HOH   A O   1 1 
HETATM 10217 O  O   . HOH   Q 12 .   ? -22.191 -21.175 -18.121 1    30.239  ? 830  HOH   A O   1 1 
HETATM 10218 O  O   . HOH   Q 12 .   ? 13.324  -38.238 -32.215 1    31.281  ? 831  HOH   A O   1 1 
HETATM 10219 O  O   . HOH   Q 12 .   ? -3.746  -13.424 -28.258 1    26.66   ? 832  HOH   A O   1 1 
HETATM 10220 O  O   . HOH   Q 12 .   ? 7.367   -32.908 -34.845 1    22.659  ? 833  HOH   A O   1 1 
HETATM 10221 O  O   . HOH   Q 12 .   ? -26.183 -12.671 -29.125 1    35.277  ? 834  HOH   A O   1 1 
HETATM 10222 O  O   . HOH   Q 12 .   ? 0.997   -10.942 -1.497  1    26.38   ? 835  HOH   A O   1 1 
HETATM 10223 O  O   . HOH   Q 12 .   ? 31.355  -18.327 -7.151  1    35.634  ? 836  HOH   A O   1 1 
HETATM 10224 O  O   . HOH   Q 12 .   ? 9.095   -21.747 -0      1    24.896  ? 837  HOH   A O   1 1 
HETATM 10225 O  O   . HOH   Q 12 .   ? 7.716   -18.273 -19.914 1    31.591  ? 838  HOH   A O   1 1 
HETATM 10226 O  O   . HOH   Q 12 .   ? 27.409  -17.536 -23.554 1    25.288  ? 839  HOH   A O   1 1 
HETATM 10227 O  O   . HOH   Q 12 .   ? -11.074 2.36    -11.188 1    17.316  ? 840  HOH   A O   1 1 
HETATM 10228 O  O   . HOH   Q 12 .   ? 6.365   -12.264 -31.696 1    31.684  ? 841  HOH   A O   1 1 
HETATM 10229 O  O   . HOH   Q 12 .   ? -3.407  6.919   -14.854 1    31.76   ? 842  HOH   A O   1 1 
HETATM 10230 O  O   . HOH   Q 12 .   ? 38.841  -20.503 -13.43  1    43.675  ? 843  HOH   A O   1 1 
HETATM 10231 O  O   . HOH   Q 12 .   ? 25.216  -25.787 -17.682 1    27.556  ? 844  HOH   A O   1 1 
HETATM 10232 O  O   . HOH   Q 12 .   ? -1.76   10.266  -8.671  1    28.874  ? 845  HOH   A O   1 1 
HETATM 10233 O  O   . HOH   Q 12 .   ? -12.42  -12.161 -27.616 1    32.049  ? 846  HOH   A O   1 1 
HETATM 10234 O  O   . HOH   Q 12 .   ? 15.317  -34.009 -8.943  1    24.057  ? 847  HOH   A O   1 1 
HETATM 10235 O  O   . HOH   Q 12 .   ? 24.292  -33.792 -15.894 1    41.298  ? 848  HOH   A O   1 1 
HETATM 10236 O  O   . HOH   Q 12 .   ? -8.139  -26.368 -3.584  1    36.276  ? 849  HOH   A O   1 1 
HETATM 10237 O  O   . HOH   Q 12 .   ? 16.245  -0.166  -2.536  1    25.93   ? 850  HOH   A O   1 1 
HETATM 10238 O  O   . HOH   Q 12 .   ? -19.011 -1      -9.458  1    21.747  ? 851  HOH   A O   1 1 
HETATM 10239 O  O   . HOH   Q 12 .   ? -10.421 -6.858  -23.526 1    18.016  ? 852  HOH   A O   1 1 
HETATM 10240 O  O   . HOH   Q 12 .   ? -19.148 -28.816 -17.34  1    34.461  ? 853  HOH   A O   1 1 
HETATM 10241 O  O   . HOH   Q 12 .   ? -3.028  -35.277 -31.479 1    42.018  ? 854  HOH   A O   1 1 
HETATM 10242 O  O   . HOH   Q 12 .   ? -21.811 -4.814  -26.932 1    27.602  ? 855  HOH   A O   1 1 
HETATM 10243 O  O   . HOH   Q 12 .   ? -9.001  -7.083  -5.151  1    18.118  ? 856  HOH   A O   1 1 
HETATM 10244 O  O   . HOH   Q 12 .   ? 12.33   -6.859  -5.353  1    17.455  ? 857  HOH   A O   1 1 
HETATM 10245 O  O   . HOH   Q 12 .   ? 20.332  -1.855  -23.144 1    25.641  ? 858  HOH   A O   1 1 
HETATM 10246 O  O   . HOH   Q 12 .   ? -6.189  -12.295 -27.852 1    35.785  ? 859  HOH   A O   1 1 
HETATM 10247 O  O   . HOH   Q 12 .   ? 18.68   -3.019  -25.234 1    26.765  ? 860  HOH   A O   1 1 
HETATM 10248 O  O   . HOH   Q 12 .   ? 26      0.048   -6.61   1    27.363  ? 861  HOH   A O   1 1 
HETATM 10249 O  O   . HOH   Q 12 .   ? 12.263  -30.22  -18.007 1    20.926  ? 862  HOH   A O   1 1 
HETATM 10250 O  O   . HOH   Q 12 .   ? -14.219 -19.379 -7.434  1    40.186  ? 863  HOH   A O   1 1 
HETATM 10251 O  O   . HOH   Q 12 .   ? 13.83   -41.691 -18.087 1    32.154  ? 864  HOH   A O   1 1 
HETATM 10252 O  O   . HOH   Q 12 .   ? 4.937   -10.366 -23.161 1    26.047  ? 865  HOH   A O   1 1 
HETATM 10253 O  O   . HOH   Q 12 .   ? 1.071   -2.547  -32.468 1    32.622  ? 866  HOH   A O   1 1 
HETATM 10254 O  O   . HOH   Q 12 .   ? -11.74  4.362   -4.504  1    33.128  ? 867  HOH   A O   1 1 
HETATM 10255 O  O   . HOH   Q 12 .   ? 28.938  -20.611 -22.118 1    25.77   ? 868  HOH   A O   1 1 
HETATM 10256 O  O   . HOH   Q 12 .   ? 12.396  -3.002  -35.443 1    37.643  ? 869  HOH   A O   1 1 
HETATM 10257 O  O   . HOH   Q 12 .   ? -30.877 -16.093 -20.074 1    35.781  ? 870  HOH   A O   1 1 
HETATM 10258 O  O   . HOH   Q 12 .   ? 2.982   -4.072  -2.205  1    37.321  ? 871  HOH   A O   1 1 
HETATM 10259 O  O   . HOH   Q 12 .   ? -23.504 -20.231 -15.783 1    34.011  ? 872  HOH   A O   1 1 
HETATM 10260 O  O   . HOH   Q 12 .   ? -10.348 1.724   -8.495  1    14.721  ? 873  HOH   A O   1 1 
HETATM 10261 O  O   . HOH   Q 12 .   ? -10.304 -7.394  -2.29   1    23.769  ? 874  HOH   A O   1 1 
HETATM 10262 O  O   . HOH   Q 12 .   ? -18.355 -12.951 -16.699 1    45.078  ? 875  HOH   A O   1 1 
HETATM 10263 O  O   . HOH   Q 12 .   ? 11.382  11.805  -1.529  1    22.566  ? 876  HOH   A O   1 1 
HETATM 10264 O  O   . HOH   Q 12 .   ? 21.937  -39.144 -14.211 1    30.41   ? 877  HOH   A O   1 1 
HETATM 10265 O  O   . HOH   Q 12 .   ? 0.234   -16.015 -41.277 1    35.492  ? 878  HOH   A O   1 1 
HETATM 10266 O  O   . HOH   Q 12 .   ? 15.02   -9.232  -22.601 1    23.678  ? 879  HOH   A O   1 1 
HETATM 10267 O  O   . HOH   Q 12 .   ? -7.319  -31.315 -10.788 1    25.284  ? 880  HOH   A O   1 1 
HETATM 10268 O  O   . HOH   Q 12 .   ? 19.633  -19.893 -5.079  1    16.758  ? 881  HOH   A O   1 1 
HETATM 10269 O  O   . HOH   Q 12 .   ? -2.791  -5.403  -35.488 1    37.662  ? 882  HOH   A O   1 1 
HETATM 10270 O  O   . HOH   Q 12 .   ? 12.397  -42.767 -25.105 1    27.365  ? 883  HOH   A O   1 1 
HETATM 10271 O  O   . HOH   Q 12 .   ? 5.839   11.371  -22.943 1    36.647  ? 884  HOH   A O   1 1 
HETATM 10272 O  O   . HOH   Q 12 .   ? 3.545   -9.801  -29.53  1    40.924  ? 885  HOH   A O   1 1 
HETATM 10273 O  O   . HOH   Q 12 .   ? -14.068 -8.967  -15.299 1    25.328  ? 886  HOH   A O   1 1 
HETATM 10274 O  O   . HOH   Q 12 .   ? -9.738  -29.595 -24.127 1    19.818  ? 887  HOH   A O   1 1 
HETATM 10275 O  O   . HOH   Q 12 .   ? -9.666  8.827   -17.94  1    32.144  ? 888  HOH   A O   1 1 
HETATM 10276 O  O   . HOH   Q 12 .   ? 2.904   -39.921 -28.532 1    38.003  ? 889  HOH   A O   1 1 
HETATM 10277 O  O   . HOH   Q 12 .   ? 0.407   -20.343 -39.862 1    34.17   ? 890  HOH   A O   1 1 
HETATM 10278 O  O   . HOH   Q 12 .   ? -1.277  -7.88   -29.381 1    33.092  ? 891  HOH   A O   1 1 
HETATM 10279 O  O   . HOH   Q 12 .   ? 4.601   -19.437 0.994   1    26.005  ? 892  HOH   A O   1 1 
HETATM 10280 O  O   . HOH   Q 12 .   ? 15.867  9.532   -20.345 1    28.656  ? 893  HOH   A O   1 1 
HETATM 10281 O  O   . HOH   Q 12 .   ? -21.279 -18.51  -15.844 1    49.137  ? 894  HOH   A O   1 1 
HETATM 10282 O  O   . HOH   Q 12 .   ? 12.125  -1.472  -2.738  1    19.783  ? 895  HOH   A O   1 1 
HETATM 10283 O  O   . HOH   Q 12 .   ? -30.133 -37.591 -5.587  1    45.49   ? 896  HOH   A O   1 1 
HETATM 10284 O  O   . HOH   Q 12 .   ? 9.625   -37.464 -8.83   1    31.266  ? 897  HOH   A O   1 1 
HETATM 10285 O  O   . HOH   Q 12 .   ? -0.929  -33.73  -37.091 1    40.39   ? 898  HOH   A O   1 1 
HETATM 10286 O  O   . HOH   Q 12 .   ? -21.047 -30.834 -17.389 1    26.788  ? 899  HOH   A O   1 1 
HETATM 10287 O  O   . HOH   Q 12 .   ? 7.869   -9.82   -23.186 1    35.85   ? 900  HOH   A O   1 1 
HETATM 10288 O  O   . HOH   Q 12 .   ? 4.003   -1.155  0.143   1    33.369  ? 901  HOH   A O   1 1 
HETATM 10289 O  O   . HOH   Q 12 .   ? 10.004  -15.565 3.491   1    43.467  ? 902  HOH   A O   1 1 
HETATM 10290 O  O   . HOH   Q 12 .   ? 13.595  -2.605  -20.563 1    18.112  ? 903  HOH   A O   1 1 
HETATM 10291 O  O   . HOH   Q 12 .   ? 9.515   -5.986  -25.751 1    25.014  ? 904  HOH   A O   1 1 
HETATM 10292 O  O   . HOH   Q 12 .   ? 22.653  -15.398 -31.038 1    35.666  ? 905  HOH   A O   1 1 
HETATM 10293 O  O   . HOH   Q 12 .   ? -31.656 -15.817 -9.928  1    62.111  ? 906  HOH   A O   1 1 
HETATM 10294 O  O   . HOH   Q 12 .   ? -7.256  -16.015 -0.223  1    43.601  ? 907  HOH   A O   1 1 
HETATM 10295 O  O   . HOH   Q 12 .   ? 6.145   -4.901  1.331   1    37.493  ? 908  HOH   A O   1 1 
HETATM 10296 O  O   . HOH   Q 12 .   ? -4.437  -30.434 -13.597 1    20.663  ? 909  HOH   A O   1 1 
HETATM 10297 O  O   . HOH   Q 12 .   ? 12.797  6.674   -9.439  1    24.494  ? 910  HOH   A O   1 1 
HETATM 10298 O  O   . HOH   Q 12 .   ? -7.287  -6.054  -16.4   1    12.151  ? 911  HOH   A O   1 1 
HETATM 10299 O  O   . HOH   Q 12 .   ? 12.772  -31.929 -30.549 1    30.625  ? 912  HOH   A O   1 1 
HETATM 10300 O  O   . HOH   Q 12 .   ? -9.223  -3.352  -12.694 1    25.366  ? 913  HOH   A O   1 1 
HETATM 10301 O  O   . HOH   Q 12 .   ? -18.983 -17.812 -33.997 1    32.286  ? 914  HOH   A O   1 1 
HETATM 10302 O  O   . HOH   Q 12 .   ? 31.161  1.172   -13.991 1    38.853  ? 915  HOH   A O   1 1 
HETATM 10303 O  O   . HOH   Q 12 .   ? -15.766 -12.364 -35.064 1    25.658  ? 916  HOH   A O   1 1 
HETATM 10304 O  O   . HOH   Q 12 .   ? -6.809  -3.818  -1.888  1    29.624  ? 917  HOH   A O   1 1 
HETATM 10305 O  O   . HOH   Q 12 .   ? 9.423   -1.051  -19.095 1    19.339  ? 918  HOH   A O   1 1 
HETATM 10306 O  O   . HOH   Q 12 .   ? 32.749  -15.003 -7.354  1    44.573  ? 919  HOH   A O   1 1 
HETATM 10307 O  O   . HOH   Q 12 .   ? 30.768  3.857   -17.412 1    43.849  ? 920  HOH   A O   1 1 
HETATM 10308 O  O   . HOH   Q 12 .   ? 15.681  -17.641 -40.266 1    40.759  ? 921  HOH   A O   1 1 
HETATM 10309 O  O   . HOH   Q 12 .   ? 9.39    -37.988 -30.446 1    33.725  ? 922  HOH   A O   1 1 
HETATM 10310 O  O   . HOH   Q 12 .   ? 8.905   -18.074 -40.001 1    31.281  ? 923  HOH   A O   1 1 
HETATM 10311 O  O   . HOH   Q 12 .   ? 13.985  -30.337 -28.899 1    27.126  ? 924  HOH   A O   1 1 
HETATM 10312 O  O   . HOH   Q 12 .   ? -23.301 -15.669 -32.117 1    54.497  ? 925  HOH   A O   1 1 
HETATM 10313 O  O   . HOH   Q 12 .   ? 20.353  3.38    -12.571 1    19.406  ? 926  HOH   A O   1 1 
HETATM 10314 O  O   . HOH   Q 12 .   ? 3.048   7.58    -29.193 1    29.627  ? 927  HOH   A O   1 1 
HETATM 10315 O  O   . HOH   Q 12 .   ? 29.318  -20.392 -7.459  1    24.069  ? 928  HOH   A O   1 1 
HETATM 10316 O  O   . HOH   Q 12 .   ? -32.158 -29.238 -20.088 1    37.362  ? 929  HOH   A O   1 1 
HETATM 10317 O  O   . HOH   Q 12 .   ? -8.085  -32.888 -33.265 1    35.265  ? 930  HOH   A O   1 1 
HETATM 10318 O  O   . HOH   Q 12 .   ? -8.409  -27.918 -9.452  1    35.958  ? 931  HOH   A O   1 1 
HETATM 10319 O  O   . HOH   Q 12 .   ? -27.994 -28.284 -27.524 1    43.616  ? 932  HOH   A O   1 1 
HETATM 10320 O  O   . HOH   Q 12 .   ? 24.939  -1.81   -9.184  1    21.348  ? 933  HOH   A O   1 1 
HETATM 10321 O  O   . HOH   Q 12 .   ? 16.355  -14.766 -27.975 1    32.167  ? 934  HOH   A O   1 1 
HETATM 10322 O  O   . HOH   Q 12 .   ? 21.291  -29.709 -8.22   1    31.712  ? 935  HOH   A O   1 1 
HETATM 10323 O  O   . HOH   Q 12 .   ? 11.317  -22.429 -19.215 1    32.552  ? 936  HOH   A O   1 1 
HETATM 10324 O  O   . HOH   Q 12 .   ? 17.794  11.46   -34.645 1    37.703  ? 937  HOH   A O   1 1 
HETATM 10325 O  O   . HOH   Q 12 .   ? 10.898  -41.428 -26.78  1    25.864  ? 938  HOH   A O   1 1 
HETATM 10326 O  O   . HOH   Q 12 .   ? 28.2    -6.636  -14.164 1    36.339  ? 939  HOH   A O   1 1 
HETATM 10327 O  O   . HOH   Q 12 .   ? -16.007 -24.517 -9.307  1    35.846  ? 940  HOH   A O   1 1 
HETATM 10328 O  O   . HOH   Q 12 .   ? 12.506  -38.715 -29.441 1    39.224  ? 941  HOH   A O   1 1 
HETATM 10329 O  O   . HOH   Q 12 .   ? 36.549  -25.591 -24.32  1    38.79   ? 942  HOH   A O   1 1 
HETATM 10330 O  O   . HOH   Q 12 .   ? -7.813  -18.359 -2.75   1    26.332  ? 943  HOH   A O   1 1 
HETATM 10331 O  O   . HOH   Q 12 .   ? -3.469  -19.98  -16.84  1    17.594  ? 944  HOH   A O   1 1 
HETATM 10332 O  O   . HOH   Q 12 .   ? -3.249  4.7     -29.998 1    29.225  ? 945  HOH   A O   1 1 
HETATM 10333 O  O   . HOH   Q 12 .   ? -16.688 -14.122 -28.29  1    38.749  ? 946  HOH   A O   1 1 
HETATM 10334 O  O   . HOH   Q 12 .   ? 2.397   12.263  -23.162 1    36.392  ? 947  HOH   A O   1 1 
HETATM 10335 O  O   . HOH   Q 12 .   ? -13.627 2.521   -11.806 1    16.238  ? 948  HOH   A O   1 1 
HETATM 10336 O  O   . HOH   Q 12 .   ? -5.937  -20.593 -17.281 1    25.435  ? 949  HOH   A O   1 1 
HETATM 10337 O  O   . HOH   Q 12 .   ? 17.824  -28.455 -16.412 1    24.447  ? 950  HOH   A O   1 1 
HETATM 10338 O  O   . HOH   Q 12 .   ? 9.863   -30.759 -6.398  1    22.766  ? 951  HOH   A O   1 1 
HETATM 10339 O  O   . HOH   Q 12 .   ? 36.222  -12.774 -8.629  1    51.174  ? 952  HOH   A O   1 1 
HETATM 10340 O  O   . HOH   Q 12 .   ? -11.051 -14.379 -2.482  1    21.846  ? 953  HOH   A O   1 1 
HETATM 10341 O  O   . HOH   Q 12 .   ? 4.943   -41.887 -21.198 1    34.62   ? 954  HOH   A O   1 1 
HETATM 10342 O  O   . HOH   Q 12 .   ? 21.139  -13.573 -7.452  1    18.495  ? 955  HOH   A O   1 1 
HETATM 10343 O  O   . HOH   Q 12 .   ? -9.358  -25.263 -21.931 1    19.655  ? 956  HOH   A O   1 1 
HETATM 10344 O  O   . HOH   Q 12 .   ? 2.389   -23.967 -20.799 1    16.744  ? 957  HOH   A O   1 1 
HETATM 10345 O  O   . HOH   Q 12 .   ? 26.186  -9.041  -2.69   1    24.738  ? 958  HOH   A O   1 1 
HETATM 10346 O  O   . HOH   Q 12 .   ? 8.821   -15.771 -38.82  1    35.097  ? 959  HOH   A O   1 1 
HETATM 10347 O  O   . HOH   Q 12 .   ? -5.482  -12.185 -9.695  1    18.07   ? 960  HOH   A O   1 1 
HETATM 10348 O  O   . HOH   Q 12 .   ? 10.511  -17.603 -19.268 1    31.407  ? 961  HOH   A O   1 1 
HETATM 10349 O  O   . HOH   Q 12 .   ? -29.149 -19.101 -28.916 1    42.26   ? 962  HOH   A O   1 1 
HETATM 10350 O  O   . HOH   Q 12 .   ? 4.094   14.005  -12.772 1    22.698  ? 963  HOH   A O   1 1 
HETATM 10351 O  O   . HOH   Q 12 .   ? 28.774  -6.131  -9.558  1    25.277  ? 964  HOH   A O   1 1 
HETATM 10352 O  O   . HOH   Q 12 .   ? -2.926  -16.714 -19.105 1    21.294  ? 965  HOH   A O   1 1 
HETATM 10353 O  O   . HOH   Q 12 .   ? -0.949  -25.438 0.11    1    45.216  ? 966  HOH   A O   1 1 
HETATM 10354 O  O   . HOH   Q 12 .   ? -1.57   8.553   -27.292 1    28.197  ? 967  HOH   A O   1 1 
HETATM 10355 O  O   . HOH   Q 12 .   ? -5.546  9.289   -20.266 1    26.468  ? 968  HOH   A O   1 1 
HETATM 10356 O  O   . HOH   Q 12 .   ? 4.833   -19.419 -17.209 1    22.274  ? 969  HOH   A O   1 1 
HETATM 10357 O  O   . HOH   Q 12 .   ? 20.236  -4.105  -6.468  1    19.88   ? 970  HOH   A O   1 1 
HETATM 10358 O  O   . HOH   Q 12 .   ? 27.351  -23.064 -20.85  1    45.895  ? 971  HOH   A O   1 1 
HETATM 10359 O  O   . HOH   Q 12 .   ? 16.286  -2.463  -23.985 1    19.503  ? 972  HOH   A O   1 1 
HETATM 10360 O  O   . HOH   Q 12 .   ? 19.7    -27.542 -36.083 1    29.795  ? 973  HOH   A O   1 1 
HETATM 10361 O  O   . HOH   Q 12 .   ? 0.6     5.856   -20.81  1    18.259  ? 974  HOH   A O   1 1 
HETATM 10362 O  O   . HOH   Q 12 .   ? -7.948  -21.423 -24.607 1    36.736  ? 975  HOH   A O   1 1 
HETATM 10363 O  O   . HOH   Q 12 .   ? -14.365 -2.248  -4.838  1    30.725  ? 976  HOH   A O   1 1 
HETATM 10364 O  O   . HOH   Q 12 .   ? 26.324  6.34    -10.549 1    36.191  ? 977  HOH   A O   1 1 
HETATM 10365 O  O   . HOH   Q 12 .   ? 7.128   -21.137 -41.158 1    29.737  ? 978  HOH   A O   1 1 
HETATM 10366 O  O   . HOH   Q 12 .   ? 28.221  -25.349 -21.901 1    32.672  ? 979  HOH   A O   1 1 
HETATM 10367 O  O   . HOH   Q 12 .   ? -14.37  -23.603 -15.046 1    54.816  ? 980  HOH   A O   1 1 
HETATM 10368 O  O   . HOH   Q 12 .   ? 6.215   -10.853 -35.462 1    39.228  ? 981  HOH   A O   1 1 
HETATM 10369 O  O   . HOH   Q 12 .   ? 1.923   -7.8    -26.188 1    22.443  ? 982  HOH   A O   1 1 
HETATM 10370 O  O   . HOH   Q 12 .   ? -8.231  -26.07  -35.22  1    29.237  ? 983  HOH   A O   1 1 
HETATM 10371 O  O   . HOH   Q 12 .   ? 34.432  -28.231 -20.394 1    37.043  ? 984  HOH   A O   1 1 
HETATM 10372 O  O   . HOH   Q 12 .   ? 10.26   5.552   -10.411 1    27.757  ? 985  HOH   A O   1 1 
HETATM 10373 O  O   . HOH   Q 12 .   ? -6.674  -22.925 -15.937 1    22.838  ? 986  HOH   A O   1 1 
HETATM 10374 O  O   . HOH   Q 12 .   ? -4.515  12.636  -9.94   1    28.656  ? 987  HOH   A O   1 1 
HETATM 10375 O  O   . HOH   Q 12 .   ? 35.628  -15.596 -20.797 1    36.57   ? 988  HOH   A O   1 1 
HETATM 10376 O  O   . HOH   Q 12 .   ? 5.684   -13.577 -37.789 1    27.477  ? 989  HOH   A O   1 1 
HETATM 10377 O  O   . HOH   Q 12 .   ? 6.803   -16.285 -23.453 1    30.613  ? 990  HOH   A O   1 1 
HETATM 10378 O  O   . HOH   Q 12 .   ? 12.044  -29     -28.502 1    19.703  ? 991  HOH   A O   1 1 
HETATM 10379 O  O   . HOH   Q 12 .   ? 22.61   -13.629 -5.033  1    21.845  ? 992  HOH   A O   1 1 
HETATM 10380 O  O   . HOH   Q 12 .   ? 12.568  -6.884  -13.337 1    19.085  ? 993  HOH   A O   1 1 
HETATM 10381 O  O   . HOH   Q 12 .   ? -9.108  4.78    -2.09   1    30.192  ? 994  HOH   A O   1 1 
HETATM 10382 O  O   . HOH   Q 12 .   ? -0.956  2.977   -14.877 1    15.465  ? 995  HOH   A O   1 1 
HETATM 10383 O  O   . HOH   Q 12 .   ? 10.159  6.877   -6.983  1    30.241  ? 996  HOH   A O   1 1 
HETATM 10384 O  O   . HOH   Q 12 .   ? -16.52  -8.493  -26.116 1    29.809  ? 997  HOH   A O   1 1 
HETATM 10385 O  O   . HOH   Q 12 .   ? -23.649 -5.215  -7.772  1    31.299  ? 998  HOH   A O   1 1 
HETATM 10386 O  O   . HOH   Q 12 .   ? -12.27  -4.644  -31.832 1    41.304  ? 999  HOH   A O   1 1 
HETATM 10387 O  O   . HOH   Q 12 .   ? 10.556  -23.547 -6.782  1    15.774  ? 1000 HOH   A O   1 1 
HETATM 10388 O  O   . HOH   Q 12 .   ? -0.137  -3.305  -34.553 1    40.019  ? 1001 HOH   A O   1 1 
HETATM 10389 O  O   . HOH   Q 12 .   ? 17.528  -36.614 -22.094 1    32.281  ? 1002 HOH   A O   1 1 
HETATM 10390 O  O   . HOH   Q 12 .   ? 23.226  -24.099 -9.092  1    17.953  ? 1003 HOH   A O   1 1 
HETATM 10391 O  O   . HOH   Q 12 .   ? 13.579  16.472  -5.965  1    45.534  ? 1004 HOH   A O   1 1 
HETATM 10392 O  O   . HOH   Q 12 .   ? -12.723 0.245   -7.692  1    40.68   ? 1005 HOH   A O   1 1 
HETATM 10393 O  O   . HOH   Q 12 .   ? 3.887   -0.909  -18.923 1    25.177  ? 1006 HOH   A O   1 1 
HETATM 10394 O  O   . HOH   Q 12 .   ? -14.162 6.811   -17.677 1    33.783  ? 1007 HOH   A O   1 1 
HETATM 10395 O  O   . HOH   Q 12 .   ? 5.26    -14.022 -29.568 1    31.02   ? 1008 HOH   A O   1 1 
HETATM 10396 O  O   . HOH   Q 12 .   ? 5.217   0.725   -17.475 1    18.985  ? 1009 HOH   A O   1 1 
HETATM 10397 O  O   . HOH   Q 12 .   ? 15.051  -19.385 1.696   1    39.848  ? 1010 HOH   A O   1 1 
HETATM 10398 O  O   . HOH   Q 12 .   ? -12.013 -29.154 -25.703 1    25.152  ? 1011 HOH   A O   1 1 
HETATM 10399 O  O   . HOH   Q 12 .   ? 16.895  -35.109 -31.299 1    44.948  ? 1012 HOH   A O   1 1 
HETATM 10400 O  O   . HOH   Q 12 .   ? 8.438   8.613   -28.534 1    32.836  ? 1013 HOH   A O   1 1 
HETATM 10401 O  O   . HOH   Q 12 .   ? 20.413  -16.152 -8.509  1    20.571  ? 1014 HOH   A O   1 1 
HETATM 10402 O  O   . HOH   Q 12 .   ? 23.664  9.414   -12.116 1    39.413  ? 1015 HOH   A O   1 1 
HETATM 10403 O  O   . HOH   Q 12 .   ? 7.459   -10.096 0.256   1    36.595  ? 1016 HOH   A O   1 1 
HETATM 10404 O  O   . HOH   Q 12 .   ? 6.263   -24.431 1.06    1    38.591  ? 1017 HOH   A O   1 1 
HETATM 10405 O  O   . HOH   Q 12 .   ? -3.318  -23.884 -0.087  1    30.006  ? 1018 HOH   A O   1 1 
HETATM 10406 O  O   . HOH   Q 12 .   ? 4.817   9.808   -27.71  1    36.678  ? 1019 HOH   A O   1 1 
HETATM 10407 O  O   . HOH   Q 12 .   ? 34.566  -16.191 -11.015 1    36.237  ? 1020 HOH   A O   1 1 
HETATM 10408 O  O   . HOH   Q 12 .   ? 20.846  -34.422 -18.77  1    42.55   ? 1021 HOH   A O   1 1 
HETATM 10409 O  O   . HOH   Q 12 .   ? -11.451 -28.207 -28.658 1    26.166  ? 1022 HOH   A O   1 1 
HETATM 10410 O  O   . HOH   Q 12 .   ? 11.964  -6.96   -26.805 1    25.013  ? 1023 HOH   A O   1 1 
HETATM 10411 O  O   . HOH   Q 12 .   ? 2.615   -7.615  -23.191 1    30.777  ? 1024 HOH   A O   1 1 
HETATM 10412 O  O   . HOH   Q 12 .   ? -12.907 -11.312 -14.957 1    23.714  ? 1025 HOH   A O   1 1 
HETATM 10413 O  O   . HOH   Q 12 .   ? 15.276  -20.494 -44.376 1    42.36   ? 1026 HOH   A O   1 1 
HETATM 10414 O  O   . HOH   Q 12 .   ? -13.517 0.071   -30.424 1    43.583  ? 1027 HOH   A O   1 1 
HETATM 10415 O  O   . HOH   Q 12 .   ? 7.691   5.313   -7.871  1    24.891  ? 1028 HOH   A O   1 1 
HETATM 10416 O  O   . HOH   Q 12 .   ? 22.783  -26.939 -18.275 1    29.077  ? 1029 HOH   A O   1 1 
HETATM 10417 O  O   . HOH   Q 12 .   ? 12.895  -16.97  -23.078 1    36.67   ? 1030 HOH   A O   1 1 
HETATM 10418 O  O   . HOH   Q 12 .   ? -4.603  2.352   -30.644 1    30.29   ? 1031 HOH   A O   1 1 
HETATM 10419 O  O   . HOH   Q 12 .   ? -21.003 1.493   -14.591 1    37.711  ? 1032 HOH   A O   1 1 
HETATM 10420 O  O   . HOH   Q 12 .   ? 21.349  -27.056 -9.615  1    30.986  ? 1033 HOH   A O   1 1 
HETATM 10421 O  O   . HOH   Q 12 .   ? 0.044   -4.367  -30.291 1    30.412  ? 1034 HOH   A O   1 1 
HETATM 10422 O  O   . HOH   Q 12 .   ? -18.902 1.801   -15.8   1    25.452  ? 1035 HOH   A O   1 1 
HETATM 10423 O  O   . HOH   Q 12 .   ? -1.03   -6.502  -32.182 1    38.919  ? 1036 HOH   A O   1 1 
HETATM 10424 O  O   . HOH   Q 12 .   ? -8.247  -26.431 -6.657  1    25.603  ? 1037 HOH   A O   1 1 
HETATM 10425 O  O   . HOH   Q 12 .   ? 22.555  -10.532 -0.61   1    38.818  ? 1038 HOH   A O   1 1 
HETATM 10426 O  O   . HOH   Q 12 .   ? 5.09    6.609   -7.814  1    23.073  ? 1039 HOH   A O   1 1 
HETATM 10427 O  O   . HOH   Q 12 .   ? 1.913   -5.782  -33.042 1    40.531  ? 1040 HOH   A O   1 1 
HETATM 10428 O  O   . HOH   Q 12 .   ? 12.556  -13.539 -37.447 1    38.147  ? 1041 HOH   A O   1 1 
HETATM 10429 O  O   . HOH   Q 12 .   ? -1.487  4.593   -32.193 1    31.614  ? 1042 HOH   A O   1 1 
HETATM 10430 O  O   . HOH   Q 12 .   ? 27.367  -23.721 -32.621 1    35.999  ? 1043 HOH   A O   1 1 
HETATM 10431 O  O   . HOH   Q 12 .   ? 3.47    -21.67  -0.04   1    29.323  ? 1044 HOH   A O   1 1 
HETATM 10432 O  O   . HOH   Q 12 .   ? -11.704 -13.481 -39.861 1    31.332  ? 1045 HOH   A O   1 1 
HETATM 10433 O  O   . HOH   Q 12 .   ? 3.756   -12.656 -27.698 1    27.209  ? 1046 HOH   A O   1 1 
HETATM 10434 O  O   . HOH   Q 12 .   ? 21.448  7.318   -28.017 1    36.692  ? 1047 HOH   A O   1 1 
HETATM 10435 O  O   . HOH   Q 12 .   ? 28.362  -25.74  -24.254 1    42.593  ? 1048 HOH   A O   1 1 
HETATM 10436 O  O   . HOH   Q 12 .   ? 8.464   7.366   -11.196 1    26.917  ? 1049 HOH   A O   1 1 
HETATM 10437 O  O   . HOH   Q 12 .   ? 11.05   13.817  -19.096 1    41.669  ? 1050 HOH   A O   1 1 
HETATM 10438 O  O   . HOH   Q 12 .   ? 7.31    -7.735  -26.984 1    34.631  ? 1051 HOH   A O   1 1 
HETATM 10439 O  O   . HOH   Q 12 .   ? 24.808  -28.879 -32.348 1    39.338  ? 1052 HOH   A O   1 1 
HETATM 10440 O  O   . HOH   Q 12 .   ? -10.194 9.085   -9.019  1    19.57   ? 1053 HOH   A O   1 1 
HETATM 10441 O  O   . HOH   Q 12 .   ? 6.669   -35.497 -33.406 1    28.355  ? 1054 HOH   A O   1 1 
HETATM 10442 O  O   . HOH   Q 12 .   ? -13.085 -26.777 -11.246 1    44.849  ? 1055 HOH   A O   1 1 
HETATM 10443 O  O   . HOH   Q 12 .   ? -3.214  -5.092  -3.633  1    28.414  ? 1056 HOH   A O   1 1 
HETATM 10444 O  O   . HOH   Q 12 .   ? -22.636 -7.205  -26.621 1    25.168  ? 1057 HOH   A O   1 1 
HETATM 10445 O  O   . HOH   Q 12 .   ? -5.864  -14.847 -9.646  1    19.369  ? 1058 HOH   A O   1 1 
HETATM 10446 O  O   . HOH   Q 12 .   ? 12.255  -43.571 -21.622 1    41.71   ? 1059 HOH   A O   1 1 
HETATM 10447 O  O   . HOH   Q 12 .   ? -31.012 -3.37   -19.661 1    27.632  ? 1060 HOH   A O   1 1 
HETATM 10448 O  O   . HOH   Q 12 .   ? -10.012 -12.343 -1.165  1    36.936  ? 1061 HOH   A O   1 1 
HETATM 10449 O  O   . HOH   Q 12 .   ? -19.464 -13.459 -22.607 1    35.971  ? 1062 HOH   A O   1 1 
HETATM 10450 O  O   . HOH   Q 12 .   ? 29.552  -22.966 -11.639 1    30.172  ? 1063 HOH   A O   1 1 
HETATM 10451 O  O   . HOH   Q 12 .   ? 16.66   12.586  -10.683 1    37.043  ? 1064 HOH   A O   1 1 
HETATM 10452 O  O   . HOH   Q 12 .   ? -5.362  -14.455 0.782   1    34.24   ? 1065 HOH   A O   1 1 
HETATM 10453 O  O   . HOH   Q 12 .   ? -7.86   -14.189 -20.237 1    44.9    ? 1066 HOH   A O   1 1 
HETATM 10454 O  O   . HOH   Q 12 .   ? 23.027  13.83   -25.799 1    52.542  ? 1067 HOH   A O   1 1 
HETATM 10455 O  O   . HOH   Q 12 .   ? 39.546  -20.28  -15.734 1    37.214  ? 1068 HOH   A O   1 1 
HETATM 10456 O  O   . HOH   Q 12 .   ? 10.708  -15.032 -19.1   1    27.208  ? 1069 HOH   A O   1 1 
HETATM 10457 O  O   . HOH   Q 12 .   ? 16.69   -39.788 -9.908  1    39.451  ? 1070 HOH   A O   1 1 
HETATM 10458 O  O   . HOH   Q 12 .   ? 21.953  11.529  -13.786 1    39.916  ? 1071 HOH   A O   1 1 
HETATM 10459 O  O   . HOH   Q 12 .   ? -16.337 -0.443  -8.533  1    28.479  ? 1072 HOH   A O   1 1 
HETATM 10460 O  O   . HOH   Q 12 .   ? -13.419 -18.488 -36.859 1    36.66   ? 1073 HOH   A O   1 1 
HETATM 10461 O  O   . HOH   Q 12 .   ? -7.341  -18.494 -18.486 1    38.585  ? 1074 HOH   A O   1 1 
HETATM 10462 O  O   . HOH   Q 12 .   ? 11.927  1.47    -3.66   1    22.975  ? 1075 HOH   A O   1 1 
HETATM 10463 O  O   . HOH   Q 12 .   ? 4.13    15.99   -15.957 1    37.303  ? 1076 HOH   A O   1 1 
HETATM 10464 O  O   . HOH   Q 12 .   ? 1.779   -36.543 -11.299 1    24.335  ? 1077 HOH   A O   1 1 
HETATM 10465 O  O   . HOH   Q 12 .   ? 3.561   -19.465 3.586   1    32.123  ? 1078 HOH   A O   1 1 
HETATM 10466 O  O   . HOH   Q 12 .   ? -3.465  -13.945 3.026   1    32.097  ? 1079 HOH   A O   1 1 
HETATM 10467 O  O   . HOH   Q 12 .   ? 29.83   -21.385 -29.173 1    38.706  ? 1080 HOH   A O   1 1 
HETATM 10468 O  O   . HOH   Q 12 .   ? 23.718  -29.072 -20.215 1    26.593  ? 1081 HOH   A O   1 1 
HETATM 10469 O  O   . HOH   Q 12 .   ? 11.888  -43.197 -19.228 1    42.531  ? 1082 HOH   A O   1 1 
HETATM 10470 O  O   . HOH   Q 12 .   ? 8.7     -13.043 -19.764 1    33.403  ? 1083 HOH   A O   1 1 
HETATM 10471 O  O   . HOH   Q 12 .   ? -15.063 -11.823 -1.289  1    24.837  ? 1084 HOH   A O   1 1 
HETATM 10472 O  O   . HOH   Q 12 .   ? 2.645   -31.943 1.95    1    47.533  ? 1085 HOH   A O   1 1 
HETATM 10473 O  O   . HOH   Q 12 .   ? 28.98   -26.649 -17.402 1    34.666  ? 1086 HOH   A O   1 1 
HETATM 10474 O  O   . HOH   Q 12 .   ? 7.17    -19.948 1.666   1    39.135  ? 1087 HOH   A O   1 1 
HETATM 10475 O  O   . HOH   Q 12 .   ? -7.492  -22.983 -13.38  1    28.102  ? 1088 HOH   A O   1 1 
HETATM 10476 O  O   . HOH   Q 12 .   ? 1.051   -22.69  -1.388  1    22.885  ? 1089 HOH   A O   1 1 
HETATM 10477 O  O   . HOH   Q 12 .   ? 29.167  -23.65  -30.709 1    45.395  ? 1090 HOH   A O   1 1 
HETATM 10478 O  O   . HOH   Q 12 .   ? -11.668 -11.667 -17.368 1    52.48   ? 1091 HOH   A O   1 1 
HETATM 10479 O  O   . HOH   Q 12 .   ? -20.412 0.855   -9.973  1    42.517  ? 1092 HOH   A O   1 1 
HETATM 10480 O  O   . HOH   Q 12 .   ? 27.381  -26.438 -19.597 1    43.437  ? 1093 HOH   A O   1 1 
HETATM 10481 O  O   . HOH   Q 12 .   ? 8.658   -29.221 -4.499  1    23.391  ? 1094 HOH   A O   1 1 
HETATM 10482 O  O   . HOH   Q 12 .   ? 18.403  -40.545 -26.316 1    48.972  ? 1095 HOH   A O   1 1 
HETATM 10483 O  O   . HOH   Q 12 .   ? -0.475  -35.571 -10.212 1    23.943  ? 1096 HOH   A O   1 1 
HETATM 10484 O  O   . HOH   Q 12 .   ? 9.94    -33.46  -6.053  1    35.022  ? 1097 HOH   A O   1 1 
HETATM 10485 O  O   . HOH   Q 12 .   ? -16.001 -10.472 -24.7   1    32.866  ? 1098 HOH   A O   1 1 
HETATM 10486 O  O   . HOH   Q 12 .   ? 13.021  -29.261 -2.741  1    53.347  ? 1099 HOH   A O   1 1 
HETATM 10487 O  O   . HOH   Q 12 .   ? -29.296 -11.263 -25.088 1    36.378  ? 1100 HOH   A O   1 1 
HETATM 10488 O  O   . HOH   Q 12 .   ? 15.369  -8.846  0.405   1    52.802  ? 1101 HOH   A O   1 1 
HETATM 10489 O  O   . HOH   Q 12 .   ? 11.738  -9.325  -26.623 1    36.861  ? 1102 HOH   A O   1 1 
HETATM 10490 O  O   . HOH   Q 12 .   ? 35.03   -27.316 -25.883 1    50.502  ? 1103 HOH   A O   1 1 
HETATM 10491 O  O   . HOH   Q 12 .   ? -13.434 -25.578 -8.427  1    38.937  ? 1104 HOH   A O   1 1 
HETATM 10492 O  O   . HOH   Q 12 .   ? 29.055  -8.057  -16.546 1    35.958  ? 1105 HOH   A O   1 1 
HETATM 10493 O  O   . HOH   Q 12 .   ? 5.546   9.675   -43.969 1    65.154  ? 1106 HOH   A O   1 1 
HETATM 10494 O  O   . HOH   Q 12 .   ? 30.85   -27.701 -13.816 1    45.922  ? 1107 HOH   A O   1 1 
HETATM 10495 O  O   . HOH   Q 12 .   ? 39.203  -18.248 -21.305 1    42.045  ? 1108 HOH   A O   1 1 
HETATM 10496 O  O   . HOH   Q 12 .   ? -18.581 3.953   -14.697 1    41.221  ? 1109 HOH   A O   1 1 
HETATM 10497 O  O   . HOH   Q 12 .   ? 21.092  -13.868 -2.598  1    32.444  ? 1110 HOH   A O   1 1 
HETATM 10498 O  O   . HOH   Q 12 .   ? -13.079 -21.744 -36.324 1    50.202  ? 1111 HOH   A O   1 1 
HETATM 10499 O  O   . HOH   Q 12 .   ? -12.1   -3.59   -34.261 1    51.671  ? 1112 HOH   A O   1 1 
HETATM 10500 O  O   . HOH   Q 12 .   ? 18.633  -22.588 -0.111  1    37.796  ? 1113 HOH   A O   1 1 
HETATM 10501 O  O   . HOH   Q 12 .   ? 16.289  13.189  -7.884  1    45.548  ? 1114 HOH   A O   1 1 
HETATM 10502 O  O   . HOH   Q 12 .   ? -19.955 -2.426  -7.419  1    34.417  ? 1115 HOH   A O   1 1 
HETATM 10503 O  O   . HOH   Q 12 .   ? 15.702  -17.179 -24.107 1    46.439  ? 1116 HOH   A O   1 1 
HETATM 10504 O  O   . HOH   Q 12 .   ? 37.485  -17.47  -15.978 1    42.739  ? 1117 HOH   A O   1 1 
HETATM 10505 O  O   . HOH   Q 12 .   ? 1.355   -7.408  -30.204 1    53.455  ? 1118 HOH   A O   1 1 
HETATM 10506 O  O   . HOH   Q 12 .   ? 38.499  -20.721 -18.108 1    40.335  ? 1119 HOH   A O   1 1 
HETATM 10507 O  O   . HOH   Q 12 .   ? -7.288  -6.377  -2.367  1    31.263  ? 1120 HOH   A O   1 1 
HETATM 10508 O  O   . HOH   Q 12 .   ? 18.125  11.028  -6.195  1    35.179  ? 1121 HOH   A O   1 1 
HETATM 10509 O  O   . HOH   Q 12 .   ? 25.99   -28.902 -19.926 1    35.827  ? 1122 HOH   A O   1 1 
HETATM 10510 O  O   . HOH   Q 12 .   ? -14.678 1.164   -9.623  1    31.342  ? 1123 HOH   A O   1 1 
HETATM 10511 O  O   . HOH   Q 12 .   ? -11.107 -9.365  -23.925 1    30.045  ? 1124 HOH   A O   1 1 
HETATM 10512 O  O   . HOH   Q 12 .   ? 5.195   -6.512  -39.832 1    46.367  ? 1125 HOH   A O   1 1 
HETATM 10513 O  O   . HOH   Q 12 .   ? 8.571   8.794   -8.877  1    35.851  ? 1126 HOH   A O   1 1 
HETATM 10514 O  O   . HOH   Q 12 .   ? -28.464 -1.058  -17.106 1    38.559  ? 1127 HOH   A O   1 1 
HETATM 10515 O  O   . HOH   Q 12 .   ? 16.784  -15.413 1.865   1    42.62   ? 1128 HOH   A O   1 1 
HETATM 10516 O  O   . HOH   Q 12 .   ? -4.679  -18.157 -40.207 1    59.125  ? 1129 HOH   A O   1 1 
HETATM 10517 O  O   . HOH   Q 12 .   ? 24.123  -26.394 -7.823  1    33.954  ? 1130 HOH   A O   1 1 
HETATM 10518 O  O   . HOH   Q 12 .   ? 32.568  2.945   -16.465 1    55.661  ? 1131 HOH   A O   1 1 
HETATM 10519 O  O   . HOH   Q 12 .   ? 20.244  -19.62  -2.633  1    37.543  ? 1132 HOH   A O   1 1 
HETATM 10520 O  O   . HOH   Q 12 .   ? -20.756 -33.851 -16.597 1    42.262  ? 1133 HOH   A O   1 1 
HETATM 10521 O  O   . HOH   Q 12 .   ? 8.31    -9.742  -26.23  1    40.432  ? 1134 HOH   A O   1 1 
HETATM 10522 O  O   . HOH   Q 12 .   ? 24.698  -30.399 -7.889  1    51.55   ? 1135 HOH   A O   1 1 
HETATM 10523 O  O   . HOH   Q 12 .   ? -13.008 -21.611 -8.414  1    41.573  ? 1136 HOH   A O   1 1 
HETATM 10524 O  O   . HOH   Q 12 .   ? 32.865  -20.257 -9.939  1    41.139  ? 1137 HOH   A O   1 1 
HETATM 10525 O  O   . HOH   Q 12 .   ? 11.004  -40.605 -29.388 1    32.935  ? 1138 HOH   A O   1 1 
HETATM 10526 O  O   . HOH   Q 12 .   ? 5.174   -44.536 -14.743 1    39.407  ? 1139 HOH   A O   1 1 
HETATM 10527 O  O   . HOH   Q 12 .   ? -12.292 3.55    -7.318  1    28.692  ? 1140 HOH   A O   1 1 
HETATM 10528 O  O   . HOH   Q 12 .   ? -17.244 -14.155 -36.511 1    34.821  ? 1141 HOH   A O   1 1 
HETATM 10529 O  O   . HOH   Q 12 .   ? 3.493   -23.141 2.523   1    44.841  ? 1142 HOH   A O   1 1 
HETATM 10530 O  O   . HOH   Q 12 .   ? -31.007 -1.546  -18.216 1    42.466  ? 1143 HOH   A O   1 1 
HETATM 10531 O  O   . HOH   Q 12 .   ? 28.741  -30.288 -11.574 1    38.988  ? 1144 HOH   A O   1 1 
HETATM 10532 O  O   . HOH   Q 12 .   ? 29.393  -21.948 -5.104  1    36.123  ? 1145 HOH   A O   1 1 
HETATM 10533 O  O   . HOH   Q 12 .   ? -5.229  -35.248 -30.488 1    45.668  ? 1146 HOH   A O   1 1 
HETATM 10534 O  O   . HOH   Q 12 .   ? 18.709  -17.924 -0.79   1    38.307  ? 1147 HOH   A O   1 1 
HETATM 10535 O  O   . HOH   Q 12 .   ? -9.707  5.58    -28.604 1    44.988  ? 1148 HOH   A O   1 1 
HETATM 10536 O  O   . HOH   Q 12 .   ? 7.004   -10.537 -37.864 1    39.859  ? 1149 HOH   A O   1 1 
HETATM 10537 O  O   . HOH   Q 12 .   ? -7.245  4.931   -29.85  1    51.389  ? 1150 HOH   A O   1 1 
HETATM 10538 O  O   . HOH   Q 12 .   ? -27.332 1.231   -18.214 1    40.233  ? 1151 HOH   A O   1 1 
HETATM 10539 O  O   . HOH   Q 12 .   ? 30.68   -21.736 -9.406  1    23.776  ? 1152 HOH   A O   1 1 
HETATM 10540 O  O   . HOH   Q 12 .   ? -7.644  10.134  -18.797 1    30.974  ? 1153 HOH   A O   1 1 
HETATM 10541 O  O   . HOH   Q 12 .   ? -10.844 -14.835 -16.782 1    41.582  ? 1154 HOH   A O   1 1 
HETATM 10542 O  O   . HOH   Q 12 .   ? -12.706 7.255   -24.587 1    39.158  ? 1155 HOH   A O   1 1 
HETATM 10543 O  O   . HOH   Q 12 .   ? -22.387 -2.691  -6.86   1    37.425  ? 1156 HOH   A O   1 1 
HETATM 10544 O  O   . HOH   Q 12 .   ? -27.625 -20.727 -30.93  1    53.175  ? 1157 HOH   A O   1 1 
HETATM 10545 O  O   . HOH   Q 12 .   ? 6.216   -8.836  -39.782 1    45.722  ? 1158 HOH   A O   1 1 
HETATM 10546 O  O   . HOH   Q 12 .   ? 9.553   -10.633 -38.179 1    44.917  ? 1159 HOH   A O   1 1 
HETATM 10547 O  O   . HOH   Q 12 .   ? 30.922  -24.321 -6.087  1    46.551  ? 1160 HOH   A O   1 1 
HETATM 10548 O  O   . HOH   R 12 .   ? 3.21    -11.784 47.522  1    97.878  ? 801  HOH   B O   1 2 
HETATM 10549 O  O   . HOH   R 12 .   ? 9.311   28.351  22.456  1    36.853  ? 802  HOH   B O   1 2 
HETATM 10550 O  O   . HOH   R 12 .   ? 10.939  8.264   40.36   1    40.366  ? 803  HOH   B O   1 2 
HETATM 10551 O  O   . HOH   R 12 .   ? -13.241 0.73    25.071  1    45.927  ? 804  HOH   B O   1 2 
HETATM 10552 O  O   . HOH   R 12 .   ? -8.659  -15.335 46.143  1    74.917  ? 805  HOH   B O   1 2 
HETATM 10553 O  O   . HOH   R 12 .   ? 1.414   -3.996  34.931  1    45.337  ? 806  HOH   B O   1 2 
HETATM 10554 O  O   . HOH   R 12 .   ? 1.151   -6.705  33.77   1    40.181  ? 807  HOH   B O   1 2 
HETATM 10555 O  O   . HOH   R 12 .   ? 6.142   23.712  23.873  1    34.412  ? 808  HOH   B O   1 2 
HETATM 10556 O  O   . HOH   R 12 .   ? -2.649  38.797  14.263  1    38.603  ? 809  HOH   B O   1 2 
HETATM 10557 O  O   . HOH   R 12 .   ? 21.448  16.15   14.717  1    39.46   ? 810  HOH   B O   1 2 
HETATM 10558 O  O   . HOH   R 12 .   ? -26.154 26.235  29.341  1    47.309  ? 811  HOH   B O   1 2 
HETATM 10559 O  O   . HOH   R 12 .   ? -10.881 40.44   29.602  1    55.489  ? 812  HOH   B O   1 2 
HETATM 10560 O  O   . HOH   R 12 .   ? 22.94   8.035   14.742  1    39.281  ? 813  HOH   B O   1 2 
HETATM 10561 O  O   . HOH   R 12 .   ? 2.938   22.2    14.487  1    32.247  ? 814  HOH   B O   1 2 
HETATM 10562 O  O   . HOH   R 12 .   ? 8.781   14.543  26.457  1    32.54   ? 815  HOH   B O   1 2 
HETATM 10563 O  O   . HOH   R 12 .   ? -8.302  34.001  37.026  1    41.54   ? 816  HOH   B O   1 2 
HETATM 10564 O  O   . HOH   R 12 .   ? 1.233   -3.237  7.363   1    44.202  ? 817  HOH   B O   1 2 
HETATM 10565 O  O   . HOH   R 12 .   ? -7.546  2.767   7.439   1    27.944  ? 818  HOH   B O   1 2 
HETATM 10566 O  O   . HOH   R 12 .   ? -0.096  -5.807  11.84   1    37.99   ? 819  HOH   B O   1 2 
HETATM 10567 O  O   . HOH   R 12 .   ? -14.971 30.382  36.197  1    29.925  ? 820  HOH   B O   1 2 
HETATM 10568 O  O   . HOH   R 12 .   ? 20.482  8.001   7.928   1    36.992  ? 821  HOH   B O   1 2 
HETATM 10569 O  O   . HOH   R 12 .   ? 13.653  3.056   -0.9    1    36.659  ? 822  HOH   B O   1 2 
HETATM 10570 O  O   . HOH   R 12 .   ? 12.522  14.487  22.319  1    28.7    ? 823  HOH   B O   1 2 
HETATM 10571 O  O   . HOH   R 12 .   ? 20.83   20.399  9.029   1    34.331  ? 824  HOH   B O   1 2 
HETATM 10572 O  O   . HOH   R 12 .   ? 3.263   -4.491  30.831  1    52.48   ? 825  HOH   B O   1 2 
HETATM 10573 O  O   . HOH   R 12 .   ? -22.667 29.767  34.434  1    34.776  ? 826  HOH   B O   1 2 
HETATM 10574 O  O   . HOH   R 12 .   ? 8.553   20.644  38.663  1    59.226  ? 827  HOH   B O   1 2 
HETATM 10575 O  O   . HOH   R 12 .   ? -9.745  37.836  9.109   1    42.794  ? 828  HOH   B O   1 2 
HETATM 10576 O  O   . HOH   R 12 .   ? 15.124  10.817  35.746  1    37.391  ? 829  HOH   B O   1 2 
HETATM 10577 O  O   . HOH   R 12 .   ? -3.37   9.659   33.471  1    30.603  ? 830  HOH   B O   1 2 
HETATM 10578 O  O   . HOH   R 12 .   ? 7.1     -1.09   1.392   1    25.716  ? 831  HOH   B O   1 2 
HETATM 10579 O  O   . HOH   R 12 .   ? -17.048 24.054  22.378  1    28.618  ? 832  HOH   B O   1 2 
HETATM 10580 O  O   . HOH   R 12 .   ? -13.563 8.538   29.616  1    31.548  ? 833  HOH   B O   1 2 
HETATM 10581 O  O   . HOH   R 12 .   ? -18.428 13.894  2.388   1    40.515  ? 834  HOH   B O   1 2 
HETATM 10582 O  O   . HOH   R 12 .   ? 15.157  5.955   5.379   1    43.584  ? 835  HOH   B O   1 2 
HETATM 10583 O  O   . HOH   R 12 .   ? 3.099   18.926  40.418  1    32.533  ? 836  HOH   B O   1 2 
HETATM 10584 O  O   . HOH   R 12 .   ? 6.159   32.876  18.212  1    46.24   ? 837  HOH   B O   1 2 
HETATM 10585 O  O   . HOH   R 12 .   ? -6.189  13.446  0.669   1    20.792  ? 838  HOH   B O   1 2 
HETATM 10586 O  O   . HOH   R 12 .   ? -5.093  11.109  37.625  1    31.59   ? 839  HOH   B O   1 2 
HETATM 10587 O  O   . HOH   R 12 .   ? -2.263  32.142  -9.853  1    52.785  ? 840  HOH   B O   1 2 
HETATM 10588 O  O   . HOH   R 12 .   ? -2.879  35.29   10.558  1    40.998  ? 841  HOH   B O   1 2 
HETATM 10589 O  O   . HOH   R 12 .   ? 12.958  23.97   -3.95   1    27.443  ? 842  HOH   B O   1 2 
HETATM 10590 O  O   . HOH   R 12 .   ? 4.412   30.385  2.442   1    27.796  ? 843  HOH   B O   1 2 
HETATM 10591 O  O   . HOH   R 12 .   ? 16.183  26.228  27.548  1    49.766  ? 844  HOH   B O   1 2 
HETATM 10592 O  O   . HOH   R 12 .   ? 10.793  27.979  32.555  1    33.138  ? 845  HOH   B O   1 2 
HETATM 10593 O  O   . HOH   R 12 .   ? 15.882  21.897  18.456  1    29.956  ? 846  HOH   B O   1 2 
HETATM 10594 O  O   . HOH   R 12 .   ? 24.53   15.014  29.948  1    53.483  ? 847  HOH   B O   1 2 
HETATM 10595 O  O   . HOH   R 12 .   ? -1.129  -9.669  47.451  1    90.884  ? 848  HOH   B O   1 2 
HETATM 10596 O  O   . HOH   R 12 .   ? -6.307  4.025   -0.57   1    30.849  ? 849  HOH   B O   1 2 
HETATM 10597 O  O   . HOH   R 12 .   ? 19.896  -0.845  13.066  1    53.198  ? 850  HOH   B O   1 2 
HETATM 10598 O  O   . HOH   R 12 .   ? 5.336   34.258  28.35   1    32.279  ? 851  HOH   B O   1 2 
HETATM 10599 O  O   . HOH   R 12 .   ? 3.134   -8.435  11.536  1    38.87   ? 852  HOH   B O   1 2 
HETATM 10600 O  O   . HOH   R 12 .   ? 12.163  8.04    22.825  1    27.863  ? 853  HOH   B O   1 2 
HETATM 10601 O  O   . HOH   R 12 .   ? -4.191  10.325  24.03   1    24.871  ? 854  HOH   B O   1 2 
HETATM 10602 O  O   . HOH   R 12 .   ? 6.217   26.423  21.678  1    37.716  ? 855  HOH   B O   1 2 
HETATM 10603 O  O   . HOH   R 12 .   ? -26.511 16.818  23.311  1    44.428  ? 856  HOH   B O   1 2 
HETATM 10604 O  O   . HOH   R 12 .   ? 6.432   33.091  26.396  1    36.717  ? 857  HOH   B O   1 2 
HETATM 10605 O  O   . HOH   R 12 .   ? -9.014  28.772  -6.404  1    36.037  ? 858  HOH   B O   1 2 
HETATM 10606 O  O   . HOH   R 12 .   ? -17.325 5.022   12.492  1    44.033  ? 859  HOH   B O   1 2 
HETATM 10607 O  O   . HOH   R 12 .   ? 1.792   10.54   33.011  1    45.248  ? 860  HOH   B O   1 2 
HETATM 10608 O  O   . HOH   R 12 .   ? 7.558   5.584   16.85   1    19.029  ? 861  HOH   B O   1 2 
HETATM 10609 O  O   . HOH   R 12 .   ? -14.462 22.465  3.83    1    34.043  ? 862  HOH   B O   1 2 
HETATM 10610 O  O   . HOH   R 12 .   ? -11.78  32.286  27.523  1    30.799  ? 863  HOH   B O   1 2 
HETATM 10611 O  O   . HOH   R 12 .   ? -2.02   8.082   11.885  1    22.134  ? 864  HOH   B O   1 2 
HETATM 10612 O  O   . HOH   R 12 .   ? -7.863  40.851  26.619  1    39.104  ? 865  HOH   B O   1 2 
HETATM 10613 O  O   . HOH   R 12 .   ? -17.343 14.737  13.343  1    26.561  ? 866  HOH   B O   1 2 
HETATM 10614 O  O   . HOH   R 12 .   ? 8.781   11.384  28.621  1    36.668  ? 867  HOH   B O   1 2 
HETATM 10615 O  O   . HOH   R 12 .   ? -16.068 27.4    16.645  1    28.999  ? 868  HOH   B O   1 2 
HETATM 10616 O  O   . HOH   R 12 .   ? 22.296  15.264  9.952   1    36.594  ? 869  HOH   B O   1 2 
HETATM 10617 O  O   . HOH   R 12 .   ? 10.711  21.504  -11.357 1    41.664  ? 870  HOH   B O   1 2 
HETATM 10618 O  O   . HOH   R 12 .   ? -18.486 27.002  17.702  1    38.84   ? 871  HOH   B O   1 2 
HETATM 10619 O  O   . HOH   R 12 .   ? 6.721   19.544  5.831   1    18.686  ? 872  HOH   B O   1 2 
HETATM 10620 O  O   . HOH   R 12 .   ? -9.183  30.71   -5.309  1    35.652  ? 873  HOH   B O   1 2 
HETATM 10621 O  O   . HOH   R 12 .   ? -9.205  -2.033  17.738  1    41.446  ? 874  HOH   B O   1 2 
HETATM 10622 O  O   . HOH   R 12 .   ? 6.932   28.11   34.221  1    43.403  ? 875  HOH   B O   1 2 
HETATM 10623 O  O   . HOH   R 12 .   ? -12.877 38.517  9.007   1    42.707  ? 876  HOH   B O   1 2 
HETATM 10624 O  O   . HOH   R 12 .   ? -1.487  3.325   16.209  1    25.347  ? 877  HOH   B O   1 2 
HETATM 10625 O  O   . HOH   R 12 .   ? -22.625 14.651  18.163  1    34.954  ? 878  HOH   B O   1 2 
HETATM 10626 O  O   . HOH   R 12 .   ? -4.284  21.754  13.819  1    33.919  ? 879  HOH   B O   1 2 
HETATM 10627 O  O   . HOH   R 12 .   ? 15.697  17.471  36.617  1    52.076  ? 880  HOH   B O   1 2 
HETATM 10628 O  O   . HOH   R 12 .   ? 0.781   22.062  -14.673 1    42.898  ? 881  HOH   B O   1 2 
HETATM 10629 O  O   . HOH   R 12 .   ? 11.73   -8.236  15.884  1    41.013  ? 882  HOH   B O   1 2 
HETATM 10630 O  O   . HOH   R 12 .   ? 8.27    19.087  18.189  1    22.06   ? 883  HOH   B O   1 2 
HETATM 10631 O  O   . HOH   R 12 .   ? 1.202   -2.739  12.352  1    28.444  ? 884  HOH   B O   1 2 
HETATM 10632 O  O   . HOH   R 12 .   ? 18.916  16.987  -1.147  1    37.777  ? 885  HOH   B O   1 2 
HETATM 10633 O  O   . HOH   R 12 .   ? 6.659   13.717  -3.537  1    27.001  ? 886  HOH   B O   1 2 
HETATM 10634 O  O   . HOH   R 12 .   ? -21.68  28.867  1.375   1    47.932  ? 887  HOH   B O   1 2 
HETATM 10635 O  O   . HOH   R 12 .   ? -14.318 22.321  -6.653  1    30.613  ? 888  HOH   B O   1 2 
HETATM 10636 O  O   . HOH   R 12 .   ? 4.924   23.755  5.428   1    18.75   ? 889  HOH   B O   1 2 
HETATM 10637 O  O   . HOH   R 12 .   ? 19.611  17.656  1.743   1    37.036  ? 890  HOH   B O   1 2 
HETATM 10638 O  O   . HOH   R 12 .   ? 16.82   1.506   -0.319  1    35.009  ? 891  HOH   B O   1 2 
HETATM 10639 O  O   . HOH   R 12 .   ? 8.104   1.416   14.046  1    30.921  ? 892  HOH   B O   1 2 
HETATM 10640 O  O   . HOH   R 12 .   ? -6.886  28.489  12.838  1    34.196  ? 893  HOH   B O   1 2 
HETATM 10641 O  O   . HOH   R 12 .   ? 2.624   22.883  -6.446  1    22.633  ? 894  HOH   B O   1 2 
HETATM 10642 O  O   . HOH   R 12 .   ? -18.751 32.948  12.352  1    45.639  ? 895  HOH   B O   1 2 
HETATM 10643 O  O   . HOH   R 12 .   ? -16.332 4.923   9.893   1    40.094  ? 896  HOH   B O   1 2 
HETATM 10644 O  O   . HOH   R 12 .   ? -17.346 -9.781  40.275  1    58.653  ? 897  HOH   B O   1 2 
HETATM 10645 O  O   . HOH   R 12 .   ? -19.365 9.267   9.257   1    36.209  ? 898  HOH   B O   1 2 
HETATM 10646 O  O   . HOH   R 12 .   ? 1.375   43.799  18.057  1    52.11   ? 899  HOH   B O   1 2 
HETATM 10647 O  O   . HOH   R 12 .   ? 13.619  -3.12   12.518  1    26.134  ? 900  HOH   B O   1 2 
HETATM 10648 O  O   . HOH   R 12 .   ? 19.11   28.072  19.605  1    50.701  ? 901  HOH   B O   1 2 
HETATM 10649 O  O   . HOH   R 12 .   ? 11.152  8.507   6.582   1    15.961  ? 902  HOH   B O   1 2 
HETATM 10650 O  O   . HOH   R 12 .   ? 6.011   8.111   -12.761 1    17.892  ? 903  HOH   B O   1 2 
HETATM 10651 O  O   . HOH   R 12 .   ? 8.756   29.793  26.256  1    34.859  ? 904  HOH   B O   1 2 
HETATM 10652 O  O   . HOH   R 12 .   ? -5.957  28.913  17.386  1    39.989  ? 905  HOH   B O   1 2 
HETATM 10653 O  O   . HOH   R 12 .   ? 5.848   27.959  5.674   1    20.586  ? 906  HOH   B O   1 2 
HETATM 10654 O  O   . HOH   R 12 .   ? -20.358 29.542  35.404  1    32.19   ? 907  HOH   B O   1 2 
HETATM 10655 O  O   . HOH   R 12 .   ? 4.593   0.956   22.333  1    39.278  ? 908  HOH   B O   1 2 
HETATM 10656 O  O   . HOH   R 12 .   ? 10.172  -2.656  9.179   1    21.399  ? 909  HOH   B O   1 2 
HETATM 10657 O  O   . HOH   R 12 .   ? 4.691   2.16    6       1    21.43   ? 910  HOH   B O   1 2 
HETATM 10658 O  O   . HOH   R 12 .   ? 12.22   -1.562  10.558  1    26.802  ? 911  HOH   B O   1 2 
HETATM 10659 O  O   . HOH   R 12 .   ? 6.923   16.443  25.877  1    38.285  ? 912  HOH   B O   1 2 
HETATM 10660 O  O   . HOH   R 12 .   ? 21.365  -0.33   20.369  1    48.744  ? 913  HOH   B O   1 2 
HETATM 10661 O  O   . HOH   R 12 .   ? -0.926  32.598  37.645  1    42.352  ? 914  HOH   B O   1 2 
HETATM 10662 O  O   . HOH   R 12 .   ? -8.441  31.248  36.103  1    27.646  ? 915  HOH   B O   1 2 
HETATM 10663 O  O   . HOH   R 12 .   ? 8.717   15.1    8.912   1    31.064  ? 916  HOH   B O   1 2 
HETATM 10664 O  O   . HOH   R 12 .   ? -7.032  22.875  21.22   1    39.929  ? 917  HOH   B O   1 2 
HETATM 10665 O  O   . HOH   R 12 .   ? -20.448 36.209  10.505  1    43.005  ? 918  HOH   B O   1 2 
HETATM 10666 O  O   . HOH   R 12 .   ? 24.485  13.991  33.887  1    51.701  ? 919  HOH   B O   1 2 
HETATM 10667 O  O   . HOH   R 12 .   ? 6.026   14.821  -6.172  1    25.809  ? 920  HOH   B O   1 2 
HETATM 10668 O  O   . HOH   R 12 .   ? -6.497  16.844  19.331  1    25.935  ? 921  HOH   B O   1 2 
HETATM 10669 O  O   . HOH   R 12 .   ? -6.374  19.724  -4.716  1    25.95   ? 922  HOH   B O   1 2 
HETATM 10670 O  O   . HOH   R 12 .   ? -17.372 32.175  34.038  1    34.829  ? 923  HOH   B O   1 2 
HETATM 10671 O  O   . HOH   R 12 .   ? -1.38   31.547  15.697  1    41.98   ? 924  HOH   B O   1 2 
HETATM 10672 O  O   . HOH   R 12 .   ? 0.56    26.945  9.796   1    26.392  ? 925  HOH   B O   1 2 
HETATM 10673 O  O   . HOH   R 12 .   ? 6.881   0.019   21.814  1    35.792  ? 926  HOH   B O   1 2 
HETATM 10674 O  O   . HOH   R 12 .   ? -13.428 22.159  1.709   1    23.125  ? 927  HOH   B O   1 2 
HETATM 10675 O  O   . HOH   R 12 .   ? -4.218  13.686  -7.016  1    25.046  ? 928  HOH   B O   1 2 
HETATM 10676 O  O   . HOH   R 12 .   ? 5.27    30.658  4.98    1    30.761  ? 929  HOH   B O   1 2 
HETATM 10677 O  O   . HOH   R 12 .   ? -18.178 31.809  15.064  1    38.401  ? 930  HOH   B O   1 2 
HETATM 10678 O  O   . HOH   R 12 .   ? -5.764  7.45    27.22   1    32.331  ? 931  HOH   B O   1 2 
HETATM 10679 O  O   . HOH   R 12 .   ? -5.42   23.82   -10.604 1    30.383  ? 932  HOH   B O   1 2 
HETATM 10680 O  O   . HOH   R 12 .   ? 1.23    25.117  12.689  1    36.394  ? 933  HOH   B O   1 2 
HETATM 10681 O  O   . HOH   R 12 .   ? -4.889  24.788  -7.278  1    22.535  ? 934  HOH   B O   1 2 
HETATM 10682 O  O   . HOH   R 12 .   ? -6.126  22.092  16.013  1    32.711  ? 935  HOH   B O   1 2 
HETATM 10683 O  O   . HOH   R 12 .   ? 12.794  35.508  6.147   1    44.029  ? 936  HOH   B O   1 2 
HETATM 10684 O  O   . HOH   R 12 .   ? 22.066  19.383  14.821  1    43.585  ? 937  HOH   B O   1 2 
HETATM 10685 O  O   . HOH   R 12 .   ? -3.609  10.994  -4.085  1    22.097  ? 938  HOH   B O   1 2 
HETATM 10686 O  O   . HOH   R 12 .   ? 16.417  9.584   -4.312  1    27.29   ? 939  HOH   B O   1 2 
HETATM 10687 O  O   . HOH   R 12 .   ? -7.126  17.604  25.573  1    22.3    ? 940  HOH   B O   1 2 
HETATM 10688 O  O   . HOH   R 12 .   ? 16.02   13.074  7.212   1    21.511  ? 941  HOH   B O   1 2 
HETATM 10689 O  O   . HOH   R 12 .   ? -7.133  5.272   26.336  1    42.262  ? 942  HOH   B O   1 2 
HETATM 10690 O  O   . HOH   R 12 .   ? 6.525   24.33   12.626  1    25.665  ? 943  HOH   B O   1 2 
HETATM 10691 O  O   . HOH   R 12 .   ? -2.575  24.866  18.193  1    37.53   ? 944  HOH   B O   1 2 
HETATM 10692 O  O   . HOH   R 12 .   ? 1.581   25.821  -12.579 1    40.626  ? 945  HOH   B O   1 2 
HETATM 10693 O  O   . HOH   R 12 .   ? -2.09   2.834   -1.428  1    45.416  ? 946  HOH   B O   1 2 
HETATM 10694 O  O   . HOH   R 12 .   ? -11.499 32.562  30.36   1    26.114  ? 947  HOH   B O   1 2 
HETATM 10695 O  O   . HOH   R 12 .   ? 3.642   19.772  16.377  1    25.431  ? 948  HOH   B O   1 2 
HETATM 10696 O  O   . HOH   R 12 .   ? -21.008 26.05   8.223   1    33.17   ? 949  HOH   B O   1 2 
HETATM 10697 O  O   . HOH   R 12 .   ? 2.333   33.972  10.251  1    46.046  ? 950  HOH   B O   1 2 
HETATM 10698 O  O   . HOH   R 12 .   ? -10.306 30.276  27.795  1    27.259  ? 951  HOH   B O   1 2 
HETATM 10699 O  O   . HOH   R 12 .   ? 7.924   7.872   -2.717  1    24.007  ? 952  HOH   B O   1 2 
HETATM 10700 O  O   . HOH   R 12 .   ? -21.247 21.286  35.94   1    54.079  ? 953  HOH   B O   1 2 
HETATM 10701 O  O   . HOH   R 12 .   ? -1.961  18.678  4.939   1    18.093  ? 954  HOH   B O   1 2 
HETATM 10702 O  O   . HOH   R 12 .   ? 8.627   15.074  6.249   1    23.265  ? 955  HOH   B O   1 2 
HETATM 10703 O  O   . HOH   R 12 .   ? 9.697   36.979  4.528   1    38.608  ? 956  HOH   B O   1 2 
HETATM 10704 O  O   . HOH   R 12 .   ? 8.25    -6.1    3.006   1    34.552  ? 957  HOH   B O   1 2 
HETATM 10705 O  O   . HOH   R 12 .   ? 11.453  12.141  -14.875 1    44.484  ? 958  HOH   B O   1 2 
HETATM 10706 O  O   . HOH   R 12 .   ? -16.316 -8.633  26.083  1    61.38   ? 959  HOH   B O   1 2 
HETATM 10707 O  O   . HOH   R 12 .   ? 9.085   12.714  -3.283  1    25.866  ? 960  HOH   B O   1 2 
HETATM 10708 O  O   . HOH   R 12 .   ? 6.901   23.564  15.475  1    40.354  ? 961  HOH   B O   1 2 
HETATM 10709 O  O   . HOH   R 12 .   ? -5.882  10.727  -0.714  1    30.617  ? 962  HOH   B O   1 2 
HETATM 10710 O  O   . HOH   R 12 .   ? 10.967  18.794  21.759  1    28.245  ? 963  HOH   B O   1 2 
HETATM 10711 O  O   . HOH   R 12 .   ? 5.598   26.966  12.361  1    18.559  ? 964  HOH   B O   1 2 
HETATM 10712 O  O   . HOH   R 12 .   ? 10.444  -6.915  13.844  1    43.541  ? 965  HOH   B O   1 2 
HETATM 10713 O  O   . HOH   R 12 .   ? -2.452  4.112   2.169   1    33.951  ? 966  HOH   B O   1 2 
HETATM 10714 O  O   . HOH   R 12 .   ? -0.488  11.899  22.815  1    30.981  ? 967  HOH   B O   1 2 
HETATM 10715 O  O   . HOH   R 12 .   ? -10.63  30.048  37.302  1    27.064  ? 968  HOH   B O   1 2 
HETATM 10716 O  O   . HOH   R 12 .   ? -15.484 21.468  -0.579  1    35.463  ? 969  HOH   B O   1 2 
HETATM 10717 O  O   . HOH   R 12 .   ? 8.882   0.204   31.711  1    44.067  ? 970  HOH   B O   1 2 
HETATM 10718 O  O   . HOH   R 12 .   ? 6.467   -7.748  11.893  1    39.95   ? 971  HOH   B O   1 2 
HETATM 10719 O  O   . HOH   R 12 .   ? -3.907  8.711   26.005  1    32.353  ? 972  HOH   B O   1 2 
HETATM 10720 O  O   . HOH   R 12 .   ? -2.529  -3.829  9.502   1    49.856  ? 973  HOH   B O   1 2 
HETATM 10721 O  O   . HOH   R 12 .   ? 4.666   21.651  20.991  1    28.972  ? 974  HOH   B O   1 2 
HETATM 10722 O  O   . HOH   R 12 .   ? -3.719  18.446  43.784  1    47.021  ? 975  HOH   B O   1 2 
HETATM 10723 O  O   . HOH   R 12 .   ? -24.361 12.975  13.948  1    45.816  ? 976  HOH   B O   1 2 
HETATM 10724 O  O   . HOH   R 12 .   ? 13.81   19.907  18.967  1    40.642  ? 977  HOH   B O   1 2 
HETATM 10725 O  O   . HOH   R 12 .   ? -25.183 27.433  33.202  1    41.725  ? 978  HOH   B O   1 2 
HETATM 10726 O  O   . HOH   R 12 .   ? 5.758   11.235  -5.865  1    34.294  ? 979  HOH   B O   1 2 
HETATM 10727 O  O   . HOH   R 12 .   ? -3.321  3.367   18.32   1    28.31   ? 980  HOH   B O   1 2 
HETATM 10728 O  O   . HOH   R 12 .   ? -19.218 38.278  -0.727  1    53.344  ? 981  HOH   B O   1 2 
HETATM 10729 O  O   . HOH   R 12 .   ? -15.544 36.608  30.555  1    47.424  ? 982  HOH   B O   1 2 
HETATM 10730 O  O   . HOH   R 12 .   ? -16.87  11.568  -0.447  1    66.339  ? 983  HOH   B O   1 2 
HETATM 10731 O  O   . HOH   R 12 .   ? -17.905 6.577   8.201   1    47.679  ? 984  HOH   B O   1 2 
HETATM 10732 O  O   . HOH   R 12 .   ? 6.461   17.695  15.934  1    31.263  ? 985  HOH   B O   1 2 
HETATM 10733 O  O   . HOH   R 12 .   ? -0.28   0.522   7.028   1    35.195  ? 986  HOH   B O   1 2 
HETATM 10734 O  O   . HOH   R 12 .   ? 21.726  19.932  6.282   1    38.477  ? 987  HOH   B O   1 2 
HETATM 10735 O  O   . HOH   R 12 .   ? 13.447  33.262  -1.85   1    34.874  ? 988  HOH   B O   1 2 
HETATM 10736 O  O   . HOH   R 12 .   ? 15.981  -2.943  4.779   1    32.345  ? 989  HOH   B O   1 2 
HETATM 10737 O  O   . HOH   R 12 .   ? -20.232 12.418  3.498   1    46.365  ? 990  HOH   B O   1 2 
HETATM 10738 O  O   . HOH   R 12 .   ? -25.303 24.291  12.036  1    36.159  ? 991  HOH   B O   1 2 
HETATM 10739 O  O   . HOH   R 12 .   ? -9.018  -3.144  12.102  1    48.818  ? 992  HOH   B O   1 2 
HETATM 10740 O  O   . HOH   R 12 .   ? 9.721   17.868  -11.485 1    38.581  ? 993  HOH   B O   1 2 
HETATM 10741 O  O   . HOH   R 12 .   ? 0.797   5.97    24.261  1    43.37   ? 994  HOH   B O   1 2 
HETATM 10742 O  O   . HOH   R 12 .   ? -18.868 33.962  16.867  1    29.971  ? 995  HOH   B O   1 2 
HETATM 10743 O  O   . HOH   R 12 .   ? 5.854   10.106  -3.397  1    27.113  ? 996  HOH   B O   1 2 
HETATM 10744 O  O   . HOH   R 12 .   ? -0.769  10.992  -5.347  1    21.234  ? 997  HOH   B O   1 2 
HETATM 10745 O  O   . HOH   R 12 .   ? -24.483 15.841  12.759  1    52.769  ? 998  HOH   B O   1 2 
HETATM 10746 O  O   . HOH   R 12 .   ? 15.536  -12.265 31.429  1    57.847  ? 999  HOH   B O   1 2 
HETATM 10747 O  O   . HOH   R 12 .   ? 6.639   34.421  23.617  1    42.904  ? 1000 HOH   B O   1 2 
HETATM 10748 O  O   . HOH   R 12 .   ? 22.777  21.626  11.054  1    43.314  ? 1001 HOH   B O   1 2 
HETATM 10749 O  O   . HOH   R 12 .   ? -16.24  3.886   15.228  1    38.339  ? 1002 HOH   B O   1 2 
HETATM 10750 O  O   . HOH   R 12 .   ? -7.43   8.359   -0.122  1    39.169  ? 1003 HOH   B O   1 1 
HETATM 10751 O  O   . HOH   R 12 .   ? 18.501  0.765   30.408  1    49.141  ? 1004 HOH   B O   1 2 
HETATM 10752 O  O   . HOH   R 12 .   ? -10.821 -2.679  40.747  1    58.849  ? 1005 HOH   B O   1 2 
HETATM 10753 O  O   . HOH   R 12 .   ? -0.981  10.309  31.706  1    51.128  ? 1006 HOH   B O   1 2 
HETATM 10754 O  O   . HOH   R 12 .   ? 9.3     -6.494  -1.004  1    31.344  ? 1007 HOH   B O   1 2 
HETATM 10755 O  O   . HOH   R 12 .   ? 1.313   -1.782  -1.784  1    42.519  ? 1008 HOH   B O   1 2 
HETATM 10756 O  O   . HOH   R 12 .   ? -10.344 38.578  -2.326  1    39.068  ? 1009 HOH   B O   1 2 
HETATM 10757 O  O   . HOH   R 12 .   ? 1.661   -4.587  0.95    1    55.272  ? 1010 HOH   B O   1 2 
HETATM 10758 O  O   . HOH   R 12 .   ? -0.396  -3.211  9.711   1    30.99   ? 1011 HOH   B O   1 2 
HETATM 10759 O  O   . HOH   R 12 .   ? 0.211   22.355  15.294  1    43.812  ? 1012 HOH   B O   1 2 
HETATM 10760 O  O   . HOH   R 12 .   ? -4.239  22.254  19.758  1    30.942  ? 1013 HOH   B O   1 2 
HETATM 10761 O  O   . HOH   R 12 .   ? 4.678   23.744  -13.382 1    53.14   ? 1014 HOH   B O   1 2 
HETATM 10762 O  O   . HOH   R 12 .   ? -5.765  13.12   -4.718  1    39.437  ? 1015 HOH   B O   1 2 
HETATM 10763 O  O   . HOH   R 12 .   ? 5.535   16.19   -13.644 1    33.76   ? 1016 HOH   B O   1 2 
HETATM 10764 O  O   . HOH   R 12 .   ? -1.088  45.621  16.325  1    50.616  ? 1017 HOH   B O   1 2 
HETATM 10765 O  O   . HOH   R 12 .   ? 11.662  -5.204  12.559  1    40.764  ? 1018 HOH   B O   1 2 
HETATM 10766 O  O   . HOH   R 12 .   ? 8.725   10.966  -5.706  1    35.588  ? 1019 HOH   B O   1 2 
HETATM 10767 O  O   . HOH   R 12 .   ? 22.342  18.08   1.537   1    42.14   ? 1020 HOH   B O   1 2 
HETATM 10768 O  O   . HOH   R 12 .   ? 13.326  21.022  -11.592 1    52.736  ? 1021 HOH   B O   1 2 
HETATM 10769 O  O   . HOH   R 12 .   ? 8.321   16.445  -13.354 1    42.811  ? 1022 HOH   B O   1 2 
HETATM 10770 O  O   . HOH   R 12 .   ? -3.244  3.993   26.417  1    46.677  ? 1023 HOH   B O   1 2 
HETATM 10771 O  O   . HOH   R 12 .   ? 4.446   24.28   15.874  1    37.982  ? 1024 HOH   B O   1 2 
HETATM 10772 O  O   . HOH   R 12 .   ? 18.655  0.712   0.817   1    45.367  ? 1025 HOH   B O   1 2 
HETATM 10773 O  O   . HOH   R 12 .   ? 11.325  -5.13   8.603   1    43.207  ? 1026 HOH   B O   1 2 
HETATM 10774 O  O   . HOH   R 12 .   ? -18.338 31.348  36.237  1    33.214  ? 1027 HOH   B O   1 2 
HETATM 10775 O  O   . HOH   R 12 .   ? 6.061   6.991   -4.714  1    36.401  ? 1028 HOH   B O   1 2 
HETATM 10776 O  O   . HOH   R 12 .   ? 13.087  31.337  23.673  1    49.577  ? 1029 HOH   B O   1 2 
HETATM 10777 O  O   . HOH   R 12 .   ? -30.931 34.45   9.298   1    51.481  ? 1030 HOH   B O   1 2 
HETATM 10778 O  O   . HOH   R 12 .   ? 26.791  14.338  1.73    1    48.725  ? 1031 HOH   B O   1 2 
# 
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   . LEU A 1   ? 0.287545  0.560939 0.716579 0.0665377   -0.154017   -0.123858   1    LEU A N   
2     C  CA  . LEU A 1   ? 0.253965  0.519956 0.673002 0.0596218   -0.150019   -0.123504   1    LEU A CA  
3     C  C   . LEU A 1   ? 0.261258  0.535288 0.704074 0.0579945   -0.162147   -0.134785   1    LEU A C   
4     O  O   . LEU A 1   ? 0.237999  0.525481 0.715589 0.0567383   -0.164935   -0.14155    1    LEU A O   
5     C  CB  . LEU A 1   ? 0.251849  0.517064 0.678396 0.050618    -0.13028    -0.117149   1    LEU A CB  
6     C  CG  . LEU A 1   ? 0.239865  0.495906 0.655127 0.0430549   -0.122456   -0.11406    1    LEU A CG  
7     C  CD1 . LEU A 1   ? 0.230382  0.472667 0.606768 0.0472812   -0.126095   -0.109368   1    LEU A CD1 
8     C  CD2 . LEU A 1   ? 0.217975  0.47385  0.640908 0.0350491   -0.103317   -0.107166   1    LEU A CD2 
9     N  N   . ASP A 2   ? 0.268984  0.535165 0.692601 0.059147    -0.170907   -0.137641   2    ASP A N   
10    C  CA  . ASP A 2   ? 0.307217  0.579794 0.750457 0.0582875   -0.184086   -0.149354   2    ASP A CA  
11    C  C   . ASP A 2   ? 0.264297  0.54476  0.743801 0.0478551   -0.174638   -0.152716   2    ASP A C   
12    O  O   . ASP A 2   ? 0.225994  0.500574 0.701817 0.0405569   -0.158768   -0.145442   2    ASP A O   
13    C  CB  . ASP A 2   ? 0.409892  0.671539 0.82582  0.0597574   -0.191397   -0.151458   2    ASP A CB  
14    C  CG  . ASP A 2   ? 0.516271  0.784107 0.949491 0.0605148   -0.207531   -0.164822   2    ASP A CG  
15    O  OD1 . ASP A 2   ? 0.633756  0.908124 1.07031  0.0684153   -0.223168   -0.171106   2    ASP A OD1 
16    O  OD2 . ASP A 2   ? 0.582317  0.848904 1.02823  0.0530986   -0.204484   -0.169095   2    ASP A OD2 
17    N  N   . PRO A 3   ? 0.253403  0.547087 0.769044 0.0465776   -0.183629   -0.163407   3    PRO A N   
18    C  CA  . PRO A 3   ? 0.252806  0.553757 0.804352 0.0359542   -0.173759   -0.166228   3    PRO A CA  
19    C  C   . PRO A 3   ? 0.257658  0.547793 0.801519 0.0274468   -0.164547   -0.16323    3    PRO A C   
20    O  O   . PRO A 3   ? 0.239959  0.529203 0.794565 0.0191039   -0.147863   -0.156848   3    PRO A O   
21    C  CB  . PRO A 3   ? 0.245637  0.560686 0.831921 0.0374086   -0.189673   -0.180058   3    PRO A CB  
22    C  CG  . PRO A 3   ? 0.251032  0.569621 0.824833 0.0494907   -0.204485   -0.182213   3    PRO A CG  
23    C  CD  . PRO A 3   ? 0.274797  0.576884 0.799407 0.0548788   -0.204155   -0.17367    3    PRO A CD  
24    N  N   . GLY A 4   ? 0.260963  0.542382 0.784776 0.0300268   -0.175302   -0.16758    4    GLY A N   
25    C  CA  . GLY A 4   ? 0.265625  0.535474 0.779121 0.0234189   -0.167941   -0.164899   4    GLY A CA  
26    C  C   . GLY A 4   ? 0.27284   0.531068 0.75739  0.0218147   -0.152014   -0.151203   4    GLY A C   
27    O  O   . GLY A 4   ? 0.291866  0.540455 0.768799 0.0161045   -0.144037   -0.14744    4    GLY A O   
28    N  N   . LEU A 5   ? 0.24106   0.499648 0.709436 0.0269707   -0.147622   -0.143799   5    LEU A N   
29    C  CA  . LEU A 5   ? 0.229567  0.47725  0.670772 0.0254735   -0.133406   -0.131645   5    LEU A CA  
30    C  C   . LEU A 5   ? 0.190007  0.442507 0.647575 0.0196069   -0.116873   -0.124639   5    LEU A C   
31    O  O   . LEU A 5   ? 0.172882  0.41743  0.61156  0.0174708   -0.104026   -0.114737   5    LEU A O   
32    C  CB  . LEU A 5   ? 0.260045  0.501144 0.665707 0.0345408   -0.137919   -0.12687    5    LEU A CB  
33    C  CG  . LEU A 5   ? 0.294831  0.528069 0.675134 0.0400925   -0.150612   -0.131129   5    LEU A CG  
34    C  CD1 . LEU A 5   ? 0.307375  0.535338 0.655461 0.049188    -0.155385   -0.126423   5    LEU A CD1 
35    C  CD2 . LEU A 5   ? 0.273757  0.496065 0.640777 0.0350117   -0.144331   -0.128743   5    LEU A CD2 
36    N  N   . GLN A 6   ? 0.182009  0.448057 0.674456 0.0174348   -0.117485   -0.130196   6    GLN A N   
37    C  CA  . GLN A 6   ? 0.160756  0.433288 0.668871 0.0132886   -0.102425   -0.124585   6    GLN A CA  
38    C  C   . GLN A 6   ? 0.142789  0.414061 0.668971 0.00227865  -0.0892138  -0.121863   6    GLN A C   
39    O  O   . GLN A 6   ? 0.14549   0.417989 0.68981  -0.00176979 -0.0953618  -0.128688   6    GLN A O   
40    C  CB  . GLN A 6   ? 0.156546  0.445667 0.697928 0.0157298   -0.108654   -0.132546   6    GLN A CB  
41    C  CG  . GLN A 6   ? 0.1664    0.457825 0.693919 0.0269977   -0.121647   -0.134844   6    GLN A CG  
42    C  CD  . GLN A 6   ? 0.186374  0.494375 0.747702 0.0300153   -0.128072   -0.142604   6    GLN A CD  
43    O  OE1 . GLN A 6   ? 0.196886  0.515865 0.793127 0.0234123   -0.120968   -0.145975   6    GLN A OE1 
44    N  NE2 . GLN A 6   ? 0.204194  0.514466 0.756968 0.0401614   -0.142549   -0.146028   6    GLN A NE2 
45    N  N   . PRO A 7   ? 0.126209  0.396679 0.652277 -0.00272225 -0.0714822  -0.112932   7    PRO A N   
46    C  CA  . PRO A 7   ? 0.126775  0.396847 0.672246 -0.0133323  -0.0580734  -0.109668   7    PRO A CA  
47    C  C   . PRO A 7   ? 0.13638   0.421045 0.726126 -0.018785   -0.057025   -0.116928   7    PRO A C   
48    O  O   . PRO A 7   ? 0.130738  0.428256 0.737998 -0.0157587  -0.0572373  -0.120429   7    PRO A O   
49    C  CB  . PRO A 7   ? 0.120303  0.386244 0.649242 -0.015238   -0.0404512  -0.0982685  7    PRO A CB  
50    C  CG  . PRO A 7   ? 0.113718  0.385106 0.632476 -0.00655037 -0.0440023  -0.0987989  7    PRO A CG  
51    C  CD  . PRO A 7   ? 0.119079  0.389615 0.628252 0.00164329  -0.0635478  -0.10606    7    PRO A CD  
52    N  N   . GLY A 8   ? 0.15174   0.433841 0.759813 -0.027281   -0.0542486  -0.118358   8    GLY A N   
53    C  CA  . GLY A 8   ? 0.167438  0.4616   0.818719 -0.0349437  -0.0496939  -0.123527   8    GLY A CA  
54    C  C   . GLY A 8   ? 0.179163  0.474141 0.837368 -0.04262    -0.0277391  -0.113645   8    GLY A C   
55    O  O   . GLY A 8   ? 0.215514  0.507134 0.85039  -0.0399162  -0.0179814  -0.10535    8    GLY A O   
56    N  N   . GLN A 9   ? 0.185581  0.484427 0.875354 -0.0523992  -0.0198528  -0.114539   9    GLN A N   
57    C  CA  . GLN A 9   ? 0.197154  0.496517 0.895211 -0.0606472  0.00152275  -0.105158   9    GLN A CA  
58    C  C   . GLN A 9   ? 0.205101  0.487782 0.890425 -0.0680687  0.00916227  -0.0965934  9    GLN A C   
59    O  O   . GLN A 9   ? 0.17954   0.455301 0.869159 -0.0699007  -0.00089822 -0.101026   9    GLN A O   
60    C  CB  . GLN A 9   ? 0.213079  0.53011  0.95865  -0.0667116  0.00711282  -0.111525   9    GLN A CB  
61    C  CG  . GLN A 9   ? 0.237128  0.561516 0.989741 -0.0705653  0.0279466   -0.104224   9    GLN A CG  
62    C  CD  . GLN A 9   ? 0.270456  0.5926   0.989883 -0.0629781  0.0335444   -0.0978753  9    GLN A CD  
63    O  OE1 . GLN A 9   ? 0.235241  0.558845 0.937853 -0.0528013  0.0212015   -0.101935   9    GLN A OE1 
64    N  NE2 . GLN A 9   ? 0.291283  0.609196 1.00083  -0.0683927  0.0534506   -0.087216   9    GLN A NE2 
65    N  N   . PHE A 10  ? 0.22816   0.504327 0.896206 -0.0715554  0.0268442   -0.0843325  10   PHE A N   
66    C  CA  . PHE A 10  ? 0.237275  0.497081 0.889023 -0.0779696  0.036888    -0.0734861  10   PHE A CA  
67    C  C   . PHE A 10  ? 0.236913  0.500321 0.897139 -0.0850563  0.0585572   -0.064356   10   PHE A C   
68    O  O   . PHE A 10  ? 0.255255  0.529958 0.918185 -0.0821799  0.0649662   -0.0648996  10   PHE A O   
69    C  CB  . PHE A 10  ? 0.210396  0.455288 0.816917 -0.0710289  0.0316833   -0.0676817  10   PHE A CB  
70    C  CG  . PHE A 10  ? 0.200975  0.444923 0.79803  -0.0627999  0.0110646   -0.0773372  10   PHE A CG  
71    C  CD1 . PHE A 10  ? 0.214779  0.451494 0.818153 -0.0646108  0.00023045  -0.0826065  10   PHE A CD1 
72    C  CD2 . PHE A 10  ? 0.197653  0.448151 0.7807   -0.0532626  0.00264682  -0.0815154  10   PHE A CD2 
73    C  CE1 . PHE A 10  ? 0.207195  0.443679 0.80137  -0.0569401  -0.018207   -0.0919701  10   PHE A CE1 
74    C  CE2 . PHE A 10  ? 0.186433  0.435447 0.75878  -0.0457121  -0.0156201  -0.0895705  10   PHE A CE2 
75    C  CZ  . PHE A 10  ? 0.190233  0.432995 0.768421 -0.0475504  -0.025827   -0.0950689  10   PHE A CZ  
76    N  N   . SER A 11  ? 0.258889  0.513023 0.925222 -0.0943842  0.0698324   -0.0564424  11   SER A N   
77    C  CA  . SER A 11  ? 0.271421  0.527256 0.942414 -0.101403   0.0913047   -0.0465963  11   SER A CA  
78    C  C   . SER A 11  ? 0.306781  0.553312 0.935023 -0.0967272  0.0993653   -0.0360252  11   SER A C   
79    O  O   . SER A 11  ? 0.328091  0.56382  0.924642 -0.0900697  0.0892812   -0.0346969  11   SER A O   
80    C  CB  . SER A 11  ? 0.305542  0.551788 0.992177 -0.112104   0.0993413   -0.0405686  11   SER A CB  
81    O  OG  . SER A 11  ? 0.300358  0.532678 0.973642 -0.109914   0.0849365   -0.0423131  11   SER A OG  
82    N  N   . ALA A 12  ? 0.332944  0.584183 0.9615   -0.100401   0.117764    -0.0290154  12   ALA A N   
83    C  CA  . ALA A 12  ? 0.353256  0.599316 0.945837 -0.096142   0.127027    -0.0205074  12   ALA A CA  
84    C  C   . ALA A 12  ? 0.371544  0.598924 0.938043 -0.100904   0.136603    -0.00656076 12   ALA A C   
85    O  O   . ALA A 12  ? 0.379174  0.605013 0.936345 -0.104739   0.153834    0.00265781  12   ALA A O   
86    C  CB  . ALA A 12  ? 0.345222  0.606575 0.954016 -0.0979125  0.14218     -0.021153   12   ALA A CB  
87    N  N   . ASP A 13  ? 0.400343  0.613342 0.953029 -0.0998816  0.125149    -0.00506784 13   ASP A N   
88    C  CA  . ASP A 13  ? 0.400486  0.595516 0.935466 -0.104945   0.132191    0.00727096  13   ASP A CA  
89    C  C   . ASP A 13  ? 0.390588  0.572036 0.905735 -0.100032   0.116069    0.00606942  13   ASP A C   
90    O  O   . ASP A 13  ? 0.325403  0.511966 0.843629 -0.0937799  0.100196    -0.0046384  13   ASP A O   
91    C  CB  . ASP A 13  ? 0.466577  0.661113 1.03387  -0.116125   0.142042    0.0103945   13   ASP A CB  
92    C  CG  . ASP A 13  ? 0.516171  0.71655  1.11951  -0.118538   0.129126    -0.00134919 13   ASP A CG  
93    O  OD1 . ASP A 13  ? 0.51377   0.709626 1.10879  -0.112594   0.111612    -0.00826515 13   ASP A OD1 
94    O  OD2 . ASP A 13  ? 0.575491  0.785252 1.21534  -0.126308   0.136533    -0.00400918 13   ASP A OD2 
95    N  N   . GLU A 14  ? 0.355525  0.51967  0.850499 -0.102765   0.120452    0.0171878   14   GLU A N   
96    C  CA  . GLU A 14  ? 0.346355  0.497429 0.819316 -0.0975413  0.106995    0.0170082   14   GLU A CA  
97    C  C   . GLU A 14  ? 0.390663  0.541618 0.888512 -0.0986336  0.0929059   0.00682164  14   GLU A C   
98    O  O   . GLU A 14  ? 0.372917  0.518518 0.857062 -0.0923789  0.0785492   0.00160846  14   GLU A O   
99    C  CB  . GLU A 14  ? 0.388831  0.521297 0.838789 -0.10035    0.113935    0.0307433   14   GLU A CB  
100   C  CG  . GLU A 14  ? 0.377292  0.49752  0.804378 -0.0939367  0.0997151   0.0296915   14   GLU A CG  
101   C  CD  . GLU A 14  ? 0.416591  0.519333 0.811826 -0.0924152  0.101982    0.0415595   14   GLU A CD  
102   O  OE1 . GLU A 14  ? 0.3894    0.486115 0.775678 -0.0969324  0.115959    0.05348     14   GLU A OE1 
103   O  OE2 . GLU A 14  ? 0.397624  0.493384 0.776684 -0.0862129  0.0893153   0.0383893   14   GLU A OE2 
104   N  N   . ALA A 15  ? 0.394342  0.551121 0.929083 -0.106656   0.0969486   0.00354602  15   ALA A N   
105   C  CA  . ALA A 15  ? 0.399969  0.555623 0.95689  -0.107458   0.0826839   -0.00674174 15   ALA A CA  
106   C  C   . ALA A 15  ? 0.364136  0.535185 0.931018 -0.100544   0.0685536   -0.0214819  15   ALA A C   
107   O  O   . ALA A 15  ? 0.390724  0.559133 0.955522 -0.0958319  0.0527399   -0.0301431  15   ALA A O   
108   C  CB  . ALA A 15  ? 0.38327   0.536469 0.974754 -0.118308   0.0894237   -0.00536066 15   ALA A CB  
109   N  N   . GLY A 16  ? 0.349748  0.536219 0.925271 -0.0994117  0.0744296   -0.0239098  16   GLY A N   
110   C  CA  . GLY A 16  ? 0.341122  0.541667 0.920157 -0.0915409  0.0624575   -0.0355985  16   GLY A CA  
111   C  C   . GLY A 16  ? 0.298472  0.493258 0.839788 -0.0813329  0.0526785   -0.0356529  16   GLY A C   
112   O  O   . GLY A 16  ? 0.31972   0.51641  0.859219 -0.0752335  0.036722    -0.0451836  16   GLY A O   
113   N  N   . ALA A 17  ? 0.27742   0.464387 0.787814 -0.0795833  0.0620814   -0.0249082  17   ALA A N   
114   C  CA  . ALA A 17  ? 0.227189  0.405806 0.701201 -0.0713206  0.0543075   -0.0231673  17   ALA A CA  
115   C  C   . ALA A 17  ? 0.221103  0.38995  0.687499 -0.0681832  0.0393983   -0.0280315  17   ALA A C   
116   O  O   . ALA A 17  ? 0.171757  0.342396 0.62278  -0.0601835  0.027755    -0.0339822  17   ALA A O   
117   C  CB  . ALA A 17  ? 0.210676  0.379875 0.656328 -0.0719189  0.06686     -0.0103255  17   ALA A CB  
118   N  N   . GLN A 18  ? 0.209539  0.367571 0.684903 -0.0741262  0.0403914   -0.0250932  18   GLN A N   
119   C  CA  . GLN A 18  ? 0.247858  0.396043 0.718325 -0.0718035  0.0276728   -0.0298754  18   GLN A CA  
120   C  C   . GLN A 18  ? 0.227972  0.38582  0.717127 -0.0684182  0.012336    -0.0447724  18   GLN A C   
121   O  O   . GLN A 18  ? 0.197273  0.351839 0.669958 -0.061544   -0.00016041 -0.0505797  18   GLN A O   
122   C  CB  . GLN A 18  ? 0.315433  0.452963 0.804197 -0.0795322  0.0296216   -0.0276815  18   GLN A CB  
123   C  CG  . GLN A 18  ? 0.421689  0.541773 0.890607 -0.081826   0.0368976   -0.0151849  18   GLN A CG  
124   C  CD  . GLN A 18  ? 0.544433  0.65586  0.977737 -0.0738609  0.0309527   -0.0125315  18   GLN A CD  
125   O  OE1 . GLN A 18  ? 0.523334  0.639344 0.946536 -0.0665586  0.0193125   -0.0211241  18   GLN A OE1 
126   N  NE2 . GLN A 18  ? 0.538298  0.636948 0.952382 -0.0753006  0.0391583   -0.00022013 18   GLN A NE2 
127   N  N   . LEU A 19  ? 0.205637  0.374958 0.729519 -0.0735262  0.0135258   -0.050818   19   LEU A N   
128   C  CA  . LEU A 19  ? 0.21316   0.393835 0.756514 -0.0701236  -0.00100803 -0.0652235  19   LEU A CA  
129   C  C   . LEU A 19  ? 0.191259  0.380758 0.715993 -0.0607756  -0.00723331 -0.0686443  19   LEU A C   
130   O  O   . LEU A 19  ? 0.211902  0.403118 0.729654 -0.05406    -0.0219145  -0.0775767  19   LEU A O   
131   C  CB  . LEU A 19  ? 0.228219  0.420527 0.813195 -0.0776109  0.00294562  -0.0701262  19   LEU A CB  
132   C  CG  . LEU A 19  ? 0.26437   0.447699 0.870696 -0.0878339  0.0102859   -0.0661245  19   LEU A CG  
133   C  CD1 . LEU A 19  ? 0.272639  0.46813  0.916836 -0.0961508  0.0202243   -0.0669791  19   LEU A CD1 
134   C  CD2 . LEU A 19  ? 0.293214  0.469293 0.907567 -0.0874041  -0.00428595 -0.0756019  19   LEU A CD2 
135   N  N   . PHE A 20  ? 0.166989  0.360904 0.681797 -0.060145   0.00405177  -0.0612145  20   PHE A N   
136   C  CA  . PHE A 20  ? 0.179331  0.38013  0.675792 -0.0513248  -0.00105079 -0.0635209  20   PHE A CA  
137   C  C   . PHE A 20  ? 0.175756  0.366006 0.637002 -0.0439422  -0.00967485 -0.0624797  20   PHE A C   
138   O  O   . PHE A 20  ? 0.156351  0.350285 0.607623 -0.0362847  -0.021883   -0.0693285  20   PHE A O   
139   C  CB  . PHE A 20  ? 0.170832  0.374618 0.659378 -0.0527673  0.0146285   -0.0542274  20   PHE A CB  
140   C  CG  . PHE A 20  ? 0.185211  0.394763 0.654693 -0.0442529  0.0116079   -0.0552278  20   PHE A CG  
141   C  CD1 . PHE A 20  ? 0.160864  0.36083  0.594854 -0.0392181  0.011881    -0.049064   20   PHE A CD1 
142   C  CD2 . PHE A 20  ? 0.170157  0.394624 0.658599 -0.0415444  0.00927982  -0.0619501  20   PHE A CD2 
143   C  CE1 . PHE A 20  ? 0.161781  0.366081 0.579502 -0.0319     0.00940203  -0.0497928  20   PHE A CE1 
144   C  CE2 . PHE A 20  ? 0.165488  0.393835 0.636698 -0.0338072  0.00698839  -0.0621911  20   PHE A CE2 
145   C  CZ  . PHE A 20  ? 0.157764  0.375851 0.593884 -0.0290697  0.00680567  -0.0562852  20   PHE A CZ  
146   N  N   . ALA A 21  ? 0.191914  0.368625 0.633484 -0.0460941  -0.00313508 -0.0534591  21   ALA A N   
147   C  CA  . ALA A 21  ? 0.190613  0.358017 0.600564 -0.0396249  -0.00970691 -0.0520748  21   ALA A CA  
148   C  C   . ALA A 21  ? 0.23023   0.395571 0.644983 -0.036817   -0.0248393  -0.0624486  21   ALA A C   
149   O  O   . ALA A 21  ? 0.266204  0.430722 0.661452 -0.0294637  -0.0343484  -0.066429   21   ALA A O   
150   C  CB  . ALA A 21  ? 0.199613  0.354104 0.593121 -0.0430466  3.721e-05   -0.041063   21   ALA A CB  
151   N  N   . GLN A 22  ? 0.200337  0.364739 0.640704 -0.0426495  -0.0268313  -0.0669836  22   GLN A N   
152   C  CA  . GLN A 22  ? 0.254565  0.41642  0.699906 -0.0402759  -0.0409177  -0.077523   22   GLN A CA  
153   C  C   . GLN A 22  ? 0.253979  0.428412 0.706513 -0.0343502  -0.0535537  -0.0888287  22   GLN A C   
154   O  O   . GLN A 22  ? 0.239734  0.41247  0.67785  -0.027805   -0.0657501  -0.0957778  22   GLN A O   
155   C  CB  . GLN A 22  ? 0.318513  0.476281 0.792257 -0.048316   -0.0402589  -0.0803818  22   GLN A CB  
156   C  CG  . GLN A 22  ? 0.375635  0.518675 0.842472 -0.0536964  -0.0300575  -0.0697221  22   GLN A CG  
157   C  CD  . GLN A 22  ? 0.465732  0.60492  0.963724 -0.0626436  -0.027317   -0.0710402  22   GLN A CD  
158   O  OE1 . GLN A 22  ? 0.555066  0.703982 1.08301  -0.0679497  -0.0250639  -0.0747458  22   GLN A OE1 
159   N  NE2 . GLN A 22  ? 0.500327  0.625072 0.993276 -0.0644743  -0.0277373  -0.0683947  22   GLN A NE2 
160   N  N   . SER A 23  ? 0.224242  0.411411 0.699985 -0.0366377  -0.0505932  -0.0907856  23   SER A N   
161   C  CA  . SER A 23  ? 0.235468  0.434992 0.718694 -0.0306804  -0.0621452  -0.10041    23   SER A CA  
162   C  C   . SER A 23  ? 0.216698  0.41577  0.667643 -0.0217171  -0.0650098  -0.0973925  23   SER A C   
163   O  O   . SER A 23  ? 0.231404  0.433088 0.67345  -0.0146067  -0.078356   -0.104945   23   SER A O   
164   C  CB  . SER A 23  ? 0.252411  0.465542 0.768339 -0.0351583  -0.0570516  -0.10243    23   SER A CB  
165   O  OG  . SER A 23  ? 0.286882  0.511358 0.805845 -0.027962   -0.0683981  -0.110482   23   SER A OG  
166   N  N   . TYR A 24  ? 0.165865  0.361233 0.598829 -0.0219832  -0.0527753  -0.0864751  24   TYR A N   
167   C  CA  . TYR A 24  ? 0.18619   0.379789 0.589119 -0.0142706  -0.0545625  -0.0830563  24   TYR A CA  
168   C  C   . TYR A 24  ? 0.215154  0.399216 0.592579 -0.00904402 -0.0638372  -0.08524    24   TYR A C   
169   O  O   . TYR A 24  ? 0.185304  0.370523 0.544297 -0.00141501 -0.0718497  -0.0876498  24   TYR A O   
170   C  CB  . TYR A 24  ? 0.160511  0.34822  0.547202 -0.0168371  -0.0395225  -0.0708908  24   TYR A CB  
171   C  CG  . TYR A 24  ? 0.175317  0.359479 0.530993 -0.010039   -0.0397012  -0.0663752  24   TYR A CG  
172   C  CD1 . TYR A 24  ? 0.174996  0.367282 0.529057 -0.00523115 -0.0405904  -0.0671676  24   TYR A CD1 
173   C  CD2 . TYR A 24  ? 0.185339  0.35773  0.514216 -0.0086083  -0.0383464  -0.0609792  24   TYR A CD2 
174   C  CE1 . TYR A 24  ? 0.188377  0.376744 0.515311 0.00056803  -0.0404166  -0.0628661  24   TYR A CE1 
175   C  CE2 . TYR A 24  ? 0.207718  0.377117 0.509992 -0.00294562 -0.0380702  -0.0569248  24   TYR A CE2 
176   C  CZ  . TYR A 24  ? 0.197492  0.374461 0.498593 0.00141936  -0.0389236  -0.0576835  24   TYR A CZ  
177   O  OH  . TYR A 24  ? 0.197652  0.371069 0.474313 0.00636911  -0.0380175  -0.0534366  24   TYR A OH  
178   N  N   . GLN A 25  ? 0.233875  0.407658 0.60866  -0.0131481  -0.0613515  -0.0832407  25   GLN A N   
179   C  CA  . GLN A 25  ? 0.291473  0.455466 0.64125  -0.00876305 -0.0670948  -0.0839429  25   GLN A CA  
180   C  C   . GLN A 25  ? 0.330549  0.498482 0.682781 -0.00351021 -0.0827186  -0.0960872  25   GLN A C   
181   O  O   . GLN A 25  ? 0.34675   0.51159  0.675594 0.00311586  -0.0895132  -0.098152   25   GLN A O   
182   C  CB  . GLN A 25  ? 0.327222  0.480904 0.682381 -0.0147412  -0.0623571  -0.081218   25   GLN A CB  
183   C  CG  . GLN A 25  ? 0.394307  0.541263 0.743555 -0.012055   -0.0727172  -0.0890348  25   GLN A CG  
184   C  CD  . GLN A 25  ? 0.468638  0.606922 0.786303 -0.00709553 -0.0720318  -0.0846313  25   GLN A CD  
185   O  OE1 . GLN A 25  ? 0.4621    0.597369 0.764301 -0.00717132 -0.0628102  -0.0746813  25   GLN A OE1 
186   N  NE2 . GLN A 25  ? 0.483505  0.618181 0.792023 -0.00276211 -0.0817015  -0.0925063  25   GLN A NE2 
187   N  N   . SER A 26  ? 0.310845  0.485921 0.691881 -0.00658201 -0.088296   -0.104263   26   SER A N   
188   C  CA  . SER A 26  ? 0.409377  0.588848 0.794514 -0.00172467 -0.103957   -0.116646   26   SER A CA  
189   C  C   . SER A 26  ? 0.435109  0.621592 0.805919 0.00638589  -0.110693   -0.117942   26   SER A C   
190   O  O   . SER A 26  ? 0.490869  0.676144 0.844588 0.0132321   -0.121879   -0.123823   26   SER A O   
191   C  CB  . SER A 26  ? 0.445841  0.632831 0.86775  -0.0071205  -0.108082   -0.124945   26   SER A CB  
192   O  OG  . SER A 26  ? 0.433761  0.615271 0.871285 -0.0160195  -0.09657    -0.119153   26   SER A OG  
193   N  N   . SER A 27  ? 0.356192  0.549972 0.734554 0.00574142  -0.103869   -0.112597   27   SER A N   
194   C  CA  . SER A 27  ? 0.31384   0.513605 0.680546 0.0135335   -0.110485   -0.113604   27   SER A CA  
195   C  C   . SER A 27  ? 0.273562  0.465739 0.606182 0.0179922   -0.104919   -0.104432   27   SER A C   
196   O  O   . SER A 27  ? 0.297786  0.489862 0.611868 0.0254496   -0.113332   -0.106282   27   SER A O   
197   C  CB  . SER A 27  ? 0.289597  0.502132 0.682787 0.0124743   -0.10963    -0.115399   27   SER A CB  
198   O  OG  . SER A 27  ? 0.285039  0.50524  0.706782 0.010659    -0.119723   -0.126558   27   SER A OG  
199   N  N   . ALA A 28  ? 0.227901  0.4137   0.552323 0.0135941   -0.0913558  -0.0947494  28   ALA A N   
200   C  CA  . ALA A 28  ? 0.258279  0.436827 0.551865 0.017328    -0.0862893  -0.0866544  28   ALA A CA  
201   C  C   . ALA A 28  ? 0.277979  0.449454 0.546957 0.0227701   -0.094553   -0.0895827  28   ALA A C   
202   O  O   . ALA A 28  ? 0.279187  0.448147 0.525278 0.0280867   -0.0950037  -0.0858072  28   ALA A O   
203   C  CB  . ALA A 28  ? 0.21085   0.382943 0.499099 0.0118434   -0.0722439  -0.0770708  28   ALA A CB  
204   N  N   . GLU A 29  ? 0.261555  0.429212 0.534306 0.0213597   -0.100074   -0.0959231  29   GLU A N   
205   C  CA  . GLU A 29  ? 0.265561  0.426056 0.512947 0.0262833   -0.105255   -0.0977991  29   GLU A CA  
206   C  C   . GLU A 29  ? 0.287419  0.452684 0.526012 0.033864    -0.117684   -0.104192   29   GLU A C   
207   O  O   . GLU A 29  ? 0.283607  0.444627 0.496062 0.0395515   -0.120316   -0.102798   29   GLU A O   
208   C  CB  . GLU A 29  ? 0.29774   0.452747 0.549384 0.024232    -0.109373   -0.104517   29   GLU A CB  
209   C  CG  . GLU A 29  ? 0.274206  0.421694 0.530818 0.0177414   -0.0990367  -0.0987251  29   GLU A CG  
210   C  CD  . GLU A 29  ? 0.308051  0.448949 0.567418 0.0167585   -0.103865   -0.105806   29   GLU A CD  
211   O  OE1 . GLU A 29  ? 0.329027  0.47388  0.601499 0.017765    -0.114374   -0.116549   29   GLU A OE1 
212   O  OE2 . GLU A 29  ? 0.256466  0.388463 0.506385 0.0152443   -0.0981119  -0.101652   29   GLU A OE2 
213   N  N   . GLN A 30  ? 0.254425  0.428728 0.515151 0.0340672   -0.125392   -0.110991   30   GLN A N   
214   C  CA  . GLN A 30  ? 0.261793  0.439985 0.512614 0.0418712   -0.138043   -0.116605   30   GLN A CA  
215   C  C   . GLN A 30  ? 0.222215  0.400961 0.458139 0.045913    -0.133887   -0.10815    30   GLN A C   
216   O  O   . GLN A 30  ? 0.238079  0.414345 0.451426 0.0527794   -0.14009    -0.107888   30   GLN A O   
217   C  CB  . GLN A 30  ? 0.275475  0.463636 0.549907 0.043336    -0.150382   -0.126786   30   GLN A CB  
218   C  CG  . GLN A 30  ? 0.34222   0.530705 0.635251 0.0393436   -0.156224   -0.136867   30   GLN A CG  
219   C  CD  . GLN A 30  ? 0.403197  0.603269 0.730231 0.0372798   -0.162898   -0.144286   30   GLN A CD  
220   O  OE1 . GLN A 30  ? 0.419973  0.62244  0.774383 0.0296165   -0.157925   -0.146014   30   GLN A OE1 
221   N  NE2 . GLN A 30  ? 0.366759  0.573907 0.692249 0.0440674   -0.17328    -0.147632   30   GLN A NE2 
222   N  N   . VAL A 31  ? 0.21554   0.396742 0.463066 0.0416292   -0.123063   -0.101222   31   VAL A N   
223   C  CA  . VAL A 31  ? 0.223328  0.40535  0.459227 0.0456943   -0.119857   -0.0943348  31   VAL A CA  
224   C  C   . VAL A 31  ? 0.218209  0.390189 0.423666 0.0471559   -0.112606   -0.0859997  31   VAL A C   
225   O  O   . VAL A 31  ? 0.234857  0.404297 0.420677 0.0529667   -0.115126   -0.0826799  31   VAL A O   
226   C  CB  . VAL A 31  ? 0.211378  0.400788 0.46988  0.0420111   -0.112031   -0.0911659  31   VAL A CB  
227   C  CG1 . VAL A 31  ? 0.201117  0.390022 0.446332 0.0464937   -0.108486   -0.0843448  31   VAL A CG1 
228   C  CG2 . VAL A 31  ? 0.198065  0.398897 0.486512 0.0420968   -0.120855   -0.100025   31   VAL A CG2 
229   N  N   . LEU A 32  ? 0.230048  0.396308 0.432686 0.0418233   -0.103485   -0.0823039  32   LEU A N   
230   C  CA  . LEU A 32  ? 0.230763  0.38803  0.406992 0.0428917   -0.0977173  -0.076049   32   LEU A CA  
231   C  C   . LEU A 32  ? 0.22562   0.37891  0.380054 0.0489587   -0.106332   -0.0797384  32   LEU A C   
232   O  O   . LEU A 32  ? 0.236564  0.385928 0.369377 0.0530153   -0.104994   -0.0747353  32   LEU A O   
233   C  CB  . LEU A 32  ? 0.248742  0.401434 0.430142 0.0363722   -0.0890516  -0.073453   32   LEU A CB  
234   C  CG  . LEU A 32  ? 0.313267  0.467723 0.50655  0.0311104   -0.0778462  -0.0666759  32   LEU A CG  
235   C  CD1 . LEU A 32  ? 0.28188   0.431716 0.48193  0.0244642   -0.0693519  -0.0632763  32   LEU A CD1 
236   C  CD2 . LEU A 32  ? 0.332995  0.484848 0.507224 0.0339945   -0.0723184  -0.0591747  32   LEU A CD2 
237   N  N   . PHE A 33  ? 0.213807  0.368313 0.374072 0.0497964   -0.115457   -0.088854   33   PHE A N   
238   C  CA  . PHE A 33  ? 0.228496  0.379516 0.367547 0.055669    -0.123644   -0.0933786  33   PHE A CA  
239   C  C   . PHE A 33  ? 0.249187  0.401919 0.374513 0.0625989   -0.130006   -0.0916744  33   PHE A C   
240   O  O   . PHE A 33  ? 0.268196  0.415318 0.36809  0.0664878   -0.128286   -0.0870255  33   PHE A O   
241   C  CB  . PHE A 33  ? 0.276825  0.429307 0.42736  0.0550257   -0.132524   -0.104617   33   PHE A CB  
242   C  CG  . PHE A 33  ? 0.320852  0.471154 0.449999 0.0619249   -0.142564   -0.1109     33   PHE A CG  
243   C  CD1 . PHE A 33  ? 0.304393  0.447618 0.41275  0.0630861   -0.139113   -0.110698   33   PHE A CD1 
244   C  CD2 . PHE A 33  ? 0.317904  0.473272 0.446481 0.0676113   -0.154893   -0.11636    33   PHE A CD2 
245   C  CE1 . PHE A 33  ? 0.343839  0.485072 0.430156 0.0695967   -0.146921   -0.11582    33   PHE A CE1 
246   C  CE2 . PHE A 33  ? 0.348119  0.500856 0.45344  0.0743648   -0.163562   -0.121073   33   PHE A CE2 
247   C  CZ  . PHE A 33  ? 0.366383  0.512074 0.450408 0.075167    -0.159143   -0.120904   33   PHE A CZ  
248   N  N   . GLN A 34  ? 0.227566  0.387961 0.370289 0.0642828   -0.137354   -0.0951793  34   GLN A N   
249   C  CA  . GLN A 34  ? 0.24412   0.405573 0.374393 0.0716038   -0.145005   -0.0938488  34   GLN A CA  
250   C  C   . GLN A 34  ? 0.219727  0.375729 0.332719 0.0725779   -0.13551    -0.0827068  34   GLN A C   
251   O  O   . GLN A 34  ? 0.235469  0.387036 0.326074 0.0783885   -0.138676   -0.0791658  34   GLN A O   
252   C  CB  . GLN A 34  ? 0.263186  0.434288 0.417158 0.0734937   -0.154245   -0.0991481  34   GLN A CB  
253   C  CG  . GLN A 34  ? 0.26604   0.442891 0.445122 0.0682196   -0.145516   -0.0955304  34   GLN A CG  
254   C  CD  . GLN A 34  ? 0.271268  0.44829  0.44551  0.071614    -0.142095   -0.0879651  34   GLN A CD  
255   O  OE1 . GLN A 34  ? 0.305593  0.482566 0.469571 0.0788381   -0.151181   -0.0880199  34   GLN A OE1 
256   N  NE2 . GLN A 34  ? 0.238223  0.415007 0.419455 0.066782    -0.129302   -0.0814312  34   GLN A NE2 
257   N  N   . SER A 35  ? 0.203854  0.360144 0.327811 0.0669284   -0.124172   -0.0772951  35   SER A N   
258   C  CA  . SER A 35  ? 0.238736  0.390392 0.349803 0.0671062   -0.115007   -0.0676867  35   SER A CA  
259   C  C   . SER A 35  ? 0.231188  0.374075 0.316207 0.0674451   -0.109727   -0.0632583  35   SER A C   
260   O  O   . SER A 35  ? 0.230018  0.367977 0.295167 0.0714767   -0.109109   -0.0578862  35   SER A O   
261   C  CB  . SER A 35  ? 0.27441   0.428581 0.403143 0.0605778   -0.104348   -0.0643303  35   SER A CB  
262   O  OG  . SER A 35  ? 0.33938   0.489744 0.456952 0.0613462   -0.0968956  -0.0562203  35   SER A OG  
263   N  N   . VAL A 36  ? 0.21531   0.35624  0.301788 0.0631272   -0.10574    -0.0655116  36   VAL A N   
264   C  CA  . VAL A 36  ? 0.204462  0.338381 0.269137 0.0635693   -0.101394   -0.0629728  36   VAL A CA  
265   C  C   . VAL A 36  ? 0.212739  0.344216 0.256817 0.0701096   -0.109676   -0.0658973  36   VAL A C   
266   O  O   . VAL A 36  ? 0.217123  0.343247 0.239911 0.0725812   -0.105951   -0.0603141  36   VAL A O   
267   C  CB  . VAL A 36  ? 0.203173  0.335552 0.275179 0.0583531   -0.0966254  -0.0654982  36   VAL A CB  
268   C  CG1 . VAL A 36  ? 0.190234  0.31626  0.240875 0.0593867   -0.0923211  -0.0635503  36   VAL A CG1 
269   C  CG2 . VAL A 36  ? 0.193282  0.326442 0.28002  0.0522918   -0.0869528  -0.0601127  36   VAL A CG2 
270   N  N   . ALA A 37  ? 0.233565  0.369051 0.283789 0.0730935   -0.121091   -0.0744581  37   ALA A N   
271   C  CA  . ALA A 37  ? 0.257954  0.391098 0.287033 0.0797073   -0.129765   -0.0779399  37   ALA A CA  
272   C  C   . ALA A 37  ? 0.272862  0.403292 0.28582  0.0849808   -0.131248   -0.0708157  37   ALA A C   
273   O  O   . ALA A 37  ? 0.27525   0.399976 0.262791 0.0889734   -0.130951   -0.067674   37   ALA A O   
274   C  CB  . ALA A 37  ? 0.257784  0.396056 0.297517 0.0819766   -0.142612   -0.0891226  37   ALA A CB  
275   N  N   . ALA A 38  ? 0.264527  0.398927 0.293134 0.0849806   -0.13253    -0.0682295  38   ALA A N   
276   C  CA  . ALA A 38  ? 0.268336  0.399847 0.284988 0.0901444   -0.134636   -0.061618   38   ALA A CA  
277   C  C   . ALA A 38  ? 0.256709  0.380944 0.257811 0.0882702   -0.122602   -0.0517232  38   ALA A C   
278   O  O   . ALA A 38  ? 0.287792  0.406127 0.268253 0.0928109   -0.123489   -0.0462223  38   ALA A O   
279   C  CB  . ALA A 38  ? 0.26893   0.407003 0.30894  0.0905252   -0.1383     -0.0620209  38   ALA A CB  
280   N  N   . SER A 39  ? 0.256395  0.380746 0.266914 0.0817795   -0.111926   -0.0495117  39   SER A N   
281   C  CA  . SER A 39  ? 0.255437  0.373506 0.252697 0.0795039   -0.100798   -0.0413036  39   SER A CA  
282   C  C   . SER A 39  ? 0.252371  0.364885 0.225885 0.0811529   -0.0989882  -0.0406665  39   SER A C   
283   O  O   . SER A 39  ? 0.239679  0.34629  0.196058 0.0824514   -0.093952   -0.0337616  39   SER A O   
284   C  CB  . SER A 39  ? 0.268602  0.388378 0.280738 0.0726296   -0.0911454  -0.0399508  39   SER A CB  
285   O  OG  . SER A 39  ? 0.280082  0.403786 0.309882 0.0712616   -0.0899351  -0.0383771  39   SER A OG  
286   N  N   . TRP A 40  ? 0.257144  0.371691 0.230869 0.0809344   -0.102769   -0.048295   40   TRP A N   
287   C  CA  . TRP A 40  ? 0.266542  0.377098 0.219557 0.0827183   -0.101299   -0.0496804  40   TRP A CA  
288   C  C   . TRP A 40  ? 0.295361  0.402216 0.226283 0.0894856   -0.107436   -0.0475509  40   TRP A C   
289   O  O   . TRP A 40  ? 0.317905  0.419149 0.228483 0.090657    -0.10147    -0.0419115  40   TRP A O   
290   C  CB  . TRP A 40  ? 0.263929  0.377683 0.22454  0.0815052   -0.105314   -0.0596933  40   TRP A CB  
291   C  CG  . TRP A 40  ? 0.282554  0.39289  0.222354 0.0839674   -0.104116   -0.0625177  40   TRP A CG  
292   C  CD1 . TRP A 40  ? 0.310616  0.419719 0.231905 0.0898813   -0.111652   -0.0667398  40   TRP A CD1 
293   C  CD2 . TRP A 40  ? 0.276018  0.383849 0.210739 0.0807905   -0.0941026  -0.0610125  40   TRP A CD2 
294   N  NE1 . TRP A 40  ? 0.301366  0.407464 0.206136 0.0903919   -0.105995   -0.0679606  40   TRP A NE1 
295   C  CE2 . TRP A 40  ? 0.296096  0.401661 0.209713 0.0849465   -0.0954028  -0.0646836  40   TRP A CE2 
296   C  CE3 . TRP A 40  ? 0.26525   0.372646 0.210721 0.0751935   -0.0843432  -0.0567337  40   TRP A CE3 
297   C  CZ2 . TRP A 40  ? 0.288959  0.392527 0.193778 0.0836151   -0.0869198  -0.0648072  40   TRP A CZ2 
298   C  CZ3 . TRP A 40  ? 0.249785  0.355022 0.186598 0.0741148   -0.0771461  -0.0568727  40   TRP A CZ3 
299   C  CH2 . TRP A 40  ? 0.267629  0.371271 0.18541  0.0781777   -0.0781255  -0.060805   40   TRP A CH2 
300   N  N   . ALA A 41  ? 0.291558  0.401444 0.22715  0.0938471   -0.119033   -0.0513362  41   ALA A N   
301   C  CA  . ALA A 41  ? 0.327213  0.433323 0.24077  0.100996    -0.126653   -0.0498883  41   ALA A CA  
302   C  C   . ALA A 41  ? 0.345389  0.445028 0.247395 0.101972    -0.120367   -0.0383487  41   ALA A C   
303   O  O   . ALA A 41  ? 0.43309   0.526403 0.310732 0.106144    -0.120405   -0.0335311  41   ALA A O   
304   C  CB  . ALA A 41  ? 0.350434  0.461555 0.273448 0.105742    -0.141361   -0.0563157  41   ALA A CB  
305   N  N   . HIS A 42  ? 0.344146  0.44514  0.263891 0.0981219   -0.114987   -0.0341     42   HIS A N   
306   C  CA  . HIS A 42  ? 0.365008  0.459884 0.277522 0.0988959   -0.109725   -0.0239943  42   HIS A CA  
307   C  C   . HIS A 42  ? 0.339129  0.428647 0.238643 0.0950353   -0.0971583  -0.0183225  42   HIS A C   
308   O  O   . HIS A 42  ? 0.36186   0.444268 0.241253 0.0974471   -0.0942308  -0.0115557  42   HIS A O   
309   C  CB  . HIS A 42  ? 0.35067   0.449084 0.286702 0.0964139   -0.108261   -0.0223773  42   HIS A CB  
310   C  CG  . HIS A 42  ? 0.418119  0.509738 0.347932 0.0962135   -0.101277   -0.0127844  42   HIS A CG  
311   N  ND1 . HIS A 42  ? 0.457728  0.547423 0.390893 0.090376    -0.0893478  -0.00870224 42   HIS A ND1 
312   C  CD2 . HIS A 42  ? 0.452678  0.538115 0.372075 0.10129     -0.104805   -0.00644352 42   HIS A CD2 
313   C  CE1 . HIS A 42  ? 0.456074  0.539111 0.383011 0.0916174   -0.0859129  -0.00082814 42   HIS A CE1 
314   N  NE2 . HIS A 42  ? 0.433373  0.513347 0.352097 0.0981418   -0.0948582  0.00098711  42   HIS A NE2 
315   N  N   . ASP A 43  ? 0.332857  0.425881 0.243759 0.0892412   -0.0902474  -0.0214469  43   ASP A N   
316   C  CA  . ASP A 43  ? 0.340415  0.429741 0.2436   0.0851612   -0.0784403  -0.0166613  43   ASP A CA  
317   C  C   . ASP A 43  ? 0.361469  0.44736  0.2419   0.087335    -0.076392   -0.0169847  43   ASP A C   
318   O  O   . ASP A 43  ? 0.392747  0.474373 0.263044 0.0854041   -0.0672346  -0.0111136  43   ASP A O   
319   C  CB  . ASP A 43  ? 0.335665  0.429462 0.257438 0.0788802   -0.0723717  -0.0195699  43   ASP A CB  
320   C  CG  . ASP A 43  ? 0.374711  0.470381 0.314835 0.0758348   -0.0699714  -0.0167882  43   ASP A CG  
321   O  OD1 . ASP A 43  ? 0.35157   0.44598  0.293039 0.0788242   -0.0739224  -0.0137732  43   ASP A OD1 
322   O  OD2 . ASP A 43  ? 0.369049  0.467371 0.321819 0.0708244   -0.064405   -0.0178809  43   ASP A OD2 
323   N  N   . THR A 44  ? 0.345292  0.433255 0.218177 0.0912464   -0.0845354  -0.024114   44   THR A N   
324   C  CA  . THR A 44  ? 0.379483  0.464494 0.229483 0.0939313   -0.0827037  -0.0251867  44   THR A CA  
325   C  C   . THR A 44  ? 0.440111  0.519486 0.267945 0.100326    -0.0882587  -0.0204285  44   THR A C   
326   O  O   . THR A 44  ? 0.487419  0.564403 0.293557 0.103772    -0.0885924  -0.0219467  44   THR A O   
327   C  CB  . THR A 44  ? 0.402219  0.492165 0.255254 0.094513    -0.0876673  -0.0364791  44   THR A CB  
328   O  OG1 . THR A 44  ? 0.366093  0.459082 0.225397 0.0983414   -0.100677   -0.042013   44   THR A OG1 
329   C  CG2 . THR A 44  ? 0.351318  0.445285 0.224424 0.0883091   -0.081422   -0.0400575  44   THR A CG2 
330   N  N   . ASN A 45  ? 0.435986  0.513365 0.269098 0.102449    -0.0933977  -0.0153669  45   ASN A N   
331   C  CA  . ASN A 45  ? 0.437483  0.509119 0.250106 0.109347    -0.100695   -0.0110203  45   ASN A CA  
332   C  C   . ASN A 45  ? 0.443949  0.513231 0.267494 0.110561    -0.104015   -0.00468595 45   ASN A C   
333   O  O   . ASN A 45  ? 0.46122   0.53478  0.297351 0.113661    -0.114955   -0.00912436 45   ASN A O   
334   C  CB  . ASN A 45  ? 0.475623  0.551427 0.283415 0.114496    -0.11351    -0.0207503  45   ASN A CB  
335   C  CG  . ASN A 45  ? 0.529132  0.59961  0.315434 0.122507    -0.123451   -0.0174089  45   ASN A CG  
336   O  OD1 . ASN A 45  ? 0.56214   0.624217 0.331629 0.124382    -0.119209   -0.00689419 45   ASN A OD1 
337   N  ND2 . ASN A 45  ? 0.561029  0.6359   0.347266 0.127286    -0.13682    -0.0262852  45   ASN A ND2 
338   N  N   . ILE A 46  ? 0.434566  0.497748 0.256095 0.10777     -0.0943607  0.00479006  46   ILE A N   
339   C  CA  . ILE A 46  ? 0.450126  0.512022 0.287455 0.107436    -0.0953281  0.00938816  46   ILE A CA  
340   C  C   . ILE A 46  ? 0.478482  0.534065 0.302223 0.115143    -0.105095   0.014402    46   ILE A C   
341   O  O   . ILE A 46  ? 0.538721  0.585669 0.338388 0.117944    -0.102892   0.021579    46   ILE A O   
342   C  CB  . ILE A 46  ? 0.415055  0.472672 0.256731 0.101767    -0.0824938  0.0165792   46   ILE A CB  
343   C  CG1 . ILE A 46  ? 0.410245  0.474012 0.263878 0.0948909   -0.0740303  0.0115917   46   ILE A CG1 
344   C  CG2 . ILE A 46  ? 0.410309  0.466652 0.268879 0.10172     -0.0836439  0.020174    46   ILE A CG2 
345   C  CD1 . ILE A 46  ? 0.397886  0.458762 0.258669 0.0893867   -0.0629852  0.0172645   46   ILE A CD1 
346   N  N   . THR A 47  ? 0.523025  0.583587 0.360741 0.11901     -0.116765   0.0095975   47   THR A N   
347   C  CA  . THR A 47  ? 0.519685  0.575033 0.346795 0.12714     -0.128043   0.0135718   47   THR A CA  
348   C  C   . THR A 47  ? 0.488115  0.548507 0.34181  0.128211    -0.134163   0.01137     47   THR A C   
349   O  O   . THR A 47  ? 0.456231  0.525594 0.33391  0.123383    -0.131807   0.00474693  47   THR A O   
350   C  CB  . THR A 47  ? 0.563817  0.620554 0.373885 0.133516    -0.139973   0.00813745  47   THR A CB  
351   O  OG1 . THR A 47  ? 0.560788  0.628813 0.392307 0.133696    -0.149341   -0.00339378 47   THR A OG1 
352   C  CG2 . THR A 47  ? 0.579352  0.632658 0.363508 0.132792    -0.134042   0.00828613  47   THR A CG2 
353   N  N   . ALA A 48  ? 0.53027   0.584546 0.379788 0.134586    -0.141444   0.0173111   48   ALA A N   
354   C  CA  . ALA A 48  ? 0.509763  0.568896 0.384791 0.136563    -0.147547   0.0151004   48   ALA A CA  
355   C  C   . ALA A 48  ? 0.478716  0.550708 0.372145 0.137777    -0.158151   0.00311006  48   ALA A C   
356   O  O   . ALA A 48  ? 0.45204   0.532936 0.373345 0.134688    -0.157491   -0.00238703 48   ALA A O   
357   C  CB  . ALA A 48  ? 0.507336  0.556816 0.372145 0.144535    -0.155264   0.0234133   48   ALA A CB  
358   N  N   . GLU A 49  ? 0.476552  0.549405 0.353927 0.141964    -0.167314   -0.00112423 49   GLU A N   
359   C  CA  . GLU A 49  ? 0.523833  0.608054 0.417097 0.14357     -0.178738   -0.0128463  49   GLU A CA  
360   C  C   . GLU A 49  ? 0.488122  0.581213 0.399562 0.135088    -0.170748   -0.0207251  49   GLU A C   
361   O  O   . GLU A 49  ? 0.460963  0.564411 0.399335 0.133199    -0.174854   -0.0287726  49   GLU A O   
362   C  CB  . GLU A 49  ? 0.59497   0.676281 0.463226 0.150905    -0.191021   -0.0149422  49   GLU A CB  
363   C  CG  . GLU A 49  ? 0.71066   0.80339  0.593522 0.152737    -0.203978   -0.028161   49   GLU A CG  
364   C  CD  . GLU A 49  ? 0.797702  0.9012   0.714913 0.153722    -0.21272    -0.0348214  49   GLU A CD  
365   O  OE1 . GLU A 49  ? 0.896057  1.00759  0.822014 0.157001    -0.226041   -0.0448696  49   GLU A OE1 
366   O  OE2 . GLU A 49  ? 0.81706   0.921797 0.753905 0.150953    -0.206122   -0.0309933  49   GLU A OE2 
367   N  N   . ASN A 50  ? 0.448456  0.537526 0.345504 0.130062    -0.15947    -0.0184937  50   ASN A N   
368   C  CA  . ASN A 50  ? 0.398409  0.494411 0.312949 0.121989    -0.150984   -0.0243887  50   ASN A CA  
369   C  C   . ASN A 50  ? 0.354854  0.454055 0.294004 0.116935    -0.143017   -0.0221199  50   ASN A C   
370   O  O   . ASN A 50  ? 0.321578  0.429023 0.283067 0.111879    -0.140662   -0.0284409  50   ASN A O   
371   C  CB  . ASN A 50  ? 0.380005  0.471694 0.275162 0.118358    -0.141561   -0.0232726  50   ASN A CB  
372   C  CG  . ASN A 50  ? 0.440956  0.531828 0.315445 0.123394    -0.150347   -0.0283985  50   ASN A CG  
373   O  OD1 . ASN A 50  ? 0.451525  0.548024 0.333443 0.127487    -0.163384   -0.0360936  50   ASN A OD1 
374   N  ND2 . ASN A 50  ? 0.429756  0.514257 0.278819 0.123386    -0.143843   -0.0250115  50   ASN A ND2 
375   N  N   . ALA A 51  ? 0.354051  0.446205 0.288829 0.117557    -0.137339   -0.0129741  51   ALA A N   
376   C  CA  . ALA A 51  ? 0.334628  0.430643 0.292746 0.112622    -0.129661   -0.0124687  51   ALA A CA  
377   C  C   . ALA A 51  ? 0.365639  0.470831 0.349216 0.115243    -0.138727   -0.0186243  51   ALA A C   
378   O  O   . ALA A 51  ? 0.343636  0.456553 0.350574 0.11024     -0.133974   -0.0228219  51   ALA A O   
379   C  CB  . ALA A 51  ? 0.348529  0.435229 0.298307 0.112313    -0.121506   -0.00263131 51   ALA A CB  
380   N  N   . ARG A 52  ? 0.355399  0.460069 0.334138 0.123138    -0.15193    -0.0194075  52   ARG A N   
381   C  CA  . ARG A 52  ? 0.396989  0.511201 0.401186 0.126188    -0.161468   -0.0257733  52   ARG A CA  
382   C  C   . ARG A 52  ? 0.352775  0.478334 0.375929 0.121691    -0.163404   -0.0362929  52   ARG A C   
383   O  O   . ARG A 52  ? 0.315354  0.450067 0.366283 0.118233    -0.161302   -0.0409964  52   ARG A O   
384   C  CB  . ARG A 52  ? 0.458243  0.569123 0.451831 0.136018    -0.17616    -0.024384   52   ARG A CB  
385   C  CG  . ARG A 52  ? 0.567599  0.686943 0.588366 0.140156    -0.185111   -0.0288255  52   ARG A CG  
386   C  CD  . ARG A 52  ? 0.631359  0.749866 0.645111 0.150419    -0.202775   -0.0298451  52   ARG A CD  
387   N  NE  . ARG A 52  ? 0.717279  0.839921 0.722552 0.152725    -0.213982   -0.0374661  52   ARG A NE  
388   C  CZ  . ARG A 52  ? 0.749254  0.882394 0.77001  0.14834     -0.216026   -0.0480532  52   ARG A CZ  
389   N  NH1 . ARG A 52  ? 0.75554   0.898016 0.805161 0.141036    -0.208004   -0.0529425  52   ARG A NH1 
390   N  NH2 . ARG A 52  ? 0.778578  0.912368 0.785159 0.151341    -0.22618    -0.0538424  52   ARG A NH2 
391   N  N   . ARG A 53  ? 0.370667  0.495175 0.378538 0.121305    -0.166336   -0.0399263  53   ARG A N   
392   C  CA  . ARG A 53  ? 0.353146  0.486876 0.377682 0.117179    -0.168758   -0.050018   53   ARG A CA  
393   C  C   . ARG A 53  ? 0.313878  0.450356 0.353538 0.108155    -0.154848   -0.0497934  53   ARG A C   
394   O  O   . ARG A 53  ? 0.297764  0.443174 0.362063 0.104158    -0.155119   -0.0565409  53   ARG A O   
395   C  CB  . ARG A 53  ? 0.408063  0.539309 0.412268 0.118777    -0.174272   -0.054484   53   ARG A CB  
396   C  CG  . ARG A 53  ? 0.489301  0.620171 0.481661 0.127759    -0.19051    -0.057491   53   ARG A CG  
397   C  CD  . ARG A 53  ? 0.556881  0.686305 0.530847 0.128467    -0.194724   -0.0635859  53   ARG A CD  
398   N  NE  . ARG A 53  ? 0.753152  0.880107 0.708235 0.137662    -0.209582   -0.0651298  53   ARG A NE  
399   C  CZ  . ARG A 53  ? 0.821432  0.938685 0.74225  0.142394    -0.210125   -0.0595072  53   ARG A CZ  
400   N  NH1 . ARG A 53  ? 0.846026  0.961345 0.751817 0.151125    -0.224404   -0.0603973  53   ARG A NH1 
401   N  NH2 . ARG A 53  ? 0.806319  0.915895 0.708261 0.138649    -0.196554   -0.0526495  53   ARG A NH2 
402   N  N   . GLN A 54  ? 0.29526   0.423995 0.320353 0.104758    -0.142635   -0.0420125  54   GLN A N   
403   C  CA  . GLN A 54  ? 0.269498  0.400413 0.306749 0.0966244   -0.130319   -0.0418257  54   GLN A CA  
404   C  C   . GLN A 54  ? 0.244839  0.381473 0.306407 0.0948548   -0.12681    -0.0413953  54   GLN A C   
405   O  O   . GLN A 54  ? 0.219373  0.361996 0.299959 0.0889403   -0.120787   -0.0445005  54   GLN A O   
406   C  CB  . GLN A 54  ? 0.267429  0.388897 0.282441 0.0944653   -0.119929   -0.0340478  54   GLN A CB  
407   C  CG  . GLN A 54  ? 0.289748  0.4121   0.312215 0.086621    -0.107888   -0.0334906  54   GLN A CG  
408   C  CD  . GLN A 54  ? 0.294425  0.418805 0.332836 0.0835887   -0.100493   -0.0302642  54   GLN A CD  
409   O  OE1 . GLN A 54  ? 0.314804  0.444723 0.370903 0.0783202   -0.0954731  -0.0331402  54   GLN A OE1 
410   N  NE2 . GLN A 54  ? 0.277632  0.397347 0.310106 0.0871028   -0.0999808  -0.024492   54   GLN A NE2 
411   N  N   . GLU A 55  ? 0.270919  0.404839 0.330585 0.100074    -0.129788   -0.0369801  55   GLU A N   
412   C  CA  . GLU A 55  ? 0.279705  0.419194 0.362215 0.0992843   -0.126622   -0.0371984  55   GLU A CA  
413   C  C   . GLU A 55  ? 0.264643  0.416191 0.373648 0.0991286   -0.133908   -0.0461932  55   GLU A C   
414   O  O   . GLU A 55  ? 0.252553  0.411067 0.383253 0.0940918   -0.127027   -0.0486338  55   GLU A O   
415   C  CB  . GLU A 55  ? 0.335644  0.469616 0.412828 0.105307    -0.128874   -0.0313514  55   GLU A CB  
416   C  CG  . GLU A 55  ? 0.400848  0.524071 0.458993 0.103017    -0.118154   -0.0227534  55   GLU A CG  
417   C  CD  . GLU A 55  ? 0.488343  0.603696 0.537872 0.109434    -0.121493   -0.0164104  55   GLU A CD  
418   O  OE1 . GLU A 55  ? 0.470473  0.590992 0.537913 0.113528    -0.127292   -0.0190414  55   GLU A OE1 
419   O  OE2 . GLU A 55  ? 0.504104  0.608485 0.530932 0.110471    -0.118511   -0.0090759  55   GLU A OE2 
420   N  N   . GLU A 56  ? 0.2632    0.417352 0.370641 0.104389    -0.147526   -0.0512651  56   GLU A N   
421   C  CA  . GLU A 56  ? 0.275518  0.441697 0.410243 0.103954    -0.154986   -0.0605407  56   GLU A CA  
422   C  C   . GLU A 56  ? 0.23697   0.407733 0.383609 0.0956052   -0.148273   -0.0652787  56   GLU A C   
423   O  O   . GLU A 56  ? 0.217003  0.397389 0.391165 0.0917821   -0.146796   -0.0704989  56   GLU A O   
424   C  CB  . GLU A 56  ? 0.346001  0.514503 0.477467 0.111586    -0.172306   -0.0659464  56   GLU A CB  
425   C  CG  . GLU A 56  ? 0.522124  0.688487 0.650854 0.120099    -0.18024    -0.0621894  56   GLU A CG  
426   C  CD  . GLU A 56  ? 0.676672  0.852222 0.835292 0.122208    -0.182147   -0.0646406  56   GLU A CD  
427   O  OE1 . GLU A 56  ? 0.696584  0.883473 0.884749 0.117138    -0.178588   -0.0709817  56   GLU A OE1 
428   O  OE2 . GLU A 56  ? 0.667772  0.838789 0.82039  0.129254    -0.186948   -0.0598617  56   GLU A OE2 
429   N  N   . ALA A 57  ? 0.235954  0.399719 0.36262  0.0926547   -0.143904   -0.0634456  57   ALA A N   
430   C  CA  . ALA A 57  ? 0.227226  0.394056 0.364815 0.0851903   -0.138047   -0.0675246  57   ALA A CA  
431   C  C   . ALA A 57  ? 0.224586  0.39272  0.37485  0.0785564   -0.123785   -0.0632307  57   ALA A C   
432   O  O   . ALA A 57  ? 0.217985  0.391971 0.388522 0.0725614   -0.119311   -0.0668422  57   ALA A O   
433   C  CB  . ALA A 57  ? 0.230448  0.389391 0.343665 0.0844299   -0.137112   -0.0668898  57   ALA A CB  
434   N  N   . ALA A 58  ? 0.220096  0.382263 0.357777 0.0795779   -0.116552   -0.0554395  58   ALA A N   
435   C  CA  . ALA A 58  ? 0.226322  0.389082 0.372787 0.0737134   -0.103266   -0.0515903  58   ALA A CA  
436   C  C   . ALA A 58  ? 0.201036  0.37394  0.37576  0.073228    -0.103092   -0.0552272  58   ALA A C   
437   O  O   . ALA A 58  ? 0.210822  0.38789  0.400451 0.0672042   -0.0939851  -0.0555326  58   ALA A O   
438   C  CB  . ALA A 58  ? 0.24639   0.400357 0.373326 0.0747723   -0.0960167  -0.043385   58   ALA A CB  
439   N  N   . LEU A 59  ? 0.200362  0.377586 0.383084 0.0796861   -0.113301   -0.0581697  59   LEU A N   
440   C  CA  . LEU A 59  ? 0.191182  0.37912  0.402673 0.0798766   -0.113504   -0.0622744  59   LEU A CA  
441   C  C   . LEU A 59  ? 0.183644  0.381047 0.418739 0.0749404   -0.115327   -0.069819   59   LEU A C   
442   O  O   . LEU A 59  ? 0.174102  0.379734 0.433264 0.0704568   -0.108419   -0.0720094  59   LEU A O   
443   C  CB  . LEU A 59  ? 0.211802  0.400985 0.423401 0.0889887   -0.126637   -0.0638796  59   LEU A CB  
444   C  CG  . LEU A 59  ? 0.238779  0.429636 0.459603 0.0931466   -0.124483   -0.0614245  59   LEU A CG  
445   C  CD1 . LEU A 59  ? 0.242552  0.440318 0.478229 0.100977    -0.138872   -0.0665598  59   LEU A CD1 
446   C  CD2 . LEU A 59  ? 0.204781  0.398873 0.439255 0.0884127   -0.110068   -0.0595207  59   LEU A CD2 
447   N  N   . LEU A 60  ? 0.198831  0.395285 0.427845 0.0760791   -0.125235   -0.0743449  60   LEU A N   
448   C  CA  . LEU A 60  ? 0.212375  0.416375 0.463179 0.0709807   -0.127232   -0.0817448  60   LEU A CA  
449   C  C   . LEU A 60  ? 0.200311  0.402529 0.455325 0.0619722   -0.112725   -0.0785292  60   LEU A C   
450   O  O   . LEU A 60  ? 0.180687  0.39094  0.461653 0.0566633   -0.10834    -0.081945   60   LEU A O   
451   C  CB  . LEU A 60  ? 0.250948  0.452804 0.491734 0.0736927   -0.139826   -0.0874573  60   LEU A CB  
452   C  CG  . LEU A 60  ? 0.310372  0.519916 0.575541 0.0689885   -0.14416    -0.0965428  60   LEU A CG  
453   C  CD1 . LEU A 60  ? 0.321802  0.544419 0.62051  0.0692025   -0.147762   -0.102137   60   LEU A CD1 
454   C  CD2 . LEU A 60  ? 0.337056  0.543901 0.588267 0.0739214   -0.158697   -0.102739   60   LEU A CD2 
455   N  N   A SER A 61  ? 0.189569  0.381231 0.419228 0.0603597   -0.10578    -0.0720277  61   SER A N   
456   N  N   B SER A 61  ? 0.190974  0.382812 0.421052 0.0604096   -0.105445   -0.0718272  61   SER A N   
457   C  CA  A SER A 61  ? 0.192416  0.380874 0.422047 0.0527958   -0.0925857  -0.0678291  61   SER A CA  
458   C  CA  B SER A 61  ? 0.184474  0.373711 0.416362 0.0525943   -0.0929498  -0.0684333  61   SER A CA  
459   C  C   A SER A 61  ? 0.184219  0.378178 0.430485 0.0494702   -0.0818938  -0.0652154  61   SER A C   
460   C  C   B SER A 61  ? 0.177349  0.370884 0.422687 0.0493061   -0.0813287  -0.0648378  61   SER A C   
461   O  O   A SER A 61  ? 0.182432  0.379396 0.443504 0.0427448   -0.0737265  -0.0652911  61   SER A O   
462   O  O   B SER A 61  ? 0.171791  0.367628 0.430094 0.0425341   -0.0723828  -0.0642433  61   SER A O   
463   C  CB  A SER A 61  ? 0.192511  0.369675 0.39296  0.0528232   -0.0871396  -0.0609411  61   SER A CB  
464   C  CB  B SER A 61  ? 0.183553  0.361657 0.387489 0.0520846   -0.0888713  -0.0628935  61   SER A CB  
465   O  OG  A SER A 61  ? 0.213878  0.386426 0.399366 0.0555189   -0.0957482  -0.0637965  61   SER A OG  
466   O  OG  B SER A 61  ? 0.178508  0.354909 0.387419 0.0455567   -0.0836107  -0.0634806  61   SER A OG  
467   N  N   . GLN A 62  ? 0.173941  0.368014 0.415574 0.0542316   -0.0812405  -0.0623613  62   GLN A N   
468   C  CA  . GLN A 62  ? 0.180015  0.379676 0.436855 0.0520159   -0.0712422  -0.0607724  62   GLN A CA  
469   C  C   . GLN A 62  ? 0.154061  0.366605 0.444072 0.0501265   -0.0730175  -0.0675976  62   GLN A C   
470   O  O   . GLN A 62  ? 0.138234  0.356036 0.444159 0.0448866   -0.062272   -0.0670336  62   GLN A O   
471   C  CB  . GLN A 62  ? 0.189323  0.386355 0.436409 0.0579651   -0.0708751  -0.0573162  62   GLN A CB  
472   C  CG  . GLN A 62  ? 0.218856  0.404361 0.438409 0.0572785   -0.0640623  -0.0499451  62   GLN A CG  
473   C  CD  . GLN A 62  ? 0.221904  0.401165 0.425099 0.0643736   -0.0691828  -0.0468427  62   GLN A CD  
474   O  OE1 . GLN A 62  ? 0.187516  0.36828  0.392368 0.070388    -0.0805349  -0.049545   62   GLN A OE1 
475   N  NE2 . GLN A 62  ? 0.187534  0.358679 0.373021 0.0634738   -0.0614178  -0.0409123  62   GLN A NE2 
476   N  N   . GLU A 63  ? 0.171983  0.390088 0.472882 0.0546399   -0.0864516  -0.0741249  63   GLU A N   
477   C  CA  . GLU A 63  ? 0.190701  0.421995 0.525611 0.0527187   -0.0884119  -0.0811895  63   GLU A CA  
478   C  C   . GLU A 63  ? 0.170373  0.40369  0.519217 0.0438098   -0.0820761  -0.0828457  63   GLU A C   
479   O  O   . GLU A 63  ? 0.134818  0.376432 0.508048 0.0386145   -0.073584   -0.0842124  63   GLU A O   
480   C  CB  . GLU A 63  ? 0.259464  0.496198 0.603799 0.0585072   -0.105639   -0.0889484  63   GLU A CB  
481   C  CG  . GLU A 63  ? 0.346604  0.58671  0.692793 0.0672899   -0.113557   -0.0898332  63   GLU A CG  
482   C  CD  . GLU A 63  ? 0.429368  0.676378 0.788414 0.0725692   -0.13113    -0.0983281  63   GLU A CD  
483   O  OE1 . GLU A 63  ? 0.463786  0.723684 0.855359 0.0712224   -0.133913   -0.105478   63   GLU A OE1 
484   O  OE2 . GLU A 63  ? 0.514579  0.754036 0.850579 0.0777745   -0.141987   -0.098013   63   GLU A OE2 
485   N  N   . PHE A 64  ? 0.17507   0.399877 0.506842 0.0422795   -0.0856807  -0.0822183  64   PHE A N   
486   C  CA  . PHE A 64  ? 0.173008  0.396343 0.513063 0.0343938   -0.0806502  -0.0829335  64   PHE A CA  
487   C  C   . PHE A 64  ? 0.147413  0.367969 0.485953 0.0279738   -0.0636289  -0.0754561  64   PHE A C   
488   O  O   . PHE A 64  ? 0.133698  0.360136 0.494707 0.0216223   -0.0559506  -0.0762833  64   PHE A O   
489   C  CB  . PHE A 64  ? 0.178254  0.391887 0.49584  0.0360041   -0.0884013  -0.0835291  64   PHE A CB  
490   C  CG  . PHE A 64  ? 0.197501  0.408446 0.523749 0.0285071   -0.0845458  -0.0847528  64   PHE A CG  
491   C  CD1 . PHE A 64  ? 0.18932   0.406805 0.539826 0.0263332   -0.0925619  -0.0935159  64   PHE A CD1 
492   C  CD2 . PHE A 64  ? 0.223618  0.425227 0.534345 0.0239369   -0.0736292  -0.0773427  64   PHE A CD2 
493   C  CE1 . PHE A 64  ? 0.210159  0.424343 0.570248 0.0192831   -0.0888985  -0.0945575  64   PHE A CE1 
494   C  CE2 . PHE A 64  ? 0.247112  0.445218 0.566212 0.0174404   -0.0706642  -0.0781343  64   PHE A CE2 
495   C  CZ  . PHE A 64  ? 0.203685  0.40785  0.547914 0.0149435   -0.077851   -0.086552   64   PHE A CZ  
496   N  N   . ALA A 65  ? 0.159919  0.37188  0.472302 0.0298814   -0.0578445  -0.0682493  65   ALA A N   
497   C  CA  . ALA A 65  ? 0.151882  0.359914 0.458034 0.0245895   -0.0429604  -0.0611305  65   ALA A CA  
498   C  C   . ALA A 65  ? 0.160974  0.37897  0.489358 0.0224628   -0.0342297  -0.0617895  65   ALA A C   
499   O  O   . ALA A 65  ? 0.154527  0.373558 0.491529 0.0159012   -0.022829   -0.0588777  65   ALA A O   
500   C  CB  . ALA A 65  ? 0.176525  0.374725 0.45245  0.0278138   -0.0401017  -0.0546378  65   ALA A CB  
501   N  N   . GLU A 66  ? 0.145502  0.370825 0.483224 0.0283408   -0.0394904  -0.0655851  66   GLU A N   
502   C  CA  . GLU A 66  ? 0.150702  0.38606  0.509831 0.0270024   -0.0308922  -0.0668491  66   GLU A CA  
503   C  C   . GLU A 66  ? 0.140372  0.385993 0.53184  0.0211689   -0.0295894  -0.0720884  66   GLU A C   
504   O  O   . GLU A 66  ? 0.133015  0.384293 0.539872 0.0157323   -0.0167593  -0.0706564  66   GLU A O   
505   C  CB  . GLU A 66  ? 0.202637  0.44247  0.564076 0.0356474   -0.0391506  -0.0701825  66   GLU A CB  
506   C  CG  . GLU A 66  ? 0.238642  0.491962 0.629574 0.0359055   -0.0344498  -0.0746544  66   GLU A CG  
507   C  CD  . GLU A 66  ? 0.34397   0.603044 0.743368 0.0450295   -0.046033   -0.0795845  66   GLU A CD  
508   O  OE1 . GLU A 66  ? 0.32173   0.586466 0.731227 0.0466152   -0.0384229  -0.0799269  66   GLU A OE1 
509   O  OE2 . GLU A 66  ? 0.340666  0.598585 0.736518 0.0507453   -0.061619   -0.082923   66   GLU A OE2 
510   N  N   . ALA A 67  ? 0.137931  0.387    0.541739 0.0224293   -0.0426871  -0.0787552  67   ALA A N   
511   C  CA  . ALA A 67  ? 0.160415  0.419995 0.598253 0.0165432   -0.0412871  -0.0843353  67   ALA A CA  
512   C  C   . ALA A 67  ? 0.160329  0.414095 0.598127 0.00708627  -0.0298305  -0.0793933  67   ALA A C   
513   O  O   . ALA A 67  ? 0.152633  0.413147 0.612445 0.00065245  -0.0187445  -0.0789179  67   ALA A O   
514   C  CB  . ALA A 67  ? 0.164352  0.429602 0.617538 0.0198278   -0.0582402  -0.0935704  67   ALA A CB  
515   N  N   . TRP A 68  ? 0.1532    0.394168 0.565988 0.00642848  -0.0321081  -0.0753525  68   TRP A N   
516   C  CA  . TRP A 68  ? 0.163715  0.39812  0.576884 -0.00178035 -0.0235216  -0.0709505  68   TRP A CA  
517   C  C   . TRP A 68  ? 0.174969  0.404968 0.575241 -0.00530346 -0.007104   -0.0617144  68   TRP A C   
518   O  O   . TRP A 68  ? 0.187524  0.418556 0.600861 -0.0126885  0.00413372  -0.0585101  68   TRP A O   
519   C  CB  . TRP A 68  ? 0.144306  0.367052 0.536375 -0.00054311 -0.0321081  -0.0705663  68   TRP A CB  
520   C  CG  . TRP A 68  ? 0.146096  0.373728 0.557103 8.125e-05   -0.0456088  -0.080217   68   TRP A CG  
521   C  CD1 . TRP A 68  ? 0.141829  0.372913 0.550958 0.00733635  -0.0607289  -0.0873984  68   TRP A CD1 
522   C  CD2 . TRP A 68  ? 0.13959   0.36798  0.572969 -0.00698901 -0.0454047  -0.0836549  68   TRP A CD2 
523   N  NE1 . TRP A 68  ? 0.149664  0.384177 0.578102 0.00544451  -0.0703429  -0.0957546  68   TRP A NE1 
524   C  CE2 . TRP A 68  ? 0.14695   0.379547 0.590813 -0.00341957 -0.061331   -0.0938304  68   TRP A CE2 
525   C  CE3 . TRP A 68  ? 0.144946  0.369561 0.588584 -0.0158173  -0.0336205  -0.0787536  68   TRP A CE3 
526   C  CZ2 . TRP A 68  ? 0.151765  0.385946 0.618919 -0.00868571 -0.0658179  -0.100286   68   TRP A CZ2 
527   C  CZ3 . TRP A 68  ? 0.147519  0.373188 0.614839 -0.0212649  -0.0375084  -0.0843002  68   TRP A CZ3 
528   C  CH2 . TRP A 68  ? 0.151304  0.381589 0.63023  -0.0177846  -0.0534905  -0.0952361  68   TRP A CH2 
529   N  N   . GLY A 69  ? 0.17099   0.396859 0.547167 0.00023242  -0.00600151 -0.057965   69   GLY A N   
530   C  CA  . GLY A 69  ? 0.16787   0.391578 0.531828 -0.00112603 0.00782277  -0.0510881  69   GLY A CA  
531   C  C   . GLY A 69  ? 0.183259  0.418334 0.571517 -0.00456543 0.0190432   -0.0522121  69   GLY A C   
532   O  O   . GLY A 69  ? 0.201452  0.434824 0.589651 -0.0106569  0.032599    -0.0466542  69   GLY A O   
533   N  N   . GLN A 70  ? 0.206601  0.453641 0.615879 -0.0004871  0.0140487   -0.0592854  70   GLN A N   
534   C  CA  . GLN A 70  ? 0.208781  0.467684 0.642745 -0.00358036 0.025401    -0.0609653  70   GLN A CA  
535   C  C   . GLN A 70  ? 0.207406  0.471995 0.668971 -0.0120056  0.0305441   -0.0623778  70   GLN A C   
536   O  O   . GLN A 70  ? 0.214284  0.486147 0.692317 -0.0169017  0.0441853   -0.0611355  70   GLN A O   
537   C  CB  . GLN A 70  ? 0.291322  0.563542 0.748242 0.00226768  0.018547    -0.0692413  70   GLN A CB  
538   C  CG  . GLN A 70  ? 0.418029  0.685437 0.852682 0.0114548   0.0107373   -0.0691091  70   GLN A CG  
539   C  CD  . GLN A 70  ? 0.49608   0.776167 0.952801 0.0171035   0.00780629  -0.0757678  70   GLN A CD  
540   O  OE1 . GLN A 70  ? 0.548534  0.830697 1.00802  0.0242282   -0.00669737 -0.0806136  70   GLN A OE1 
541   N  NE2 . GLN A 70  ? 0.500547  0.789318 0.973613 0.0139302   0.0218898   -0.0760296  70   GLN A NE2 
542   N  N   . LYS A 71  ? 0.200557  0.463183 0.670181 -0.0133936  0.0193595   -0.0660712  71   LYS A N   
543   C  CA  . LYS A 71  ? 0.198597  0.464304 0.693227 -0.0221245  0.0243643   -0.0667989  71   LYS A CA  
544   C  C   . LYS A 71  ? 0.221499  0.475492 0.698656 -0.0289504  0.0378331   -0.0564705  71   LYS A C   
545   O  O   . LYS A 71  ? 0.239065  0.496815 0.733409 -0.036383   0.0508948   -0.0535423  71   LYS A O   
546   C  CB  . LYS A 71  ? 0.173382  0.43872  0.680067 -0.0220106  0.00883788  -0.0738148  71   LYS A CB  
547   C  CG  . LYS A 71  ? 0.158039  0.427665 0.69613  -0.0311413  0.0127919   -0.0761559  71   LYS A CG  
548   C  CD  . LYS A 71  ? 0.161554  0.447684 0.738132 -0.035035   0.02        -0.0809669  71   LYS A CD  
549   C  CE  . LYS A 71  ? 0.141524  0.440458 0.736028 -0.0278405  0.00621523  -0.0915204  71   LYS A CE  
550   N  NZ  . LYS A 71  ? 0.130633  0.445738 0.760952 -0.0314114  0.0154417   -0.0953113  71   LYS A NZ  
551   N  N   . ALA A 72  ? 0.233717  0.473799 0.678117 -0.0263688  0.0340746   -0.0511867  72   ALA A N   
552   C  CA  . ALA A 72  ? 0.258149  0.486046 0.682554 -0.031446   0.0448804   -0.0411696  72   ALA A CA  
553   C  C   . ALA A 72  ? 0.260024  0.491211 0.680754 -0.0335687  0.0615003   -0.0355475  72   ALA A C   
554   O  O   . ALA A 72  ? 0.269518  0.500353 0.699107 -0.040853   0.0742027   -0.0304743  72   ALA A O   
555   C  CB  . ALA A 72  ? 0.235415  0.450153 0.626522 -0.0268845  0.0373982   -0.0376586  72   ALA A CB  
556   N  N   . LYS A 73  ? 0.32312   0.559656 0.736469 -0.0273763  0.0616158   -0.0377756  73   LYS A N   
557   C  CA  . LYS A 73  ? 0.336728  0.579154 0.752101 -0.0290167  0.0770221   -0.034974   73   LYS A CA  
558   C  C   . LYS A 73  ? 0.384128  0.63806  0.833225 -0.0357682  0.087122    -0.0370001  73   LYS A C   
559   O  O   . LYS A 73  ? 0.474331  0.725094 0.922054 -0.0425717  0.101185    -0.0300523  73   LYS A O   
560   C  CB  . LYS A 73  ? 0.390842  0.638312 0.798171 -0.021117   0.0749956   -0.0386718  73   LYS A CB  
561   C  CG  . LYS A 73  ? 0.395578  0.629722 0.766944 -0.0164794  0.069208    -0.0342354  73   LYS A CG  
562   C  CD  . LYS A 73  ? 0.371778  0.608223 0.731253 -0.0117991  0.0754556   -0.0342834  73   LYS A CD  
563   C  CE  . LYS A 73  ? 0.387856  0.615614 0.722813 -0.0052735  0.0644634   -0.0340237  73   LYS A CE  
564   N  NZ  . LYS A 73  ? 0.530014  0.758934 0.853891 -0.00200083 0.0723979   -0.0335654  73   LYS A NZ  
565   N  N   . GLU A 74  ? 0.370375  0.637562 0.849496 -0.0338036  0.0799553   -0.0463018  74   GLU A N   
566   C  CA  . GLU A 74  ? 0.334161  0.615598 0.849472 -0.0390559  0.0891053   -0.0501254  74   GLU A CA  
567   C  C   . GLU A 74  ? 0.300897  0.577594 0.825333 -0.0494436  0.099501    -0.0439032  74   GLU A C   
568   O  O   . GLU A 74  ? 0.259558  0.542286 0.797748 -0.0552587  0.11531     -0.0410475  74   GLU A O   
569   C  CB  . GLU A 74  ? 0.315166  0.608216 0.85818  -0.0347297  0.0737301   -0.0613805  74   GLU A CB  
570   C  CG  . GLU A 74  ? 0.366642  0.674775 0.953474 -0.0406731  0.0782327   -0.0673366  74   GLU A CG  
571   C  CD  . GLU A 74  ? 0.346334  0.663851 0.961918 -0.0382423  0.0610005   -0.0782706  74   GLU A CD  
572   O  OE1 . GLU A 74  ? 0.31309   0.627029 0.91613  -0.0305992  0.04367     -0.0825585  74   GLU A OE1 
573   O  OE2 . GLU A 74  ? 0.322031  0.650424 0.973601 -0.0446235  0.065284    -0.0824443  74   GLU A OE2 
574   N  N   . LEU A 75  ? 0.330783  0.595971 0.84674  -0.0517032  0.0911035   -0.0414897  75   LEU A N   
575   C  CA  . LEU A 75  ? 0.342883  0.603    0.871479 -0.0613976  0.0987179   -0.0364198  75   LEU A CA  
576   C  C   . LEU A 75  ? 0.352535  0.597263 0.850514 -0.0649922  0.109965    -0.0237841  75   LEU A C   
577   O  O   . LEU A 75  ? 0.344196  0.584893 0.85105  -0.0733398  0.120813    -0.017462   75   LEU A O   
578   C  CB  . LEU A 75  ? 0.328326  0.584184 0.867014 -0.0617911  0.0827618   -0.041692   75   LEU A CB  
579   C  CG  . LEU A 75  ? 0.296772  0.567094 0.869077 -0.0595838  0.0704817   -0.054345   75   LEU A CG  
580   C  CD1 . LEU A 75  ? 0.292882  0.554733 0.863597 -0.0591492  0.0547816   -0.0581439  75   LEU A CD1 
581   C  CD2 . LEU A 75  ? 0.318873  0.602406 0.930288 -0.0671615  0.0814016   -0.0568895  75   LEU A CD2 
582   N  N   . TYR A 76  ? 0.372419  0.607633 0.834731 -0.0589015  0.106596    -0.019852   76   TYR A N   
583   C  CA  . TYR A 76  ? 0.38825   0.607339 0.822715 -0.0617859  0.112155    -0.00895833 76   TYR A CA  
584   C  C   . TYR A 76  ? 0.465303  0.680104 0.86742  -0.0574971  0.119321    -0.00338931 76   TYR A C   
585   O  O   . TYR A 76  ? 0.455487  0.656797 0.829405 -0.057117   0.119559    0.0041996   76   TYR A O   
586   C  CB  . TYR A 76  ? 0.376124  0.584159 0.798169 -0.0589438  0.0964821   -0.0101127  76   TYR A CB  
587   C  CG  . TYR A 76  ? 0.330306  0.54131  0.781466 -0.0622582  0.0870896   -0.0168895  76   TYR A CG  
588   C  CD1 . TYR A 76  ? 0.328155  0.541445 0.80615  -0.0711824  0.0959656   -0.0150588  76   TYR A CD1 
589   C  CD2 . TYR A 76  ? 0.302731  0.514104 0.754096 -0.0564895  0.0695748   -0.0252331  76   TYR A CD2 
590   C  CE1 . TYR A 76  ? 0.318529  0.534886 0.825127 -0.0744866  0.087182    -0.0221531  76   TYR A CE1 
591   C  CE2 . TYR A 76  ? 0.308338  0.522648 0.785882 -0.0592412  0.0604113   -0.0324402  76   TYR A CE2 
592   C  CZ  . TYR A 76  ? 0.316179  0.532998 0.821942 -0.0682893  0.068942    -0.0311943  76   TYR A CZ  
593   O  OH  . TYR A 76  ? 0.305239  0.524884 0.838574 -0.07148    0.0599279   -0.0388635  76   TYR A OH  
594   N  N   . GLU A 77  ? 0.603476  0.829601 1.01019  -0.0542791  0.125239    -0.00736085 77   GLU A N   
595   C  CA  . GLU A 77  ? 0.682582  0.905165 1.05931  -0.0483947  0.127734    -0.00506773 77   GLU A CA  
596   C  C   . GLU A 77  ? 0.732108  0.943029 1.08294  -0.0522929  0.139766    0.00619861  77   GLU A C   
597   O  O   . GLU A 77  ? 0.756571  0.956195 1.07742  -0.0487377  0.134861    0.010383    77   GLU A O   
598   C  CB  . GLU A 77  ? 0.641608  0.877274 1.02679  -0.0437963  0.132062    -0.0115611  77   GLU A CB  
599   C  CG  . GLU A 77  ? 0.623571  0.853963 0.977548 -0.0368296  0.130789    -0.0106491  77   GLU A CG  
600   C  CD  . GLU A 77  ? 0.608487  0.826746 0.934809 -0.0315859  0.11754     -0.00910809 77   GLU A CD  
601   O  OE1 . GLU A 77  ? 0.693093  0.904782 1.01903  -0.0323241  0.107082    -0.00847322 77   GLU A OE1 
602   O  OE2 . GLU A 77  ? 0.569863  0.785179 0.874357 -0.0265752  0.118039    -0.00884266 77   GLU A OE2 
603   N  N   . PRO A 78  ? 0.701214  0.914349 1.06261  -0.0596029  0.155533    0.0115757   78   PRO A N   
604   C  CA  . PRO A 78  ? 0.753871  0.954699 1.08983  -0.0634421  0.166463    0.023261    78   PRO A CA  
605   C  C   . PRO A 78  ? 0.69794   0.883971 1.02523  -0.0664605  0.159476    0.0299206   78   PRO A C   
606   O  O   . PRO A 78  ? 0.732984  0.907409 1.03289  -0.0625331  0.151633    0.0334476   78   PRO A O   
607   C  CB  . PRO A 78  ? 0.710411  0.919654 1.06669  -0.0707807  0.184873    0.0260145   78   PRO A CB  
608   C  CG  . PRO A 78  ? 0.738771  0.966202 1.12589  -0.0684929  0.18368     0.0144566   78   PRO A CG  
609   C  CD  . PRO A 78  ? 0.756331  0.983851 1.15424  -0.0644421  0.163801    0.00695746  78   PRO A CD  
610   N  N   . ILE A 79  ? 0.619114  0.806775 0.973607 -0.0734787  0.162165    0.0305581   79   ILE A N   
611   C  CA  . ILE A 79  ? 0.590653  0.766162 0.94779  -0.0792898  0.161047    0.0374601   79   ILE A CA  
612   C  C   . ILE A 79  ? 0.522955  0.687086 0.864585 -0.0747569  0.144351    0.0366181   79   ILE A C   
613   O  O   . ILE A 79  ? 0.479386  0.631397 0.819077 -0.0785962  0.142774    0.0427748   79   ILE A O   
614   C  CB  . ILE A 79  ? 0.623725  0.809061 1.02238  -0.085805   0.163083    0.0323138   79   ILE A CB  
615   C  CG1 . ILE A 79  ? 0.604362  0.793885 1.02119  -0.0822816  0.144631    0.0212483   79   ILE A CG1 
616   C  CG2 . ILE A 79  ? 0.593823  0.795277 1.01051  -0.0874991  0.176407    0.0288086   79   ILE A CG2 
617   C  CD1 . ILE A 79  ? 0.556722  0.761497 1.01529  -0.085884   0.144337    0.0120862   79   ILE A CD1 
618   N  N   . TRP A 80  ? 0.478346  0.646386 0.81116  -0.0667985  0.132005    0.028792    80   TRP A N   
619   C  CA  . TRP A 80  ? 0.476374  0.635413 0.798426 -0.0627975  0.116572    0.0268091   80   TRP A CA  
620   C  C   . TRP A 80  ? 0.486693  0.630772 0.775538 -0.0615243  0.117964    0.0365837   80   TRP A C   
621   O  O   . TRP A 80  ? 0.447083  0.580579 0.728305 -0.0607487  0.109164    0.0383755   80   TRP A O   
622   C  CB  . TRP A 80  ? 0.461653  0.628213 0.782453 -0.0548504  0.103539    0.0166286   80   TRP A CB  
623   C  CG  . TRP A 80  ? 0.487147  0.652756 0.779895 -0.0481835  0.103117    0.017344    80   TRP A CG  
624   C  CD1 . TRP A 80  ? 0.506273  0.681288 0.798087 -0.0455572  0.10959     0.0146735   80   TRP A CD1 
625   C  CD2 . TRP A 80  ? 0.45094   0.606126 0.714924 -0.0432043  0.0953005   0.0199241   80   TRP A CD2 
626   N  NE1 . TRP A 80  ? 0.471717  0.642251 0.736195 -0.0395267  0.106119    0.0154158   80   TRP A NE1 
627   C  CE2 . TRP A 80  ? 0.46781   0.626564 0.715073 -0.0381525  0.097577    0.0187584   80   TRP A CE2 
628   C  CE3 . TRP A 80  ? 0.451043  0.594497 0.702925 -0.0425297  0.0869218   0.0227747   80   TRP A CE3 
629   C  CZ2 . TRP A 80  ? 0.466097  0.617266 0.686042 -0.0329735  0.0916363   0.0204222   80   TRP A CZ2 
630   C  CZ3 . TRP A 80  ? 0.418451  0.555092 0.643546 -0.0372002  0.0814101   0.0244486   80   TRP A CZ3 
631   C  CH2 . TRP A 80  ? 0.476484  0.617123 0.686188 -0.0326559  0.0836599   0.0232666   80   TRP A CH2 
632   N  N   . GLN A 81  ? 0.450174  0.593945 0.71989  -0.061044   0.128977    0.0423189   81   GLN A N   
633   C  CA  . GLN A 81  ? 0.503312  0.634309 0.740247 -0.0588076  0.129382    0.0506596   81   GLN A CA  
634   C  C   . GLN A 81  ? 0.459358  0.578401 0.694316 -0.065241   0.136583    0.061604    81   GLN A C   
635   O  O   . GLN A 81  ? 0.483645  0.590224 0.695314 -0.0634518  0.133457    0.0683624   81   GLN A O   
636   C  CB  . GLN A 81  ? 0.524055  0.65907  0.741258 -0.0557804  0.137888    0.051948    81   GLN A CB  
637   C  CG  . GLN A 81  ? 0.562525  0.70263  0.770245 -0.0479374  0.127741    0.0436849   81   GLN A CG  
638   C  CD  . GLN A 81  ? 0.596322  0.743851 0.794556 -0.045419   0.136521    0.0418997   81   GLN A CD  
639   O  OE1 . GLN A 81  ? 0.577211  0.726386 0.762486 -0.0392646  0.130254    0.0371673   81   GLN A OE1 
640   N  NE2 . GLN A 81  ? 0.631875  0.783606 0.836638 -0.0502258  0.151413    0.045581    81   GLN A NE2 
641   N  N   . GLN A 82  ? 0.44533   0.568394 0.706135 -0.0724666  0.145424    0.0628909   82   GLN A N   
642   C  CA  . GLN A 82  ? 0.458465  0.570651 0.720892 -0.0795761  0.154385    0.0738386   82   GLN A CA  
643   C  C   . GLN A 82  ? 0.413728  0.519928 0.697603 -0.0829497  0.14561     0.0721133   82   GLN A C   
644   O  O   . GLN A 82  ? 0.380232  0.476113 0.668666 -0.0889872  0.151432    0.0807769   82   GLN A O   
645   C  CB  . GLN A 82  ? 0.487508  0.606932 0.760279 -0.0856319  0.172523    0.0779668   82   GLN A CB  
646   C  CG  . GLN A 82  ? 0.539323  0.655454 0.780245 -0.0835654  0.183002    0.0855322   82   GLN A CG  
647   C  CD  . GLN A 82  ? 0.552394  0.682534 0.790235 -0.0786003  0.185233    0.0771622   82   GLN A CD  
648   O  OE1 . GLN A 82  ? 0.605605  0.741351 0.843529 -0.0722445  0.172992    0.0677419   82   GLN A OE1 
649   N  NE2 . GLN A 82  ? 0.609162  0.744999 0.845167 -0.0815993  0.201554    0.0805572   82   GLN A NE2 
650   N  N   . PHE A 83  ? 0.405971  0.51799  0.702614 -0.0789421  0.131421    0.0608767   83   PHE A N   
651   C  CA  . PHE A 83  ? 0.392726  0.498905 0.708327 -0.081418   0.121942    0.0578109   83   PHE A CA  
652   C  C   . PHE A 83  ? 0.387358  0.475032 0.684632 -0.0816971  0.119297    0.0672672   83   PHE A C   
653   O  O   . PHE A 83  ? 0.40177   0.482365 0.670652 -0.0760379  0.114766    0.0706031   83   PHE A O   
654   C  CB  . PHE A 83  ? 0.35742   0.471067 0.684507 -0.0761573  0.106021    0.0444766   83   PHE A CB  
655   C  CG  . PHE A 83  ? 0.328131  0.459233 0.680613 -0.0759469  0.104791    0.0336198   83   PHE A CG  
656   C  CD1 . PHE A 83  ? 0.34331   0.483621 0.718159 -0.0822516  0.117499    0.0345855   83   PHE A CD1 
657   C  CD2 . PHE A 83  ? 0.309425  0.447753 0.662743 -0.0691147  0.0910759   0.0227213   83   PHE A CD2 
658   C  CE1 . PHE A 83  ? 0.360046  0.516984 0.759548 -0.0815768  0.115909    0.0243461   83   PHE A CE1 
659   C  CE2 . PHE A 83  ? 0.328605  0.482502 0.70489  -0.068355   0.0891769   0.0131762   83   PHE A CE2 
660   C  CZ  . PHE A 83  ? 0.342483  0.505981 0.74178  -0.0742616  0.101316    0.0137924   83   PHE A CZ  
661   N  N   . THR A 84  ? 0.39867   0.47871  0.715073 -0.0881158  0.120791    0.0705247   84   THR A N   
662   C  CA  . THR A 84  ? 0.434274  0.496288 0.738107 -0.088546   0.117561    0.0789558   84   THR A CA  
663   C  C   . THR A 84  ? 0.397598  0.456078 0.693744 -0.0814445  0.100687    0.0712251   84   THR A C   
664   O  O   . THR A 84  ? 0.381359  0.426478 0.657831 -0.0785539  0.0965332   0.0774398   84   THR A O   
665   C  CB  . THR A 84  ? 0.45132   0.506577 0.781018 -0.0977005  0.124118    0.0838034   84   THR A CB  
666   O  OG1 . THR A 84  ? 0.514404  0.572387 0.841618 -0.102927   0.14129     0.0928454   84   THR A OG1 
667   C  CG2 . THR A 84  ? 0.472349  0.508456 0.796358 -0.0986394  0.119485    0.0911761   84   THR A CG2 
668   N  N   . ASP A 85  ? 0.338338  0.408627 0.650542 -0.0786307  0.0910734   0.0577974   85   ASP A N   
669   C  CA  . ASP A 85  ? 0.301867  0.368965 0.60992  -0.0726919  0.0757331   0.0498408   85   ASP A CA  
670   C  C   . ASP A 85  ? 0.276606  0.347617 0.557446 -0.0646482  0.0713801   0.0481018   85   ASP A C   
671   O  O   . ASP A 85  ? 0.264752  0.348815 0.548602 -0.0620531  0.0704225   0.0410859   85   ASP A O   
672   C  CB  . ASP A 85  ? 0.286382  0.362518 0.622124 -0.0731534  0.0665183   0.0365904   85   ASP A CB  
673   C  CG  . ASP A 85  ? 0.289227  0.36167  0.621773 -0.067437   0.0511574   0.0278141   85   ASP A CG  
674   O  OD1 . ASP A 85  ? 0.267721  0.335546 0.575752 -0.0612491  0.0462096   0.0290879   85   ASP A OD1 
675   O  OD2 . ASP A 85  ? 0.338443  0.412983 0.694053 -0.0692256  0.0440049   0.0190035   85   ASP A OD2 
676   N  N   . PRO A 86  ? 0.287207  0.347723 0.543104 -0.06013    0.0673317   0.0531447   86   PRO A N   
677   C  CA  . PRO A 86  ? 0.289385  0.354218 0.520742 -0.0531761  0.0642957   0.0516828   86   PRO A CA  
678   C  C   . PRO A 86  ? 0.270311  0.344616 0.506584 -0.0479068  0.0531545   0.0392195   86   PRO A C   
679   O  O   . PRO A 86  ? 0.272089  0.35446  0.49759  -0.0437711  0.0526118   0.0361064   86   PRO A O   
680   C  CB  . PRO A 86  ? 0.287572  0.33846  0.495418 -0.0498519  0.0609804   0.0591637   86   PRO A CB  
681   C  CG  . PRO A 86  ? 0.30068   0.340648 0.523958 -0.0533045  0.0575791   0.0605528   86   PRO A CG  
682   C  CD  . PRO A 86  ? 0.283247  0.327851 0.534842 -0.0609647  0.0643962   0.059416    86   PRO A CD  
683   N  N   . GLN A 87  ? 0.260428  0.332226 0.510019 -0.0474475  0.0437286   0.03246     87   GLN A N   
684   C  CA  . GLN A 87  ? 0.243423  0.323138 0.495502 -0.0421911  0.0328737   0.021       87   GLN A CA  
685   C  C   . GLN A 87  ? 0.254466  0.348343 0.52387  -0.0433486  0.0341779   0.0142657   87   GLN A C   
686   O  O   . GLN A 87  ? 0.250155  0.352131 0.512216 -0.0381183  0.0293465   0.00849896  87   GLN A O   
687   C  CB  . GLN A 87  ? 0.290564  0.364424 0.553726 -0.0416988  0.0230164   0.0146966   87   GLN A CB  
688   C  CG  . GLN A 87  ? 0.380262  0.441726 0.625675 -0.0384654  0.0193752   0.0190123   87   GLN A CG  
689   C  CD  . GLN A 87  ? 0.552639  0.609769 0.809172 -0.0370581  0.00920311  0.0107196   87   GLN A CD  
690   O  OE1 . GLN A 87  ? 0.703552  0.768299 0.974944 -0.0366407  0.00299618  0.0005      87   GLN A OE1 
691   N  NE2 . GLN A 87  ? 0.579445  0.624341 0.829585 -0.0361152  0.00705384  0.0145465   87   GLN A NE2 
692   N  N   . LEU A 88  ? 0.242587  0.339124 0.535211 -0.0500997  0.0407576   0.0153051   88   LEU A N   
693   C  CA  . LEU A 88  ? 0.2411    0.351551 0.55301  -0.0518955  0.0436877   0.00984419  88   LEU A CA  
694   C  C   . LEU A 88  ? 0.261553  0.37865  0.558457 -0.0496642  0.0517852   0.0136907   88   LEU A C   
695   O  O   . LEU A 88  ? 0.227122  0.355717 0.528847 -0.0462967  0.0489636   0.00688027  88   LEU A O   
696   C  CB  . LEU A 88  ? 0.217383  0.328174 0.557271 -0.060379   0.0507232   0.0115173   88   LEU A CB  
697   C  CG  . LEU A 88  ? 0.228749  0.354974 0.593104 -0.0626212  0.0536789   0.00511478  88   LEU A CG  
698   C  CD1 . LEU A 88  ? 0.21586   0.350036 0.586793 -0.0567463  0.0387738   -0.00774639 88   LEU A CD1 
699   C  CD2 . LEU A 88  ? 0.234276  0.361298 0.628744 -0.0717421  0.0613864   0.00671861  88   LEU A CD2 
700   N  N   . ARG A 89  ? 0.270639  0.380346 0.548486 -0.0510008  0.0613435   0.0242946   89   ARG A N   
701   C  CA  . ARG A 89  ? 0.284708  0.40071  0.547149 -0.0479993  0.067475    0.0261359   89   ARG A CA  
702   C  C   . ARG A 89  ? 0.257635  0.375957 0.503305 -0.0399929  0.057158    0.0202893   89   ARG A C   
703   O  O   . ARG A 89  ? 0.231208  0.358434 0.474078 -0.036377   0.0571114   0.016234    89   ARG A O   
704   C  CB  . ARG A 89  ? 0.338122  0.445097 0.578168 -0.049416   0.0772818   0.0376181   89   ARG A CB  
705   C  CG  . ARG A 89  ? 0.361998  0.466584 0.613196 -0.0571005  0.0902807   0.0453916   89   ARG A CG  
706   C  CD  . ARG A 89  ? 0.413859  0.511904 0.639603 -0.0573832  0.100569    0.0560397   89   ARG A CD  
707   N  NE  . ARG A 89  ? 0.420558  0.50574  0.622248 -0.0538859  0.0944656   0.0613983   89   ARG A NE  
708   C  CZ  . ARG A 89  ? 0.440881  0.512839 0.639161 -0.0564374  0.0941168   0.0689621   89   ARG A CZ  
709   N  NH1 . ARG A 89  ? 0.432709  0.495129 0.606771 -0.0520717  0.089095    0.0734396   89   ARG A NH1 
710   N  NH2 . ARG A 89  ? 0.405577  0.473751 0.624235 -0.0632014  0.0990854   0.0723463   89   ARG A NH2 
711   N  N   . ARG A 90  ? 0.242997  0.352789 0.47682  -0.0369026  0.0483555   0.0199251   90   ARG A N   
712   C  CA  . ARG A 90  ? 0.222654  0.334292 0.439253 -0.0297884  0.0403686   0.0155674   90   ARG A CA  
713   C  C   . ARG A 90  ? 0.227635  0.349421 0.459081 -0.0269196  0.0321318   0.00513568  90   ARG A C   
714   O  O   . ARG A 90  ? 0.199204  0.326578 0.421578 -0.0218801  0.0290183   0.00166348  90   ARG A O   
715   C  CB  . ARG A 90  ? 0.224486  0.325885 0.426209 -0.0268542  0.0330213   0.0167566   90   ARG A CB  
716   C  CG  . ARG A 90  ? 0.280291  0.372002 0.462809 -0.0276731  0.0390551   0.0267454   90   ARG A CG  
717   C  CD  . ARG A 90  ? 0.312302  0.393335 0.484017 -0.0253473  0.0323116   0.0284774   90   ARG A CD  
718   N  NE  . ARG A 90  ? 0.395014  0.471138 0.543563 -0.0233632  0.0360414   0.0356935   90   ARG A NE  
719   C  CZ  . ARG A 90  ? 0.404628  0.481428 0.535616 -0.01818    0.031932    0.0342492   90   ARG A CZ  
720   N  NH1 . ARG A 90  ? 0.454543  0.528022 0.566931 -0.0171098  0.0360311   0.0404388   90   ARG A NH1 
721   N  NH2 . ARG A 90  ? 0.343062  0.424144 0.474679 -0.0141125  0.0240182   0.0265788   90   ARG A NH2 
722   N  N   . ILE A 91  ? 0.206216  0.329732 0.460441 -0.0300419  0.0281232   0.00018599  91   ILE A N   
723   C  CA  . ILE A 91  ? 0.221084  0.353682 0.488959 -0.0270255  0.0189194   -0.0099507  91   ILE A CA  
724   C  C   . ILE A 91  ? 0.242333  0.386752 0.52167  -0.0272332  0.0240701   -0.0118794  91   ILE A C   
725   O  O   . ILE A 91  ? 0.208134  0.35901  0.483217 -0.0217607  0.0184452   -0.0169128  91   ILE A O   
726   C  CB  . ILE A 91  ? 0.216711  0.348531 0.506959 -0.030377   0.0129469   -0.015593   91   ILE A CB  
727   C  CG1 . ILE A 91  ? 0.2215    0.341765 0.500822 -0.0290743  0.00658136  -0.0153287  91   ILE A CG1 
728   C  CG2 . ILE A 91  ? 0.21137   0.354437 0.517772 -0.0274934  0.0039857   -0.0262048  91   ILE A CG2 
729   C  CD1 . ILE A 91  ? 0.23847   0.355408 0.54036  -0.0336533  0.00286205  -0.019467   91   ILE A CD1 
730   N  N   . ILE A 92  ? 0.233378  0.379986 0.526267 -0.0333808  0.0352596   -0.00737128 92   ILE A N   
731   C  CA  . ILE A 92  ? 0.233363  0.391834 0.539285 -0.0338723  0.0415576   -0.00940613 92   ILE A CA  
732   C  C   . ILE A 92  ? 0.214591  0.374112 0.498183 -0.0287471  0.0444417   -0.00704156 92   ILE A C   
733   O  O   . ILE A 92  ? 0.214413  0.383422 0.503652 -0.0252786  0.0434086   -0.0118293  92   ILE A O   
734   C  CB  . ILE A 92  ? 0.250459  0.410903 0.573616 -0.0417084  0.05483     -0.00437164 92   ILE A CB  
735   C  CG1 . ILE A 92  ? 0.230116  0.390514 0.580571 -0.0475324  0.0522244   -0.00755139 92   ILE A CG1 
736   C  CG2 . ILE A 92  ? 0.286047  0.458724 0.619125 -0.041701   0.0634774   -0.00580241 92   ILE A CG2 
737   C  CD1 . ILE A 92  ? 0.228255  0.399144 0.602022 -0.0453886  0.0409148   -0.019287   92   ILE A CD1 
738   N  N   . GLY A 93  ? 0.225888  0.375691 0.485717 -0.0287413  0.0491486   0.00071794  93   GLY A N   
739   C  CA  . GLY A 93  ? 0.228917  0.378425 0.466669 -0.0244793  0.0523637   0.00326461  93   GLY A CA  
740   C  C   . GLY A 93  ? 0.204883  0.357263 0.435041 -0.0173893  0.041563    -0.00305799 93   GLY A C   
741   O  O   . GLY A 93  ? 0.212214  0.370367 0.439691 -0.0141391  0.0432599   -0.00502878 93   GLY A O   
742   N  N   . ALA A 94  ? 0.210627  0.359028 0.438668 -0.0150971  0.0307373   -0.00644225 94   ALA A N   
743   C  CA  . ALA A 94  ? 0.207218  0.357444 0.427905 -0.0086401  0.0201521   -0.0120798  94   ALA A CA  
744   C  C   . ALA A 94  ? 0.230212  0.391591 0.47086  -0.00665356 0.0158171   -0.019435   94   ALA A C   
745   O  O   . ALA A 94  ? 0.238061  0.403284 0.472694 -0.00176619 0.0136704   -0.0214755  94   ALA A O   
746   C  CB  . ALA A 94  ? 0.22325   0.366952 0.439427 -0.00759998 0.0110665   -0.0141302  94   ALA A CB  
747   N  N   . VAL A 95  ? 0.192412  0.358705 0.457536 -0.0104498  0.0144378   -0.0233395  95   VAL A N   
748   C  CA  . VAL A 95  ? 0.195016  0.372524 0.482494 -0.00881831 0.00910652  -0.0310445  95   VAL A CA  
749   C  C   . VAL A 95  ? 0.18845   0.374076 0.480958 -0.00777536 0.0169595   -0.0304579  95   VAL A C   
750   O  O   . VAL A 95  ? 0.191838  0.384228 0.488737 -0.00256869 0.0112645   -0.0354158  95   VAL A O   
751   C  CB  . VAL A 95  ? 0.176422  0.357718 0.491137 -0.014041   0.00709744  -0.0353273  95   VAL A CB  
752   C  CG1 . VAL A 95  ? 0.16726   0.360985 0.505673 -0.0116851  -4.806e-05  -0.0441649  95   VAL A CG1 
753   C  CG2 . VAL A 95  ? 0.181069  0.354223 0.49072  -0.0141091  -0.00183274 -0.0373956  95   VAL A CG2 
754   N  N   . ARG A 96  ? 0.195315  0.380129 0.486775 -0.0123766  0.0301975   -0.0244334  96   ARG A N   
755   C  CA  . ARG A 96  ? 0.195576  0.388266 0.491989 -0.0114076  0.0385671   -0.0245604  96   ARG A CA  
756   C  C   . ARG A 96  ? 0.235322  0.425011 0.508579 -0.00523235 0.0376275   -0.0233402  96   ARG A C   
757   O  O   . ARG A 96  ? 0.245302  0.441166 0.522061 -0.00359466 0.0438997   -0.0243224  96   ARG A O   
758   C  CB  . ARG A 96  ? 0.27267   0.465104 0.573888 -0.0183929  0.0535313   -0.0185272  96   ARG A CB  
759   C  CG  . ARG A 96  ? 0.419949  0.615615 0.715442 -0.0190157  0.066875    -0.0151186  96   ARG A CG  
760   C  CD  . ARG A 96  ? 0.430751  0.615478 0.693033 -0.0171442  0.0700018   -0.00847386 96   ARG A CD  
761   N  NE  . ARG A 96  ? 0.516977  0.7061   0.773405 -0.0156134  0.0797963   -0.00805096 96   ARG A NE  
762   C  CZ  . ARG A 96  ? 0.527845  0.715593 0.767501 -0.00992587 0.0777365   -0.00940966 96   ARG A CZ  
763   N  NH1 . ARG A 96  ? 0.477962  0.671756 0.719132 -0.00871785 0.0865906   -0.0109797  96   ARG A NH1 
764   N  NH2 . ARG A 96  ? 0.521512  0.701971 0.74393  -0.0056149  0.0673893   -0.00946485 96   ARG A NH2 
765   N  N   . THR A 97  ? 0.220044  0.400378 0.470508 -0.00207142 0.0309104   -0.0212564  97   THR A N   
766   C  CA  . THR A 97  ? 0.249608  0.427381 0.480965 0.00354629  0.0294372   -0.0206805  97   THR A CA  
767   C  C   . THR A 97  ? 0.219381  0.400488 0.45458  0.00971495  0.0173587   -0.0265894  97   THR A C   
768   O  O   . THR A 97  ? 0.236857  0.414826 0.470042 0.0108337   0.00794726  -0.0284951  97   THR A O   
769   C  CB  . THR A 97  ? 0.27302   0.439413 0.477938 0.00328825  0.0305197   -0.0146822  97   THR A CB  
770   O  OG1 . THR A 97  ? 0.315332  0.482138 0.518367 -0.00044474 0.042953    -0.0103839  97   THR A OG1 
771   C  CG2 . THR A 97  ? 0.249184  0.411918 0.435385 0.00900674  0.0262919   -0.0148234  97   THR A CG2 
772   N  N   . LEU A 98  ? 0.249524  0.437591 0.492779 0.0135163   0.0178319   -0.0298718  98   LEU A N   
773   C  CA  . LEU A 98  ? 0.256163  0.449267 0.508841 0.019278    0.00667891  -0.0357194  98   LEU A CA  
774   C  C   . LEU A 98  ? 0.236982  0.422743 0.467366 0.0253034   4.458e-05   -0.0343323  98   LEU A C   
775   O  O   . LEU A 98  ? 0.255074  0.44055  0.484568 0.0297967   -0.0109997  -0.0372959  98   LEU A O   
776   C  CB  . LEU A 98  ? 0.257096  0.462151 0.534234 0.0208348   0.00861194  -0.0407625  98   LEU A CB  
777   C  CG  . LEU A 98  ? 0.248967  0.463994 0.555557 0.0166107   0.00916267  -0.0451328  98   LEU A CG  
778   C  CD1 . LEU A 98  ? 0.26976   0.485701 0.581916 0.00898764  0.0237596   -0.0410581  98   LEU A CD1 
779   C  CD2 . LEU A 98  ? 0.247496  0.47496  0.578761 0.0203418   0.00668497  -0.0516533  98   LEU A CD2 
780   N  N   . GLY A 99  ? 0.220087  0.399642 0.432133 0.0252475   0.00681122  -0.0297626  99   GLY A N   
781   C  CA  . GLY A 99  ? 0.200601  0.373499 0.393661 0.0303549   0.00240244  -0.0282447  99   GLY A CA  
782   C  C   . GLY A 99  ? 0.154617  0.332021 0.356736 0.0366668   -0.00461624 -0.0323336  99   GLY A C   
783   O  O   . GLY A 99  ? 0.145421  0.330543 0.3641   0.037487    -0.00079001 -0.0353186  99   GLY A O   
784   N  N   . SER A 100 ? 0.159395  0.331596 0.349869 0.0411949   -0.0144415  -0.032145   100  SER A N   
785   C  CA  . SER A 100 ? 0.180484  0.354551 0.375416 0.0479833   -0.0224583  -0.0347664  100  SER A CA  
786   C  C   . SER A 100 ? 0.193849  0.379051 0.414968 0.0492748   -0.0271551  -0.0407388  100  SER A C   
787   O  O   . SER A 100 ? 0.201807  0.391451 0.433685 0.0545393   -0.031211   -0.0436192  100  SER A O   
788   C  CB  . SER A 100 ? 0.206496  0.372527 0.382857 0.0517041   -0.0314551  -0.0327354  100  SER A CB  
789   O  OG  . SER A 100 ? 0.207634  0.375592 0.387731 0.0508714   -0.0387863  -0.0353786  100  SER A OG  
790   N  N   . ALA A 101 ? 0.163361  0.353646 0.397454 0.0442667   -0.0261948  -0.0429182  101  ALA A N   
791   C  CA  . ALA A 101 ? 0.156758  0.358719 0.418994 0.0443005   -0.029619   -0.0490823  101  ALA A CA  
792   C  C   . ALA A 101 ? 0.15432   0.364621 0.434492 0.0434509   -0.0201407  -0.050735   101  ALA A C   
793   O  O   . ALA A 101 ? 0.167489  0.388732 0.473178 0.0447201   -0.0227327  -0.0563159  101  ALA A O   
794   C  CB  . ALA A 101 ? 0.139119  0.343724 0.411833 0.0387611   -0.0309016  -0.0511811  101  ALA A CB  
795   N  N   . ASN A 102 ? 0.146145  0.351947 0.413807 0.0417489   -0.0092614  -0.0465521  102  ASN A N   
796   C  CA  . ASN A 102 ? 0.143835  0.357288 0.426485 0.0416243   0.00022066  -0.04865    102  ASN A CA  
797   C  C   . ASN A 102 ? 0.13762   0.352502 0.423888 0.0495568   -0.0055001  -0.0514545  102  ASN A C   
798   O  O   . ASN A 102 ? 0.145394  0.368541 0.449288 0.0510169   -0.00041446 -0.0551199  102  ASN A O   
799   C  CB  . ASN A 102 ? 0.146359  0.354521 0.413484 0.0378712   0.0132721   -0.0440685  102  ASN A CB  
800   C  CG  . ASN A 102 ? 0.165341  0.375402 0.437036 0.0298867   0.0223434   -0.0418328  102  ASN A CG  
801   O  OD1 . ASN A 102 ? 0.139141  0.358994 0.43459  0.0268516   0.0254936   -0.045064   102  ASN A OD1 
802   N  ND2 . ASN A 102 ? 0.172016  0.372629 0.422085 0.0264417   0.0261738   -0.0361958  102  ASN A ND2 
803   N  N   . LEU A 103 ? 0.125802  0.331902 0.394453 0.0546775   -0.0151431  -0.0493135  103  LEU A N   
804   C  CA  . LEU A 103 ? 0.113453  0.319074 0.384407 0.0623384   -0.0204156  -0.05097    103  LEU A CA  
805   C  C   . LEU A 103 ? 0.112005  0.328296 0.408419 0.0665692   -0.0296536  -0.0570635  103  LEU A C   
806   O  O   . LEU A 103 ? 0.107721  0.327266 0.410516 0.0655058   -0.037383   -0.0590418  103  LEU A O   
807   C  CB  . LEU A 103 ? 0.105175  0.298006 0.350413 0.0661748   -0.0280524  -0.0462469  103  LEU A CB  
808   C  CG  . LEU A 103 ? 0.104583  0.28662  0.324812 0.0626746   -0.0203929  -0.0405229  103  LEU A CG  
809   C  CD1 . LEU A 103 ? 0.0984882 0.269378 0.296314 0.0657344   -0.0285621  -0.0361818  103  LEU A CD1 
810   C  CD2 . LEU A 103 ? 0.101047  0.282721 0.32284  0.0640184   -0.0116534  -0.0411377  103  LEU A CD2 
811   N  N   . PRO A 104 ? 0.122339  0.343502 0.432969 0.0724099   -0.0309201  -0.060485   104  PRO A N   
812   C  CA  . PRO A 104 ? 0.132117  0.362371 0.465132 0.077874    -0.0424578  -0.0660845  104  PRO A CA  
813   C  C   . PRO A 104 ? 0.141229  0.362571 0.456547 0.0832898   -0.0576746  -0.0634928  104  PRO A C   
814   O  O   . PRO A 104 ? 0.135551  0.344276 0.42412  0.0837802   -0.057753   -0.0575751  104  PRO A O   
815   C  CB  . PRO A 104 ? 0.131653  0.367446 0.481048 0.082953    -0.0387056  -0.0696058  104  PRO A CB  
816   C  CG  . PRO A 104 ? 0.133977  0.359324 0.461881 0.0818336   -0.0280775  -0.0649255  104  PRO A CG  
817   C  CD  . PRO A 104 ? 0.125714  0.343714 0.431754 0.0742122   -0.0218751  -0.0596133  104  PRO A CD  
818   N  N   . LEU A 105 ? 0.142281  0.370377 0.472449 0.0874306   -0.0705029  -0.0680717  105  LEU A N   
819   C  CA  . LEU A 105 ? 0.153531  0.374354 0.467097 0.0923915   -0.0851838  -0.0662754  105  LEU A CA  
820   C  C   . LEU A 105 ? 0.148111  0.355208 0.436801 0.0984649   -0.0885124  -0.0599179  105  LEU A C   
821   O  O   . LEU A 105 ? 0.163597  0.359961 0.426583 0.0980293   -0.0911599  -0.0548207  105  LEU A O   
822   C  CB  . LEU A 105 ? 0.156895  0.388986 0.494966 0.0973213   -0.0983528  -0.0734291  105  LEU A CB  
823   C  CG  . LEU A 105 ? 0.181196  0.407747 0.504888 0.103702    -0.115491   -0.0730015  105  LEU A CG  
824   C  CD1 . LEU A 105 ? 0.194335  0.41317  0.494817 0.09879     -0.115956   -0.0701302  105  LEU A CD1 
825   C  CD2 . LEU A 105 ? 0.191054  0.429266 0.539666 0.109396    -0.130146   -0.0807951  105  LEU A CD2 
826   N  N   . ALA A 106 ? 0.153357  0.360489 0.450227 0.104199    -0.0882968  -0.0602446  106  ALA A N   
827   C  CA  . ALA A 106 ? 0.153078  0.346549 0.428525 0.109907    -0.0916158  -0.0540932  106  ALA A CA  
828   C  C   . ALA A 106 ? 0.15166   0.333843 0.401375 0.104098    -0.0812057  -0.0477394  106  ALA A C   
829   O  O   . ALA A 106 ? 0.159018  0.329    0.384346 0.106023    -0.0852817  -0.0417429  106  ALA A O   
830   C  CB  . ALA A 106 ? 0.15274   0.348362 0.444267 0.116077    -0.0908677  -0.0562012  106  ALA A CB  
831   N  N   . LYS A 107 ? 0.133686  0.319949 0.388567 0.0970235   -0.0677641  -0.0489242  107  LYS A N   
832   C  CA  . LYS A 107 ? 0.134808  0.310845 0.36651  0.0920821   -0.0587304  -0.0433732  107  LYS A CA  
833   C  C   . LYS A 107 ? 0.131076  0.303725 0.346908 0.0874961   -0.060892   -0.040777   107  LYS A C   
834   O  O   . LYS A 107 ? 0.124384  0.286405 0.316974 0.0858971   -0.0588958  -0.0353251  107  LYS A O   
835   C  CB  . LYS A 107 ? 0.131461  0.312089 0.371464 0.086768    -0.0442081  -0.0452678  107  LYS A CB  
836   C  CG  . LYS A 107 ? 0.149025  0.327881 0.395217 0.091648    -0.0411113  -0.0464839  107  LYS A CG  
837   C  CD  . LYS A 107 ? 0.173568  0.357229 0.426796 0.0869585   -0.0266396  -0.0491174  107  LYS A CD  
838   C  CE  . LYS A 107 ? 0.202441  0.388821 0.47035  0.0922934   -0.0241655  -0.0532096  107  LYS A CE  
839   N  NZ  . LYS A 107 ? 0.225573  0.405731 0.478483 0.0879722   -0.0127497  -0.0513877  107  LYS A NZ  
840   N  N   . ARG A 108 ? 0.14069   0.322617 0.370469 0.085272    -0.0647315  -0.045158   108  ARG A N   
841   C  CA  . ARG A 108 ? 0.140564  0.319183 0.356575 0.0817525   -0.0680516  -0.0436752  108  ARG A CA  
842   C  C   . ARG A 108 ? 0.151233  0.320573 0.347033 0.0876289   -0.0792186  -0.0402177  108  ARG A C   
843   O  O   . ARG A 108 ? 0.167392  0.328681 0.341768 0.0853488   -0.0784691  -0.0362325  108  ARG A O   
844   C  CB  . ARG A 108 ? 0.157821  0.347503 0.393975 0.0796601   -0.0731201  -0.0499068  108  ARG A CB  
845   C  CG  . ARG A 108 ? 0.158616  0.355362 0.408596 0.0714289   -0.0627893  -0.0520767  108  ARG A CG  
846   C  CD  . ARG A 108 ? 0.169936  0.377219 0.442222 0.0705782   -0.0700551  -0.0587057  108  ARG A CD  
847   N  NE  . ARG A 108 ? 0.167122  0.384625 0.463614 0.0651557   -0.059693   -0.0617382  108  ARG A NE  
848   C  CZ  . ARG A 108 ? 0.182087  0.409822 0.50237  0.0617574   -0.0613614  -0.0672754  108  ARG A CZ  
849   N  NH1 . ARG A 108 ? 0.179307  0.409608 0.504923 0.064177    -0.074674   -0.0717609  108  ARG A NH1 
850   N  NH2 . ARG A 108 ? 0.191877  0.426874 0.529838 0.055629    -0.0491719  -0.0682413  108  ARG A NH2 
851   N  N   . GLN A 109 ? 0.165916  0.336735 0.368923 0.0952682   -0.089585   -0.0418179  109  GLN A N   
852   C  CA  . GLN A 109 ? 0.189302  0.350748 0.371971 0.101401    -0.100255   -0.0378413  109  GLN A CA  
853   C  C   . GLN A 109 ? 0.178989  0.326991 0.338669 0.101636    -0.0942559  -0.0300557  109  GLN A C   
854   O  O   . GLN A 109 ? 0.177488  0.316692 0.314579 0.101941    -0.0966971  -0.0255065  109  GLN A O   
855   C  CB  . GLN A 109 ? 0.195833  0.361612 0.391626 0.109838    -0.113091   -0.0409683  109  GLN A CB  
856   C  CG  . GLN A 109 ? 0.210945  0.390127 0.429113 0.109302    -0.120333   -0.0492104  109  GLN A CG  
857   C  CD  . GLN A 109 ? 0.233656  0.419801 0.47139  0.117234    -0.131653   -0.0535087  109  GLN A CD  
858   O  OE1 . GLN A 109 ? 0.234247  0.423705 0.487755 0.119641    -0.128021   -0.0543927  109  GLN A OE1 
859   N  NE2 . GLN A 109 ? 0.257153  0.443767 0.490583 0.122453    -0.146173   -0.0555711  109  GLN A NE2 
860   N  N   . GLN A 110 ? 0.177317  0.32409  0.343706 0.10145     -0.0862928  -0.0290631  110  GLN A N   
861   C  CA  . GLN A 110 ? 0.185749  0.320595 0.33433  0.100872    -0.079719   -0.022772   110  GLN A CA  
862   C  C   . GLN A 110 ? 0.168311  0.299518 0.301189 0.0934251   -0.0714256  -0.0201542  110  GLN A C   
863   O  O   . GLN A 110 ? 0.168013  0.28896  0.279935 0.093509    -0.0714142  -0.0145617  110  GLN A O   
864   C  CB  . GLN A 110 ? 0.229344  0.36647  0.392936 0.101307    -0.0723136  -0.0248176  110  GLN A CB  
865   C  CG  . GLN A 110 ? 0.313052  0.43771  0.461958 0.101924    -0.0671659  -0.0193873  110  GLN A CG  
866   C  CD  . GLN A 110 ? 0.370246  0.497055 0.532971 0.10184     -0.0589549  -0.0225086  110  GLN A CD  
867   O  OE1 . GLN A 110 ? 0.329642  0.467187 0.514785 0.103321    -0.0582663  -0.0285523  110  GLN A OE1 
868   N  NE2 . GLN A 110 ? 0.361752  0.478446 0.511343 0.100061    -0.0525074  -0.0187893  110  GLN A NE2 
869   N  N   . TYR A 111 ? 0.141427  0.281032 0.284853 0.0872827   -0.064968   -0.0240318  111  TYR A N   
870   C  CA  . TYR A 111 ? 0.14399   0.27977  0.273118 0.0806247   -0.057322   -0.021385   111  TYR A CA  
871   C  C   . TYR A 111 ? 0.141371  0.272816 0.254029 0.0810298   -0.0639782  -0.01937    111  TYR A C   
872   O  O   . TYR A 111 ? 0.131055  0.254612 0.224736 0.0787587   -0.0606209  -0.0149572  111  TYR A O   
873   C  CB  . TYR A 111 ? 0.134226  0.279921 0.279333 0.0747962   -0.050837   -0.0257921  111  TYR A CB  
874   C  CG  . TYR A 111 ? 0.155549  0.298757 0.289773 0.0679733   -0.0433453  -0.0237089  111  TYR A CG  
875   C  CD1 . TYR A 111 ? 0.148565  0.288017 0.276163 0.0644182   -0.0333829  -0.0212354  111  TYR A CD1 
876   C  CD2 . TYR A 111 ? 0.160811  0.305628 0.292441 0.0653829   -0.0467258  -0.024794   111  TYR A CD2 
877   C  CE1 . TYR A 111 ? 0.17855   0.316069 0.297132 0.0586202   -0.0272996  -0.0193828  111  TYR A CE1 
878   C  CE2 . TYR A 111 ? 0.178727  0.321418 0.302469 0.0595194   -0.0401678  -0.0230561  111  TYR A CE2 
879   C  CZ  . TYR A 111 ? 0.190129  0.328995 0.306759 0.0563272   -0.0307737  -0.0199877  111  TYR A CZ  
880   O  OH  . TYR A 111 ? 0.225144  0.36157  0.333396 0.0512122   -0.0255699  -0.0180554  111  TYR A OH  
881   N  N   . ASN A 112 ? 0.149564  0.287317 0.270975 0.0834804   -0.0730527  -0.0235461  112  ASN A N   
882   C  CA  . ASN A 112 ? 0.166066  0.300769 0.272822 0.0841094   -0.0796178  -0.0231077  112  ASN A CA  
883   C  C   . ASN A 112 ? 0.185796  0.309707 0.270918 0.0892105   -0.0840825  -0.0172254  112  ASN A C   
884   O  O   . ASN A 112 ? 0.211845  0.329708 0.278242 0.0876578   -0.082877   -0.0141874  112  ASN A O   
885   C  CB  . ASN A 112 ? 0.162119  0.305211 0.282221 0.0867008   -0.0900605  -0.0293918  112  ASN A CB  
886   C  CG  . ASN A 112 ? 0.162112  0.315443 0.303898 0.0809308   -0.0854021  -0.0348993  112  ASN A CG  
887   O  OD1 . ASN A 112 ? 0.173002  0.325517 0.313269 0.0746405   -0.0752419  -0.0333832  112  ASN A OD1 
888   N  ND2 . ASN A 112 ? 0.15653   0.319352 0.318717 0.0828836   -0.0927244  -0.0411014  112  ASN A ND2 
889   N  N   . ALA A 113 ? 0.191352  0.312722 0.279504 0.0951719   -0.0887203  -0.0154925  113  ALA A N   
890   C  CA  . ALA A 113 ? 0.210826  0.320552 0.278666 0.0999039   -0.0921055  -0.00870545 113  ALA A CA  
891   C  C   . ALA A 113 ? 0.212924  0.313701 0.266398 0.0956187   -0.0815537  -0.00288192 113  ALA A C   
892   O  O   . ALA A 113 ? 0.23978   0.331631 0.272699 0.0965682   -0.0820803  0.00252616  113  ALA A O   
893   C  CB  . ALA A 113 ? 0.215549  0.323805 0.291656 0.107366    -0.0993137  -0.00786848 113  ALA A CB  
894   N  N   . LEU A 114 ? 0.186174  0.289234 0.250424 0.0913226   -0.0722816  -0.0040205  114  LEU A N   
895   C  CA  . LEU A 114 ? 0.199043  0.294489 0.251797 0.0872597   -0.0630449  0.00045636  114  LEU A CA  
896   C  C   . LEU A 114 ? 0.206394  0.301069 0.245743 0.0825156   -0.059949   0.00136596  114  LEU A C   
897   O  O   . LEU A 114 ? 0.216919  0.30339  0.240029 0.0813973   -0.0567052  0.00638961  114  LEU A O   
898   C  CB  . LEU A 114 ? 0.185168  0.284295 0.252019 0.0838255   -0.0544792  -0.00218768 114  LEU A CB  
899   C  CG  . LEU A 114 ? 0.210961  0.308037 0.288191 0.0887274   -0.0558563  -0.00232842 114  LEU A CG  
900   C  CD1 . LEU A 114 ? 0.210868  0.315515 0.304528 0.0851662   -0.0477589  -0.00733541 114  LEU A CD1 
901   C  CD2 . LEU A 114 ? 0.22808   0.312138 0.290319 0.0895865   -0.0534362  0.00406458  114  LEU A CD2 
902   N  N   . LEU A 115 ? 0.205001  0.308102 0.252333 0.0794218   -0.060247   -0.00355833 115  LEU A N   
903   C  CA  . LEU A 115 ? 0.215379  0.31745  0.251208 0.0750614   -0.056975   -0.00305127 115  LEU A CA  
904   C  C   . LEU A 115 ? 0.216561  0.312453 0.233639 0.0787081   -0.0627707  5.731e-05   115  LEU A C   
905   O  O   . LEU A 115 ? 0.198546  0.289198 0.200532 0.0765595   -0.0587367  0.00331536  115  LEU A O   
906   C  CB  . LEU A 115 ? 0.246783  0.357907 0.294851 0.0719046   -0.0578425  -0.00886334 115  LEU A CB  
907   C  CG  . LEU A 115 ? 0.282635  0.400178 0.347724 0.0673967   -0.0509341  -0.0116217  115  LEU A CG  
908   C  CD1 . LEU A 115 ? 0.281922  0.406058 0.355719 0.0633861   -0.0509964  -0.0159409  115  LEU A CD1 
909   C  CD2 . LEU A 115 ? 0.322452  0.435029 0.380067 0.0636132   -0.0415741  -0.00797101 115  LEU A CD2 
910   N  N   . SER A 116 ? 0.207378  0.304575 0.225722 0.0844387   -0.0725557  -0.00138932 116  SER A N   
911   C  CA  . SER A 116 ? 0.239151  0.331155 0.238837 0.0885132   -0.0789877  0.00095131  116  SER A CA  
912   C  C   . SER A 116 ? 0.25352   0.334123 0.23608  0.0901154   -0.0754954  0.00917401  116  SER A C   
913   O  O   . SER A 116 ? 0.265156  0.340237 0.229372 0.0893346   -0.0730801  0.0126808   116  SER A O   
914   C  CB  . SER A 116 ? 0.256599  0.353238 0.26333  0.0945177   -0.0910563  -0.00302827 116  SER A CB  
915   O  OG  . SER A 116 ? 0.327484  0.417858 0.313416 0.0992427   -0.0974602  -9.3e-06    116  SER A OG  
916   N  N   . GLN A 117 ? 0.240645  0.317494 0.229809 0.0921285   -0.0745512  0.012196    117  GLN A N   
917   C  CA  . GLN A 117 ? 0.260808  0.32603  0.235884 0.0936992   -0.0717385  0.0200914   117  GLN A CA  
918   C  C   . GLN A 117 ? 0.260712  0.322539 0.230082 0.0870882   -0.0605275  0.0226311   117  GLN A C   
919   O  O   . GLN A 117 ? 0.249557  0.302874 0.202575 0.0868388   -0.05748    0.0286695   117  GLN A O   
920   C  CB  . GLN A 117 ? 0.290563  0.352502 0.277031 0.0969395   -0.0727167  0.0217719   117  GLN A CB  
921   C  CG  . GLN A 117 ? 0.386777  0.45032  0.378805 0.104623    -0.0844129  0.0205318   117  GLN A CG  
922   C  CD  . GLN A 117 ? 0.555402  0.617766 0.56333  0.107613    -0.0848017  0.0204314   117  GLN A CD  
923   O  OE1 . GLN A 117 ? 0.704003  0.757305 0.708493 0.106993    -0.0793836  0.0253535   117  GLN A OE1 
924   N  NE2 . GLN A 117 ? 0.667428  0.739491 0.6948   0.110514    -0.0906219  0.0140925   117  GLN A NE2 
925   N  N   . MET A 118 ? 0.222232  0.290664 0.204974 0.0818968   -0.0545523  0.0182016   118  MET A N   
926   C  CA  . MET A 118 ? 0.230757  0.296785 0.209021 0.0758977   -0.0450148  0.0199203   118  MET A CA  
927   C  C   . MET A 118 ? 0.235543  0.301785 0.200258 0.073802    -0.0437171  0.0203528   118  MET A C   
928   O  O   . MET A 118 ? 0.244272  0.304615 0.197354 0.0716871   -0.038437   0.0246991   118  MET A O   
929   C  CB  . MET A 118 ? 0.197801  0.270691 0.191532 0.0713923   -0.0397278  0.0151909   118  MET A CB  
930   C  CG  . MET A 118 ? 0.198004  0.269206 0.202897 0.0725841   -0.0379823  0.0150539   118  MET A CG  
931   S  SD  . MET A 118 ? 0.217512  0.294451 0.233583 0.066428    -0.0293655  0.0108327   118  MET A SD  
932   C  CE  . MET A 118 ? 0.191664  0.280519 0.219834 0.0646645   -0.0309491  0.00481412  118  MET A CE  
933   N  N   . SER A 119 ? 0.244563  0.31743  0.211013 0.0747876   -0.048889   0.0156294   119  SER A N   
934   C  CA  . SER A 119 ? 0.277015  0.350436 0.231218 0.073607    -0.0484343  0.0148423   119  SER A CA  
935   C  C   . SER A 119 ? 0.295474  0.360725 0.229529 0.0772915   -0.050062   0.0205384   119  SER A C   
936   O  O   . SER A 119 ? 0.29189   0.353889 0.213735 0.0750427   -0.0445145  0.0231694   119  SER A O   
937   C  CB  . SER A 119 ? 0.301322  0.382824 0.263179 0.0746251   -0.0549667  0.00800023  119  SER A CB  
938   O  OG  . SER A 119 ? 0.391882  0.473349 0.340779 0.0754574   -0.0570705  0.00640066  119  SER A OG  
939   N  N   . ARG A 120 ? 0.287745  0.349709 0.218255 0.0831098   -0.0575695  0.022606    120  ARG A N   
940   C  CA  . ARG A 120 ? 0.31119   0.364566 0.221296 0.087265    -0.0597963  0.0288066   120  ARG A CA  
941   C  C   . ARG A 120 ? 0.32107   0.365075 0.223817 0.0848118   -0.0512994  0.036633    120  ARG A C   
942   O  O   . ARG A 120 ? 0.341     0.37883  0.226197 0.0848103   -0.0477338  0.0417456   120  ARG A O   
943   C  CB  . ARG A 120 ? 0.328846  0.380341 0.238453 0.0945299   -0.0706635  0.0296306   120  ARG A CB  
944   C  CG  . ARG A 120 ? 0.431191  0.47204  0.317859 0.0992273   -0.0729274  0.0375563   120  ARG A CG  
945   C  CD  . ARG A 120 ? 0.520173  0.556585 0.403515 0.107274    -0.0840608  0.040367    120  ARG A CD  
946   N  NE  . ARG A 120 ? 0.668924  0.702893 0.568461 0.107734    -0.0834411  0.0423355   120  ARG A NE  
947   C  CZ  . ARG A 120 ? 0.709383  0.734942 0.609169 0.105254    -0.075726   0.0486153   120  ARG A CZ  
948   N  NH1 . ARG A 120 ? 0.681295  0.697623 0.563439 0.103179    -0.0688061  0.0560067   120  ARG A NH1 
949   N  NH2 . ARG A 120 ? 0.733531  0.760085 0.652119 0.104976    -0.0750176  0.0470645   120  ARG A NH2 
950   N  N   . ILE A 121 ? 0.305959  0.348434 0.222126 0.082871    -0.047951   0.0376333   121  ILE A N   
951   C  CA  . ILE A 121 ? 0.30969   0.343333 0.221001 0.0801048   -0.0402001  0.044169    121  ILE A CA  
952   C  C   . ILE A 121 ? 0.29954   0.335043 0.205873 0.0741725   -0.0315209  0.0438054   121  ILE A C   
953   O  O   . ILE A 121 ? 0.324978  0.353579 0.218723 0.0729521   -0.0262954  0.0496732   121  ILE A O   
954   C  CB  . ILE A 121 ? 0.319318  0.351972 0.247207 0.0788996   -0.0383104  0.0434306   121  ILE A CB  
955   C  CG1 . ILE A 121 ? 0.344718  0.372167 0.273834 0.0858025   -0.0464172  0.046187    121  ILE A CG1 
956   C  CG2 . ILE A 121 ? 0.320515  0.346526 0.247454 0.0739094   -0.0290286  0.0475554   121  ILE A CG2 
957   C  CD1 . ILE A 121 ? 0.348458  0.377302 0.296271 0.0861714   -0.0465407  0.0432225   121  ILE A CD1 
958   N  N   . TYR A 122 ? 0.263514  0.308032 0.18059  0.0705082   -0.0297482  0.0372629   122  TYR A N   
959   C  CA  . TYR A 122 ? 0.256682  0.303291 0.171641 0.0650874   -0.0218825  0.0365628   122  TYR A CA  
960   C  C   . TYR A 122 ? 0.285995  0.33207  0.184386 0.0663829   -0.0215649  0.0376852   122  TYR A C   
961   O  O   . TYR A 122 ? 0.297383  0.340396 0.187635 0.0635603   -0.0143907  0.0410713   122  TYR A O   
962   C  CB  . TYR A 122 ? 0.231094  0.286748 0.160928 0.061615    -0.0211023  0.0297137   122  TYR A CB  
963   C  CG  . TYR A 122 ? 0.230133  0.288257 0.159026 0.0565651   -0.0140306  0.0286782   122  TYR A CG  
964   C  CD1 . TYR A 122 ? 0.232543  0.294667 0.155075 0.0564963   -0.0141657  0.0259465   122  TYR A CD1 
965   C  CD2 . TYR A 122 ? 0.220373  0.276714 0.155292 0.0522678   -0.00773467 0.0300322   122  TYR A CD2 
966   C  CE1 . TYR A 122 ? 0.233077  0.297397 0.155385 0.0524557   -0.0078144  0.0250785   122  TYR A CE1 
967   C  CE2 . TYR A 122 ? 0.211758  0.270847 0.14704  0.0480667   -0.00211472 0.028863    122  TYR A CE2 
968   C  CZ  . TYR A 122 ? 0.242735  0.305886 0.172125 0.0482539   -0.00206136 0.0265678   122  TYR A CZ  
969   O  OH  . TYR A 122 ? 0.249699  0.31581  0.181221 0.0444142   0.00341656  0.0252387   122  TYR A OH  
970   N  N   A SER A 123 ? 0.287084  0.337039 0.181435 0.0703908   -0.0289996  0.0339352   123  SER A N   
971   N  N   B SER A 123 ? 0.295624  0.345265 0.189631 0.0705668   -0.0291419  0.0341716   123  SER A N   
972   C  CA  A SER A 123 ? 0.302255  0.353124 0.181689 0.0715272   -0.0286705  0.032959    123  SER A CA  
973   C  CA  B SER A 123 ? 0.329477  0.380511 0.209151 0.0717149   -0.0291162  0.0327646   123  SER A CA  
974   C  C   A SER A 123 ? 0.330948  0.372568 0.190666 0.0742697   -0.0268266  0.0408108   123  SER A C   
975   C  C   B SER A 123 ? 0.356355  0.399072 0.215261 0.0760258   -0.0302596  0.0393781   123  SER A C   
976   O  O   A SER A 123 ? 0.339413  0.380023 0.18714  0.0728022   -0.0207841  0.0423398   123  SER A O   
977   O  O   B SER A 123 ? 0.403735  0.446508 0.247651 0.0772522   -0.0291199  0.0389828   123  SER A O   
978   C  CB  A SER A 123 ? 0.297346  0.354588 0.177774 0.0748776   -0.0372659  0.0260406   123  SER A CB  
979   C  CB  B SER A 123 ? 0.332308  0.391795 0.218017 0.0730105   -0.0356266  0.0244082   123  SER A CB  
980   O  OG  A SER A 123 ? 0.296248  0.351009 0.17427  0.0805033   -0.0462689  0.0272415   123  SER A OG  
981   O  OG  B SER A 123 ? 0.322646  0.388299 0.22074  0.0679088   -0.0308625  0.019807    123  SER A OG  
982   N  N   . THR A 124 ? 0.345466  0.380166 0.202628 0.0781182   -0.0314104  0.0460196   124  THR A N   
983   C  CA  . THR A 124 ? 0.376077  0.401163 0.21284  0.0819432   -0.0317127  0.0539216   124  THR A CA  
984   C  C   . THR A 124 ? 0.376562  0.392351 0.212103 0.0786978   -0.0231948  0.0623921   124  THR A C   
985   O  O   . THR A 124 ? 0.412581  0.418946 0.231388 0.0809951   -0.0216663  0.0704147   124  THR A O   
986   C  CB  . THR A 124 ? 0.386048  0.408339 0.216969 0.0894248   -0.0434913  0.054801    124  THR A CB  
987   O  OG1 . THR A 124 ? 0.366137  0.386237 0.21262  0.0900751   -0.0462667  0.056123    124  THR A OG1 
988   C  CG2 . THR A 124 ? 0.373094  0.404576 0.206085 0.0924894   -0.0524419  0.0459112   124  THR A CG2 
989   N  N   . ALA A 125 ? 0.348941  0.366989 0.201241 0.0731933   -0.0173637  0.0607153   125  ALA A N   
990   C  CA  . ALA A 125 ? 0.375523  0.384924 0.228569 0.0697094   -0.00959381 0.0677682   125  ALA A CA  
991   C  C   . ALA A 125 ? 0.378721  0.385011 0.217204 0.0668767   -0.0005747  0.0724742   125  ALA A C   
992   O  O   . ALA A 125 ? 0.367829  0.381726 0.203843 0.0651035   0.00224575  0.0676967   125  ALA A O   
993   C  CB  . ALA A 125 ? 0.34093   0.354619 0.214249 0.0643568   -0.00561273 0.0635108   125  ALA A CB  
994   N  N   . LYS A 126 ? 0.404332  0.39947  0.234902 0.0662598   0.00434877  0.0816483   126  LYS A N   
995   C  CA  . LYS A 126 ? 0.462949  0.454568 0.28055  0.0631432   0.0142783   0.0870655   126  LYS A CA  
996   C  C   . LYS A 126 ? 0.448395  0.432624 0.274608 0.0575582   0.0229685   0.0928748   126  LYS A C   
997   O  O   . LYS A 126 ? 0.433884  0.41158  0.26928  0.0580178   0.0201305   0.0952991   126  LYS A O   
998   C  CB  . LYS A 126 ? 0.503795  0.485904 0.297974 0.0690906   0.0109753   0.0950373   126  LYS A CB  
999   C  CG  . LYS A 126 ? 0.573951  0.561223 0.355167 0.0753639   0.00195997  0.0904591   126  LYS A CG  
1000  C  CD  . LYS A 126 ? 0.609188  0.607729 0.387939 0.0737268   0.00474649  0.0823884   126  LYS A CD  
1001  C  CE  . LYS A 126 ? 0.709366  0.708742 0.468738 0.0806516   -0.00351013 0.0804834   126  LYS A CE  
1002  N  NZ  . LYS A 126 ? 0.742638  0.747673 0.512515 0.0847642   -0.0161589  0.0733208   126  LYS A NZ  
1003  N  N   . VAL A 127 ? 0.462682  0.447961 0.286706 0.0522964   0.0337063   0.0947873   127  VAL A N   
1004  C  CA  . VAL A 127 ? 0.45332   0.430575 0.283806 0.0469459   0.0423459   0.101195    127  VAL A CA  
1005  C  C   . VAL A 127 ? 0.510101  0.476699 0.319254 0.0481188   0.0482313   0.112112    127  VAL A C   
1006  O  O   . VAL A 127 ? 0.502288  0.472618 0.296409 0.0489869   0.0520839   0.112318    127  VAL A O   
1007  C  CB  . VAL A 127 ? 0.434096  0.420287 0.280384 0.0396648   0.050518    0.0956528   127  VAL A CB  
1008  C  CG1 . VAL A 127 ? 0.4595    0.437436 0.312849 0.0338214   0.0596128   0.102149    127  VAL A CG1 
1009  C  CG2 . VAL A 127 ? 0.420983  0.41687  0.286095 0.0387439   0.0446782   0.085603    127  VAL A CG2 
1010  N  N   . CYS A 128 ? 0.561172  0.514093 0.368794 0.0482768   0.0490603   0.121159    128  CYS A N   
1011  C  CA  . CYS A 128 ? 0.67802   0.618912 0.463813 0.0498814   0.0541141   0.132956    128  CYS A CA  
1012  C  C   . CYS A 128 ? 0.71339   0.648161 0.505398 0.0421535   0.0674048   0.139456    128  CYS A C   
1013  O  O   . CYS A 128 ? 0.703501  0.63686  0.516202 0.0374536   0.0690468   0.137656    128  CYS A O   
1014  C  CB  . CYS A 128 ? 0.702391  0.629951 0.479888 0.0562326   0.045376    0.140361    128  CYS A CB  
1015  S  SG  . CYS A 128 ? 0.943211  0.877399 0.71232  0.0658193   0.0294393   0.133672    128  CYS A SG  
1016  N  N   . LEU A 129 ? 0.76875   0.700606 0.542844 0.0409228   0.0768491   0.146304    129  LEU A N   
1017  C  CA  . LEU A 129 ? 0.912708  0.833444 0.683651 0.0355655   0.0892113   0.157297    129  LEU A CA  
1018  C  C   . LEU A 129 ? 0.910122  0.841567 0.692891 0.0275685   0.101914    0.152915    129  LEU A C   
1019  O  O   . LEU A 129 ? 0.924956  0.848959 0.709504 0.0217852   0.113467    0.160992    129  LEU A O   
1020  C  CB  . LEU A 129 ? 0.975386  0.88119  0.756804 0.0340232   0.0881169   0.164674    129  LEU A CB  
1021  C  CG  . LEU A 129 ? 1.05301   0.94712  0.821981 0.0425601   0.0760165   0.170207    129  LEU A CG  
1022  C  CD1 . LEU A 129 ? 1.02439   0.903793 0.806021 0.041557    0.0742311   0.176315    129  LEU A CD1 
1023  C  CD2 . LEU A 129 ? 1.05746   0.944135 0.793874 0.0487941   0.0754326   0.179547    129  LEU A CD2 
1024  N  N   . THR A 135 ? 0.806277  0.724955 0.464882 0.070492    0.0580438   0.161323    135  THR A N   
1025  C  CA  . THR A 135 ? 0.878646  0.813023 0.544618 0.0661748   0.0651784   0.150842    135  THR A CA  
1026  C  C   . THR A 135 ? 0.811464  0.756854 0.510485 0.061262    0.0631875   0.140224    135  THR A C   
1027  O  O   . THR A 135 ? 0.770506  0.712994 0.488406 0.0549989   0.0693811   0.142711    135  THR A O   
1028  C  CB  . THR A 135 ? 0.963183  0.894862 0.619694 0.0604499   0.0823959   0.15788     135  THR A CB  
1029  O  OG1 . THR A 135 ? 1.04561   0.960717 0.677189 0.0643718   0.0826949   0.171853    135  THR A OG1 
1030  C  CG2 . THR A 135 ? 1.00682   0.951096 0.653342 0.0606182   0.0879091   0.149891    135  THR A CG2 
1031  N  N   . CYS A 136 ? 0.766208  0.724154 0.471424 0.0641111   0.0545988   0.128213    136  CYS A N   
1032  C  CA  . CYS A 136 ? 0.724315  0.68991  0.456274 0.0624348   0.0476336   0.119332    136  CYS A CA  
1033  C  C   . CYS A 136 ? 0.65952   0.640757 0.40393  0.0595992   0.0493759   0.10725     136  CYS A C   
1034  O  O   . CYS A 136 ? 0.659666  0.647468 0.392047 0.0630723   0.0469176   0.10177     136  CYS A O   
1035  C  CB  . CYS A 136 ? 0.725587  0.689939 0.455698 0.0697738   0.0322673   0.116749    136  CYS A CB  
1036  S  SG  . CYS A 136 ? 0.872495  0.819092 0.59757  0.0732808   0.0275523   0.129179    136  CYS A SG  
1037  N  N   . TRP A 137 ? 0.58086   0.567699 0.349952 0.0537994   0.0522745   0.102605    137  TRP A N   
1038  C  CA  . TRP A 137 ? 0.522699  0.523546 0.304594 0.0513394   0.0532433   0.0916831   137  TRP A CA  
1039  C  C   . TRP A 137 ? 0.491301  0.498164 0.285706 0.0542137   0.0411593   0.0834615   137  TRP A C   
1040  O  O   . TRP A 137 ? 0.515782  0.518521 0.32121  0.0542141   0.0362654   0.0848477   137  TRP A O   
1041  C  CB  . TRP A 137 ? 0.54719   0.551556 0.348146 0.04346     0.0633196   0.09097     137  TRP A CB  
1042  C  CG  . TRP A 137 ? 0.620579  0.622184 0.412091 0.0399055   0.0765534   0.0972449   137  TRP A CG  
1043  C  CD1 . TRP A 137 ? 0.692309  0.693097 0.461432 0.0427527   0.0811412   0.0999874   137  TRP A CD1 
1044  C  CD2 . TRP A 137 ? 0.65376   0.653489 0.45854  0.0326578   0.0873512   0.101183    137  TRP A CD2 
1045  N  NE1 . TRP A 137 ? 0.719919  0.718457 0.487158 0.0376768   0.0949356   0.10593     137  TRP A NE1 
1046  C  CE2 . TRP A 137 ? 0.709524  0.707584 0.499557 0.0312313   0.0988773   0.106688    137  TRP A CE2 
1047  C  CE3 . TRP A 137 ? 0.708627  0.708267 0.536486 0.0272166   0.0883972   0.10005     137  TRP A CE3 
1048  C  CZ2 . TRP A 137 ? 0.744969  0.741344 0.544233 0.0242008   0.111652    0.11152     137  TRP A CZ2 
1049  C  CZ3 . TRP A 137 ? 0.742367  0.740366 0.579336 0.0204332   0.100077    0.104159    137  TRP A CZ3 
1050  C  CH2 . TRP A 137 ? 0.720234  0.716814 0.544006 0.0187505   0.111724    0.109927    137  TRP A CH2 
1051  N  N   . SER A 138 ? 0.472509  0.488851 0.265322 0.0566124   0.0368871   0.0749062   138  SER A N   
1052  C  CA  . SER A 138 ? 0.449539  0.473166 0.255936 0.0582629   0.0271902   0.066355    138  SER A CA  
1053  C  C   . SER A 138 ? 0.408054  0.440477 0.234896 0.0525933   0.0316821   0.0600402   138  SER A C   
1054  O  O   . SER A 138 ? 0.374247  0.408921 0.203006 0.0483578   0.0413975   0.0607354   138  SER A O   
1055  C  CB  . SER A 138 ? 0.511592  0.540054 0.305486 0.0634773   0.0207483   0.0605442   138  SER A CB  
1056  O  OG  . SER A 138 ? 0.593993  0.627799 0.381815 0.061705    0.02875     0.0574786   138  SER A OG  
1057  N  N   . LEU A 139 ? 0.36526   0.402895 0.207465 0.0526212   0.0246596   0.05389     139  LEU A N   
1058  C  CA  . LEU A 139 ? 0.37549   0.420935 0.235751 0.0478716   0.0276926   0.0481335   139  LEU A CA  
1059  C  C   . LEU A 139 ? 0.397876  0.451139 0.255521 0.0475864   0.0310211   0.0424577   139  LEU A C   
1060  O  O   . LEU A 139 ? 0.397359  0.454816 0.262961 0.0434274   0.0383307   0.0410668   139  LEU A O   
1061  C  CB  . LEU A 139 ? 0.333498  0.38261  0.208221 0.048297    0.0199      0.0431058   139  LEU A CB  
1062  C  CG  . LEU A 139 ? 0.347765  0.404555 0.239324 0.044088    0.0217589   0.0372566   139  LEU A CG  
1063  C  CD1 . LEU A 139 ? 0.329795  0.38552  0.230255 0.0387704   0.029379    0.0397365   139  LEU A CD1 
1064  C  CD2 . LEU A 139 ? 0.345296  0.404157 0.247781 0.0450601   0.01437     0.0337096   139  LEU A CD2 
1065  N  N   . ASP A 140 ? 0.409863  0.465337 0.257781 0.0522413   0.0249672   0.0384731   140  ASP A N   
1066  C  CA  . ASP A 140 ? 0.420364  0.482753 0.265335 0.0529758   0.0267556   0.0319908   140  ASP A CA  
1067  C  C   . ASP A 140 ? 0.446249  0.505137 0.268189 0.0572894   0.0277117   0.0341171   140  ASP A C   
1068  O  O   . ASP A 140 ? 0.43808   0.493655 0.249818 0.062011    0.0195492   0.034418    140  ASP A O   
1069  C  CB  . ASP A 140 ? 0.429954  0.49845  0.285578 0.0544129   0.0183229   0.0238353   140  ASP A CB  
1070  C  CG  . ASP A 140 ? 0.548344  0.624287 0.40712  0.0544214   0.0197711   0.0159746   140  ASP A CG  
1071  O  OD1 . ASP A 140 ? 0.566301  0.643751 0.418391 0.0536663   0.0278298   0.01611     140  ASP A OD1 
1072  O  OD2 . ASP A 140 ? 0.509876  0.590061 0.37849  0.0551892   0.0131642   0.0096038   140  ASP A OD2 
1073  N  N   . PRO A 141 ? 0.479973  0.539926 0.29272  0.0561586   0.0373376   0.0351764   141  PRO A N   
1074  C  CA  . PRO A 141 ? 0.456671  0.522097 0.282968 0.050886    0.0467987   0.0336731   141  PRO A CA  
1075  C  C   . PRO A 141 ? 0.438958  0.500275 0.270196 0.0458222   0.0560515   0.0414176   141  PRO A C   
1076  O  O   . PRO A 141 ? 0.43646   0.503106 0.282764 0.0412713   0.0622258   0.0393778   141  PRO A O   
1077  C  CB  . PRO A 141 ? 0.464283  0.534194 0.277886 0.0532584   0.0517568   0.0290836   141  PRO A CB  
1078  C  CG  . PRO A 141 ? 0.496372  0.55851  0.284227 0.0577116   0.0509386   0.0347924   141  PRO A CG  
1079  C  CD  . PRO A 141 ? 0.482037  0.538759 0.270369 0.0603779   0.0393353   0.0370581   141  PRO A CD  
1080  N  N   . ASP A 142 ? 0.446563  0.49814  0.265549 0.0467344   0.0566788   0.0502325   142  ASP A N   
1081  C  CA  . ASP A 142 ? 0.476017  0.521945 0.29482  0.0424046   0.0667044   0.0585259   142  ASP A CA  
1082  C  C   . ASP A 142 ? 0.449835  0.498111 0.292384 0.0365256   0.0688638   0.057729    142  ASP A C   
1083  O  O   . ASP A 142 ? 0.428001  0.479789 0.279571 0.0317288   0.0782107   0.0579863   142  ASP A O   
1084  C  CB  . ASP A 142 ? 0.497812  0.531467 0.299952 0.045066    0.0649948   0.0682686   142  ASP A CB  
1085  C  CG  . ASP A 142 ? 0.566239  0.596834 0.342495 0.0512304   0.0624814   0.0696257   142  ASP A CG  
1086  O  OD1 . ASP A 142 ? 0.552084  0.588477 0.32023  0.0517552   0.0681728   0.0656923   142  ASP A OD1 
1087  O  OD2 . ASP A 142 ? 0.615996  0.638584 0.380743 0.055714    0.0545647   0.0742021   142  ASP A OD2 
1088  N  N   . LEU A 143 ? 0.391996  0.437534 0.243765 0.0369164   0.0607106   0.0574437   143  LEU A N   
1089  C  CA  . LEU A 143 ? 0.3865    0.433236 0.258658 0.0317954   0.0620506   0.0566316   143  LEU A CA  
1090  C  C   . LEU A 143 ? 0.359536  0.417637 0.247224 0.0296846   0.0618456   0.0478345   143  LEU A C   
1091  O  O   . LEU A 143 ? 0.405103  0.466508 0.307333 0.024859    0.0667738   0.0467761   143  LEU A O   
1092  C  CB  . LEU A 143 ? 0.379229  0.419794 0.256525 0.0329366   0.0542422   0.0584892   143  LEU A CB  
1093  C  CG  . LEU A 143 ? 0.401937  0.430253 0.266205 0.0351082   0.0540611   0.0676655   143  LEU A CG  
1094  C  CD1 . LEU A 143 ? 0.396001  0.420351 0.26709  0.0372653   0.045233    0.0673043   143  LEU A CD1 
1095  C  CD2 . LEU A 143 ? 0.417102  0.438725 0.282999 0.0302837   0.063849    0.0748901   143  LEU A CD2 
1096  N  N   . THR A 144 ? 0.344834  0.408769 0.229565 0.0333204   0.056298    0.0415248   144  THR A N   
1097  C  CA  . THR A 144 ? 0.339375  0.412971 0.237645 0.0319471   0.0557822   0.0337583   144  THR A CA  
1098  C  C   . THR A 144 ? 0.373171  0.451514 0.274998 0.0287379   0.0661609   0.0334319   144  THR A C   
1099  O  O   . THR A 144 ? 0.339092  0.422639 0.257597 0.0248486   0.0686985   0.0307477   144  THR A O   
1100  C  CB  . THR A 144 ? 0.335364  0.412899 0.228287 0.0365547   0.0487894   0.0276628   144  THR A CB  
1101  O  OG1 . THR A 144 ? 0.35072   0.424546 0.244443 0.0385109   0.0400252   0.0281919   144  THR A OG1 
1102  C  CG2 . THR A 144 ? 0.312642  0.398786 0.219895 0.035655    0.046934    0.0199668   144  THR A CG2 
1103  N  N   . ASN A 145 ? 0.364476  0.440863 0.250429 0.030405    0.0722697   0.0364225   145  ASN A N   
1104  C  CA  . ASN A 145 ? 0.382305  0.464036 0.27068  0.027813    0.0830539   0.0356862   145  ASN A CA  
1105  C  C   . ASN A 145 ? 0.366647  0.446557 0.267469 0.0217234   0.0903349   0.0405587   145  ASN A C   
1106  O  O   . ASN A 145 ? 0.430064  0.517505 0.345538 0.0182655   0.0960008   0.0371027   145  ASN A O   
1107  C  CB  . ASN A 145 ? 0.419469  0.49917  0.285841 0.0313198   0.0880936   0.0377341   145  ASN A CB  
1108  C  CG  . ASN A 145 ? 0.463925  0.549145 0.324244 0.0363891   0.0824195   0.0294955   145  ASN A CG  
1109  O  OD1 . ASN A 145 ? 0.466222  0.55766  0.341073 0.0365247   0.0767784   0.0224073   145  ASN A OD1 
1110  N  ND2 . ASN A 145 ? 0.476993  0.559567 0.315784 0.0407387   0.0832952   0.030116    145  ASN A ND2 
1111  N  N   . ILE A 146 ? 0.364492  0.434462 0.260485 0.020478    0.0901457   0.0482605   146  ILE A N   
1112  C  CA  . ILE A 146 ? 0.363395  0.430294 0.27218  0.0145566   0.0960956   0.052652    146  ILE A CA  
1113  C  C   . ILE A 146 ? 0.384935  0.45878  0.316525 0.0115584   0.0917368   0.0460301   146  ILE A C   
1114  O  O   . ILE A 146 ? 0.373837  0.453486 0.320594 0.0069481   0.0980605   0.044106    146  ILE A O   
1115  C  CB  . ILE A 146 ? 0.39089   0.444565 0.29046  0.0145069   0.095224    0.0617641   146  ILE A CB  
1116  C  CG1 . ILE A 146 ? 0.451252  0.497818 0.327111 0.0173172   0.100548    0.0692177   146  ILE A CG1 
1117  C  CG2 . ILE A 146 ? 0.37565   0.425813 0.291294 0.00810411  0.100348    0.0651247   146  ILE A CG2 
1118  C  CD1 . ILE A 146 ? 0.449899  0.482662 0.314188 0.01911     0.0971371   0.0781386   146  ILE A CD1 
1119  N  N   . LEU A 147 ? 0.320376  0.393807 0.254235 0.0142257   0.0810895   0.0425843   147  LEU A N   
1120  C  CA  . LEU A 147 ? 0.330233  0.40914  0.282691 0.0118844   0.0764074   0.0369028   147  LEU A CA  
1121  C  C   . LEU A 147 ? 0.327633  0.417932 0.290635 0.0112278   0.078692    0.0301092   147  LEU A C   
1122  O  O   . LEU A 147 ? 0.298526  0.393894 0.278659 0.00758218  0.0793577   0.0269108   147  LEU A O   
1123  C  CB  . LEU A 147 ? 0.273057  0.350118 0.224201 0.0151846   0.0657275   0.0344583   147  LEU A CB  
1124  C  CG  . LEU A 147 ? 0.293535  0.361341 0.244314 0.01441     0.0629756   0.0390616   147  LEU A CG  
1125  C  CD1 . LEU A 147 ? 0.279253  0.348848 0.247757 0.00970854  0.0631235   0.0364986   147  LEU A CD1 
1126  C  CD2 . LEU A 147 ? 0.299587  0.357679 0.238898 0.0141815   0.0683277   0.0474483   147  LEU A CD2 
1127  N  N   . ALA A 148 ? 0.336211  0.430311 0.289377 0.0150828   0.0791627   0.0274847   148  ALA A N   
1128  C  CA  . ALA A 148 ? 0.353109  0.457614 0.31598  0.0154866   0.0806442   0.0205177   148  ALA A CA  
1129  C  C   . ALA A 148 ? 0.399429  0.509238 0.370641 0.011676    0.0918523   0.0208648   148  ALA A C   
1130  O  O   . ALA A 148 ? 0.390618  0.509109 0.37889  0.00996949  0.092552    0.0154764   148  ALA A O   
1131  C  CB  . ALA A 148 ? 0.351602  0.458108 0.302875 0.0208392   0.077153    0.0166493   148  ALA A CB  
1132  N  N   . SER A 149 ? 0.414365  0.519144 0.374987 0.010138    0.100705    0.0273321   149  SER A N   
1133  C  CA  . SER A 149 ? 0.438894  0.550332 0.406298 0.00720563  0.112331    0.0267119   149  SER A CA  
1134  C  C   . SER A 149 ? 0.486996  0.593806 0.459658 0.00125222  0.121202    0.0336648   149  SER A C   
1135  O  O   . SER A 149 ? 0.612523  0.725675 0.596244 -0.00250591 0.131078    0.0329798   149  SER A O   
1136  C  CB  . SER A 149 ? 0.500542  0.61301  0.45003  0.0112449   0.117394    0.0263845   149  SER A CB  
1137  O  OG  . SER A 149 ? 0.554597  0.656016 0.483368 0.0120736   0.119669    0.0349822   149  SER A OG  
1138  N  N   . SER A 150 ? 0.461704  0.557188 0.426601 0.00031394  0.118714    0.0406558   150  SER A N   
1139  C  CA  . SER A 150 ? 0.460614  0.551169 0.433363 -0.00579093 0.126833    0.0468671   150  SER A CA  
1140  C  C   . SER A 150 ? 0.473311  0.569941 0.472318 -0.0103942  0.123915    0.0415214   150  SER A C   
1141  O  O   . SER A 150 ? 0.371683  0.470824 0.377165 -0.00839174 0.113303    0.036011    150  SER A O   
1142  C  CB  . SER A 150 ? 0.429559  0.505879 0.387699 -0.00516462 0.124868    0.0555855   150  SER A CB  
1143  O  OG  . SER A 150 ? 0.47677   0.547588 0.445853 -0.0113698  0.131225    0.0608493   150  SER A OG  
1144  N  N   . ARG A 151 ? 0.4133    0.512242 0.42695  -0.0165851  0.133568    0.0432377   151  ARG A N   
1145  C  CA  . ARG A 151 ? 0.399006  0.504271 0.438676 -0.0214813  0.13181     0.0379945   151  ARG A CA  
1146  C  C   . ARG A 151 ? 0.445373  0.541396 0.490851 -0.0275625  0.13778     0.0448539   151  ARG A C   
1147  O  O   . ARG A 151 ? 0.436974  0.53674  0.504437 -0.0333988  0.140412    0.0424201   151  ARG A O   
1148  C  CB  . ARG A 151 ? 0.388038  0.508311 0.44452  -0.0225768  0.136455    0.0307031   151  ARG A CB  
1149  C  CG  . ARG A 151 ? 0.348689  0.476694 0.39944  -0.0162467  0.130391    0.024082    151  ARG A CG  
1150  C  CD  . ARG A 151 ? 0.403804  0.534243 0.460502 -0.0131714  0.116552    0.0177999   151  ARG A CD  
1151  N  NE  . ARG A 151 ? 0.411589  0.549212 0.464073 -0.00765512 0.11296     0.0120708   151  ARG A NE  
1152  C  CZ  . ARG A 151 ? 0.466102  0.601372 0.506063 -0.0020365  0.103783    0.0101054   151  ARG A CZ  
1153  N  NH1 . ARG A 151 ? 0.433947  0.577244 0.477117 0.00172021  0.101527    0.00379865  151  ARG A NH1 
1154  N  NH2 . ARG A 151 ? 0.369368  0.495004 0.396342 -0.00020897 0.0965266   0.0136741   151  ARG A NH2 
1155  N  N   . SER A 152 ? 0.412487  0.495596 0.437549 -0.025784   0.139131    0.0535388   152  SER A N   
1156  C  CA  . SER A 152 ? 0.41934   0.490801 0.446682 -0.0306366  0.143986    0.0612918   152  SER A CA  
1157  C  C   . SER A 152 ? 0.408365  0.471488 0.43544  -0.0288391  0.132119    0.0605522   152  SER A C   
1158  O  O   . SER A 152 ? 0.371144  0.428494 0.380536 -0.0230116  0.124832    0.0622862   152  SER A O   
1159  C  CB  . SER A 152 ? 0.463756  0.52578  0.469157 -0.0296917  0.153307    0.071824    152  SER A CB  
1160  O  OG  . SER A 152 ? 0.46905   0.515533 0.467104 -0.030331   0.151387    0.0798918   152  SER A OG  
1161  N  N   . TYR A 153 ? 0.368724  0.432412 0.416821 -0.0337939  0.130044    0.0568987   153  TYR A N   
1162  C  CA  . TYR A 153 ? 0.359538  0.416883 0.409863 -0.0324451  0.11946     0.0545751   153  TYR A CA  
1163  C  C   . TYR A 153 ? 0.391219  0.43281  0.422956 -0.0296243  0.118506    0.0636079   153  TYR A C   
1164  O  O   . TYR A 153 ? 0.362966  0.400365 0.386539 -0.0249465  0.109059    0.062287    153  TYR A O   
1165  C  CB  . TYR A 153 ? 0.337195  0.396704 0.412837 -0.0391087  0.119826    0.0499682   153  TYR A CB  
1166  C  CG  . TYR A 153 ? 0.330221  0.384893 0.40899  -0.0374463  0.108407    0.0455041   153  TYR A CG  
1167  C  CD1 . TYR A 153 ? 0.349392  0.389504 0.419787 -0.0366107  0.106696    0.0513086   153  TYR A CD1 
1168  C  CD2 . TYR A 153 ? 0.314176  0.378615 0.403777 -0.0364     0.0994595   0.0355267   153  TYR A CD2 
1169  C  CE1 . TYR A 153 ? 0.35477   0.390816 0.427972 -0.0347992  0.0969807   0.0466619   153  TYR A CE1 
1170  C  CE2 . TYR A 153 ? 0.308546  0.368575 0.398771 -0.034584   0.0897679   0.0314553   153  TYR A CE2 
1171  C  CZ  . TYR A 153 ? 0.308919  0.355136 0.391238 -0.0338092  0.0888614   0.0366944   153  TYR A CZ  
1172  O  OH  . TYR A 153 ? 0.307383  0.348984 0.390278 -0.0318773  0.0803704   0.032581    153  TYR A OH  
1173  N  N   . ALA A 154 ? 0.385619  0.418406 0.410021 -0.032119   0.12843     0.0731721   154  ALA A N   
1174  C  CA  . ALA A 154 ? 0.397729  0.414582 0.406126 -0.0295966  0.127393    0.0823606   154  ALA A CA  
1175  C  C   . ALA A 154 ? 0.404027  0.41933  0.387177 -0.0216687  0.122848    0.0851251   154  ALA A C   
1176  O  O   . ALA A 154 ? 0.412801  0.418741 0.385209 -0.0171792  0.115504    0.0880839   154  ALA A O   
1177  C  CB  . ALA A 154 ? 0.412556  0.41975  0.421616 -0.0351867  0.139794    0.0923723   154  ALA A CB  
1178  N  N   . MET A 155 ? 0.403371  0.427665 0.377907 -0.0199768  0.127412    0.0839792   155  MET A N   
1179  C  CA  . MET A 155 ? 0.443169  0.467779 0.394994 -0.0127912  0.123432    0.0850972   155  MET A CA  
1180  C  C   . MET A 155 ? 0.396759  0.426606 0.350056 -0.00790732 0.110346    0.0769401   155  MET A C   
1181  O  O   . MET A 155 ? 0.393266  0.417648 0.331551 -0.00223618 0.103313    0.0789667   155  MET A O   
1182  C  CB  . MET A 155 ? 0.482665  0.518003 0.429512 -0.0125405  0.131       0.0827892   155  MET A CB  
1183  C  CG  . MET A 155 ? 0.565636  0.599403 0.486458 -0.00567988 0.129272    0.0852986   155  MET A CG  
1184  S  SD  . MET A 155 ? 0.661891  0.676778 0.559756 -0.00316845 0.130214    0.0988585   155  MET A SD  
1185  C  CE  . MET A 155 ? 0.771606  0.782054 0.659269 0.00469333  0.113823    0.0964974   155  MET A CE  
1186  N  N   . LEU A 156 ? 0.350275  0.391644 0.320938 -0.00988674 0.107588    0.0677379   156  LEU A N   
1187  C  CA  . LEU A 156 ? 0.311427  0.358013 0.28557  -0.00626989 0.0963075   0.060128    156  LEU A CA  
1188  C  C   . LEU A 156 ? 0.301201  0.337976 0.275573 -0.00510332 0.0892736   0.0618992   156  LEU A C   
1189  O  O   . LEU A 156 ? 0.307981  0.344213 0.274391 2.619e-05   0.0808117   0.0599154   156  LEU A O   
1190  C  CB  . LEU A 156 ? 0.283512  0.342032 0.277765 -0.00963383 0.0956023   0.0514744   156  LEU A CB  
1191  C  CG  . LEU A 156 ? 0.275344  0.345162 0.271143 -0.00963665 0.101029    0.0479788   156  LEU A CG  
1192  C  CD1 . LEU A 156 ? 0.251697  0.332161 0.270427 -0.0136037  0.100665    0.0403388   156  LEU A CD1 
1193  C  CD2 . LEU A 156 ? 0.242033  0.315964 0.224225 -0.00338224 0.0956286   0.0449846   156  LEU A CD2 
1194  N  N   . LEU A 157 ? 0.300261  0.32944  0.284338 -0.00978313 0.0930447   0.065366    157  LEU A N   
1195  C  CA  . LEU A 157 ? 0.301283  0.321037 0.288034 -0.0089526  0.0869823   0.0661952   157  LEU A CA  
1196  C  C   . LEU A 157 ? 0.323674  0.332759 0.291203 -0.00351836 0.0845224   0.0737574   157  LEU A C   
1197  O  O   . LEU A 157 ? 0.286831  0.292735 0.250967 0.00083948  0.0761871   0.0721869   157  LEU A O   
1198  C  CB  . LEU A 157 ? 0.313118  0.32695  0.315901 -0.0154118  0.0917308   0.0675468   157  LEU A CB  
1199  C  CG  . LEU A 157 ? 0.32716   0.33077  0.334616 -0.0147885  0.0859329   0.0674959   157  LEU A CG  
1200  C  CD1 . LEU A 157 ? 0.341433  0.35298  0.355555 -0.0124735  0.0764984   0.0575265   157  LEU A CD1 
1201  C  CD2 . LEU A 157 ? 0.3482    0.343954 0.37066  -0.0211154  0.0909237   0.0694533   157  LEU A CD2 
1202  N  N   . PHE A 158 ? 0.340117  0.343422 0.295676 -0.00399106 0.092289    0.0822459   158  PHE A N   
1203  C  CA  . PHE A 158 ? 0.348476  0.341537 0.283999 0.00145419  0.0900091   0.0901042   158  PHE A CA  
1204  C  C   . PHE A 158 ? 0.335721  0.335222 0.260653 0.00820923  0.0809697   0.0852918   158  PHE A C   
1205  O  O   . PHE A 158 ? 0.338831  0.33196  0.256777 0.0131201   0.0734941   0.0870417   158  PHE A O   
1206  C  CB  . PHE A 158 ? 0.381199  0.369845 0.303304 5.1e-05     0.100346    0.0989201   158  PHE A CB  
1207  C  CG  . PHE A 158 ? 0.411856  0.388579 0.311989 0.00600188  0.0972333   0.107743    158  PHE A CG  
1208  C  CD1 . PHE A 158 ? 0.445863  0.407889 0.346024 0.00626926  0.0956606   0.114905    158  PHE A CD1 
1209  C  CD2 . PHE A 158 ? 0.416792  0.39693  0.297093 0.0116      0.095097    0.108274    158  PHE A CD2 
1210  C  CE1 . PHE A 158 ? 0.491196  0.441917 0.371222 0.0122957   0.0919841   0.123361    158  PHE A CE1 
1211  C  CE2 . PHE A 158 ? 0.447755  0.417043 0.307736 0.0175235   0.0909613   0.11606     158  PHE A CE2 
1212  C  CZ  . PHE A 158 ? 0.47523   0.429995 0.334969 0.0179754   0.0893516   0.123828    158  PHE A CZ  
1213  N  N   . ALA A 159 ? 0.308937  0.320753 0.233599 0.00846888  0.0818012   0.0793097   159  ALA A N   
1214  C  CA  . ALA A 159 ? 0.295892  0.313915 0.211534 0.014271    0.0739812   0.0745511   159  ALA A CA  
1215  C  C   . ALA A 159 ? 0.28493   0.30588  0.211977 0.0156125   0.0647334   0.0678909   159  ALA A C   
1216  O  O   . ALA A 159 ? 0.278748  0.29839  0.198778 0.0207782   0.0569591   0.067083    159  ALA A O   
1217  C  CB  . ALA A 159 ? 0.283711  0.313449 0.198774 0.013814    0.0774924   0.0693657   159  ALA A CB  
1218  N  N   . TRP A 160 ? 0.261337  0.287272 0.205904 0.0110445   0.0656652   0.0626056   160  TRP A N   
1219  C  CA  . TRP A 160 ? 0.24016   0.269114 0.194728 0.0119599   0.0579495   0.0561687   160  TRP A CA  
1220  C  C   . TRP A 160 ? 0.245177  0.263742 0.198001 0.0144428   0.0535411   0.0595239   160  TRP A C   
1221  O  O   . TRP A 160 ? 0.241301  0.261026 0.191978 0.0186275   0.0464346   0.0567687   160  TRP A O   
1222  C  CB  . TRP A 160 ? 0.21911   0.253868 0.191371 0.00663234  0.059774    0.0504902   160  TRP A CB  
1223  C  CG  . TRP A 160 ? 0.207676  0.246979 0.187663 0.0078271   0.0522689   0.0433985   160  TRP A CG  
1224  C  CD1 . TRP A 160 ? 0.198246  0.247148 0.180221 0.0091122   0.0484179   0.0374066   160  TRP A CD1 
1225  C  CD2 . TRP A 160 ? 0.220638  0.254362 0.206085 0.00818001  0.0481074   0.0419813   160  TRP A CD2 
1226  N  NE1 . TRP A 160 ? 0.187678  0.237638 0.175658 0.00978847  0.042656    0.032679    160  TRP A NE1 
1227  C  CE2 . TRP A 160 ? 0.211694  0.252771 0.20159  0.00943549  0.0424232   0.0350177   160  TRP A CE2 
1228  C  CE3 . TRP A 160 ? 0.236869  0.259718 0.223873 0.00769861  0.048844    0.0458969   160  TRP A CE3 
1229  C  CZ2 . TRP A 160 ? 0.231226  0.269767 0.226195 0.0102325   0.0380476   0.0315881   160  TRP A CZ2 
1230  C  CZ3 . TRP A 160 ? 0.265661  0.285916 0.258662 0.00884984  0.0438922   0.0419888   160  TRP A CZ3 
1231  C  CH2 . TRP A 160 ? 0.236346  0.264708 0.232985 0.0101108   0.0387818   0.0346927   160  TRP A CH2 
1232  N  N   . GLU A 161 ? 0.255038  0.263709 0.210642 0.0117116   0.0578543   0.065024    161  GLU A N   
1233  C  CA  . GLU A 161 ? 0.286259  0.284364 0.242438 0.014003    0.0538872   0.0678763   161  GLU A CA  
1234  C  C   . GLU A 161 ? 0.294083  0.286732 0.233733 0.0204618   0.0498006   0.0734212   161  GLU A C   
1235  O  O   . GLU A 161 ? 0.265785  0.256238 0.205616 0.0248396   0.0427396   0.0718736   161  GLU A O   
1236  C  CB  . GLU A 161 ? 0.327974  0.315636 0.290365 0.00936306  0.0602477   0.0734226   161  GLU A CB  
1237  C  CG  . GLU A 161 ? 0.3958    0.370459 0.358944 0.0118229   0.0568212   0.0773137   161  GLU A CG  
1238  C  CD  . GLU A 161 ? 0.445533  0.409117 0.414999 0.00667661  0.0639052   0.0834066   161  GLU A CD  
1239  O  OE1 . GLU A 161 ? 0.541003  0.502177 0.50399  0.00388215  0.0716385   0.0901724   161  GLU A OE1 
1240  O  OE2 . GLU A 161 ? 0.436977  0.394004 0.418038 0.00544297  0.0619848   0.0813234   161  GLU A OE2 
1241  N  N   . GLY A 162 ? 0.295206  0.28561  0.220874 0.0210639   0.0544306   0.079786    162  GLY A N   
1242  C  CA  . GLY A 162 ? 0.308903  0.294034 0.216974 0.0273801   0.0502368   0.0851763   162  GLY A CA  
1243  C  C   . GLY A 162 ? 0.294739  0.288242 0.202087 0.0323774   0.0410744   0.0782711   162  GLY A C   
1244  O  O   . GLY A 162 ? 0.284948  0.273641 0.188753 0.0375585   0.0340206   0.079674    162  GLY A O   
1245  N  N   . TRP A 163 ? 0.271501  0.277145 0.182522 0.0309508   0.0412799   0.0712098   163  TRP A N   
1246  C  CA  . TRP A 163 ? 0.262865  0.27704  0.174548 0.0346204   0.0338054   0.0645179   163  TRP A CA  
1247  C  C   . TRP A 163 ? 0.263374  0.277709 0.187172 0.0357386   0.0278696   0.0603049   163  TRP A C   
1248  O  O   . TRP A 163 ? 0.248512  0.26306  0.170198 0.0406305   0.0208089   0.0591004   163  TRP A O   
1249  C  CB  . TRP A 163 ? 0.251517  0.277483 0.16645  0.0323817   0.035778    0.0581001   163  TRP A CB  
1250  C  CG  . TRP A 163 ? 0.244363  0.277576 0.160841 0.0358549   0.028186    0.0518942   163  TRP A CG  
1251  C  CD1 . TRP A 163 ? 0.230563  0.270828 0.159065 0.0347695   0.0249316   0.0452083   163  TRP A CD1 
1252  C  CD2 . TRP A 163 ? 0.259674  0.292281 0.164529 0.041437    0.0222963   0.0526365   163  TRP A CD2 
1253  N  NE1 . TRP A 163 ? 0.23384   0.278067 0.159817 0.0388049   0.018324    0.0419989   163  TRP A NE1 
1254  C  CE2 . TRP A 163 ? 0.256385  0.296293 0.168731 0.0429447   0.0161975   0.0460202   163  TRP A CE2 
1255  C  CE3 . TRP A 163 ? 0.294913  0.32128  0.183174 0.045266    0.0216443   0.0584179   163  TRP A CE3 
1256  C  CZ2 . TRP A 163 ? 0.272694  0.314531 0.178737 0.0478887   0.00918403  0.0442663   163  TRP A CZ2 
1257  C  CZ3 . TRP A 163 ? 0.315503  0.34361  0.196146 0.0507333   0.0138251   0.05654     163  TRP A CZ3 
1258  C  CH2 . TRP A 163 ? 0.286401  0.322376 0.177107 0.0518492   0.00759298  0.0492587   163  TRP A CH2 
1259  N  N   . HIS A 164 ? 0.239478  0.254717 0.176718 0.0311783   0.0307463   0.0572213   164  HIS A N   
1260  C  CA  . HIS A 164 ? 0.227028  0.243473 0.175296 0.0318889   0.0262258   0.052217    164  HIS A CA  
1261  C  C   . HIS A 164 ? 0.232557  0.239038 0.179275 0.0358098   0.0227829   0.0564104   164  HIS A C   
1262  O  O   . HIS A 164 ? 0.227707  0.236354 0.177842 0.0395458   0.0169938   0.0530937   164  HIS A O   
1263  C  CB  . HIS A 164 ? 0.204794  0.223908 0.166121 0.0264411   0.0296664   0.047696    164  HIS A CB  
1264  C  CG  . HIS A 164 ? 0.203056  0.233565 0.167703 0.024259    0.0300366   0.0418846   164  HIS A CG  
1265  N  ND1 . HIS A 164 ? 0.191543  0.226463 0.15367  0.0217154   0.0345282   0.0425008   164  HIS A ND1 
1266  C  CD2 . HIS A 164 ? 0.184602  0.222366 0.154992 0.0245565   0.0264674   0.0356408   164  HIS A CD2 
1267  C  CE1 . HIS A 164 ? 0.19186   0.236224 0.158351 0.0209744   0.0328668   0.0366982   164  HIS A CE1 
1268  N  NE2 . HIS A 164 ? 0.196784  0.24282  0.16801  0.0224625   0.0279991   0.0326993   164  HIS A NE2 
1269  N  N   . ASN A 165 ? 0.257966  0.253786 0.200019 0.0351102   0.026388    0.0637347   165  ASN A N   
1270  C  CA  . ASN A 165 ? 0.282124  0.267036 0.222266 0.039335    0.0228116   0.0686251   165  ASN A CA  
1271  C  C   . ASN A 165 ? 0.303451  0.288976 0.231949 0.0460776   0.0161416   0.0707712   165  ASN A C   
1272  O  O   . ASN A 165 ? 0.309184  0.292635 0.241069 0.0507799   0.00991096  0.0698094   165  ASN A O   
1273  C  CB  . ASN A 165 ? 0.30789   0.279906 0.245084 0.0369849   0.0283318   0.0770067   165  ASN A CB  
1274  C  CG  . ASN A 165 ? 0.324038  0.294015 0.275671 0.0307407   0.0334823   0.0742857   165  ASN A CG  
1275  O  OD1 . ASN A 165 ? 0.306767  0.283616 0.270189 0.0290974   0.0318211   0.0660577   165  ASN A OD1 
1276  N  ND2 . ASN A 165 ? 0.354892  0.314921 0.305948 0.027228    0.0396023   0.0810955   165  ASN A ND2 
1277  N  N   . ALA A 166 ? 0.314946  0.303114 0.229868 0.0468627   0.0172365   0.0734904   166  ALA A N   
1278  C  CA  . ALA A 166 ? 0.320607  0.307959 0.222375 0.0532608   0.0108015   0.0760945   166  ALA A CA  
1279  C  C   . ALA A 166 ? 0.315869  0.31374  0.224547 0.0562843   0.00351636  0.0679919   166  ALA A C   
1280  O  O   . ALA A 166 ? 0.310757  0.30691  0.218566 0.0619545   -0.00394202 0.0683087   166  ALA A O   
1281  C  CB  . ALA A 166 ? 0.333484  0.321724 0.218909 0.0527623   0.0147798   0.0797792   166  ALA A CB  
1282  N  N   . ALA A 167 ? 0.298087  0.306652 0.214752 0.0525075   0.00559381  0.0608651   167  ALA A N   
1283  C  CA  . ALA A 167 ? 0.29586   0.314309 0.219283 0.0544465   -4.521e-05  0.0536381   167  ALA A CA  
1284  C  C   . ALA A 167 ? 0.301962  0.321487 0.240625 0.0542814   -0.00176976 0.0495071   167  ALA A C   
1285  O  O   . ALA A 167 ? 0.313442  0.335584 0.256566 0.0584155   -0.00787571 0.046961    167  ALA A O   
1286  C  CB  . ALA A 167 ? 0.280333  0.308612 0.204536 0.051057    0.0025609   0.0485487   167  ALA A CB  
1287  N  N   . GLY A 168 ? 0.267418  0.285122 0.214315 0.0497205   0.00349663  0.048457    168  GLY A N   
1288  C  CA  . GLY A 168 ? 0.228086  0.248699 0.188572 0.0491928   0.00253136  0.0428735   168  GLY A CA  
1289  C  C   . GLY A 168 ? 0.246568  0.259935 0.211608 0.0535483   -0.00108807 0.0445411   168  GLY A C   
1290  O  O   . GLY A 168 ? 0.236107  0.254127 0.209053 0.0565068   -0.00507976 0.040138    168  GLY A O   
1291  N  N   . ILE A 169 ? 0.266002  0.267883 0.226537 0.0540714   0.00045295  0.0510922   169  ILE A N   
1292  C  CA  . ILE A 169 ? 0.292062  0.285331 0.258454 0.0577968   -0.00232194 0.052793    169  ILE A CA  
1293  C  C   . ILE A 169 ? 0.298877  0.294522 0.265879 0.0647655   -0.0102605  0.0520901   169  ILE A C   
1294  O  O   . ILE A 169 ? 0.303379  0.30112  0.282413 0.0671635   -0.0127252  0.0473237   169  ILE A O   
1295  C  CB  . ILE A 169 ? 0.288964  0.268069 0.249989 0.0570941   0.00071424  0.0610126   169  ILE A CB  
1296  C  CG1 . ILE A 169 ? 0.285274  0.262951 0.251563 0.0498685   0.00825633  0.0597336   169  ILE A CG1 
1297  C  CG2 . ILE A 169 ? 0.315236  0.284715 0.282203 0.0624133   -0.00373577 0.0630506   169  ILE A CG2 
1298  C  CD1 . ILE A 169 ? 0.318466  0.282848 0.279284 0.0479351   0.0125906   0.0684702   169  ILE A CD1 
1299  N  N   . PRO A 170 ? 0.30729   0.303374 0.26247  0.0684125   -0.014692   0.0559434   170  PRO A N   
1300  C  CA  . PRO A 170 ? 0.307414  0.306681 0.265241 0.0751422   -0.0232719  0.0543322   170  PRO A CA  
1301  C  C   . PRO A 170 ? 0.264394  0.277371 0.23382  0.0750037   -0.0255058  0.0454949   170  PRO A C   
1302  O  O   . PRO A 170 ? 0.272297  0.288796 0.250034 0.079778    -0.0314831  0.0426095   170  PRO A O   
1303  C  CB  . PRO A 170 ? 0.336642  0.332959 0.276872 0.0784814   -0.0272572  0.0602701   170  PRO A CB  
1304  C  CG  . PRO A 170 ? 0.373827  0.362074 0.302659 0.0738954   -0.0195994  0.066767    170  PRO A CG  
1305  C  CD  . PRO A 170 ? 0.320686  0.313518 0.259704 0.0667751   -0.0119306  0.0619613   170  PRO A CD  
1306  N  N   . LEU A 171 ? 0.242505  0.263273 0.213239 0.0695793   -0.0207018  0.0413338   171  LEU A N   
1307  C  CA  . LEU A 171 ? 0.231573  0.264418 0.212206 0.0686782   -0.0217788  0.0339458   171  LEU A CA  
1308  C  C   . LEU A 171 ? 0.226625  0.262064 0.222301 0.068176    -0.0197574  0.0287786   171  LEU A C   
1309  O  O   . LEU A 171 ? 0.237237  0.281496 0.242803 0.0692894   -0.0217577  0.0234666   171  LEU A O   
1310  C  CB  . LEU A 171 ? 0.217147  0.256246 0.193692 0.0632466   -0.0173251  0.031811    171  LEU A CB  
1311  C  CG  . LEU A 171 ? 0.244127  0.284721 0.208143 0.0639527   -0.0195863  0.0339854   171  LEU A CG  
1312  C  CD1 . LEU A 171 ? 0.251698  0.297135 0.213372 0.0581916   -0.0138662  0.0319285   171  LEU A CD1 
1313  C  CD2 . LEU A 171 ? 0.228587  0.276771 0.197298 0.0677728   -0.0267361  0.0299285   171  LEU A CD2 
1314  N  N   . LYS A 172 ? 0.220495  0.248528 0.218192 0.0663463   -0.0154969  0.029943    172  LYS A N   
1315  C  CA  . LYS A 172 ? 0.232008  0.263198 0.241931 0.0648336   -0.0122132  0.0239119   172  LYS A CA  
1316  C  C   . LYS A 172 ? 0.224865  0.260042 0.246637 0.0702045   -0.0165796  0.0202347   172  LYS A C   
1317  O  O   . LYS A 172 ? 0.227148  0.271225 0.258188 0.0692163   -0.0147895  0.0141688   172  LYS A O   
1318  C  CB  . LYS A 172 ? 0.228432  0.250033 0.239258 0.0626744   -0.00804739 0.0251707   172  LYS A CB  
1319  C  CG  . LYS A 172 ? 0.250498  0.276809 0.271279 0.0603005   -0.00412227 0.0177536   172  LYS A CG  
1320  C  CD  . LYS A 172 ? 0.288869  0.305805 0.311655 0.05812     -0.00063989 0.0176733   172  LYS A CD  
1321  C  CE  . LYS A 172 ? 0.329894  0.352743 0.361299 0.056726    0.00246603  0.00926735  172  LYS A CE  
1322  N  NZ  . LYS A 172 ? 0.323464  0.339106 0.35967  0.0552989   0.00523884  0.00610796  172  LYS A NZ  
1323  N  N   . PRO A 173 ? 0.242709  0.271356 0.265694 0.0760076   -0.0218909  0.0235723   173  PRO A N   
1324  C  CA  . PRO A 173 ? 0.240166  0.273879 0.276837 0.081346    -0.0262208  0.0193088   173  PRO A CA  
1325  C  C   . PRO A 173 ? 0.229021  0.275381 0.270316 0.0818251   -0.0292909  0.0154605   173  PRO A C   
1326  O  O   . PRO A 173 ? 0.221125  0.275865 0.276405 0.0827332   -0.0285953  0.00942715  173  PRO A O   
1327  C  CB  . PRO A 173 ? 0.260607  0.28416  0.296339 0.0879644   -0.0325508  0.0245465   173  PRO A CB  
1328  C  CG  . PRO A 173 ? 0.28893   0.301642 0.307869 0.0857958   -0.0312797  0.0326933   173  PRO A CG  
1329  C  CD  . PRO A 173 ? 0.250778  0.266696 0.263162 0.077959    -0.0238238  0.0316276   173  PRO A CD  
1330  N  N   . LEU A 174 ? 0.215554  0.263418 0.245666 0.0808032   -0.0319518  0.0185153   174  LEU A N   
1331  C  CA  . LEU A 174 ? 0.216643  0.275589 0.251332 0.0809337   -0.0352699  0.0147145   174  LEU A CA  
1332  C  C   . LEU A 174 ? 0.190082  0.257632 0.230607 0.0750401   -0.0284876  0.00961551  174  LEU A C   
1333  O  O   . LEU A 174 ? 0.177876  0.255046 0.230205 0.0750941   -0.0290203  0.00471658  174  LEU A O   
1334  C  CB  . LEU A 174 ? 0.232405  0.289969 0.252623 0.0813705   -0.0396529  0.0186317   174  LEU A CB  
1335  C  CG  . LEU A 174 ? 0.318015  0.369716 0.331968 0.0882541   -0.0485206  0.0229869   174  LEU A CG  
1336  C  CD1 . LEU A 174 ? 0.358248  0.396518 0.363115 0.0900776   -0.0475601  0.0298946   174  LEU A CD1 
1337  C  CD2 . LEU A 174 ? 0.300104  0.353553 0.30025  0.0883404   -0.0526238  0.0245485   174  LEU A CD2 
1338  N  N   . TYR A 175 ? 0.166189  0.230149 0.198047 0.0699382   -0.0223789  0.0111729   175  TYR A N   
1339  C  CA  . TYR A 175 ? 0.174551  0.245306 0.209171 0.0646267   -0.0165812  0.00734688  175  TYR A CA  
1340  C  C   . TYR A 175 ? 0.168246  0.243701 0.216087 0.0647      -0.0128835  0.00206602  175  TYR A C   
1341  O  O   . TYR A 175 ? 0.156256  0.240298 0.210569 0.0623203   -0.0102275  -0.0016886  175  TYR A O   
1342  C  CB  . TYR A 175 ? 0.167862  0.233733 0.191075 0.0598246   -0.0118794  0.00999078  175  TYR A CB  
1343  C  CG  . TYR A 175 ? 0.160909  0.234141 0.184804 0.0550996   -0.00807365 0.00695805  175  TYR A CG  
1344  C  CD1 . TYR A 175 ? 0.157941  0.235644 0.178238 0.0540994   -0.0103736  0.00736296  175  TYR A CD1 
1345  C  CD2 . TYR A 175 ? 0.145631  0.221147 0.173903 0.0522298   -0.00276428 0.00349906  175  TYR A CD2 
1346  C  CE1 . TYR A 175 ? 0.148639  0.232367 0.170658 0.0501717   -0.00733854 0.00494485  175  TYR A CE1 
1347  C  CE2 . TYR A 175 ? 0.14762   0.229162 0.175723 0.0483748   0.00028688  0.0014982   175  TYR A CE2 
1348  C  CZ  . TYR A 175 ? 0.139039  0.224209 0.164141 0.0472577   -0.00198324 0.00263237  175  TYR A CZ  
1349  O  OH  . TYR A 175 ? 0.142616  0.232583 0.16771  0.0436099   0.00072729  0.00127655  175  TYR A OH  
1350  N  N   A GLU A 176 ? 0.173255  0.242624 0.224672 0.0673154   -0.0122632  0.00189054  176  GLU A N   
1351  N  N   B GLU A 176 ? 0.169115  0.238493 0.220629 0.0673322   -0.0122446  0.00185488  176  GLU A N   
1352  C  CA  A GLU A 176 ? 0.185613  0.258768 0.249325 0.0682464   -0.00863072 -0.00364067 176  GLU A CA  
1353  C  CA  B GLU A 176 ? 0.173415  0.246621 0.23734  0.0683173   -0.00865443 -0.00369662 176  GLU A CA  
1354  C  C   A GLU A 176 ? 0.175495  0.25854  0.25307  0.0712509   -0.0112368  -0.00733071 176  GLU A C   
1355  C  C   B GLU A 176 ? 0.168959  0.252111 0.246565 0.0712368   -0.0112629  -0.00733709 176  GLU A C   
1356  O  O   A GLU A 176 ? 0.15368   0.244683 0.23971  0.0692534   -0.00616039 -0.0121323  176  GLU A O   
1357  O  O   B GLU A 176 ? 0.152548  0.243723 0.238532 0.0692042   -0.00624548 -0.0120868  176  GLU A O   
1358  C  CB  A GLU A 176 ? 0.211763  0.275296 0.277265 0.0715      -0.00898205 -0.00300437 176  GLU A CB  
1359  C  CB  B GLU A 176 ? 0.184829  0.249176 0.251911 0.0717534   -0.00881896 -0.00367201 176  GLU A CB  
1360  C  CG  A GLU A 176 ? 0.237466  0.291089 0.291429 0.0681702   -0.00646991 0.00056992  176  GLU A CG  
1361  C  CG  B GLU A 176 ? 0.186663  0.256054 0.268112 0.0739229   -0.00558595 -0.010394   176  GLU A CG  
1362  C  CD  A GLU A 176 ? 0.278039  0.321747 0.336412 0.0717418   -0.00727812 0.00093047  176  GLU A CD  
1363  C  CD  B GLU A 176 ? 0.20177   0.262698 0.288363 0.0773669   -0.0050821  -0.0120362  176  GLU A CD  
1364  O  OE1 A GLU A 176 ? 0.294546  0.341332 0.365197 0.0762478   -0.00866045 -0.00300457 176  GLU A OE1 
1365  O  OE1 B GLU A 176 ? 0.209564  0.259286 0.288573 0.0777305   -0.00711637 -0.00730531 176  GLU A OE1 
1366  O  OE2 A GLU A 176 ? 0.270597  0.303925 0.32214  0.0703193   -0.00655042 0.00477147  176  GLU A OE2 
1367  O  OE2 B GLU A 176 ? 0.194791  0.260111 0.293449 0.0795901   -0.00218752 -0.0182131  176  GLU A OE2 
1368  N  N   . ASP A 177 ? 0.17361   0.256161 0.2533   0.0759641   -0.0190504  -0.00506794 177  ASP A N   
1369  C  CA  . ASP A 177 ? 0.17933   0.271337 0.274484 0.0794037   -0.0228634  -0.00895649 177  ASP A CA  
1370  C  C   . ASP A 177 ? 0.162024  0.263355 0.258608 0.0752921   -0.021999   -0.010612   177  ASP A C   
1371  O  O   . ASP A 177 ? 0.146078  0.25699  0.256833 0.0745961   -0.0195049  -0.0152954  177  ASP A O   
1372  C  CB  . ASP A 177 ? 0.219251  0.307989 0.315537 0.085975    -0.0327823  -0.00625779 177  ASP A CB  
1373  C  CG  . ASP A 177 ? 0.29489   0.374741 0.393798 0.0914335   -0.0351334  -0.00470099 177  ASP A CG  
1374  O  OD1 . ASP A 177 ? 0.340336  0.417595 0.443321 0.0904165   -0.028896   -0.00716309 177  ASP A OD1 
1375  O  OD2 . ASP A 177 ? 0.348682  0.423614 0.44481  0.0968416   -0.0434793  -0.00099935 177  ASP A OD2 
1376  N  N   . PHE A 178 ? 0.144523  0.242556 0.226588 0.072016    -0.0226822  -0.00686805 178  PHE A N   
1377  C  CA  . PHE A 178 ? 0.14457   0.249618 0.226832 0.0679319   -0.021858   -0.00813563 178  PHE A CA  
1378  C  C   . PHE A 178 ? 0.13551   0.245646 0.222728 0.0629676   -0.012933   -0.0111254  178  PHE A C   
1379  O  O   . PHE A 178 ? 0.131015  0.249617 0.228567 0.0610017   -0.011278   -0.0140848  178  PHE A O   
1380  C  CB  . PHE A 178 ? 0.157815  0.257769 0.223453 0.0656849   -0.0236228  -0.00397553 178  PHE A CB  
1381  C  CG  . PHE A 178 ? 0.174398  0.279414 0.239222 0.0599592   -0.0190588  -0.00533211 178  PHE A CG  
1382  C  CD1 . PHE A 178 ? 0.192873  0.30506  0.265199 0.0591838   -0.0220445  -0.00780405 178  PHE A CD1 
1383  C  CD2 . PHE A 178 ? 0.206024  0.307972 0.262563 0.0555615   -0.0125523  -0.00402205 178  PHE A CD2 
1384  C  CE1 . PHE A 178 ? 0.194674  0.310395 0.267046 0.0540672   -0.0178914  -0.00859162 178  PHE A CE1 
1385  C  CE2 . PHE A 178 ? 0.234196  0.340028 0.289939 0.0508361   -0.0088363  -0.00477038 178  PHE A CE2 
1386  C  CZ  . PHE A 178 ? 0.230711  0.342967 0.294136 0.0500633   -0.0113596  -0.00670938 178  PHE A CZ  
1387  N  N   . THR A 179 ? 0.140372  0.245072 0.219921 0.0608912   -0.00728245 -0.0102829  179  THR A N   
1388  C  CA  . THR A 179 ? 0.13732   0.245343 0.217255 0.0564077   0.00089804  -0.0125904  179  THR A CA  
1389  C  C   . THR A 179 ? 0.121213  0.237339 0.217159 0.0575935   0.00447654  -0.0174395  179  THR A C   
1390  O  O   . THR A 179 ? 0.107824  0.230902 0.208962 0.0542028   0.00929445  -0.0192039  179  THR A O   
1391  C  CB  . THR A 179 ? 0.152899  0.25334  0.223003 0.0551943   0.00477222  -0.0118722  179  THR A CB  
1392  O  OG1 . THR A 179 ? 0.198447  0.293651 0.255187 0.0527417   0.00297759  -0.00767994 179  THR A OG1 
1393  C  CG2 . THR A 179 ? 0.158053  0.262246 0.228481 0.0516606   0.0125524   -0.0150361  179  THR A CG2 
1394  N  N   . ALA A 180 ? 0.12706   0.242055 0.231454 0.0625765   0.00240466  -0.0194699  180  ALA A N   
1395  C  CA  . ALA A 180 ? 0.121826  0.245113 0.243275 0.0643555   0.00600925  -0.0247253  180  ALA A CA  
1396  C  C   . ALA A 180 ? 0.114775  0.248184 0.249718 0.0639062   0.00375849  -0.0262882  180  ALA A C   
1397  O  O   . ALA A 180 ? 0.106518  0.248293 0.252054 0.0615008   0.0102066   -0.0295955  180  ALA A O   
1398  C  CB  . ALA A 180 ? 0.130093  0.249921 0.259324 0.0705146   0.0030712   -0.0267111  180  ALA A CB  
1399  N  N   . LEU A 181 ? 0.111264  0.244121 0.246402 0.0662151   -0.00526654 -0.0242146  181  LEU A N   
1400  C  CA  . LEU A 181 ? 0.111301  0.253664 0.260958 0.066185    -0.00879282 -0.0266318  181  LEU A CA  
1401  C  C   . LEU A 181 ? 0.109774  0.255455 0.255904 0.0595026   -0.00384236 -0.0257378  181  LEU A C   
1402  O  O   . LEU A 181 ? 0.110096  0.264788 0.270764 0.0570865   -0.00045018 -0.0286545  181  LEU A O   
1403  C  CB  . LEU A 181 ? 0.116611  0.256903 0.265239 0.0707081   -0.0204594  -0.0251228  181  LEU A CB  
1404  C  CG  . LEU A 181 ? 0.136254  0.275161 0.293206 0.078106    -0.0268247  -0.0263008  181  LEU A CG  
1405  C  CD1 . LEU A 181 ? 0.153854  0.286839 0.300094 0.0818686   -0.0376852  -0.0226314  181  LEU A CD1 
1406  C  CD2 . LEU A 181 ? 0.137336  0.288272 0.319329 0.080553    -0.0281414  -0.0322295  181  LEU A CD2 
1407  N  N   . SER A 182 ? 0.111534  0.249796 0.239424 0.0565821   -0.00316699 -0.0216516  182  SER A N   
1408  C  CA  . SER A 182 ? 0.11687   0.256796 0.240428 0.0508255   0.00049814  -0.0202611  182  SER A CA  
1409  C  C   . SER A 182 ? 0.114363  0.259021 0.243574 0.047141    0.0107749   -0.0219341  182  SER A C   
1410  O  O   . SER A 182 ? 0.134109  0.284838 0.272012 0.0434557   0.0142388   -0.0226461  182  SER A O   
1411  C  CB  . SER A 182 ? 0.130096  0.26111  0.233695 0.0490806   4.366e-05   -0.0160075  182  SER A CB  
1412  O  OG  . SER A 182 ? 0.141995  0.274123 0.241864 0.0441056   0.00263338  -0.0145936  182  SER A OG  
1413  N  N   . ASN A 183 ? 0.10574   0.247023 0.22903  0.0479139   0.0159732   -0.0224538  183  ASN A N   
1414  C  CA  . ASN A 183 ? 0.1066    0.251796 0.232458 0.0450655   0.0259264   -0.024312   183  ASN A CA  
1415  C  C   . ASN A 183 ? 0.110796  0.266538 0.258101 0.0458486   0.0290479   -0.0285455  183  ASN A C   
1416  O  O   . ASN A 183 ? 0.105269  0.266574 0.257998 0.0417885   0.0362745   -0.0288512  183  ASN A O   
1417  C  CB  . ASN A 183 ? 0.115091  0.255338 0.232616 0.0467348   0.0300181   -0.0257571  183  ASN A CB  
1418  C  CG  . ASN A 183 ? 0.140494  0.272558 0.238298 0.0439653   0.0304894   -0.0222475  183  ASN A CG  
1419  O  OD1 . ASN A 183 ? 0.146835  0.277918 0.237876 0.0405331   0.0293595   -0.0188044  183  ASN A OD1 
1420  N  ND2 . ASN A 183 ? 0.132858  0.258898 0.222913 0.0457622   0.0311188   -0.0233556  183  ASN A ND2 
1421  N  N   A GLU A 184 ? 0.109775  0.268245 0.269811 0.0511226   0.023706    -0.0316318  184  GLU A N   
1422  N  N   B GLU A 184 ? 0.110761  0.269177 0.270739 0.0511523   0.023632    -0.031617   184  GLU A N   
1423  C  CA  A GLU A 184 ? 0.117317  0.286921 0.300502 0.0522759   0.025923    -0.0363005  184  GLU A CA  
1424  C  CA  B GLU A 184 ? 0.115859  0.285292 0.299063 0.052498    0.0253506   -0.036265   184  GLU A CA  
1425  C  C   A GLU A 184 ? 0.118338  0.294724 0.312299 0.048307    0.0247845   -0.0358839  184  GLU A C   
1426  C  C   B GLU A 184 ? 0.119036  0.295251 0.31253  0.0482347   0.0249602   -0.0358081  184  GLU A C   
1427  O  O   A GLU A 184 ? 0.125905  0.310946 0.33437  0.0452907   0.0318857   -0.038115   184  GLU A O   
1428  O  O   B GLU A 184 ? 0.124176  0.308889 0.331635 0.0451895   0.0325117   -0.0380178  184  GLU A O   
1429  C  CB  A GLU A 184 ? 0.130013  0.299985 0.323622 0.0594006   0.0176117   -0.0390337  184  GLU A CB  
1430  C  CB  B GLU A 184 ? 0.117311  0.286972 0.31036  0.0592903   0.0153344   -0.038332   184  GLU A CB  
1431  C  CG  A GLU A 184 ? 0.145351  0.327795 0.365611 0.0613494   0.0182653   -0.0444912  184  GLU A CG  
1432  C  CG  B GLU A 184 ? 0.125741  0.292139 0.319677 0.0644045   0.0165511   -0.0408385  184  GLU A CG  
1433  C  CD  A GLU A 184 ? 0.171825  0.356747 0.406979 0.0689944   0.00991365  -0.0480248  184  GLU A CD  
1434  C  CD  B GLU A 184 ? 0.127328  0.293014 0.330583 0.0714551   0.00561548  -0.0418722  184  GLU A CD  
1435  O  OE1 A GLU A 184 ? 0.209343  0.385913 0.436019 0.0739742   0.00529959  -0.0469488  184  GLU A OE1 
1436  O  OE1 B GLU A 184 ? 0.131993  0.306696 0.353318 0.0729845   0.00105073  -0.0446274  184  GLU A OE1 
1437  O  OE2 A GLU A 184 ? 0.170662  0.366227 0.427657 0.069989    0.00774705  -0.051941   184  GLU A OE2 
1438  O  OE2 B GLU A 184 ? 0.12729   0.283224 0.319871 0.0752872   0.00146861  -0.0397719  184  GLU A OE2 
1439  N  N   . ALA A 185 ? 0.128453  0.300624 0.315153 0.0479431   0.0164222   -0.0330803  185  ALA A N   
1440  C  CA  . ALA A 185 ? 0.136218  0.312996 0.331425 0.0441394   0.0143191   -0.0329176  185  ALA A CA  
1441  C  C   . ALA A 185 ? 0.146637  0.323454 0.337154 0.0372772   0.0243206   -0.0301901  185  ALA A C   
1442  O  O   . ALA A 185 ? 0.15179   0.336438 0.358403 0.03376     0.0295586   -0.0317705  185  ALA A O   
1443  C  CB  . ALA A 185 ? 0.132408  0.302351 0.315159 0.0456745   0.00393733  -0.0304499  185  ALA A CB  
1444  N  N   . TYR A 186 ? 0.149614  0.317675 0.318629 0.0354172   0.0271854   -0.0259642  186  TYR A N   
1445  C  CA  . TYR A 186 ? 0.151487  0.317834 0.313206 0.0295061   0.0346355   -0.0224115  186  TYR A CA  
1446  C  C   . TYR A 186 ? 0.141286  0.312189 0.307114 0.0273535   0.0464613   -0.0233046  186  TYR A C   
1447  O  O   . TYR A 186 ? 0.14665   0.318959 0.31314  0.0222505   0.0538148   -0.0207724  186  TYR A O   
1448  C  CB  . TYR A 186 ? 0.143282  0.299467 0.281992 0.0285627   0.0326868   -0.0179423  186  TYR A CB  
1449  C  CG  . TYR A 186 ? 0.173067  0.32714  0.311797 0.0285943   0.0237324   -0.0170591  186  TYR A CG  
1450  C  CD1 . TYR A 186 ? 0.191521  0.347446 0.337151 0.0243264   0.0244022   -0.0159737  186  TYR A CD1 
1451  C  CD2 . TYR A 186 ? 0.20006   0.350117 0.332218 0.0329503   0.0149187   -0.0174918  186  TYR A CD2 
1452  C  CE1 . TYR A 186 ? 0.182963  0.337034 0.329013 0.0246109   0.0160804   -0.0162493  186  TYR A CE1 
1453  C  CE2 . TYR A 186 ? 0.227356  0.375528 0.35783  0.0332061   0.00712533  -0.0171635  186  TYR A CE2 
1454  C  CZ  . TYR A 186 ? 0.223231  0.373521 0.360604 0.0291151   0.00766254  -0.0169643  186  TYR A CZ  
1455  O  OH  . TYR A 186 ? 0.242759  0.391641 0.379807 0.0296582   -0.00015976 -0.0178668  186  TYR A OH  
1456  N  N   . LYS A 187 ? 0.149907  0.322359 0.317275 0.0312495   0.048699    -0.026668   187  LYS A N   
1457  C  CA  . LYS A 187 ? 0.197405  0.374723 0.368414 0.0296671   0.0603518   -0.02842    187  LYS A CA  
1458  C  C   . LYS A 187 ? 0.21976   0.408308 0.414967 0.0271903   0.0652627   -0.0308233  187  LYS A C   
1459  O  O   . LYS A 187 ? 0.195086  0.387603 0.392697 0.0233727   0.0764214   -0.0301943  187  LYS A O   
1460  C  CB  . LYS A 187 ? 0.278865  0.456238 0.450027 0.0349933   0.0611972   -0.0329246  187  LYS A CB  
1461  C  CG  . LYS A 187 ? 0.411191  0.591121 0.578413 0.0335447   0.0738526   -0.0347848  187  LYS A CG  
1462  C  CD  . LYS A 187 ? 0.542797  0.730074 0.725277 0.0376529   0.0786702   -0.0415308  187  LYS A CD  
1463  C  CE  . LYS A 187 ? 0.600863  0.793792 0.783729 0.0345627   0.0928642   -0.0429967  187  LYS A CE  
1464  N  NZ  . LYS A 187 ? 0.727434  0.92917  0.928393 0.0384527   0.0982127   -0.0502024  187  LYS A NZ  
1465  N  N   . GLN A 188 ? 0.213476  0.407247 0.426697 0.028931    0.0571094   -0.0333854  188  GLN A N   
1466  C  CA  . GLN A 188 ? 0.24412   0.44882  0.482037 0.0257877   0.0614015   -0.03581    188  GLN A CA  
1467  C  C   . GLN A 188 ? 0.241246  0.443947 0.477993 0.0191326   0.0631436   -0.031199   188  GLN A C   
1468  O  O   . GLN A 188 ? 0.252255  0.462734 0.508061 0.0150624   0.0684665   -0.0321439  188  GLN A O   
1469  C  CB  . GLN A 188 ? 0.24482   0.456708 0.504332 0.0302994   0.0514467   -0.0411213  188  GLN A CB  
1470  C  CG  . GLN A 188 ? 0.339664  0.555707 0.607319 0.036665    0.051409    -0.0462151  188  GLN A CG  
1471  C  CD  . GLN A 188 ? 0.479168  0.699437 0.762873 0.04231     0.0385586   -0.0503151  188  GLN A CD  
1472  O  OE1 . GLN A 188 ? 0.563769  0.776599 0.835638 0.0474269   0.0286013   -0.0494233  188  GLN A OE1 
1473  N  NE2 . GLN A 188 ? 0.533681  0.765651 0.844184 0.0411592   0.0382541   -0.0544971  188  GLN A NE2 
1474  N  N   . ASP A 189 ? 0.232704  0.424998 0.448497 0.0178952   0.0589418   -0.0262909  189  ASP A N   
1475  C  CA  . ASP A 189 ? 0.224454  0.413226 0.436762 0.0117832   0.0618798   -0.0213917  189  ASP A CA  
1476  C  C   . ASP A 189 ? 0.24645   0.431597 0.443814 0.0081654   0.074159    -0.0167438  189  ASP A C   
1477  O  O   . ASP A 189 ? 0.291011  0.472146 0.48337  0.00319075  0.0779653   -0.0116704  189  ASP A O   
1478  C  CB  . ASP A 189 ? 0.243644  0.423924 0.443398 0.012432    0.0511917   -0.0189952  189  ASP A CB  
1479  C  CG  . ASP A 189 ? 0.252493  0.435559 0.464357 0.0156686   0.038821    -0.0232232  189  ASP A CG  
1480  O  OD1 . ASP A 189 ? 0.269045  0.460347 0.504104 0.01404     0.0376516   -0.02677    189  ASP A OD1 
1481  O  OD2 . ASP A 189 ? 0.25562   0.43233  0.453316 0.0194693   0.0301917   -0.0228308  189  ASP A OD2 
1482  N  N   . GLY A 190 ? 0.241931  0.428031 0.431766 0.0107463   0.0802685   -0.01847    190  GLY A N   
1483  C  CA  . GLY A 190 ? 0.254501  0.437033 0.427573 0.00815511  0.0911808   -0.0148031  190  GLY A CA  
1484  C  C   . GLY A 190 ? 0.260869  0.432236 0.40612  0.00966323  0.0873905   -0.0113862  190  GLY A C   
1485  O  O   . GLY A 190 ? 0.290579  0.458106 0.420059 0.00760175  0.0947679   -0.00803072 190  GLY A O   
1486  N  N   . PHE A 191 ? 0.253579  0.420016 0.392469 0.0133933   0.076377    -0.0124167  191  PHE A N   
1487  C  CA  . PHE A 191 ? 0.234443  0.391399 0.349921 0.0147357   0.0728064   -0.00987525 191  PHE A CA  
1488  C  C   . PHE A 191 ? 0.241636  0.398315 0.351079 0.0190948   0.0738263   -0.0142019  191  PHE A C   
1489  O  O   . PHE A 191 ? 0.267666  0.429353 0.390941 0.0226715   0.0716232   -0.0190142  191  PHE A O   
1490  C  CB  . PHE A 191 ? 0.207249  0.358694 0.31865  0.0158324   0.0615035   -0.00826151 191  PHE A CB  
1491  C  CG  . PHE A 191 ? 0.223394  0.373712 0.338837 0.0114504   0.0608628   -0.00423156 191  PHE A CG  
1492  C  CD1 . PHE A 191 ? 0.203893  0.347302 0.303792 0.00842458  0.0631501   0.0012811   191  PHE A CD1 
1493  C  CD2 . PHE A 191 ? 0.20922   0.365384 0.344978 0.0104203   0.0580331   -0.00624738 191  PHE A CD2 
1494  C  CE1 . PHE A 191 ? 0.214791  0.356228 0.319197 0.00454436  0.0627199   0.00507809  191  PHE A CE1 
1495  C  CE2 . PHE A 191 ? 0.226712  0.381175 0.36722  0.00620182  0.0575309   -0.00302728 191  PHE A CE2 
1496  C  CZ  . PHE A 191 ? 0.214047  0.36071  0.338765 0.00328278  0.0600631   0.00283894  191  PHE A CZ  
1497  N  N   . THR A 192 ? 0.231483  0.382135 0.321055 0.0190529   0.0765426   -0.0128399  192  THR A N   
1498  C  CA  . THR A 192 ? 0.242553  0.391981 0.326406 0.0230526   0.0770305   -0.0175477  192  THR A CA  
1499  C  C   . THR A 192 ? 0.201167  0.347084 0.28717  0.0272027   0.0666848   -0.01951    192  THR A C   
1500  O  O   . THR A 192 ? 0.197254  0.344292 0.288818 0.0311485   0.0660598   -0.0241634  192  THR A O   
1501  C  CB  . THR A 192 ? 0.31025   0.454212 0.37263  0.0217746   0.0816158   -0.0160333  192  THR A CB  
1502  O  OG1 . THR A 192 ? 0.422822  0.566464 0.482984 0.0256048   0.0825869   -0.0218647  192  THR A OG1 
1503  C  CG2 . THR A 192 ? 0.257225  0.392933 0.303799 0.0207565   0.0746955   -0.0117275  192  THR A CG2 
1504  N  N   . ASP A 193 ? 0.168219  0.309955 0.250901 0.0264536   0.058806    -0.0159088  193  ASP A N   
1505  C  CA  . ASP A 193 ? 0.149697  0.287764 0.232913 0.0299362   0.0496112   -0.0166473  193  ASP A CA  
1506  C  C   . ASP A 193 ? 0.138344  0.274212 0.220265 0.0281364   0.0432657   -0.012768   193  ASP A C   
1507  O  O   . ASP A 193 ? 0.126609  0.262765 0.206566 0.0242881   0.0458269   -0.0096152  193  ASP A O   
1508  C  CB  . ASP A 193 ? 0.166026  0.297135 0.235386 0.0318869   0.0480199   -0.0175579  193  ASP A CB  
1509  C  CG  . ASP A 193 ? 0.195733  0.321208 0.247484 0.0289906   0.0487134   -0.0143376  193  ASP A CG  
1510  O  OD1 . ASP A 193 ? 0.175105  0.297747 0.222626 0.0274163   0.0438925   -0.0105593  193  ASP A OD1 
1511  O  OD2 . ASP A 193 ? 0.216055  0.340608 0.258887 0.0284411   0.0542929   -0.0159952  193  ASP A OD2 
1512  N  N   . THR A 194 ? 0.123939  0.256852 0.205938 0.0310274   0.0350589   -0.0128372  194  THR A N   
1513  C  CA  . THR A 194 ? 0.12173   0.253183 0.203276 0.0299947   0.0288657   -0.0103022  194  THR A CA  
1514  C  C   . THR A 194 ? 0.13307   0.25896  0.199715 0.0268953   0.0295078   -0.00648669 194  THR A C   
1515  O  O   . THR A 194 ? 0.130308  0.256065 0.197809 0.0245269   0.0278453   -0.00430865 194  THR A O   
1516  C  CB  . THR A 194 ? 0.111643  0.240415 0.193216 0.0341581   0.0205638   -0.0109846  194  THR A CB  
1517  O  OG1 . THR A 194 ? 0.11886   0.25245  0.214427 0.0377753   0.0189918   -0.0144396  194  THR A OG1 
1518  C  CG2 . THR A 194 ? 0.109661  0.237198 0.189747 0.0334838   0.0143055   -0.00921211 194  THR A CG2 
1519  N  N   . GLY A 195 ? 0.133982  0.255187 0.187917 0.0271068   0.0312206   -0.00604972 195  GLY A N   
1520  C  CA  . GLY A 195 ? 0.144347  0.260718 0.185207 0.0247507   0.0306803   -0.0028191  195  GLY A CA  
1521  C  C   . GLY A 195 ? 0.156932  0.274733 0.196562 0.0211742   0.0361483   -0.00039769 195  GLY A C   
1522  O  O   . GLY A 195 ? 0.163918  0.279109 0.199067 0.0191217   0.0344224   0.00285411  195  GLY A O   
1523  N  N   . ALA A 196 ? 0.144225  0.266476 0.189855 0.0204718   0.0428592   -0.00181311 196  ALA A N   
1524  C  CA  . ALA A 196 ? 0.136944  0.260193 0.181407 0.0168316   0.0489859   0.00132053  196  ALA A CA  
1525  C  C   . ALA A 196 ? 0.140154  0.265257 0.196187 0.0147086   0.0467391   0.00329004  196  ALA A C   
1526  O  O   . ALA A 196 ? 0.130994  0.253424 0.183609 0.0116539   0.0481718   0.0074232   196  ALA A O   
1527  C  CB  . ALA A 196 ? 0.12809   0.256237 0.176518 0.0163218   0.0580546   -0.00067899 196  ALA A CB  
1528  N  N   . TYR A 197 ? 0.130928  0.260592 0.201533 0.0164366   0.0431686   7.82e-05    197  TYR A N   
1529  C  CA  . TYR A 197 ? 0.130872  0.262008 0.212368 0.0147258   0.0395692   0.00081592  197  TYR A CA  
1530  C  C   . TYR A 197 ? 0.136635  0.261564 0.208445 0.0149025   0.0328732   0.0030014   197  TYR A C   
1531  O  O   . TYR A 197 ? 0.164378  0.28751  0.238365 0.0121321   0.0325636   0.00551246  197  TYR A O   
1532  C  CB  . TYR A 197 ? 0.130455  0.267908 0.228562 0.0171666   0.0359299   -0.00370297 197  TYR A CB  
1533  C  CG  . TYR A 197 ? 0.137017  0.275218 0.244587 0.0163095   0.029549    -0.00420414 197  TYR A CG  
1534  C  CD1 . TYR A 197 ? 0.152185  0.291822 0.269126 0.0119557   0.0327309   -0.00253476 197  TYR A CD1 
1535  C  CD2 . TYR A 197 ? 0.149778  0.286604 0.255933 0.0197707   0.0207252   -0.00628307 197  TYR A CD2 
1536  C  CE1 . TYR A 197 ? 0.172512  0.312579 0.299002 0.0111763   0.0265358   -0.00395893 197  TYR A CE1 
1537  C  CE2 . TYR A 197 ? 0.186509  0.324066 0.300305 0.0193791   0.0145397   -0.00772737 197  TYR A CE2 
1538  C  CZ  . TYR A 197 ? 0.168077  0.307516 0.292878 0.015123    0.0172993   -0.00706297 197  TYR A CZ  
1539  O  OH  . TYR A 197 ? 0.234936  0.374366 0.366837 0.0147763   0.0108244   -0.0091574  197  TYR A OH  
1540  N  N   . TRP A 198 ? 0.120966  0.242661 0.183505 0.0179013   0.0280955   0.00207045  198  TRP A N   
1541  C  CA  . TRP A 198 ? 0.143754  0.260678 0.198907 0.017986    0.0225918   0.00371152  198  TRP A CA  
1542  C  C   . TRP A 198 ? 0.153406  0.265876 0.198833 0.0152276   0.0254832   0.00787366  198  TRP A C   
1543  O  O   . TRP A 198 ? 0.152649  0.262441 0.198314 0.013993    0.0226863   0.00963388  198  TRP A O   
1544  C  CB  . TRP A 198 ? 0.142529  0.256646 0.189129 0.021237    0.0180504   0.00251499  198  TRP A CB  
1545  C  CG  . TRP A 198 ? 0.147523  0.264    0.200757 0.0245413   0.013498    -0.0004583  198  TRP A CG  
1546  C  CD1 . TRP A 198 ? 0.139816  0.261062 0.206208 0.0254289   0.0111512   -0.00290928 198  TRP A CD1 
1547  C  CD2 . TRP A 198 ? 0.148438  0.261729 0.194131 0.0274991   0.00997569  -0.00082916 198  TRP A CD2 
1548  N  NE1 . TRP A 198 ? 0.133052  0.254161 0.19941  0.0293042   0.00601613  -0.00470037 198  TRP A NE1 
1549  C  CE2 . TRP A 198 ? 0.151534  0.267308 0.20481  0.030464    0.00545992  -0.00302315 198  TRP A CE2 
1550  C  CE3 . TRP A 198 ? 0.121053  0.229563 0.154837 0.0277648   0.0100799   0.00059291  198  TRP A CE3 
1551  C  CZ2 . TRP A 198 ? 0.135156  0.247806 0.182635 0.0338041   0.00157897  -0.0029823  198  TRP A CZ2 
1552  C  CZ3 . TRP A 198 ? 0.122756  0.228661 0.152626 0.030518    0.0065117   0.00037594  198  TRP A CZ3 
1553  C  CH2 . TRP A 198 ? 0.131954  0.239476 0.167742 0.0335267   0.00256306  -0.00099493 198  TRP A CH2 
1554  N  N   . ARG A 199 ? 0.134234  0.245623 0.170896 0.0146889   0.0304912   0.00914054  199  ARG A N   
1555  C  CA  . ARG A 199 ? 0.166479  0.273465 0.192476 0.0126222   0.0327588   0.0133344   199  ARG A CA  
1556  C  C   . ARG A 199 ? 0.180923  0.287841 0.213416 0.00920641  0.0365934   0.0168441   199  ARG A C   
1557  O  O   . ARG A 199 ? 0.178369  0.280457 0.205069 0.00772115  0.0359218   0.02092     199  ARG A O   
1558  C  CB  . ARG A 199 ? 0.151727  0.257644 0.165656 0.0130074   0.0370593   0.0134109   199  ARG A CB  
1559  C  CG  . ARG A 199 ? 0.168249  0.27298  0.175845 0.0157612   0.0333222   0.0102667   199  ARG A CG  
1560  C  CD  . ARG A 199 ? 0.175974  0.27933  0.17204  0.0162451   0.0364442   0.00918801  199  ARG A CD  
1561  N  NE  . ARG A 199 ? 0.185449  0.292375 0.184295 0.0160007   0.0433926   0.00745099  199  ARG A NE  
1562  C  CZ  . ARG A 199 ? 0.190865  0.300297 0.194733 0.018211    0.0441903   0.00286138  199  ARG A CZ  
1563  N  NH1 . ARG A 199 ? 0.178514  0.291575 0.185243 0.0182471   0.0509199   0.00073507  199  ARG A NH1 
1564  N  NH2 . ARG A 199 ? 0.159965  0.268038 0.166341 0.0203734   0.0385474   0.00076017  199  ARG A NH2 
1565  N  N   . SER A 200 ? 0.165115  0.277197 0.210699 0.00784     0.0407428   0.0154823   200  SER A N   
1566  C  CA  . SER A 200 ? 0.18439   0.296437 0.237829 0.00394479  0.0453734   0.0189735   200  SER A CA  
1567  C  C   . SER A 200 ? 0.196464  0.304885 0.255582 0.00279559  0.039744    0.0203719   200  SER A C   
1568  O  O   . SER A 200 ? 0.19937   0.304423 0.260707 -0.00048517 0.0427227   0.0247644   200  SER A O   
1569  C  CB  . SER A 200 ? 0.188791  0.308515 0.258929 0.00262111  0.0506467   0.016228    200  SER A CB  
1570  O  OG  . SER A 200 ? 0.190626  0.313749 0.274869 0.00386002  0.0440723   0.0121172   200  SER A OG  
1571  N  N   . TRP A 201 ? 0.182038  0.29032  0.242451 0.00554144  0.031853    0.0168872   201  TRP A N   
1572  C  CA  . TRP A 201 ? 0.221834  0.326819 0.287195 0.00493477  0.0265202   0.0170873   201  TRP A CA  
1573  C  C   . TRP A 201 ? 0.258914  0.356414 0.313005 0.00406549  0.0263424   0.0222118   201  TRP A C   
1574  O  O   . TRP A 201 ? 0.238785  0.332611 0.297489 0.00329505  0.022848    0.0229241   201  TRP A O   
1575  C  CB  . TRP A 201 ? 0.243887  0.349857 0.309025 0.00855849  0.01869     0.012398    201  TRP A CB  
1576  C  CG  . TRP A 201 ? 0.244402  0.356708 0.319699 0.010296    0.0167543   0.00752507  201  TRP A CG  
1577  C  CD1 . TRP A 201 ? 0.262415  0.380052 0.352791 0.00859643  0.0191789   0.00576243  201  TRP A CD1 
1578  C  CD2 . TRP A 201 ? 0.257584  0.371398 0.328783 0.0142761   0.0118433   0.00407407  201  TRP A CD2 
1579  N  NE1 . TRP A 201 ? 0.283609  0.406196 0.379858 0.0117458   0.0150836   0.00106446  201  TRP A NE1 
1580  C  CE2 . TRP A 201 ? 0.278363  0.398152 0.36204  0.0152943   0.0107387   0.00039929  201  TRP A CE2 
1581  C  CE3 . TRP A 201 ? 0.24472   0.355374 0.303521 0.0169797   0.00848654  0.00397446  201  TRP A CE3 
1582  C  CZ2 . TRP A 201 ? 0.264962  0.386683 0.347526 0.0193108   0.00583029  -0.00282205 201  TRP A CZ2 
1583  C  CZ3 . TRP A 201 ? 0.284491  0.397011 0.342254 0.0203566   0.00479751  0.00107284  201  TRP A CZ3 
1584  C  CH2 . TRP A 201 ? 0.315934  0.433425 0.384665 0.0216827   0.00319551  -0.00201869 201  TRP A CH2 
1585  N  N   . TYR A 202 ? 0.219544  0.314717 0.258994 0.00485183  0.0287972   0.0249426   202  TYR A N   
1586  C  CA  . TYR A 202 ? 0.206732  0.295126 0.235514 0.00482315  0.0271915   0.0294547   202  TYR A CA  
1587  C  C   . TYR A 202 ? 0.256286  0.341066 0.282866 0.00148178  0.0336366   0.035721    202  TYR A C   
1588  O  O   . TYR A 202 ? 0.261715  0.339871 0.279905 0.0011709   0.0328078   0.0408204   202  TYR A O   
1589  C  CB  . TYR A 202 ? 0.181058  0.268616 0.195786 0.00768637  0.0247029   0.028616    202  TYR A CB  
1590  C  CG  . TYR A 202 ? 0.172398  0.261672 0.189987 0.0103838   0.01839     0.0239368   202  TYR A CG  
1591  C  CD1 . TYR A 202 ? 0.166997  0.261192 0.188063 0.0119066   0.01806     0.0194461   202  TYR A CD1 
1592  C  CD2 . TYR A 202 ? 0.161646  0.247512 0.178823 0.0115282   0.0131578   0.0241175   202  TYR A CD2 
1593  C  CE1 . TYR A 202 ? 0.167272  0.262486 0.189514 0.0143006   0.0129634   0.0159245   202  TYR A CE1 
1594  C  CE2 . TYR A 202 ? 0.15497   0.242789 0.174045 0.0139179   0.00853526  0.019805    202  TYR A CE2 
1595  C  CZ  . TYR A 202 ? 0.14182   0.234094 0.162863 0.0151353   0.00863716  0.0160658   202  TYR A CZ  
1596  O  OH  . TYR A 202 ? 0.137866  0.231586 0.159194 0.0174592   0.004759    0.0125344   202  TYR A OH  
1597  N  N   . ASN A 203 ? 0.246319  0.335408 0.280765 -0.00095727 0.0403067   0.0356034   203  ASN A N   
1598  C  CA  . ASN A 203 ? 0.310588  0.396835 0.34399  -0.00462638 0.0479743   0.0417126   203  ASN A CA  
1599  C  C   . ASN A 203 ? 0.354107  0.433619 0.367685 -0.00395728 0.0491461   0.0476091   203  ASN A C   
1600  O  O   . ASN A 203 ? 0.338894  0.411075 0.349018 -0.00557716 0.0493858   0.0539742   203  ASN A O   
1601  C  CB  . ASN A 203 ? 0.371925  0.455793 0.420882 -0.00799501 0.0479343   0.0436673   203  ASN A CB  
1602  C  CG  . ASN A 203 ? 0.45717   0.540064 0.508505 -0.0124421  0.0578418   0.0493776   203  ASN A CG  
1603  O  OD1 . ASN A 203 ? 0.501694  0.590464 0.552903 -0.0131669  0.0649207   0.0482406   203  ASN A OD1 
1604  N  ND2 . ASN A 203 ? 0.421331  0.496309 0.473471 -0.0152374  0.0589187   0.0558738   203  ASN A ND2 
1605  N  N   . SER A 204 ? 0.314351  0.39593  0.31499  -0.00133356 0.0492322   0.0453328   204  SER A N   
1606  C  CA  . SER A 204 ? 0.360082  0.435949 0.341548 1.324e-05   0.0484916   0.0495783   204  SER A CA  
1607  C  C   . SER A 204 ? 0.363507  0.443168 0.334045 0.00100619  0.0536505   0.04719     204  SER A C   
1608  O  O   . SER A 204 ? 0.357277  0.441706 0.32889  0.00332076  0.0513402   0.0408601   204  SER A O   
1609  C  CB  . SER A 204 ? 0.406845  0.480213 0.384966 0.00321908  0.0388012   0.0475719   204  SER A CB  
1610  O  OG  . SER A 204 ? 0.553736  0.62184  0.515089 0.00493694  0.0362632   0.051198    204  SER A OG  
1611  N  N   . PRO A 205 ? 0.421119  0.498879 0.380889 -0.00064112 0.0613877   0.0517302   205  PRO A N   
1612  C  CA  . PRO A 205 ? 0.416668  0.498704 0.367045 0.00062241  0.0664851   0.0479118   205  PRO A CA  
1613  C  C   . PRO A 205 ? 0.444104  0.524593 0.379383 0.00433332  0.0600943   0.0446301   205  PRO A C   
1614  O  O   . PRO A 205 ? 0.485821  0.5703   0.416758 0.0058833   0.062358    0.0392443   205  PRO A O   
1615  C  CB  . PRO A 205 ? 0.427907  0.507578 0.369089 -0.00218844 0.076796    0.0542825   205  PRO A CB  
1616  C  CG  . PRO A 205 ? 0.47377   0.544679 0.411199 -0.00355072 0.0735575   0.0625829   205  PRO A CG  
1617  C  CD  . PRO A 205 ? 0.401903  0.473322 0.358093 -0.00372144 0.0661784   0.0603846   205  PRO A CD  
1618  N  N   . THR A 206 ? 0.366963  0.441785 0.295122 0.00579721  0.0521807   0.0474713   206  THR A N   
1619  C  CA  . THR A 206 ? 0.361603  0.435719 0.277561 0.00904791  0.0458369   0.0438709   206  THR A CA  
1620  C  C   . THR A 206 ? 0.366541  0.442931 0.293662 0.0107505   0.0377178   0.0389023   206  THR A C   
1621  O  O   . THR A 206 ? 0.317128  0.392163 0.237468 0.012997    0.0310902   0.0370366   206  THR A O   
1622  C  CB  . THR A 206 ? 0.373652  0.440608 0.272248 0.0101063   0.0424983   0.0498958   206  THR A CB  
1623  O  OG1 . THR A 206 ? 0.392585  0.455277 0.299841 0.00904164  0.039332    0.0551284   206  THR A OG1 
1624  C  CG2 . THR A 206 ? 0.414762  0.478763 0.297594 0.00894533  0.0504735   0.0549851   206  THR A CG2 
1625  N  N   . PHE A 207 ? 0.303308  0.38335  0.247274 0.0097549   0.0381944   0.0366026   207  PHE A N   
1626  C  CA  . PHE A 207 ? 0.284616  0.366416 0.237928 0.0113088   0.0313484   0.0325753   207  PHE A CA  
1627  C  C   . PHE A 207 ? 0.275583  0.358801 0.222986 0.0136992   0.0271531   0.0275309   207  PHE A C   
1628  O  O   . PHE A 207 ? 0.259751  0.341445 0.206186 0.015075    0.0207198   0.027054    207  PHE A O   
1629  C  CB  . PHE A 207 ? 0.267958  0.354478 0.237233 0.0104599   0.0333365   0.0295059   207  PHE A CB  
1630  C  CG  . PHE A 207 ? 0.242696  0.33026  0.220972 0.0118344   0.0269525   0.0265439   207  PHE A CG  
1631  C  CD1 . PHE A 207 ? 0.238337  0.322405 0.217667 0.0121756   0.0218179   0.0287502   207  PHE A CD1 
1632  C  CD2 . PHE A 207 ? 0.248436  0.340257 0.233804 0.0130501   0.0263117   0.0215686   207  PHE A CD2 
1633  C  CE1 . PHE A 207 ? 0.218508  0.304008 0.205416 0.0135481   0.0168977   0.0255467   207  PHE A CE1 
1634  C  CE2 . PHE A 207 ? 0.196921  0.289399 0.18868  0.0143552   0.0211209   0.0193173   207  PHE A CE2 
1635  C  CZ  . PHE A 207 ? 0.208234  0.297878 0.20066  0.0144878   0.0168501   0.0211193   207  PHE A CZ  
1636  N  N   . GLU A 208 ? 0.267936  0.354186 0.212997 0.014194    0.0306854   0.0233087   208  GLU A N   
1637  C  CA  . GLU A 208 ? 0.273865  0.361079 0.215681 0.0160603   0.0268953   0.0180514   208  GLU A CA  
1638  C  C   . GLU A 208 ? 0.275748  0.359755 0.204249 0.0171343   0.0224232   0.018773    208  GLU A C   
1639  O  O   . GLU A 208 ? 0.244522  0.328643 0.174651 0.0182348   0.0165232   0.0161958   208  GLU A O   
1640  C  CB  . GLU A 208 ? 0.303232  0.393426 0.245458 0.0166504   0.0313255   0.01292     208  GLU A CB  
1641  C  CG  . GLU A 208 ? 0.351861  0.445558 0.308912 0.0165035   0.0333095   0.0112448   208  GLU A CG  
1642  C  CD  . GLU A 208 ? 0.415967  0.512463 0.375626 0.0175626   0.0374829   0.00627457  208  GLU A CD  
1643  O  OE1 . GLU A 208 ? 0.39432   0.489983 0.352934 0.019028    0.0343323   0.00216473  208  GLU A OE1 
1644  O  OE2 . GLU A 208 ? 0.403646  0.502974 0.366854 0.0168648   0.0439577   0.00646153  208  GLU A OE2 
1645  N  N   . ASP A 209 ? 0.267528  0.348873 0.183409 0.0168466   0.0251946   0.0223137   209  ASP A N   
1646  C  CA  . ASP A 209 ? 0.34317   0.42108  0.245197 0.0183043   0.020076    0.0236347   209  ASP A CA  
1647  C  C   . ASP A 209 ? 0.315312  0.390491 0.220818 0.0188829   0.0133847   0.027543    209  ASP A C   
1648  O  O   . ASP A 209 ? 0.308085  0.382843 0.21042  0.0206268   0.00643328  0.0256593   209  ASP A O   
1649  C  CB  . ASP A 209 ? 0.419608  0.494171 0.306138 0.017979    0.0246725   0.0283331   209  ASP A CB  
1650  C  CG  . ASP A 209 ? 0.507638  0.584632 0.387147 0.0179533   0.031464    0.0241926   209  ASP A CG  
1651  O  OD1 . ASP A 209 ? 0.517649  0.59818  0.403424 0.0186728   0.0308295   0.0171262   209  ASP A OD1 
1652  O  OD2 . ASP A 209 ? 0.631521  0.706689 0.500302 0.017138    0.0379427   0.0282247   209  ASP A OD2 
1653  N  N   . ASP A 210 ? 0.321891  0.395509 0.235422 0.0175093   0.0152214   0.0323183   210  ASP A N   
1654  C  CA  . ASP A 210 ? 0.304561  0.375501 0.223467 0.0182874   0.00920069  0.0353292   210  ASP A CA  
1655  C  C   . ASP A 210 ? 0.286948  0.36157  0.215859 0.0195084   0.00382021  0.0299077   210  ASP A C   
1656  O  O   . ASP A 210 ? 0.247955  0.321675 0.176541 0.0212601   -0.00266839 0.0298104   210  ASP A O   
1657  C  CB  . ASP A 210 ? 0.322777  0.391331 0.249992 0.01638     0.0124783   0.0402394   210  ASP A CB  
1658  C  CG  . ASP A 210 ? 0.422502  0.486124 0.339248 0.01498     0.0175213   0.0471106   210  ASP A CG  
1659  O  OD1 . ASP A 210 ? 0.443347  0.504664 0.344075 0.0162141   0.0170469   0.0485933   210  ASP A OD1 
1660  O  OD2 . ASP A 210 ? 0.501297  0.563471 0.425891 0.0126034   0.0219708   0.0507182   210  ASP A OD2 
1661  N  N   . LEU A 211 ? 0.239957  0.31878  0.177339 0.018735    0.00668618  0.025421    211  LEU A N   
1662  C  CA  . LEU A 211 ? 0.217353  0.299297 0.163746 0.0195289   0.00301886  0.0209417   211  LEU A CA  
1663  C  C   . LEU A 211 ? 0.216692  0.299712 0.157248 0.0206096   -0.00055698 0.0170733   211  LEU A C   
1664  O  O   . LEU A 211 ? 0.218162  0.302605 0.163618 0.021465    -0.00527214 0.0150136   211  LEU A O   
1665  C  CB  . LEU A 211 ? 0.228332  0.313396 0.182986 0.0186661   0.00715453  0.0179769   211  LEU A CB  
1666  C  CG  . LEU A 211 ? 0.239822  0.325133 0.203332 0.0176578   0.00971577  0.0201268   211  LEU A CG  
1667  C  CD1 . LEU A 211 ? 0.25195   0.340478 0.221377 0.0172872   0.0136775   0.0171288   211  LEU A CD1 
1668  C  CD2 . LEU A 211 ? 0.24621   0.331563 0.217602 0.01837     0.0056433   0.0199587   211  LEU A CD2 
1669  N  N   . GLU A 212 ? 0.224415  0.307181 0.155546 0.0205      0.00195266  0.0154017   212  GLU A N   
1670  C  CA  . GLU A 212 ? 0.26338   0.347067 0.189533 0.0214041   -0.00184178 0.0107426   212  GLU A CA  
1671  C  C   . GLU A 212 ? 0.285764  0.367866 0.206597 0.0229604   -0.00874426 0.0125994   212  GLU A C   
1672  O  O   . GLU A 212 ? 0.281168  0.365366 0.205801 0.0236734   -0.0140289  0.0088058   212  GLU A O   
1673  C  CB  . GLU A 212 ? 0.305033  0.388666 0.222262 0.0213031   0.00202326  0.00747941  212  GLU A CB  
1674  C  CG  . GLU A 212 ? 0.432007  0.516007 0.34314  0.0222923   -0.00279916 0.00214632  212  GLU A CG  
1675  C  CD  . GLU A 212 ? 0.662069  0.746258 0.567017 0.0223609   0.00064702  -0.00321967 212  GLU A CD  
1676  O  OE1 . GLU A 212 ? 0.711121  0.794034 0.605993 0.022539    0.00558494  -0.00127607 212  GLU A OE1 
1677  O  OE2 . GLU A 212 ? 0.838466  0.923837 0.748749 0.0221868   -0.0011093  -0.0093512  212  GLU A OE2 
1678  N  N   . HIS A 213 ? 0.28778   0.366136 0.201058 0.0234768   -0.00872314 0.0185578   213  HIS A N   
1679  C  CA  . HIS A 213 ? 0.34212   0.417996 0.249247 0.0255725   -0.0157459  0.0211823   213  HIS A CA  
1680  C  C   . HIS A 213 ? 0.314607  0.392207 0.235204 0.0263984   -0.0206345  0.0208712   213  HIS A C   
1681  O  O   . HIS A 213 ? 0.279514  0.35826  0.201127 0.0283218   -0.0277423  0.0191335   213  HIS A O   
1682  C  CB  . HIS A 213 ? 0.376801  0.44699  0.271261 0.0258481   -0.0136339  0.028464    213  HIS A CB  
1683  C  CG  . HIS A 213 ? 0.595418  0.664514 0.474339 0.025583    -0.00929922 0.0278915   213  HIS A CG  
1684  N  ND1 . HIS A 213 ? 0.682311  0.746283 0.546872 0.0256187   -0.00598224 0.0344217   213  HIS A ND1 
1685  C  CD2 . HIS A 213 ? 0.667005  0.739204 0.542635 0.0252023   -0.0067285  0.0215722   213  HIS A CD2 
1686  C  CE1 . HIS A 213 ? 0.658372  0.72292  0.510543 0.0254676   -0.0015554  0.031857    213  HIS A CE1 
1687  N  NE2 . HIS A 213 ? 0.748801  0.818302 0.60787  0.0253422   -0.00221074 0.0236875   213  HIS A NE2 
1688  N  N   . LEU A 214 ? 0.273182  0.351343 0.204535 0.0251303   -0.0168987  0.0221163   214  LEU A N   
1689  C  CA  . LEU A 214 ? 0.263108  0.343405 0.207327 0.0258593   -0.0200563  0.02089     214  LEU A CA  
1690  C  C   . LEU A 214 ? 0.223722  0.309177 0.174386 0.0258312   -0.0221682  0.0146378   214  LEU A C   
1691  O  O   . LEU A 214 ? 0.21512   0.302798 0.17176  0.0273056   -0.0274963  0.0128631   214  LEU A O   
1692  C  CB  . LEU A 214 ? 0.258059  0.338493 0.212082 0.0246408   -0.0158922  0.0219535   214  LEU A CB  
1693  C  CG  . LEU A 214 ? 0.325208  0.400587 0.278241 0.0244321   -0.0146265  0.0278337   214  LEU A CG  
1694  C  CD1 . LEU A 214 ? 0.309277  0.385838 0.272777 0.0230098   -0.01075    0.0270585   214  LEU A CD1 
1695  C  CD2 . LEU A 214 ? 0.315605  0.388285 0.27019  0.026917    -0.0211067  0.030117    214  LEU A CD2 
1696  N  N   . TYR A 215 ? 0.210106  0.29739  0.161186 0.0241047   -0.0176466  0.0114339   215  TYR A N   
1697  C  CA  . TYR A 215 ? 0.209308  0.300525 0.167438 0.0234595   -0.0184885  0.00602067  215  TYR A CA  
1698  C  C   . TYR A 215 ? 0.228769  0.321421 0.184107 0.0245095   -0.0247857  0.00292257  215  TYR A C   
1699  O  O   . TYR A 215 ? 0.195006  0.291434 0.159961 0.0245076   -0.0278479  -0.00047476 215  TYR A O   
1700  C  CB  . TYR A 215 ? 0.223409  0.315073 0.182124 0.0217744   -0.0131633  0.00341397  215  TYR A CB  
1701  C  CG  . TYR A 215 ? 0.23265   0.327465 0.201127 0.0209266   -0.0138592  -0.00069911 215  TYR A CG  
1702  C  CD1 . TYR A 215 ? 0.267961  0.36445  0.245435 0.0207787   -0.0124925  7.007e-05   215  TYR A CD1 
1703  C  CD2 . TYR A 215 ? 0.224622  0.320501 0.193315 0.0201732   -0.015592   -0.00531272 215  TYR A CD2 
1704  C  CE1 . TYR A 215 ? 0.278453  0.377666 0.26443  0.0198241   -0.0121617  -0.00280953 215  TYR A CE1 
1705  C  CE2 . TYR A 215 ? 0.236335  0.334746 0.215278 0.0188704   -0.0154961  -0.00837662 215  TYR A CE2 
1706  C  CZ  . TYR A 215 ? 0.26324   0.363311 0.250411 0.0186513   -0.0134201  -0.0067076  215  TYR A CZ  
1707  O  OH  . TYR A 215 ? 0.282572  0.385163 0.279315 0.0172492   -0.0124442  -0.00896574 215  TYR A OH  
1708  N  N   . GLN A 216 ? 0.201295  0.291219 0.143636 0.0254431   -0.026693   0.0039493   216  GLN A N   
1709  C  CA  . GLN A 216 ? 0.239057  0.330347 0.177671 0.0268033   -0.0337158  0.00044942  216  GLN A CA  
1710  C  C   . GLN A 216 ? 0.234969  0.328187 0.180884 0.0288472   -0.0405987  0.00121487  216  GLN A C   
1711  O  O   . GLN A 216 ? 0.244122  0.341067 0.195257 0.0293877   -0.0461542  -0.00346922 216  GLN A O   
1712  C  CB  . GLN A 216 ? 0.304613  0.392323 0.225648 0.0281514   -0.0355189  0.00162654  216  GLN A CB  
1713  C  CG  . GLN A 216 ? 0.420083  0.506827 0.334256 0.0265536   -0.0291908  -0.00096737 216  GLN A CG  
1714  C  CD  . GLN A 216 ? 0.564361  0.647406 0.459543 0.0279218   -0.0291652  0.00084283  216  GLN A CD  
1715  O  OE1 . GLN A 216 ? 0.595007  0.675413 0.481201 0.030031    -0.0339575  0.00506259  216  GLN A OE1 
1716  N  NE2 . GLN A 216 ? 0.506814  0.589346 0.39538  0.0269995   -0.0236615  -0.00215147 216  GLN A NE2 
1717  N  N   . GLN A 217 ? 0.229719  0.320473 0.176941 0.03005     -0.0404627  0.00661733  217  GLN A N   
1718  C  CA  . GLN A 217 ? 0.256761  0.348983 0.211854 0.0325206   -0.0468466  0.00729338  217  GLN A CA  
1719  C  C   . GLN A 217 ? 0.226597  0.324656 0.19917  0.0315885   -0.0455361  0.00326224  217  GLN A C   
1720  O  O   . GLN A 217 ? 0.211251  0.313255 0.1936   0.0333164   -0.0508763  0.00089888  217  GLN A O   
1721  C  CB  . GLN A 217 ? 0.291624  0.378366 0.243604 0.0338742   -0.0461408  0.0142101   217  GLN A CB  
1722  C  CG  . GLN A 217 ? 0.380201  0.460288 0.314791 0.0348644   -0.0468964  0.019871    217  GLN A CG  
1723  C  CD  . GLN A 217 ? 0.42906   0.50348  0.364108 0.0362378   -0.0473355  0.026664    217  GLN A CD  
1724  O  OE1 . GLN A 217 ? 0.476564  0.550074 0.415818 0.0392842   -0.0541547  0.0279498   217  GLN A OE1 
1725  N  NE2 . GLN A 217 ? 0.396993  0.467724 0.329718 0.0340291   -0.0402329  0.0306414   217  GLN A NE2 
1726  N  N   . LEU A 218 ? 0.202291  0.301098 0.178894 0.0290453   -0.0383436  0.00247384  218  LEU A N   
1727  C  CA  . LEU A 218 ? 0.188771  0.292238 0.17957  0.0282409   -0.0360176  -0.00032039 218  LEU A CA  
1728  C  C   . LEU A 218 ? 0.181718  0.28962  0.178649 0.0261687   -0.0354187  -0.00572428 218  LEU A C   
1729  O  O   . LEU A 218 ? 0.188508  0.301103 0.197644 0.0255095   -0.0344284  -0.00848842 218  LEU A O   
1730  C  CB  . LEU A 218 ? 0.168935  0.270243 0.159726 0.0269235   -0.0291594  0.00205111  218  LEU A CB  
1731  C  CG  . LEU A 218 ? 0.193182  0.29008  0.180647 0.0284122   -0.0293801  0.00692332  218  LEU A CG  
1732  C  CD1 . LEU A 218 ? 0.218189  0.313412 0.205273 0.0267704   -0.0230563  0.00829621  218  LEU A CD1 
1733  C  CD2 . LEU A 218 ? 0.235961  0.334555 0.233298 0.0306983   -0.0326357  0.00658844  218  LEU A CD2 
1734  N  N   . GLU A 219 ? 0.181718  0.287772 0.170399 0.0248852   -0.034975   -0.00724162 219  GLU A N   
1735  C  CA  . GLU A 219 ? 0.183617  0.292525 0.178627 0.0224618   -0.0336476  -0.0123171  219  GLU A CA  
1736  C  C   . GLU A 219 ? 0.19292   0.30782  0.200437 0.0225675   -0.0388694  -0.016792   219  GLU A C   
1737  O  O   . GLU A 219 ? 0.171955  0.290321 0.190788 0.0202387   -0.0359636  -0.0198213  219  GLU A O   
1738  C  CB  . GLU A 219 ? 0.23457   0.340591 0.219173 0.021734    -0.034024   -0.0144647  219  GLU A CB  
1739  C  CG  . GLU A 219 ? 0.331526  0.438654 0.323648 0.018812    -0.0305326  -0.0187962  219  GLU A CG  
1740  C  CD  . GLU A 219 ? 0.474629  0.578759 0.459544 0.017787    -0.0296126  -0.0221722  219  GLU A CD  
1741  O  OE1 . GLU A 219 ? 0.482542  0.584396 0.454767 0.0194537   -0.0322439  -0.0220764  219  GLU A OE1 
1742  O  OE2 . GLU A 219 ? 0.566793  0.670432 0.558518 0.0154263   -0.0259119  -0.0247529  219  GLU A OE2 
1743  N  N   . PRO A 220 ? 0.198594  0.315073 0.205039 0.0251022   -0.0469197  -0.0177468  220  PRO A N   
1744  C  CA  . PRO A 220 ? 0.208258  0.331592 0.229333 0.0251711   -0.0519893  -0.0227341  220  PRO A CA  
1745  C  C   . PRO A 220 ? 0.196696  0.324893 0.233305 0.0246572   -0.0480471  -0.0228086  220  PRO A C   
1746  O  O   . PRO A 220 ? 0.209184  0.343551 0.260309 0.0229329   -0.048288   -0.0274483  220  PRO A O   
1747  C  CB  . PRO A 220 ? 0.211977  0.335231 0.227812 0.0291423   -0.0616192  -0.0220976  220  PRO A CB  
1748  C  CG  . PRO A 220 ? 0.2244    0.339958 0.219264 0.0301331   -0.0612654  -0.0178525  220  PRO A CG  
1749  C  CD  . PRO A 220 ? 0.223538  0.335409 0.215424 0.0280808   -0.0515388  -0.0138995  220  PRO A CD  
1750  N  N   . LEU A 221 ? 0.176745  0.302548 0.210933 0.0263266   -0.044982   -0.0181915  221  LEU A N   
1751  C  CA  . LEU A 221 ? 0.158925  0.289235 0.206177 0.0264543   -0.0413443  -0.0187963  221  LEU A CA  
1752  C  C   . LEU A 221 ? 0.159158  0.2906   0.210812 0.0225326   -0.0332191  -0.0201721  221  LEU A C   
1753  O  O   . LEU A 221 ? 0.126482  0.263611 0.191456 0.0210246   -0.0300717  -0.0229837  221  LEU A O   
1754  C  CB  . LEU A 221 ? 0.174891  0.301184 0.217072 0.0288139   -0.0395057  -0.0141516  221  LEU A CB  
1755  C  CG  . LEU A 221 ? 0.212118  0.338021 0.25575  0.0330035   -0.0466738  -0.0127538  221  LEU A CG  
1756  C  CD1 . LEU A 221 ? 0.232802  0.355056 0.265496 0.0345881   -0.0540376  -0.0111798  221  LEU A CD1 
1757  C  CD2 . LEU A 221 ? 0.190512  0.31218  0.23176  0.0346937   -0.0437982  -0.00891114 221  LEU A CD2 
1758  N  N   . TYR A 222 ? 0.135595  0.261128 0.175632 0.0210293   -0.0291943  -0.0175946  222  TYR A N   
1759  C  CA  . TYR A 222 ? 0.128525  0.253542 0.171109 0.0178273   -0.0219436  -0.0179178  222  TYR A CA  
1760  C  C   . TYR A 222 ? 0.123096  0.251482 0.175147 0.0149106   -0.0225717  -0.022537   222  TYR A C   
1761  O  O   . TYR A 222 ? 0.131752  0.262843 0.193522 0.0124156   -0.0174081  -0.0235938  222  TYR A O   
1762  C  CB  . TYR A 222 ? 0.116988  0.235323 0.146876 0.0172718   -0.0182974  -0.0146902  222  TYR A CB  
1763  C  CG  . TYR A 222 ? 0.132126  0.249392 0.165107 0.0144669   -0.0116842  -0.0147182  222  TYR A CG  
1764  C  CD1 . TYR A 222 ? 0.129816  0.24782  0.165591 0.0143912   -0.00629154 -0.0126931  222  TYR A CD1 
1765  C  CD2 . TYR A 222 ? 0.143149  0.257901 0.175462 0.0120992   -0.0108017  -0.0166712  222  TYR A CD2 
1766  C  CE1 . TYR A 222 ? 0.130006  0.246517 0.167879 0.011989    -0.00042637 -0.0120289  222  TYR A CE1 
1767  C  CE2 . TYR A 222 ? 0.131804  0.244366 0.16707  0.00969626  -0.0048856  -0.0159081  222  TYR A CE2 
1768  C  CZ  . TYR A 222 ? 0.122786  0.236034 0.160254 0.00966153  0.00030877  -0.0131071  222  TYR A CZ  
1769  O  OH  . TYR A 222 ? 0.113308  0.223603 0.151965 0.00762368  0.00612529  -0.0113443  222  TYR A OH  
1770  N  N   . LEU A 223 ? 0.126224  0.254258 0.175421 0.0150824   -0.0287458  -0.0254066  223  LEU A N   
1771  C  CA  . LEU A 223 ? 0.130769  0.261529 0.189603 0.0120474   -0.0298434  -0.0306041  223  LEU A CA  
1772  C  C   . LEU A 223 ? 0.117475  0.25661  0.194754 0.0112614   -0.030646   -0.0338678  223  LEU A C   
1773  O  O   . LEU A 223 ? 0.116965  0.258609 0.205867 0.00762355  -0.0270822  -0.0366013  223  LEU A O   
1774  C  CB  . LEU A 223 ? 0.155987  0.285575 0.208428 0.0128743   -0.037628   -0.0343472  223  LEU A CB  
1775  C  CG  . LEU A 223 ? 0.21885   0.340981 0.254394 0.0132303   -0.0362634  -0.0326249  223  LEU A CG  
1776  C  CD1 . LEU A 223 ? 0.222654  0.34394  0.250128 0.0144979   -0.044025   -0.0369016  223  LEU A CD1 
1777  C  CD2 . LEU A 223 ? 0.24248   0.36085  0.279668 0.0100572   -0.0287058  -0.0323061  223  LEU A CD2 
1778  N  N   . ASN A 224 ? 0.118633  0.261949 0.19939  0.0146346   -0.0355106  -0.0338234  224  ASN A N   
1779  C  CA  . ASN A 224 ? 0.121212  0.273461 0.221084 0.0143186   -0.0362492  -0.0375232  224  ASN A CA  
1780  C  C   . ASN A 224 ? 0.115569  0.269813 0.222576 0.0124746   -0.0262343  -0.0355733  224  ASN A C   
1781  O  O   . ASN A 224 ? 0.122479  0.283076 0.245747 0.00958213  -0.0223501  -0.0386807  224  ASN A O   
1782  C  CB  . ASN A 224 ? 0.132473  0.288286 0.234674 0.0190446   -0.0447631  -0.038197   224  ASN A CB  
1783  C  CG  . ASN A 224 ? 0.16286   0.32026  0.265313 0.0199552   -0.0550235  -0.0424995  224  ASN A CG  
1784  O  OD1 . ASN A 224 ? 0.176501  0.341151 0.295325 0.0182874   -0.0579909  -0.0482721  224  ASN A OD1 
1785  N  ND2 . ASN A 224 ? 0.159626  0.310706 0.244494 0.0226569   -0.0606015  -0.0399878  224  ASN A ND2 
1786  N  N   . LEU A 225 ? 0.111371  0.260512 0.20653  0.0141538   -0.0219826  -0.03061    225  LEU A N   
1787  C  CA  . LEU A 225 ? 0.108219  0.258581 0.207022 0.0128914   -0.0127212  -0.028763   225  LEU A CA  
1788  C  C   . LEU A 225 ? 0.118359  0.266817 0.219469 0.00809935  -0.00573028 -0.0284852  225  LEU A C   
1789  O  O   . LEU A 225 ? 0.107721  0.260466 0.220003 0.0054521   0.00079734  -0.0293704  225  LEU A O   
1790  C  CB  . LEU A 225 ? 0.0970304 0.241552 0.181703 0.0154726   -0.0103943  -0.0240555  225  LEU A CB  
1791  C  CG  . LEU A 225 ? 0.108969  0.25416  0.19462  0.0145507   -0.00139467 -0.0224198  225  LEU A CG  
1792  C  CD1 . LEU A 225 ? 0.0946739 0.247705 0.193012 0.0166789   -0.00122628 -0.0254586  225  LEU A CD1 
1793  C  CD2 . LEU A 225 ? 0.116208  0.254877 0.187159 0.0167095   -0.0001272  -0.0183448  225  LEU A CD2 
1794  N  N   . HIS A 226 ? 0.12628   0.267695 0.216626 0.00693634  -0.00670911 -0.0270483  226  HIS A N   
1795  C  CA  . HIS A 226 ? 0.128814  0.266318 0.220179 0.00279833  -0.00150575 -0.0266269  226  HIS A CA  
1796  C  C   . HIS A 226 ? 0.124038  0.267287 0.233393 -0.00102811 -0.00113343 -0.0312896  226  HIS A C   
1797  O  O   . HIS A 226 ? 0.134854  0.278386 0.251832 -0.00459807 0.00648013  -0.0302334  226  HIS A O   
1798  C  CB  . HIS A 226 ? 0.120471  0.250201 0.198411 0.00318162  -0.00446872 -0.0256973  226  HIS A CB  
1799  C  CG  . HIS A 226 ? 0.11756   0.241988 0.196222 -0.00039124 -0.00060943 -0.0257712  226  HIS A CG  
1800  N  ND1 . HIS A 226 ? 0.11346   0.239079 0.202855 -0.0036748  -0.00246294 -0.0304769  226  HIS A ND1 
1801  C  CD2 . HIS A 226 ? 0.117905  0.2349   0.187348 -0.00077906 0.00442467  -0.0216601  226  HIS A CD2 
1802  C  CE1 . HIS A 226 ? 0.120131  0.239007 0.207779 -0.00620018 0.00203107  -0.0290231  226  HIS A CE1 
1803  N  NE2 . HIS A 226 ? 0.120246  0.233817 0.195512 -0.00423814 0.00594111  -0.023594   226  HIS A NE2 
1804  N  N   . ALA A 227 ? 0.116278  0.263964 0.232523 -0.00035833 -0.00940488 -0.0363485  227  ALA A N   
1805  C  CA  . ALA A 227 ? 0.112665  0.266265 0.247471 -0.0040416  -0.0105995  -0.0418774  227  ALA A CA  
1806  C  C   . ALA A 227 ? 0.111347  0.273479 0.263061 -0.00548578 -0.00472899 -0.0425713  227  ALA A C   
1807  O  O   . ALA A 227 ? 0.106744  0.271584 0.272807 -0.0102148  0.0007178   -0.0442191  227  ALA A O   
1808  C  CB  . ALA A 227 ? 0.109507  0.266553 0.246903 -0.00206782 -0.0222444  -0.0475475  227  ALA A CB  
1809  N  N   . PHE A 228 ? 0.113466  0.279333 0.263273 -0.00143335 -0.00532283 -0.0412409  228  PHE A N   
1810  C  CA  . PHE A 228 ? 0.121695  0.296569 0.287478 -0.00189236 -0.00022223 -0.0428432  228  PHE A CA  
1811  C  C   . PHE A 228 ? 0.117256  0.288828 0.279719 -0.0049019  0.0122096   -0.0381882  228  PHE A C   
1812  O  O   . PHE A 228 ? 0.108522  0.285778 0.285849 -0.00846252 0.0195808   -0.0393725  228  PHE A O   
1813  C  CB  . PHE A 228 ? 0.138205  0.315611 0.299562 0.00396551  -0.00469518 -0.0424257  228  PHE A CB  
1814  C  CG  . PHE A 228 ? 0.169401  0.356385 0.346552 0.00465843  0.00044929  -0.0446681  228  PHE A CG  
1815  C  CD1 . PHE A 228 ? 0.194827  0.392435 0.393684 0.00448291  -0.00365264 -0.0507727  228  PHE A CD1 
1816  C  CD2 . PHE A 228 ? 0.188304  0.374041 0.358631 0.00599401  0.00866228  -0.0413261  228  PHE A CD2 
1817  C  CE1 . PHE A 228 ? 0.217271  0.424472 0.432097 0.00527897  0.00153877  -0.0534326  228  PHE A CE1 
1818  C  CE2 . PHE A 228 ? 0.214998  0.409983 0.399945 0.00677058  0.0139466   -0.0442018  228  PHE A CE2 
1819  C  CZ  . PHE A 228 ? 0.216902  0.422528 0.424059 0.00640655  0.0107384   -0.0500984  228  PHE A CZ  
1820  N  N   . VAL A 229 ? 0.103036  0.26567  0.245879 -0.00323827 0.0146603   -0.0327241  229  VAL A N   
1821  C  CA  . VAL A 229 ? 0.105145  0.263503 0.241704 -0.00530552 0.0252766   -0.0277755  229  VAL A CA  
1822  C  C   . VAL A 229 ? 0.102949  0.257436 0.245173 -0.010948   0.0300866   -0.0268844  229  VAL A C   
1823  O  O   . VAL A 229 ? 0.112489  0.268069 0.261322 -0.0144362  0.0395222   -0.0248544  229  VAL A O   
1824  C  CB  . VAL A 229 ? 0.109688  0.259604 0.224752 -0.00182664 0.0251179   -0.0227454  229  VAL A CB  
1825  C  CG1 . VAL A 229 ? 0.114605  0.258705 0.22138  -0.00381623 0.0346369   -0.0174169  229  VAL A CG1 
1826  C  CG2 . VAL A 229 ? 0.116251  0.269653 0.227585 0.00319944  0.022079    -0.0234385  229  VAL A CG2 
1827  N  N   . ARG A 230 ? 0.105728  0.255547 0.246008 -0.0119776  0.0238124   -0.0286191  230  ARG A N   
1828  C  CA  . ARG A 230 ? 0.108611  0.254081 0.255834 -0.0171947  0.0269143   -0.0288303  230  ARG A CA  
1829  C  C   . ARG A 230 ? 0.119267  0.273331 0.28977  -0.0218454  0.0311345   -0.0325092  230  ARG A C   
1830  O  O   . ARG A 230 ? 0.118011  0.269176 0.294621 -0.0266191  0.0398633   -0.0297134  230  ARG A O   
1831  C  CB  . ARG A 230 ? 0.111051  0.251053 0.253293 -0.0170027  0.018635    -0.0317901  230  ARG A CB  
1832  C  CG  . ARG A 230 ? 0.122157  0.25575  0.270273 -0.0219575  0.0215039   -0.0321763  230  ARG A CG  
1833  C  CD  . ARG A 230 ? 0.137727  0.26601  0.278701 -0.020742   0.0129329   -0.0360348  230  ARG A CD  
1834  N  NE  . ARG A 230 ? 0.13754   0.27368  0.284165 -0.0187089  0.00313669  -0.0426987  230  ARG A NE  
1835  C  CZ  . ARG A 230 ? 0.142582  0.276037 0.278962 -0.0159106  -0.00538361 -0.045975   230  ARG A CZ  
1836  N  NH1 . ARG A 230 ? 0.140751  0.264847 0.264838 -0.0156523  -0.00473328 -0.0445043  230  ARG A NH1 
1837  N  NH2 . ARG A 230 ? 0.133374  0.273416 0.272673 -0.013501   -0.0145088  -0.0511059  230  ARG A NH2 
1838  N  N   . ARG A 231 ? 0.121808  0.286291 0.305641 -0.0203748  0.0250945   -0.0384496  231  ARG A N   
1839  C  CA  . ARG A 231 ? 0.129142  0.303908 0.337839 -0.0243603  0.0284595   -0.042916   231  ARG A CA  
1840  C  C   . ARG A 231 ? 0.131307  0.309204 0.343639 -0.0260437  0.0414326   -0.0387595  231  ARG A C   
1841  O  O   . ARG A 231 ? 0.131408  0.311834 0.358692 -0.0316085  0.0497705   -0.0386218  231  ARG A O   
1842  C  CB  . ARG A 231 ? 0.132883  0.317907 0.352663 -0.0208291  0.0179022   -0.0498167  231  ARG A CB  
1843  C  CG  . ARG A 231 ? 0.165629  0.363512 0.413322 -0.0239869  0.0206182   -0.0552523  231  ARG A CG  
1844  C  CD  . ARG A 231 ? 0.206807  0.404602 0.471346 -0.0310158  0.0227145   -0.0583029  231  ARG A CD  
1845  N  NE  . ARG A 231 ? 0.243816  0.439396 0.50748  -0.0302023  0.0099019   -0.0637065  231  ARG A NE  
1846  C  CZ  . ARG A 231 ? 0.292862  0.489664 0.572779 -0.0351104  0.00673291  -0.0693624  231  ARG A CZ  
1847  N  NH1 . ARG A 231 ? 0.282703  0.482911 0.582955 -0.0417478  0.0157984   -0.0699565  231  ARG A NH1 
1848  N  NH2 . ARG A 231 ? 0.286496  0.48091  0.561873 -0.0333306  -0.00556332 -0.0746001  231  ARG A NH2 
1849  N  N   . ALA A 232 ? 0.141325  0.319306 0.340097 -0.0211429  0.0432191   -0.0356762  232  ALA A N   
1850  C  CA  . ALA A 232 ? 0.135901  0.316284 0.333769 -0.0216409  0.0550859   -0.0320184  232  ALA A CA  
1851  C  C   . ALA A 232 ? 0.141207  0.311341 0.328998 -0.0256645  0.0644581   -0.0249965  232  ALA A C   
1852  O  O   . ALA A 232 ? 0.145973  0.318435 0.342728 -0.029895   0.0751582   -0.0229996  232  ALA A O   
1853  C  CB  . ALA A 232 ? 0.128191  0.308288 0.310569 -0.0152173  0.0531506   -0.0305969  232  ALA A CB  
1854  N  N   . LEU A 233 ? 0.131866  0.290462 0.302305 -0.0246233  0.0605751   -0.0211912  233  LEU A N   
1855  C  CA  . LEU A 233 ? 0.148915  0.297131 0.310312 -0.0279102  0.0686959   -0.014275   233  LEU A CA  
1856  C  C   . LEU A 233 ? 0.155267  0.302735 0.334581 -0.0348832  0.0726615   -0.0152176  233  LEU A C   
1857  O  O   . LEU A 233 ? 0.157936  0.300455 0.337412 -0.0389301  0.0830124   -0.00962781 233  LEU A O   
1858  C  CB  . LEU A 233 ? 0.139966  0.276874 0.281606 -0.0248519  0.0625767   -0.0110699  233  LEU A CB  
1859  C  CG  . LEU A 233 ? 0.145123  0.280979 0.268189 -0.018635   0.0601409   -0.00891123 233  LEU A CG  
1860  C  CD1 . LEU A 233 ? 0.141941  0.268515 0.249603 -0.0158098  0.0527222   -0.00730872 233  LEU A CD1 
1861  C  CD2 . LEU A 233 ? 0.161208  0.295163 0.274381 -0.0182643  0.0705525   -0.0030625  233  LEU A CD2 
1862  N  N   . HIS A 234 ? 0.156292  0.307933 0.350243 -0.0363069  0.0640647   -0.0222337  234  HIS A N   
1863  C  CA  . HIS A 234 ? 0.174468  0.32606  0.388161 -0.0431199  0.0665326   -0.0246619  234  HIS A CA  
1864  C  C   . HIS A 234 ? 0.181802  0.342804 0.414611 -0.0475466  0.0772364   -0.0248131  234  HIS A C   
1865  O  O   . HIS A 234 ? 0.174748  0.331968 0.416849 -0.053683   0.0861194   -0.0215965  234  HIS A O   
1866  C  CB  . HIS A 234 ? 0.17292   0.32783  0.396839 -0.04285    0.0537855   -0.0332162  234  HIS A CB  
1867  C  CG  . HIS A 234 ? 0.210031  0.365365 0.455394 -0.0495486  0.0543449   -0.0374097  234  HIS A CG  
1868  N  ND1 . HIS A 234 ? 0.213028  0.380954 0.484347 -0.0530056  0.0549745   -0.0435507  234  HIS A ND1 
1869  C  CD2 . HIS A 234 ? 0.217964  0.363289 0.464742 -0.0534698  0.0543834   -0.0369057  234  HIS A CD2 
1870  C  CE1 . HIS A 234 ? 0.235955  0.401486 0.523966 -0.0591867  0.0552516   -0.04671    234  HIS A CE1 
1871  N  NE2 . HIS A 234 ? 0.235083  0.386454 0.508166 -0.0595332  0.0549633   -0.0427025  234  HIS A NE2 
1872  N  N   . ARG A 235 ? 0.192963  0.366058 0.432162 -0.0443828  0.0766371   -0.0285533  235  ARG A N   
1873  C  CA  . ARG A 235 ? 0.22628   0.409949 0.48548  -0.048306   0.0870449   -0.0297428  235  ARG A CA  
1874  C  C   . ARG A 235 ? 0.225582  0.403083 0.472154 -0.050082   0.101719    -0.0206914  235  ARG A C   
1875  O  O   . ARG A 235 ? 0.236815  0.419412 0.498645 -0.0552809  0.112991    -0.0196831  235  ARG A O   
1876  C  CB  . ARG A 235 ? 0.257748  0.456205 0.528244 -0.0444969  0.0854622   -0.0355678  235  ARG A CB  
1877  C  CG  . ARG A 235 ? 0.34303   0.550224 0.625975 -0.041143   0.0711475   -0.0444697  235  ARG A CG  
1878  C  CD  . ARG A 235 ? 0.428867  0.648767 0.719417 -0.036095   0.0703226   -0.0487338  235  ARG A CD  
1879  N  NE  . ARG A 235 ? 0.619108  0.843463 0.911488 -0.0304855  0.0551075   -0.0548038  235  ARG A NE  
1880  C  CZ  . ARG A 235 ? 0.6862    0.915216 0.993433 -0.0309456  0.0434359   -0.0616024  235  ARG A CZ  
1881  N  NH1 . ARG A 235 ? 0.653618  0.885416 0.957664 -0.0248043  0.0303625   -0.0655115  235  ARG A NH1 
1882  N  NH2 . ARG A 235 ? 0.705514  0.935944 1.03039  -0.03743    0.0444      -0.0645269  235  ARG A NH2 
1883  N  N   . ARG A 236 ? 0.23594   0.402738 0.455065 -0.0458415  0.101681    -0.014164   236  ARG A N   
1884  C  CA  . ARG A 236 ? 0.258042  0.418176 0.461796 -0.0465795  0.114242    -0.00538282 236  ARG A CA  
1885  C  C   . ARG A 236 ? 0.268428  0.413735 0.463833 -0.0504861  0.117682    0.00199277  236  ARG A C   
1886  O  O   . ARG A 236 ? 0.272588  0.414031 0.467634 -0.0546434  0.129985    0.00846309  236  ARG A O   
1887  C  CB  . ARG A 236 ? 0.29369   0.45074  0.471875 -0.0393369  0.112522    -0.0023951  236  ARG A CB  
1888  C  CG  . ARG A 236 ? 0.376903  0.548055 0.567757 -0.0358572  0.107219    -0.0108003  236  ARG A CG  
1889  C  CD  . ARG A 236 ? 0.516782  0.694489 0.701766 -0.0326638  0.115441    -0.0104048  236  ARG A CD  
1890  N  NE  . ARG A 236 ? 0.562866  0.754946 0.76396  -0.0298724  0.113125    -0.0184201  236  ARG A NE  
1891  C  CZ  . ARG A 236 ? 0.608129  0.80696  0.819912 -0.0266068  0.101332    -0.0255094  236  ARG A CZ  
1892  N  NH1 . ARG A 236 ? 0.447197  0.641213 0.658747 -0.0264597  0.0895574   -0.0269844  236  ARG A NH1 
1893  N  NH2 . ARG A 236 ? 0.605021  0.815894 0.828913 -0.0235566  0.102034    -0.0313162  236  ARG A NH2 
1894  N  N   . TYR A 237 ? 0.241292  0.377988 0.429081 -0.0487842  0.107202    0.00128306  237  TYR A N   
1895  C  CA  . TYR A 237 ? 0.258072  0.379721 0.436074 -0.051144   0.109498    0.00823042  237  TYR A CA  
1896  C  C   . TYR A 237 ? 0.26744   0.387134 0.467141 -0.0579335  0.108926    0.00512923  237  TYR A C   
1897  O  O   . TYR A 237 ? 0.30936   0.417068 0.506026 -0.0613784  0.113895    0.0113652   237  TYR A O   
1898  C  CB  . TYR A 237 ? 0.237402  0.349794 0.393297 -0.0451335  0.100094    0.00991932  237  TYR A CB  
1899  C  CG  . TYR A 237 ? 0.253748  0.365372 0.387485 -0.0394006  0.102602    0.0146545   237  TYR A CG  
1900  C  CD1 . TYR A 237 ? 0.289169  0.392218 0.408451 -0.0398542  0.112144    0.0238565   237  TYR A CD1 
1901  C  CD2 . TYR A 237 ? 0.237776  0.357022 0.365565 -0.0337279  0.095687    0.00994967  237  TYR A CD2 
1902  C  CE1 . TYR A 237 ? 0.309399  0.411339 0.407644 -0.0344401  0.113646    0.0276025   237  TYR A CE1 
1903  C  CE2 . TYR A 237 ? 0.258373  0.376309 0.366595 -0.0286662  0.097579    0.0136381   237  TYR A CE2 
1904  C  CZ  . TYR A 237 ? 0.298307  0.408269 0.391994 -0.0289934  0.106508    0.0219663   237  TYR A CZ  
1905  O  OH  . TYR A 237 ? 0.320243  0.428765 0.393842 -0.0237134  0.107388    0.0249111   237  TYR A OH  
1906  N  N   . GLY A 238 ? 0.253519  0.384071 0.474449 -0.0595274  0.102171    -0.00445968 238  GLY A N   
1907  C  CA  . GLY A 238 ? 0.261529  0.39097  0.504632 -0.0661489  0.101166    -0.00854379 238  GLY A CA  
1908  C  C   . GLY A 238 ? 0.278343  0.399348 0.516211 -0.0644628  0.0892921   -0.0123003  238  GLY A C   
1909  O  O   . GLY A 238 ? 0.248823  0.362744 0.464911 -0.0588396  0.0838435   -0.00983666 238  GLY A O   
1910  N  N   . ASP A 239 ? 0.305936  0.427485 0.565103 -0.0698517  0.0861663   -0.0184059  239  ASP A N   
1911  C  CA  . ASP A 239 ? 0.34691   0.463301 0.606896 -0.0690853  0.0746178   -0.024884   239  ASP A CA  
1912  C  C   . ASP A 239 ? 0.364347  0.463355 0.608491 -0.0686695  0.0760121   -0.0184392  239  ASP A C   
1913  O  O   . ASP A 239 ? 0.375777  0.469031 0.610565 -0.065266   0.0667272   -0.0220839  239  ASP A O   
1914  C  CB  . ASP A 239 ? 0.430113  0.552956 0.71981  -0.0755193  0.0719024   -0.0337248  239  ASP A CB  
1915  C  CG  . ASP A 239 ? 0.593614  0.716672 0.884806 -0.0732199  0.0572885   -0.0437145  239  ASP A CG  
1916  O  OD1 . ASP A 239 ? 0.591222  0.722886 0.875486 -0.067508   0.0481543   -0.0485954  239  ASP A OD1 
1917  O  OD2 . ASP A 239 ? 0.6436    0.757439 0.941424 -0.0768241  0.0551852   -0.0463164  239  ASP A OD2 
1918  N  N   . ARG A 240 ? 0.337326  0.427662 0.577824 -0.0717911  0.0877088   -0.00867085 240  ARG A N   
1919  C  CA  . ARG A 240 ? 0.345823  0.419397 0.571527 -0.070688   0.0883758   -0.00224687 240  ARG A CA  
1920  C  C   . ARG A 240 ? 0.32755   0.397523 0.525706 -0.0623115  0.0833908   0.00116281  240  ARG A C   
1921  O  O   . ARG A 240 ? 0.319123  0.379338 0.507472 -0.0595193  0.077693    0.00095991  240  ARG A O   
1922  C  CB  . ARG A 240 ? 0.416743  0.482053 0.647536 -0.0766133  0.101945    0.00738073  240  ARG A CB  
1923  C  CG  . ARG A 240 ? 0.468227  0.515948 0.679838 -0.0746073  0.105464    0.0177056   240  ARG A CG  
1924  C  CD  . ARG A 240 ? 0.538906  0.577531 0.760528 -0.0819074  0.118119    0.026187    240  ARG A CD  
1925  N  NE  . ARG A 240 ? 0.631501  0.653364 0.832143 -0.0791049  0.121943    0.0377121   240  ARG A NE  
1926  C  CZ  . ARG A 240 ? 0.673189  0.680053 0.868317 -0.0775363  0.117273    0.0396073   240  ARG A CZ  
1927  N  NH1 . ARG A 240 ? 0.600684  0.605447 0.811362 -0.0796177  0.109531    0.0305148   240  ARG A NH1 
1928  N  NH2 . ARG A 240 ? 0.627393  0.621254 0.801411 -0.0736691  0.120464    0.0505732   240  ARG A NH2 
1929  N  N   . TYR A 241 ? 0.280285  0.358499 0.467111 -0.0581528  0.084996    0.00335839  241  TYR A N   
1930  C  CA  . TYR A 241 ? 0.278688  0.352653 0.440565 -0.0508645  0.0812648   0.00727263  241  TYR A CA  
1931  C  C   . TYR A 241 ? 0.233413  0.31678  0.390677 -0.0455985  0.0706919   -0.00026264 241  TYR A C   
1932  O  O   . TYR A 241 ? 0.210924  0.291034 0.349837 -0.039921   0.0665783   0.00177351  241  TYR A O   
1933  C  CB  . TYR A 241 ? 0.311088  0.385275 0.460607 -0.0495978  0.0909267   0.0159939   241  TYR A CB  
1934  C  CG  . TYR A 241 ? 0.339561  0.400765 0.485255 -0.0530345  0.1006      0.0258615   241  TYR A CG  
1935  C  CD1 . TYR A 241 ? 0.37497   0.421671 0.511152 -0.0515171  0.0976806   0.0298659   241  TYR A CD1 
1936  C  CD2 . TYR A 241 ? 0.371754  0.434786 0.524394 -0.0578958  0.112726    0.0311153   241  TYR A CD2 
1937  C  CE1 . TYR A 241 ? 0.423658  0.457175 0.556072 -0.0542752  0.105816    0.0394949   241  TYR A CE1 
1938  C  CE2 . TYR A 241 ? 0.423692  0.473671 0.571385 -0.0610007  0.121695    0.041107    241  TYR A CE2 
1939  C  CZ  . TYR A 241 ? 0.514983  0.549775 0.65247  -0.0591217  0.117894    0.0455376   241  TYR A CZ  
1940  O  OH  . TYR A 241 ? 0.61506   0.635916 0.747859 -0.0620311  0.126488    0.0560848   241  TYR A OH  
1941  N  N   . ILE A 242 ? 0.204613  0.300047 0.378325 -0.0473199  0.0669212   -0.00821779 242  ILE A N   
1942  C  CA  . ILE A 242 ? 0.192795  0.296805 0.363308 -0.0426081  0.0567182   -0.0150669  242  ILE A CA  
1943  C  C   . ILE A 242 ? 0.184139  0.291014 0.370526 -0.0452335  0.0487111   -0.0243082  242  ILE A C   
1944  O  O   . ILE A 242 ? 0.191261  0.302573 0.398718 -0.0508197  0.051307    -0.0277784  242  ILE A O   
1945  C  CB  . ILE A 242 ? 0.195175  0.312106 0.369848 -0.0409496  0.0584109   -0.0163438  242  ILE A CB  
1946  C  CG1 . ILE A 242 ? 0.194922  0.309652 0.35383  -0.0383025  0.0665321   -0.00815532 242  ILE A CG1 
1947  C  CG2 . ILE A 242 ? 0.176013  0.300096 0.347503 -0.0360412  0.047104    -0.0228836  242  ILE A CG2 
1948  C  CD1 . ILE A 242 ? 0.200212  0.310477 0.33675  -0.031695   0.0610199   -0.00584935 242  ILE A CD1 
1949  N  N   . ASN A 243 ? 0.179465  0.283972 0.355353 -0.0411338  0.0392132   -0.0283459  243  ASN A N   
1950  C  CA  . ASN A 243 ? 0.173427  0.280015 0.358274 -0.0418901  0.0296757   -0.0377249  243  ASN A CA  
1951  C  C   . ASN A 243 ? 0.158964  0.275932 0.339834 -0.0371728  0.0211398   -0.0424621  243  ASN A C   
1952  O  O   . ASN A 243 ? 0.14975   0.26504  0.312013 -0.0317177  0.017929    -0.0400713  243  ASN A O   
1953  C  CB  . ASN A 243 ? 0.191772  0.286313 0.365831 -0.0406805  0.0267656   -0.0379777  243  ASN A CB  
1954  C  CG  . ASN A 243 ? 0.197273  0.292501 0.377793 -0.041116   0.0171582   -0.0480787  243  ASN A CG  
1955  O  OD1 . ASN A 243 ? 0.193877  0.299065 0.383442 -0.0410591  0.0104758   -0.0550277  243  ASN A OD1 
1956  N  ND2 . ASN A 243 ? 0.207379  0.292018 0.381429 -0.0406502  0.0157313   -0.0491543  243  ASN A ND2 
1957  N  N   . LEU A 244 ? 0.152352  0.279962 0.351885 -0.0393745  0.0175485   -0.0489821  244  LEU A N   
1958  C  CA  . LEU A 244 ? 0.152711  0.290327 0.351227 -0.0350225  0.00922292  -0.0533095  244  LEU A CA  
1959  C  C   . LEU A 244 ? 0.159498  0.294061 0.344355 -0.0308408  -0.00167242 -0.0578691  244  LEU A C   
1960  O  O   . LEU A 244 ? 0.147918  0.288437 0.326876 -0.0263508  -0.00873274 -0.0597912  244  LEU A O   
1961  C  CB  . LEU A 244 ? 0.15764   0.30702  0.381846 -0.0385443  0.00719492  -0.059995   244  LEU A CB  
1962  C  CG  . LEU A 244 ? 0.162678  0.317705 0.400189 -0.0419151  0.0184888   -0.0557254  244  LEU A CG  
1963  C  CD1 . LEU A 244 ? 0.166959  0.334302 0.434119 -0.046246   0.0170917   -0.0631881  244  LEU A CD1 
1964  C  CD2 . LEU A 244 ? 0.152842  0.311343 0.376829 -0.0364289  0.0200576   -0.05107    244  LEU A CD2 
1965  N  N   . ARG A 245 ? 0.172632  0.297616 0.351645 -0.0319885  -0.00255681 -0.0591777  245  ARG A N   
1966  C  CA  . ARG A 245 ? 0.187227  0.309095 0.351265 -0.0278196  -0.0115703  -0.0633521  245  ARG A CA  
1967  C  C   . ARG A 245 ? 0.190254  0.301293 0.334671 -0.0252666  -0.00791354 -0.0578826  245  ARG A C   
1968  O  O   . ARG A 245 ? 0.18359   0.290996 0.315543 -0.0222556  -0.0136215  -0.0612158  245  ARG A O   
1969  C  CB  . ARG A 245 ? 0.218454  0.34076  0.393148 -0.0301854  -0.0194126  -0.0734472  245  ARG A CB  
1970  C  CG  . ARG A 245 ? 0.258662  0.393069 0.452085 -0.031554   -0.0255853  -0.0799489  245  ARG A CG  
1971  C  CD  . ARG A 245 ? 0.310915  0.447185 0.515504 -0.0335046  -0.034983   -0.09097    245  ARG A CD  
1972  N  NE  . ARG A 245 ? 0.422821  0.552218 0.640871 -0.0396178  -0.02944    -0.0926653  245  ARG A NE  
1973  C  CZ  . ARG A 245 ? 0.502128  0.631875 0.736236 -0.0434812  -0.0348742  -0.102214   245  ARG A CZ  
1974  N  NH1 . ARG A 245 ? 0.517545  0.656723 0.760815 -0.0425608  -0.0459808  -0.111421   245  ARG A NH1 
1975  N  NH2 . ARG A 245 ? 0.483481  0.603899 0.725292 -0.0482244  -0.0294882  -0.102595   245  ARG A NH2 
1976  N  N   . GLY A 246 ? 0.184801  0.291316 0.326091 -0.0260828  0.00141382  -0.0496335  246  GLY A N   
1977  C  CA  . GLY A 246 ? 0.166984  0.263368 0.292755 -0.0239198  0.00513325  -0.0443117  246  GLY A CA  
1978  C  C   . GLY A 246 ? 0.171878  0.26933  0.284424 -0.0201792  0.0089332   -0.0366241  246  GLY A C   
1979  O  O   . GLY A 246 ? 0.156651  0.262015 0.27197  -0.0193247  0.00895305  -0.0356577  246  GLY A O   
1980  N  N   . PRO A 247 ? 0.155551  0.245187 0.253757 -0.0174816  0.0115992   -0.0316402  247  PRO A N   
1981  C  CA  . PRO A 247 ? 0.157681  0.247698 0.243739 -0.0140135  0.0147265   -0.0249336  247  PRO A CA  
1982  C  C   . PRO A 247 ? 0.153394  0.243974 0.245059 -0.0163867  0.0226157   -0.0192955  247  PRO A C   
1983  O  O   . PRO A 247 ? 0.159465  0.246967 0.261861 -0.0207009  0.0270661   -0.0187547  247  PRO A O   
1984  C  CB  . PRO A 247 ? 0.155833  0.237075 0.228766 -0.0111842  0.0153714   -0.0220724  247  PRO A CB  
1985  C  CG  . PRO A 247 ? 0.166861  0.244417 0.244053 -0.0125202  0.0113104   -0.0287964  247  PRO A CG  
1986  C  CD  . PRO A 247 ? 0.16499   0.245032 0.259943 -0.0177041  0.0116425   -0.032817   247  PRO A CD  
1987  N  N   . ILE A 248 ? 0.143304  0.238069 0.228017 -0.0136533  0.024352    -0.0155163  248  ILE A N   
1988  C  CA  . ILE A 248 ? 0.13689   0.232491 0.22425  -0.0152761  0.0321923   -0.0103863  248  ILE A CA  
1989  C  C   . ILE A 248 ? 0.147977  0.233634 0.224086 -0.0142672  0.0368025   -0.00367589 248  ILE A C   
1990  O  O   . ILE A 248 ? 0.14197   0.224449 0.205644 -0.0102862  0.0336254   -0.00239503 248  ILE A O   
1991  C  CB  . ILE A 248 ? 0.131726  0.235216 0.215188 -0.0121203  0.0316788   -0.00984875 248  ILE A CB  
1992  C  CG1 . ILE A 248 ? 0.131216  0.244311 0.226729 -0.0125794  0.026166    -0.0164281  248  ILE A CG1 
1993  C  CG2 . ILE A 248 ? 0.143579  0.248011 0.228005 -0.0134357  0.0404167   -0.00500221 248  ILE A CG2 
1994  C  CD1 . ILE A 248 ? 0.134159  0.254362 0.226532 -0.00879843 0.0240468   -0.0166749  248  ILE A CD1 
1995  N  N   . PRO A 249 ? 0.153043  0.233889 0.232887 -0.0175193  0.0443387   0.00111124  249  PRO A N   
1996  C  CA  . PRO A 249 ? 0.172629  0.244088 0.239956 -0.0157026  0.0483468   0.00848832  249  PRO A CA  
1997  C  C   . PRO A 249 ? 0.177721  0.251776 0.230719 -0.0108133  0.047864    0.011522    249  PRO A C   
1998  O  O   . PRO A 249 ? 0.18481   0.266729 0.23905  -0.010406   0.0494181   0.0106696   249  PRO A O   
1999  C  CB  . PRO A 249 ? 0.183184  0.251131 0.257861 -0.0204472  0.0572038   0.0132224   249  PRO A CB  
2000  C  CG  . PRO A 249 ? 0.169449  0.242074 0.263344 -0.0254232  0.0561685   0.00682983  249  PRO A CG  
2001  C  CD  . PRO A 249 ? 0.153789  0.237713 0.250381 -0.023116   0.0492228   -0.0001814  249  PRO A CD  
2002  N  N   . ALA A 250 ? 0.168389  0.235766 0.208876 -0.00704986 0.0456911   0.0147151   250  ALA A N   
2003  C  CA  . ALA A 250 ? 0.17807   0.248748 0.207292 -0.0022998  0.0424546   0.0150904   250  ALA A CA  
2004  C  C   . ALA A 250 ? 0.195206  0.266163 0.21615  -0.00101809 0.0476341   0.020207    250  ALA A C   
2005  O  O   . ALA A 250 ? 0.199712  0.273777 0.212262 0.00269262  0.0451912   0.0200545   250  ALA A O   
2006  C  CB  . ALA A 250 ? 0.192904  0.25736  0.214112 0.00111889  0.0380472   0.0157789   250  ALA A CB  
2007  N  N   . HIS A 251 ? 0.185898  0.253691 0.209072 -0.00413527 0.0549113   0.0244697   251  HIS A N   
2008  C  CA  . HIS A 251 ? 0.209656  0.27709  0.222486 -0.00264129 0.0603074   0.0294712   251  HIS A CA  
2009  C  C   . HIS A 251 ? 0.213812  0.290382 0.234485 -0.00515803 0.0658728   0.0273203   251  HIS A C   
2010  O  O   . HIS A 251 ? 0.204629  0.281984 0.217366 -0.00423455 0.0714724   0.0306381   251  HIS A O   
2011  C  CB  . HIS A 251 ? 0.218785  0.275203 0.225828 -0.0038598  0.0654984   0.0370744   251  HIS A CB  
2012  C  CG  . HIS A 251 ? 0.247272  0.301924 0.268013 -0.00996724 0.0715716   0.0378735   251  HIS A CG  
2013  N  ND1 . HIS A 251 ? 0.242917  0.299884 0.279354 -0.0133487  0.0685648   0.0321161   251  HIS A ND1 
2014  C  CD2 . HIS A 251 ? 0.267418  0.317831 0.288715 -0.0134745  0.0805558   0.0437846   251  HIS A CD2 
2015  C  CE1 . HIS A 251 ? 0.258399  0.312425 0.305689 -0.0187214  0.0748285   0.0340657   251  HIS A CE1 
2016  N  NE2 . HIS A 251 ? 0.27548   0.325359 0.314219 -0.019144   0.0826786   0.0415256   251  HIS A NE2 
2017  N  N   . LEU A 252 ? 0.182599  0.266951 0.217913 -0.00742222 0.0634037   0.0210153   252  LEU A N   
2018  C  CA  . LEU A 252 ? 0.209584  0.302986 0.255362 -0.0098878  0.0687788   0.0186167   252  LEU A CA  
2019  C  C   . LEU A 252 ? 0.192365  0.295195 0.238634 -0.00639755 0.0643547   0.0133586   252  LEU A C   
2020  O  O   . LEU A 252 ? 0.213348  0.324772 0.270405 -0.0077992  0.0674802   0.0100765   252  LEU A O   
2021  C  CB  . LEU A 252 ? 0.195265  0.291353 0.260302 -0.0153493  0.0698204   0.0152131   252  LEU A CB  
2022  C  CG  . LEU A 252 ? 0.219043  0.305516 0.287171 -0.0195519  0.0742336   0.0197098   252  LEU A CG  
2023  C  CD1 . LEU A 252 ? 0.234017  0.324616 0.323929 -0.0251149  0.0740377   0.0144561   252  LEU A CD1 
2024  C  CD2 . LEU A 252 ? 0.245492  0.328267 0.305913 -0.0206703  0.084591    0.0271264   252  LEU A CD2 
2025  N  N   . LEU A 253 ? 0.18817   0.289478 0.223866 -0.00187961 0.0575228   0.0125994   253  LEU A N   
2026  C  CA  . LEU A 253 ? 0.173726  0.282731 0.211945 0.00098324  0.05252     0.00759068  253  LEU A CA  
2027  C  C   . LEU A 253 ? 0.179208  0.289507 0.206077 0.00494536  0.0540696   0.0085433   253  LEU A C   
2028  O  O   . LEU A 253 ? 0.192449  0.307664 0.220404 0.00776263  0.0495613   0.00471656  253  LEU A O   
2029  C  CB  . LEU A 253 ? 0.156044  0.264114 0.194875 0.00237389  0.0435737   0.00464857  253  LEU A CB  
2030  C  CG  . LEU A 253 ? 0.162319  0.270997 0.213783 -0.0014419  0.0418325   0.00184661  253  LEU A CG  
2031  C  CD1 . LEU A 253 ? 0.164782  0.268849 0.211876 -0.00030524 0.0350762   0.00073273  253  LEU A CD1 
2032  C  CD2 . LEU A 253 ? 0.136131  0.254778 0.201528 -0.00213561 0.039848    -0.00360107 253  LEU A CD2 
2033  N  N   . GLY A 254 ? 0.19222   0.297971 0.208391 0.00523085  0.0602421   0.0134014   254  GLY A N   
2034  C  CA  . GLY A 254 ? 0.214367  0.322485 0.220569 0.00877182  0.0624334   0.0131396   254  GLY A CA  
2035  C  C   . GLY A 254 ? 0.266027  0.368108 0.256364 0.0129948   0.0575514   0.0152952   254  GLY A C   
2036  O  O   . GLY A 254 ? 0.304083  0.407134 0.284468 0.0163423   0.0581928   0.0147167   254  GLY A O   
2037  N  N   . ASP A 255 ? 0.257999  0.354635 0.247256 0.0130587   0.052013    0.0167339   255  ASP A N   
2038  C  CA  . ASP A 255 ? 0.238657  0.331371 0.217216 0.016977    0.0460737   0.0174249   255  ASP A CA  
2039  C  C   . ASP A 255 ? 0.212367  0.296834 0.187629 0.0163377   0.0446582   0.0217285   255  ASP A C   
2040  O  O   . ASP A 255 ? 0.202544  0.285678 0.186799 0.0132211   0.0447783   0.0215603   255  ASP A O   
2041  C  CB  . ASP A 255 ? 0.284624  0.382087 0.269901 0.0181784   0.0394923   0.0123839   255  ASP A CB  
2042  C  CG  . ASP A 255 ? 0.301152  0.395972 0.279655 0.0214524   0.0331574   0.0121348   255  ASP A CG  
2043  O  OD1 . ASP A 255 ? 0.411782  0.508371 0.384725 0.0243968   0.0316629   0.0104347   255  ASP A OD1 
2044  O  OD2 . ASP A 255 ? 0.328524  0.419615 0.307874 0.0210312   0.0299722   0.0132955   255  ASP A OD2 
2045  N  N   . MET A 256 ? 0.201839  0.280932 0.165091 0.0196823   0.0422795   0.0247913   256  MET A N   
2046  C  CA  . MET A 256 ? 0.205182  0.276198 0.165912 0.0198273   0.0405632   0.0287817   256  MET A CA  
2047  C  C   . MET A 256 ? 0.192348  0.263851 0.162644 0.0188152   0.0357314   0.0255849   256  MET A C   
2048  O  O   . MET A 256 ? 0.199941  0.265849 0.173234 0.0174658   0.0358315   0.0274561   256  MET A O   
2049  C  CB  . MET A 256 ? 0.219331  0.286108 0.166907 0.0245264   0.0368768   0.0313696   256  MET A CB  
2050  C  CG  . MET A 256 ? 0.212247  0.269754 0.156302 0.0255868   0.0352797   0.0363405   256  MET A CG  
2051  S  SD  . MET A 256 ? 0.250077  0.299266 0.192956 0.0221929   0.0430044   0.0432576   256  MET A SD  
2052  C  CE  . MET A 256 ? 0.218624  0.265922 0.143066 0.0255395   0.0458927   0.0477776   256  MET A CE  
2053  N  N   . TRP A 257 ? 0.172074  0.249484 0.146227 0.0197907   0.0314234   0.0208871   257  TRP A N   
2054  C  CA  . TRP A 257 ? 0.171086  0.249124 0.151945 0.0191188   0.0273387   0.018039    257  TRP A CA  
2055  C  C   . TRP A 257 ? 0.171607  0.254524 0.162618 0.0160196   0.0276259   0.0143378   257  TRP A C   
2056  O  O   . TRP A 257 ? 0.155759  0.239517 0.150625 0.0157062   0.0240717   0.0117061   257  TRP A O   
2057  C  CB  . TRP A 257 ? 0.161821  0.241389 0.139685 0.022275    0.0220394   0.0162946   257  TRP A CB  
2058  C  CG  . TRP A 257 ? 0.184545  0.259573 0.153661 0.0254088   0.0210835   0.0195755   257  TRP A CG  
2059  C  CD1 . TRP A 257 ? 0.210418  0.279636 0.177987 0.0265758   0.0199021   0.0220557   257  TRP A CD1 
2060  C  CD2 . TRP A 257 ? 0.194815  0.270353 0.155251 0.0280568   0.0210746   0.0206506   257  TRP A CD2 
2061  N  NE1 . TRP A 257 ? 0.209258  0.275512 0.167951 0.0299569   0.0184738   0.0248968   257  TRP A NE1 
2062  C  CE2 . TRP A 257 ? 0.207253  0.277181 0.160648 0.0308882   0.0191001   0.0240352   257  TRP A CE2 
2063  C  CE3 . TRP A 257 ? 0.226966  0.307027 0.184793 0.0286639   0.0222647   0.0186635   257  TRP A CE3 
2064  C  CZ2 . TRP A 257 ? 0.229242  0.297915 0.171942 0.034209    0.0179456   0.0256519   257  TRP A CZ2 
2065  C  CZ3 . TRP A 257 ? 0.225246  0.304163 0.172525 0.0318129   0.0217606   0.019735    257  TRP A CZ3 
2066  C  CH2 . TRP A 257 ? 0.23922   0.312326 0.178291 0.0344408   0.0196856   0.0234521   257  TRP A CH2 
2067  N  N   . ALA A 258 ? 0.166375  0.252838 0.161374 0.0140715   0.0316687   0.0139535   258  ALA A N   
2068  C  CA  . ALA A 258 ? 0.176869  0.269328 0.182448 0.0117629   0.0311465   0.00995203  258  ALA A CA  
2069  C  C   . ALA A 258 ? 0.186188  0.282954 0.191923 0.0140466   0.0257124   0.00670661  258  ALA A C   
2070  O  O   . ALA A 258 ? 0.175406  0.275162 0.187656 0.0130229   0.022601    0.00367357  258  ALA A O   
2071  C  CB  . ALA A 258 ? 0.151136  0.241386 0.164556 0.00847959  0.0309226   0.00880754  258  ALA A CB  
2072  N  N   . GLN A 259 ? 0.173862  0.270674 0.172514 0.0171306   0.0243128   0.00731567  259  GLN A N   
2073  C  CA  . GLN A 259 ? 0.181536  0.280531 0.180591 0.0188953   0.019168    0.00504568  259  GLN A CA  
2074  C  C   . GLN A 259 ? 0.205706  0.310279 0.20921  0.0197509   0.0186235   0.00231196  259  GLN A C   
2075  O  O   . GLN A 259 ? 0.212286  0.318788 0.218594 0.0206082   0.0145589   0.00048139  259  GLN A O   
2076  C  CB  . GLN A 259 ? 0.197214  0.293623 0.189131 0.0216315   0.0165575   0.00614763  259  GLN A CB  
2077  C  CG  . GLN A 259 ? 0.25372   0.350736 0.240148 0.0238894   0.0177971   0.00641461  259  GLN A CG  
2078  C  CD  . GLN A 259 ? 0.313691  0.408051 0.294065 0.026454    0.0146457   0.0072081   259  GLN A CD  
2079  O  OE1 . GLN A 259 ? 0.299999  0.390333 0.277049 0.0267688   0.0145011   0.00961475  259  GLN A OE1 
2080  N  NE2 . GLN A 259 ? 0.310735  0.407308 0.290767 0.0283983   0.0119065   0.00488738  259  GLN A NE2 
2081  N  N   . SER A 260 ? 0.216559  0.323323 0.220244 0.0198079   0.0229097   0.0022039   260  SER A N   
2082  C  CA  . SER A 260 ? 0.247607  0.360391 0.25916  0.0201914   0.0225776   -0.00121758 260  SER A CA  
2083  C  C   . SER A 260 ? 0.214917  0.330919 0.230887 0.0183973   0.0290139   -0.00140611 260  SER A C   
2084  O  O   . SER A 260 ? 0.206176  0.319025 0.216041 0.0175604   0.0339295   0.00164413  260  SER A O   
2085  C  CB  . SER A 260 ? 0.376292  0.490257 0.385101 0.0234332   0.0201025   -0.00308714 260  SER A CB  
2086  O  OG  . SER A 260 ? 0.385875  0.49909  0.387382 0.0246971   0.0242209   -0.00240216 260  SER A OG  
2087  N  N   . TRP A 261 ? 0.165727  0.287762 0.193241 0.0175256   0.0287723   -0.00466805 261  TRP A N   
2088  C  CA  . TRP A 261 ? 0.17373   0.299444 0.209059 0.0146905   0.0350219   -0.00499664 261  TRP A CA  
2089  C  C   . TRP A 261 ? 0.169657  0.301786 0.209425 0.016226    0.0391219   -0.007907   261  TRP A C   
2090  O  O   . TRP A 261 ? 0.17672   0.313942 0.226403 0.013894    0.0442997   -0.00917779 261  TRP A O   
2091  C  CB  . TRP A 261 ? 0.150081  0.278795 0.197932 0.0120179   0.0319632   -0.00722876 261  TRP A CB  
2092  C  CG  . TRP A 261 ? 0.141365  0.264314 0.185547 0.0105915   0.0281326   -0.00555897 261  TRP A CG  
2093  C  CD1 . TRP A 261 ? 0.157821  0.273431 0.190465 0.0112354   0.0275197   -0.00210387 261  TRP A CD1 
2094  C  CD2 . TRP A 261 ? 0.132622  0.257208 0.185506 0.00860661  0.0238846   -0.00815267 261  TRP A CD2 
2095  N  NE1 . TRP A 261 ? 0.135687  0.248322 0.169693 0.00963976  0.0241781   -0.00246256 261  TRP A NE1 
2096  C  CE2 . TRP A 261 ? 0.130808  0.248689 0.17636  0.00799804  0.0217701   -0.00626342 261  TRP A CE2 
2097  C  CE3 . TRP A 261 ? 0.119983  0.251436 0.186566 0.00754963  0.0213995   -0.0123704  261  TRP A CE3 
2098  C  CZ2 . TRP A 261 ? 0.133276  0.250688 0.183265 0.00635836  0.0174574   -0.00871868 261  TRP A CZ2 
2099  C  CZ3 . TRP A 261 ? 0.120948  0.251947 0.19172  0.00603188  0.0162233   -0.014599   261  TRP A CZ3 
2100  C  CH2 . TRP A 261 ? 0.131521  0.25537  0.193235 0.00547238  0.01434     -0.0129069  261  TRP A CH2 
2101  N  N   . GLU A 262 ? 0.20849   0.340576 0.241983 0.0200043   0.0371753   -0.00939219 262  GLU A N   
2102  C  CA  . GLU A 262 ? 0.267461  0.405605 0.305065 0.0220135   0.0410813   -0.0131389  262  GLU A CA  
2103  C  C   . GLU A 262 ? 0.255849  0.396375 0.292667 0.019998    0.0511457   -0.0119522  262  GLU A C   
2104  O  O   . GLU A 262 ? 0.209284  0.357159 0.255949 0.0199993   0.0558564   -0.0154782  262  GLU A O   
2105  C  CB  . GLU A 262 ? 0.354967  0.491486 0.384715 0.0263332   0.0378034   -0.0152256  262  GLU A CB  
2106  C  CG  . GLU A 262 ? 0.457956  0.58731  0.471532 0.0274225   0.0370773   -0.0118604  262  GLU A CG  
2107  C  CD  . GLU A 262 ? 0.612491  0.736343 0.622723 0.0275203   0.029675    -0.00967731 262  GLU A CD  
2108  O  OE1 . GLU A 262 ? 0.433877  0.556233 0.44785  0.0248592   0.0281821   -0.00737641 262  GLU A OE1 
2109  O  OE2 . GLU A 262 ? 0.636702  0.757733 0.64084  0.0301297   0.025512    -0.0105165  262  GLU A OE2 
2110  N  N   . ASN A 263 ? 0.241207  0.375526 0.266783 0.0182496   0.0550395   -0.00673325 263  ASN A N   
2111  C  CA  . ASN A 263 ? 0.271734  0.406725 0.293885 0.0163653   0.0650769   -0.00430257 263  ASN A CA  
2112  C  C   . ASN A 263 ? 0.254472  0.394223 0.291906 0.0116416   0.0708451   -0.00429016 263  ASN A C   
2113  O  O   . ASN A 263 ? 0.275664  0.417369 0.312842 0.00971007  0.0805137   -0.00264637 263  ASN A O   
2114  C  CB  . ASN A 263 ? 0.330428  0.456174 0.336055 0.0160105   0.0669877   0.00217886  263  ASN A CB  
2115  C  CG  . ASN A 263 ? 0.32306   0.445586 0.313447 0.0207376   0.0633541   0.00163812  263  ASN A CG  
2116  O  OD1 . ASN A 263 ? 0.451998  0.568759 0.435178 0.0222143   0.0567621   0.0034446   263  ASN A OD1 
2117  N  ND2 . ASN A 263 ? 0.315279  0.441828 0.301281 0.0231522   0.0677511   -0.00135049 263  ASN A ND2 
2118  N  N   . ILE A 264 ? 0.201457  0.343086 0.252193 0.00952535  0.0654273   -0.00607335 264  ILE A N   
2119  C  CA  . ILE A 264 ? 0.191648  0.338846 0.25879  0.00503676  0.0707247   -0.00712019 264  ILE A CA  
2120  C  C   . ILE A 264 ? 0.179     0.33686  0.26336  0.00640398  0.0681007   -0.0139784  264  ILE A C   
2121  O  O   . ILE A 264 ? 0.175784  0.339818 0.277772 0.00317275  0.0690961   -0.0165431  264  ILE A O   
2122  C  CB  . ILE A 264 ? 0.20652   0.348652 0.278018 0.00118545  0.0674151   -0.00479747 264  ILE A CB  
2123  C  CG1 . ILE A 264 ? 0.210755  0.351709 0.282812 0.00338084  0.0561629   -0.00737177 264  ILE A CG1 
2124  C  CG2 . ILE A 264 ? 0.22538   0.357098 0.28244  -0.00024131 0.0711356   0.00209541  264  ILE A CG2 
2125  C  CD1 . ILE A 264 ? 0.26915   0.411097 0.354109 -0.00013194 0.0522824   -0.00929539 264  ILE A CD1 
2126  N  N   . TYR A 265 ? 0.167053  0.326891 0.247203 0.0112571   0.0644882   -0.0171113  265  TYR A N   
2127  C  CA  . TYR A 265 ? 0.173946  0.343327 0.26983  0.0135192   0.0621941   -0.0235248  265  TYR A CA  
2128  C  C   . TYR A 265 ? 0.190863  0.369545 0.302386 0.0106671   0.0716187   -0.0260167  265  TYR A C   
2129  O  O   . TYR A 265 ? 0.169689  0.356151 0.300766 0.00950777  0.069065    -0.0301614  265  TYR A O   
2130  C  CB  . TYR A 265 ? 0.160043  0.328832 0.248007 0.0190908   0.0586465   -0.0261942  265  TYR A CB  
2131  C  CG  . TYR A 265 ? 0.161963  0.340209 0.266994 0.0219656   0.0566846   -0.0329046  265  TYR A CG  
2132  C  CD1 . TYR A 265 ? 0.143838  0.324499 0.261284 0.0227429   0.0474686   -0.0352006  265  TYR A CD1 
2133  C  CD2 . TYR A 265 ? 0.168384  0.352987 0.276742 0.0241249   0.0641003   -0.0369446  265  TYR A CD2 
2134  C  CE1 . TYR A 265 ? 0.149487  0.337703 0.281846 0.0261639   0.044435    -0.0409174  265  TYR A CE1 
2135  C  CE2 . TYR A 265 ? 0.171569  0.364533 0.296347 0.0273868   0.0618237   -0.0434464  265  TYR A CE2 
2136  C  CZ  . TYR A 265 ? 0.157151  0.351861 0.294661 0.0283765   0.0517035   -0.0452099  265  TYR A CZ  
2137  O  OH  . TYR A 265 ? 0.160331  0.362735 0.314917 0.0319411   0.0481649   -0.0511724  265  TYR A OH  
2138  N  N   . ASP A 266 ? 0.217895  0.396037 0.32123  0.00938112  0.082766    -0.0234025  266  ASP A N   
2139  C  CA  . ASP A 266 ? 0.280418  0.467984 0.398552 0.00663411  0.0933622   -0.0257439  266  ASP A CA  
2140  C  C   . ASP A 266 ? 0.261025  0.451485 0.396773 0.0008079   0.0941561   -0.0251961  266  ASP A C   
2141  O  O   . ASP A 266 ? 0.236772  0.437485 0.392361 -0.00117124 0.0989681   -0.0293019  266  ASP A O   
2142  C  CB  . ASP A 266 ? 0.34552   0.531774 0.450201 0.00633867  0.105833    -0.0226922  266  ASP A CB  
2143  C  CG  . ASP A 266 ? 0.447843  0.621444 0.528052 0.0059652   0.106755    -0.014938   266  ASP A CG  
2144  O  OD1 . ASP A 266 ? 0.366583  0.533459 0.446002 0.00249434  0.103762    -0.0102441  266  ASP A OD1 
2145  O  OD2 . ASP A 266 ? 0.529145  0.699603 0.591032 0.00943853  0.110302    -0.0139429  266  ASP A OD2 
2146  N  N   . MET A 267 ? 0.248822  0.430754 0.379029 -0.00181338 0.0888766   -0.0209672  267  MET A N   
2147  C  CA  . MET A 267 ? 0.250176  0.434537 0.397668 -0.00743144 0.0893421   -0.0213225  267  MET A CA  
2148  C  C   . MET A 267 ? 0.208686  0.398109 0.371081 -0.0062198  0.077467    -0.0270478  267  MET A C   
2149  O  O   . MET A 267 ? 0.257987  0.451733 0.437955 -0.0103612  0.0767191   -0.0293596  267  MET A O   
2150  C  CB  . MET A 267 ? 0.289293  0.461644 0.42499  -0.0105932  0.0881423   -0.0149982  267  MET A CB  
2151  C  CG  . MET A 267 ? 0.375741  0.541954 0.500068 -0.013457   0.0999728   -0.00812943 267  MET A CG  
2152  S  SD  . MET A 267 ? 0.409058  0.563549 0.531006 -0.0187228  0.0992929   -0.00218522 267  MET A SD  
2153  C  CE  . MET A 267 ? 0.272079  0.416959 0.366379 -0.012201   0.0922308   0.00116149  267  MET A CE  
2154  N  N   . VAL A 268 ? 0.172829  0.361233 0.328248 -0.0007325  0.0679659   -0.0291871  268  VAL A N   
2155  C  CA  . VAL A 268 ? 0.176545  0.367968 0.342944 0.00052821  0.0561689   -0.0334092  268  VAL A CA  
2156  C  C   . VAL A 268 ? 0.185528  0.386556 0.364732 0.00518959  0.0518281   -0.039524   268  VAL A C   
2157  O  O   . VAL A 268 ? 0.179801  0.383972 0.368774 0.0068014   0.0417413   -0.0430524  268  VAL A O   
2158  C  CB  . VAL A 268 ? 0.184733  0.36598  0.334473 0.00249381  0.0466914   -0.0304395  268  VAL A CB  
2159  C  CG1 . VAL A 268 ? 0.212301  0.384254 0.352144 -0.00165211 0.0492204   -0.0253571  268  VAL A CG1 
2160  C  CG2 . VAL A 268 ? 0.175505  0.352    0.308274 0.00754266  0.0452047   -0.028608   268  VAL A CG2 
2161  N  N   . VAL A 269 ? 0.187843  0.392385 0.364973 0.00804384  0.0584035   -0.0407096  269  VAL A N   
2162  C  CA  . VAL A 269 ? 0.179424  0.390846 0.365653 0.0134959   0.0540276   -0.0461949  269  VAL A CA  
2163  C  C   . VAL A 269 ? 0.18128   0.404105 0.393946 0.012643    0.0504891   -0.0520368  269  VAL A C   
2164  O  O   . VAL A 269 ? 0.178875  0.409636 0.406947 0.00869504  0.0587969   -0.0539823  269  VAL A O   
2165  C  CB  . VAL A 269 ? 0.188837  0.403141 0.370441 0.0159876   0.0637351   -0.0475372  269  VAL A CB  
2166  C  CG1 . VAL A 269 ? 0.180392  0.399345 0.366843 0.0112095   0.0778162   -0.0464775  269  VAL A CG1 
2167  C  CG2 . VAL A 269 ? 0.197437  0.420056 0.392506 0.0215797   0.0605084   -0.0543827  269  VAL A CG2 
2168  N  N   . PRO A 270 ? 0.194412  0.418435 0.413635 0.0162115   0.0378457   -0.0548881  270  PRO A N   
2169  C  CA  . PRO A 270 ? 0.205893  0.441079 0.450638 0.0156875   0.0333846   -0.0607389  270  PRO A CA  
2170  C  C   . PRO A 270 ? 0.178702  0.426617 0.443866 0.0177883   0.039297    -0.0667938  270  PRO A C   
2171  O  O   . PRO A 270 ? 0.225599  0.483856 0.513047 0.0146842   0.0417645   -0.0708961  270  PRO A O   
2172  C  CB  . PRO A 270 ? 0.224222  0.45533  0.465312 0.0198702   0.0182664   -0.0610635  270  PRO A CB  
2173  C  CG  . PRO A 270 ? 0.228677  0.450751 0.44948  0.0240661   0.0175142   -0.0574952  270  PRO A CG  
2174  C  CD  . PRO A 270 ? 0.216688  0.431017 0.419162 0.0202077   0.0273102   -0.0520758  270  PRO A CD  
2175  N  N   . PHE A 271 ? 0.154026  0.401655 0.412832 0.0227425   0.0423763   -0.0678747  271  PHE A N   
2176  C  CA  . PHE A 271 ? 0.157716  0.418106 0.437322 0.0253964   0.0478114   -0.0746785  271  PHE A CA  
2177  C  C   . PHE A 271 ? 0.169605  0.430217 0.439588 0.0250145   0.0623596   -0.0740797  271  PHE A C   
2178  O  O   . PHE A 271 ? 0.149107  0.408006 0.41145  0.0302078   0.0630025   -0.0759446  271  PHE A O   
2179  C  CB  . PHE A 271 ? 0.146521  0.410062 0.436446 0.0327826   0.0362785   -0.0794811  271  PHE A CB  
2180  C  CG  . PHE A 271 ? 0.142897  0.405779 0.439906 0.0331523   0.0218153   -0.0795058  271  PHE A CG  
2181  C  CD1 . PHE A 271 ? 0.149397  0.424062 0.472067 0.0311936   0.0192966   -0.0845623  271  PHE A CD1 
2182  C  CD2 . PHE A 271 ? 0.139176  0.3897   0.416531 0.0352505   0.0112193   -0.074541   271  PHE A CD2 
2183  C  CE1 . PHE A 271 ? 0.163132  0.436776 0.490057 0.0318085   0.00541949  -0.0848987  271  PHE A CE1 
2184  C  CE2 . PHE A 271 ? 0.158189  0.407635 0.439185 0.0358356   -0.00161088 -0.0744392  271  PHE A CE2 
2185  C  CZ  . PHE A 271 ? 0.139241  0.399863 0.443842 0.0342061   -0.00487453 -0.0796208  271  PHE A CZ  
2186  N  N   . PRO A 272 ? 0.241427  0.503847 0.511189 0.0187759   0.0747666   -0.0714827  272  PRO A N   
2187  C  CA  . PRO A 272 ? 0.300617  0.564237 0.561458 0.0183117   0.0895348   -0.0709376  272  PRO A CA  
2188  C  C   . PRO A 272 ? 0.338143  0.612928 0.612198 0.0227034   0.0964871   -0.0783501  272  PRO A C   
2189  O  O   . PRO A 272 ? 0.403719  0.676804 0.663714 0.0237101   0.106702    -0.0777914  272  PRO A O   
2190  C  CB  . PRO A 272 ? 0.31429   0.578922 0.578272 0.0102336   0.100374    -0.0667402  272  PRO A CB  
2191  C  CG  . PRO A 272 ? 0.283893  0.554978 0.571876 0.00726115  0.0922183   -0.0696085  272  PRO A CG  
2192  C  CD  . PRO A 272 ? 0.246191  0.509747 0.5254   0.0119309   0.0752639   -0.0692924  272  PRO A CD  
2193  N  N   . ASP A 273 ? 0.29466   0.580466 0.594357 0.0260222   0.0906846   -0.0856253  273  ASP A N   
2194  C  CA  . ASP A 273 ? 0.308867  0.6053   0.621778 0.030677    0.0975711   -0.0932597  273  ASP A CA  
2195  C  C   . ASP A 273 ? 0.262288  0.5523   0.562574 0.0386263   0.090493    -0.0956994  273  ASP A C   
2196  O  O   . ASP A 273 ? 0.253702  0.550209 0.560651 0.0433606   0.0959616   -0.102272   273  ASP A O   
2197  C  CB  . ASP A 273 ? 0.389885  0.702474 0.73834  0.0303407   0.0970299   -0.10041    273  ASP A CB  
2198  C  CG  . ASP A 273 ? 0.544089  0.87019  0.908991 0.0272627   0.114605    -0.104562   273  ASP A CG  
2199  O  OD1 . ASP A 273 ? 0.587738  0.910299 0.938872 0.0214635   0.12756     -0.0990796  273  ASP A OD1 
2200  O  OD2 . ASP A 273 ? 0.582155  0.922489 0.974579 0.0305534   0.115457    -0.113072   273  ASP A OD2 
2201  N  N   . LYS A 274 ? 0.23459   0.511521 0.516764 0.0400021   0.0786549   -0.0905916  274  LYS A N   
2202  C  CA  . LYS A 274 ? 0.250396  0.519778 0.521787 0.0467579   0.0703469   -0.0920615  274  LYS A CA  
2203  C  C   . LYS A 274 ? 0.29051   0.550832 0.534713 0.0467215   0.0778353   -0.0889966  274  LYS A C   
2204  O  O   . LYS A 274 ? 0.308768  0.567397 0.54109  0.041615    0.0876244   -0.0845345  274  LYS A O   
2205  C  CB  . LYS A 274 ? 0.203284  0.464665 0.47243  0.0480086   0.0540395   -0.0883752  274  LYS A CB  
2206  C  CG  . LYS A 274 ? 0.239658  0.510176 0.535144 0.0494823   0.0451092   -0.092357   274  LYS A CG  
2207  C  CD  . LYS A 274 ? 0.234789  0.516267 0.552742 0.0556246   0.0459038   -0.101276   274  LYS A CD  
2208  C  CE  . LYS A 274 ? 0.273746  0.56148  0.614666 0.0594406   0.033387    -0.105008   274  LYS A CE  
2209  N  NZ  . LYS A 274 ? 0.283488  0.583306 0.648145 0.0648856   0.0365025   -0.114082   274  LYS A NZ  
2210  N  N   . PRO A 275 ? 0.313908  0.567566 0.547339 0.0524549   0.0729263   -0.0911963  275  PRO A N   
2211  C  CA  . PRO A 275 ? 0.296072  0.542222 0.504894 0.0530313   0.079445    -0.0897758  275  PRO A CA  
2212  C  C   . PRO A 275 ? 0.252262  0.488382 0.440196 0.0476042   0.0790927   -0.080443   275  PRO A C   
2213  O  O   . PRO A 275 ? 0.196223  0.42704  0.384097 0.0459365   0.0694511   -0.0759394  275  PRO A O   
2214  C  CB  . PRO A 275 ? 0.29579   0.534504 0.50061  0.0595436   0.0685152   -0.0927762  275  PRO A CB  
2215  C  CG  . PRO A 275 ? 0.347039  0.594565 0.579397 0.0635311   0.0625667   -0.0988638  275  PRO A CG  
2216  C  CD  . PRO A 275 ? 0.303509  0.555044 0.546692 0.0584596   0.059821    -0.0944652  275  PRO A CD  
2217  N  N   . ASN A 276 ? 0.284529  0.517952 0.454434 0.0453977   0.0894698   -0.0778393  276  ASN A N   
2218  C  CA  . ASN A 276 ? 0.271571  0.495113 0.421002 0.0410082   0.0896697   -0.0692411  276  ASN A CA  
2219  C  C   . ASN A 276 ? 0.257504  0.469274 0.38849  0.0442303   0.0800623   -0.0673268  276  ASN A C   
2220  O  O   . ASN A 276 ? 0.271812  0.480967 0.390741 0.0479181   0.082061    -0.0705293  276  ASN A O   
2221  C  CB  . ASN A 276 ? 0.328089  0.553584 0.46662  0.0379167   0.104382    -0.0671088  276  ASN A CB  
2222  C  CG  . ASN A 276 ? 0.322857  0.537268 0.439532 0.0341127   0.104306    -0.0580752  276  ASN A CG  
2223  O  OD1 . ASN A 276 ? 0.369321  0.576333 0.482422 0.0329461   0.0942957   -0.0537284  276  ASN A OD1 
2224  N  ND2 . ASN A 276 ? 0.368547  0.581504 0.470075 0.0323621   0.115526    -0.055031   276  ASN A ND2 
2225  N  N   . LEU A 277 ? 0.227148  0.431868 0.355819 0.0427084   0.0698388   -0.0623593  277  LEU A N   
2226  C  CA  . LEU A 277 ? 0.25141   0.445903 0.367017 0.0453984   0.060124    -0.0606392  277  LEU A CA  
2227  C  C   . LEU A 277 ? 0.280468  0.465961 0.372716 0.043412    0.0620164   -0.0549186  277  LEU A C   
2228  O  O   . LEU A 277 ? 0.273692  0.450941 0.354999 0.0451677   0.0546192   -0.0533883  277  LEU A O   
2229  C  CB  . LEU A 277 ? 0.219336  0.410853 0.343022 0.0446121   0.049085    -0.0577305  277  LEU A CB  
2230  C  CG  . LEU A 277 ? 0.235572  0.434072 0.380932 0.0478629   0.0438659   -0.0630621  277  LEU A CG  
2231  C  CD1 . LEU A 277 ? 0.218681  0.412346 0.366429 0.04703     0.0327823   -0.0589339  277  LEU A CD1 
2232  C  CD2 . LEU A 277 ? 0.252586  0.449787 0.398211 0.0538568   0.0416945   -0.0688799  277  LEU A CD2 
2233  N  N   . ASP A 278 ? 0.273358  0.460084 0.359237 0.0395379   0.0712777   -0.0512381  278  ASP A N   
2234  C  CA  . ASP A 278 ? 0.381939  0.560088 0.445123 0.0387853   0.072836    -0.0462811  278  ASP A CA  
2235  C  C   . ASP A 278 ? 0.300255  0.480766 0.353295 0.0418548   0.0809349   -0.050536   278  ASP A C   
2236  O  O   . ASP A 278 ? 0.3171    0.50407  0.373313 0.0405068   0.0915446   -0.0516003  278  ASP A O   
2237  C  CB  . ASP A 278 ? 0.412688  0.586039 0.470025 0.0335635   0.0741102   -0.0382685  278  ASP A CB  
2238  C  CG  . ASP A 278 ? 0.624007  0.79053  0.659188 0.0329528   0.0792014   -0.0333412  278  ASP A CG  
2239  O  OD1 . ASP A 278 ? 0.530199  0.691445 0.551399 0.036499    0.074861    -0.0343778  278  ASP A OD1 
2240  O  OD2 . ASP A 278 ? 0.707249  0.873894 0.739535 0.0291419   0.0877451   -0.0287582  278  ASP A OD2 
2241  N  N   . VAL A 279 ? 0.296079  0.471899 0.338566 0.0461761   0.075675    -0.0538513  279  VAL A N   
2242  C  CA  . VAL A 279 ? 0.27457   0.453334 0.309396 0.050038    0.081853    -0.0600558  279  VAL A CA  
2243  C  C   . VAL A 279 ? 0.292948  0.465802 0.302957 0.0496767   0.0864591   -0.0559016  279  VAL A C   
2244  O  O   . VAL A 279 ? 0.275042  0.448462 0.273336 0.0534279   0.0901391   -0.06097    279  VAL A O   
2245  C  CB  . VAL A 279 ? 0.286867  0.463239 0.325221 0.0550583   0.0725112   -0.0666964  279  VAL A CB  
2246  C  CG1 . VAL A 279 ? 0.298449  0.480206 0.360803 0.0561842   0.0679341   -0.0705634  279  VAL A CG1 
2247  C  CG2 . VAL A 279 ? 0.253831  0.419858 0.27877  0.0554947   0.0627968   -0.0633347  279  VAL A CG2 
2248  N  N   . THR A 280 ? 0.282602  0.449313 0.284087 0.0457486   0.0853982   -0.0471594  280  THR A N   
2249  C  CA  . THR A 280 ? 0.32648   0.487228 0.304524 0.0456928   0.0895971   -0.0424326  280  THR A CA  
2250  C  C   . THR A 280 ? 0.346138  0.512182 0.316666 0.0466303   0.102392    -0.0448696  280  THR A C   
2251  O  O   . THR A 280 ? 0.359091  0.522647 0.310935 0.050193    0.104179    -0.0471848  280  THR A O   
2252  C  CB  . THR A 280 ? 0.315697  0.470214 0.2882   0.0411011   0.0894749   -0.03258    280  THR A CB  
2253  O  OG1 . THR A 280 ? 0.288022  0.437979 0.265939 0.0408465   0.0780625   -0.0312713  280  THR A OG1 
2254  C  CG2 . THR A 280 ? 0.326371  0.4743   0.274324 0.0418061   0.0935092   -0.0274971  280  THR A CG2 
2255  N  N   . SER A 281 ? 0.390549  0.56444  0.375827 0.0434629   0.111716    -0.0447678  281  SER A N   
2256  C  CA  . SER A 281 ? 0.427189  0.605745 0.403714 0.0438063   0.125427    -0.0459757  281  SER A CA  
2257  C  C   . SER A 281 ? 0.386881  0.569626 0.35941  0.049887    0.126108    -0.0562337  281  SER A C   
2258  O  O   . SER A 281 ? 0.41521   0.597215 0.36849  0.0521678   0.133382    -0.0572998  281  SER A O   
2259  C  CB  . SER A 281 ? 0.489714  0.676533 0.483801 0.0389153   0.136476    -0.0441631  281  SER A CB  
2260  O  OG  . SER A 281 ? 0.573591  0.770103 0.593011 0.0401437   0.134419    -0.0520929  281  SER A OG  
2261  N  N   . THR A 282 ? 0.359514  0.545346 0.348314 0.0529021   0.117613    -0.063702   282  THR A N   
2262  C  CA  . THR A 282 ? 0.338074  0.527158 0.325653 0.0588972   0.11706     -0.0743056  282  THR A CA  
2263  C  C   . THR A 282 ? 0.32389   0.503971 0.287597 0.062629    0.110173    -0.0753399  282  THR A C   
2264  O  O   . THR A 282 ? 0.34153   0.522853 0.291912 0.0668502   0.114501    -0.0818381  282  THR A O   
2265  C  CB  . THR A 282 ? 0.341147  0.534849 0.354305 0.0608866   0.109361    -0.0809605  282  THR A CB  
2266  O  OG1 . THR A 282 ? 0.33553   0.538302 0.36991  0.0575528   0.115934    -0.0801259  282  THR A OG1 
2267  C  CG2 . THR A 282 ? 0.321781  0.519335 0.338253 0.067109    0.10926     -0.0926787  282  THR A CG2 
2268  N  N   . MET A 283 ? 0.305975  0.477485 0.265083 0.0612675   0.0992185   -0.0696813  283  MET A N   
2269  C  CA  . MET A 283 ? 0.315252  0.478795 0.253495 0.0644903   0.092142    -0.0705271  283  MET A CA  
2270  C  C   . MET A 283 ? 0.330105  0.491684 0.242883 0.065023    0.101042    -0.0671692  283  MET A C   
2271  O  O   . MET A 283 ? 0.331982  0.491909 0.228139 0.0695203   0.100379    -0.0727825  283  MET A O   
2272  C  CB  . MET A 283 ? 0.281609  0.437139 0.219464 0.062123    0.0810527   -0.0635846  283  MET A CB  
2273  C  CG  . MET A 283 ? 0.272525  0.428526 0.232133 0.0618251   0.0717734   -0.0661382  283  MET A CG  
2274  S  SD  . MET A 283 ? 0.284085  0.431879 0.244575 0.0586034   0.0607243   -0.0579327  283  MET A SD  
2275  C  CE  . MET A 283 ? 0.293278  0.433613 0.234121 0.0622298   0.0527452   -0.0601995  283  MET A CE  
2276  N  N   . LEU A 284 ? 0.362286  0.523619 0.272023 0.0604388   0.109204    -0.0579705  284  LEU A N   
2277  C  CA  . LEU A 284 ? 0.429396  0.588275 0.31519  0.0604376   0.119069    -0.0530729  284  LEU A CA  
2278  C  C   . LEU A 284 ? 0.451765  0.618358 0.333381 0.0634133   0.130586    -0.0608104  284  LEU A C   
2279  O  O   . LEU A 284 ? 0.483747  0.647963 0.342638 0.067743    0.132113    -0.0642418  284  LEU A O   
2280  C  CB  . LEU A 284 ? 0.502467  0.659877 0.392603 0.0541119   0.125713    -0.0418813  284  LEU A CB  
2281  C  CG  . LEU A 284 ? 0.514224  0.662859 0.4035   0.0516442   0.11541     -0.0338209  284  LEU A CG  
2282  C  CD1 . LEU A 284 ? 0.571049  0.719035 0.469509 0.0452471   0.121917    -0.0245066  284  LEU A CD1 
2283  C  CD2 . LEU A 284 ? 0.568418  0.708029 0.429746 0.0550827   0.110771    -0.0306387  284  LEU A CD2 
2284  N  N   . GLN A 285 ? 0.418558  0.594947 0.323302 0.0616339   0.137773    -0.0647884  285  GLN A N   
2285  C  CA  . GLN A 285 ? 0.449025  0.634063 0.353058 0.0644527   0.149559    -0.0728653  285  GLN A CA  
2286  C  C   . GLN A 285 ? 0.425601  0.609274 0.31889  0.0714632   0.142706    -0.0838277  285  GLN A C   
2287  O  O   . GLN A 285 ? 0.416311  0.601622 0.291409 0.0750011   0.150471    -0.088505   285  GLN A O   
2288  C  CB  . GLN A 285 ? 0.44067   0.637051 0.374941 0.0617465   0.156547    -0.0760998  285  GLN A CB  
2289  C  CG  . GLN A 285 ? 0.599559  0.806428 0.53679  0.0646129   0.169735    -0.0850837  285  GLN A CG  
2290  C  CD  . GLN A 285 ? 0.65587   0.867549 0.608264 0.0702898   0.162797    -0.0981244  285  GLN A CD  
2291  O  OE1 . GLN A 285 ? 0.672284  0.884391 0.646691 0.0699658   0.152301    -0.0996654  285  GLN A OE1 
2292  N  NE2 . GLN A 285 ? 0.653551  0.867954 0.593189 0.0757265   0.168167    -0.107436   285  GLN A NE2 
2293  N  N   . GLN A 286 ? 0.392646  0.57285  0.296455 0.0734217   0.128217    -0.0879739  286  GLN A N   
2294  C  CA  . GLN A 286 ? 0.392512  0.572132 0.291557 0.0797642   0.121817    -0.0997731  286  GLN A CA  
2295  C  C   . GLN A 286 ? 0.414227  0.584571 0.285299 0.0825998   0.114477    -0.098816   286  GLN A C   
2296  O  O   . GLN A 286 ? 0.430236  0.59933  0.293534 0.0878738   0.109217    -0.108723   286  GLN A O   
2297  C  CB  . GLN A 286 ? 0.386377  0.565397 0.30986  0.0802922   0.10933     -0.103995   286  GLN A CB  
2298  C  CG  . GLN A 286 ? 0.366244  0.554887 0.315646 0.0816349   0.113727    -0.111957   286  GLN A CG  
2299  C  CD  . GLN A 286 ? 0.373285  0.560501 0.346493 0.082088    0.101651    -0.11455    286  GLN A CD  
2300  O  OE1 . GLN A 286 ? 0.349034  0.527989 0.31976  0.0817812   0.0896587   -0.111927   286  GLN A OE1 
2301  N  NE2 . GLN A 286 ? 0.380569  0.575994 0.377668 0.0830971   0.104843    -0.119954   286  GLN A NE2 
2302  N  N   . GLY A 287 ? 0.414248  0.577734 0.271381 0.0793257   0.112813    -0.0873267  287  GLY A N   
2303  C  CA  . GLY A 287 ? 0.444148  0.59968  0.274573 0.0826875   0.105941    -0.0869239  287  GLY A CA  
2304  C  C   . GLY A 287 ? 0.416285  0.56545  0.252096 0.0835623   0.0892932   -0.088175   287  GLY A C   
2305  O  O   . GLY A 287 ? 0.43204   0.576934 0.251836 0.0878179   0.0817666   -0.0933144  287  GLY A O   
2306  N  N   . TRP A 288 ? 0.358431  0.507136 0.216488 0.0795778   0.0836243   -0.0837851  288  TRP A N   
2307  C  CA  . TRP A 288 ? 0.340852  0.483772 0.204415 0.0799451   0.069175    -0.0843825  288  TRP A CA  
2308  C  C   . TRP A 288 ? 0.349964  0.485395 0.193268 0.0794855   0.0644605   -0.0761822  288  TRP A C   
2309  O  O   . TRP A 288 ? 0.35058   0.484529 0.186799 0.0763132   0.0709459   -0.066273   288  TRP A O   
2310  C  CB  . TRP A 288 ? 0.316194  0.460101 0.20541  0.0754727   0.0657571   -0.0799066  288  TRP A CB  
2311  C  CG  . TRP A 288 ? 0.310696  0.460367 0.222209 0.0766208   0.0660408   -0.088076   288  TRP A CG  
2312  C  CD1 . TRP A 288 ? 0.320407  0.478014 0.239863 0.0775776   0.0761823   -0.0929923  288  TRP A CD1 
2313  C  CD2 . TRP A 288 ? 0.290299  0.437961 0.220145 0.0768834   0.0556808   -0.0915662  288  TRP A CD2 
2314  N  NE1 . TRP A 288 ? 0.300611  0.461131 0.241954 0.0790915   0.0719111   -0.0999323  288  TRP A NE1 
2315  C  CE2 . TRP A 288 ? 0.283778  0.437775 0.231491 0.0784678   0.0594703   -0.0984903  288  TRP A CE2 
2316  C  CE3 . TRP A 288 ? 0.297564  0.438786 0.231104 0.0757239   0.0442474   -0.0888978  288  TRP A CE3 
2317  C  CZ2 . TRP A 288 ? 0.266944  0.419734 0.234467 0.0792272   0.0513761   -0.102339   288  TRP A CZ2 
2318  C  CZ3 . TRP A 288 ? 0.289764  0.430131 0.242988 0.0758532   0.0372833   -0.0923462  288  TRP A CZ3 
2319  C  CH2 . TRP A 288 ? 0.271635  0.417213 0.240933 0.0777168   0.0405972   -0.098752   288  TRP A CH2 
2320  N  N   . GLN A 289 ? 0.348775  0.479499 0.187277 0.0821471   0.0524191   -0.080035   289  GLN A N   
2321  C  CA  . GLN A 289 ? 0.384482  0.508419 0.208566 0.0822021   0.0449746   -0.0734649  289  GLN A CA  
2322  C  C   . GLN A 289 ? 0.350839  0.471957 0.191951 0.0804514   0.0329855   -0.0732229  289  GLN A C   
2323  O  O   . GLN A 289 ? 0.334587  0.45809  0.19507  0.0800157   0.0298212   -0.0791597  289  GLN A O   
2324  C  CB  . GLN A 289 ? 0.431222  0.552913 0.232305 0.0880081   0.0405985   -0.0804932  289  GLN A CB  
2325  C  CG  . GLN A 289 ? 0.541223  0.665323 0.321338 0.0908206   0.0519977   -0.0823183  289  GLN A CG  
2326  C  CD  . GLN A 289 ? 0.616944  0.738259 0.38185  0.0883059   0.0609077   -0.0696482  289  GLN A CD  
2327  O  OE1 . GLN A 289 ? 0.620156  0.739037 0.394807 0.0837362   0.0607106   -0.059774   289  GLN A OE1 
2328  N  NE2 . GLN A 289 ? 0.726378  0.847612 0.466905 0.0912667   0.0691996   -0.0698185  289  GLN A NE2 
2329  N  N   . ALA A 290 ? 0.332648  0.448438 0.165882 0.0800006   0.0259155   -0.0669984  290  ALA A N   
2330  C  CA  . ALA A 290 ? 0.315572  0.429049 0.164148 0.0782817   0.0153622   -0.0666328  290  ALA A CA  
2331  C  C   . ALA A 290 ? 0.324162  0.438807 0.182465 0.0808281   0.00797079  -0.0781254  290  ALA A C   
2332  O  O   . ALA A 290 ? 0.286935  0.401949 0.16561  0.0785097   0.00412509  -0.0794907  290  ALA A O   
2333  C  CB  . ALA A 290 ? 0.315177  0.423522 0.152797 0.0788035   0.00809386  -0.060714   290  ALA A CB  
2334  N  N   . THR A 291 ? 0.344317  0.458951 0.187456 0.0856602   0.00582107  -0.0863438  291  THR A N   
2335  C  CA  . THR A 291 ? 0.389012  0.503831 0.241771 0.0880513   -0.0022252  -0.0977727  291  THR A CA  
2336  C  C   . THR A 291 ? 0.353245  0.471427 0.225992 0.0870254   0.00199592  -0.103001   291  THR A C   
2337  O  O   . THR A 291 ? 0.356463  0.473286 0.247559 0.085885    -0.00473557 -0.106574   291  THR A O   
2338  C  CB  . THR A 291 ? 0.479398  0.593532 0.310589 0.0937387   -0.00561642 -0.10623    291  THR A CB  
2339  O  OG1 . THR A 291 ? 0.618429  0.73009  0.45808  0.0944409   -0.0184243  -0.111774   291  THR A OG1 
2340  C  CG2 . THR A 291 ? 0.503014  0.620803 0.331832 0.0969981   0.00066086  -0.116395   291  THR A CG2 
2341  N  N   . HIS A 292 ? 0.356039  0.478455 0.227688 0.0870174   0.0130422   -0.102517   292  HIS A N   
2342  C  CA  . HIS A 292 ? 0.326467  0.452432 0.218528 0.0864406   0.0165181   -0.107151   292  HIS A CA  
2343  C  C   . HIS A 292 ? 0.296833  0.421424 0.209743 0.0816681   0.0133198   -0.0999296  292  HIS A C   
2344  O  O   . HIS A 292 ? 0.271394  0.395377 0.202799 0.0814145   0.00909664  -0.104021   292  HIS A O   
2345  C  CB  . HIS A 292 ? 0.364177  0.496075 0.253248 0.086694    0.0296501   -0.106611   292  HIS A CB  
2346  C  CG  . HIS A 292 ? 0.412771  0.546311 0.278929 0.0909818   0.0352599   -0.112018   292  HIS A CG  
2347  N  ND1 . HIS A 292 ? 0.448968  0.580625 0.292221 0.0908574   0.0390075   -0.104836   292  HIS A ND1 
2348  C  CD2 . HIS A 292 ? 0.451152  0.587322 0.312093 0.095823    0.0373628   -0.123878   292  HIS A CD2 
2349  C  CE1 . HIS A 292 ? 0.498878  0.631999 0.32237  0.0954206   0.0434913   -0.111626   292  HIS A CE1 
2350  N  NE2 . HIS A 292 ? 0.463698  0.599887 0.297409 0.0985289   0.042678    -0.123701   292  HIS A NE2 
2351  N  N   . MET A 293 ? 0.260811  0.384275 0.16987  0.0780396   0.015199    -0.0890232  293  MET A N   
2352  C  CA  . MET A 293 ? 0.242766  0.365121 0.168906 0.07361     0.0129511   -0.0819696  293  MET A CA  
2353  C  C   . MET A 293 ? 0.223751  0.341879 0.160606 0.0732036   0.00228954  -0.0843988  293  MET A C   
2354  O  O   . MET A 293 ? 0.196489  0.313967 0.15101  0.0712499   3.9e-07     -0.08375    293  MET A O   
2355  C  CB  . MET A 293 ? 0.246138  0.367318 0.164276 0.0702572   0.0162661   -0.0708615  293  MET A CB  
2356  C  CG  . MET A 293 ? 0.277809  0.403063 0.188184 0.0699077   0.0278235   -0.0681854  293  MET A CG  
2357  S  SD  . MET A 293 ? 0.332389  0.45523  0.229927 0.0666095   0.0332401   -0.055943   293  MET A SD  
2358  C  CE  . MET A 293 ? 0.273698  0.395746 0.192135 0.0615641   0.0296854   -0.0495537  293  MET A CE  
2359  N  N   . PHE A 294 ? 0.223095  0.338152 0.14928  0.0747768   -0.00438146 -0.086265   294  PHE A N   
2360  C  CA  . PHE A 294 ? 0.216033  0.32751  0.153342 0.0737793   -0.0140775  -0.088163   294  PHE A CA  
2361  C  C   . PHE A 294 ? 0.21642   0.327316 0.165208 0.0760779   -0.0176333  -0.0987151  294  PHE A C   
2362  O  O   . PHE A 294 ? 0.213699  0.321782 0.179117 0.0741445   -0.0227506  -0.0992306  294  PHE A O   
2363  C  CB  . PHE A 294 ? 0.220895  0.33022  0.145053 0.0753576   -0.0208286  -0.0887408  294  PHE A CB  
2364  C  CG  . PHE A 294 ? 0.220016  0.32822  0.140833 0.0723188   -0.0202603  -0.0778355  294  PHE A CG  
2365  C  CD1 . PHE A 294 ? 0.236386  0.345284 0.141997 0.0724813   -0.0134869  -0.0713729  294  PHE A CD1 
2366  C  CD2 . PHE A 294 ? 0.215818  0.322092 0.149799 0.0691047   -0.0256656  -0.0739188  294  PHE A CD2 
2367  C  CE1 . PHE A 294 ? 0.231211  0.338425 0.135178 0.0697814   -0.0128635  -0.0616945  294  PHE A CE1 
2368  C  CE2 . PHE A 294 ? 0.210171  0.315633 0.142185 0.0665488   -0.0244532  -0.0646147  294  PHE A CE2 
2369  C  CZ  . PHE A 294 ? 0.218454  0.324119 0.135464 0.067107    -0.0186431  -0.0588681  294  PHE A CZ  
2370  N  N   . ARG A 295 ? 0.226884  0.339953 0.16689  0.0802483   -0.0147473  -0.107184   295  ARG A N   
2371  C  CA  . ARG A 295 ? 0.241821  0.354036 0.193461 0.0827873   -0.0177738  -0.11785    295  ARG A CA  
2372  C  C   . ARG A 295 ? 0.232398  0.345592 0.202675 0.0813885   -0.0138276  -0.116327   295  ARG A C   
2373  O  O   . ARG A 295 ? 0.220275  0.33017  0.207091 0.0813907   -0.0186892  -0.120408   295  ARG A O   
2374  C  CB  . ARG A 295 ? 0.273317  0.387906 0.209727 0.0880557   -0.0153003  -0.128092   295  ARG A CB  
2375  C  CG  . ARG A 295 ? 0.303962  0.416754 0.223253 0.0906343   -0.0219923  -0.132565   295  ARG A CG  
2376  C  CD  . ARG A 295 ? 0.30647   0.415127 0.239764 0.0907046   -0.0330025  -0.140168   295  ARG A CD  
2377  N  NE  . ARG A 295 ? 0.322747  0.430349 0.241113 0.0933823   -0.0406308  -0.145408   295  ARG A NE  
2378  C  CZ  . ARG A 295 ? 0.327536  0.432268 0.254087 0.0939562   -0.0509122  -0.153321   295  ARG A CZ  
2379  N  NH1 . ARG A 295 ? 0.323372  0.425039 0.273402 0.0915214   -0.0544913  -0.15595    295  ARG A NH1 
2380  N  NH2 . ARG A 295 ? 0.341157  0.445829 0.252816 0.0967861   -0.0578266  -0.157954   295  ARG A NH2 
2381  N  N   . VAL A 296 ? 0.236462  0.353849 0.204813 0.080132    -0.00542263 -0.110123   296  VAL A N   
2382  C  CA  . VAL A 296 ? 0.229796  0.348563 0.216316 0.0791533   -0.0028077  -0.108775   296  VAL A CA  
2383  C  C   . VAL A 296 ? 0.210581  0.324728 0.210507 0.075024    -0.00864138 -0.101188   296  VAL A C   
2384  O  O   . VAL A 296 ? 0.202623  0.314111 0.218609 0.0750859   -0.01187    -0.102806   296  VAL A O   
2385  C  CB  . VAL A 296 ? 0.237764  0.363015 0.219937 0.0787153   0.00753711  -0.104816   296  VAL A CB  
2386  C  CG1 . VAL A 296 ? 0.234738  0.36207  0.235455 0.0771038   0.00943022  -0.101419   296  VAL A CG1 
2387  C  CG2 . VAL A 296 ? 0.265248  0.395079 0.236327 0.0830628   0.0141071   -0.113404   296  VAL A CG2 
2388  N  N   . ALA A 297 ? 0.204468  0.317109 0.197409 0.0717223   -0.0102056  -0.0931457  297  ALA A N   
2389  C  CA  . ALA A 297 ? 0.196042  0.304615 0.198986 0.0677701   -0.0149939  -0.0859756  297  ALA A CA  
2390  C  C   . ALA A 297 ? 0.198725  0.302107 0.211846 0.0683166   -0.0227654  -0.0916303  297  ALA A C   
2391  O  O   . ALA A 297 ? 0.181468  0.281272 0.208812 0.0666025   -0.0254291  -0.0892824  297  ALA A O   
2392  C  CB  . ALA A 297 ? 0.186865  0.295129 0.179385 0.0649627   -0.0152378  -0.0782085  297  ALA A CB  
2393  N  N   . GLU A 298 ? 0.214084  0.316759 0.219317 0.0706544   -0.0265978  -0.0989346  298  GLU A N   
2394  C  CA  . GLU A 298 ? 0.226979  0.324788 0.242537 0.0707714   -0.034351   -0.104953   298  GLU A CA  
2395  C  C   . GLU A 298 ? 0.238451  0.333577 0.269009 0.0725375   -0.0349443  -0.110606   298  GLU A C   
2396  O  O   . GLU A 298 ? 0.238347  0.327836 0.283854 0.0706565   -0.0398291  -0.110219   298  GLU A O   
2397  C  CB  . GLU A 298 ? 0.247275  0.346036 0.250118 0.0740343   -0.0379727  -0.113666   298  GLU A CB  
2398  C  CG  . GLU A 298 ? 0.274059  0.368147 0.288538 0.0741905   -0.0465178  -0.121558   298  GLU A CG  
2399  C  CD  . GLU A 298 ? 0.326575  0.42176  0.328971 0.0781292   -0.0510647  -0.132153   298  GLU A CD  
2400  O  OE1 . GLU A 298 ? 0.340241  0.438342 0.33034  0.0824678   -0.0472463  -0.138612   298  GLU A OE1 
2401  O  OE2 . GLU A 298 ? 0.352264  0.445733 0.357422 0.0768232   -0.0584492  -0.133865   298  GLU A OE2 
2402  N  N   . GLU A 299 ? 0.226937  0.325949 0.253886 0.0763092   -0.0296874  -0.115967   299  GLU A N   
2403  C  CA  . GLU A 299 ? 0.245212  0.342122 0.286237 0.0790431   -0.0303136  -0.122696   299  GLU A CA  
2404  C  C   . GLU A 299 ? 0.216117  0.310099 0.272473 0.076395    -0.0304039  -0.11432    299  GLU A C   
2405  O  O   . GLU A 299 ? 0.213703  0.302108 0.284917 0.0771183   -0.0344361  -0.117019   299  GLU A O   
2406  C  CB  . GLU A 299 ? 0.252664  0.3554   0.285917 0.0839002   -0.0241786  -0.13101    299  GLU A CB  
2407  C  CG  . GLU A 299 ? 0.289773  0.390416 0.336236 0.088085    -0.0256737  -0.141565   299  GLU A CG  
2408  C  CD  . GLU A 299 ? 0.31872   0.418636 0.382592 0.0880195   -0.024211   -0.137492   299  GLU A CD  
2409  O  OE1 . GLU A 299 ? 0.298033  0.402974 0.360349 0.0864282   -0.0186782  -0.129671   299  GLU A OE1 
2410  O  OE2 . GLU A 299 ? 0.357926  0.451729 0.437808 0.089569    -0.0291809  -0.14191    299  GLU A OE2 
2411  N  N   . PHE A 300 ? 0.204369  0.301438 0.256816 0.0734651   -0.0264247  -0.104229   300  PHE A N   
2412  C  CA  . PHE A 300 ? 0.196092  0.289966 0.26061  0.070841    -0.0275589  -0.0958229  300  PHE A CA  
2413  C  C   . PHE A 300 ? 0.188874  0.274707 0.261673 0.0677964   -0.0341625  -0.0928648  300  PHE A C   
2414  O  O   . PHE A 300 ? 0.179579  0.259599 0.265774 0.0678161   -0.0373005  -0.0919217  300  PHE A O   
2415  C  CB  . PHE A 300 ? 0.185551  0.284449 0.243382 0.0683      -0.0223958  -0.086698   300  PHE A CB  
2416  C  CG  . PHE A 300 ? 0.187266  0.284853 0.256428 0.0672035   -0.0227332  -0.0801545  300  PHE A CG  
2417  C  CD1 . PHE A 300 ? 0.196524  0.287046 0.27328  0.0645472   -0.0276533  -0.074137   300  PHE A CD1 
2418  C  CD2 . PHE A 300 ? 0.186709  0.290074 0.259462 0.0691366   -0.0183662  -0.0806054  300  PHE A CD2 
2419  C  CE1 . PHE A 300 ? 0.203538  0.292211 0.288559 0.0639679   -0.028633   -0.0677946  300  PHE A CE1 
2420  C  CE2 . PHE A 300 ? 0.200076  0.30227  0.283216 0.0685935   -0.0200311  -0.074939   300  PHE A CE2 
2421  C  CZ  . PHE A 300 ? 0.193042  0.287543 0.281108 0.0662087   -0.0254314  -0.0684536  300  PHE A CZ  
2422  N  N   . PHE A 301 ? 0.190435  0.275884 0.255795 0.0652785   -0.0361697  -0.0914248  301  PHE A N   
2423  C  CA  . PHE A 301 ? 0.220333  0.299406 0.294208 0.0619676   -0.0415453  -0.0890507  301  PHE A CA  
2424  C  C   . PHE A 301 ? 0.240731  0.31381  0.327071 0.0639087   -0.046565   -0.0977692  301  PHE A C   
2425  O  O   . PHE A 301 ? 0.23913   0.305168 0.33866  0.061813    -0.0494422  -0.094296   301  PHE A O   
2426  C  CB  . PHE A 301 ? 0.217043  0.297972 0.282367 0.0594524   -0.0431158  -0.0873338  301  PHE A CB  
2427  C  CG  . PHE A 301 ? 0.230302  0.314377 0.287919 0.0563713   -0.0393532  -0.0770239  301  PHE A CG  
2428  C  CD1 . PHE A 301 ? 0.252991  0.343063 0.296565 0.0576861   -0.0346458  -0.0756643  301  PHE A CD1 
2429  C  CD2 . PHE A 301 ? 0.224139  0.304805 0.288584 0.0521443   -0.0400721  -0.0687309  301  PHE A CD2 
2430  C  CE1 . PHE A 301 ? 0.243334  0.335624 0.280902 0.0549182   -0.0313536  -0.0667304  301  PHE A CE1 
2431  C  CE2 . PHE A 301 ? 0.220202  0.303722 0.277508 0.0496624   -0.0366445  -0.0603356  301  PHE A CE2 
2432  C  CZ  . PHE A 301 ? 0.225602  0.314765 0.269983 0.0510592   -0.0325807  -0.0594882  301  PHE A CZ  
2433  N  N   . THR A 302 ? 0.233545  0.308812 0.315463 0.0679278   -0.0475281  -0.109049   302  THR A N   
2434  C  CA  . THR A 302 ? 0.234888  0.304222 0.32918  0.0699796   -0.0524587  -0.118363   302  THR A CA  
2435  C  C   . THR A 302 ? 0.223918  0.289372 0.330979 0.0723809   -0.051617   -0.1187     302  THR A C   
2436  O  O   . THR A 302 ? 0.218204  0.275815 0.339486 0.0724985   -0.0562874  -0.12234    302  THR A O   
2437  C  CB  . THR A 302 ? 0.271006  0.343174 0.35691  0.0737585   -0.0545869  -0.131228   302  THR A CB  
2438  O  OG1 . THR A 302 ? 0.274093  0.352998 0.348541 0.0777957   -0.0484068  -0.134153   302  THR A OG1 
2439  C  CG2 . THR A 302 ? 0.279261  0.354061 0.354636 0.0716304   -0.0574672  -0.130827   302  THR A CG2 
2440  N  N   . SER A 303 ? 0.211859  0.282566 0.315079 0.0744259   -0.0461566  -0.115533   303  SER A N   
2441  C  CA  . SER A 303 ? 0.216114  0.284081 0.332083 0.0771148   -0.0458381  -0.115292   303  SER A CA  
2442  C  C   . SER A 303 ? 0.219625  0.278673 0.347422 0.0736038   -0.0496151  -0.105634   303  SER A C   
2443  O  O   . SER A 303 ? 0.221599  0.273905 0.363119 0.0756035   -0.0525049  -0.106472   303  SER A O   
2444  C  CB  . SER A 303 ? 0.201686  0.277959 0.312241 0.0788806   -0.0395352  -0.112112   303  SER A CB  
2445  O  OG  . SER A 303 ? 0.207275  0.284172 0.316096 0.0751233   -0.0381774  -0.0997373  303  SER A OG  
2446  N  N   . LEU A 304 ? 0.206079  0.264822 0.327977 0.0685197   -0.0494446  -0.0965334  304  LEU A N   
2447  C  CA  . LEU A 304 ? 0.219087  0.270008 0.348948 0.0646141   -0.0517453  -0.0863074  304  LEU A CA  
2448  C  C   . LEU A 304 ? 0.250003  0.29281  0.3893   0.0619383   -0.0565155  -0.0889629  304  LEU A C   
2449  O  O   . LEU A 304 ? 0.258858  0.294728 0.404622 0.0580108   -0.0578302  -0.080556   304  LEU A O   
2450  C  CB  . LEU A 304 ? 0.200368  0.255554 0.31937  0.0604282   -0.0484747  -0.0758866  304  LEU A CB  
2451  C  CG  . LEU A 304 ? 0.186346  0.249304 0.296542 0.0616996   -0.043787   -0.0717873  304  LEU A CG  
2452  C  CD1 . LEU A 304 ? 0.175465  0.241315 0.275993 0.0574016   -0.0411889  -0.0622848  304  LEU A CD1 
2453  C  CD2 . LEU A 304 ? 0.195497  0.255495 0.31468  0.0642142   -0.0447708  -0.0689462  304  LEU A CD2 
2454  N  N   . GLU A 305 ? 0.251393  0.295189 0.391309 0.0638909   -0.0589333  -0.100615   305  GLU A N   
2455  C  CA  . GLU A 305 ? 0.279863  0.317929 0.428354 0.061014    -0.0637366  -0.104684   305  GLU A CA  
2456  C  C   . GLU A 305 ? 0.275399  0.315809 0.418802 0.0555059   -0.0630533  -0.0972313  305  GLU A C   
2457  O  O   . GLU A 305 ? 0.31933   0.353913 0.473367 0.051437    -0.0659122  -0.0955177  305  GLU A O   
2458  C  CB  . GLU A 305 ? 0.337074  0.362988 0.504007 0.0596306   -0.0675642  -0.103259   305  GLU A CB  
2459  C  CG  . GLU A 305 ? 0.432137  0.453718 0.608509 0.0651614   -0.0700045  -0.113146   305  GLU A CG  
2460  C  CD  . GLU A 305 ? 0.541947  0.550214 0.736357 0.0643042   -0.0734014  -0.109504   305  GLU A CD  
2461  O  OE1 . GLU A 305 ? 0.556881  0.558479 0.755955 0.0595504   -0.0731729  -0.0975981  305  GLU A OE1 
2462  O  OE2 . GLU A 305 ? 0.545208  0.549252 0.749043 0.0687689   -0.0761946  -0.119154   305  GLU A OE2 
2463  N  N   . LEU A 306 ? 0.252104  0.301051 0.380382 0.0552686   -0.0591102  -0.0931134  306  LEU A N   
2464  C  CA  . LEU A 306 ? 0.242306  0.294731 0.365549 0.0513456   -0.0593521  -0.0898684  306  LEU A CA  
2465  C  C   . LEU A 306 ? 0.255999  0.313147 0.373143 0.0536391   -0.0627272  -0.10104    306  LEU A C   
2466  O  O   . LEU A 306 ? 0.2663    0.323786 0.382161 0.0581266   -0.0642396  -0.111125   306  LEU A O   
2467  C  CB  . LEU A 306 ? 0.225158  0.283201 0.335991 0.0501759   -0.0539659  -0.0799891  306  LEU A CB  
2468  C  CG  . LEU A 306 ? 0.255831  0.309036 0.371649 0.0478404   -0.0516144  -0.0690755  306  LEU A CG  
2469  C  CD1 . LEU A 306 ? 0.249974  0.30907  0.353458 0.0468391   -0.0468573  -0.0608824  306  LEU A CD1 
2470  C  CD2 . LEU A 306 ? 0.281315  0.32732  0.40884  0.0429309   -0.053391   -0.0638415  306  LEU A CD2 
2471  N  N   . SER A 307 ? 0.231279  0.291961 0.345029 0.0509475   -0.0644204  -0.100039   307  SER A N   
2472  C  CA  . SER A 307 ? 0.253178  0.317229 0.36248  0.0533319   -0.0693651  -0.111024   307  SER A CA  
2473  C  C   . SER A 307 ? 0.243071  0.314341 0.33205  0.0578862   -0.0666648  -0.114026   307  SER A C   
2474  O  O   . SER A 307 ? 0.215598  0.290998 0.293529 0.0574227   -0.0614168  -0.105765   307  SER A O   
2475  C  CB  . SER A 307 ? 0.270915  0.337061 0.384025 0.0495173   -0.0727824  -0.109369   307  SER A CB  
2476  O  OG  . SER A 307 ? 0.330116  0.390024 0.461274 0.0445338   -0.0732279  -0.104407   307  SER A OG  
2477  N  N   . PRO A 308 ? 0.254975  0.327785 0.337969 0.0622337   -0.070207   -0.126021   308  PRO A N   
2478  C  CA  . PRO A 308 ? 0.26405   0.343366 0.326096 0.0663751   -0.0680573  -0.129176   308  PRO A CA  
2479  C  C   . PRO A 308 ? 0.262778  0.346    0.316471 0.0646172   -0.0703659  -0.12496    308  PRO A C   
2480  O  O   . PRO A 308 ? 0.253662  0.335208 0.319445 0.0608393   -0.0745977  -0.122957   308  PRO A O   
2481  C  CB  . PRO A 308 ? 0.272374  0.350762 0.333102 0.0710785   -0.07298    -0.144394   308  PRO A CB  
2482  C  CG  . PRO A 308 ? 0.280258  0.353186 0.360492 0.0679108   -0.0804954  -0.148475   308  PRO A CG  
2483  C  CD  . PRO A 308 ? 0.282598  0.350483 0.377983 0.0635393   -0.0764002  -0.137544   308  PRO A CD  
2484  N  N   . MET A 309 ? 0.260122  0.348413 0.293873 0.067408    -0.0672053  -0.123411   309  MET A N   
2485  C  CA  . MET A 309 ? 0.283162  0.374828 0.307063 0.0672434   -0.0704873  -0.121109   309  MET A CA  
2486  C  C   . MET A 309 ? 0.296482  0.388115 0.320893 0.0697405   -0.0797853  -0.133012   309  MET A C   
2487  O  O   . MET A 309 ? 0.328302  0.419634 0.346101 0.0739808   -0.0814218  -0.143255   309  MET A O   
2488  C  CB  . MET A 309 ? 0.273465  0.36917  0.27552  0.0697832   -0.0646608  -0.116104   309  MET A CB  
2489  C  CG  . MET A 309 ? 0.285074  0.381378 0.286672 0.0673692   -0.0561079  -0.105375   309  MET A CG  
2490  S  SD  . MET A 309 ? 0.284716  0.379779 0.299808 0.0614387   -0.0564541  -0.0944886  309  MET A SD  
2491  C  CE  . MET A 309 ? 0.275375  0.365563 0.31079  0.0584923   -0.0550365  -0.0935356  309  MET A CE  
2492  N  N   . PRO A 310 ? 0.284786  0.377029 0.318241 0.0673275   -0.0865785  -0.133143   310  PRO A N   
2493  C  CA  . PRO A 310 ? 0.274536  0.367349 0.309427 0.0697435   -0.0964163  -0.145089   310  PRO A CA  
2494  C  C   . PRO A 310 ? 0.280098  0.376612 0.289961 0.0755558   -0.0988486  -0.149488   310  PRO A C   
2495  O  O   . PRO A 310 ? 0.264145  0.362941 0.257315 0.0767578   -0.0935473  -0.141425   310  PRO A O   
2496  C  CB  . PRO A 310 ? 0.282874  0.376873 0.334365 0.0652831   -0.101852   -0.141987   310  PRO A CB  
2497  C  CG  . PRO A 310 ? 0.259455  0.35517  0.307135 0.0625111   -0.0945118  -0.127932   310  PRO A CG  
2498  C  CD  . PRO A 310 ? 0.268724  0.36166  0.312175 0.06235     -0.0851872  -0.122681   310  PRO A CD  
2499  N  N   . PRO A 311 ? 0.288835  0.38575  0.295488 0.0791873   -0.107731   -0.162204   311  PRO A N   
2500  C  CA  . PRO A 311 ? 0.31624   0.41619  0.297742 0.0849882   -0.111289   -0.166346   311  PRO A CA  
2501  C  C   . PRO A 311 ? 0.311434  0.414515 0.283633 0.0848479   -0.112693   -0.157064   311  PRO A C   
2502  O  O   . PRO A 311 ? 0.322572  0.426841 0.271106 0.0884942   -0.109281   -0.152982   311  PRO A O   
2503  C  CB  . PRO A 311 ? 0.324158  0.423905 0.308909 0.0879858   -0.122706   -0.181766   311  PRO A CB  
2504  C  CG  . PRO A 311 ? 0.321808  0.417444 0.333206 0.0839909   -0.123153   -0.186652   311  PRO A CG  
2505  C  CD  . PRO A 311 ? 0.299304  0.393256 0.326228 0.0778505   -0.114962   -0.173089   311  PRO A CD  
2506  N  N   . GLU A 312 ? 0.306439  0.410592 0.297791 0.0805488   -0.11687    -0.153265   312  GLU A N   
2507  C  CA  . GLU A 312 ? 0.296021  0.403256 0.281721 0.0805457   -0.118664   -0.145008   312  GLU A CA  
2508  C  C   . GLU A 312 ? 0.27889   0.385589 0.252368 0.0796047   -0.107606   -0.131747   312  GLU A C   
2509  O  O   . GLU A 312 ? 0.27386   0.381957 0.2319   0.0820324   -0.10795    -0.125929   312  GLU A O   
2510  C  CB  . GLU A 312 ? 0.312595  0.421247 0.324881 0.075116    -0.122057   -0.142627   312  GLU A CB  
2511  C  CG  . GLU A 312 ? 0.340644  0.450938 0.367487 0.0755275   -0.134173   -0.154978   312  GLU A CG  
2512  C  CD  . GLU A 312 ? 0.384481  0.491127 0.428761 0.0731268   -0.135302   -0.164016   312  GLU A CD  
2513  O  OE1 . GLU A 312 ? 0.399246  0.50174  0.442568 0.0721787   -0.127277   -0.162176   312  GLU A OE1 
2514  O  OE2 . GLU A 312 ? 0.414462  0.522379 0.47439  0.072408    -0.144971   -0.173597   312  GLU A OE2 
2515  N  N   . PHE A 313 ? 0.257049  0.36144  0.237386 0.0763896   -0.0984467  -0.127343   313  PHE A N   
2516  C  CA  . PHE A 313 ? 0.251158  0.355174 0.221523 0.0753146   -0.0880374  -0.116091   313  PHE A CA  
2517  C  C   . PHE A 313 ? 0.266388  0.370691 0.210135 0.0805125   -0.0848678  -0.117044   313  PHE A C   
2518  O  O   . PHE A 313 ? 0.273296  0.378046 0.202979 0.0813635   -0.0813747  -0.108685   313  PHE A O   
2519  C  CB  . PHE A 313 ? 0.238644  0.340396 0.222441 0.0713432   -0.080245   -0.112507   313  PHE A CB  
2520  C  CG  . PHE A 313 ? 0.232335  0.334189 0.205437 0.0707984   -0.0699947  -0.103071   313  PHE A CG  
2521  C  CD1 . PHE A 313 ? 0.233892  0.335881 0.193484 0.0738985   -0.0644658  -0.105753   313  PHE A CD1 
2522  C  CD2 . PHE A 313 ? 0.215846  0.318031 0.193027 0.0672123   -0.0658696  -0.0922107  313  PHE A CD2 
2523  C  CE1 . PHE A 313 ? 0.229655  0.33233  0.18131  0.0730801   -0.0552657  -0.0975809  313  PHE A CE1 
2524  C  CE2 . PHE A 313 ? 0.214974  0.317252 0.183827 0.0664716   -0.0570684  -0.0843096  313  PHE A CE2 
2525  C  CZ  . PHE A 313 ? 0.223704  0.326337 0.180589 0.0692011   -0.0517222  -0.0868705  313  PHE A CZ  
2526  N  N   . TRP A 314 ? 0.271333  0.375051 0.208427 0.0838613   -0.0854688  -0.126944   314  TRP A N   
2527  C  CA  . TRP A 314 ? 0.299898  0.404043 0.211419 0.0886304   -0.0808353  -0.128063   314  TRP A CA  
2528  C  C   . TRP A 314 ? 0.337902  0.442724 0.229572 0.0931683   -0.0880773  -0.129174   314  TRP A C   
2529  O  O   . TRP A 314 ? 0.358433  0.462938 0.228152 0.0957968   -0.0833014  -0.123571   314  TRP A O   
2530  C  CB  . TRP A 314 ? 0.302419  0.406106 0.213082 0.091368    -0.0798734  -0.139702   314  TRP A CB  
2531  C  CG  . TRP A 314 ? 0.286241  0.388896 0.214984 0.0876566   -0.0727052  -0.137615   314  TRP A CG  
2532  C  CD1 . TRP A 314 ? 0.274542  0.375015 0.225727 0.0852933   -0.0760543  -0.143142   314  TRP A CD1 
2533  C  CD2 . TRP A 314 ? 0.280541  0.384014 0.206679 0.0859697   -0.0612859  -0.128938   314  TRP A CD2 
2534  N  NE1 . TRP A 314 ? 0.267657  0.367302 0.228532 0.082921    -0.067837   -0.13846    314  TRP A NE1 
2535  C  CE2 . TRP A 314 ? 0.266037  0.367973 0.213114 0.0830949   -0.0590839  -0.129913   314  TRP A CE2 
2536  C  CE3 . TRP A 314 ? 0.290455  0.395557 0.19951  0.0865181   -0.0530427  -0.120502   314  TRP A CE3 
2537  C  CZ2 . TRP A 314 ? 0.256827  0.359516 0.208365 0.0811496   -0.0497973  -0.123346   314  TRP A CZ2 
2538  C  CZ3 . TRP A 314 ? 0.277949  0.384036 0.192705 0.0840121   -0.0432724  -0.114243   314  TRP A CZ3 
2539  C  CH2 . TRP A 314 ? 0.260506  0.365754 0.196164 0.0815592   -0.0421602  -0.115936   314  TRP A CH2 
2540  N  N   . GLU A 315 ? 0.343336  0.448938 0.243794 0.0938634   -0.0997872  -0.135566   315  GLU A N   
2541  C  CA  . GLU A 315 ? 0.38259   0.488915 0.264468 0.098979    -0.108428   -0.137874   315  GLU A CA  
2542  C  C   . GLU A 315 ? 0.365826  0.472333 0.245346 0.0978203   -0.108172   -0.125533   315  GLU A C   
2543  O  O   . GLU A 315 ? 0.390482  0.496355 0.249235 0.102297    -0.111697   -0.122982   315  GLU A O   
2544  C  CB  . GLU A 315 ? 0.417903  0.52571  0.311396 0.100447    -0.122127   -0.150364   315  GLU A CB  
2545  C  CG  . GLU A 315 ? 0.490404  0.597403 0.382319 0.102973    -0.124002   -0.164263   315  GLU A CG  
2546  C  CD  . GLU A 315 ? 0.618015  0.724503 0.477079 0.109758    -0.123021   -0.167963   315  GLU A CD  
2547  O  OE1 . GLU A 315 ? 0.730005  0.837246 0.574731 0.114181    -0.132743   -0.170647   315  GLU A OE1 
2548  O  OE2 . GLU A 315 ? 0.738658  0.844198 0.585787 0.110915    -0.112848   -0.168033   315  GLU A OE2 
2549  N  N   . GLY A 316 ? 0.333795  0.440847 0.234591 0.0921932   -0.104847   -0.118463   316  GLY A N   
2550  C  CA  . GLY A 316 ? 0.331002  0.438697 0.234539 0.0910728   -0.106374   -0.108942   316  GLY A CA  
2551  C  C   . GLY A 316 ? 0.320503  0.426226 0.217355 0.0887224   -0.0948619  -0.0961315  316  GLY A C   
2552  O  O   . GLY A 316 ? 0.301261  0.406381 0.193011 0.0893265   -0.0954015  -0.0881547  316  GLY A O   
2553  N  N   . SER A 317 ? 0.314137  0.418747 0.210103 0.0865604   -0.0847276  -0.0946293  317  SER A N   
2554  C  CA  . SER A 317 ? 0.30455   0.407965 0.200896 0.0830909   -0.0743121  -0.0834925  317  SER A CA  
2555  C  C   . SER A 317 ? 0.328958  0.430123 0.200191 0.0863973   -0.0699841  -0.0769657  317  SER A C   
2556  O  O   . SER A 317 ? 0.324549  0.424973 0.176349 0.0910982   -0.0717793  -0.0815412  317  SER A O   
2557  C  CB  . SER A 317 ? 0.285445  0.388968 0.191183 0.0799187   -0.0661165  -0.0846329  317  SER A CB  
2558  O  OG  . SER A 317 ? 0.257315  0.361488 0.187264 0.0756408   -0.0681873  -0.0859953  317  SER A OG  
2559  N  N   . MET A 318 ? 0.310213  0.409839 0.18141  0.0837813   -0.0634805  -0.0661978  318  MET A N   
2560  C  CA  . MET A 318 ? 0.33479   0.431362 0.18398  0.085882    -0.0572498  -0.0589667  318  MET A CA  
2561  C  C   . MET A 318 ? 0.319393  0.416124 0.170955 0.0821747   -0.0448787  -0.0547077  318  MET A C   
2562  O  O   . MET A 318 ? 0.291913  0.388834 0.158025 0.077757    -0.0411447  -0.0490398  318  MET A O   
2563  C  CB  . MET A 318 ? 0.339075  0.433006 0.186647 0.0857454   -0.0588801  -0.0494557  318  MET A CB  
2564  C  CG  . MET A 318 ? 0.382348  0.471799 0.205166 0.0888047   -0.0544952  -0.0425197  318  MET A CG  
2565  S  SD  . MET A 318 ? 0.430088  0.515152 0.253927 0.0876962   -0.0537289  -0.0301155  318  MET A SD  
2566  C  CE  . MET A 318 ? 0.352388  0.437462 0.18882  0.0809205   -0.0406642  -0.0234327  318  MET A CE  
2567  N  N   . LEU A 319 ? 0.335477  0.432675 0.173964 0.0840319   -0.0388307  -0.0581133  319  LEU A N   
2568  C  CA  . LEU A 319 ? 0.342305  0.441482 0.189299 0.0804793   -0.0284109  -0.0570466  319  LEU A CA  
2569  C  C   . LEU A 319 ? 0.371107  0.468755 0.20249  0.0802456   -0.0178932  -0.0494694  319  LEU A C   
2570  O  O   . LEU A 319 ? 0.385717  0.485432 0.223588 0.0773642   -0.00891717 -0.0478575  319  LEU A O   
2571  C  CB  . LEU A 319 ? 0.364287  0.466457 0.216898 0.0816404   -0.0282047  -0.067744   319  LEU A CB  
2572  C  CG  . LEU A 319 ? 0.348302  0.451434 0.21831  0.0813936   -0.0377416  -0.0760485  319  LEU A CG  
2573  C  CD1 . LEU A 319 ? 0.389404  0.494414 0.263075 0.0831078   -0.0367082  -0.0866691  319  LEU A CD1 
2574  C  CD2 . LEU A 319 ? 0.340997  0.444169 0.232757 0.0764601   -0.0386276  -0.0713665  319  LEU A CD2 
2575  N  N   . GLU A 320 ? 0.382461  0.476383 0.193207 0.0834523   -0.0191424  -0.0449611  320  GLU A N   
2576  C  CA  . GLU A 320 ? 0.428249  0.519033 0.224507 0.0827508   -0.00982936 -0.0355869  320  GLU A CA  
2577  C  C   . GLU A 320 ? 0.442027  0.527377 0.230833 0.0839318   -0.0153134  -0.027379   320  GLU A C   
2578  O  O   . GLU A 320 ? 0.435599  0.52024  0.222637 0.0872852   -0.0263748  -0.0308319  320  GLU A O   
2579  C  CB  . GLU A 320 ? 0.475156  0.565565 0.247592 0.0869233   -0.00535743 -0.0386385  320  GLU A CB  
2580  C  CG  . GLU A 320 ? 0.534953  0.630744 0.313924 0.0858291   0.00268585  -0.0456533  320  GLU A CG  
2581  C  CD  . GLU A 320 ? 0.650916  0.74725  0.407062 0.090365    0.00698367  -0.0507131  320  GLU A CD  
2582  O  OE1 . GLU A 320 ? 0.78108   0.873008 0.513723 0.0943167   0.00419671  -0.0477585  320  GLU A OE1 
2583  O  OE2 . GLU A 320 ? 0.669002  0.770176 0.430809 0.0902267   0.0130846   -0.0578328  320  GLU A OE2 
2584  N  N   . LYS A 321 ? 0.430602  0.51224  0.216462 0.0812281   -0.00773767 -0.0170119  321  LYS A N   
2585  C  CA  . LYS A 321 ? 0.455531  0.530434 0.228251 0.0833884   -0.0109092  -0.00837318 321  LYS A CA  
2586  C  C   . LYS A 321 ? 0.473653  0.54529  0.219936 0.0897747   -0.0155268  -0.00969824 321  LYS A C   
2587  O  O   . LYS A 321 ? 0.465138  0.536601 0.19442  0.0911583   -0.00818076 -0.0103772  321  LYS A O   
2588  C  CB  . LYS A 321 ? 0.461652  0.532404 0.231756 0.0796707   0.00014422  0.0021869   321  LYS A CB  
2589  C  CG  . LYS A 321 ? 0.511483  0.574999 0.276278 0.0812906   -0.00522345 0.0107364   321  LYS A CG  
2590  C  CD  . LYS A 321 ? 0.522394  0.581714 0.293854 0.0765392   0.00325284  0.0203535   321  LYS A CD  
2591  C  CE  . LYS A 321 ? 0.568076  0.618497 0.327582 0.0795073   -0.0009404  0.0292106   321  LYS A CE  
2592  N  NZ  . LYS A 321 ? 0.544234  0.591355 0.317412 0.0746903   0.00433113  0.0361634   321  LYS A NZ  
2593  N  N   . PRO A 322 ? 0.481481  0.550726 0.222797 0.094171    -0.0278483  -0.0104213  322  PRO A N   
2594  C  CA  . PRO A 322 ? 0.526156  0.591554 0.240066 0.100843    -0.0333321  -0.0109579  322  PRO A CA  
2595  C  C   . PRO A 322 ? 0.591929  0.649892 0.280871 0.102034    -0.0245212  -0.00027731 322  PRO A C   
2596  O  O   . PRO A 322 ? 0.604646  0.657489 0.296464 0.099166    -0.0192683  0.0102371   322  PRO A O   
2597  C  CB  . PRO A 322 ? 0.508022  0.571921 0.226203 0.104387    -0.047618   -0.011181   322  PRO A CB  
2598  C  CG  . PRO A 322 ? 0.469568  0.539475 0.21891  0.0999362   -0.0506694  -0.0162089  322  PRO A CG  
2599  C  CD  . PRO A 322 ? 0.438675  0.509829 0.200748 0.0933044   -0.0375035  -0.0122212  322  PRO A CD  
2600  N  N   . ALA A 323 ? 0.651373  0.708621 0.31605  0.106069    -0.0223107  -0.00327105 323  ALA A N   
2601  C  CA  . ALA A 323 ? 0.815286  0.865464 0.45338  0.10743     -0.0130698  0.00647718  323  ALA A CA  
2602  C  C   . ALA A 323 ? 0.896807  0.938857 0.512978 0.113856    -0.0233991  0.0124616   323  ALA A C   
2603  O  O   . ALA A 323 ? 0.979295  1.01289  0.575164 0.114885    -0.0174564  0.0237814   323  ALA A O   
2604  C  CB  . ALA A 323 ? 0.773492  0.827191 0.395182 0.108827    -0.00470312 0.00011132  323  ALA A CB  
2605  N  N   . ASP A 324 ? 0.926545  0.971109 0.548325 0.118046    -0.039006   0.00498917  324  ASP A N   
2606  C  CA  . ASP A 324 ? 1.03734   1.07608  0.637235 0.125616    -0.0513214  0.00721329  324  ASP A CA  
2607  C  C   . ASP A 324 ? 1.02578   1.056    0.626285 0.126002    -0.0538289  0.0202968   324  ASP A C   
2608  O  O   . ASP A 324 ? 1.2382    1.26334  0.824065 0.132457    -0.0653783  0.0229352   324  ASP A O   
2609  C  CB  . ASP A 324 ? 1.00957   1.05467  0.619921 0.129424    -0.0675262  -0.00553155 324  ASP A CB  
2610  C  CG  . ASP A 324 ? 0.98823   1.03724  0.631346 0.126317    -0.074914   -0.00700521 324  ASP A CG  
2611  O  OD1 . ASP A 324 ? 0.961853  1.00905  0.620375 0.120993    -0.0671133  0.00108314  324  ASP A OD1 
2612  O  OD2 . ASP A 324 ? 0.976338  1.03032  0.629704 0.129172    -0.0883003  -0.0165045  324  ASP A OD2 
2613  N  N   . GLY A 325 ? 1.02076   1.04935  0.63848  0.119498    -0.0437994  0.0279451   325  GLY A N   
2614  C  CA  . GLY A 325 ? 1.05981   1.08088  0.683539 0.119348    -0.0463939  0.0387825   325  GLY A CA  
2615  C  C   . GLY A 325 ? 1.07148   1.09678  0.718364 0.120852    -0.0604193  0.0334895   325  GLY A C   
2616  O  O   . GLY A 325 ? 1.12447   1.14584  0.762933 0.127111    -0.072678   0.0353104   325  GLY A O   
2617  N  N   . ARG A 326 ? 0.901437  0.934745 0.577814 0.115165    -0.0584211  0.0272765   326  ARG A N   
2618  C  CA  . ARG A 326 ? 0.758685  0.796423 0.459628 0.115305    -0.0689156  0.0230103   326  ARG A CA  
2619  C  C   . ARG A 326 ? 0.708591  0.748473 0.434887 0.107844    -0.0600936  0.0254698   326  ARG A C   
2620  O  O   . ARG A 326 ? 0.716297  0.758659 0.446254 0.102629    -0.0489007  0.0247158   326  ARG A O   
2621  C  CB  . ARG A 326 ? 0.73198   0.777868 0.436126 0.118528    -0.0798734  0.00981017  326  ARG A CB  
2622  C  CG  . ARG A 326 ? 0.684695  0.74042  0.418544 0.114324    -0.0824875  -0.00029781 326  ARG A CG  
2623  C  CD  . ARG A 326 ? 0.727527  0.78943  0.461136 0.118158    -0.0938824  -0.0127066  326  ARG A CD  
2624  N  NE  . ARG A 326 ? 0.784309  0.849011 0.506361 0.118168    -0.0898595  -0.0203976  326  ARG A NE  
2625  C  CZ  . ARG A 326 ? 0.705219  0.776913 0.444487 0.11438     -0.0880381  -0.0299735  326  ARG A CZ  
2626  N  NH1 . ARG A 326 ? 0.653699  0.730064 0.421569 0.109676    -0.0887239  -0.0320699  326  ARG A NH1 
2627  N  NH2 . ARG A 326 ? 0.71771   0.791287 0.445433 0.115282    -0.0848582  -0.037122   326  ARG A NH2 
2628  N  N   . GLU A 327 ? 0.632918  0.671289 0.375354 0.107613    -0.064627   0.0289606   327  GLU A N   
2629  C  CA  . GLU A 327 ? 0.63771   0.678906 0.404626 0.101045    -0.0578553  0.0296605   327  GLU A CA  
2630  C  C   . GLU A 327 ? 0.551534  0.603446 0.339453 0.0981458   -0.0606414  0.0184931   327  GLU A C   
2631  O  O   . GLU A 327 ? 0.535571  0.59208  0.328445 0.101625    -0.0715125  0.0114793   327  GLU A O   
2632  C  CB  . GLU A 327 ? 0.643985  0.680942 0.422563 0.102022    -0.0619936  0.0353699   327  GLU A CB  
2633  C  CG  . GLU A 327 ? 0.709008  0.73388  0.469718 0.105199    -0.0605977  0.0471501   327  GLU A CG  
2634  C  CD  . GLU A 327 ? 0.84093   0.859941 0.603915 0.0994      -0.0474382  0.0552159   327  GLU A CD  
2635  O  OE1 . GLU A 327 ? 0.957296  0.965616 0.704123 0.101553    -0.0451624  0.0651754   327  GLU A OE1 
2636  O  OE2 . GLU A 327 ? 0.774744  0.799128 0.555097 0.0929333   -0.0398334  0.0520043   327  GLU A OE2 
2637  N  N   . VAL A 328 ? 0.493134  0.548769 0.294108 0.0917427   -0.0510715  0.0170067   328  VAL A N   
2638  C  CA  . VAL A 328 ? 0.417777  0.482142 0.23897  0.0886484   -0.0529477  0.00790868  328  VAL A CA  
2639  C  C   . VAL A 328 ? 0.380062  0.445578 0.220269 0.0825989   -0.045648   0.0106455   328  VAL A C   
2640  O  O   . VAL A 328 ? 0.421876  0.482052 0.258008 0.0805582   -0.0382943  0.0182029   328  VAL A O   
2641  C  CB  . VAL A 328 ? 0.446718  0.51552  0.262544 0.0878644   -0.0500358  0.00062393  328  VAL A CB  
2642  C  CG1 . VAL A 328 ? 0.417438  0.485611 0.213886 0.0939142   -0.0573639  -0.00366291 328  VAL A CG1 
2643  C  CG2 . VAL A 328 ? 0.422847  0.490369 0.234344 0.083612    -0.0370149  0.00435034  328  VAL A CG2 
2644  N  N   . VAL A 329 ? 0.340577  0.412665 0.201059 0.0797028   -0.0476384  0.0045736   329  VAL A N   
2645  C  CA  . VAL A 329 ? 0.333458  0.40716  0.209673 0.0739657   -0.0403722  0.00613967  329  VAL A CA  
2646  C  C   . VAL A 329 ? 0.380966  0.457031 0.254682 0.0708182   -0.0329196  0.00354074  329  VAL A C   
2647  O  O   . VAL A 329 ? 0.371118  0.451797 0.247997 0.0711133   -0.0357074  -0.00363897 329  VAL A O   
2648  C  CB  . VAL A 329 ? 0.290573  0.370194 0.18801  0.072217    -0.0450036  0.00093046  329  VAL A CB  
2649  C  CG1 . VAL A 329 ? 0.246523  0.328011 0.158121 0.0664395   -0.0375862  0.00189979  329  VAL A CG1 
2650  C  CG2 . VAL A 329 ? 0.302159  0.380832 0.205631 0.0752382   -0.0518891  0.0027201   329  VAL A CG2 
2651  N  N   . CYS A 330 ? 0.426225  0.499303 0.295811 0.0678537   -0.0236841  0.00889502  330  CYS A N   
2652  C  CA  . CYS A 330 ? 0.418338  0.494306 0.285551 0.0656452   -0.0169931  0.00599645  330  CYS A CA  
2653  C  C   . CYS A 330 ? 0.402301  0.483471 0.288051 0.0611776   -0.0145306  0.00210518  330  CYS A C   
2654  O  O   . CYS A 330 ? 0.440843  0.525636 0.327716 0.060443    -0.0121154  -0.00272823 330  CYS A O   
2655  C  CB  . CYS A 330 ? 0.446287  0.518025 0.300879 0.0645776   -0.00796605 0.012239    330  CYS A CB  
2656  S  SG  . CYS A 330 ? 0.55486   0.623954 0.383697 0.069873    -0.00853488 0.0119297   330  CYS A SG  
2657  N  N   . HIS A 331 ? 0.329414  0.410759 0.228862 0.0586456   -0.015326   0.0039798   331  HIS A N   
2658  C  CA  . HIS A 331 ? 0.3043    0.389621 0.219267 0.0545322   -0.0128534  0.00143704  331  HIS A CA  
2659  C  C   . HIS A 331 ? 0.280806  0.370553 0.201451 0.0553953   -0.0175001  -0.00595715 331  HIS A C   
2660  O  O   . HIS A 331 ? 0.285753  0.376321 0.20757  0.0579556   -0.0247186  -0.00906163 331  HIS A O   
2661  C  CB  . HIS A 331 ? 0.29691   0.38182  0.223682 0.0527825   -0.0145717  0.00360285  331  HIS A CB  
2662  C  CG  . HIS A 331 ? 0.298178  0.38608  0.237828 0.0486625   -0.0114394  0.00226816  331  HIS A CG  
2663  N  ND1 . HIS A 331 ? 0.337758  0.424184 0.279152 0.0456024   -0.00542051 0.00588719  331  HIS A ND1 
2664  C  CD2 . HIS A 331 ? 0.27172   0.363381 0.221935 0.0471229   -0.0132341  -0.00188234 331  HIS A CD2 
2665  C  CE1 . HIS A 331 ? 0.315093  0.404575 0.267023 0.0426903   -0.0042746  0.00385278  331  HIS A CE1 
2666  N  NE2 . HIS A 331 ? 0.284167  0.376432 0.241284 0.0435036   -0.00864368 -0.00031133 331  HIS A NE2 
2667  N  N   . ALA A 332 ? 0.243993  0.336515 0.169412 0.0533557   -0.0137772  -0.00904985 332  ALA A N   
2668  C  CA  . ALA A 332 ? 0.242469  0.338099 0.172682 0.0543292   -0.0175531  -0.0162372  332  ALA A CA  
2669  C  C   . ALA A 332 ? 0.224448  0.321589 0.169187 0.0529269   -0.0228305  -0.0182485  332  ALA A C   
2670  O  O   . ALA A 332 ? 0.230507  0.327655 0.184365 0.0498158   -0.0205663  -0.0148782  332  ALA A O   
2671  C  CB  . ALA A 332 ? 0.216761  0.314613 0.152061 0.0522551   -0.0122819  -0.0182863  332  ALA A CB  
2672  N  N   . SER A 333 ? 0.209612  0.308215 0.157154 0.0549      -0.0293161  -0.0241158  333  SER A N   
2673  C  CA  . SER A 333 ? 0.20862   0.308905 0.171355 0.0530958   -0.0335901  -0.0260807  333  SER A CA  
2674  C  C   . SER A 333 ? 0.212792  0.314624 0.180916 0.054208    -0.0389332  -0.0337973  333  SER A C   
2675  O  O   . SER A 333 ? 0.236244  0.337992 0.194221 0.0576235   -0.041625   -0.0382555  333  SER A O   
2676  C  CB  . SER A 333 ? 0.222495  0.322806 0.187235 0.0540652   -0.0374712  -0.0234982  333  SER A CB  
2677  O  OG  . SER A 333 ? 0.260404  0.359681 0.212467 0.0585463   -0.0420683  -0.0245905  333  SER A OG  
2678  N  N   . ALA A 334 ? 0.188392  0.29123  0.172285 0.0512307   -0.040213   -0.0352731  334  ALA A N   
2679  C  CA  . ALA A 334 ? 0.189217  0.292878 0.182292 0.0513887   -0.0454361  -0.0423841  334  ALA A CA  
2680  C  C   . ALA A 334 ? 0.200215  0.306003 0.204564 0.050833    -0.0512767  -0.0439691  334  ALA A C   
2681  O  O   . ALA A 334 ? 0.202313  0.308886 0.214152 0.0483211   -0.0490286  -0.0391817  334  ALA A O   
2682  C  CB  . ALA A 334 ? 0.177144  0.279632 0.181468 0.0479567   -0.0421019  -0.0420236  334  ALA A CB  
2683  N  N   . TRP A 335 ? 0.18448   0.291485 0.192612 0.0526773   -0.0583595  -0.0514601  335  TRP A N   
2684  C  CA  . TRP A 335 ? 0.204721  0.314756 0.222125 0.0531931   -0.0650816  -0.0540816  335  TRP A CA  
2685  C  C   . TRP A 335 ? 0.206922  0.31798  0.240997 0.0512353   -0.0698105  -0.0610969  335  TRP A C   
2686  O  O   . TRP A 335 ? 0.219099  0.329047 0.250645 0.053023    -0.0733775  -0.0679983  335  TRP A O   
2687  C  CB  . TRP A 335 ? 0.224355  0.335198 0.227511 0.0586401   -0.0714678  -0.0569207  335  TRP A CB  
2688  C  CG  . TRP A 335 ? 0.241601  0.350783 0.229803 0.0606233   -0.0677607  -0.0496458  335  TRP A CG  
2689  C  CD1 . TRP A 335 ? 0.246304  0.352449 0.220766 0.0607568   -0.0606936  -0.0450856  335  TRP A CD1 
2690  C  CD2 . TRP A 335 ? 0.255622  0.365823 0.242285 0.0628062   -0.0710667  -0.0462495  335  TRP A CD2 
2691  N  NE1 . TRP A 335 ? 0.253209  0.357762 0.217791 0.0623305   -0.0588712  -0.0386531  335  TRP A NE1 
2692  C  CE2 . TRP A 335 ? 0.25588   0.362514 0.227374 0.0638272   -0.0652436  -0.039094   335  TRP A CE2 
2693  C  CE3 . TRP A 335 ? 0.253857  0.367732 0.25181  0.0640109   -0.0783495  -0.048755   335  TRP A CE3 
2694  C  CZ2 . TRP A 335 ? 0.257018  0.36251  0.222975 0.0663184   -0.0667442  -0.0341736  335  TRP A CZ2 
2695  C  CZ3 . TRP A 335 ? 0.241723  0.3553   0.234815 0.0667376   -0.0798784  -0.0440186  335  TRP A CZ3 
2696  C  CH2 . TRP A 335 ? 0.264472  0.373394 0.241279 0.0680161   -0.0743477  -0.0367743  335  TRP A CH2 
2697  N  N   . ASP A 336 ? 0.200702  0.313718 0.252415 0.0473444   -0.0692319  -0.0592998  336  ASP A N   
2698  C  CA  . ASP A 336 ? 0.197061  0.311405 0.267209 0.0449963   -0.0739592  -0.0655145  336  ASP A CA  
2699  C  C   . ASP A 336 ? 0.208513  0.32816  0.285749 0.0468817   -0.0815648  -0.0692793  336  ASP A C   
2700  O  O   . ASP A 336 ? 0.17995   0.302186 0.259353 0.0465107   -0.0794666  -0.0642431  336  ASP A O   
2701  C  CB  . ASP A 336 ? 0.1949    0.307945 0.279756 0.0392389   -0.0673831  -0.0603295  336  ASP A CB  
2702  C  CG  . ASP A 336 ? 0.229646  0.342111 0.334162 0.0357525   -0.070277   -0.0655059  336  ASP A CG  
2703  O  OD1 . ASP A 336 ? 0.220497  0.335137 0.330446 0.0376336   -0.0784507  -0.0739334  336  ASP A OD1 
2704  O  OD2 . ASP A 336 ? 0.26646   0.375852 0.380669 0.0311274   -0.0644515  -0.060965   336  ASP A OD2 
2705  N  N   . PHE A 337 ? 0.213092  0.334389 0.293227 0.0494051   -0.0907155  -0.078486   337  PHE A N   
2706  C  CA  . PHE A 337 ? 0.219212  0.346073 0.308693 0.0512541   -0.0992897  -0.0831832  337  PHE A CA  
2707  C  C   . PHE A 337 ? 0.224678  0.355224 0.342033 0.0460928   -0.100344   -0.085965   337  PHE A C   
2708  O  O   . PHE A 337 ? 0.237209  0.373566 0.365997 0.0472789   -0.107518   -0.090297   337  PHE A O   
2709  C  CB  . PHE A 337 ? 0.243431  0.370471 0.320557 0.0569867   -0.109301   -0.0919735  337  PHE A CB  
2710  C  CG  . PHE A 337 ? 0.250181  0.374732 0.300085 0.0623315   -0.108227   -0.0877635  337  PHE A CG  
2711  C  CD1 . PHE A 337 ? 0.248395  0.367979 0.281896 0.0625272   -0.100577   -0.0839536  337  PHE A CD1 
2712  C  CD2 . PHE A 337 ? 0.25607   0.383124 0.297516 0.0671575   -0.11476    -0.0873306  337  PHE A CD2 
2713  C  CE1 . PHE A 337 ? 0.255199  0.372518 0.265276 0.0667096   -0.0985053  -0.0794415  337  PHE A CE1 
2714  C  CE2 . PHE A 337 ? 0.273886  0.397581 0.290277 0.0717376   -0.113193   -0.0824364  337  PHE A CE2 
2715  C  CZ  . PHE A 337 ? 0.271733  0.390596 0.272639 0.0712077   -0.104608   -0.0783559  337  PHE A CZ  
2716  N  N   . TYR A 338 ? 0.227943  0.355232 0.356799 0.0405935   -0.0938049  -0.0837787  338  TYR A N   
2717  C  CA  . TYR A 338 ? 0.249582  0.379501 0.404651 0.0348994   -0.0928263  -0.0848507  338  TYR A CA  
2718  C  C   . TYR A 338 ? 0.275479  0.408119 0.44691  0.0347965   -0.102897   -0.0960679  338  TYR A C   
2719  O  O   . TYR A 338 ? 0.250027  0.386919 0.445062 0.0306477   -0.103751   -0.0980492  338  TYR A O   
2720  C  CB  . TYR A 338 ? 0.25319   0.38886  0.417368 0.0333345   -0.0891123  -0.079291   338  TYR A CB  
2721  C  CG  . TYR A 338 ? 0.268971  0.400874 0.422465 0.0313987   -0.0778937  -0.0687468  338  TYR A CG  
2722  C  CD1 . TYR A 338 ? 0.273196  0.402206 0.436843 0.0255447   -0.0695823  -0.0636662  338  TYR A CD1 
2723  C  CD2 . TYR A 338 ? 0.300457  0.43141  0.433777 0.035406    -0.0758564  -0.063848   338  TYR A CD2 
2724  C  CE1 . TYR A 338 ? 0.310879  0.436146 0.463081 0.0242807   -0.0605242  -0.0548786  338  TYR A CE1 
2725  C  CE2 . TYR A 338 ? 0.320854  0.448397 0.444833 0.033693    -0.0664903  -0.055321   338  TYR A CE2 
2726  C  CZ  . TYR A 338 ? 0.329056  0.454074 0.462423 0.0282419   -0.0591309  -0.0511238  338  TYR A CZ  
2727  O  OH  . TYR A 338 ? 0.401032  0.52296  0.525436 0.0266628   -0.0506923  -0.0432473  338  TYR A OH  
2728  N  N   . ASN A 339 ? 0.264036  0.394373 0.424372 0.0390049   -0.110241   -0.103933   339  ASN A N   
2729  C  CA  . ASN A 339 ? 0.256884  0.389341 0.432909 0.0388526   -0.120258   -0.115579   339  ASN A CA  
2730  C  C   . ASN A 339 ? 0.265125  0.39024  0.442191 0.0370743   -0.118938   -0.119491   339  ASN A C   
2731  O  O   . ASN A 339 ? 0.279287  0.40385  0.464027 0.0378275   -0.12701    -0.130091   339  ASN A O   
2732  C  CB  . ASN A 339 ? 0.282351  0.418885 0.446042 0.0458593   -0.131929   -0.12344    339  ASN A CB  
2733  C  CG  . ASN A 339 ? 0.27684   0.408551 0.410931 0.0516519   -0.132319   -0.124085   339  ASN A CG  
2734  O  OD1 . ASN A 339 ? 0.252518  0.378512 0.375619 0.0506418   -0.123722   -0.118654   339  ASN A OD1 
2735  N  ND2 . ASN A 339 ? 0.274491  0.408582 0.395218 0.0579389   -0.142342   -0.130935   339  ASN A ND2 
2736  N  N   . ARG A 340 ? 0.261684  0.380881 0.429179 0.0354738   -0.109165   -0.111249   340  ARG A N   
2737  C  CA  . ARG A 340 ? 0.304767  0.416463 0.474528 0.0337713   -0.106849   -0.113439   340  ARG A CA  
2738  C  C   . ARG A 340 ? 0.310115  0.419583 0.463323 0.0396791   -0.112945   -0.122514   340  ARG A C   
2739  O  O   . ARG A 340 ? 0.321008  0.424721 0.477654 0.0390966   -0.112717   -0.126764   340  ARG A O   
2740  C  CB  . ARG A 340 ? 0.365721  0.475385 0.563225 0.0278044   -0.108106   -0.117162   340  ARG A CB  
2741  C  CG  . ARG A 340 ? 0.370832  0.481405 0.581885 0.021671    -0.0993314  -0.106662   340  ARG A CG  
2742  C  CD  . ARG A 340 ? 0.425063  0.532588 0.662858 0.0154851   -0.0996965  -0.109676   340  ARG A CD  
2743  N  NE  . ARG A 340 ? 0.51795   0.633912 0.769577 0.0159463   -0.108474   -0.118139   340  ARG A NE  
2744  C  CZ  . ARG A 340 ? 0.606624  0.727937 0.882324 0.0108586   -0.107919   -0.117911   340  ARG A CZ  
2745  N  NH1 . ARG A 340 ? 0.523138  0.641951 0.810456 0.00447671  -0.0975139  -0.108331   340  ARG A NH1 
2746  N  NH2 . ARG A 340 ? 0.545825  0.67508  0.833556 0.0124327   -0.118058   -0.127682   340  ARG A NH2 
2747  N  N   . LYS A 341 ? 0.311834  0.425256 0.44582  0.045506    -0.117407   -0.124592   341  LYS A N   
2748  C  CA  . LYS A 341 ? 0.327346  0.439605 0.444172 0.0514787   -0.123505   -0.133742   341  LYS A CA  
2749  C  C   . LYS A 341 ? 0.31135   0.423492 0.39992  0.056259    -0.118871   -0.1277     341  LYS A C   
2750  O  O   . LYS A 341 ? 0.312268  0.420891 0.386318 0.0591532   -0.116416   -0.13017    341  LYS A O   
2751  C  CB  . LYS A 341 ? 0.363408  0.480925 0.485333 0.0543272   -0.136178   -0.144327   341  LYS A CB  
2752  C  CG  . LYS A 341 ? 0.516564  0.632051 0.654224 0.0532883   -0.143555   -0.156956   341  LYS A CG  
2753  C  CD  . LYS A 341 ? 0.619783  0.73052  0.782405 0.0461651   -0.138358   -0.155156   341  LYS A CD  
2754  C  CE  . LYS A 341 ? 0.648048  0.755687 0.824645 0.045808    -0.146216   -0.168605   341  LYS A CE  
2755  N  NZ  . LYS A 341 ? 0.679072  0.781902 0.882275 0.0384914   -0.141972   -0.166267   341  LYS A NZ  
2756  N  N   . ASP A 342 ? 0.279279  0.395305 0.361105 0.0572009   -0.117894   -0.12048    342  ASP A N   
2757  C  CA  . ASP A 342 ? 0.289367  0.40502  0.345384 0.0616199   -0.11429    -0.114783   342  ASP A CA  
2758  C  C   . ASP A 342 ? 0.265643  0.378949 0.319071 0.058357    -0.102574   -0.102944   342  ASP A C   
2759  O  O   . ASP A 342 ? 0.241568  0.356377 0.307537 0.054386    -0.098991   -0.0963079  342  ASP A O   
2760  C  CB  . ASP A 342 ? 0.298742  0.418809 0.346673 0.0655118   -0.120873   -0.114077   342  ASP A CB  
2761  C  CG  . ASP A 342 ? 0.359479  0.48152  0.403141 0.070304    -0.13319    -0.126105   342  ASP A CG  
2762  O  OD1 . ASP A 342 ? 0.336268  0.455842 0.358663 0.0749698   -0.134141   -0.13001    342  ASP A OD1 
2763  O  OD2 . ASP A 342 ? 0.360332  0.486473 0.422814 0.0691241   -0.141455   -0.132059   342  ASP A OD2 
2764  N  N   . PHE A 343 ? 0.249914  0.359954 0.286582 0.0603312   -0.0967494  -0.100937   343  PHE A N   
2765  C  CA  . PHE A 343 ? 0.228717  0.336757 0.261708 0.0577328   -0.0863574  -0.0905492  343  PHE A CA  
2766  C  C   . PHE A 343 ? 0.225388  0.332436 0.234198 0.0621526   -0.083011   -0.0891796  343  PHE A C   
2767  O  O   . PHE A 343 ? 0.251739  0.358062 0.251825 0.065648    -0.0861535  -0.0970587  343  PHE A O   
2768  C  CB  . PHE A 343 ? 0.216448  0.320656 0.260339 0.0544625   -0.081831   -0.0911578  343  PHE A CB  
2769  C  CG  . PHE A 343 ? 0.209842  0.313373 0.277745 0.0499826   -0.0848826  -0.0938515  343  PHE A CG  
2770  C  CD1 . PHE A 343 ? 0.198206  0.301891 0.278958 0.0450034   -0.0801854  -0.0858179  343  PHE A CD1 
2771  C  CD2 . PHE A 343 ? 0.226961  0.329654 0.304453 0.050653    -0.092194   -0.104481   343  PHE A CD2 
2772  C  CE1 . PHE A 343 ? 0.197491  0.300303 0.299989 0.0405103   -0.0818252  -0.0875131  343  PHE A CE1 
2773  C  CE2 . PHE A 343 ? 0.220742  0.322312 0.321768 0.0459367   -0.0944213  -0.106553   343  PHE A CE2 
2774  C  CZ  . PHE A 343 ? 0.205696  0.307173 0.318898 0.0407244   -0.0886383  -0.0974655  343  PHE A CZ  
2775  N  N   . ARG A 344 ? 0.1946    0.301823 0.192854 0.0622365   -0.0774726  -0.0801341  344  ARG A N   
2776  C  CA  . ARG A 344 ? 0.213483  0.319945 0.188945 0.0663292   -0.0748661  -0.078194   344  ARG A CA  
2777  C  C   . ARG A 344 ? 0.208122  0.313249 0.178316 0.0641649   -0.0651098  -0.0683413  344  ARG A C   
2778  O  O   . ARG A 344 ? 0.200959  0.306272 0.182489 0.0603493   -0.0620857  -0.0622915  344  ARG A O   
2779  C  CB  . ARG A 344 ? 0.220831  0.328658 0.184854 0.0703163   -0.0813033  -0.0779062  344  ARG A CB  
2780  C  CG  . ARG A 344 ? 0.242818  0.352319 0.207892 0.0736312   -0.092098   -0.0885552  344  ARG A CG  
2781  C  CD  . ARG A 344 ? 0.262921  0.37359  0.215909 0.0780451   -0.0989003  -0.0870143  344  ARG A CD  
2782  N  NE  . ARG A 344 ? 0.288836  0.402086 0.247773 0.0805896   -0.11063    -0.0974944  344  ARG A NE  
2783  C  CZ  . ARG A 344 ? 0.338256  0.453034 0.28823  0.0853614   -0.11981    -0.0992811  344  ARG A CZ  
2784  N  NH1 . ARG A 344 ? 0.32643   0.439966 0.263858 0.0876113   -0.118354   -0.0905586  344  ARG A NH1 
2785  N  NH2 . ARG A 344 ? 0.350088  0.467379 0.30452  0.0879757   -0.130997   -0.10994    344  ARG A NH2 
2786  N  N   . ILE A 345 ? 0.220039  0.324028 0.172847 0.0666714   -0.0601201  -0.067326   345  ILE A N   
2787  C  CA  . ILE A 345 ? 0.210728  0.313718 0.157522 0.064937    -0.0516662  -0.0582174  345  ILE A CA  
2788  C  C   . ILE A 345 ? 0.220785  0.322691 0.147807 0.0685877   -0.051849   -0.0546945  345  ILE A C   
2789  O  O   . ILE A 345 ? 0.234133  0.335865 0.147795 0.0727933   -0.0556307  -0.0597662  345  ILE A O   
2790  C  CB  . ILE A 345 ? 0.199271  0.301963 0.146192 0.0636975   -0.0440761  -0.0584862  345  ILE A CB  
2791  C  CG1 . ILE A 345 ? 0.179729  0.282198 0.146557 0.059397    -0.0429848  -0.0578032  345  ILE A CG1 
2792  C  CG2 . ILE A 345 ? 0.188968  0.291033 0.124623 0.0631886   -0.036097   -0.0505405  345  ILE A CG2 
2793  C  CD1 . ILE A 345 ? 0.165528  0.267711 0.136654 0.0589973   -0.0385256  -0.0606764  345  ILE A CD1 
2794  N  N   . LYS A 346 ? 0.228297  0.328938 0.153433 0.0670255   -0.047896   -0.0459728  346  LYS A N   
2795  C  CA  . LYS A 346 ? 0.27125   0.369409 0.177956 0.070012    -0.0467007  -0.0408801  346  LYS A CA  
2796  C  C   . LYS A 346 ? 0.263928  0.360688 0.167517 0.0671706   -0.0362041  -0.0341278  346  LYS A C   
2797  O  O   . LYS A 346 ? 0.244036  0.340599 0.158074 0.0636431   -0.0331484  -0.0290633  346  LYS A O   
2798  C  CB  . LYS A 346 ? 0.266096  0.363717 0.176509 0.0708569   -0.0526758  -0.037253   346  LYS A CB  
2799  C  CG  . LYS A 346 ? 0.308724  0.402375 0.201673 0.0736354   -0.0511419  -0.0302956  346  LYS A CG  
2800  C  CD  . LYS A 346 ? 0.314566  0.406858 0.211314 0.0746269   -0.0555733  -0.0253064  346  LYS A CD  
2801  C  CE  . LYS A 346 ? 0.334407  0.427268 0.247219 0.0701468   -0.0512454  -0.0207245  346  LYS A CE  
2802  N  NZ  . LYS A 346 ? 0.330357  0.423029 0.247513 0.0655747   -0.041866   -0.0180295  346  LYS A NZ  
2803  N  N   . GLN A 347 ? 0.27978   0.375857 0.169084 0.0687583   -0.0306771  -0.0344009  347  GLN A N   
2804  C  CA  . GLN A 347 ? 0.283562  0.379182 0.172296 0.0657669   -0.0207378  -0.0287581  347  GLN A CA  
2805  C  C   . GLN A 347 ? 0.299809  0.393185 0.167394 0.0685044   -0.0157915  -0.0261399  347  GLN A C   
2806  O  O   . GLN A 347 ? 0.325158  0.419332 0.181445 0.0720683   -0.0173306  -0.0319853  347  GLN A O   
2807  C  CB  . GLN A 347 ? 0.27839   0.377383 0.179772 0.0633576   -0.0170311  -0.0333667  347  GLN A CB  
2808  C  CG  . GLN A 347 ? 0.272604  0.372367 0.174396 0.0606359   -0.00718044 -0.0289492  347  GLN A CG  
2809  C  CD  . GLN A 347 ? 0.257297  0.360315 0.174143 0.0583816   -0.00480165 -0.0326375  347  GLN A CD  
2810  O  OE1 . GLN A 347 ? 0.253554  0.357133 0.182371 0.0578782   -0.0101474  -0.0365581  347  GLN A OE1 
2811  N  NE2 . GLN A 347 ? 0.259098  0.364063 0.176775 0.0567753   0.00317365  -0.03078    347  GLN A NE2 
2812  N  N   . CYS A 348 ? 0.281253  0.371551 0.143499 0.0667153   -0.00946924 -0.0174982  348  CYS A N   
2813  C  CA  . CYS A 348 ? 0.3108    0.39848  0.154177 0.0682853   -0.00272527 -0.0135855  348  CYS A CA  
2814  C  C   . CYS A 348 ? 0.308264  0.399796 0.156145 0.0656536   0.00701245  -0.015402   348  CYS A C   
2815  O  O   . CYS A 348 ? 0.29949   0.390516 0.150821 0.0621382   0.0149415   -0.00961111 348  CYS A O   
2816  C  CB  . CYS A 348 ? 0.360624  0.442441 0.197334 0.0675742   -0.00077406 -0.00359252 348  CYS A CB  
2817  S  SG  . CYS A 348 ? 0.402335  0.480016 0.232518 0.0721247   -0.0129413  -0.00218651 348  CYS A SG  
2818  N  N   . THR A 349 ? 0.313109  0.408742 0.162909 0.0673933   0.00593482  -0.0240905  349  THR A N   
2819  C  CA  . THR A 349 ? 0.306311  0.40664  0.166953 0.0649234   0.0132749   -0.0270841  349  THR A CA  
2820  C  C   . THR A 349 ? 0.304829  0.40548  0.154318 0.0643072   0.0244275   -0.0231655  349  THR A C   
2821  O  O   . THR A 349 ? 0.320494  0.419013 0.150424 0.0675063   0.02631     -0.0226912  349  THR A O   
2822  C  CB  . THR A 349 ? 0.316284  0.420171 0.180743 0.0675956   0.00958777  -0.0376356  349  THR A CB  
2823  O  OG1 . THR A 349 ? 0.308526  0.411451 0.182582 0.0679369   -0.00060228 -0.040688   349  THR A OG1 
2824  C  CG2 . THR A 349 ? 0.321874  0.430463 0.20272  0.0651698   0.0148264   -0.0408962  349  THR A CG2 
2825  N  N   . ARG A 350 ? 0.30117   0.404577 0.163511 0.060111    0.0316922   -0.020378   350  ARG A N   
2826  C  CA  . ARG A 350 ? 0.319385  0.424856 0.176388 0.0587113   0.0433999   -0.0178592  350  ARG A CA  
2827  C  C   . ARG A 350 ? 0.311245  0.424143 0.183482 0.0579733   0.0473133   -0.0251015  350  ARG A C   
2828  O  O   . ARG A 350 ? 0.263314  0.37829  0.151541 0.0573472   0.0415299   -0.0291192  350  ARG A O   
2829  C  CB  . ARG A 350 ? 0.32391   0.426724 0.185388 0.0540743   0.0490227   -0.00848068 350  ARG A CB  
2830  C  CG  . ARG A 350 ? 0.39254   0.487285 0.239443 0.054939    0.0462071   -0.00055232 350  ARG A CG  
2831  C  CD  . ARG A 350 ? 0.389803  0.481587 0.24645  0.0502323   0.0492046   0.00710464  350  ARG A CD  
2832  N  NE  . ARG A 350 ? 0.405221  0.498686 0.28013  0.0483225   0.0423679   0.00496042  350  ARG A NE  
2833  C  CZ  . ARG A 350 ? 0.392628  0.490115 0.284867 0.0445055   0.0449426   0.0040046   350  ARG A CZ  
2834  N  NH1 . ARG A 350 ? 0.373079  0.47446  0.270006 0.0419228   0.0541036   0.00421903  350  ARG A NH1 
2835  N  NH2 . ARG A 350 ? 0.429121  0.527173 0.333947 0.0435057   0.0382209   0.00240051  350  ARG A NH2 
2836  N  N   . VAL A 351 ? 0.334409  0.451045 0.200677 0.058565    0.0569721   -0.0269406  351  VAL A N   
2837  C  CA  . VAL A 351 ? 0.351662  0.475725 0.231242 0.059033    0.0606914   -0.0348959  351  VAL A CA  
2838  C  C   . VAL A 351 ? 0.329037  0.457218 0.227227 0.0541426   0.0666926   -0.0313548  351  VAL A C   
2839  O  O   . VAL A 351 ? 0.356132  0.487037 0.252883 0.0519708   0.077345    -0.0282148  351  VAL A O   
2840  C  CB  . VAL A 351 ? 0.349666  0.47665  0.21425  0.0624286   0.0685515   -0.0396524  351  VAL A CB  
2841  C  CG1 . VAL A 351 ? 0.356422  0.491281 0.235893 0.0638255   0.0716089   -0.0493209  351  VAL A CG1 
2842  C  CG2 . VAL A 351 ? 0.392904  0.515236 0.236883 0.0674208   0.0616823   -0.0429388  351  VAL A CG2 
2843  N  N   . THR A 352 ? 0.306789  0.435468 0.222398 0.0524972   0.0596446   -0.0321841  352  THR A N   
2844  C  CA  . THR A 352 ? 0.304225  0.436609 0.238497 0.0483165   0.0624166   -0.0297674  352  THR A CA  
2845  C  C   . THR A 352 ? 0.278338  0.4128   0.229318 0.0491888   0.0543898   -0.0351102  352  THR A C   
2846  O  O   . THR A 352 ? 0.234244  0.364959 0.182746 0.0513574   0.0458728   -0.0374013  352  THR A O   
2847  C  CB  . THR A 352 ? 0.309818  0.437387 0.244293 0.0441859   0.0618687   -0.0208393  352  THR A CB  
2848  O  OG1 . THR A 352 ? 0.310706  0.433966 0.248065 0.0445158   0.0514893   -0.0201823  352  THR A OG1 
2849  C  CG2 . THR A 352 ? 0.32229   0.445205 0.240147 0.0431308   0.0683387   -0.0137297  352  THR A CG2 
2850  N  N   . MET A 353 ? 0.259968  0.399812 0.22877  0.0470435   0.0566418   -0.036068   353  MET A N   
2851  C  CA  . MET A 353 ? 0.257718  0.398548 0.242196 0.0475858   0.0489841   -0.0393635  353  MET A CA  
2852  C  C   . MET A 353 ? 0.269485  0.403898 0.253115 0.0459591   0.0405751   -0.0345624  353  MET A C   
2853  O  O   . MET A 353 ? 0.249982  0.381754 0.236496 0.0477474   0.0330441   -0.0372016  353  MET A O   
2854  C  CB  . MET A 353 ? 0.269658  0.417575 0.272654 0.0457966   0.0525799   -0.0407287  353  MET A CB  
2855  C  CG  . MET A 353 ? 0.306626  0.454991 0.32452  0.047047    0.0443941   -0.0437949  353  MET A CG  
2856  S  SD  . MET A 353 ? 0.357776  0.515489 0.396601 0.0456032   0.0487227   -0.0458573  353  MET A SD  
2857  C  CE  . MET A 353 ? 0.373583  0.53029  0.424128 0.0497921   0.0390872   -0.0513565  353  MET A CE  
2858  N  N   . ASP A 354 ? 0.276435  0.407973 0.256582 0.0425478   0.0418776   -0.0276384  354  ASP A N   
2859  C  CA  . ASP A 354 ? 0.267202  0.393379 0.247428 0.0414409   0.0342483   -0.0241184  354  ASP A CA  
2860  C  C   . ASP A 354 ? 0.231343  0.352624 0.199584 0.0441034   0.0290637   -0.0249205  354  ASP A C   
2861  O  O   . ASP A 354 ? 0.200818  0.319099 0.172243 0.0441572   0.0221505   -0.0247124  354  ASP A O   
2862  C  CB  . ASP A 354 ? 0.319441  0.443213 0.299805 0.0376097   0.0357802   -0.0174967  354  ASP A CB  
2863  C  CG  . ASP A 354 ? 0.446245  0.56658  0.412472 0.0371077   0.0408541   -0.0129791  354  ASP A CG  
2864  O  OD1 . ASP A 354 ? 0.491001  0.614214 0.456012 0.0360537   0.0489768   -0.0123494  354  ASP A OD1 
2865  O  OD2 . ASP A 354 ? 0.598942  0.713682 0.555648 0.0379345   0.0366984   -0.0100245  354  ASP A OD2 
2866  N  N   . GLN A 355 ? 0.22321   0.34369  0.177516 0.0461651   0.0324489   -0.0255441  355  GLN A N   
2867  C  CA  . GLN A 355 ? 0.235127  0.351841 0.178466 0.0492524   0.0267492   -0.0276079  355  GLN A CA  
2868  C  C   . GLN A 355 ? 0.219897  0.338064 0.169793 0.0519917   0.0216743   -0.035336   355  GLN A C   
2869  O  O   . GLN A 355 ? 0.205546  0.320637 0.155199 0.0531001   0.0144359   -0.036942   355  GLN A O   
2870  C  CB  . GLN A 355 ? 0.254674  0.370093 0.179755 0.0513676   0.0313329   -0.0267094  355  GLN A CB  
2871  C  CG  . GLN A 355 ? 0.273649  0.384529 0.19076  0.0491978   0.0332059   -0.0181925  355  GLN A CG  
2872  C  CD  . GLN A 355 ? 0.289762  0.395552 0.201179 0.0506162   0.0247679   -0.0163784  355  GLN A CD  
2873  O  OE1 . GLN A 355 ? 0.282063  0.386272 0.18178  0.0542299   0.0211208   -0.0191734  355  GLN A OE1 
2874  N  NE2 . GLN A 355 ? 0.257921  0.36184  0.178634 0.0480846   0.0211414   -0.0128261  355  GLN A NE2 
2875  N  N   . LEU A 356 ? 0.203816  0.326709 0.161435 0.0530045   0.0254316   -0.0403435  356  LEU A N   
2876  C  CA  . LEU A 356 ? 0.19924   0.322648 0.165713 0.0554388   0.0203994   -0.0473791  356  LEU A CA  
2877  C  C   . LEU A 356 ? 0.18705   0.307631 0.16588  0.0533242   0.0136721   -0.0447952  356  LEU A C   
2878  O  O   . LEU A 356 ? 0.192072  0.30968  0.173806 0.0545879   0.00727848  -0.0479866  356  LEU A O   
2879  C  CB  . LEU A 356 ? 0.203489  0.332709 0.178729 0.0567525   0.0258898   -0.0523912  356  LEU A CB  
2880  C  CG  . LEU A 356 ? 0.216114  0.345388 0.199925 0.060111    0.021252    -0.0606582  356  LEU A CG  
2881  C  CD1 . LEU A 356 ? 0.236591  0.363296 0.20784  0.063691    0.0182172   -0.0668285  356  LEU A CD1 
2882  C  CD2 . LEU A 356 ? 0.219752  0.355741 0.214043 0.0613065   0.0276093   -0.0648059  356  LEU A CD2 
2883  N  N   A SER A 357 ? 0.181973  0.303259 0.167796 0.0500125   0.0151589   -0.0391125  357  SER A N   
2884  N  N   B SER A 357 ? 0.180898  0.302288 0.166463 0.0500398   0.0153825   -0.0391433  357  SER A N   
2885  C  CA  A SER A 357 ? 0.166373  0.284568 0.160766 0.0480379   0.00936942  -0.0359817  357  SER A CA  
2886  C  CA  B SER A 357 ? 0.170222  0.288669 0.164154 0.0478129   0.0100068   -0.0355036  357  SER A CA  
2887  C  C   A SER A 357 ? 0.171368  0.284923 0.15883  0.0473639   0.0048577   -0.0332049  357  SER A C   
2888  C  C   B SER A 357 ? 0.174145  0.287877 0.161498 0.0474666   0.00508124  -0.0334099  357  SER A C   
2889  O  O   A SER A 357 ? 0.158695  0.269456 0.152062 0.047107    -0.00058677 -0.0336766  357  SER A O   
2890  O  O   B SER A 357 ? 0.169425  0.280503 0.162655 0.0476313   -0.00044882 -0.0347756  357  SER A O   
2891  C  CB  A SER A 357 ? 0.177247  0.29716  0.179308 0.0449466   0.0112763   -0.031166   357  SER A CB  
2892  C  CB  B SER A 357 ? 0.165395  0.28532  0.163634 0.044517    0.012874    -0.0300125  357  SER A CB  
2893  O  OG  A SER A 357 ? 0.182177  0.306926 0.194102 0.0459068   0.0138419   -0.034527   357  SER A OG  
2894  O  OG  B SER A 357 ? 0.157981  0.273967 0.156664 0.0423373   0.00867424  -0.025385   357  SER A OG  
2895  N  N   . THR A 358 ? 0.179589  0.292248 0.155886 0.0468519   0.0072854   -0.0297264  358  THR A N   
2896  C  CA  . THR A 358 ? 0.196255  0.305258 0.166546 0.0469575   0.0027551   -0.0278072  358  THR A CA  
2897  C  C   . THR A 358 ? 0.188908  0.296933 0.157642 0.0499062   -0.00248247 -0.0340151  358  THR A C   
2898  O  O   . THR A 358 ? 0.187178  0.292943 0.159002 0.0494348   -0.00779566 -0.0337387  358  THR A O   
2899  C  CB  . THR A 358 ? 0.213753  0.321462 0.171201 0.0469748   0.0060005   -0.0235199  358  THR A CB  
2900  O  OG1 . THR A 358 ? 0.223633  0.331655 0.185302 0.04378     0.00993751  -0.0183293  358  THR A OG1 
2901  C  CG2 . THR A 358 ? 0.230389  0.334672 0.183087 0.0474777   0.00074667  -0.0213752  358  THR A CG2 
2902  N  N   . VAL A 359 ? 0.20534   0.315148 0.168276 0.0529298   -0.00076467 -0.03966    359  VAL A N   
2903  C  CA  . VAL A 359 ? 0.200679  0.309602 0.163047 0.055902    -0.00610627 -0.0470344  359  VAL A CA  
2904  C  C   . VAL A 359 ? 0.182422  0.289711 0.16041  0.0547716   -0.0110636  -0.0492705  359  VAL A C   
2905  O  O   . VAL A 359 ? 0.167516  0.272403 0.148833 0.0547022   -0.0171123  -0.0510421  359  VAL A O   
2906  C  CB  . VAL A 359 ? 0.217694  0.329109 0.171938 0.0594778   -0.00263481 -0.0535996  359  VAL A CB  
2907  C  CG1 . VAL A 359 ? 0.211272  0.321594 0.167456 0.0625046   -0.00869865 -0.062546   359  VAL A CG1 
2908  C  CG2 . VAL A 359 ? 0.214557  0.326053 0.150526 0.0607281   0.00137838  -0.0506391  359  VAL A CG2 
2909  N  N   . HIS A 360 ? 0.165725  0.274046 0.154048 0.0535138   -0.0086098  -0.0481732  360  HIS A N   
2910  C  CA  . HIS A 360 ? 0.16379   0.269474 0.166049 0.0524407   -0.0128372  -0.0488031  360  HIS A CA  
2911  C  C   . HIS A 360 ? 0.156153  0.258983 0.161824 0.0491264   -0.0157558  -0.0427002  360  HIS A C   
2912  O  O   . HIS A 360 ? 0.140507  0.240252 0.153994 0.0483709   -0.0202842  -0.0438621  360  HIS A O   
2913  C  CB  . HIS A 360 ? 0.165747  0.273052 0.177445 0.0523732   -0.0101561  -0.0483708  360  HIS A CB  
2914  C  CG  . HIS A 360 ? 0.194944  0.304801 0.208317 0.0559415   -0.00827203 -0.0558835  360  HIS A CG  
2915  N  ND1 . HIS A 360 ? 0.218879  0.333403 0.223566 0.0576197   -0.00222157 -0.0581274  360  HIS A ND1 
2916  C  CD2 . HIS A 360 ? 0.204012  0.312222 0.226846 0.0582787   -0.0112532  -0.0619341  360  HIS A CD2 
2917  C  CE1 . HIS A 360 ? 0.210071  0.326564 0.218874 0.0609772   -0.0011638  -0.0657038  360  HIS A CE1 
2918  N  NE2 . HIS A 360 ? 0.219461  0.331887 0.23947  0.0615817   -0.00708006 -0.0683614  360  HIS A NE2 
2919  N  N   . HIS A 361 ? 0.152976  0.256813 0.153675 0.0470743   -0.0126645  -0.0364673  361  HIS A N   
2920  C  CA  . HIS A 361 ? 0.167426  0.26922  0.170584 0.0442065   -0.0143867  -0.0310523  361  HIS A CA  
2921  C  C   . HIS A 361 ? 0.170546  0.270959 0.172707 0.0448054   -0.0190726  -0.0334894  361  HIS A C   
2922  O  O   . HIS A 361 ? 0.158133  0.256516 0.16863  0.0429769   -0.0221884  -0.0326068  361  HIS A O   
2923  C  CB  . HIS A 361 ? 0.161015  0.264132 0.157533 0.0426658   -0.0101947  -0.025493   361  HIS A CB  
2924  C  CG  . HIS A 361 ? 0.168022  0.269298 0.166881 0.0401451   -0.0116734  -0.0207994  361  HIS A CG  
2925  N  ND1 . HIS A 361 ? 0.161984  0.262148 0.167023 0.0376134   -0.0113229  -0.0169204  361  HIS A ND1 
2926  C  CD2 . HIS A 361 ? 0.184455  0.285049 0.17991  0.0402035   -0.0136589  -0.0198918  361  HIS A CD2 
2927  C  CE1 . HIS A 361 ? 0.172921  0.271933 0.17835  0.0360718   -0.0123859  -0.0141621  361  HIS A CE1 
2928  N  NE2 . HIS A 361 ? 0.174014  0.27353  0.174693 0.0375789   -0.0137663  -0.0158602  361  HIS A NE2 
2929  N  N   . GLU A 362 ? 0.174675  0.276333 0.166555 0.047348    -0.0194511  -0.036358   362  GLU A N   
2930  C  CA  . GLU A 362 ? 0.192221  0.293309 0.182243 0.0483347   -0.0246039  -0.038593   362  GLU A CA  
2931  C  C   . GLU A 362 ? 0.195048  0.295045 0.193448 0.0493235   -0.0295941  -0.0456572  362  GLU A C   
2932  O  O   . GLU A 362 ? 0.185492  0.284603 0.191556 0.0482745   -0.0343365  -0.0470705  362  GLU A O   
2933  C  CB  . GLU A 362 ? 0.199838  0.301906 0.174798 0.0514733   -0.024467   -0.0398451  362  GLU A CB  
2934  C  CG  . GLU A 362 ? 0.229369  0.33135  0.195853 0.0506353   -0.0200122  -0.0328588  362  GLU A CG  
2935  C  CD  . GLU A 362 ? 0.274981  0.376063 0.247564 0.0480043   -0.0209868  -0.0274827  362  GLU A CD  
2936  O  OE1 . GLU A 362 ? 0.251579  0.352597 0.230918 0.0476614   -0.025948   -0.0286423  362  GLU A OE1 
2937  O  OE2 . GLU A 362 ? 0.280669  0.381434 0.251363 0.0462531   -0.0161395  -0.0222758  362  GLU A OE2 
2938  N  N   . MET A 363 ? 0.17603   0.276175 0.174407 0.0512833   -0.028395   -0.050525   363  MET A N   
2939  C  CA  . MET A 363 ? 0.18861   0.286804 0.196458 0.052182    -0.0330595  -0.0575633  363  MET A CA  
2940  C  C   . MET A 363 ? 0.154968  0.24992  0.178125 0.0487889   -0.0343423  -0.0545151  363  MET A C   
2941  O  O   . MET A 363 ? 0.156226  0.2487   0.189089 0.0482685   -0.0389561  -0.0586286  363  MET A O   
2942  C  CB  . MET A 363 ? 0.201354  0.300353 0.206296 0.0555332   -0.0313977  -0.0642389  363  MET A CB  
2943  C  CG  . MET A 363 ? 0.268402  0.365287 0.279918 0.0574503   -0.0372348  -0.0735143  363  MET A CG  
2944  S  SD  . MET A 363 ? 0.295548  0.39413  0.300975 0.0623551   -0.0348473  -0.082897   363  MET A SD  
2945  C  CE  . MET A 363 ? 0.305874  0.407881 0.289272 0.0648137   -0.0335744  -0.0827681  363  MET A CE  
2946  N  N   . GLY A 364 ? 0.140274  0.234815 0.165738 0.0463805   -0.0303518  -0.0472865  364  GLY A N   
2947  C  CA  . GLY A 364 ? 0.123142  0.214133 0.16025  0.0431464   -0.0313142  -0.0431675  364  GLY A CA  
2948  C  C   . GLY A 364 ? 0.135384  0.22604  0.176865 0.0406163   -0.0339236  -0.0415265  364  GLY A C   
2949  O  O   . GLY A 364 ? 0.129798  0.217333 0.182557 0.0384279   -0.0361478  -0.0415756  364  GLY A O   
2950  N  N   . HIS A 365 ? 0.131859  0.225647 0.16534  0.0407474   -0.0331219  -0.0394279  365  HIS A N   
2951  C  CA  . HIS A 365 ? 0.147974  0.2428   0.186043 0.0391955   -0.0359264  -0.0390687  365  HIS A CA  
2952  C  C   . HIS A 365 ? 0.157279  0.251675 0.202361 0.0403268   -0.0419909  -0.046964   365  HIS A C   
2953  O  O   . HIS A 365 ? 0.169217  0.262467 0.227262 0.0376742   -0.04443    -0.0476173  365  HIS A O   
2954  C  CB  . HIS A 365 ? 0.155934  0.253883 0.183126 0.0404282   -0.0347447  -0.0364242  365  HIS A CB  
2955  C  CG  . HIS A 365 ? 0.173011  0.27122  0.195731 0.0387565   -0.0294954  -0.0291909  365  HIS A CG  
2956  N  ND1 . HIS A 365 ? 0.191287  0.288147 0.221766 0.035354    -0.0272358  -0.0245141  365  HIS A ND1 
2957  C  CD2 . HIS A 365 ? 0.187521  0.28676  0.199768 0.0397001   -0.0261453  -0.0259339  365  HIS A CD2 
2958  C  CE1 . HIS A 365 ? 0.181207  0.278658 0.205741 0.0345835   -0.0232601  -0.0194531  365  HIS A CE1 
2959  N  NE2 . HIS A 365 ? 0.195276  0.293987 0.209659 0.0369992   -0.0224866  -0.0202055  365  HIS A NE2 
2960  N  N   . ILE A 366 ? 0.153195  0.248681 0.189696 0.0441973   -0.0443266  -0.0532944  366  ILE A N   
2961  C  CA  . ILE A 366 ? 0.167535  0.262735 0.209537 0.045696    -0.0507908  -0.0619391  366  ILE A CA  
2962  C  C   . ILE A 366 ? 0.171177  0.26207  0.228582 0.0434986   -0.0520402  -0.0643014  366  ILE A C   
2963  O  O   . ILE A 366 ? 0.170528  0.260539 0.240005 0.0419526   -0.056773   -0.0683806  366  ILE A O   
2964  C  CB  . ILE A 366 ? 0.183109  0.279684 0.211574 0.0505788   -0.0525457  -0.0688419  366  ILE A CB  
2965  C  CG1 . ILE A 366 ? 0.192226  0.291953 0.204203 0.0529741   -0.0518177  -0.0659854  366  ILE A CG1 
2966  C  CG2 . ILE A 366 ? 0.203395  0.299091 0.239078 0.0520646   -0.0598873  -0.0790483  366  ILE A CG2 
2967  C  CD1 . ILE A 366 ? 0.195002  0.296833 0.209109 0.053193    -0.0579149  -0.066929   366  ILE A CD1 
2968  N  N   . GLN A 367 ? 0.158596  0.24658  0.216461 0.043621    -0.048314   -0.0623546  367  GLN A N   
2969  C  CA  . GLN A 367 ? 0.159739  0.242389 0.231744 0.0420192   -0.0497598  -0.064013   367  GLN A CA  
2970  C  C   . GLN A 367 ? 0.176003  0.256198 0.260692 0.036989    -0.049395   -0.0580463  367  GLN A C   
2971  O  O   . GLN A 367 ? 0.169635  0.246018 0.268006 0.0351168   -0.0525928  -0.0612347  367  GLN A O   
2972  C  CB  . GLN A 367 ? 0.1569    0.237159 0.227287 0.0431909   -0.0458599  -0.061318   367  GLN A CB  
2973  C  CG  . GLN A 367 ? 0.17872   0.25258  0.262671 0.042945    -0.0482474  -0.0643648  367  GLN A CG  
2974  C  CD  . GLN A 367 ? 0.211932  0.284676 0.300034 0.0457131   -0.0533227  -0.0756632  367  GLN A CD  
2975  O  OE1 . GLN A 367 ? 0.220495  0.288155 0.322535 0.0439106   -0.0570391  -0.078633   367  GLN A OE1 
2976  N  NE2 . GLN A 367 ? 0.212627  0.289601 0.288939 0.0500548   -0.0533139  -0.0822463  367  GLN A NE2 
2977  N  N   . TYR A 368 ? 0.155577  0.237656 0.236113 0.0347121   -0.0450395  -0.0495703  368  TYR A N   
2978  C  CA  . TYR A 368 ? 0.172369  0.252897 0.263417 0.0300514   -0.0435127  -0.0439086  368  TYR A CA  
2979  C  C   . TYR A 368 ? 0.172485  0.255734 0.273036 0.028867    -0.0480372  -0.049162   368  TYR A C   
2980  O  O   . TYR A 368 ? 0.186895  0.267216 0.302316 0.025546    -0.0492554  -0.0497158  368  TYR A O   
2981  C  CB  . TYR A 368 ? 0.16121   0.245014 0.243357 0.0289913   -0.0386255  -0.036285   368  TYR A CB  
2982  C  CG  . TYR A 368 ? 0.16189   0.24218  0.248086 0.0252877   -0.0340884  -0.0279282  368  TYR A CG  
2983  C  CD1 . TYR A 368 ? 0.167345  0.243513 0.266984 0.0215549   -0.0339818  -0.0261259  368  TYR A CD1 
2984  C  CD2 . TYR A 368 ? 0.160482  0.241492 0.236457 0.0255251   -0.0298783  -0.021931   368  TYR A CD2 
2985  C  CE1 . TYR A 368 ? 0.175193  0.247863 0.276063 0.0182952   -0.0292774  -0.0177814  368  TYR A CE1 
2986  C  CE2 . TYR A 368 ? 0.171159  0.248934 0.248411 0.0226151   -0.0260854  -0.0145346  368  TYR A CE2 
2987  C  CZ  . TYR A 368 ? 0.182383  0.255917 0.27102  0.019129    -0.0255824  -0.0121599  368  TYR A CZ  
2988  O  OH  . TYR A 368 ? 0.184209  0.25435  0.271429 0.0164832   -0.0213278  -0.00427099 368  TYR A OH  
2989  N  N   . TYR A 369 ? 0.172617  0.261151 0.26512  0.0317388   -0.0509268  -0.0532989  369  TYR A N   
2990  C  CA  . TYR A 369 ? 0.173606  0.265611 0.275467 0.0310664   -0.0561808  -0.0584637  369  TYR A CA  
2991  C  C   . TYR A 369 ? 0.184073  0.273109 0.297464 0.0311768   -0.0619907  -0.0672486  369  TYR A C   
2992  O  O   . TYR A 369 ? 0.172934  0.262346 0.302365 0.0282303   -0.0651577  -0.0701752  369  TYR A O   
2993  C  CB  . TYR A 369 ? 0.162817  0.259866 0.252019 0.0354718   -0.0600472  -0.062633   369  TYR A CB  
2994  C  CG  . TYR A 369 ? 0.155963  0.255862 0.231299 0.0368011   -0.0559262  -0.0561211  369  TYR A CG  
2995  C  CD1 . TYR A 369 ? 0.140955  0.241007 0.219206 0.0335165   -0.0501849  -0.0479594  369  TYR A CD1 
2996  C  CD2 . TYR A 369 ? 0.157704  0.259743 0.216948 0.0414242   -0.0579863  -0.0585504  369  TYR A CD2 
2997  C  CE1 . TYR A 369 ? 0.144971  0.247141 0.211583 0.0347871   -0.0468484  -0.0428783  369  TYR A CE1 
2998  C  CE2 . TYR A 369 ? 0.164863  0.268624 0.212585 0.0424426   -0.0543649  -0.0524533  369  TYR A CE2 
2999  C  CZ  . TYR A 369 ? 0.163911  0.267709 0.216185 0.0390799   -0.0489968  -0.0449694  369  TYR A CZ  
3000  O  OH  . TYR A 369 ? 0.188585  0.293487 0.231132 0.0398601   -0.0454834  -0.0394673  369  TYR A OH  
3001  N  N   . LEU A 370 ? 0.19586   0.282    0.30226  0.0345823   -0.0633455  -0.07218    370  LEU A N   
3002  C  CA  . LEU A 370 ? 0.199562  0.281878 0.316881 0.0350006   -0.0686366  -0.0811229  370  LEU A CA  
3003  C  C   . LEU A 370 ? 0.201832  0.277651 0.336933 0.0301341   -0.0666724  -0.0773912  370  LEU A C   
3004  O  O   . LEU A 370 ? 0.211233  0.284349 0.361703 0.0283707   -0.0712811  -0.0836167  370  LEU A O   
3005  C  CB  . LEU A 370 ? 0.203499  0.283893 0.310301 0.0398427   -0.0694653  -0.0872623  370  LEU A CB  
3006  C  CG  . LEU A 370 ? 0.215567  0.301321 0.302674 0.0448959   -0.0704823  -0.090817   370  LEU A CG  
3007  C  CD1 . LEU A 370 ? 0.203254  0.287455 0.280594 0.0492099   -0.0691111  -0.0958889  370  LEU A CD1 
3008  C  CD2 . LEU A 370 ? 0.21685   0.305753 0.306608 0.0462341   -0.0785631  -0.09947    370  LEU A CD2 
3009  N  N   . GLN A 371 ? 0.173723  0.24619  0.30636  0.028252    -0.0601918  -0.0676607  371  GLN A N   
3010  C  CA  . GLN A 371 ? 0.186687  0.251629 0.3341   0.0241346   -0.0584286  -0.0635234  371  GLN A CA  
3011  C  C   . GLN A 371 ? 0.181485  0.247373 0.342163 0.018422    -0.0564944  -0.05874    371  GLN A C   
3012  O  O   . GLN A 371 ? 0.188462  0.248587 0.365126 0.0145342   -0.0566061  -0.0580659  371  GLN A O   
3013  C  CB  . GLN A 371 ? 0.215343  0.275952 0.355113 0.0244987   -0.0530282  -0.0548992  371  GLN A CB  
3014  C  CG  . GLN A 371 ? 0.215836  0.275128 0.347306 0.02969     -0.0545161  -0.0599653  371  GLN A CG  
3015  C  CD  . GLN A 371 ? 0.240964  0.293909 0.384713 0.0306329   -0.0591016  -0.0677062  371  GLN A CD  
3016  O  OE1 . GLN A 371 ? 0.260488  0.307282 0.419953 0.0268959   -0.0603782  -0.0669143  371  GLN A OE1 
3017  N  NE2 . GLN A 371 ? 0.277641  0.331718 0.414582 0.0357019   -0.0612093  -0.0754632  371  GLN A NE2 
3018  N  N   . TYR A 372 ? 0.183042  0.25605  0.338383 0.0178946   -0.0546096  -0.0558246  372  TYR A N   
3019  C  CA  . TYR A 372 ? 0.207467  0.282117 0.376103 0.0125285   -0.0515807  -0.0511888  372  TYR A CA  
3020  C  C   . TYR A 372 ? 0.219942  0.301238 0.399782 0.0120674   -0.0571837  -0.059047   372  TYR A C   
3021  O  O   . TYR A 372 ? 0.203915  0.289076 0.394889 0.00815539  -0.054619   -0.0560757  372  TYR A O   
3022  C  CB  . TYR A 372 ? 0.177981  0.255303 0.337155 0.0111897   -0.044325   -0.0412374  372  TYR A CB  
3023  C  CG  . TYR A 372 ? 0.165754  0.249858 0.309043 0.0146478   -0.0434914  -0.0402673  372  TYR A CG  
3024  C  CD1 . TYR A 372 ? 0.149667  0.240742 0.291705 0.0171946   -0.0482514  -0.0463818  372  TYR A CD1 
3025  C  CD2 . TYR A 372 ? 0.153534  0.236522 0.283497 0.0151178   -0.0377694  -0.0324031  372  TYR A CD2 
3026  C  CE1 . TYR A 372 ? 0.152127  0.248006 0.279773 0.0202133   -0.0470565  -0.0442837  372  TYR A CE1 
3027  C  CE2 . TYR A 372 ? 0.147794  0.236055 0.26438  0.0177798   -0.0364765  -0.0309845  372  TYR A CE2 
3028  C  CZ  . TYR A 372 ? 0.149308  0.243578 0.264822 0.0202283   -0.040787   -0.0364876  372  TYR A CZ  
3029  O  OH  . TYR A 372 ? 0.161891  0.260056 0.26468  0.0227592   -0.0393382  -0.0343061  372  TYR A OH  
3030  N  N   . LYS A 373 ? 0.230121  0.313094 0.407034 0.01625     -0.0648248  -0.0692942  373  LYS A N   
3031  C  CA  . LYS A 373 ? 0.238135  0.328546 0.420588 0.0174826   -0.0715185  -0.0770776  373  LYS A CA  
3032  C  C   . LYS A 373 ? 0.25757   0.348522 0.465647 0.01192     -0.0731112  -0.0795628  373  LYS A C   
3033  O  O   . LYS A 373 ? 0.260598  0.359091 0.477672 0.0115997   -0.077238   -0.0838269  373  LYS A O   
3034  C  CB  . LYS A 373 ? 0.232973  0.32441  0.406934 0.0230749   -0.0799624  -0.0882325  373  LYS A CB  
3035  C  CG  . LYS A 373 ? 0.2539    0.338502 0.436947 0.0229754   -0.083812   -0.095694   373  LYS A CG  
3036  C  CD  . LYS A 373 ? 0.283542  0.370489 0.454491 0.0292078   -0.0916134  -0.106942   373  LYS A CD  
3037  C  CE  . LYS A 373 ? 0.328844  0.411092 0.50967  0.03006     -0.0980368  -0.118213   373  LYS A CE  
3038  N  NZ  . LYS A 373 ? 0.362256  0.436875 0.540433 0.029606    -0.0917414  -0.112678   373  LYS A NZ  
3039  N  N   . ASP A 374 ? 0.248971  0.331927 0.469109 0.00768497  -0.0699053  -0.0767268  374  ASP A N   
3040  C  CA  . ASP A 374 ? 0.346583  0.428385 0.592437 0.00177645  -0.0707387  -0.0789431  374  ASP A CA  
3041  C  C   . ASP A 374 ? 0.333439  0.416876 0.588797 -0.00418002 -0.0617529  -0.0685878  374  ASP A C   
3042  O  O   . ASP A 374 ? 0.356267  0.440885 0.63389  -0.00957051 -0.0611824  -0.0697465  374  ASP A O   
3043  C  CB  . ASP A 374 ? 0.36672   0.439165 0.622754 0.00090676  -0.0743118  -0.0843555  374  ASP A CB  
3044  C  CG  . ASP A 374 ? 0.421494  0.495994 0.675727 0.00587626  -0.084904   -0.0984582  374  ASP A CG  
3045  O  OD1 . ASP A 374 ? 0.45399   0.537119 0.712028 0.0071404   -0.0910385  -0.105493   374  ASP A OD1 
3046  O  OD2 . ASP A 374 ? 0.45058   0.518302 0.699386 0.00880142  -0.0872127  -0.102646   374  ASP A OD2 
3047  N  N   . LEU A 375 ? 0.301336  0.386013 0.540279 -0.00314181 -0.0547955  -0.0592824  375  LEU A N   
3048  C  CA  . LEU A 375 ? 0.276402  0.363201 0.522001 -0.00815649 -0.0459838  -0.0501861  375  LEU A CA  
3049  C  C   . LEU A 375 ? 0.276466  0.374802 0.531687 -0.00833549 -0.0480565  -0.0544489  375  LEU A C   
3050  O  O   . LEU A 375 ? 0.242648  0.347088 0.491489 -0.00334936 -0.0554577  -0.0617189  375  LEU A O   
3051  C  CB  . LEU A 375 ? 0.249312  0.333782 0.474144 -0.00673847 -0.0384274  -0.0397919  375  LEU A CB  
3052  C  CG  . LEU A 375 ? 0.241632  0.315258 0.456239 -0.00595521 -0.0365337  -0.034777   375  LEU A CG  
3053  C  CD1 . LEU A 375 ? 0.238982  0.311498 0.434729 -0.00484213 -0.0296143  -0.0249293  375  LEU A CD1 
3054  C  CD2 . LEU A 375 ? 0.245782  0.310147 0.476705 -0.0108216  -0.0351608  -0.0327259  375  LEU A CD2 
3055  N  N   . PRO A 376 ? 0.287082  0.388865 0.555997 -0.013699   -0.0407294  -0.0490025  376  PRO A N   
3056  C  CA  . PRO A 376 ? 0.269813  0.383082 0.545442 -0.0132741  -0.0406989  -0.0510387  376  PRO A CA  
3057  C  C   . PRO A 376 ? 0.262152  0.379233 0.514906 -0.00714895 -0.0413551  -0.0494344  376  PRO A C   
3058  O  O   . PRO A 376 ? 0.275456  0.387439 0.509346 -0.00591749 -0.0358144  -0.0419411  376  PRO A O   
3059  C  CB  . PRO A 376 ? 0.295964  0.409562 0.583415 -0.0199471  -0.0291187  -0.0423114  376  PRO A CB  
3060  C  CG  . PRO A 376 ? 0.29648   0.400208 0.596223 -0.0252092  -0.0272824  -0.0404127  376  PRO A CG  
3061  C  CD  . PRO A 376 ? 0.303701  0.398331 0.584308 -0.0204673  -0.0324468  -0.0413074  376  PRO A CD  
3062  N  N   . VAL A 377 ? 0.234736  0.360542 0.489946 -0.00338662 -0.0483233  -0.0563265  377  VAL A N   
3063  C  CA  . VAL A 377 ? 0.270482  0.399493 0.505237 0.00258886  -0.049772   -0.0551862  377  VAL A CA  
3064  C  C   . VAL A 377 ? 0.259081  0.386665 0.48141  0.00161327  -0.0393186  -0.0450117  377  VAL A C   
3065  O  O   . VAL A 377 ? 0.229668  0.355057 0.430958 0.00585201  -0.039295   -0.042448   377  VAL A O   
3066  C  CB  . VAL A 377 ? 0.351983  0.490943 0.593232 0.00620396  -0.0568819  -0.0616197  377  VAL A CB  
3067  C  CG1 . VAL A 377 ? 0.376535  0.515721 0.614601 0.0108115   -0.069128   -0.0713826  377  VAL A CG1 
3068  C  CG2 . VAL A 377 ? 0.314711  0.461333 0.582955 0.00143775  -0.0543746  -0.0630243  377  VAL A CG2 
3069  N  N   . SER A 378 ? 0.229563  0.359003 0.464454 -0.0036771  -0.0305751  -0.0397455  378  SER A N   
3070  C  CA  . SER A 378 ? 0.220127  0.349177 0.441846 -0.00379061 -0.0214553  -0.0314019  378  SER A CA  
3071  C  C   . SER A 378 ? 0.221377  0.3405   0.424505 -0.00391225 -0.0173455  -0.0245685  378  SER A C   
3072  O  O   . SER A 378 ? 0.220597  0.338675 0.407318 -0.00215082 -0.0127222  -0.0192514  378  SER A O   
3073  C  CB  . SER A 378 ? 0.220998  0.354539 0.458715 -0.00905927 -0.0125198  -0.0276812  378  SER A CB  
3074  O  OG  . SER A 378 ? 0.24825   0.392342 0.503821 -0.00839451 -0.016062   -0.0340314  378  SER A OG  
3075  N  N   . LEU A 379 ? 0.212905  0.324927 0.420142 -0.00593049 -0.0193793  -0.0251391  379  LEU A N   
3076  C  CA  . LEU A 379 ? 0.226795  0.329317 0.419436 -0.00589369 -0.0164682  -0.0191167  379  LEU A CA  
3077  C  C   . LEU A 379 ? 0.223754  0.323113 0.402265 -0.00055847 -0.0237473  -0.0234501  379  LEU A C   
3078  O  O   . LEU A 379 ? 0.239659  0.331377 0.409526 -0.00019419 -0.0229098  -0.0201614  379  LEU A O   
3079  C  CB  . LEU A 379 ? 0.205436  0.301685 0.413835 -0.0112615  -0.0145131  -0.0174527  379  LEU A CB  
3080  C  CG  . LEU A 379 ? 0.213628  0.31316  0.438832 -0.0173332  -0.0066102  -0.0134995  379  LEU A CG  
3081  C  CD1 . LEU A 379 ? 0.210083  0.300318 0.446377 -0.0224173  -0.00413813 -0.00988365 379  LEU A CD1 
3082  C  CD2 . LEU A 379 ? 0.204866  0.306237 0.416006 -0.0172152  0.00206453  -0.00575547 379  LEU A CD2 
3083  N  N   . ARG A 380 ? 0.21884   0.323928 0.395196 0.00363911  -0.0306626  -0.0306145  380  ARG A N   
3084  C  CA  . ARG A 380 ? 0.212578  0.315468 0.374064 0.00888926  -0.0366317  -0.0347833  380  ARG A CA  
3085  C  C   . ARG A 380 ? 0.1843    0.287731 0.325957 0.0120444   -0.0332326  -0.0298898  380  ARG A C   
3086  O  O   . ARG A 380 ? 0.186197  0.294123 0.319607 0.0158624   -0.0362014  -0.0323652  380  ARG A O   
3087  C  CB  . ARG A 380 ? 0.207987  0.315674 0.375436 0.0118925   -0.0459307  -0.0447375  380  ARG A CB  
3088  C  CG  . ARG A 380 ? 0.231831  0.336567 0.416592 0.00920618  -0.0502479  -0.0506314  380  ARG A CG  
3089  C  CD  . ARG A 380 ? 0.226978  0.336906 0.414939 0.0130516   -0.0606398  -0.0614625  380  ARG A CD  
3090  N  NE  . ARG A 380 ? 0.234097  0.345131 0.444818 0.00980316  -0.0654858  -0.0683759  380  ARG A NE  
3091  C  CZ  . ARG A 380 ? 0.213903  0.331254 0.432092 0.0121473   -0.0743893  -0.0774443  380  ARG A CZ  
3092  N  NH1 . ARG A 380 ? 0.223087  0.344302 0.425387 0.0181933   -0.0797792  -0.0806108  380  ARG A NH1 
3093  N  NH2 . ARG A 380 ? 0.198776  0.318042 0.440195 0.00842573  -0.078042   -0.0831942  380  ARG A NH2 
3094  N  N   . ARG A 381 ? 0.189863  0.288297 0.323997 0.0103473   -0.0269816  -0.0225352  381  ARG A N   
3095  C  CA  . ARG A 381 ? 0.197754  0.296645 0.315347 0.0124866   -0.0232762  -0.0177896  381  ARG A CA  
3096  C  C   . ARG A 381 ? 0.172036  0.263741 0.282096 0.0117935   -0.0204324  -0.0128091  381  ARG A C   
3097  O  O   . ARG A 381 ? 0.183288  0.270121 0.302144 0.00930276  -0.0204605  -0.0120989  381  ARG A O   
3098  C  CB  . ARG A 381 ? 0.239301  0.342017 0.358747 0.0102508   -0.0170495  -0.013051   381  ARG A CB  
3099  C  CG  . ARG A 381 ? 0.347365  0.457867 0.474546 0.0110516   -0.0183228  -0.0164123  381  ARG A CG  
3100  C  CD  . ARG A 381 ? 0.427242  0.540791 0.541737 0.01596     -0.0212092  -0.0181005  381  ARG A CD  
3101  N  NE  . ARG A 381 ? 0.59059   0.701683 0.697206 0.0193543   -0.0275295  -0.0223418  381  ARG A NE  
3102  C  CZ  . ARG A 381 ? 0.571214  0.68247  0.66424  0.0236435   -0.0304803  -0.0237355  381  ARG A CZ  
3103  N  NH1 . ARG A 381 ? 0.533796  0.64808  0.621411 0.0257227   -0.029717   -0.0223303  381  ARG A NH1 
3104  N  NH2 . ARG A 381 ? 0.528193  0.636322 0.613569 0.0258374   -0.0338619  -0.0265625  381  ARG A NH2 
3105  N  N   . GLY A 382 ? 0.166514  0.257516 0.261895 0.0138253   -0.0181476  -0.00930449 382  GLY A N   
3106  C  CA  . GLY A 382 ? 0.183371  0.268142 0.272343 0.0137337   -0.0165816  -0.00508724 382  GLY A CA  
3107  C  C   . GLY A 382 ? 0.184137  0.265964 0.275692 0.00968251  -0.0106314  0.00223033  382  GLY A C   
3108  O  O   . GLY A 382 ? 0.184125  0.269852 0.280568 0.00748946  -0.00718352 0.00336021  382  GLY A O   
3109  N  N   . ALA A 383 ? 0.170474  0.245531 0.259097 0.00888432  -0.00945055 0.00703674  383  ALA A N   
3110  C  CA  . ALA A 383 ? 0.195579  0.267198 0.283821 0.0053133   -0.00357894 0.0146545   383  ALA A CA  
3111  C  C   . ALA A 383 ? 0.186694  0.26268  0.263744 0.00566623  0.00090553  0.01752     383  ALA A C   
3112  O  O   . ALA A 383 ? 0.184811  0.261884 0.263655 0.0027464   0.00646099  0.0211779   383  ALA A O   
3113  C  CB  . ALA A 383 ? 0.206223  0.269129 0.291702 0.00524903  -0.00424366 0.0194837   383  ALA A CB  
3114  N  N   . ASN A 384 ? 0.162567  0.241308 0.228911 0.00913616  -0.00112643 0.0153782   384  ASN A N   
3115  C  CA  . ASN A 384 ? 0.162549  0.246552 0.222187 0.00979633  0.00179814  0.0152855   384  ASN A CA  
3116  C  C   . ASN A 384 ? 0.177997  0.265381 0.234092 0.0134321   -0.00271345 0.0098509   384  ASN A C   
3117  O  O   . ASN A 384 ? 0.181305  0.266816 0.238912 0.0151265   -0.00703258 0.00689039  384  ASN A O   
3118  C  CB  . ASN A 384 ? 0.165742  0.247422 0.213612 0.00923075  0.0059779   0.0209731   384  ASN A CB  
3119  C  CG  . ASN A 384 ? 0.150058  0.228566 0.18745  0.0117686   0.00295011  0.022045    384  ASN A CG  
3120  O  OD1 . ASN A 384 ? 0.152862  0.233634 0.188143 0.0144732   -0.00058444 0.017973    384  ASN A OD1 
3121  N  ND2 . ASN A 384 ? 0.163294  0.237209 0.193233 0.0110301   0.00469942  0.0275692   384  ASN A ND2 
3122  N  N   . PRO A 385 ? 0.170791  0.262724 0.222062 0.0148897   -0.00175627 0.00832581  385  PRO A N   
3123  C  CA  . PRO A 385 ? 0.166595  0.260637 0.213488 0.0182066   -0.00560334 0.00415337  385  PRO A CA  
3124  C  C   . PRO A 385 ? 0.1586    0.250186 0.196797 0.0201257   -0.0071339  0.00443655  385  PRO A C   
3125  O  O   . PRO A 385 ? 0.150927  0.243442 0.187376 0.0225404   -0.0102202  0.00076442  385  PRO A O   
3126  C  CB  . PRO A 385 ? 0.154024  0.252011 0.197767 0.0190275   -0.00354581 0.00386316  385  PRO A CB  
3127  C  CG  . PRO A 385 ? 0.16012   0.259836 0.212543 0.0161663   0.00026744  0.00550996  385  PRO A CG  
3128  C  CD  . PRO A 385 ? 0.164999  0.260114 0.216444 0.0134798   0.00309315  0.0100896   385  PRO A CD  
3129  N  N   . GLY A 386 ? 0.182551  0.271387 0.215285 0.0192087   -0.00496554 0.00857824  386  GLY A N   
3130  C  CA  . GLY A 386 ? 0.155538  0.242874 0.182459 0.0210405   -0.0067921  0.00847621  386  GLY A CA  
3131  C  C   . GLY A 386 ? 0.162982  0.247497 0.195344 0.0220078   -0.0102089  0.0066371   386  GLY A C   
3132  O  O   . GLY A 386 ? 0.164784  0.249912 0.194853 0.0242958   -0.0121361  0.00417063  386  GLY A O   
3133  N  N   . PHE A 387 ? 0.152123  0.233586 0.192304 0.0202038   -0.0105292  0.00768561  387  PHE A N   
3134  C  CA  . PHE A 387 ? 0.179092  0.257252 0.226165 0.021128    -0.0140348  0.00513856  387  PHE A CA  
3135  C  C   . PHE A 387 ? 0.184617  0.266281 0.233335 0.0235467   -0.0169838  -0.00176366 387  PHE A C   
3136  O  O   . PHE A 387 ? 0.165876  0.246522 0.214996 0.0258395   -0.0194151  -0.00493693 387  PHE A O   
3137  C  CB  . PHE A 387 ? 0.170698  0.244735 0.227996 0.0184321   -0.0140265  0.00662465  387  PHE A CB  
3138  C  CG  . PHE A 387 ? 0.181505  0.249245 0.237986 0.0165677   -0.0121753  0.0135567   387  PHE A CG  
3139  C  CD1 . PHE A 387 ? 0.19221   0.26005  0.23938  0.0155775   -0.00854901 0.0190263   387  PHE A CD1 
3140  C  CD2 . PHE A 387 ? 0.19646   0.257655 0.260707 0.0160564   -0.014273   0.014552    387  PHE A CD2 
3141  C  CE1 . PHE A 387 ? 0.211785  0.273491 0.255862 0.0142979   -0.00716411 0.0256534   387  PHE A CE1 
3142  C  CE2 . PHE A 387 ? 0.229149  0.283496 0.291507 0.0144975   -0.0126398  0.021937    387  PHE A CE2 
3143  C  CZ  . PHE A 387 ? 0.22275   0.277526 0.273962 0.0138187   -0.00920018 0.027584    387  PHE A CZ  
3144  N  N   . HIS A 388 ? 0.161081  0.246585 0.211248 0.0232223   -0.0169898  -0.0041935  388  HIS A N   
3145  C  CA  . HIS A 388 ? 0.17701   0.26522  0.226908 0.0258648   -0.0203835  -0.0104995  388  HIS A CA  
3146  C  C   . HIS A 388 ? 0.180465  0.270549 0.220024 0.0285911   -0.0196656  -0.0113272  388  HIS A C   
3147  O  O   . HIS A 388 ? 0.192336  0.283147 0.229929 0.0311551   -0.021697   -0.0159321  388  HIS A O   
3148  C  CB  . HIS A 388 ? 0.187045  0.279134 0.239154 0.0253563   -0.020747   -0.0117853  388  HIS A CB  
3149  C  CG  . HIS A 388 ? 0.204598  0.297657 0.264272 0.0261633   -0.025404   -0.0177568  388  HIS A CG  
3150  N  ND1 . HIS A 388 ? 0.207204  0.300765 0.263011 0.0294419   -0.0292255  -0.0235714  388  HIS A ND1 
3151  C  CD2 . HIS A 388 ? 0.208186  0.302323 0.279687 0.0239982   -0.0268543  -0.0192155  388  HIS A CD2 
3152  C  CE1 . HIS A 388 ? 0.215989  0.31061  0.280358 0.0294877   -0.0337138  -0.0287945  388  HIS A CE1 
3153  N  NE2 . HIS A 388 ? 0.205676  0.300502 0.281032 0.025939    -0.0324005  -0.0262015  388  HIS A NE2 
3154  N  N   . GLU A 389 ? 0.170112  0.261146 0.203128 0.0279404   -0.0163877  -0.00712319 389  GLU A N   
3155  C  CA  . GLU A 389 ? 0.176473  0.269399 0.201447 0.0298632   -0.01517    -0.00769691 389  GLU A CA  
3156  C  C   . GLU A 389 ? 0.158818  0.250332 0.184779 0.030906    -0.0155836  -0.0081818  389  GLU A C   
3157  O  O   . GLU A 389 ? 0.206783  0.300495 0.228509 0.0325882   -0.0145601  -0.00984441 389  GLU A O   
3158  C  CB  . GLU A 389 ? 0.175717  0.269854 0.194811 0.0287702   -0.011956   -0.00384744 389  GLU A CB  
3159  C  CG  . GLU A 389 ? 0.176319  0.27209  0.194821 0.0283955   -0.0114675  -0.00357322 389  GLU A CG  
3160  C  CD  . GLU A 389 ? 0.197698  0.295094 0.214655 0.030789    -0.0140774  -0.00753334 389  GLU A CD  
3161  O  OE1 . GLU A 389 ? 0.180719  0.279378 0.200937 0.0310634   -0.0160032  -0.00883979 389  GLU A OE1 
3162  O  OE2 . GLU A 389 ? 0.176027  0.273748 0.187791 0.0326677   -0.0141266  -0.00942668 389  GLU A OE2 
3163  N  N   . ALA A 390 ? 0.141064  0.228961 0.1727   0.0299432   -0.0167406  -0.00628809 390  ALA A N   
3164  C  CA  . ALA A 390 ? 0.166245  0.253016 0.199145 0.0315113   -0.0176409  -0.0065287  390  ALA A CA  
3165  C  C   . ALA A 390 ? 0.170955  0.256557 0.209789 0.0338676   -0.0203534  -0.0119049  390  ALA A C   
3166  O  O   . ALA A 390 ? 0.168671  0.254468 0.209378 0.0359297   -0.0209969  -0.0134256  390  ALA A O   
3167  C  CB  . ALA A 390 ? 0.148079  0.230723 0.182521 0.0299692   -0.0179478  -0.00111867 390  ALA A CB  
3168  N  N   . ILE A 391 ? 0.156028  0.240586 0.19885  0.0337486   -0.0222295  -0.0153232  391  ILE A N   
3169  C  CA  . ILE A 391 ? 0.165263  0.247481 0.214958 0.0358022   -0.025293   -0.0207784  391  ILE A CA  
3170  C  C   . ILE A 391 ? 0.166866  0.252991 0.212423 0.039281    -0.0245744  -0.0261159  391  ILE A C   
3171  O  O   . ILE A 391 ? 0.175201  0.260354 0.225321 0.0415309   -0.0254401  -0.0287058  391  ILE A O   
3172  C  CB  . ILE A 391 ? 0.188505  0.269712 0.243299 0.0350649   -0.0279691  -0.024811   391  ILE A CB  
3173  C  CG1 . ILE A 391 ? 0.182849  0.260982 0.243569 0.0312118   -0.0276588  -0.0197691  391  ILE A CG1 
3174  C  CG2 . ILE A 391 ? 0.183754  0.262247 0.245649 0.0374715   -0.0314009  -0.0316334  391  ILE A CG2 
3175  C  CD1 . ILE A 391 ? 0.20009   0.272457 0.265033 0.0297984   -0.0270827  -0.0140217  391  ILE A CD1 
3176  N  N   . GLY A 392 ? 0.152068  0.242415 0.189471 0.0400129   -0.0229882  -0.0282031  392  GLY A N   
3177  C  CA  . GLY A 392 ? 0.170993  0.264999 0.203519 0.043132    -0.0212236  -0.0330989  392  GLY A CA  
3178  C  C   . GLY A 392 ? 0.17243   0.269087 0.204157 0.0434786   -0.0178465  -0.0306782  392  GLY A C   
3179  O  O   . GLY A 392 ? 0.182657  0.28174  0.216116 0.0460641   -0.0165298  -0.0349256  392  GLY A O   
3180  N  N   . ASP A 393 ? 0.176269  0.272989 0.206092 0.0409291   -0.0163659  -0.0243609  393  ASP A N   
3181  C  CA  . ASP A 393 ? 0.187477  0.286912 0.217639 0.0408661   -0.014004   -0.0221927  393  ASP A CA  
3182  C  C   . ASP A 393 ? 0.184565  0.282148 0.224014 0.0424538   -0.0166806  -0.023123   393  ASP A C   
3183  O  O   . ASP A 393 ? 0.186437  0.287551 0.229065 0.0441199   -0.0154146  -0.0250623  393  ASP A O   
3184  C  CB  . ASP A 393 ? 0.234688  0.334081 0.260903 0.0380098   -0.0126641  -0.0162181  393  ASP A CB  
3185  C  CG  . ASP A 393 ? 0.303619  0.405104 0.321481 0.0368845   -0.00953452 -0.0149984  393  ASP A CG  
3186  O  OD1 . ASP A 393 ? 0.285541  0.387471 0.299085 0.0380834   -0.0092905  -0.0177989  393  ASP A OD1 
3187  O  OD2 . ASP A 393 ? 0.344876  0.447297 0.360293 0.0350655   -0.00762118 -0.0114272  393  ASP A OD2 
3188  N  N   . VAL A 394 ? 0.190673  0.28267  0.235242 0.0419449   -0.0202744  -0.0214547  394  VAL A N   
3189  C  CA  . VAL A 394 ? 0.222674  0.311776 0.275896 0.0439261   -0.0232824  -0.0217907  394  VAL A CA  
3190  C  C   . VAL A 394 ? 0.199986  0.291384 0.258305 0.0475425   -0.0232873  -0.0293129  394  VAL A C   
3191  O  O   . VAL A 394 ? 0.187106  0.28026  0.251615 0.0499551   -0.0238796  -0.0308177  394  VAL A O   
3192  C  CB  . VAL A 394 ? 0.249452  0.330764 0.307388 0.0426432   -0.0267496  -0.0182709  394  VAL A CB  
3193  C  CG1 . VAL A 394 ? 0.289708  0.366945 0.355876 0.0450718   -0.0302459  -0.0176296  394  VAL A CG1 
3194  C  CG2 . VAL A 394 ? 0.235067  0.314667 0.28724  0.0392057   -0.0257463  -0.0109718  394  VAL A CG2 
3195  N  N   . LEU A 395 ? 0.19772   0.288989 0.254246 0.0482663   -0.0231558  -0.0345279  395  LEU A N   
3196  C  CA  . LEU A 395 ? 0.213126  0.306833 0.273238 0.0520124   -0.0226592  -0.0424249  395  LEU A CA  
3197  C  C   . LEU A 395 ? 0.19145   0.292789 0.247342 0.0531071   -0.0175749  -0.0440041  395  LEU A C   
3198  O  O   . LEU A 395 ? 0.192656  0.297172 0.254875 0.0560856   -0.016454   -0.0484964  395  LEU A O   
3199  C  CB  . LEU A 395 ? 0.274078  0.36661  0.331174 0.0528421   -0.023774   -0.0484784  395  LEU A CB  
3200  C  CG  . LEU A 395 ? 0.324645  0.410216 0.390877 0.0531181   -0.02884    -0.0511055  395  LEU A CG  
3201  C  CD1 . LEU A 395 ? 0.313911  0.393859 0.383928 0.0495497   -0.0309937  -0.0431095  395  LEU A CD1 
3202  C  CD2 . LEU A 395 ? 0.371371  0.456912 0.433572 0.0535077   -0.030446   -0.0573309  395  LEU A CD2 
3203  N  N   . ALA A 396 ? 0.17844   0.282802 0.224594 0.0507135   -0.0141204  -0.0405035  396  ALA A N   
3204  C  CA  . ALA A 396 ? 0.191137  0.302144 0.233567 0.0511268   -0.00855203 -0.0415331  396  ALA A CA  
3205  C  C   . ALA A 396 ? 0.184459  0.29837  0.235971 0.0513107   -0.0083804  -0.0397845  396  ALA A C   
3206  O  O   . ALA A 396 ? 0.20044   0.320535 0.254425 0.0524122   -0.00406395 -0.0426121  396  ALA A O   
3207  C  CB  . ALA A 396 ? 0.165335  0.277705 0.196856 0.0483618   -0.00522111 -0.0371707  396  ALA A CB  
3208  N  N   . LEU A 397 ? 0.167507  0.27737  0.223694 0.0501982   -0.0128441  -0.0350576  397  LEU A N   
3209  C  CA  . LEU A 397 ? 0.156542  0.26901  0.221556 0.0511319   -0.0142457  -0.0339479  397  LEU A CA  
3210  C  C   . LEU A 397 ? 0.168789  0.283451 0.244726 0.0553607   -0.0150247  -0.0402682  397  LEU A C   
3211  O  O   . LEU A 397 ? 0.184121  0.304752 0.267928 0.0568271   -0.0137382  -0.0422525  397  LEU A O   
3212  C  CB  . LEU A 397 ? 0.174566  0.281285 0.240879 0.0498885   -0.0195603  -0.0276789  397  LEU A CB  
3213  C  CG  . LEU A 397 ? 0.180685  0.286246 0.237771 0.0459902   -0.0186437  -0.0216299  397  LEU A CG  
3214  C  CD1 . LEU A 397 ? 0.165515  0.264821 0.221889 0.0449404   -0.0233168  -0.0154772  397  LEU A CD1 
3215  C  CD2 . LEU A 397 ? 0.202262  0.314623 0.259142 0.0448616   -0.0153792  -0.021633   397  LEU A CD2 
3216  N  N   . SER A 398 ? 0.167374  0.277295 0.245582 0.0574888   -0.0174757  -0.0439576  398  SER A N   
3217  C  CA  . SER A 398 ? 0.150197  0.261635 0.239368 0.0619461   -0.0182982  -0.0507757  398  SER A CA  
3218  C  C   . SER A 398 ? 0.163608  0.282884 0.24975  0.0632429   -0.0114185  -0.0573003  398  SER A C   
3219  O  O   . SER A 398 ? 0.149481  0.274891 0.244481 0.0660255   -0.00892632 -0.0620397  398  SER A O   
3220  C  CB  . SER A 398 ? 0.161616  0.265123 0.253962 0.0636267   -0.0226695  -0.0535953  398  SER A CB  
3221  O  OG  . SER A 398 ? 0.172923  0.268959 0.271208 0.0634195   -0.0286252  -0.048091   398  SER A OG  
3222  N  N   . VAL A 399 ? 0.155505  0.274567 0.228866 0.0613616   -0.00823246 -0.0574426  399  VAL A N   
3223  C  CA  . VAL A 399 ? 0.176991  0.301934 0.244919 0.0629837   -0.00180978 -0.0634676  399  VAL A CA  
3224  C  C   . VAL A 399 ? 0.182208  0.315466 0.252802 0.0620437   0.00437317  -0.062379   399  VAL A C   
3225  O  O   . VAL A 399 ? 0.211053  0.350343 0.28354  0.0642869   0.0099372   -0.0681795  399  VAL A O   
3226  C  CB  . VAL A 399 ? 0.169933  0.29258  0.222246 0.061312    -0.00042075 -0.0627196  399  VAL A CB  
3227  C  CG1 . VAL A 399 ? 0.166156  0.294913 0.209188 0.0624199   0.00730243  -0.0666455  399  VAL A CG1 
3228  C  CG2 . VAL A 399 ? 0.165147  0.281227 0.217767 0.062845    -0.00615344 -0.0665312  399  VAL A CG2 
3229  N  N   . SER A 400 ? 0.192616  0.326293 0.262058 0.0583919   0.00417059  -0.0552467  400  SER A N   
3230  C  CA  . SER A 400 ? 0.216734  0.357919 0.288274 0.0565749   0.0102863   -0.0540695  400  SER A CA  
3231  C  C   . SER A 400 ? 0.192728  0.339756 0.281384 0.0588239   0.00951255  -0.0572732  400  SER A C   
3232  O  O   . SER A 400 ? 0.183048  0.337896 0.277724 0.0578924   0.0149319   -0.0582988  400  SER A O   
3233  C  CB  . SER A 400 ? 0.252225  0.391595 0.317769 0.0521067   0.00981348  -0.0464418  400  SER A CB  
3234  O  OG  . SER A 400 ? 0.259777  0.395663 0.331704 0.0516854   0.00282791  -0.0428392  400  SER A OG  
3235  N  N   . THR A 401 ? 0.168405  0.311722 0.266246 0.0618901   0.00267596  -0.0589128  401  THR A N   
3236  C  CA  . THR A 401 ? 0.154863  0.303994 0.269721 0.0646797   0.00125688  -0.0621194  401  THR A CA  
3237  C  C   . THR A 401 ? 0.162973  0.321245 0.284421 0.0670741   0.00908403  -0.0698628  401  THR A C   
3238  O  O   . THR A 401 ? 0.17424   0.332029 0.290847 0.0693612   0.0124513   -0.0753324  401  THR A O   
3239  C  CB  . THR A 401 ? 0.162027  0.304932 0.286215 0.0683201   -0.00751648 -0.0625344  401  THR A CB  
3240  O  OG1 . THR A 401 ? 0.15205   0.290392 0.274901 0.0713162   -0.00799866 -0.067806   401  THR A OG1 
3241  C  CG2 . THR A 401 ? 0.164361  0.298543 0.282468 0.0659244   -0.0145057  -0.0543585  401  THR A CG2 
3242  N  N   . PRO A 402 ? 0.170423  0.337693 0.306213 0.0675036   0.0112856   -0.0717425  402  PRO A N   
3243  C  CA  . PRO A 402 ? 0.166407  0.343131 0.31164  0.0702342   0.0189302   -0.0797165  402  PRO A CA  
3244  C  C   . PRO A 402 ? 0.183676  0.35823  0.334048 0.0759429   0.0170264   -0.0873128  402  PRO A C   
3245  O  O   . PRO A 402 ? 0.176539  0.354563 0.323335 0.0778464   0.0240911   -0.0937466  402  PRO A O   
3246  C  CB  . PRO A 402 ? 0.161514  0.347721 0.325125 0.0698564   0.0189958   -0.0801394  402  PRO A CB  
3247  C  CG  . PRO A 402 ? 0.160002  0.342433 0.317419 0.065224    0.0146874   -0.071851   402  PRO A CG  
3248  C  CD  . PRO A 402 ? 0.154882  0.324597 0.296809 0.0646713   0.00797713  -0.0665164  402  PRO A CD  
3249  N  N   . GLU A 403 ? 0.195516  0.36339  0.353487 0.078866    0.00733023  -0.0866526  403  GLU A N   
3250  C  CA  . GLU A 403 ? 0.231204  0.396584 0.395893 0.0843739   0.00553248  -0.0944053  403  GLU A CA  
3251  C  C   . GLU A 403 ? 0.202466  0.361297 0.350186 0.0838765   0.00757841  -0.0963851  403  GLU A C   
3252  O  O   . GLU A 403 ? 0.192009  0.352604 0.340447 0.0875523   0.0112618   -0.105064   403  GLU A O   
3253  C  CB  . GLU A 403 ? 0.329901  0.486358 0.502509 0.0865084   -0.00587314 -0.0906856  403  GLU A CB  
3254  C  CG  . GLU A 403 ? 0.50724   0.662763 0.695656 0.0931101   -0.00930913 -0.0985008  403  GLU A CG  
3255  C  CD  . GLU A 403 ? 0.660967  0.804373 0.854098 0.0952986   -0.0203614  -0.0943981  403  GLU A CD  
3256  O  OE1 . GLU A 403 ? 0.684175  0.818308 0.866213 0.0916748   -0.0251754  -0.0858724  403  GLU A OE1 
3257  O  OE2 . GLU A 403 ? 0.712153  0.855549 0.921304 0.101035    -0.0237189  -0.100177   403  GLU A OE2 
3258  N  N   . HIS A 404 ? 0.176075  0.327122 0.309404 0.0797604   0.00432563  -0.0889332  404  HIS A N   
3259  C  CA  . HIS A 404 ? 0.162901  0.308375 0.281475 0.0794461   0.00526796  -0.091172   404  HIS A CA  
3260  C  C   . HIS A 404 ? 0.162115  0.314629 0.269209 0.0788618   0.0153523   -0.0950357  404  HIS A C   
3261  O  O   . HIS A 404 ? 0.166892  0.31907  0.268049 0.0817179   0.0178615   -0.102406   404  HIS A O   
3262  C  CB  . HIS A 404 ? 0.155141  0.291919 0.262077 0.0752228   0.00015677  -0.082756   404  HIS A CB  
3263  C  CG  . HIS A 404 ? 0.166697  0.297896 0.262533 0.0757957   -0.00066135 -0.0865727  404  HIS A CG  
3264  N  ND1 . HIS A 404 ? 0.181815  0.305746 0.283915 0.078507    -0.00683964 -0.090705   404  HIS A ND1 
3265  C  CD2 . HIS A 404 ? 0.179835  0.31152  0.259644 0.074312    0.00328282  -0.087333   404  HIS A CD2 
3266  C  CE1 . HIS A 404 ? 0.198229  0.319258 0.289238 0.0786352   -0.00660445 -0.094925   404  HIS A CE1 
3267  N  NE2 . HIS A 404 ? 0.194182  0.320214 0.271139 0.076509    -0.00053166 -0.0931658  404  HIS A NE2 
3268  N  N   . LEU A 405 ? 0.156464  0.314816 0.259602 0.0751028   0.0211611   -0.0899334  405  LEU A N   
3269  C  CA  . LEU A 405 ? 0.165411  0.329987 0.257645 0.0742313   0.0315268   -0.092161   405  LEU A CA  
3270  C  C   . LEU A 405 ? 0.181759  0.353684 0.282613 0.0789422   0.037525    -0.102352   405  LEU A C   
3271  O  O   . LEU A 405 ? 0.179677  0.353575 0.268771 0.0804124   0.04416     -0.107315   405  LEU A O   
3272  C  CB  . LEU A 405 ? 0.16872   0.338711 0.261159 0.0695344   0.0368129   -0.0854081  405  LEU A CB  
3273  C  CG  . LEU A 405 ? 0.166364  0.32963  0.249529 0.0649272   0.0319843   -0.0758536  405  LEU A CG  
3274  C  CD1 . LEU A 405 ? 0.16812   0.336809 0.255669 0.060711    0.0363037   -0.0705485  405  LEU A CD1 
3275  C  CD2 . LEU A 405 ? 0.179394  0.337142 0.241618 0.0639194   0.0335524   -0.0741958  405  LEU A CD2 
3276  N  N   . HIS A 406 ? 0.188883  0.365333 0.310387 0.0816124   0.0353779   -0.105679   406  HIS A N   
3277  C  CA  . HIS A 406 ? 0.212883  0.396425 0.344567 0.0867145   0.0408004   -0.116315   406  HIS A CA  
3278  C  C   . HIS A 406 ? 0.232538  0.409475 0.356995 0.0909447   0.0377629   -0.123836   406  HIS A C   
3279  O  O   . HIS A 406 ? 0.218581  0.400299 0.338812 0.0940584   0.0451377   -0.132341   406  HIS A O   
3280  C  CB  . HIS A 406 ? 0.224893  0.414093 0.38168  0.0894769   0.0375858   -0.118775   406  HIS A CB  
3281  C  CG  . HIS A 406 ? 0.255243  0.452182 0.424754 0.0950813   0.0430629   -0.130138   406  HIS A CG  
3282  N  ND1 . HIS A 406 ? 0.280554  0.489274 0.451961 0.0946951   0.0554858   -0.134224   406  HIS A ND1 
3283  C  CD2 . HIS A 406 ? 0.287361  0.482153 0.468651 0.101151    0.0386237   -0.138449   406  HIS A CD2 
3284  C  CE1 . HIS A 406 ? 0.311088  0.525518 0.495539 0.100586    0.0586689   -0.145158   406  HIS A CE1 
3285  N  NE2 . HIS A 406 ? 0.300582  0.506314 0.490914 0.104744    0.0482252   -0.148109   406  HIS A NE2 
3286  N  N   . LYS A 407 ? 0.233538  0.399666 0.357744 0.0911728   0.0270564   -0.121283   407  LYS A N   
3287  C  CA  . LYS A 407 ? 0.255104  0.414724 0.376151 0.0951585   0.0232328   -0.129305   407  LYS A CA  
3288  C  C   . LYS A 407 ? 0.256542  0.414837 0.354661 0.0939862   0.0276181   -0.131043   407  LYS A C   
3289  O  O   . LYS A 407 ? 0.275821  0.432862 0.369036 0.0978262   0.0282996   -0.140427   407  LYS A O   
3290  C  CB  . LYS A 407 ? 0.300225  0.447687 0.424324 0.094833    0.011612    -0.125907   407  LYS A CB  
3291  C  CG  . LYS A 407 ? 0.363844  0.508535 0.508407 0.0969441   0.004512    -0.124168   407  LYS A CG  
3292  C  CD  . LYS A 407 ? 0.403567  0.536426 0.547058 0.0942222   -0.00524617 -0.115942   407  LYS A CD  
3293  C  CE  . LYS A 407 ? 0.44385   0.573782 0.605097 0.0962599   -0.0119929  -0.112545   407  LYS A CE  
3294  N  NZ  . LYS A 407 ? 0.405604  0.525606 0.563218 0.0926045   -0.019386   -0.102333   407  LYS A NZ  
3295  N  N   . ILE A 408 ? 0.241128  0.399238 0.324557 0.0890393   0.0300501   -0.122374   408  ILE A N   
3296  C  CA  . ILE A 408 ? 0.25284   0.409098 0.314047 0.0885531   0.0331385   -0.123682   408  ILE A CA  
3297  C  C   . ILE A 408 ? 0.258268  0.423513 0.309277 0.0884674   0.0456741   -0.125134   408  ILE A C   
3298  O  O   . ILE A 408 ? 0.271791  0.435794 0.302526 0.0869557   0.0491422   -0.122539   408  ILE A O   
3299  C  CB  . ILE A 408 ? 0.253928  0.402582 0.303793 0.0841088   0.0269882   -0.114398   408  ILE A CB  
3300  C  CG1 . ILE A 408 ? 0.235635  0.387066 0.285834 0.0790631   0.0299365   -0.103579   408  ILE A CG1 
3301  C  CG2 . ILE A 408 ? 0.24176   0.381782 0.302253 0.0847168   0.0159984   -0.114716   408  ILE A CG2 
3302  C  CD1 . ILE A 408 ? 0.236396  0.381548 0.273753 0.0748878   0.0258214   -0.0948316  408  ILE A CD1 
3303  N  N   . GLY A 409 ? 0.242165  0.416439 0.307529 0.0897783   0.0525996   -0.128319   409  GLY A N   
3304  C  CA  . GLY A 409 ? 0.266634  0.449845 0.324263 0.0899126   0.0657046   -0.130782   409  GLY A CA  
3305  C  C   . GLY A 409 ? 0.260903  0.447106 0.31187  0.0840746   0.0721497   -0.120212   409  GLY A C   
3306  O  O   . GLY A 409 ? 0.287136  0.478743 0.327436 0.0834281   0.0832833   -0.120533   409  GLY A O   
3307  N  N   . LEU A 410 ? 0.238297  0.421238 0.296401 0.0799705   0.065895    -0.111307   410  LEU A N   
3308  C  CA  . LEU A 410 ? 0.238485  0.422587 0.290337 0.0742618   0.070625    -0.101316   410  LEU A CA  
3309  C  C   . LEU A 410 ? 0.241176  0.43382  0.314021 0.0718455   0.0744141   -0.099274   410  LEU A C   
3310  O  O   . LEU A 410 ? 0.23836   0.433059 0.309614 0.0669822   0.0791856   -0.0920809  410  LEU A O   
3311  C  CB  . LEU A 410 ? 0.221763  0.396242 0.263252 0.0710022   0.0620218   -0.0927734  410  LEU A CB  
3312  C  CG  . LEU A 410 ? 0.228992  0.396351 0.247515 0.0721578   0.0600057   -0.0929928  410  LEU A CG  
3313  C  CD1 . LEU A 410 ? 0.208111  0.366934 0.219792 0.0690778   0.0513456   -0.0850092  410  LEU A CD1 
3314  C  CD2 . LEU A 410 ? 0.245388  0.41556  0.245127 0.0721415   0.0707432   -0.092899   410  LEU A CD2 
3315  N  N   . LEU A 411 ? 0.238387  0.436504 0.331888 0.0754429   0.0726254   -0.106232   411  LEU A N   
3316  C  CA  . LEU A 411 ? 0.237669  0.443932 0.351996 0.0733474   0.0743904   -0.104464   411  LEU A CA  
3317  C  C   . LEU A 411 ? 0.270037  0.48431  0.403777 0.0787445   0.0761974   -0.114772   411  LEU A C   
3318  O  O   . LEU A 411 ? 0.284302  0.494709 0.4278   0.0828484   0.0669236   -0.118653   411  LEU A O   
3319  C  CB  . LEU A 411 ? 0.251869  0.452237 0.372956 0.0708857   0.062884    -0.0972965  411  LEU A CB  
3320  C  CG  . LEU A 411 ? 0.267502  0.475444 0.407407 0.0679369   0.0633433   -0.0943548  411  LEU A CG  
3321  C  CD1 . LEU A 411 ? 0.274574  0.486849 0.40734  0.0623123   0.0740469   -0.0893326  411  LEU A CD1 
3322  C  CD2 . LEU A 411 ? 0.257619  0.457771 0.399179 0.066376    0.0509818   -0.0877764  411  LEU A CD2 
3323  N  N   . ASP A 412 ? 0.301223  0.526554 0.441325 0.0786254   0.0884839   -0.118898   412  ASP A N   
3324  C  CA  . ASP A 412 ? 0.397084  0.631054 0.554624 0.0843048   0.0921332   -0.130041   412  ASP A CA  
3325  C  C   . ASP A 412 ? 0.376589  0.617117 0.563153 0.085492    0.0864186   -0.131441   412  ASP A C   
3326  O  O   . ASP A 412 ? 0.39401   0.636022 0.595865 0.0913036   0.0815839   -0.139101   412  ASP A O   
3327  C  CB  . ASP A 412 ? 0.480797  0.72409  0.632975 0.0846282   0.108076    -0.135309   412  ASP A CB  
3328  C  CG  . ASP A 412 ? 0.667103  0.905417 0.799704 0.089189    0.11013     -0.14224    412  ASP A CG  
3329  O  OD1 . ASP A 412 ? 0.67622   0.902651 0.790886 0.0891447   0.101514    -0.138874   412  ASP A OD1 
3330  O  OD2 . ASP A 412 ? 0.793791  1.04043  0.930132 0.0929581   0.119986    -0.151626   412  ASP A OD2 
3331  N  N   . ARG A 413 ? 0.400044  0.644068 0.594391 0.0802675   0.0862464   -0.124269   413  ARG A N   
3332  C  CA  . ARG A 413 ? 0.399483  0.650729 0.621647 0.0817082   0.0803842   -0.126183   413  ARG A CA  
3333  C  C   . ARG A 413 ? 0.396144  0.636111 0.617543 0.0826786   0.0642931   -0.120997   413  ARG A C   
3334  O  O   . ARG A 413 ? 0.296954  0.527882 0.501599 0.078504    0.0601824   -0.112574   413  ARG A O   
3335  C  CB  . ARG A 413 ? 0.385331  0.646139 0.616581 0.0755718   0.0881698   -0.121982   413  ARG A CB  
3336  C  CG  . ARG A 413 ? 0.363061  0.638643 0.62497  0.0760897   0.091036    -0.127005   413  ARG A CG  
3337  C  CD  . ARG A 413 ? 0.330464  0.609787 0.59457  0.0683693   0.0951429   -0.119778   413  ARG A CD  
3338  N  NE  . ARG A 413 ? 0.368147  0.653229 0.657205 0.0686004   0.0854326   -0.120174   413  ARG A NE  
3339  C  CZ  . ARG A 413 ? 0.359853  0.649471 0.659401 0.0630026   0.0845231   -0.115819   413  ARG A CZ  
3340  N  NH1 . ARG A 413 ? 0.339689  0.634551 0.66175  0.0647405   0.0740294   -0.117731   413  ARG A NH1 
3341  N  NH2 . ARG A 413 ? 0.331288  0.620179 0.619485 0.0559958   0.09387     -0.110002   413  ARG A NH2 
3342  N  N   . VAL A 414 ? 0.374051  0.614501 0.613714 0.0883242   0.0556243   -0.125913   414  VAL A N   
3343  C  CA  . VAL A 414 ? 0.40528   0.636041 0.646948 0.0893425   0.0408513   -0.120525   414  VAL A CA  
3344  C  C   . VAL A 414 ? 0.356038  0.595266 0.620085 0.0889236   0.0362454   -0.119394   414  VAL A C   
3345  O  O   . VAL A 414 ? 0.40063   0.652169 0.685905 0.0916255   0.0407917   -0.126544   414  VAL A O   
3346  C  CB  . VAL A 414 ? 0.505359  0.731092 0.753811 0.0967251   0.0348875   -0.127632   414  VAL A CB  
3347  C  CG1 . VAL A 414 ? 0.513748  0.725517 0.757378 0.0977921   0.0208047   -0.12149    414  VAL A CG1 
3348  C  CG2 . VAL A 414 ? 0.465778  0.690313 0.701575 0.0989462   0.0432101   -0.134734   414  VAL A CG2 
3349  N  N   . THR A 415 ? 0.269943  0.50357  0.530307 0.0857013   0.0273938   -0.111126   415  THR A N   
3350  C  CA  . THR A 415 ? 0.289702  0.530672 0.57094  0.0861275   0.0208912   -0.110776   415  THR A CA  
3351  C  C   . THR A 415 ? 0.279262  0.508036 0.553755 0.0870797   0.00637144  -0.103671   415  THR A C   
3352  O  O   . THR A 415 ? 0.314228  0.531383 0.567174 0.0845055   0.00467719  -0.0975828  415  THR A O   
3353  C  CB  . THR A 415 ? 0.296578  0.546525 0.581049 0.0794428   0.0277175   -0.108015   415  THR A CB  
3354  O  OG1 . THR A 415 ? 0.313621  0.553519 0.573661 0.073906    0.0281586   -0.0996097  415  THR A OG1 
3355  C  CG2 . THR A 415 ? 0.276268  0.539389 0.570144 0.0779577   0.0428442   -0.114302   415  THR A CG2 
3356  N  N   . ASN A 416 ? 0.226801  0.458027 0.519149 0.0910382   -0.00388267 -0.104487   416  ASN A N   
3357  C  CA  . ASN A 416 ? 0.229181  0.449161 0.513181 0.0912779   -0.0168865  -0.0966292  416  ASN A CA  
3358  C  C   . ASN A 416 ? 0.206528  0.434444 0.506592 0.0911903   -0.0240105  -0.095948   416  ASN A C   
3359  O  O   . ASN A 416 ? 0.236648  0.467564 0.554586 0.0970567   -0.0321545  -0.0992265  416  ASN A O   
3360  C  CB  . ASN A 416 ? 0.242622  0.451788 0.526502 0.0975934   -0.0252638  -0.0969459  416  ASN A CB  
3361  C  CG  . ASN A 416 ? 0.260692  0.456596 0.53238  0.0973281   -0.03714    -0.0876528  416  ASN A CG  
3362  O  OD1 . ASN A 416 ? 0.232394  0.424717 0.489041 0.091863    -0.0375107  -0.080774   416  ASN A OD1 
3363  N  ND2 . ASN A 416 ? 0.288743  0.476532 0.565953 0.103181    -0.0464858  -0.0871154  416  ASN A ND2 
3364  N  N   . ASP A 417 ? 0.181413  0.413485 0.476855 0.0848169   -0.0208136  -0.0926098  417  ASP A N   
3365  C  CA  . ASP A 417 ? 0.175173  0.415666 0.486459 0.0842558   -0.027345   -0.0930952  417  ASP A CA  
3366  C  C   . ASP A 417 ? 0.150381  0.385127 0.444539 0.0779612   -0.0295415  -0.085592   417  ASP A C   
3367  O  O   . ASP A 417 ? 0.132462  0.358966 0.405388 0.0739006   -0.0238897  -0.0808741  417  ASP A O   
3368  C  CB  . ASP A 417 ? 0.195168  0.452685 0.528591 0.0826819   -0.0176814  -0.100758   417  ASP A CB  
3369  C  CG  . ASP A 417 ? 0.247768  0.507462 0.570032 0.0767409   -0.00186491 -0.100808   417  ASP A CG  
3370  O  OD1 . ASP A 417 ? 0.205114  0.462768 0.515867 0.0702268   0.00110487  -0.0957333  417  ASP A OD1 
3371  O  OD2 . ASP A 417 ? 0.319777  0.582679 0.644287 0.0789825   0.0072001   -0.105965   417  ASP A OD2 
3372  N  N   . THR A 418 ? 0.134231  0.374062 0.438633 0.0773122   -0.0376186  -0.0853051  418  THR A N   
3373  C  CA  . THR A 418 ? 0.1373    0.370153 0.424667 0.0724455   -0.0416673  -0.0785657  418  THR A CA  
3374  C  C   . THR A 418 ? 0.135667  0.371215 0.415404 0.0648194   -0.0290604  -0.0777309  418  THR A C   
3375  O  O   . THR A 418 ? 0.109502  0.335465 0.368173 0.0609584   -0.0285489  -0.071508   418  THR A O   
3376  C  CB  . THR A 418 ? 0.157397  0.393267 0.453786 0.0737709   -0.054528   -0.0783535  418  THR A CB  
3377  O  OG1 . THR A 418 ? 0.159365  0.411242 0.481678 0.0728699   -0.0500738  -0.0860256  418  THR A OG1 
3378  C  CG2 . THR A 418 ? 0.159238  0.391304 0.461934 0.0818478   -0.067497   -0.0782437  418  THR A CG2 
3379  N  N   . GLU A 419 ? 0.121563  0.369536 0.418016 0.0627818   -0.0187174  -0.0836027  419  GLU A N   
3380  C  CA  . GLU A 419 ? 0.130634  0.379301 0.418293 0.0553765   -0.00754898 -0.0813484  419  GLU A CA  
3381  C  C   . GLU A 419 ? 0.117646  0.356387 0.382055 0.0543138   0.00038911  -0.0773471  419  GLU A C   
3382  O  O   . GLU A 419 ? 0.111706  0.344034 0.359308 0.049271    0.00412711  -0.0721076  419  GLU A O   
3383  C  CB  . GLU A 419 ? 0.15832   0.421795 0.467608 0.0525266   0.00334107  -0.0874698  419  GLU A CB  
3384  C  CG  . GLU A 419 ? 0.206357  0.481054 0.540688 0.0523116   -0.0038803  -0.0919398  419  GLU A CG  
3385  C  CD  . GLU A 419 ? 0.273232  0.554903 0.628173 0.0600212   -0.0125504  -0.0979084  419  GLU A CD  
3386  O  OE1 . GLU A 419 ? 0.244166  0.522555 0.597212 0.0661633   -0.0134451  -0.0993835  419  GLU A OE1 
3387  O  OE2 . GLU A 419 ? 0.452492  0.744131 0.828779 0.0598596   -0.0189348  -0.101949   419  GLU A OE2 
3388  N  N   . SER A 420 ? 0.113542  0.351779 0.378349 0.0590511   0.00334254  -0.0805757  420  SER A N   
3389  C  CA  . SER A 420 ? 0.1293    0.358289 0.372362 0.0584645   0.00960156  -0.0776112  420  SER A CA  
3390  C  C   . SER A 420 ? 0.127768  0.342927 0.350564 0.0580973   0.00123563  -0.0704512  420  SER A C   
3391  O  O   . SER A 420 ? 0.112648  0.320342 0.31604  0.0550282   0.00604123  -0.0662043  420  SER A O   
3392  C  CB  . SER A 420 ? 0.145026  0.374765 0.392137 0.0642517   0.0118962   -0.0830667  420  SER A CB  
3393  O  OG  . SER A 420 ? 0.15162   0.395076 0.417935 0.0646653   0.0208292   -0.0901533  420  SER A OG  
3394  N  N   . ASP A 421 ? 0.124421  0.336154 0.351439 0.0613645   -0.0111041  -0.0689723  421  ASP A N   
3395  C  CA  . ASP A 421 ? 0.151644  0.350311 0.359379 0.060919    -0.0183032  -0.0618896  421  ASP A CA  
3396  C  C   . ASP A 421 ? 0.131974  0.328346 0.32848  0.0548674   -0.0172418  -0.057016   421  ASP A C   
3397  O  O   . ASP A 421 ? 0.129385  0.316299 0.30682  0.052578    -0.016444   -0.0517211  421  ASP A O   
3398  C  CB  . ASP A 421 ? 0.221407  0.416054 0.433862 0.0655315   -0.0314433  -0.0603049  421  ASP A CB  
3399  C  CG  . ASP A 421 ? 0.351952  0.537379 0.560098 0.0707197   -0.0364832  -0.0591699  421  ASP A CG  
3400  O  OD1 . ASP A 421 ? 0.382381  0.562712 0.580641 0.0704308   -0.0304395  -0.0592754  421  ASP A OD1 
3401  O  OD2 . ASP A 421 ? 0.43705   0.619702 0.651337 0.0750688   -0.04711    -0.057932   421  ASP A OD2 
3402  N  N   . ILE A 422 ? 0.123857  0.328807 0.333401 0.0524745   -0.0179491  -0.0591927  422  ILE A N   
3403  C  CA  . ILE A 422 ? 0.102492  0.305531 0.303252 0.0466234   -0.0162577  -0.0556365  422  ILE A CA  
3404  C  C   . ILE A 422 ? 0.0971323 0.298097 0.28636  0.0423444   -0.00408752 -0.0537815  422  ILE A C   
3405  O  O   . ILE A 422 ? 0.0985028 0.291476 0.271    0.0391486   -0.00343413 -0.0486853  422  ILE A O   
3406  C  CB  . ILE A 422 ? 0.109865  0.323069 0.329093 0.0445863   -0.0187704  -0.0594497  422  ILE A CB  
3407  C  CG1 . ILE A 422 ? 0.11964   0.333352 0.346386 0.0488862   -0.0330624  -0.0603343  422  ILE A CG1 
3408  C  CG2 . ILE A 422 ? 0.0989117 0.311078 0.311822 0.0378649   -0.0139403  -0.0570776  422  ILE A CG2 
3409  C  CD1 . ILE A 422 ? 0.149102  0.349959 0.354529 0.0499985   -0.0409483  -0.0538415  422  ILE A CD1 
3410  N  N   . ASN A 423 ? 0.100466  0.30874  0.298536 0.0424146   0.00545872  -0.0578939  423  ASN A N   
3411  C  CA  . ASN A 423 ? 0.0984389 0.30449  0.284283 0.0388946   0.0168207   -0.0558199  423  ASN A CA  
3412  C  C   . ASN A 423 ? 0.0953076 0.289578 0.259473 0.0403168   0.0149247   -0.0514212  423  ASN A C   
3413  O  O   . ASN A 423 ? 0.0854315 0.273239 0.234181 0.0368859   0.0179936   -0.0466926  423  ASN A O   
3414  C  CB  . ASN A 423 ? 0.100387  0.315084 0.295925 0.0399236   0.027276    -0.0609539  423  ASN A CB  
3415  C  CG  . ASN A 423 ? 0.108753  0.335195 0.323531 0.0363115   0.0339878   -0.0642693  423  ASN A CG  
3416  O  OD1 . ASN A 423 ? 0.112143  0.340044 0.333055 0.0323534   0.0310885   -0.0627814  423  ASN A OD1 
3417  N  ND2 . ASN A 423 ? 0.111455  0.346412 0.336273 0.0375097   0.0432489   -0.0691421  423  ASN A ND2 
3418  N  N   . TYR A 424 ? 0.101333  0.29272  0.265444 0.0454871   0.00978265  -0.0532023  424  TYR A N   
3419  C  CA  . TYR A 424 ? 0.113563  0.294402 0.259432 0.0465948   0.00827477  -0.0497373  424  TYR A CA  
3420  C  C   . TYR A 424 ? 0.114593  0.287079 0.248611 0.0443272   0.00174553  -0.0435194  424  TYR A C   
3421  O  O   . TYR A 424 ? 0.088024  0.253905 0.206449 0.042025    0.00431699  -0.0395891  424  TYR A O   
3422  C  CB  . TYR A 424 ? 0.123317  0.302276 0.273902 0.0523683   0.00359134  -0.0531648  424  TYR A CB  
3423  C  CG  . TYR A 424 ? 0.128679  0.296866 0.263008 0.0532301   0.00123568  -0.0500099  424  TYR A CG  
3424  C  CD1 . TYR A 424 ? 0.137283  0.303235 0.259262 0.0521816   0.00829401  -0.0503972  424  TYR A CD1 
3425  C  CD2 . TYR A 424 ? 0.134998  0.295153 0.266208 0.0550078   -0.0080886  -0.0464837  424  TYR A CD2 
3426  C  CE1 . TYR A 424 ? 0.15149   0.308252 0.26026  0.0527613   0.00548731  -0.0480115  424  TYR A CE1 
3427  C  CE2 . TYR A 424 ? 0.146108  0.29683  0.264083 0.055043    -0.00970038 -0.0435109  424  TYR A CE2 
3428  C  CZ  . TYR A 424 ? 0.166744  0.316274 0.275046 0.0541819   -0.00325079 -0.0450067  424  TYR A CZ  
3429  O  OH  . TYR A 424 ? 0.190533  0.331702 0.287297 0.0541457   -0.0049581  -0.0429762  424  TYR A OH  
3430  N  N   . LEU A 425 ? 0.116736  0.289606 0.25788  0.0453178   -0.00692873 -0.0428221  425  LEU A N   
3431  C  CA  . LEU A 425 ? 0.12061   0.285295 0.248913 0.0435453   -0.0127276  -0.0371647  425  LEU A CA  
3432  C  C   . LEU A 425 ? 0.128352  0.292872 0.249785 0.0381797   -0.00801026 -0.0347215  425  LEU A C   
3433  O  O   . LEU A 425 ? 0.113051  0.270148 0.220064 0.0361578   -0.00853606 -0.0302352  425  LEU A O   
3434  C  CB  . LEU A 425 ? 0.116601  0.281262 0.251748 0.0461973   -0.0231904  -0.0368568  425  LEU A CB  
3435  C  CG  . LEU A 425 ? 0.134118  0.294117 0.270871 0.0514499   -0.0296914  -0.0365659  425  LEU A CG  
3436  C  CD1 . LEU A 425 ? 0.138416  0.299744 0.283178 0.0542542   -0.0399199  -0.0363972  425  LEU A CD1 
3437  C  CD2 . LEU A 425 ? 0.14525   0.294076 0.265055 0.0510867   -0.0302197  -0.0313712  425  LEU A CD2 
3438  N  N   . LEU A 426 ? 0.129185  0.301968 0.261957 0.0356989   -0.00257973 -0.0378258  426  LEU A N   
3439  C  CA  . LEU A 426 ? 0.127106  0.299003 0.254761 0.0305513   0.0024081   -0.0355412  426  LEU A CA  
3440  C  C   . LEU A 426 ? 0.129385  0.295887 0.242478 0.0293206   0.00989509  -0.0325734  426  LEU A C   
3441  O  O   . LEU A 426 ? 0.122563  0.282542 0.223221 0.0268036   0.0105842   -0.0284565  426  LEU A O   
3442  C  CB  . LEU A 426 ? 0.148014  0.330234 0.293661 0.0281785   0.00694848  -0.039728   426  LEU A CB  
3443  C  CG  . LEU A 426 ? 0.21111   0.392951 0.356143 0.0225178   0.0112766   -0.0379882  426  LEU A CG  
3444  C  CD1 . LEU A 426 ? 0.218292  0.397351 0.353537 0.0203657   0.0220584   -0.0352791  426  LEU A CD1 
3445  C  CD2 . LEU A 426 ? 0.192349  0.366361 0.325945 0.0212089   0.00442991  -0.0346076  426  LEU A CD2 
3446  N  N   . LYS A 427 ? 0.127259  0.296384 0.241509 0.0315384   0.015139    -0.0350057  427  LYS A N   
3447  C  CA  . LYS A 427 ? 0.134002  0.297958 0.233238 0.0309247   0.0212087   -0.0324939  427  LYS A CA  
3448  C  C   . LYS A 427 ? 0.130931  0.285443 0.215902 0.0320959   0.0153287   -0.0287537  427  LYS A C   
3449  O  O   . LYS A 427 ? 0.125849  0.274885 0.198391 0.0300483   0.0176499   -0.0250004  427  LYS A O   
3450  C  CB  . LYS A 427 ? 0.152983  0.320782 0.253859 0.0338291   0.0268301   -0.0364699  427  LYS A CB  
3451  C  CG  . LYS A 427 ? 0.179658  0.341479 0.262586 0.0336135   0.0319102   -0.0338929  427  LYS A CG  
3452  C  CD  . LYS A 427 ? 0.217592  0.38506  0.30213  0.0352052   0.0403829   -0.038031   427  LYS A CD  
3453  C  CE  . LYS A 427 ? 0.283064  0.445467 0.34935  0.0357369   0.0452455   -0.0363132  427  LYS A CE  
3454  N  NZ  . LYS A 427 ? 0.339504  0.495184 0.39787  0.0386978   0.0374309   -0.0364159  427  LYS A NZ  
3455  N  N   . MET A 428 ? 0.11903   0.271535 0.206302 0.0354903   0.00817707  -0.0296995  428  MET A N   
3456  C  CA  . MET A 428 ? 0.141017  0.284976 0.216963 0.0360645   0.00279415  -0.0259033  428  MET A CA  
3457  C  C   . MET A 428 ? 0.13172   0.271837 0.201481 0.0329923   7.768e-05   -0.0216982  428  MET A C   
3458  O  O   . MET A 428 ? 0.118302  0.252127 0.176513 0.0319862   -0.00025866 -0.0182139  428  MET A O   
3459  C  CB  . MET A 428 ? 0.14995   0.291955 0.230901 0.0399193   -0.00419168 -0.0270253  428  MET A CB  
3460  C  CG  . MET A 428 ? 0.198257  0.342071 0.283622 0.0433761   -0.00208863 -0.0315125  428  MET A CG  
3461  S  SD  . MET A 428 ? 0.273082  0.413515 0.345506 0.0432409   0.0038379   -0.0320963  428  MET A SD  
3462  C  CE  . MET A 428 ? 0.204125  0.334691 0.265877 0.042367    -0.0022208  -0.0267724  428  MET A CE  
3463  N  N   . ALA A 429 ? 0.110846  0.254836 0.188769 0.0316991   -0.00245493 -0.0225054  429  ALA A N   
3464  C  CA  . ALA A 429 ? 0.114969  0.25587  0.187264 0.028757    -0.00429972 -0.0197547  429  ALA A CA  
3465  C  C   . ALA A 429 ? 0.121443  0.260515 0.187046 0.0254014   0.00263578  -0.017933   429  ALA A C   
3466  O  O   . ALA A 429 ? 0.114542  0.247907 0.170287 0.024058    0.00178173  -0.0148285  429  ALA A O   
3467  C  CB  . ALA A 429 ? 0.110671  0.256839 0.193927 0.0279383   -0.00814516 -0.02219    429  ALA A CB  
3468  N  N   . LEU A 430 ? 0.111107  0.254477 0.181397 0.0242872   0.00967996  -0.0195261  430  LEU A N   
3469  C  CA  . LEU A 430 ? 0.133051  0.273109 0.195588 0.0213214   0.0158202   -0.0166764  430  LEU A CA  
3470  C  C   . LEU A 430 ? 0.146795  0.279912 0.194823 0.0227508   0.0157406   -0.0135745  430  LEU A C   
3471  O  O   . LEU A 430 ? 0.140356  0.26863  0.180084 0.0210249   0.0176821   -0.0104199  430  LEU A O   
3472  C  CB  . LEU A 430 ? 0.116643  0.261683 0.184653 0.0199624   0.0242538   -0.0179996  430  LEU A CB  
3473  C  CG  . LEU A 430 ? 0.116469  0.269125 0.201053 0.0175969   0.0257124   -0.0211292  430  LEU A CG  
3474  C  CD1 . LEU A 430 ? 0.113828  0.272235 0.20414  0.016672    0.0354403   -0.0225771  430  LEU A CD1 
3475  C  CD2 . LEU A 430 ? 0.108665  0.258884 0.194878 0.0135302   0.0250128   -0.0195541  430  LEU A CD2 
3476  N  N   . GLU A 431 ? 0.171459  0.304247 0.21772  0.0260653   0.0133992   -0.0148906  431  GLU A N   
3477  C  CA  . GLU A 431 ? 0.198412  0.325671 0.233416 0.0275348   0.0127022   -0.0130056  431  GLU A CA  
3478  C  C   . GLU A 431 ? 0.197905  0.320318 0.228981 0.027578    0.00678306  -0.010665   431  GLU A C   
3479  O  O   . GLU A 431 ? 0.21454   0.332367 0.237266 0.0270779   0.00673262  -0.00811525 431  GLU A O   
3480  C  CB  . GLU A 431 ? 0.214479  0.343728 0.250878 0.0308009   0.0131545   -0.0163695  431  GLU A CB  
3481  C  CG  . GLU A 431 ? 0.339184  0.463196 0.365726 0.032439    0.0113806   -0.0154761  431  GLU A CG  
3482  C  CD  . GLU A 431 ? 0.426032  0.551606 0.453776 0.0357323   0.0116356   -0.019803   431  GLU A CD  
3483  O  OE1 . GLU A 431 ? 0.430578  0.552196 0.452607 0.0371851   0.00898453  -0.0200833  431  GLU A OE1 
3484  O  OE2 . GLU A 431 ? 0.452708  0.583703 0.487867 0.0368295   0.0145614   -0.0233706  431  GLU A OE2 
3485  N  N   . LYS A 432 ? 0.152303  0.275708 0.189275 0.0284589   0.00177201  -0.0114411  432  LYS A N   
3486  C  CA  . LYS A 432 ? 0.140921  0.259408 0.173095 0.0289696   -0.00314856 -0.00896069 432  LYS A CA  
3487  C  C   . LYS A 432 ? 0.151627  0.268959 0.182019 0.0269694   -0.0053774  -0.00724076 432  LYS A C   
3488  O  O   . LYS A 432 ? 0.179487  0.292397 0.202349 0.0261632   -0.00610732 -0.00461075 432  LYS A O   
3489  C  CB  . LYS A 432 ? 0.147327  0.265466 0.184463 0.0316929   -0.00800879 -0.00982541 432  LYS A CB  
3490  C  CG  . LYS A 432 ? 0.185475  0.304413 0.225069 0.0341002   -0.00636247 -0.0126616  432  LYS A CG  
3491  C  CD  . LYS A 432 ? 0.194653  0.308698 0.22606  0.0339837   -0.00575677 -0.0111261  432  LYS A CD  
3492  C  CE  . LYS A 432 ? 0.229901  0.344579 0.262984 0.0364923   -0.00473562 -0.0149027  432  LYS A CE  
3493  N  NZ  . LYS A 432 ? 0.203788  0.314342 0.230635 0.0366237   -0.00523668 -0.0144418  432  LYS A NZ  
3494  N  N   A ILE A 433 ? 0.125088  0.246671 0.16295  0.0263846   -0.00684837 -0.00925951 433  ILE A N   
3495  N  N   B ILE A 433 ? 0.128405  0.250031 0.166278 0.0263481   -0.00670063 -0.00927948 433  ILE A N   
3496  C  CA  A ILE A 433 ? 0.112253  0.23282  0.148116 0.024795    -0.00981861 -0.0086655  433  ILE A CA  
3497  C  CA  B ILE A 433 ? 0.115384  0.23623  0.151709 0.0247429   -0.00964521 -0.00881633 433  ILE A CA  
3498  C  C   A ILE A 433 ? 0.114415  0.233639 0.146889 0.0218199   -0.0053924  -0.00818888 433  ILE A C   
3499  C  C   B ILE A 433 ? 0.115893  0.235062 0.148258 0.0218282   -0.0053064  -0.0081492  433  ILE A C   
3500  O  O   A ILE A 433 ? 0.114534  0.230073 0.140366 0.0208314   -0.00655391 -0.00684704 433  ILE A O   
3501  O  O   B ILE A 433 ? 0.116499  0.231958 0.142173 0.0208944   -0.00653651 -0.00677352 433  ILE A O   
3502  C  CB  A ILE A 433 ? 0.102819  0.228506 0.148537 0.0254178   -0.014197   -0.0116033  433  ILE A CB  
3503  C  CB  B ILE A 433 ? 0.105305  0.231918 0.152502 0.0250048   -0.0129737  -0.0120894  433  ILE A CB  
3504  C  CG1 A ILE A 433 ? 0.0973915 0.222974 0.145883 0.0290135   -0.0195945  -0.0114005  433  ILE A CG1 
3505  C  CG1 B ILE A 433 ? 0.100938  0.227996 0.151503 0.0284801   -0.0185894  -0.012235   433  ILE A CG1 
3506  C  CG2 A ILE A 433 ? 0.107392  0.232014 0.14998  0.0236943   -0.0174122  -0.0118977  433  ILE A CG2 
3507  C  CG2 B ILE A 433 ? 0.107875  0.234078 0.153523 0.0229204   -0.0155787  -0.0127872  433  ILE A CG2 
3508  C  CD1 A ILE A 433 ? 0.0895843 0.221206 0.150249 0.0306613   -0.0243441  -0.0147887  433  ILE A CD1 
3509  C  CD1 B ILE A 433 ? 0.0974835 0.218252 0.137959 0.0296926   -0.0233402  -0.00856032 433  ILE A CD1 
3510  N  N   . ALA A 434 ? 0.111963  0.233615 0.148504 0.0205021   2.313e-05   -0.00908593 434  ALA A N   
3511  C  CA  . ALA A 434 ? 0.116627  0.235641 0.150003 0.017846    0.0041204   -0.00788302 434  ALA A CA  
3512  C  C   . ALA A 434 ? 0.121823  0.234852 0.144277 0.0184258   0.00488829  -0.00479385 434  ALA A C   
3513  O  O   . ALA A 434 ? 0.12743   0.23715  0.146648 0.0168433   0.00614063  -0.00383812 434  ALA A O   
3514  C  CB  . ALA A 434 ? 0.120922  0.242528 0.158837 0.0165361   0.0103627   -0.00818952 434  ALA A CB  
3515  N  N   . PHE A 435 ? 0.116673  0.228516 0.134917 0.0206677   0.00425384  -0.00370409 435  PHE A N   
3516  C  CA  . PHE A 435 ? 0.119563  0.226843 0.129708 0.0213483   0.00442504  -0.00134293 435  PHE A CA  
3517  C  C   . PHE A 435 ? 0.135783  0.240439 0.142388 0.0210208   0.00140837  -0.00044134 435  PHE A C   
3518  O  O   . PHE A 435 ? 0.148009  0.249475 0.149779 0.0207499   0.00246418  0.00096581  435  PHE A O   
3519  C  CB  . PHE A 435 ? 0.122433  0.229897 0.131356 0.0237016   0.00369247  -0.00146162 435  PHE A CB  
3520  C  CG  . PHE A 435 ? 0.137633  0.241399 0.140355 0.0243883   0.00349427  0.00035228  435  PHE A CG  
3521  C  CD1 . PHE A 435 ? 0.156574  0.258831 0.155037 0.0246454   0.00626068  0.00126032  435  PHE A CD1 
3522  C  CD2 . PHE A 435 ? 0.151471  0.253327 0.153042 0.0247537   0.00065735  0.00133984  435  PHE A CD2 
3523  C  CE1 . PHE A 435 ? 0.149798  0.249312 0.144055 0.0255645   0.00532426  0.00251174  435  PHE A CE1 
3524  C  CE2 . PHE A 435 ? 0.142762  0.242249 0.140961 0.0250922   0.00079542  0.00256474  435  PHE A CE2 
3525  C  CZ  . PHE A 435 ? 0.133694  0.232445 0.128968 0.0256892   0.00266057  0.00275789  435  PHE A CZ  
3526  N  N   . LEU A 436 ? 0.135521  0.241442 0.144043 0.0213831   -0.00237009 -0.00118143 436  LEU A N   
3527  C  CA  . LEU A 436 ? 0.156931  0.260142 0.160051 0.0214977   -0.00491007 0.00017448  436  LEU A CA  
3528  C  C   . LEU A 436 ? 0.157853  0.25867  0.156507 0.0200615   -0.00311097 0.00015581  436  LEU A C   
3529  O  O   . LEU A 436 ? 0.153328  0.251593 0.147031 0.0203486   -0.00227681 0.00179311  436  LEU A O   
3530  C  CB  . LEU A 436 ? 0.151123  0.255554 0.155526 0.0223032   -0.00962191 -0.00034386 436  LEU A CB  
3531  C  CG  . LEU A 436 ? 0.170281  0.275589 0.178685 0.02441     -0.0120402  0.00018512  436  LEU A CG  
3532  C  CD1 . LEU A 436 ? 0.172251  0.279002 0.183005 0.0256141   -0.0175132  -0.00050268 436  LEU A CD1 
3533  C  CD2 . LEU A 436 ? 0.163099  0.264542 0.167404 0.0252031   -0.0117887  0.00307639  436  LEU A CD2 
3534  N  N   . PRO A 437 ? 0.165546  0.267235 0.166928 0.0185117   -0.00263787 -0.00205444 437  PRO A N   
3535  C  CA  . PRO A 437 ? 0.158181  0.257124 0.156314 0.0173425   -0.00126444 -0.00293357 437  PRO A CA  
3536  C  C   . PRO A 437 ? 0.170329  0.266623 0.166531 0.0177166   0.00237256  -0.00098267 437  PRO A C   
3537  O  O   . PRO A 437 ? 0.159605  0.253478 0.151926 0.0179725   0.0032488   -0.00077655 437  PRO A O   
3538  C  CB  . PRO A 437 ? 0.176099  0.276305 0.180423 0.0153645   -0.00098916 -0.00574457 437  PRO A CB  
3539  C  CG  . PRO A 437 ? 0.178668  0.283165 0.190402 0.0153494   -0.00103488 -0.00601781 437  PRO A CG  
3540  C  CD  . PRO A 437 ? 0.169876  0.275461 0.179175 0.0176936   -0.00355269 -0.00443332 437  PRO A CD  
3541  N  N   . PHE A 438 ? 0.146835  0.243747 0.145517 0.0180258   0.00437852  0.00019645  438  PHE A N   
3542  C  CA  . PHE A 438 ? 0.160365  0.25443  0.156388 0.0188341   0.00685027  0.0020593   438  PHE A CA  
3543  C  C   . PHE A 438 ? 0.16649   0.26031  0.159478 0.0204946   0.00573337  0.00325414  438  PHE A C   
3544  O  O   . PHE A 438 ? 0.165167  0.256993 0.156382 0.0211392   0.00658206  0.00385899  438  PHE A O   
3545  C  CB  . PHE A 438 ? 0.14808   0.242644 0.14543  0.0189875   0.0091826   0.00313488  438  PHE A CB  
3546  C  CG  . PHE A 438 ? 0.156076  0.24716  0.14947  0.0202677   0.0109344   0.00538767  438  PHE A CG  
3547  C  CD1 . PHE A 438 ? 0.164871  0.251929 0.158006 0.0195138   0.0127963   0.00631943  438  PHE A CD1 
3548  C  CD2 . PHE A 438 ? 0.145635  0.237217 0.135993 0.0224587   0.0100648   0.00630359  438  PHE A CD2 
3549  C  CE1 . PHE A 438 ? 0.175938  0.259239 0.16532  0.0212932   0.0135532   0.00875692  438  PHE A CE1 
3550  C  CE2 . PHE A 438 ? 0.163003  0.251515 0.149388 0.0241382   0.0106023   0.00823357  438  PHE A CE2 
3551  C  CZ  . PHE A 438 ? 0.181563  0.265877 0.167233 0.0237158   0.012256    0.00978134  438  PHE A CZ  
3552  N  N   . GLY A 439 ? 0.151848  0.247739 0.145649 0.0212576   0.00390372  0.0034647   439  GLY A N   
3553  C  CA  . GLY A 439 ? 0.128464  0.223989 0.121133 0.022209    0.00284017  0.00452295  439  GLY A CA  
3554  C  C   . GLY A 439 ? 0.170498  0.264827 0.1606   0.0215603   0.00312712  0.00490584  439  GLY A C   
3555  O  O   . GLY A 439 ? 0.153478  0.247354 0.14357  0.0219693   0.00394215  0.00575541  439  GLY A O   
3556  N  N   . TYR A 440 ? 0.150235  0.244425 0.138358 0.0206107   0.00250496  0.00389881  440  TYR A N   
3557  C  CA  . TYR A 440 ? 0.156615  0.249693 0.1404   0.0202498   0.00317115  0.00396663  440  TYR A CA  
3558  C  C   . TYR A 440 ? 0.164282  0.256051 0.147859 0.0202112   0.00583372  0.00252598  440  TYR A C   
3559  O  O   . TYR A 440 ? 0.198025  0.289475 0.180268 0.0205292   0.00788497  0.00276039  440  TYR A O   
3560  C  CB  . TYR A 440 ? 0.178002  0.271371 0.159007 0.019704    0.0006995   0.00257698  440  TYR A CB  
3561  C  CG  . TYR A 440 ? 0.215541  0.307642 0.189294 0.019632    0.00095756  0.00276977  440  TYR A CG  
3562  C  CD1 . TYR A 440 ? 0.255826  0.347087 0.226937 0.0197586   0.00337352  0.00520989  440  TYR A CD1 
3563  C  CD2 . TYR A 440 ? 0.244037  0.335897 0.213668 0.0193289   -0.00076207 7.358e-05   440  TYR A CD2 
3564  C  CE1 . TYR A 440 ? 0.289856  0.379993 0.253229 0.019598    0.00482275  0.00558179  440  TYR A CE1 
3565  C  CE2 . TYR A 440 ? 0.287115  0.37772  0.247871 0.0195829   -0.00053943 6.354e-05   440  TYR A CE2 
3566  C  CZ  . TYR A 440 ? 0.276772  0.366413 0.233803 0.0196976   0.00288811  0.00300856  440  TYR A CZ  
3567  O  OH  . TYR A 440 ? 0.251198  0.339573 0.198279 0.0198645   0.0042731   0.00314675  440  TYR A OH  
3568  N  N   . LEU A 441 ? 0.145869  0.236753 0.131847 0.0198958   0.00621264  0.00119323  441  LEU A N   
3569  C  CA  . LEU A 441 ? 0.151486  0.24003  0.137555 0.0199112   0.00813139  -0.00054293 441  LEU A CA  
3570  C  C   . LEU A 441 ? 0.150932  0.238482 0.139002 0.021449    0.00978414  0.00070482  441  LEU A C   
3571  O  O   . LEU A 441 ? 0.166751  0.252727 0.155322 0.0221238   0.0113727   -0.00072576 441  LEU A O   
3572  C  CB  . LEU A 441 ? 0.148142  0.234944 0.136727 0.0186789   0.0080817   -0.00237768 441  LEU A CB  
3573  C  CG  . LEU A 441 ? 0.134254  0.219937 0.126318 0.0185662   0.00912147  -0.0004085  441  LEU A CG  
3574  C  CD1 . LEU A 441 ? 0.129354  0.211063 0.122096 0.0197465   0.0110136   0.00077537  441  LEU A CD1 
3575  C  CD2 . LEU A 441 ? 0.132988  0.219058 0.128847 0.0163709   0.00882344  -0.00199378 441  LEU A CD2 
3576  N  N   . VAL A 442 ? 0.124194  0.212492 0.11385  0.0223402   0.00906773  0.00281717  442  VAL A N   
3577  C  CA  . VAL A 442 ? 0.133202  0.220398 0.124694 0.0242067   0.00944071  0.00375109  442  VAL A CA  
3578  C  C   . VAL A 442 ? 0.126143  0.214813 0.119604 0.0250776   0.0103836   0.00295575  442  VAL A C   
3579  O  O   . VAL A 442 ? 0.147889  0.235225 0.143769 0.0265567   0.0112269   0.00220713  442  VAL A O   
3580  C  CB  . VAL A 442 ? 0.131791  0.219873 0.123266 0.0253318   0.00786094  0.00550211  442  VAL A CB  
3581  C  CG1 . VAL A 442 ? 0.139949  0.227481 0.132945 0.0277849   0.00689154  0.00616391  442  VAL A CG1 
3582  C  CG2 . VAL A 442 ? 0.134694  0.221272 0.124405 0.0247444   0.00834242  0.00642905  442  VAL A CG2 
3583  N  N   . ASP A 443 ? 0.120549  0.211888 0.113992 0.02431     0.0104686   0.00330703  443  ASP A N   
3584  C  CA  . ASP A 443 ? 0.142948  0.236236 0.139329 0.0246544   0.0124838   0.00272293  443  ASP A CA  
3585  C  C   . ASP A 443 ? 0.140125  0.232808 0.133314 0.0240037   0.0152966   0.00077803  443  ASP A C   
3586  O  O   . ASP A 443 ? 0.148454  0.242697 0.144423 0.0246167   0.0180439   -0.00046291 443  ASP A O   
3587  C  CB  . ASP A 443 ? 0.15624   0.252011 0.155054 0.023876    0.0121737   0.00421092  443  ASP A CB  
3588  C  CG  . ASP A 443 ? 0.172826  0.269935 0.177145 0.0252819   0.0096255   0.00443682  443  ASP A CG  
3589  O  OD1 . ASP A 443 ? 0.164688  0.260609 0.169343 0.0271838   0.00811405  0.0039709   443  ASP A OD1 
3590  O  OD2 . ASP A 443 ? 0.174503  0.273224 0.182099 0.0245056   0.00881509  0.00513395  443  ASP A OD2 
3591  N  N   . GLN A 444 ? 0.141003  0.231933 0.128846 0.0228922   0.0146185   -5.434e-05  444  GLN A N   
3592  C  CA  . GLN A 444 ? 0.157858  0.247921 0.142442 0.0228237   0.0169117   -0.00306104 444  GLN A CA  
3593  C  C   . GLN A 444 ? 0.142986  0.231087 0.132194 0.0244419   0.0179175   -0.00530479 444  GLN A C   
3594  O  O   . GLN A 444 ? 0.158986  0.24756  0.149218 0.0254147   0.0208019   -0.00792542 444  GLN A O   
3595  C  CB  . GLN A 444 ? 0.186581  0.274975 0.165625 0.0216668   0.0151957   -0.00492738 444  GLN A CB  
3596  C  CG  . GLN A 444 ? 0.276303  0.365978 0.250345 0.0206318   0.0133539   -0.00273815 444  GLN A CG  
3597  C  CD  . GLN A 444 ? 0.341468  0.430306 0.309261 0.0199735   0.0112118   -0.00508481 444  GLN A CD  
3598  O  OE1 . GLN A 444 ? 0.372437  0.46035  0.336284 0.0202114   0.0125649   -0.00856718 444  GLN A OE1 
3599  N  NE2 . GLN A 444 ? 0.335339  0.424728 0.303065 0.0194119   0.00750645  -0.00382526 444  GLN A NE2 
3600  N  N   . TRP A 445 ? 0.12138   0.207069 0.11339  0.024937    0.0158315   -0.00409556 445  TRP A N   
3601  C  CA  . TRP A 445 ? 0.125295  0.207945 0.121605 0.0267975   0.0162455   -0.00506887 445  TRP A CA  
3602  C  C   . TRP A 445 ? 0.1244    0.209701 0.126057 0.0290528   0.0171806   -0.00494254 445  TRP A C   
3603  O  O   . TRP A 445 ? 0.118806  0.203636 0.12433  0.0308019   0.0190166   -0.00759865 445  TRP A O   
3604  C  CB  . TRP A 445 ? 0.122946  0.202037 0.119863 0.02684     0.0142499   -0.00251212 445  TRP A CB  
3605  C  CG  . TRP A 445 ? 0.138752  0.213361 0.139451 0.0290454   0.0143701   -0.00254879 445  TRP A CG  
3606  C  CD1 . TRP A 445 ? 0.159115  0.228868 0.161296 0.0288482   0.0152636   -0.00472845 445  TRP A CD1 
3607  C  CD2 . TRP A 445 ? 0.148752  0.222589 0.152497 0.0320195   0.0129058   -0.00028848 445  TRP A CD2 
3608  N  NE1 . TRP A 445 ? 0.15927   0.22499  0.165487 0.0316927   0.014835    -0.00375198 445  TRP A NE1 
3609  C  CE2 . TRP A 445 ? 0.16337   0.231479 0.170055 0.0337645   0.013071    -0.00072463 445  TRP A CE2 
3610  C  CE3 . TRP A 445 ? 0.149166  0.226334 0.153576 0.0334899   0.0108741   0.00181574  445  TRP A CE3 
3611  C  CZ2 . TRP A 445 ? 0.181725  0.247348 0.191508 0.0373186   0.011088    0.00131388  445  TRP A CZ2 
3612  C  CZ3 . TRP A 445 ? 0.156352  0.231808 0.1639   0.0368912   0.00869442  0.00313917  445  TRP A CZ3 
3613  C  CH2 . TRP A 445 ? 0.167853  0.237647 0.177663 0.0389098   0.00868499  0.00318777  445  TRP A CH2 
3614  N  N   . ARG A 446 ? 0.120485  0.208662 0.123801 0.0292566   0.0155961   -0.00238136 446  ARG A N   
3615  C  CA  . ARG A 446 ? 0.137074  0.228202 0.147489 0.0313887   0.0155954   -0.00268788 446  ARG A CA  
3616  C  C   . ARG A 446 ? 0.132819  0.228259 0.146424 0.0308338   0.019522    -0.0048023  446  ARG A C   
3617  O  O   . ARG A 446 ? 0.123835  0.221687 0.145076 0.0328202   0.0206318   -0.00652107 446  ARG A O   
3618  C  CB  . ARG A 446 ? 0.167241  0.25956  0.177797 0.0315006   0.0121822   -2.776e-05  446  ARG A CB  
3619  C  CG  . ARG A 446 ? 0.200048  0.295428 0.218081 0.0338047   0.0100464   -0.0001933  446  ARG A CG  
3620  C  CD  . ARG A 446 ? 0.194824  0.28872  0.210387 0.035194    0.00553639  0.00185665  446  ARG A CD  
3621  N  NE  . ARG A 446 ? 0.164877  0.259377 0.175766 0.0328279   0.00513879  0.00298669  446  ARG A NE  
3622  C  CZ  . ARG A 446 ? 0.183365  0.278291 0.192687 0.0335504   0.00181173  0.00375212  446  ARG A CZ  
3623  N  NH1 . ARG A 446 ? 0.133293  0.228318 0.144353 0.0365053   -0.00180851 0.00365114  446  ARG A NH1 
3624  N  NH2 . ARG A 446 ? 0.160029  0.25526  0.165911 0.0316364   0.00180452  0.00425932  446  ARG A NH2 
3625  N  N   . TRP A 447 ? 0.126769  0.223311 0.13469  0.0282738   0.0216822   -0.0044303  447  TRP A N   
3626  C  CA  . TRP A 447 ? 0.13643   0.236398 0.145341 0.0275747   0.0265786   -0.00597753 447  TRP A CA  
3627  C  C   . TRP A 447 ? 0.146616  0.245446 0.155619 0.0291604   0.0294207   -0.0101398  447  TRP A C   
3628  O  O   . TRP A 447 ? 0.134139  0.236551 0.148983 0.030151    0.0333453   -0.0123443  447  TRP A O   
3629  C  CB  . TRP A 447 ? 0.141517  0.241312 0.141587 0.0249059   0.0280547   -0.00420515 447  TRP A CB  
3630  C  CG  . TRP A 447 ? 0.138674  0.239358 0.139954 0.0234527   0.0257811   -0.0004755  447  TRP A CG  
3631  C  CD1 . TRP A 447 ? 0.137582  0.240523 0.147447 0.0238876   0.0238965   0.00061047  447  TRP A CD1 
3632  C  CD2 . TRP A 447 ? 0.160737  0.259794 0.154461 0.0215205   0.0248163   0.00221259  447  TRP A CD2 
3633  N  NE1 . TRP A 447 ? 0.164242  0.266691 0.172571 0.0222141   0.0220081   0.00344806  447  TRP A NE1 
3634  C  CE2 . TRP A 447 ? 0.158462  0.258422 0.157239 0.0208455   0.0226245   0.00477381  447  TRP A CE2 
3635  C  CE3 . TRP A 447 ? 0.166048  0.262798 0.149496 0.0206863   0.0248385   0.00228724  447  TRP A CE3 
3636  C  CZ2 . TRP A 447 ? 0.154863  0.253051 0.149394 0.0194246   0.020809    0.00770077  447  TRP A CZ2 
3637  C  CZ3 . TRP A 447 ? 0.1653    0.260683 0.144213 0.0194446   0.0226539   0.00554031  447  TRP A CZ3 
3638  C  CH2 . TRP A 447 ? 0.159381  0.255273 0.144177 0.0189015   0.020808    0.0082471   447  TRP A CH2 
3639  N  N   . GLY A 448 ? 0.15326   0.24727  0.157573 0.0294597   0.0274158   -0.0115283  448  GLY A N   
3640  C  CA  . GLY A 448 ? 0.148732  0.240829 0.153881 0.0310743   0.0297061   -0.0162084  448  GLY A CA  
3641  C  C   . GLY A 448 ? 0.143423  0.235337 0.159211 0.0343591   0.0291169   -0.0173154  448  GLY A C   
3642  O  O   . GLY A 448 ? 0.137954  0.230456 0.158215 0.0363782   0.0320577   -0.0214436  448  GLY A O   
3643  N  N   . VAL A 449 ? 0.138311  0.22871  0.157484 0.0352928   0.0248359   -0.0138401  449  VAL A N   
3644  C  CA  . VAL A 449 ? 0.139492  0.229332 0.167916 0.038936    0.0231042   -0.0142913  449  VAL A CA  
3645  C  C   . VAL A 449 ? 0.142102  0.239341 0.179635 0.0400336   0.0254296   -0.0157034  449  VAL A C   
3646  O  O   . VAL A 449 ? 0.169495  0.268483 0.215716 0.0428989   0.0270519   -0.0190073  449  VAL A O   
3647  C  CB  . VAL A 449 ? 0.143507  0.229726 0.170948 0.0398314   0.0178223   -0.00990053 449  VAL A CB  
3648  C  CG1 . VAL A 449 ? 0.149535  0.236297 0.186242 0.0441042   0.0149732   -0.00978236 449  VAL A CG1 
3649  C  CG2 . VAL A 449 ? 0.146392  0.225346 0.167275 0.0387218   0.016461    -0.00839003 449  VAL A CG2 
3650  N  N   . PHE A 450 ? 0.140218  0.242111 0.177398 0.0377069   0.0258604   -0.0134916  450  PHE A N   
3651  C  CA  . PHE A 450 ? 0.136374  0.245518 0.184078 0.0380771   0.0284314   -0.0147836  450  PHE A CA  
3652  C  C   . PHE A 450 ? 0.147018  0.259341 0.195676 0.0375806   0.0356633   -0.0185709  450  PHE A C   
3653  O  O   . PHE A 450 ? 0.136213  0.253807 0.19631  0.0393762   0.038481    -0.0214316  450  PHE A O   
3654  C  CB  . PHE A 450 ? 0.128937  0.241339 0.176111 0.0350537   0.0278463   -0.0116225  450  PHE A CB  
3655  C  CG  . PHE A 450 ? 0.136914  0.248634 0.18686  0.0362986   0.0210341   -0.0092986  450  PHE A CG  
3656  C  CD1 . PHE A 450 ? 0.14438   0.258244 0.204793 0.039936    0.0172429   -0.0106468  450  PHE A CD1 
3657  C  CD2 . PHE A 450 ? 0.155901  0.26566  0.198609 0.0340161   0.0184879   -0.00620387 450  PHE A CD2 
3658  C  CE1 . PHE A 450 ? 0.146053  0.259196 0.206923 0.0413484   0.010639    -0.00880613 450  PHE A CE1 
3659  C  CE2 . PHE A 450 ? 0.15179   0.261204 0.195946 0.0352656   0.0126844   -0.00479953 450  PHE A CE2 
3660  C  CZ  . PHE A 450 ? 0.15671   0.267849 0.209324 0.0389079   0.00873715  -0.00614039 450  PHE A CZ  
3661  N  N   . SER A 451 ? 0.145257  0.254763 0.182211 0.03547     0.038645    -0.0190707  451  SER A N   
3662  C  CA  . SER A 451 ? 0.168459  0.281188 0.204627 0.0352339   0.0458392   -0.0228301  451  SER A CA  
3663  C  C   . SER A 451 ? 0.191711  0.30219  0.231508 0.0387274   0.0467365   -0.0282876  451  SER A C   
3664  O  O   . SER A 451 ? 0.176437  0.290072 0.217304 0.0394169   0.0529708   -0.0326576  451  SER A O   
3665  C  CB  . SER A 451 ? 0.19843   0.309052 0.219653 0.0322269   0.0483646   -0.0218174  451  SER A CB  
3666  O  OG  . SER A 451 ? 0.192541  0.296854 0.205859 0.0328177   0.0447953   -0.0234427  451  SER A OG  
3667  N  N   . GLY A 452 ? 0.182968  0.28775  0.224686 0.0409509   0.0409527   -0.027971   452  GLY A N   
3668  C  CA  . GLY A 452 ? 0.191044  0.292204 0.236905 0.0443222   0.0413774   -0.0329358  452  GLY A CA  
3669  C  C   . GLY A 452 ? 0.187559  0.28269  0.222078 0.0430392   0.041952    -0.0357797  452  GLY A C   
3670  O  O   . GLY A 452 ? 0.213459  0.304105 0.250788 0.0454245   0.0417475   -0.0400944  452  GLY A O   
3671  N  N   . ARG A 453 ? 0.187043  0.281615 0.209459 0.0394815   0.0420548   -0.0338187  453  ARG A N   
3672  C  CA  . ARG A 453 ? 0.216011  0.304866 0.228855 0.0382474   0.0406501   -0.036444   453  ARG A CA  
3673  C  C   . ARG A 453 ? 0.196295  0.277776 0.21215  0.0388071   0.0351673   -0.0350962  453  ARG A C   
3674  O  O   . ARG A 453 ? 0.202331  0.278491 0.21637  0.0389074   0.034411    -0.0391471  453  ARG A O   
3675  C  CB  . ARG A 453 ? 0.255938  0.345736 0.256097 0.03466     0.0402884   -0.0338438  453  ARG A CB  
3676  C  CG  . ARG A 453 ? 0.408505  0.503367 0.404281 0.0347079   0.0469524   -0.0367774  453  ARG A CG  
3677  C  CD  . ARG A 453 ? 0.625815  0.721194 0.607363 0.0318724   0.0473263   -0.0346312  453  ARG A CD  
3678  N  NE  . ARG A 453 ? 0.840645  0.940148 0.81526  0.0316444   0.0542977   -0.0362385  453  ARG A NE  
3679  C  CZ  . ARG A 453 ? 0.94476   1.04294  0.906063 0.0315991   0.0561635   -0.0402775  453  ARG A CZ  
3680  N  NH1 . ARG A 453 ? 1.00928   1.10283  0.966931 0.0324555   0.052287    -0.045565   453  ARG A NH1 
3681  N  NH2 . ARG A 453 ? 0.849346  0.950668 0.801008 0.0307203   0.0620448   -0.0392137  453  ARG A NH2 
3682  N  N   . THR A 454 ? 0.179844  0.26068  0.199397 0.0388185   0.0314173   -0.0293309  454  THR A N   
3683  C  CA  . THR A 454 ? 0.165193  0.239029 0.187595 0.0396062   0.0271893   -0.0269439  454  THR A CA  
3684  C  C   . THR A 454 ? 0.160946  0.234283 0.193884 0.0437695   0.0258904   -0.0260205  454  THR A C   
3685  O  O   . THR A 454 ? 0.14853   0.22494  0.184104 0.0445277   0.0236774   -0.0218246  454  THR A O   
3686  C  CB  . THR A 454 ? 0.171537  0.244951 0.188528 0.0368893   0.0239726   -0.0210993  454  THR A CB  
3687  O  OG1 . THR A 454 ? 0.163679  0.238166 0.172262 0.0336353   0.024714    -0.0224705  454  THR A OG1 
3688  C  CG2 . THR A 454 ? 0.149929  0.215989 0.168458 0.0372293   0.0206939   -0.0179488  454  THR A CG2 
3689  N  N   . PRO A 455 ? 0.166168  0.235496 0.205696 0.0468576   0.0266157   -0.0302277  455  PRO A N   
3690  C  CA  . PRO A 455 ? 0.170773  0.238193 0.220551 0.0514045   0.0242009   -0.0291533  455  PRO A CA  
3691  C  C   . PRO A 455 ? 0.186632  0.245773 0.23442  0.0516258   0.0193329   -0.0231905  455  PRO A C   
3692  O  O   . PRO A 455 ? 0.180606  0.235266 0.221065 0.04819     0.0187989   -0.0210918  455  PRO A O   
3693  C  CB  . PRO A 455 ? 0.190775  0.255421 0.247498 0.0544551   0.0269234   -0.036374   455  PRO A CB  
3694  C  CG  . PRO A 455 ? 0.199378  0.259903 0.247374 0.0509032   0.0285112   -0.0396105  455  PRO A CG  
3695  C  CD  . PRO A 455 ? 0.171092  0.237576 0.208768 0.0465418   0.0295208   -0.0370013  455  PRO A CD  
3696  N  N   . PRO A 456 ? 0.198568  0.255574 0.25275  0.0557599   0.0156372   -0.020072   456  PRO A N   
3697  C  CA  . PRO A 456 ? 0.200769  0.248591 0.251532 0.0563714   0.0115102   -0.0137944  456  PRO A CA  
3698  C  C   . PRO A 456 ? 0.201831  0.239576 0.250395 0.0545067   0.0124229   -0.014083   456  PRO A C   
3699  O  O   . PRO A 456 ? 0.213784  0.246307 0.256006 0.0520617   0.0112207   -0.00878874 456  PRO A O   
3700  C  CB  . PRO A 456 ? 0.20685   0.252995 0.265827 0.0623359   0.00731766  -0.0119441  456  PRO A CB  
3701  C  CG  . PRO A 456 ? 0.199873  0.257883 0.266406 0.0637571   0.00869626  -0.0161936  456  PRO A CG  
3702  C  CD  . PRO A 456 ? 0.190444  0.253982 0.255005 0.0599435   0.0150697   -0.0220094  456  PRO A CD  
3703  N  N   . SER A 457 ? 0.20781   0.243248 0.261952 0.0553901   0.0148918   -0.0206894  457  SER A N   
3704  C  CA  . SER A 457 ? 0.219028  0.244731 0.273115 0.0534839   0.0155173   -0.0222223  457  SER A CA  
3705  C  C   . SER A 457 ? 0.201479  0.228298 0.247251 0.0474516   0.0170745   -0.0224135  457  SER A C   
3706  O  O   . SER A 457 ? 0.212408  0.231456 0.258568 0.044978    0.0171178   -0.0227622  457  SER A O   
3707  C  CB  . SER A 457 ? 0.248505  0.272544 0.310439 0.055964    0.0177486   -0.0308828  457  SER A CB  
3708  O  OG  . SER A 457 ? 0.232553  0.266219 0.290433 0.0539069   0.0213768   -0.0366592  457  SER A OG  
3709  N  N   . ARG A 458 ? 0.174092  0.210198 0.213562 0.0451513   0.0180403   -0.0220677  458  ARG A N   
3710  C  CA  . ARG A 458 ? 0.161894  0.199588 0.194301 0.0400826   0.0187651   -0.0223143  458  ARG A CA  
3711  C  C   . ARG A 458 ? 0.150035  0.19234  0.176335 0.0382051   0.017561    -0.016066   458  ARG A C   
3712  O  O   . ARG A 458 ? 0.145855  0.191847 0.1667   0.0345275   0.0180373   -0.0165162  458  ARG A O   
3713  C  CB  . ARG A 458 ? 0.170772  0.214969 0.199947 0.0388474   0.0212783   -0.0293528  458  ARG A CB  
3714  C  CG  . ARG A 458 ? 0.179178  0.218339 0.212399 0.0396796   0.0224666   -0.0369661  458  ARG A CG  
3715  C  CD  . ARG A 458 ? 0.194065  0.23814  0.220671 0.0376714   0.0243219   -0.0438672  458  ARG A CD  
3716  N  NE  . ARG A 458 ? 0.206429  0.258493 0.231032 0.0398918   0.0276126   -0.0462455  458  ARG A NE  
3717  C  CZ  . ARG A 458 ? 0.218937  0.271948 0.249036 0.0435805   0.0304774   -0.0514017  458  ARG A CZ  
3718  N  NH1 . ARG A 458 ? 0.237776  0.283585 0.276184 0.0461949   0.0299083   -0.0550562  458  ARG A NH1 
3719  N  NH2 . ARG A 458 ? 0.228815  0.290025 0.256297 0.0445271   0.0344092   -0.0533107  458  ARG A NH2 
3720  N  N   . TYR A 459 ? 0.142063  0.184068 0.169066 0.0408462   0.0155341   -0.0105842  459  TYR A N   
3721  C  CA  . TYR A 459 ? 0.137487  0.184419 0.158428 0.039192    0.0144668   -0.00596787 459  TYR A CA  
3722  C  C   . TYR A 459 ? 0.134289  0.178056 0.150507 0.0350465   0.0148726   -0.00322185 459  TYR A C   
3723  O  O   . TYR A 459 ? 0.128186  0.177577 0.139916 0.0324729   0.0151082   -0.00280693 459  TYR A O   
3724  C  CB  . TYR A 459 ? 0.156569  0.202004 0.177837 0.0427413   0.0114421   -0.00060001 459  TYR A CB  
3725  C  CG  . TYR A 459 ? 0.174685  0.226486 0.200281 0.0462999   0.00984041  -0.00166605 459  TYR A CG  
3726  C  CD1 . TYR A 459 ? 0.16517   0.223992 0.195233 0.0464235   0.0121721   -0.00696728 459  TYR A CD1 
3727  C  CD2 . TYR A 459 ? 0.203481  0.253717 0.2292   0.0498845   0.00584539  0.00272687  459  TYR A CD2 
3728  C  CE1 . TYR A 459 ? 0.182346  0.247374 0.218782 0.0494325   0.0110509   -0.00792312 459  TYR A CE1 
3729  C  CE2 . TYR A 459 ? 0.221684  0.278012 0.253658 0.0533573   0.0035616   0.00123763  459  TYR A CE2 
3730  C  CZ  . TYR A 459 ? 0.197621  0.261669 0.235926 0.052844    0.00641778  -0.00412944 459  TYR A CZ  
3731  O  OH  . TYR A 459 ? 0.207719  0.27836  0.254413 0.055861    0.0046906   -0.00583669 459  TYR A OH  
3732  N  N   . ASN A 460 ? 0.136031  0.170891 0.154096 0.0344913   0.0150375   -0.00092284 460  ASN A N   
3733  C  CA  . ASN A 460 ? 0.151739  0.184427 0.16706  0.0302931   0.01617     0.00189224  460  ASN A CA  
3734  C  C   . ASN A 460 ? 0.160529  0.194613 0.178133 0.0264837   0.0173252   -0.00387105 460  ASN A C   
3735  O  O   . ASN A 460 ? 0.167689  0.205656 0.183055 0.0231617   0.0176934   -0.00354087 460  ASN A O   
3736  C  CB  . ASN A 460 ? 0.152611  0.175054 0.169152 0.030435    0.0166726   0.00723394  460  ASN A CB  
3737  C  CG  . ASN A 460 ? 0.164277  0.186977 0.174771 0.0285339   0.0176687   0.0135088   460  ASN A CG  
3738  O  OD1 . ASN A 460 ? 0.175087  0.204171 0.180027 0.029651    0.0165612   0.015245    460  ASN A OD1 
3739  N  ND2 . ASN A 460 ? 0.166662  0.183039 0.178826 0.0252331   0.0202101   0.0162535   460  ASN A ND2 
3740  N  N   . PHE A 461 ? 0.163066  0.194685 0.185117 0.0274283   0.0174884   -0.00976545 461  PHE A N   
3741  C  CA  . PHE A 461 ? 0.167686  0.200847 0.190928 0.0244978   0.0176963   -0.0164714  461  PHE A CA  
3742  C  C   . PHE A 461 ? 0.158105  0.200952 0.175019 0.0233992   0.0171855   -0.0182262  461  PHE A C   
3743  O  O   . PHE A 461 ? 0.148968  0.194368 0.164749 0.0201034   0.0164252   -0.0195616  461  PHE A O   
3744  C  CB  . PHE A 461 ? 0.188223  0.217225 0.216165 0.0268196   0.0180079   -0.0227949  461  PHE A CB  
3745  C  CG  . PHE A 461 ? 0.185269  0.216098 0.212952 0.025049    0.0177951   -0.0315411  461  PHE A CG  
3746  C  CD1 . PHE A 461 ? 0.1856    0.213242 0.216614 0.0211087   0.0167868   -0.0343115  461  PHE A CD1 
3747  C  CD2 . PHE A 461 ? 0.192195  0.228044 0.216321 0.0274237   0.0186598   -0.0371313  461  PHE A CD2 
3748  C  CE1 . PHE A 461 ? 0.187155  0.216102 0.217669 0.0199111   0.0155594   -0.0430724  461  PHE A CE1 
3749  C  CE2 . PHE A 461 ? 0.204662  0.241404 0.226699 0.0263693   0.0182963   -0.0455249  461  PHE A CE2 
3750  C  CZ  . PHE A 461 ? 0.193936  0.227019 0.219005 0.022741    0.0161791   -0.0486821  461  PHE A CZ  
3751  N  N   . ASP A 462 ? 0.158107  0.206168 0.171761 0.0261349   0.0174544   -0.0176125  462  ASP A N   
3752  C  CA  . ASP A 462 ? 0.159024  0.215051 0.166739 0.0253082   0.0172984   -0.018503   462  ASP A CA  
3753  C  C   . ASP A 462 ? 0.156678  0.215805 0.161606 0.0234861   0.0162202   -0.0133691  462  ASP A C   
3754  O  O   . ASP A 462 ? 0.138711  0.202365 0.139959 0.0215913   0.01534     -0.0144134  462  ASP A O   
3755  C  CB  . ASP A 462 ? 0.17657   0.236717 0.183556 0.0283349   0.0187692   -0.0197854  462  ASP A CB  
3756  C  CG  . ASP A 462 ? 0.215161  0.275049 0.222305 0.0294002   0.0205772   -0.0267219  462  ASP A CG  
3757  O  OD1 . ASP A 462 ? 0.223555  0.279314 0.231397 0.0279875   0.0199242   -0.0310341  462  ASP A OD1 
3758  O  OD2 . ASP A 462 ? 0.234187  0.298079 0.24144  0.0316686   0.0228927   -0.0283972  462  ASP A OD2 
3759  N  N   . TRP A 463 ? 0.146681  0.203102 0.152943 0.024429    0.0161257   -0.00805148 463  TRP A N   
3760  C  CA  . TRP A 463 ? 0.147452  0.20647  0.150991 0.0230489   0.0156043   -0.0037473  463  TRP A CA  
3761  C  C   . TRP A 463 ? 0.141299  0.199629 0.146505 0.019357    0.0158376   -0.00463727 463  TRP A C   
3762  O  O   . TRP A 463 ? 0.133098  0.196708 0.136448 0.0177531   0.0149481   -0.00514554 463  TRP A O   
3763  C  CB  . TRP A 463 ? 0.154655  0.209799 0.157824 0.0250681   0.0155723   0.00176397  463  TRP A CB  
3764  C  CG  . TRP A 463 ? 0.165717  0.222745 0.165445 0.0237995   0.0157244   0.00579957  463  TRP A CG  
3765  C  CD1 . TRP A 463 ? 0.18723   0.239968 0.186892 0.0221419   0.0174353   0.00923629  463  TRP A CD1 
3766  C  CD2 . TRP A 463 ? 0.163788  0.226796 0.159871 0.0245008   0.014555    0.00697921  463  TRP A CD2 
3767  N  NE1 . TRP A 463 ? 0.178253  0.234705 0.173995 0.0217133   0.0177665   0.0118948   463  TRP A NE1 
3768  C  CE2 . TRP A 463 ? 0.180904  0.243351 0.174484 0.0233773   0.0155967   0.0104093   463  TRP A CE2 
3769  C  CE3 . TRP A 463 ? 0.167998  0.236614 0.163224 0.0257189   0.0131271   0.0053389   463  TRP A CE3 
3770  C  CZ2 . TRP A 463 ? 0.18368   0.250947 0.173741 0.0239368   0.0147444   0.0115546   463  TRP A CZ2 
3771  C  CZ3 . TRP A 463 ? 0.171189  0.243904 0.163724 0.0259467   0.0120411   0.0069768   463  TRP A CZ3 
3772  C  CH2 . TRP A 463 ? 0.176968  0.249004 0.166903 0.0252557   0.0126066   0.00964213  463  TRP A CH2 
3773  N  N   . TRP A 464 ? 0.151475  0.203513 0.16142  0.018044    0.0167705   -0.00557849 464  TRP A N   
3774  C  CA  . TRP A 464 ? 0.156973  0.208951 0.170915 0.0140904   0.0170945   -0.00681294 464  TRP A CA  
3775  C  C   . TRP A 464 ? 0.150345  0.206472 0.164815 0.0125319   0.0148919   -0.0133579  464  TRP A C   
3776  O  O   . TRP A 464 ? 0.142704  0.202392 0.159723 0.00978618  0.013854    -0.0146395  464  TRP A O   
3777  C  CB  . TRP A 464 ? 0.16622   0.209654 0.186187 0.0125017   0.0191214   -0.00507757 464  TRP A CB  
3778  C  CG  . TRP A 464 ? 0.196654  0.237629 0.21379  0.0131337   0.0212619   0.00243585  464  TRP A CG  
3779  C  CD1 . TRP A 464 ? 0.211185  0.246184 0.225481 0.0161667   0.0218034   0.00729178  464  TRP A CD1 
3780  C  CD2 . TRP A 464 ? 0.188708  0.23385  0.204595 0.0110605   0.0228748   0.00557916  464  TRP A CD2 
3781  N  NE1 . TRP A 464 ? 0.186313  0.221243 0.196104 0.0159865   0.0236032   0.0133481   464  TRP A NE1 
3782  C  CE2 . TRP A 464 ? 0.204315  0.245612 0.215087 0.0128974   0.0247003   0.0122193   464  TRP A CE2 
3783  C  CE3 . TRP A 464 ? 0.204791  0.256685 0.223601 0.0081564   0.0227482   0.00308676  464  TRP A CE3 
3784  C  CZ2 . TRP A 464 ? 0.193207  0.23713  0.200889 0.0117191   0.0272419   0.0162253   464  TRP A CZ2 
3785  C  CZ3 . TRP A 464 ? 0.198035  0.252742 0.216004 0.00692743  0.0253031   0.00689768  464  TRP A CZ3 
3786  C  CH2 . TRP A 464 ? 0.199575  0.250309 0.211626 0.00863178  0.027874    0.0132209   464  TRP A CH2 
3787  N  N   . TYR A 465 ? 0.152093  0.208368 0.163734 0.0145869   0.0140884   -0.0174973  465  TYR A N   
3788  C  CA  . TYR A 465 ? 0.143702  0.203869 0.152561 0.0138059   0.0117788   -0.0234452  465  TYR A CA  
3789  C  C   . TYR A 465 ? 0.138629  0.205789 0.142605 0.0135283   0.0101889   -0.0211382  465  TYR A C   
3790  O  O   . TYR A 465 ? 0.128347  0.198807 0.133083 0.0116133   0.00758564  -0.02337    465  TYR A O   
3791  C  CB  . TYR A 465 ? 0.160184  0.219807 0.16487  0.0165332   0.0123931   -0.0276151  465  TYR A CB  
3792  C  CG  . TYR A 465 ? 0.175253  0.239661 0.172969 0.01624     0.010169    -0.0322539  465  TYR A CG  
3793  C  CD1 . TYR A 465 ? 0.203466  0.266734 0.202417 0.0145668   0.00751538  -0.0387935  465  TYR A CD1 
3794  C  CD2 . TYR A 465 ? 0.188385  0.258013 0.178344 0.0174989   0.0102717   -0.0298668  465  TYR A CD2 
3795  C  CE1 . TYR A 465 ? 0.2025    0.269757 0.193503 0.0146898   0.004587    -0.0428769  465  TYR A CE1 
3796  C  CE2 . TYR A 465 ? 0.201986  0.27504  0.184117 0.0173044   0.00791744  -0.032954   465  TYR A CE2 
3797  C  CZ  . TYR A 465 ? 0.213382  0.285218 0.195241 0.0162016   0.00494994  -0.0394863  465  TYR A CZ  
3798  O  OH  . TYR A 465 ? 0.206828  0.281634 0.179689 0.0164742   0.00180535  -0.0425042  465  TYR A OH  
3799  N  N   . LEU A 466 ? 0.135461  0.204651 0.13576  0.0155319   0.0113829   -0.0166162  466  LEU A N   
3800  C  CA  . LEU A 466 ? 0.136106  0.210865 0.132162 0.0157248   0.0100691   -0.0142334  466  LEU A CA  
3801  C  C   . LEU A 466 ? 0.13746   0.213895 0.137539 0.0138907   0.00958485  -0.0116014  466  LEU A C   
3802  O  O   . LEU A 466 ? 0.144239  0.224945 0.143258 0.013312    0.00735909  -0.0120668  466  LEU A O   
3803  C  CB  . LEU A 466 ? 0.134903  0.211125 0.127656 0.0181214   0.0114231   -0.0108597  466  LEU A CB  
3804  C  CG  . LEU A 466 ? 0.140082  0.216796 0.129129 0.0198154   0.0126582   -0.013388   466  LEU A CG  
3805  C  CD1 . LEU A 466 ? 0.14512   0.223063 0.134881 0.0219734   0.0143581   -0.0103224  466  LEU A CD1 
3806  C  CD2 . LEU A 466 ? 0.148788  0.228946 0.131277 0.0192421   0.0112322   -0.0150061  466  LEU A CD2 
3807  N  N   . ARG A 467 ? 0.136397  0.209575 0.140289 0.013427    0.0118641   -0.00848053 467  ARG A N   
3808  C  CA  . ARG A 467 ? 0.149072  0.224078 0.156702 0.0115883   0.0126901   -0.00616366 467  ARG A CA  
3809  C  C   . ARG A 467 ? 0.137909  0.214949 0.151748 0.00863992  0.0111049   -0.0102314  467  ARG A C   
3810  O  O   . ARG A 467 ? 0.146998  0.229108 0.163571 0.0076645   0.00996949  -0.0103963  467  ARG A O   
3811  C  CB  . ARG A 467 ? 0.156574  0.226285 0.165709 0.0115268   0.0160412   -0.00200311 467  ARG A CB  
3812  C  CG  . ARG A 467 ? 0.171584  0.240192 0.174839 0.0148778   0.0163529   0.00172062  467  ARG A CG  
3813  C  CD  . ARG A 467 ? 0.179941  0.252535 0.180158 0.0156128   0.0166343   0.00476577  467  ARG A CD  
3814  N  NE  . ARG A 467 ? 0.196947  0.26571  0.197401 0.0148022   0.0198297   0.00859418  467  ARG A NE  
3815  C  CZ  . ARG A 467 ? 0.205984  0.276915 0.204108 0.0148333   0.0216309   0.0112338   467  ARG A CZ  
3816  N  NH1 . ARG A 467 ? 0.176513  0.253874 0.174886 0.0148897   0.0204723   0.00954139  467  ARG A NH1 
3817  N  NH2 . ARG A 467 ? 0.216653  0.282964 0.212894 0.0144188   0.0250729   0.0153457   467  ARG A NH2 
3818  N  N   . THR A 468 ? 0.144161  0.217506 0.161439 0.00732577  0.0106218   -0.0141657  468  THR A N   
3819  C  CA  . THR A 468 ? 0.155288  0.230736 0.179537 0.00450358  0.00825314  -0.0190093  468  THR A CA  
3820  C  C   . THR A 468 ? 0.165688  0.24669  0.185128 0.00568579  0.00344816  -0.0224484  468  THR A C   
3821  O  O   . THR A 468 ? 0.157439  0.243469 0.181652 0.00440265  0.0007092   -0.0241533  468  THR A O   
3822  C  CB  . THR A 468 ? 0.189113  0.25846  0.218357 0.00295101  0.00858285  -0.022984   468  THR A CB  
3823  O  OG1 . THR A 468 ? 0.215211  0.279343 0.24825  0.00199512  0.013082    -0.0179615  468  THR A OG1 
3824  C  CG2 . THR A 468 ? 0.210561  0.28195  0.249346 -0.00046162 0.00589128  -0.0285602  468  THR A CG2 
3825  N  N   . LYS A 469 ? 0.140273  0.220089 0.150809 0.00812502  0.00246503  -0.0237348  469  LYS A N   
3826  C  CA  . LYS A 469 ? 0.14236   0.225866 0.145741 0.00945299  -0.001666   -0.0263941  469  LYS A CA  
3827  C  C   . LYS A 469 ? 0.136815  0.225462 0.139509 0.0100492   -0.00353817 -0.0230594  469  LYS A C   
3828  O  O   . LYS A 469 ? 0.13766   0.229813 0.140821 0.00987546  -0.00808288 -0.0256796  469  LYS A O   
3829  C  CB  . LYS A 469 ? 0.147065  0.228901 0.140177 0.0120093   -0.0005322  -0.0265309  469  LYS A CB  
3830  C  CG  . LYS A 469 ? 0.158758  0.243664 0.142216 0.0134966   -0.00371159 -0.0273021  469  LYS A CG  
3831  C  CD  . LYS A 469 ? 0.175715  0.259163 0.149404 0.0155576   -0.00120088 -0.0274964  469  LYS A CD  
3832  C  CE  . LYS A 469 ? 0.211951  0.297556 0.174617 0.0167734   -0.00408039 -0.0276738  469  LYS A CE  
3833  N  NZ  . LYS A 469 ? 0.22858   0.31309  0.182851 0.0183728   0.00016146  -0.0269957  469  LYS A NZ  
3834  N  N   . TYR A 470 ? 0.132183  0.221012 0.133613 0.0111415   -0.00059524 -0.017778   470  TYR A N   
3835  C  CA  . TYR A 470 ? 0.133225  0.226073 0.133528 0.0122313   -0.00213002 -0.0147978  470  TYR A CA  
3836  C  C   . TYR A 470 ? 0.13335   0.22912  0.142882 0.0107829   -0.001326   -0.0139516  470  TYR A C   
3837  O  O   . TYR A 470 ? 0.147067  0.247287 0.160302 0.0108202   -0.00464769 -0.015157   470  TYR A O   
3838  C  CB  . TYR A 470 ? 0.127317  0.218964 0.121821 0.0142033   0.0003359   -0.0105378  470  TYR A CB  
3839  C  CG  . TYR A 470 ? 0.147847  0.238477 0.133736 0.0155235   -0.00047169 -0.0112666  470  TYR A CG  
3840  C  CD1 . TYR A 470 ? 0.148915  0.241486 0.129605 0.016305    -0.0040543  -0.0112714  470  TYR A CD1 
3841  C  CD2 . TYR A 470 ? 0.155132  0.242829 0.138059 0.0162019   0.00261144  -0.0116626  470  TYR A CD2 
3842  C  CE1 . TYR A 470 ? 0.181563  0.272934 0.152801 0.0173633   -0.00410256 -0.0114075  470  TYR A CE1 
3843  C  CE2 . TYR A 470 ? 0.172219  0.259716 0.14728  0.0172674   0.00287004  -0.0124605  470  TYR A CE2 
3844  C  CZ  . TYR A 470 ? 0.189511  0.278666 0.158105 0.0176902   -6.022e-05  -0.0120122  470  TYR A CZ  
3845  O  OH  . TYR A 470 ? 0.246202  0.334708 0.205651 0.0186308   0.00122027  -0.0120017  470  TYR A OH  
3846  N  N   . GLN A 471 ? 0.127775  0.221121 0.140847 0.00976925  0.00313331  -0.0117675  471  GLN A N   
3847  C  CA  . GLN A 471 ? 0.132558  0.228697 0.152927 0.00847732  0.00540369  -0.0103804  471  GLN A CA  
3848  C  C   . GLN A 471 ? 0.137532  0.23504  0.168412 0.00523898  0.00543665  -0.0138066  471  GLN A C   
3849  O  O   . GLN A 471 ? 0.131443  0.233399 0.170176 0.00402693  0.00668     -0.0138375  471  GLN A O   
3850  C  CB  . GLN A 471 ? 0.14432   0.237378 0.162742 0.00885311  0.0103683   -0.00598646 471  GLN A CB  
3851  C  CG  . GLN A 471 ? 0.146438  0.240345 0.157943 0.0117838   0.00996284  -0.00320396 471  GLN A CG  
3852  C  CD  . GLN A 471 ? 0.161553  0.252306 0.169984 0.0125711   0.0138051   0.00055204  471  GLN A CD  
3853  O  OE1 . GLN A 471 ? 0.168288  0.254216 0.173076 0.0133319   0.0147109   0.00203426  471  GLN A OE1 
3854  N  NE2 . GLN A 471 ? 0.135085  0.228476 0.144583 0.0127823   0.0159243   0.00194236  471  GLN A NE2 
3855  N  N   . GLY A 472 ? 0.135373  0.229277 0.167783 0.00370523  0.00454328  -0.0170122  472  GLY A N   
3856  C  CA  . GLY A 472 ? 0.151091  0.246199 0.195636 0.00011138  0.00464808  -0.0205554  472  GLY A CA  
3857  C  C   . GLY A 472 ? 0.156241  0.249072 0.206977 -0.00229914 0.011281    -0.0166864  472  GLY A C   
3858  O  O   . GLY A 472 ? 0.167076  0.263822 0.228744 -0.0050544  0.0132055   -0.0175165  472  GLY A O   
3859  N  N   . ILE A 473 ? 0.162041  0.248488 0.205596 -0.00111881 0.015017    -0.0121484  473  ILE A N   
3860  C  CA  . ILE A 473 ? 0.159235  0.241495 0.205737 -0.00304241 0.0212345   -0.00761668 473  ILE A CA  
3861  C  C   . ILE A 473 ? 0.176369  0.249631 0.221837 -0.00351375 0.0222532   -0.00711606 473  ILE A C   
3862  O  O   . ILE A 473 ? 0.179894  0.25119  0.220367 -0.00143086 0.0186992   -0.00985183 473  ILE A O   
3863  C  CB  . ILE A 473 ? 0.161436  0.243793 0.199023 -0.00030645 0.0241703   -0.00201632 473  ILE A CB  
3864  C  CG1 . ILE A 473 ? 0.174491  0.253275 0.200677 0.00367323  0.021786    -0.00041497 473  ILE A CG1 
3865  C  CG2 . ILE A 473 ? 0.163134  0.253989 0.203136 0.00025952  0.0234712   -0.00307686 473  ILE A CG2 
3866  C  CD1 . ILE A 473 ? 0.158433  0.237692 0.176269 0.00660339  0.0233069   0.00402789  473  ILE A CD1 
3867  N  N   . CYS A 474 ? 0.167854  0.235566 0.217453 -0.00592905 0.0274728   -0.00324831 474  CYS A N   
3868  C  CA  . CYS A 474 ? 0.187848  0.245805 0.237893 -0.00633278 0.0285772   -0.0022601  474  CYS A CA  
3869  C  C   . CYS A 474 ? 0.200749  0.252592 0.245585 -0.0057522  0.0339881   0.00581661  474  CYS A C   
3870  O  O   . CYS A 474 ? 0.215064  0.26997  0.260826 -0.00730091 0.0381168   0.00915407  474  CYS A O   
3871  C  CB  . CYS A 474 ? 0.180809  0.236706 0.244462 -0.0110025  0.0287353   -0.00674666 474  CYS A CB  
3872  S  SG  . CYS A 474 ? 0.222885  0.282337 0.299317 -0.0164648  0.0347477   -0.00444141 474  CYS A SG  
3873  N  N   . PRO A 475 ? 0.211356  0.254117 0.251207 -0.00358743 0.0342919   0.00903258  475  PRO A N   
3874  C  CA  . PRO A 475 ? 0.220496  0.256438 0.254294 -0.00273269 0.0387774   0.0172093   475  PRO A CA  
3875  C  C   . PRO A 475 ? 0.233988  0.265122 0.276673 -0.00784779 0.0446025   0.0202072   475  PRO A C   
3876  O  O   . PRO A 475 ? 0.217028  0.245329 0.271142 -0.0113429  0.0442938   0.0162047   475  PRO A O   
3877  C  CB  . PRO A 475 ? 0.216807  0.244505 0.24535  0.00119847  0.0361956   0.0186342   475  PRO A CB  
3878  C  CG  . PRO A 475 ? 0.209926  0.237585 0.246095 0.00038744  0.0325516   0.0108876   475  PRO A CG  
3879  C  CD  . PRO A 475 ? 0.212123  0.250636 0.251782 -0.00151219 0.0303307   0.00487511  475  PRO A CD  
3880  N  N   . PRO A 476 ? 0.242125  0.272686 0.280048 -0.00862175 0.0503233   0.0269364   476  PRO A N   
3881  C  CA  . PRO A 476 ? 0.279765  0.305965 0.326031 -0.013901   0.0573075   0.0307013   476  PRO A CA  
3882  C  C   . PRO A 476 ? 0.305536  0.317473 0.351427 -0.0145489  0.0599033   0.0366995   476  PRO A C   
3883  O  O   . PRO A 476 ? 0.351155  0.358458 0.406004 -0.0196164  0.0657349   0.0395359   476  PRO A O   
3884  C  CB  . PRO A 476 ? 0.264797  0.296443 0.304565 -0.0140258  0.0628779   0.0352491   476  PRO A CB  
3885  C  CG  . PRO A 476 ? 0.270593  0.303797 0.294529 -0.00774836 0.0588259   0.0367986   476  PRO A CG  
3886  C  CD  . PRO A 476 ? 0.254366  0.28886  0.278903 -0.00462437 0.0505636   0.0306615   476  PRO A CD  
3887  N  N   . VAL A 477 ? 0.284139  0.289152 0.321492 -0.00955091 0.0554346   0.0382251   477  VAL A N   
3888  C  CA  . VAL A 477 ? 0.279781  0.270692 0.318224 -0.00924696 0.0561531   0.0427348   477  VAL A CA  
3889  C  C   . VAL A 477 ? 0.275658  0.265085 0.316269 -0.00566379 0.0490546   0.0362018   477  VAL A C   
3890  O  O   . VAL A 477 ? 0.250734  0.249198 0.287518 -0.00263418 0.0443735   0.0307917   477  VAL A O   
3891  C  CB  . VAL A 477 ? 0.311341  0.293364 0.335377 -0.00590383 0.058987    0.0535537   477  VAL A CB  
3892  C  CG1 . VAL A 477 ? 0.300471  0.283393 0.321228 -0.00966299 0.0674165   0.0602369   477  VAL A CG1 
3893  C  CG2 . VAL A 477 ? 0.280531  0.266552 0.290591 0.00104752  0.0534468   0.0537724   477  VAL A CG2 
3894  N  N   . THR A 478 ? 0.285749  0.263939 0.333185 -0.0061583  0.0486171   0.0362938   478  THR A N   
3895  C  CA  . THR A 478 ? 0.29513   0.271986 0.344949 -0.00253469 0.0426525   0.0295108   478  THR A CA  
3896  C  C   . THR A 478 ? 0.285134  0.263398 0.322301 0.00443582  0.0389034   0.0319957   478  THR A C   
3897  O  O   . THR A 478 ? 0.292077  0.265456 0.319693 0.00701872  0.0403192   0.0404851   478  THR A O   
3898  C  CB  . THR A 478 ? 0.346136  0.309055 0.405318 -0.00390168 0.0434642   0.0302484   478  THR A CB  
3899  O  OG1 . THR A 478 ? 0.369227  0.333638 0.439937 -0.0110087  0.0474335   0.0283675   478  THR A OG1 
3900  C  CG2 . THR A 478 ? 0.315347  0.277283 0.379419 -0.00082205 0.0380619   0.0213989   478  THR A CG2 
3901  N  N   . ARG A 479 ? 0.275189  0.260567 0.311856 0.00755295  0.0341096   0.024634    479  ARG A N   
3902  C  CA  . ARG A 479 ? 0.249659  0.23613  0.277558 0.0139815   0.0304908   0.0262304   479  ARG A CA  
3903  C  C   . ARG A 479 ? 0.263319  0.245733 0.297268 0.0169962   0.0272365   0.0203936   479  ARG A C   
3904  O  O   . ARG A 479 ? 0.273291  0.255844 0.315728 0.0143535   0.0270052   0.0131525   479  ARG A O   
3905  C  CB  . ARG A 479 ? 0.216995  0.216565 0.238847 0.0155101   0.0282491   0.0227765   479  ARG A CB  
3906  C  CG  . ARG A 479 ? 0.211333  0.217551 0.230332 0.0118386   0.0313052   0.025014    479  ARG A CG  
3907  C  CD  . ARG A 479 ? 0.211857  0.213265 0.223059 0.0121173   0.0347395   0.0342486   479  ARG A CD  
3908  N  NE  . ARG A 479 ? 0.213348  0.21593  0.2134   0.0175866   0.0318712   0.0379245   479  ARG A NE  
3909  C  CZ  . ARG A 479 ? 0.223233  0.218808 0.214377 0.0201781   0.0326693   0.0458395   479  ARG A CZ  
3910  N  NH1 . ARG A 479 ? 0.219941  0.21845  0.2016   0.0250961   0.0290366   0.0476304   479  ARG A NH1 
3911  N  NH2 . ARG A 479 ? 0.235439  0.220732 0.226941 0.0179101   0.0368979   0.0520869   479  ARG A NH2 
3912  N  N   . ASN A 480 ? 0.250365  0.229738 0.280245 0.0227748   0.0245      0.0228967   480  ASN A N   
3913  C  CA  . ASN A 480 ? 0.241363  0.218654 0.277324 0.0263226   0.0217372   0.0167101   480  ASN A CA  
3914  C  C   . ASN A 480 ? 0.234894  0.219127 0.265486 0.0319466   0.0184805   0.0164143   480  ASN A C   
3915  O  O   . ASN A 480 ? 0.214115  0.204884 0.236766 0.0322859   0.0181454   0.0200097   480  ASN A O   
3916  C  CB  . ASN A 480 ? 0.263572  0.226327 0.306434 0.0272396   0.0220286   0.0191363   480  ASN A CB  
3917  C  CG  . ASN A 480 ? 0.303842  0.25821  0.339967 0.0307851   0.0214534   0.0297442   480  ASN A CG  
3918  O  OD1 . ASN A 480 ? 0.286242  0.245459 0.314699 0.0352887   0.0187044   0.032538    480  ASN A OD1 
3919  N  ND2 . ASN A 480 ? 0.352652  0.294043 0.391457 0.0288485   0.0237953   0.035785    480  ASN A ND2 
3920  N  N   . GLU A 481 ? 0.238471  0.221675 0.274439 0.0362579   0.0162499   0.0116298   481  GLU A N   
3921  C  CA  . GLU A 481 ? 0.245174  0.236531 0.278455 0.0409616   0.0135991   0.0104967   481  GLU A CA  
3922  C  C   . GLU A 481 ? 0.272581  0.259847 0.301311 0.0457779   0.0105784   0.0183692   481  GLU A C   
3923  O  O   . GLU A 481 ? 0.282422  0.276743 0.309839 0.0495711   0.00782368  0.0176869   481  GLU A O   
3924  C  CB  . GLU A 481 ? 0.26536   0.25904  0.306392 0.0440666   0.0128917   0.00227788  481  GLU A CB  
3925  C  CG  . GLU A 481 ? 0.258299  0.260992 0.298871 0.0404686   0.0149337   -0.00540939 481  GLU A CG  
3926  C  CD  . GLU A 481 ? 0.231982  0.246316 0.265186 0.0386387   0.0151792   -0.00491765 481  GLU A CD  
3927  O  OE1 . GLU A 481 ? 0.239124  0.258306 0.268009 0.0406366   0.0136731   -0.00062171 481  GLU A OE1 
3928  O  OE2 . GLU A 481 ? 0.216245  0.234839 0.248805 0.0353724   0.0166002   -0.010251   481  GLU A OE2 
3929  N  N   . THR A 482 ? 0.27579   0.251879 0.301845 0.0456351   0.0109266   0.0259098   482  THR A N   
3930  C  CA  . THR A 482 ? 0.295837  0.269153 0.313414 0.0496935   0.00792391  0.0341019   482  THR A CA  
3931  C  C   . THR A 482 ? 0.260703  0.242622 0.267977 0.0473751   0.00880182  0.0366563   482  THR A C   
3932  O  O   . THR A 482 ? 0.269398  0.254716 0.270166 0.0511977   0.00526004  0.0395919   482  THR A O   
3933  C  CB  . THR A 482 ? 0.350259  0.308185 0.366063 0.0503096   0.00845404  0.0423567   482  THR A CB  
3934  O  OG1 . THR A 482 ? 0.390062  0.341613 0.416997 0.0536622   0.00653778  0.038337    482  THR A OG1 
3935  C  CG2 . THR A 482 ? 0.370433  0.324525 0.374734 0.0547418   0.00510259  0.0514452   482  THR A CG2 
3936  N  N   . HIS A 483 ? 0.243112  0.228407 0.249505 0.0413159   0.0131579   0.0352377   483  HIS A N   
3937  C  CA  . HIS A 483 ? 0.235969  0.230502 0.23457  0.0392256   0.0140969   0.035996    483  HIS A CA  
3938  C  C   . HIS A 483 ? 0.228171  0.235015 0.228519 0.0404445   0.0117737   0.0294449   483  HIS A C   
3939  O  O   . HIS A 483 ? 0.213768  0.223915 0.22179  0.0406081   0.0114901   0.0228326   483  HIS A O   
3940  C  CB  . HIS A 483 ? 0.217116  0.212081 0.216194 0.0326839   0.0192556   0.0361212   483  HIS A CB  
3941  C  CG  . HIS A 483 ? 0.231906  0.214586 0.230222 0.0310137   0.0223903   0.0430676   483  HIS A CG  
3942  N  ND1 . HIS A 483 ? 0.234017  0.210092 0.241841 0.027165    0.0251894   0.0411735   483  HIS A ND1 
3943  C  CD2 . HIS A 483 ? 0.233472  0.208365 0.222793 0.03315     0.0227522   0.0518774   483  HIS A CD2 
3944  C  CE1 . HIS A 483 ? 0.257881  0.222408 0.263362 0.0263162   0.0279392   0.0491875   483  HIS A CE1 
3945  N  NE2 . HIS A 483 ? 0.259685  0.223343 0.252782 0.0300854   0.0266275   0.0561516   483  HIS A NE2 
3946  N  N   . PHE A 484 ? 0.201406  0.214912 0.194253 0.0410056   0.0106149   0.0312368   484  PHE A N   
3947  C  CA  . PHE A 484 ? 0.186284  0.21066  0.180675 0.0418671   0.00859733  0.0261425   484  PHE A CA  
3948  C  C   . PHE A 484 ? 0.184264  0.214568 0.172082 0.0389428   0.0101193   0.027112    484  PHE A C   
3949  O  O   . PHE A 484 ? 0.187742  0.220685 0.168973 0.0411838   0.00780174  0.0295314   484  PHE A O   
3950  C  CB  . PHE A 484 ? 0.195133  0.220924 0.190509 0.0476617   0.00358996  0.02638     484  PHE A CB  
3951  C  CG  . PHE A 484 ? 0.206222  0.243145 0.204157 0.0482477   0.00179075  0.0217244   484  PHE A CG  
3952  C  CD1 . PHE A 484 ? 0.204697  0.248112 0.20752  0.0450452   0.00451601  0.0160945   484  PHE A CD1 
3953  C  CD2 . PHE A 484 ? 0.198966  0.239614 0.194197 0.0518564   -0.00272572 0.0230235   484  PHE A CD2 
3954  C  CE1 . PHE A 484 ? 0.207272  0.259832 0.212778 0.0453499   0.00348469  0.0126364   484  PHE A CE1 
3955  C  CE2 . PHE A 484 ? 0.188367  0.238753 0.187765 0.0517721   -0.00398082 0.0187125   484  PHE A CE2 
3956  C  CZ  . PHE A 484 ? 0.193784  0.249909 0.198543 0.048445    -0.00054348 0.013887    484  PHE A CZ  
3957  N  N   . ASP A 485 ? 0.184638  0.21635  0.174653 0.0341033   0.013807    0.0250651   485  ASP A N   
3958  C  CA  . ASP A 485 ? 0.186535  0.222872 0.172032 0.03108     0.015955    0.0260167   485  ASP A CA  
3959  C  C   . ASP A 485 ? 0.193195  0.238895 0.17715  0.0318864   0.013747    0.022966    485  ASP A C   
3960  O  O   . ASP A 485 ? 0.199611  0.24819  0.177818 0.0317743   0.0139792   0.0247952   485  ASP A O   
3961  C  CB  . ASP A 485 ? 0.172156  0.207637 0.162512 0.026071    0.0197552   0.0243715   485  ASP A CB  
3962  C  CG  . ASP A 485 ? 0.196551  0.221756 0.187803 0.0250232   0.022415    0.0289289   485  ASP A CG  
3963  O  OD1 . ASP A 485 ? 0.210364  0.229934 0.1944   0.0276493   0.0223096   0.0352096   485  ASP A OD1 
3964  O  OD2 . ASP A 485 ? 0.191716  0.213908 0.190454 0.0218387   0.0242474   0.0263781   485  ASP A OD2 
3965  N  N   . ALA A 486 ? 0.188228  0.238294 0.177268 0.0328116   0.0119173   0.0183925   486  ALA A N   
3966  C  CA  . ALA A 486 ? 0.1821    0.239936 0.170658 0.0337182   0.00982167  0.0161424   486  ALA A CA  
3967  C  C   . ALA A 486 ? 0.175385  0.233473 0.159211 0.0373241   0.00658569  0.0189398   486  ALA A C   
3968  O  O   . ALA A 486 ? 0.16899   0.232253 0.150459 0.0372541   0.00538057  0.0181438   486  ALA A O   
3969  C  CB  . ALA A 486 ? 0.166602  0.228136 0.161363 0.0342152   0.00933465  0.0115718   486  ALA A CB  
3970  N  N   . GLY A 487 ? 0.17951   0.231921 0.162132 0.0406803   0.00464732  0.0218257   487  GLY A N   
3971  C  CA  . GLY A 487 ? 0.19375   0.246335 0.171453 0.0447775   0.00030806  0.024047    487  GLY A CA  
3972  C  C   . GLY A 487 ? 0.205832  0.256777 0.172793 0.0443668   0.00119408  0.0277704   487  GLY A C   
3973  O  O   . GLY A 487 ? 0.211983  0.26445  0.173132 0.0474194   -0.00255774 0.0285303   487  GLY A O   
3974  N  N   . ALA A 488 ? 0.187489  0.23556  0.152089 0.0407181   0.00617467  0.0297017   488  ALA A N   
3975  C  CA  . ALA A 488 ? 0.188587  0.235999 0.143781 0.039936    0.0085039   0.0327925   488  ALA A CA  
3976  C  C   . ALA A 488 ? 0.195118  0.250818 0.150275 0.0383896   0.00873718  0.0289491   488  ALA A C   
3977  O  O   . ALA A 488 ? 0.207838  0.26401  0.156554 0.0373912   0.0116223   0.0304516   488  ALA A O   
3978  C  CB  . ALA A 488 ? 0.196125  0.237692 0.150243 0.0364882   0.0143386   0.0365084   488  ALA A CB  
3979  N  N   . LYS A 489 ? 0.166721  0.228469 0.1293   0.0378624   0.00662311  0.0242346   489  LYS A N   
3980  C  CA  . LYS A 489 ? 0.183408  0.251906 0.146365 0.0368786   0.00614152  0.0209418   489  LYS A CA  
3981  C  C   . LYS A 489 ? 0.198648  0.270272 0.161563 0.0402516   0.00075183  0.0189209   489  LYS A C   
3982  O  O   . LYS A 489 ? 0.201519  0.274207 0.171046 0.0412129   -0.00157454 0.0173823   489  LYS A O   
3983  C  CB  . LYS A 489 ? 0.192667  0.264873 0.164275 0.0336947   0.00749695  0.0175769   489  LYS A CB  
3984  C  CG  . LYS A 489 ? 0.209314  0.287731 0.18338  0.032747    0.00643089  0.0142962   489  LYS A CG  
3985  C  CD  . LYS A 489 ? 0.221578  0.301468 0.191708 0.0317707   0.00864891  0.0145066   489  LYS A CD  
3986  C  CE  . LYS A 489 ? 0.235993  0.321148 0.208867 0.0317124   0.00668225  0.0111699   489  LYS A CE  
3987  N  NZ  . LYS A 489 ? 0.219015  0.305628 0.187673 0.0319777   0.00841228  0.010786    489  LYS A NZ  
3988  N  N   . PHE A 490 ? 0.177707  0.251752 0.13504  0.0416358   -0.00095607 0.0179119   490  PHE A N   
3989  C  CA  . PHE A 490 ? 0.177066  0.253898 0.134145 0.0448575   -0.00667119 0.0154769   490  PHE A CA  
3990  C  C   . PHE A 490 ? 0.164449  0.245411 0.133007 0.0445897   -0.00939977 0.0122158   490  PHE A C   
3991  O  O   . PHE A 490 ? 0.152422  0.233744 0.124047 0.0473926   -0.0136197  0.0116399   490  PHE A O   
3992  C  CB  . PHE A 490 ? 0.182977  0.263161 0.135509 0.0450012   -0.00715393 0.0127995   490  PHE A CB  
3993  C  CG  . PHE A 490 ? 0.210934  0.294157 0.1646   0.0480087   -0.0136295  0.009211    490  PHE A CG  
3994  C  CD1 . PHE A 490 ? 0.221216  0.302232 0.164988 0.0521045   -0.0176831  0.00994696  490  PHE A CD1 
3995  C  CD2 . PHE A 490 ? 0.20342   0.291462 0.16795  0.0465909   -0.0156468  0.00514618  490  PHE A CD2 
3996  C  CE1 . PHE A 490 ? 0.264496  0.348753 0.210141 0.0548891   -0.0244867  0.00571583  490  PHE A CE1 
3997  C  CE2 . PHE A 490 ? 0.240413  0.331346 0.207878 0.0488901   -0.0216059  0.00140756  490  PHE A CE2 
3998  C  CZ  . PHE A 490 ? 0.242489  0.331882 0.20123  0.0530406   -0.0263654  0.00124991  490  PHE A CZ  
3999  N  N   . HIS A 491 ? 0.145638  0.229853 0.120948 0.0412664   -0.00686655 0.0101938   491  HIS A N   
4000  C  CA  . HIS A 491 ? 0.147802  0.236197 0.132751 0.0407003   -0.00862068 0.00735611  491  HIS A CA  
4001  C  C   . HIS A 491 ? 0.139384  0.227108 0.130501 0.0413741   -0.00833182 0.00774897  491  HIS A C   
4002  O  O   . HIS A 491 ? 0.143642  0.235302 0.143295 0.0415207   -0.00982384 0.00541755  491  HIS A O   
4003  C  CB  . HIS A 491 ? 0.146518  0.237052 0.135092 0.0370325   -0.00532728 0.00633036  491  HIS A CB  
4004  C  CG  . HIS A 491 ? 0.133999  0.225643 0.118859 0.0365128   -0.00550767 0.00527856  491  HIS A CG  
4005  N  ND1 . HIS A 491 ? 0.15341   0.243045 0.130697 0.0367747   -0.00363643 0.00663001  491  HIS A ND1 
4006  C  CD2 . HIS A 491 ? 0.13241   0.226915 0.121214 0.0358813   -0.0071588  0.00276866  491  HIS A CD2 
4007  C  CE1 . HIS A 491 ? 0.150706  0.242573 0.127475 0.036635    -0.00418858 0.00440464  491  HIS A CE1 
4008  N  NE2 . HIS A 491 ? 0.145596  0.239947 0.129264 0.0362076   -0.00667496 0.00208473  491  HIS A NE2 
4009  N  N   . VAL A 492 ? 0.133131  0.21605  0.120941 0.0417168   -0.00621786 0.0103466   492  VAL A N   
4010  C  CA  . VAL A 492 ? 0.150049  0.231582 0.143655 0.0428781   -0.0058893  0.0102591   492  VAL A CA  
4011  C  C   . VAL A 492 ? 0.149715  0.231459 0.145896 0.0473147   -0.0110741  0.0101581   492  VAL A C   
4012  O  O   . VAL A 492 ? 0.154798  0.24105  0.160727 0.0482276   -0.0126185  0.00737714  492  VAL A O   
4013  C  CB  . VAL A 492 ? 0.165824  0.241983 0.157357 0.0414396   -0.00201209 0.0121031   492  VAL A CB  
4014  C  CG1 . VAL A 492 ? 0.154038  0.22837  0.152123 0.0432411   -0.00189856 0.0112026   492  VAL A CG1 
4015  C  CG2 . VAL A 492 ? 0.143225  0.221432 0.135211 0.0371851   0.00187241  0.0106093   492  VAL A CG2 
4016  N  N   . PRO A 493 ? 0.158281  0.235211 0.146171 0.050315    -0.0138404  0.0132718   493  PRO A N   
4017  C  CA  . PRO A 493 ? 0.159713  0.236677 0.1486   0.0551463   -0.020122   0.013277    493  PRO A CA  
4018  C  C   . PRO A 493 ? 0.178935  0.26273  0.17213  0.0559043   -0.0246862  0.00933853  493  PRO A C   
4019  O  O   . PRO A 493 ? 0.186695  0.273448 0.187081 0.0592172   -0.0300118  0.00731345  493  PRO A O   
4020  C  CB  . PRO A 493 ? 0.176271  0.245465 0.151371 0.0576339   -0.0212468  0.018457    493  PRO A CB  
4021  C  CG  . PRO A 493 ? 0.162504  0.230784 0.130092 0.0533253   -0.0155098  0.0196516   493  PRO A CG  
4022  C  CD  . PRO A 493 ? 0.160308  0.231325 0.137228 0.0492454   -0.0108935  0.0172497   493  PRO A CD  
4023  N  N   . ASN A 494 ? 0.176311  0.262554 0.166259 0.05304     -0.0230391  0.00792809  494  ASN A N   
4024  C  CA  . ASN A 494 ? 0.200573  0.292232 0.19452  0.0534872   -0.0273864  0.00392803  494  ASN A CA  
4025  C  C   . ASN A 494 ? 0.190645  0.288104 0.198541 0.0503545   -0.0253552  0.00068315  494  ASN A C   
4026  O  O   . ASN A 494 ? 0.203916  0.305792 0.217935 0.0497414   -0.0280785  -0.00272001 494  ASN A O   
4027  C  CB  . ASN A 494 ? 0.224886  0.315824 0.208676 0.052864    -0.0274477  0.00352144  494  ASN A CB  
4028  C  CG  . ASN A 494 ? 0.293072  0.379411 0.263456 0.0570451   -0.0309333  0.00606853  494  ASN A CG  
4029  O  OD1 . ASN A 494 ? 0.295535  0.383142 0.264721 0.0609294   -0.0378761  0.00410611  494  ASN A OD1 
4030  N  ND2 . ASN A 494 ? 0.260879  0.341518 0.221254 0.0564069   -0.0262885  0.0107445   494  ASN A ND2 
4031  N  N   . VAL A 495 ? 0.164278  0.261228 0.176428 0.0481347   -0.0201424  0.00178643  495  VAL A N   
4032  C  CA  . VAL A 495 ? 0.164193  0.266282 0.188413 0.0455382   -0.0175629  -0.00067066 495  VAL A CA  
4033  C  C   . VAL A 495 ? 0.175059  0.279612 0.200495 0.0421756   -0.0164878  -0.00204536 495  VAL A C   
4034  O  O   . VAL A 495 ? 0.187991  0.297116 0.223743 0.041042    -0.0173973  -0.00454827 495  VAL A O   
4035  C  CB  . VAL A 495 ? 0.174016  0.280777 0.210944 0.0479794   -0.0208226  -0.00330775 495  VAL A CB  
4036  C  CG1 . VAL A 495 ? 0.214315  0.325076 0.261395 0.0446848   -0.0150357  -0.00461906 495  VAL A CG1 
4037  C  CG2 . VAL A 495 ? 0.169008  0.272121 0.204044 0.0520099   -0.0226038  -0.00162808 495  VAL A CG2 
4038  N  N   . THR A 496 ? 0.152599  0.254028 0.168757 0.0404406   -0.0142496  -0.00037983 496  THR A N   
4039  C  CA  . THR A 496 ? 0.169468  0.272428 0.187206 0.0376308   -0.0133562  -0.00149124 496  THR A CA  
4040  C  C   . THR A 496 ? 0.144783  0.246631 0.161473 0.0344118   -0.00780477 0.00040856  496  THR A C   
4041  O  O   . THR A 496 ? 0.161882  0.260592 0.171369 0.0343857   -0.00573817 0.00225959  496  THR A O   
4042  C  CB  . THR A 496 ? 0.184932  0.285571 0.193133 0.038599    -0.0151051  -0.00149789 496  THR A CB  
4043  O  OG1 . THR A 496 ? 0.251172  0.352478 0.258114 0.0420424   -0.020627   -0.00338094 496  THR A OG1 
4044  C  CG2 . THR A 496 ? 0.180469  0.282152 0.191019 0.0363368   -0.0147757  -0.00305252 496  THR A CG2 
4045  N  N   . PRO A 497 ? 0.125627  0.229588 0.148696 0.0316787   -0.00535707 0.00016319  497  PRO A N   
4046  C  CA  . PRO A 497 ? 0.135798  0.23832  0.155604 0.0291439   -0.00070784 0.00205428  497  PRO A CA  
4047  C  C   . PRO A 497 ? 0.151101  0.25104  0.163468 0.0283955   -0.00090251 0.00309363  497  PRO A C   
4048  O  O   . PRO A 497 ? 0.165308  0.265126 0.176587 0.0293999   -0.00384556 0.00208194  497  PRO A O   
4049  C  CB  . PRO A 497 ? 0.123034  0.227943 0.150328 0.026609    0.00152045  0.00211862  497  PRO A CB  
4050  C  CG  . PRO A 497 ? 0.130208  0.238809 0.167571 0.0279822   -0.00119908 -0.00029067 497  PRO A CG  
4051  C  CD  . PRO A 497 ? 0.143229  0.25094  0.177164 0.0309289   -0.00682261 -0.00182365 497  PRO A CD  
4052  N  N   . TYR A 498 ? 0.134149  0.232406 0.141823 0.0270466   0.00195454  0.00444215  498  TYR A N   
4053  C  CA  . TYR A 498 ? 0.134101  0.230557 0.135972 0.0266083   0.00187836  0.00506919  498  TYR A CA  
4054  C  C   . TYR A 498 ? 0.138678  0.234907 0.139958 0.0246495   0.0026672   0.0060054   498  TYR A C   
4055  O  O   . TYR A 498 ? 0.141856  0.237651 0.141581 0.0246052   0.00135168  0.00598322  498  TYR A O   
4056  C  CB  . TYR A 498 ? 0.129447  0.223864 0.126855 0.0270071   0.00325723  0.00546844  498  TYR A CB  
4057  C  CG  . TYR A 498 ? 0.125996  0.219591 0.119738 0.0274039   0.00259981  0.00564982  498  TYR A CG  
4058  C  CD1 . TYR A 498 ? 0.130004  0.223328 0.121867 0.0294446   0.00097257  0.00550235  498  TYR A CD1 
4059  C  CD2 . TYR A 498 ? 0.131016  0.22452  0.123279 0.0258804   0.00363158  0.00571052  498  TYR A CD2 
4060  C  CE1 . TYR A 498 ? 0.142473  0.235256 0.130191 0.0298279   0.00154141  0.00569401  498  TYR A CE1 
4061  C  CE2 . TYR A 498 ? 0.14403   0.237655 0.13451  0.026108    0.00396148  0.00559947  498  TYR A CE2 
4062  C  CZ  . TYR A 498 ? 0.160475  0.253787 0.148447 0.0279824   0.00341018  0.00565902  498  TYR A CZ  
4063  O  OH  . TYR A 498 ? 0.16974   0.263429 0.155269 0.0281708   0.00480739  0.00555852  498  TYR A OH  
4064  N  N   . ILE A 499 ? 0.142261  0.238763 0.144689 0.0232685   0.00483401  0.00691454  499  ILE A N   
4065  C  CA  . ILE A 499 ? 0.145872  0.241132 0.14511  0.0217729   0.00538217  0.00856437  499  ILE A CA  
4066  C  C   . ILE A 499 ? 0.140472  0.235057 0.142477 0.0216968   0.00287677  0.00922544  499  ILE A C   
4067  O  O   . ILE A 499 ? 0.137408  0.230528 0.136775 0.0214068   0.00173557  0.0103787   499  ILE A O   
4068  C  CB  . ILE A 499 ? 0.141402  0.236686 0.139446 0.0203852   0.00883267  0.00983623  499  ILE A CB  
4069  C  CG1 . ILE A 499 ? 0.179388  0.272596 0.170321 0.0194258   0.00900039  0.0117139   499  ILE A CG1 
4070  C  CG2 . ILE A 499 ? 0.134017  0.230526 0.138933 0.0194313   0.0101619   0.010734    499  ILE A CG2 
4071  C  CD1 . ILE A 499 ? 0.158629  0.251359 0.144406 0.0200163   0.00760612  0.0100262   499  ILE A CD1 
4072  N  N   . ARG A 500 ? 0.134279  0.229809 0.142217 0.022171    0.00153425  0.00812573  500  ARG A N   
4073  C  CA  . ARG A 500 ? 0.125648  0.220112 0.137132 0.0223097   -0.00107439 0.00778704  500  ARG A CA  
4074  C  C   . ARG A 500 ? 0.109948  0.203918 0.118135 0.0236532   -0.0030122  0.00675993  500  ARG A C   
4075  O  O   . ARG A 500 ? 0.11524   0.207648 0.125602 0.0237725   -0.00480281 0.00698949  500  ARG A O   
4076  C  CB  . ARG A 500 ? 0.116376  0.212422 0.134054 0.0232866   -0.00328135 0.00502756  500  ARG A CB  
4077  C  CG  . ARG A 500 ? 0.135723  0.233385 0.149888 0.025479    -0.00418352 0.00300405  500  ARG A CG  
4078  C  CD  . ARG A 500 ? 0.174062  0.273621 0.192928 0.0270433   -0.0071258  0.00017559  500  ARG A CD  
4079  N  NE  . ARG A 500 ? 0.164092  0.265374 0.19074  0.0255694   -0.00596616 0.00055731  500  ARG A NE  
4080  C  CZ  . ARG A 500 ? 0.200488  0.304467 0.234567 0.0264638   -0.0085585  -0.00201072 500  ARG A CZ  
4081  N  NH1 . ARG A 500 ? 0.175204  0.279725 0.208056 0.0290506   -0.0131542  -0.00512202 500  ARG A NH1 
4082  N  NH2 . ARG A 500 ? 0.153975  0.260206 0.197028 0.0246421   -0.00663085 -0.00170508 500  ARG A NH2 
4083  N  N   . TYR A 501 ? 0.114534  0.209709 0.118803 0.0246644   -0.00252015 0.00559418  501  TYR A N   
4084  C  CA  . TYR A 501 ? 0.11275   0.208418 0.115633 0.0256772   -0.00347372 0.00434153  501  TYR A CA  
4085  C  C   . TYR A 501 ? 0.133611  0.228819 0.134946 0.0248776   -0.00351111 0.00568473  501  TYR A C   
4086  O  O   . TYR A 501 ? 0.12929   0.224657 0.132725 0.025636    -0.00528148 0.00504994  501  TYR A O   
4087  C  CB  . TYR A 501 ? 0.121182  0.217998 0.120695 0.0265891   -0.00217609 0.0032207   501  TYR A CB  
4088  C  CG  . TYR A 501 ? 0.135182  0.232275 0.134507 0.0281314   -0.0031492  0.00185176  501  TYR A CG  
4089  C  CD1 . TYR A 501 ? 0.14453   0.242172 0.145343 0.0296462   -0.00530125 -0.00067152 501  TYR A CD1 
4090  C  CD2 . TYR A 501 ? 0.151103  0.24787  0.149113 0.0284572   -0.00256898 0.00258237  501  TYR A CD2 
4091  C  CE1 . TYR A 501 ? 0.143287  0.241301 0.142963 0.0314126   -0.00714082 -0.00252382 501  TYR A CE1 
4092  C  CE2 . TYR A 501 ? 0.144085  0.241267 0.142078 0.0303546   -0.00467126 0.00120197  501  TYR A CE2 
4093  C  CZ  . TYR A 501 ? 0.180103  0.277958 0.178432 0.0317787   -0.0071451  -0.0013731  501  TYR A CZ  
4094  O  OH  . TYR A 501 ? 0.159773  0.258123 0.157278 0.0339181   -0.010051   -0.00317302 501  TYR A OH  
4095  N  N   . PHE A 502 ? 0.151245  0.245843 0.14935  0.0236438   -0.00205104 0.00721053  502  PHE A N   
4096  C  CA  . PHE A 502 ? 0.162197  0.25597  0.15763  0.0230263   -0.00293119 0.00850554  502  PHE A CA  
4097  C  C   . PHE A 502 ? 0.166318  0.257833 0.163149 0.02317     -0.00492032 0.0106402   502  PHE A C   
4098  O  O   . PHE A 502 ? 0.150022  0.241212 0.147309 0.0240168   -0.00755321 0.0108232   502  PHE A O   
4099  C  CB  . PHE A 502 ? 0.161278  0.254621 0.15177  0.021936    -0.0011124  0.00896923  502  PHE A CB  
4100  C  CG  . PHE A 502 ? 0.174197  0.266772 0.160461 0.021733    -0.00305591 0.00969143  502  PHE A CG  
4101  C  CD1 . PHE A 502 ? 0.185815  0.280113 0.172895 0.0219814   -0.00502958 0.0076042   502  PHE A CD1 
4102  C  CD2 . PHE A 502 ? 0.183089  0.27326  0.164754 0.0213393   -0.00304898 0.0125338   502  PHE A CD2 
4103  C  CE1 . PHE A 502 ? 0.177863  0.271742 0.161072 0.0221382   -0.00788907 0.0077687   502  PHE A CE1 
4104  C  CE2 . PHE A 502 ? 0.200469  0.28944  0.176101 0.021642    -0.00550931 0.0134543   502  PHE A CE2 
4105  C  CZ  . PHE A 502 ? 0.196436  0.287452 0.173003 0.0222255   -0.00846617 0.0107326   502  PHE A CZ  
4106  N  N   . VAL A 503 ? 0.154242  0.244129 0.152479 0.0223088   -0.00366206 0.0123295   503  VAL A N   
4107  C  CA  . VAL A 503 ? 0.157398  0.24395  0.157595 0.0219522   -0.00488293 0.0151      503  VAL A CA  
4108  C  C   . VAL A 503 ? 0.166212  0.252442 0.17211  0.0236518   -0.00813518 0.0131461   503  VAL A C   
4109  O  O   . VAL A 503 ? 0.153523  0.236914 0.160231 0.0244129   -0.0106838  0.0149475   503  VAL A O   
4110  C  CB  . VAL A 503 ? 0.146677  0.232409 0.150368 0.0202295   -0.00220482 0.0164806   503  VAL A CB  
4111  C  CG1 . VAL A 503 ? 0.144533  0.226072 0.152513 0.0193551   -0.00305349 0.0194202   503  VAL A CG1 
4112  C  CG2 . VAL A 503 ? 0.141982  0.228146 0.140058 0.018794    0.00165685  0.0183279   503  VAL A CG2 
4113  N  N   . SER A 504 ? 0.127467  0.216177 0.136905 0.0245045   -0.00810619 0.00954353  504  SER A N   
4114  C  CA  . SER A 504 ? 0.149768  0.238115 0.164358 0.0262499   -0.0106925  0.00703156  504  SER A CA  
4115  C  C   . SER A 504 ? 0.143967  0.234028 0.158194 0.027891    -0.0121161  0.00577454  504  SER A C   
4116  O  O   . SER A 504 ? 0.166082  0.254856 0.18505  0.0294629   -0.0145819  0.00471209  504  SER A O   
4117  C  CB  . SER A 504 ? 0.155408  0.245803 0.172428 0.0272451   -0.0107513  0.00308589  504  SER A CB  
4118  O  OG  . SER A 504 ? 0.256528  0.350095 0.269014 0.0277184   -0.00895225 0.00177927  504  SER A OG  
4119  N  N   . PHE A 505 ? 0.138902  0.231819 0.149284 0.027566    -0.0107203  0.00545913  505  PHE A N   
4120  C  CA  . PHE A 505 ? 0.16132   0.256865 0.17373  0.0287966   -0.012028   0.00380547  505  PHE A CA  
4121  C  C   . PHE A 505 ? 0.182417  0.275599 0.195449 0.0294933   -0.0156155  0.00621883  505  PHE A C   
4122  O  O   . PHE A 505 ? 0.19792   0.292771 0.215793 0.0313381   -0.0181297  0.00456916  505  PHE A O   
4123  C  CB  . PHE A 505 ? 0.161262  0.260227 0.171163 0.0278261   -0.00951764 0.00258714  505  PHE A CB  
4124  C  CG  . PHE A 505 ? 0.18298   0.284518 0.193676 0.0283502   -0.00675745 -0.00013822 505  PHE A CG  
4125  C  CD1 . PHE A 505 ? 0.182977  0.28326  0.191665 0.0286722   -0.00579126 -0.00051674 505  PHE A CD1 
4126  C  CD2 . PHE A 505 ? 0.19629   0.301636 0.209842 0.0286035   -0.00519964 -0.00233856 505  PHE A CD2 
4127  C  CE1 . PHE A 505 ? 0.174067  0.276101 0.180926 0.0294788   -0.0035576  -0.0025124  505  PHE A CE1 
4128  C  CE2 . PHE A 505 ? 0.20713   0.314249 0.219391 0.0289734   -0.00179269 -0.00403958 505  PHE A CE2 
4129  C  CZ  . PHE A 505 ? 0.202931  0.308086 0.210845 0.0296975   -0.00122828 -0.00405526 505  PHE A CZ  
4130  N  N   . VAL A 506 ? 0.168897  0.258282 0.176902 0.0282305   -0.0157676  0.0101897   506  VAL A N   
4131  C  CA  . VAL A 506 ? 0.17989   0.265605 0.18598  0.0290336   -0.0192013  0.013644    506  VAL A CA  
4132  C  C   . VAL A 506 ? 0.179583  0.260776 0.190814 0.0299827   -0.0209112  0.0151415   506  VAL A C   
4133  O  O   . VAL A 506 ? 0.156692  0.236027 0.171928 0.0322492   -0.0248435  0.0154837   506  VAL A O   
4134  C  CB  . VAL A 506 ? 0.202949  0.286342 0.199674 0.0273018   -0.0178658  0.0173787   506  VAL A CB  
4135  C  CG1 . VAL A 506 ? 0.217214  0.295087 0.209264 0.0280517   -0.0208563  0.0224254   506  VAL A CG1 
4136  C  CG2 . VAL A 506 ? 0.179702  0.267212 0.172643 0.0266928   -0.0170562  0.014833    506  VAL A CG2 
4137  N  N   . LEU A 507 ? 0.162033  0.241401 0.174291 0.0282855   -0.0181799  0.0157361   507  LEU A N   
4138  C  CA  . LEU A 507 ? 0.184248  0.258493 0.202138 0.0285142   -0.019626   0.017255    507  LEU A CA  
4139  C  C   . LEU A 507 ? 0.145495  0.220872 0.171742 0.0312434   -0.0223469  0.0125385   507  LEU A C   
4140  O  O   . LEU A 507 ? 0.139539  0.21014  0.170882 0.0325269   -0.0251704  0.0136528   507  LEU A O   
4141  C  CB  . LEU A 507 ? 0.194115  0.268631 0.213311 0.0260486   -0.0160955  0.0168773   507  LEU A CB  
4142  C  CG  . LEU A 507 ? 0.226684  0.295833 0.251625 0.0245383   -0.0159576  0.019254    507  LEU A CG  
4143  C  CD1 . LEU A 507 ? 0.25797   0.321126 0.278266 0.0230945   -0.0152378  0.0264021   507  LEU A CD1 
4144  C  CD2 . LEU A 507 ? 0.253786  0.325765 0.281455 0.0222956   -0.0127601  0.0173462   507  LEU A CD2 
4145  N  N   . GLN A 508 ? 0.140749  0.221925 0.168343 0.0321797   -0.0211409  0.0073748   508  GLN A N   
4146  C  CA  . GLN A 508 ? 0.152179  0.234272 0.187332 0.0348137   -0.0228844  0.00253262  508  GLN A CA  
4147  C  C   . GLN A 508 ? 0.142664  0.223783 0.182307 0.0375518   -0.026667   0.00283604  508  GLN A C   
4148  O  O   . GLN A 508 ? 0.142395  0.221462 0.189593 0.0399129   -0.0289937  0.00022043  508  GLN A O   
4149  C  CB  . GLN A 508 ? 0.14187   0.230271 0.176348 0.035506    -0.0202316  -0.00268881 508  GLN A CB  
4150  C  CG  . GLN A 508 ? 0.157789  0.251315 0.189015 0.0353064   -0.0185522  -0.0028142  508  GLN A CG  
4151  C  CD  . GLN A 508 ? 0.191596  0.289724 0.220299 0.0351403   -0.0147646  -0.00632438 508  GLN A CD  
4152  O  OE1 . GLN A 508 ? 0.207444  0.309717 0.239188 0.0366948   -0.0134681  -0.0099028  508  GLN A OE1 
4153  N  NE2 . GLN A 508 ? 0.170156  0.267494 0.193445 0.0334394   -0.0128224  -0.00522262 508  GLN A NE2 
4154  N  N   . PHE A 509 ? 0.137121  0.219514 0.172614 0.037508    -0.027858   0.00570674  509  PHE A N   
4155  C  CA  . PHE A 509 ? 0.13304   0.214826 0.173347 0.0405278   -0.0325269  0.00600069  509  PHE A CA  
4156  C  C   . PHE A 509 ? 0.154753  0.227706 0.194722 0.0410972   -0.0360089  0.0115179   509  PHE A C   
4157  O  O   . PHE A 509 ? 0.153969  0.224126 0.20083  0.0442648   -0.0402653  0.0112487   509  PHE A O   
4158  C  CB  . PHE A 509 ? 0.127852  0.214065 0.164513 0.0405144   -0.0337448  0.00660663  509  PHE A CB  
4159  C  CG  . PHE A 509 ? 0.126275  0.220576 0.166233 0.0401217   -0.0301843  0.00109558  509  PHE A CG  
4160  C  CD1 . PHE A 509 ? 0.13035   0.229557 0.180349 0.0428616   -0.031098   -0.00377224 509  PHE A CD1 
4161  C  CD2 . PHE A 509 ? 0.128822  0.225547 0.16242  0.0371405   -0.0255204  0.00088141  509  PHE A CD2 
4162  C  CE1 . PHE A 509 ? 0.138516  0.244988 0.191469 0.0422269   -0.0266814  -0.00838415 509  PHE A CE1 
4163  C  CE2 . PHE A 509 ? 0.137668  0.240579 0.173882 0.0367288   -0.021845   -0.0033061  509  PHE A CE2 
4164  C  CZ  . PHE A 509 ? 0.13577   0.243806 0.181333 0.0390141   -0.02213    -0.00770181 509  PHE A CZ  
4165  N  N   . GLN A 510 ? 0.151367  0.219491 0.184024 0.038071    -0.033878   0.0167084   510  GLN A N   
4166  C  CA  . GLN A 510 ? 0.158063  0.216979 0.190784 0.0381328   -0.0361037  0.0225422   510  GLN A CA  
4167  C  C   . GLN A 510 ? 0.151772  0.207247 0.195193 0.0389475   -0.0366728  0.0194875   510  GLN A C   
4168  O  O   . GLN A 510 ? 0.155405  0.204371 0.204302 0.0411928   -0.0405865  0.0214953   510  GLN A O   
4169  C  CB  . GLN A 510 ? 0.181706  0.236472 0.205657 0.0343196   -0.0323711  0.028605    510  GLN A CB  
4170  C  CG  . GLN A 510 ? 0.205652  0.263614 0.21801  0.0334613   -0.031388   0.0308031   510  GLN A CG  
4171  C  CD  . GLN A 510 ? 0.22152   0.276386 0.224918 0.02999     -0.0268203  0.0360239   510  GLN A CD  
4172  O  OE1 . GLN A 510 ? 0.253963  0.313839 0.253345 0.0280317   -0.0229159  0.0339446   510  GLN A OE1 
4173  N  NE2 . GLN A 510 ? 0.238905  0.285526 0.239205 0.0293669   -0.027051   0.042847    510  GLN A NE2 
4174  N  N   . PHE A 511 ? 0.149933  0.209392 0.196273 0.0374469   -0.0333117  0.0144017   511  PHE A N   
4175  C  CA  . PHE A 511 ? 0.16208   0.218479 0.218287 0.038315    -0.0343334  0.0103303   511  PHE A CA  
4176  C  C   . PHE A 511 ? 0.162271  0.220332 0.226401 0.0428806   -0.0378434  0.00513864  511  PHE A C   
4177  O  O   . PHE A 511 ? 0.182514  0.234763 0.255203 0.0448767   -0.0408776  0.00405146  511  PHE A O   
4178  C  CB  . PHE A 511 ? 0.172143  0.23432  0.227923 0.0366551   -0.0308174  0.00487312  511  PHE A CB  
4179  C  CG  . PHE A 511 ? 0.210719  0.27129  0.263656 0.0325843   -0.0277786  0.00805174  511  PHE A CG  
4180  C  CD1 . PHE A 511 ? 0.214357  0.269127 0.264305 0.0301763   -0.0269487  0.0155998   511  PHE A CD1 
4181  C  CD2 . PHE A 511 ? 0.236271  0.301583 0.289244 0.0313996   -0.0256217  0.00347547  511  PHE A CD2 
4182  C  CE1 . PHE A 511 ? 0.244377  0.29904  0.292824 0.0263667   -0.0232032  0.0180843   511  PHE A CE1 
4183  C  CE2 . PHE A 511 ? 0.22532   0.290111 0.277787 0.0279849   -0.0231408  0.00584515  511  PHE A CE2 
4184  C  CZ  . PHE A 511 ? 0.231256  0.29102  0.28233  0.0253588   -0.0216021  0.0129633   511  PHE A CZ  
4185  N  N   . HIS A 512 ? 0.163531  0.229826 0.225987 0.0443869   -0.0368882  0.00131516  512  HIS A N   
4186  C  CA  . HIS A 512 ? 0.168869  0.238865 0.23975  0.0485962   -0.0389821  -0.00442984 512  HIS A CA  
4187  C  C   . HIS A 512 ? 0.173457  0.237346 0.249493 0.0515339   -0.0445522  -0.00068213 512  HIS A C   
4188  O  O   . HIS A 512 ? 0.170553  0.231576 0.256645 0.0548878   -0.0473743  -0.0041767  512  HIS A O   
4189  C  CB  . HIS A 512 ? 0.167029  0.246962 0.235129 0.0487521   -0.036168   -0.00770965 512  HIS A CB  
4190  C  CG  . HIS A 512 ? 0.172327  0.257971 0.24961  0.0525328   -0.0366254  -0.0141496  512  HIS A CG  
4191  N  ND1 . HIS A 512 ? 0.1907    0.277897 0.273617 0.0544746   -0.0349454  -0.0210416  512  HIS A ND1 
4192  C  CD2 . HIS A 512 ? 0.181425  0.271868 0.263698 0.0547705   -0.0385551  -0.0150087  512  HIS A CD2 
4193  C  CE1 . HIS A 512 ? 0.208393  0.301697 0.299568 0.0578408   -0.0349315  -0.0259872  512  HIS A CE1 
4194  N  NE2 . HIS A 512 ? 0.205484  0.30098  0.297436 0.0580123   -0.037358   -0.0223122  512  HIS A NE2 
4195  N  N   . GLU A 513 ? 0.177485  0.239447 0.24621  0.0506993   -0.0464299  0.00611677  513  GLU A N   
4196  C  CA  . GLU A 513 ? 0.191574  0.247321 0.263099 0.0538461   -0.0524344  0.0105583   513  GLU A CA  
4197  C  C   . GLU A 513 ? 0.20161   0.246269 0.278252 0.054183    -0.0543422  0.0135175   513  GLU A C   
4198  O  O   . GLU A 513 ? 0.192022  0.23198  0.277752 0.0582835   -0.0592377  0.0130014   513  GLU A O   
4199  C  CB  . GLU A 513 ? 0.238076  0.293191 0.298563 0.0529985   -0.0544147  0.0172603   513  GLU A CB  
4200  C  CG  . GLU A 513 ? 0.284153  0.331028 0.345496 0.0565629   -0.0613966  0.0230945   513  GLU A CG  
4201  C  CD  . GLU A 513 ? 0.369997  0.415716 0.417569 0.0556271   -0.0632769  0.029683    513  GLU A CD  
4202  O  OE1 . GLU A 513 ? 0.342209  0.384026 0.378586 0.0516425   -0.0592637  0.0349183   513  GLU A OE1 
4203  O  OE2 . GLU A 513 ? 0.419305  0.468728 0.467698 0.0589538   -0.0687093  0.0289107   513  GLU A OE2 
4204  N  N   . ALA A 514 ? 0.188656  0.228654 0.26052  0.049856    -0.0506737  0.0169182   514  ALA A N   
4205  C  CA  . ALA A 514 ? 0.19659   0.22576  0.274456 0.0493084   -0.0519675  0.0199572   514  ALA A CA  
4206  C  C   . ALA A 514 ? 0.184026  0.213279 0.275275 0.0516321   -0.0529224  0.0113262   514  ALA A C   
4207  O  O   . ALA A 514 ? 0.191488  0.211623 0.291185 0.0534756   -0.0564157  0.0125857   514  ALA A O   
4208  C  CB  . ALA A 514 ? 0.20344   0.229365 0.274973 0.0436092   -0.0470216  0.0247151   514  ALA A CB  
4209  N  N   . LEU A 515 ? 0.177353  0.215587 0.269698 0.0512235   -0.0495825  0.00301898  515  LEU A N   
4210  C  CA  . LEU A 515 ? 0.175925  0.21416  0.279105 0.0535223   -0.0502991  -0.00577587 515  LEU A CA  
4211  C  C   . LEU A 515 ? 0.175724  0.215859 0.287743 0.0593364   -0.0539236  -0.0104629  515  LEU A C   
4212  O  O   . LEU A 515 ? 0.17972   0.214135 0.302522 0.0621379   -0.0568352  -0.0142109  515  LEU A O   
4213  C  CB  . LEU A 515 ? 0.171974  0.219481 0.270756 0.0518626   -0.0457766  -0.012429   515  LEU A CB  
4214  C  CG  . LEU A 515 ? 0.177632  0.223899 0.270751 0.0467669   -0.042754   -0.00961162 515  LEU A CG  
4215  C  CD1 . LEU A 515 ? 0.175066  0.230639 0.263712 0.0464798   -0.0393777  -0.0167763  515  LEU A CD1 
4216  C  CD2 . LEU A 515 ? 0.189626  0.226364 0.291087 0.0450644   -0.044549   -0.0087806  515  LEU A CD2 
4217  N  N   . CYS A 516 ? 0.181244  0.228734 0.289767 0.0610057   -0.0540407  -0.00988538 516  CYS A N   
4218  C  CA  . CYS A 516 ? 0.21396   0.264126 0.332075 0.0665592   -0.0578666  -0.0134029  516  CYS A CA  
4219  C  C   . CYS A 516 ? 0.248096  0.286756 0.372461 0.0693907   -0.0642894  -0.00780755 516  CYS A C   
4220  O  O   . CYS A 516 ? 0.269926  0.306451 0.40708  0.0743008   -0.0677984  -0.0127238  516  CYS A O   
4221  C  CB  . CYS A 516 ? 0.229645  0.289873 0.343385 0.0669359   -0.0570181  -0.0130962  516  CYS A CB  
4222  S  SG  . CYS A 516 ? 0.282058  0.354688 0.391547 0.0645795   -0.0491261  -0.0209633  516  CYS A SG  
4223  N  N   . LYS A 517 ? 0.254759  0.285752 0.3699   0.0665478   -0.0656298  0.00251939  517  LYS A N   
4224  C  CA  . LYS A 517 ? 0.287351  0.306136 0.406556 0.0692152   -0.0716477  0.00927984  517  LYS A CA  
4225  C  C   . LYS A 517 ? 0.279448  0.288633 0.40882  0.0690504   -0.0718947  0.0068933   517  LYS A C   
4226  O  O   . LYS A 517 ? 0.243334  0.245397 0.383878 0.0734882   -0.076854   0.00596264  517  LYS A O   
4227  C  CB  . LYS A 517 ? 0.332238  0.343636 0.438011 0.0661882   -0.0723819  0.0213719   517  LYS A CB  
4228  C  CG  . LYS A 517 ? 0.405154  0.401401 0.513846 0.0683071   -0.0777594  0.0296423   517  LYS A CG  
4229  C  CD  . LYS A 517 ? 0.529928  0.521178 0.621804 0.0646517   -0.0765182  0.0410712   517  LYS A CD  
4230  C  CE  . LYS A 517 ? 0.678713  0.653887 0.769238 0.0652776   -0.0800221  0.0515601   517  LYS A CE  
4231  N  NZ  . LYS A 517 ? 0.728908  0.700396 0.801427 0.0636519   -0.0801125  0.0623309   517  LYS A NZ  
4232  N  N   . GLU A 518 ? 0.258447  0.267639 0.385006 0.0640395   -0.066856   0.00525321  518  GLU A N   
4233  C  CA  . GLU A 518 ? 0.286599  0.286661 0.423161 0.0631187   -0.0673111  0.00280318  518  GLU A CA  
4234  C  C   . GLU A 518 ? 0.29827   0.302155 0.447746 0.0680689   -0.0689849  -0.00923578 518  GLU A C   
4235  O  O   . GLU A 518 ? 0.326989  0.321607 0.488274 0.0702421   -0.0722983  -0.0114651  518  GLU A O   
4236  C  CB  . GLU A 518 ? 0.293971  0.295789 0.424966 0.0567805   -0.0618672  0.00270582  518  GLU A CB  
4237  C  CG  . GLU A 518 ? 0.375809  0.368565 0.518033 0.054909    -0.0624222  -0.00012616 518  GLU A CG  
4238  C  CD  . GLU A 518 ? 0.449228  0.426697 0.595115 0.0531176   -0.0645303  0.0101621   518  GLU A CD  
4239  O  OE1 . GLU A 518 ? 0.468351  0.437372 0.62523  0.0510858   -0.0650224  0.00826188  518  GLU A OE1 
4240  O  OE2 . GLU A 518 ? 0.450937  0.424426 0.58875  0.0538635   -0.0659039  0.0200875   518  GLU A OE2 
4241  N  N   . ALA A 519 ? 0.273472  0.290585 0.420795 0.0699105   -0.0664334  -0.0167785  519  ALA A N   
4242  C  CA  . ALA A 519 ? 0.285047  0.307667 0.442752 0.0745769   -0.066536   -0.0286516  519  ALA A CA  
4243  C  C   . ALA A 519 ? 0.303401  0.322248 0.472989 0.0809582   -0.072212   -0.0291148  519  ALA A C   
4244  O  O   . ALA A 519 ? 0.325742  0.347103 0.506601 0.0855421   -0.0728709  -0.0388678  519  ALA A O   
4245  C  CB  . ALA A 519 ? 0.249037  0.286326 0.399865 0.0743668   -0.0614984  -0.0343447  519  ALA A CB  
4246  N  N   . GLY A 520 ? 0.282562  0.295231 0.449589 0.08166     -0.0765463  -0.018852   520  GLY A N   
4247  C  CA  . GLY A 520 ? 0.292104  0.301759 0.470256 0.0883048   -0.0829185  -0.0188595  520  GLY A CA  
4248  C  C   . GLY A 520 ? 0.293711  0.317525 0.47345  0.0917909   -0.0826888  -0.0234252  520  GLY A C   
4249  O  O   . GLY A 520 ? 0.317415  0.341738 0.5085   0.0978455   -0.0878179  -0.0253891  520  GLY A O   
4250  N  N   . TYR A 521 ? 0.274951  0.31002  0.444048 0.0879465   -0.0771093  -0.0244243  521  TYR A N   
4251  C  CA  . TYR A 521 ? 0.310791  0.359616 0.482238 0.0902189   -0.0758847  -0.0289184  521  TYR A CA  
4252  C  C   . TYR A 521 ? 0.351847  0.400303 0.520594 0.0918391   -0.0818839  -0.020823   521  TYR A C   
4253  O  O   . TYR A 521 ? 0.338372  0.380469 0.494382 0.0884467   -0.0833991  -0.0110073  521  TYR A O   
4254  C  CB  . TYR A 521 ? 0.305563  0.364996 0.466993 0.0854181   -0.0677159  -0.0327293  521  TYR A CB  
4255  C  CG  . TYR A 521 ? 0.306091  0.379119 0.469124 0.0864665   -0.0657873  -0.0357278  521  TYR A CG  
4256  C  CD1 . TYR A 521 ? 0.314706  0.397257 0.490429 0.0906006   -0.0635472  -0.0455797  521  TYR A CD1 
4257  C  CD2 . TYR A 521 ? 0.294499  0.370694 0.447381 0.0833163   -0.0661396  -0.0289872  521  TYR A CD2 
4258  C  CE1 . TYR A 521 ? 0.33399   0.429286 0.513432 0.0911337   -0.0613018  -0.0483628  521  TYR A CE1 
4259  C  CE2 . TYR A 521 ? 0.304304  0.392675 0.460542 0.0839096   -0.0646424  -0.0321135  521  TYR A CE2 
4260  C  CZ  . TYR A 521 ? 0.296596  0.394655 0.466253 0.0874151   -0.061811   -0.0416076  521  TYR A CZ  
4261  O  OH  . TYR A 521 ? 0.351128  0.461267 0.525682 0.0874446   -0.0599385  -0.0443858  521  TYR A OH  
4262  N  N   . GLU A 522 ? 0.369621  0.425887 0.550481 0.0971939   -0.0852457  -0.0255414  522  GLU A N   
4263  C  CA  . GLU A 522 ? 0.407948  0.462595 0.588919 0.100202    -0.0932114  -0.0187969  522  GLU A CA  
4264  C  C   . GLU A 522 ? 0.387887  0.457716 0.572522 0.10106     -0.0929174  -0.0228019  522  GLU A C   
4265  O  O   . GLU A 522 ? 0.500547  0.571196 0.690014 0.105044    -0.100583   -0.0201021  522  GLU A O   
4266  C  CB  . GLU A 522 ? 0.449352  0.494348 0.643969 0.107043    -0.10138    -0.0181379  522  GLU A CB  
4267  C  CG  . GLU A 522 ? 0.550411  0.577858 0.739701 0.105465    -0.103064   -0.0108082  522  GLU A CG  
4268  C  CD  . GLU A 522 ? 0.686743  0.701066 0.886304 0.111671    -0.112066   -0.00668028 522  GLU A CD  
4269  O  OE1 . GLU A 522 ? 0.713304  0.715113 0.902247 0.110595    -0.116465   0.00518478  522  GLU A OE1 
4270  O  OE2 . GLU A 522 ? 0.673849  0.689906 0.891481 0.117697    -0.114589   -0.0148699  522  GLU A OE2 
4271  N  N   . GLY A 523 ? 0.378777  0.460452 0.56137  0.0973655   -0.0845762  -0.0289217  523  GLY A N   
4272  C  CA  . GLY A 523 ? 0.321569  0.416733 0.508201 0.0973642   -0.0841598  -0.0318545  523  GLY A CA  
4273  C  C   . GLY A 523 ? 0.283717  0.381364 0.453437 0.0908952   -0.080529   -0.0268127  523  GLY A C   
4274  O  O   . GLY A 523 ? 0.273091  0.361092 0.427709 0.0872975   -0.0803165  -0.0194337  523  GLY A O   
4275  N  N   . PRO A 524 ? 0.235666  0.346385 0.408697 0.0891157   -0.0768275  -0.031206   524  PRO A N   
4276  C  CA  . PRO A 524 ? 0.225067  0.338699 0.384115 0.0833509   -0.0736749  -0.0273893  524  PRO A CA  
4277  C  C   . PRO A 524 ? 0.229998  0.338565 0.375038 0.0782657   -0.0660791  -0.0255402  524  PRO A C   
4278  O  O   . PRO A 524 ? 0.21138   0.321097 0.359971 0.0783514   -0.0604604  -0.030813   524  PRO A O   
4279  C  CB  . PRO A 524 ? 0.211292  0.340198 0.381957 0.0827932   -0.0692165  -0.0349009  524  PRO A CB  
4280  C  CG  . PRO A 524 ? 0.214062  0.347701 0.405345 0.089442    -0.0740635  -0.0406194  524  PRO A CG  
4281  C  CD  . PRO A 524 ? 0.230308  0.353757 0.422077 0.0924084   -0.0746089  -0.0406167  524  PRO A CD  
4282  N  N   . LEU A 525 ? 0.198663  0.302244 0.327998 0.0740846   -0.0660702  -0.0186132  525  LEU A N   
4283  C  CA  . LEU A 525 ? 0.223315  0.321495 0.340517 0.0696901   -0.0600731  -0.016363   525  LEU A CA  
4284  C  C   . LEU A 525 ? 0.19235   0.299294 0.309967 0.0670032   -0.0513513  -0.0226144  525  LEU A C   
4285  O  O   . LEU A 525 ? 0.196359  0.300719 0.310955 0.0658556   -0.0469141  -0.0246626  525  LEU A O   
4286  C  CB  . LEU A 525 ? 0.233121  0.325638 0.334554 0.0660075   -0.0614298  -0.00817697 525  LEU A CB  
4287  C  CG  . LEU A 525 ? 0.290068  0.37872  0.379314 0.061044    -0.0552379  -0.00565529 525  LEU A CG  
4288  C  CD1 . LEU A 525 ? 0.284381  0.365106 0.376926 0.0620237   -0.0548929  -0.00594348 525  LEU A CD1 
4289  C  CD2 . LEU A 525 ? 0.277533  0.361667 0.352284 0.0579258   -0.0564366  0.00190815  525  LEU A CD2 
4290  N  N   . HIS A 526 ? 0.18076   0.298081 0.303198 0.0663245   -0.0490477  -0.0260891  526  HIS A N   
4291  C  CA  . HIS A 526 ? 0.172952  0.297855 0.294373 0.0635187   -0.0403316  -0.0307436  526  HIS A CA  
4292  C  C   . HIS A 526 ? 0.170313  0.300122 0.302764 0.0666993   -0.0363608  -0.0385594  526  HIS A C   
4293  O  O   . HIS A 526 ? 0.183137  0.319157 0.314025 0.0647803   -0.0287243  -0.0423606  526  HIS A O   
4294  C  CB  . HIS A 526 ? 0.169672  0.303106 0.292513 0.0609236   -0.0385506  -0.0311747  526  HIS A CB  
4295  C  CG  . HIS A 526 ? 0.20889   0.350359 0.348453 0.0643661   -0.0423571  -0.0353407  526  HIS A CG  
4296  N  ND1 . HIS A 526 ? 0.244182  0.383352 0.387389 0.0671086   -0.0517388  -0.0324859  526  HIS A ND1 
4297  C  CD2 . HIS A 526 ? 0.192539  0.344194 0.345999 0.0656273   -0.0381721  -0.0420117  526  HIS A CD2 
4298  C  CE1 . HIS A 526 ? 0.235837  0.38416  0.396454 0.0702719   -0.0539923  -0.0378379  526  HIS A CE1 
4299  N  NE2 . HIS A 526 ? 0.225866  0.382202 0.393272 0.069054    -0.0452299  -0.0436749  526  HIS A NE2 
4300  N  N   . GLN A 527 ? 0.161153  0.28866  0.304992 0.07177     -0.0412423  -0.0411969  527  GLN A N   
4301  C  CA  . GLN A 527 ? 0.17227   0.304347 0.326463 0.0751339   -0.0372551  -0.0494497  527  GLN A CA  
4302  C  C   . GLN A 527 ? 0.194821  0.316845 0.345482 0.0766382   -0.0387569  -0.0498663  527  GLN A C   
4303  O  O   . GLN A 527 ? 0.214223  0.337341 0.372969 0.0801412   -0.0371271  -0.0567786  527  GLN A O   
4304  C  CB  . GLN A 527 ? 0.181916  0.320767 0.35526  0.0802787   -0.0409236  -0.0542629  527  GLN A CB  
4305  C  CG  . GLN A 527 ? 0.211523  0.361704 0.390628 0.0782987   -0.0387348  -0.0551705  527  GLN A CG  
4306  C  CD  . GLN A 527 ? 0.288772  0.44749  0.488913 0.0831991   -0.0423669  -0.0604962  527  GLN A CD  
4307  O  OE1 . GLN A 527 ? 0.28267   0.436572 0.491166 0.0882572   -0.0504674  -0.0602197  527  GLN A OE1 
4308  N  NE2 . GLN A 527 ? 0.282855  0.454292 0.492685 0.0817616   -0.0363924  -0.0652744  527  GLN A NE2 
4309  N  N   . CYS A 528 ? 0.191509  0.303676 0.330715 0.073899    -0.0416954  -0.0428766  528  CYS A N   
4310  C  CA  . CYS A 528 ? 0.207086  0.30951  0.345754 0.0751024   -0.0437176  -0.0433521  528  CYS A CA  
4311  C  C   . CYS A 528 ? 0.198311  0.302757 0.329661 0.073011    -0.0368765  -0.0483792  528  CYS A C   
4312  O  O   . CYS A 528 ? 0.183943  0.291813 0.30424  0.0689348   -0.0322607  -0.0463121  528  CYS A O   
4313  C  CB  . CYS A 528 ? 0.242198  0.334057 0.371563 0.0723111   -0.0482093  -0.0338637  528  CYS A CB  
4314  S  SG  . CYS A 528 ? 0.312025  0.392546 0.43843  0.0711279   -0.0485375  -0.0336976  528  CYS A SG  
4315  N  N   . ASP A 529 ? 0.186779  0.288473 0.324139 0.0761276   -0.0369033  -0.0550244  529  ASP A N   
4316  C  CA  . ASP A 529 ? 0.184892  0.286754 0.314571 0.0748105   -0.0322523  -0.0600557  529  ASP A CA  
4317  C  C   . ASP A 529 ? 0.166295  0.25695  0.298518 0.0755181   -0.0370724  -0.0603761  529  ASP A C   
4318  O  O   . ASP A 529 ? 0.153189  0.240253 0.297629 0.0798429   -0.0406698  -0.0644434  529  ASP A O   
4319  C  CB  . ASP A 529 ? 0.182982  0.294531 0.317372 0.0779656   -0.0263884  -0.0696553  529  ASP A CB  
4320  C  CG  . ASP A 529 ? 0.185087  0.296618 0.311626 0.0780854   -0.0223792  -0.0764287  529  ASP A CG  
4321  O  OD1 . ASP A 529 ? 0.189345  0.295313 0.305442 0.0747425   -0.0234942  -0.0729615  529  ASP A OD1 
4322  O  OD2 . ASP A 529 ? 0.206882  0.323917 0.337883 0.0817569   -0.0184419  -0.0855176  529  ASP A OD2 
4323  N  N   . ILE A 530 ? 0.156772  0.241978 0.278977 0.0712884   -0.0371767  -0.0562695  530  ILE A N   
4324  C  CA  . ILE A 530 ? 0.169492  0.24413  0.29554  0.0710606   -0.0414873  -0.0561416  530  ILE A CA  
4325  C  C   . ILE A 530 ? 0.173237  0.248279 0.300588 0.0729412   -0.0401349  -0.0664548  530  ILE A C   
4326  O  O   . ILE A 530 ? 0.173284  0.239956 0.304385 0.0723019   -0.0435866  -0.0677208  530  ILE A O   
4327  C  CB  . ILE A 530 ? 0.184122  0.252886 0.301665 0.0657038   -0.0424135  -0.0472729  530  ILE A CB  
4328  C  CG1 . ILE A 530 ? 0.186887  0.260769 0.292287 0.062185    -0.0379946  -0.04799    530  ILE A CG1 
4329  C  CG2 . ILE A 530 ? 0.185914  0.25343  0.301459 0.0645069   -0.0442617  -0.0376072  530  ILE A CG2 
4330  C  CD1 . ILE A 530 ? 0.238964  0.307005 0.339061 0.0573635   -0.0389854  -0.040765   530  ILE A CD1 
4331  N  N   . TYR A 531 ? 0.163229  0.247861 0.286248 0.0747124   -0.0348459  -0.0734135  531  TYR A N   
4332  C  CA  . TYR A 531 ? 0.169806  0.255573 0.292123 0.0772566   -0.0333671  -0.0841262  531  TYR A CA  
4333  C  C   . TYR A 531 ? 0.171362  0.248846 0.307261 0.0806994   -0.0386227  -0.0897678  531  TYR A C   
4334  O  O   . TYR A 531 ? 0.166483  0.242491 0.314597 0.08423     -0.0408489  -0.0903338  531  TYR A O   
4335  C  CB  . TYR A 531 ? 0.174624  0.271122 0.295413 0.0805027   -0.027045   -0.0911851  531  TYR A CB  
4336  C  CG  . TYR A 531 ? 0.19892   0.298021 0.313811 0.082987    -0.0241262  -0.102023   531  TYR A CG  
4337  C  CD1 . TYR A 531 ? 0.20944   0.307068 0.310982 0.0803646   -0.024103   -0.102448   531  TYR A CD1 
4338  C  CD2 . TYR A 531 ? 0.218913  0.322631 0.341076 0.0882367   -0.0213165  -0.112009   531  TYR A CD2 
4339  C  CE1 . TYR A 531 ? 0.228287  0.328752 0.322184 0.0830356   -0.021737   -0.11236    531  TYR A CE1 
4340  C  CE2 . TYR A 531 ? 0.243642  0.349901 0.358607 0.090847    -0.0183386  -0.122359   531  TYR A CE2 
4341  C  CZ  . TYR A 531 ? 0.245262  0.350001 0.344868 0.0881566   -0.0185585  -0.122107   531  TYR A CZ  
4342  O  OH  . TYR A 531 ? 0.266924  0.374031 0.357226 0.0909281   -0.0162726  -0.132071   531  TYR A OH  
4343  N  N   . ARG A 532 ? 0.177612  0.249864 0.312341 0.0800925   -0.0408773  -0.0949577  532  ARG A N   
4344  C  CA  . ARG A 532 ? 0.20219   0.266125 0.349937 0.0831503   -0.0457257  -0.101897   532  ARG A CA  
4345  C  C   . ARG A 532 ? 0.219275  0.271569 0.378078 0.0816154   -0.051513   -0.0935191  532  ARG A C   
4346  O  O   . ARG A 532 ? 0.232535  0.27641  0.404092 0.0841604   -0.0558396  -0.0979182  532  ARG A O   
4347  C  CB  . ARG A 532 ? 0.226357  0.29466  0.3824   0.0895791   -0.0440229  -0.112618   532  ARG A CB  
4348  C  CG  . ARG A 532 ? 0.23639   0.312219 0.38323  0.0918661   -0.0394207  -0.123997   532  ARG A CG  
4349  C  CD  . ARG A 532 ? 0.284241  0.367117 0.438019 0.0979542   -0.0354063  -0.133336   532  ARG A CD  
4350  N  NE  . ARG A 532 ? 0.303116  0.39169  0.444628 0.0995744   -0.0310363  -0.143689   532  ARG A NE  
4351  C  CZ  . ARG A 532 ? 0.321832  0.419158 0.462148 0.103883    -0.0247476  -0.152235   532  ARG A CZ  
4352  N  NH1 . ARG A 532 ? 0.296696  0.39803  0.450632 0.107362    -0.0228001  -0.153203   532  ARG A NH1 
4353  N  NH2 . ARG A 532 ? 0.341868  0.443693 0.467619 0.104941    -0.0207155  -0.160115   532  ARG A NH2 
4354  N  N   . SER A 533 ? 0.214129  0.265143 0.367812 0.0775506   -0.051549   -0.0814215  533  SER A N   
4355  C  CA  . SER A 533 ? 0.215294  0.254656 0.376332 0.0755903   -0.056303   -0.0724791  533  SER A CA  
4356  C  C   . SER A 533 ? 0.220182  0.252366 0.380471 0.0707228   -0.0578543  -0.070751   533  SER A C   
4357  O  O   . SER A 533 ? 0.193584  0.22862  0.343605 0.0659884   -0.055485   -0.0649326  533  SER A O   
4358  C  CB  . SER A 533 ? 0.21657   0.257167 0.371856 0.0736091   -0.0557983  -0.0606706  533  SER A CB  
4359  O  OG  . SER A 533 ? 0.215672  0.244184 0.376698 0.0721469   -0.0601389  -0.0520736  533  SER A OG  
4360  N  N   . THR A 534 ? 0.250217  0.273363 0.422667 0.0719204   -0.0618217  -0.076263   534  THR A N   
4361  C  CA  . THR A 534 ? 0.279678  0.296021 0.454456 0.0669553   -0.063529   -0.0750581  534  THR A CA  
4362  C  C   . THR A 534 ? 0.277864  0.285653 0.453674 0.0623388   -0.0642018  -0.0610269  534  THR A C   
4363  O  O   . THR A 534 ? 0.266887  0.27346  0.439731 0.0569234   -0.0630626  -0.0568199  534  THR A O   
4364  C  CB  . THR A 534 ? 0.330893  0.340997 0.518233 0.0691839   -0.0673832  -0.0865674  534  THR A CB  
4365  O  OG1 . THR A 534 ? 0.341455  0.341421 0.542386 0.0722917   -0.0709619  -0.0849496  534  THR A OG1 
4366  C  CG2 . THR A 534 ? 0.313093  0.332657 0.495529 0.0735546   -0.0658405  -0.10029    534  THR A CG2 
4367  N  N   . LYS A 535 ? 0.276994  0.280048 0.455498 0.0645667   -0.0656605  -0.0535384  535  LYS A N   
4368  C  CA  . LYS A 535 ? 0.302435  0.298274 0.477869 0.0606463   -0.0656566  -0.0396104  535  LYS A CA  
4369  C  C   . LYS A 535 ? 0.283371  0.288178 0.443363 0.0567192   -0.0610709  -0.0334733  535  LYS A C   
4370  O  O   . LYS A 535 ? 0.250741  0.251954 0.407319 0.0513159   -0.0592966  -0.0259404  535  LYS A O   
4371  C  CB  . LYS A 535 ? 0.357833  0.349376 0.535273 0.0647813   -0.0684896  -0.0330815  535  LYS A CB  
4372  C  CG  . LYS A 535 ? 0.491263  0.471758 0.684677 0.0691281   -0.073648   -0.0365787  535  LYS A CG  
4373  C  CD  . LYS A 535 ? 0.596601  0.561414 0.797849 0.0653697   -0.0757926  -0.0292927  535  LYS A CD  
4374  C  CE  . LYS A 535 ? 0.669879  0.626388 0.864586 0.0628193   -0.0760152  -0.0135796  535  LYS A CE  
4375  N  NZ  . LYS A 535 ? 0.743239  0.697323 0.938126 0.0687001   -0.0801614  -0.00910052 535  LYS A NZ  
4376  N  N   . ALA A 536 ? 0.24833   0.264535 0.399887 0.0594081   -0.0588464  -0.036405   536  ALA A N   
4377  C  CA  . ALA A 536 ? 0.231273  0.255913 0.368864 0.0560359   -0.0546006  -0.0316522  536  ALA A CA  
4378  C  C   . ALA A 536 ? 0.226356  0.253574 0.360859 0.0519114   -0.0523958  -0.0349192  536  ALA A C   
4379  O  O   . ALA A 536 ? 0.214655  0.243223 0.341761 0.0473942   -0.0497527  -0.0283862  536  ALA A O   
4380  C  CB  . ALA A 536 ? 0.221488  0.257364 0.353186 0.0594294   -0.0524642  -0.0358464  536  ALA A CB  
4381  N  N   . GLY A 537 ? 0.211635  0.239851 0.35208  0.0537976   -0.0537817  -0.0457999  537  GLY A N   
4382  C  CA  . GLY A 537 ? 0.211903  0.243227 0.34969  0.0505986   -0.0529001  -0.0499558  537  GLY A CA  
4383  C  C   . GLY A 537 ? 0.214667  0.238128 0.359005 0.0452322   -0.0537351  -0.0441257  537  GLY A C   
4384  O  O   . GLY A 537 ? 0.226993  0.254454 0.366001 0.0413522   -0.0515284  -0.0415969  537  GLY A O   
4385  N  N   . ALA A 538 ? 0.235408  0.24784  0.39169  0.0450244   -0.0565474  -0.0417381  538  ALA A N   
4386  C  CA  . ALA A 538 ? 0.248968  0.252496 0.413547 0.0396972   -0.0566989  -0.0354979  538  ALA A CA  
4387  C  C   . ALA A 538 ? 0.246906  0.251106 0.401892 0.0357454   -0.0525     -0.0229331  538  ALA A C   
4388  O  O   . ALA A 538 ? 0.264669  0.268626 0.42094  0.030527    -0.0500797  -0.0192343  538  ALA A O   
4389  C  CB  . ALA A 538 ? 0.247337  0.237782 0.425749 0.0411389   -0.060404   -0.0345587  538  ALA A CB  
4390  N  N   . LYS A 539 ? 0.247084  0.25274  0.392928 0.0383329   -0.0516589  -0.0170708  539  LYS A N   
4391  C  CA  . LYS A 539 ? 0.252237  0.258795 0.387427 0.0351394   -0.0479385  -0.00614724 539  LYS A CA  
4392  C  C   . LYS A 539 ? 0.245254  0.262901 0.371049 0.0328281   -0.0441951  -0.00811296 539  LYS A C   
4393  O  O   . LYS A 539 ? 0.263745  0.281562 0.386895 0.0282644   -0.0408164  -0.002393   539  LYS A O   
4394  C  CB  . LYS A 539 ? 0.266787  0.270989 0.396248 0.0388437   -0.049466   -0.0002027  539  LYS A CB  
4395  C  CG  . LYS A 539 ? 0.3199    0.324956 0.436603 0.036081    -0.0461061  0.0104709   539  LYS A CG  
4396  C  CD  . LYS A 539 ? 0.367275  0.371711 0.476594 0.0398488   -0.0483361  0.0157432   539  LYS A CD  
4397  C  CE  . LYS A 539 ? 0.413036  0.404042 0.526659 0.0399706   -0.0509487  0.0239176   539  LYS A CE  
4398  N  NZ  . LYS A 539 ? 0.368772  0.357197 0.471527 0.035479    -0.0468432  0.0343321   539  LYS A NZ  
4399  N  N   . LEU A 540 ? 0.227389  0.254285 0.348182 0.0360582   -0.0444432  -0.0161284  540  LEU A N   
4400  C  CA  . LEU A 540 ? 0.228166  0.264263 0.3408   0.0343021   -0.0415642  -0.0181942  540  LEU A CA  
4401  C  C   . LEU A 540 ? 0.227555  0.263331 0.347493 0.0306718   -0.0418439  -0.0215181  540  LEU A C   
4402  O  O   . LEU A 540 ? 0.20823   0.248466 0.32412  0.0274645   -0.0390701  -0.0188619  540  LEU A O   
4403  C  CB  . LEU A 540 ? 0.232904  0.277082 0.339568 0.0387094   -0.0418241  -0.025848   540  LEU A CB  
4404  C  CG  . LEU A 540 ? 0.283789  0.337245 0.379674 0.0378485   -0.0388493  -0.0271721  540  LEU A CG  
4405  C  CD1 . LEU A 540 ? 0.268332  0.323312 0.356011 0.0352243   -0.0354736  -0.0181358  540  LEU A CD1 
4406  C  CD2 . LEU A 540 ? 0.31588   0.376225 0.405696 0.0421834   -0.0382524  -0.0336921  540  LEU A CD2 
4407  N  N   A ARG A 541 ? 0.229571  0.260526 0.36133  0.0314401   -0.045561   -0.0282343  541  ARG A N   
4408  N  N   B ARG A 541 ? 0.232969  0.263646 0.364955 0.0312954   -0.0455204  -0.027933   541  ARG A N   
4409  C  CA  A ARG A 541 ? 0.238123  0.269314 0.378745 0.0282719   -0.0469181  -0.0329396  541  ARG A CA  
4410  C  CA  B ARG A 541 ? 0.250394  0.281354 0.391402 0.0282798   -0.0470227  -0.0330571  541  ARG A CA  
4411  C  C   A ARG A 541 ? 0.244138  0.271773 0.389008 0.022447    -0.0435376  -0.0237068  541  ARG A C   
4412  C  C   B ARG A 541 ? 0.252794  0.279468 0.399747 0.0223412   -0.0440417  -0.0243961  541  ARG A C   
4413  O  O   A ARG A 541 ? 0.236726  0.26983  0.382135 0.0194688   -0.0420126  -0.0242851  541  ARG A O   
4414  O  O   B ARG A 541 ? 0.253774  0.284295 0.405184 0.0190158   -0.0433958  -0.0261414  541  ARG A O   
4415  C  CB  A ARG A 541 ? 0.245213  0.270412 0.399337 0.0298002   -0.0518392  -0.0417054  541  ARG A CB  
4416  C  CB  B ARG A 541 ? 0.267153  0.292296 0.42095  0.0302739   -0.0519882  -0.042048   541  ARG A CB  
4417  C  CG  A ARG A 541 ? 0.250159  0.277739 0.412963 0.027495    -0.0546287  -0.0495957  541  ARG A CG  
4418  C  CG  B ARG A 541 ? 0.300332  0.326998 0.463776 0.0283132   -0.055241   -0.0507087  541  ARG A CG  
4419  C  CD  A ARG A 541 ? 0.261926  0.284978 0.435241 0.0303915   -0.0600835  -0.0607503  541  ARG A CD  
4420  C  CD  B ARG A 541 ? 0.32041   0.343153 0.492893 0.0318793   -0.0606032  -0.0622997  541  ARG A CD  
4421  N  NE  A ARG A 541 ? 0.262995  0.28731  0.446684 0.0282427   -0.0640724  -0.0692854  541  ARG A NE  
4422  N  NE  B ARG A 541 ? 0.343569  0.354346 0.528741 0.0312981   -0.0618348  -0.0590909  541  ARG A NE  
4423  C  CZ  A ARG A 541 ? 0.271035  0.300656 0.452452 0.031502    -0.0684459  -0.0814258  541  ARG A CZ  
4424  C  CZ  B ARG A 541 ? 0.352643  0.357996 0.539493 0.0356716   -0.0633197  -0.0603612  541  ARG A CZ  
4425  N  NH1 A ARG A 541 ? 0.253166  0.288039 0.420895 0.0371264   -0.0684497  -0.0867094  541  ARG A NH1 
4426  N  NH1 B ARG A 541 ? 0.31582   0.327414 0.493431 0.0413582   -0.0635873  -0.0666104  541  ARG A NH1 
4427  N  NH2 A ARG A 541 ? 0.275216  0.304837 0.468619 0.0289096   -0.0727722  -0.0882716  541  ARG A NH2 
4428  N  NH2 B ARG A 541 ? 0.346959  0.340414 0.545235 0.034183    -0.0641633  -0.0546298  541  ARG A NH2 
4429  N  N   . LYS A 542 ? 0.260995  0.279659 0.408301 0.0211143   -0.0421759  -0.0149872  542  LYS A N   
4430  C  CA  . LYS A 542 ? 0.295732  0.309956 0.446898 0.0154237   -0.0380494  -0.00576134 542  LYS A CA  
4431  C  C   . LYS A 542 ? 0.25406   0.277018 0.393784 0.0135355   -0.0332412  -0.00153388 542  LYS A C   
4432  O  O   . LYS A 542 ? 0.269016  0.294087 0.414303 0.00908473  -0.0302681  5.582e-05   542  LYS A O   
4433  C  CB  . LYS A 542 ? 0.295524  0.29869  0.446243 0.0152089   -0.0371913  0.00411132  542  LYS A CB  
4434  C  CG  . LYS A 542 ? 0.410344  0.402631 0.577258 0.0145612   -0.0406245  0.0019571   542  LYS A CG  
4435  C  CD  . LYS A 542 ? 0.567233  0.547118 0.733618 0.0153062   -0.0408447  0.0118083   542  LYS A CD  
4436  C  CE  . LYS A 542 ? 0.661503  0.629538 0.845603 0.0143893   -0.0442093  0.00959717  542  LYS A CE  
4437  N  NZ  . LYS A 542 ? 0.692829  0.651103 0.876963 0.0190813   -0.0480485  0.0128146   542  LYS A NZ  
4438  N  N   . VAL A 543 ? 0.223648  0.252463 0.349249 0.0170888   -0.0327891  -0.00130077 543  VAL A N   
4439  C  CA  . VAL A 543 ? 0.222236  0.259102 0.337298 0.0158676   -0.0287679  0.00148349  543  VAL A CA  
4440  C  C   . VAL A 543 ? 0.234525  0.279062 0.353916 0.0152758   -0.0298719  -0.0063617  543  VAL A C   
4441  O  O   . VAL A 543 ? 0.228399  0.276455 0.349822 0.0118684   -0.0267346  -0.00414668 543  VAL A O   
4442  C  CB  . VAL A 543 ? 0.208762  0.250081 0.309155 0.0195673   -0.0283148  0.0028089   543  VAL A CB  
4443  C  CG1 . VAL A 543 ? 0.212093  0.261682 0.302999 0.0184864   -0.0246536  0.0040072   543  VAL A CG1 
4444  C  CG2 . VAL A 543 ? 0.216681  0.251002 0.312458 0.0202715   -0.0279837  0.0108278   543  VAL A CG2 
4445  N  N   . LEU A 544 ? 0.225449  0.272855 0.34543  0.0190052   -0.0343311  -0.0155556  544  LEU A N   
4446  C  CA  . LEU A 544 ? 0.205358  0.26046  0.325527 0.0195268   -0.0361498  -0.0228312  544  LEU A CA  
4447  C  C   . LEU A 544 ? 0.200774  0.255108 0.335974 0.0152983   -0.0370077  -0.0246325  544  LEU A C   
4448  O  O   . LEU A 544 ? 0.189553  0.250264 0.325231 0.0137262   -0.0359632  -0.0252098  544  LEU A O   
4449  C  CB  . LEU A 544 ? 0.198148  0.255667 0.314662 0.024426    -0.0404548  -0.032137   544  LEU A CB  
4450  C  CG  . LEU A 544 ? 0.228949  0.287759 0.333381 0.0282429   -0.0390015  -0.0306576  544  LEU A CG  
4451  C  CD1 . LEU A 544 ? 0.227342  0.289649 0.327796 0.0328862   -0.0420138  -0.0402931  544  LEU A CD1 
4452  C  CD2 . LEU A 544 ? 0.211898  0.276301 0.304837 0.027248    -0.0347583  -0.0246714  544  LEU A CD2 
4453  N  N   . ARG A 545 ? 0.21074   0.257136 0.358915 0.0134002   -0.0386544  -0.0250036  545  ARG A N   
4454  C  CA  . ARG A 545 ? 0.28199   0.326803 0.447462 0.00897484  -0.0396579  -0.0272873  545  ARG A CA  
4455  C  C   . ARG A 545 ? 0.284717  0.330995 0.453474 0.00372239  -0.0333884  -0.0188546  545  ARG A C   
4456  O  O   . ARG A 545 ? 0.27675   0.326349 0.458546 0.00039438  -0.0337717  -0.0219469  545  ARG A O   
4457  C  CB  . ARG A 545 ? 0.28539   0.320425 0.46553  0.00790208  -0.0428984  -0.0300055  545  ARG A CB  
4458  C  CG  . ARG A 545 ? 0.378664  0.414479 0.557526 0.0131726   -0.0494235  -0.0413553  545  ARG A CG  
4459  C  CD  . ARG A 545 ? 0.409935  0.436889 0.60604  0.012152    -0.0537067  -0.046849   545  ARG A CD  
4460  N  NE  . ARG A 545 ? 0.477134  0.506695 0.68875  0.00850391  -0.0566581  -0.0532603  545  ARG A NE  
4461  C  CZ  . ARG A 545 ? 0.508158  0.544388 0.720992 0.0108595   -0.0624698  -0.0647776  545  ARG A CZ  
4462  N  NH1 . ARG A 545 ? 0.507647  0.548855 0.705577 0.0168597   -0.0653002  -0.0711878  545  ARG A NH1 
4463  N  NH2 . ARG A 545 ? 0.473506  0.511396 0.702832 0.00714109  -0.0655022  -0.0699611  545  ARG A NH2 
4464  N  N   . ALA A 546 ? 0.267102  0.311979 0.424086 0.00328092  -0.0278596  -0.00924192 546  ALA A N   
4465  C  CA  . ALA A 546 ? 0.270452  0.316186 0.429434 -0.00155394 -0.0210272  -0.00121368 546  ALA A CA  
4466  C  C   . ALA A 546 ? 0.261274  0.318047 0.418007 -0.00159593 -0.0196311  -0.00407488 546  ALA A C   
4467  O  O   . ALA A 546 ? 0.282973  0.342465 0.447599 -0.00579097 -0.0149422  -0.00097686 546  ALA A O   
4468  C  CB  . ALA A 546 ? 0.262578  0.303099 0.40794  -0.00131871 -0.0164117  0.00902775  546  ALA A CB  
4469  N  N   . GLY A 547 ? 0.22097   0.284027 0.367315 0.00305949  -0.0232451  -0.00963691 547  GLY A N   
4470  C  CA  . GLY A 547 ? 0.226546  0.298767 0.368754 0.00354545  -0.0217055  -0.0107568  547  GLY A CA  
4471  C  C   . GLY A 547 ? 0.254135  0.326511 0.390314 0.00085339  -0.0138545  -0.00162644 547  GLY A C   
4472  O  O   . GLY A 547 ? 0.232871  0.299662 0.359116 0.00117786  -0.0112558  0.00465392  547  GLY A O   
4473  N  N   . SER A 548 ? 0.227227  0.305714 0.370794 -0.00181183 -0.0103358  -0.00129559 548  SER A N   
4474  C  CA  . SER A 548 ? 0.229075  0.308732 0.367601 -0.00429193 -0.00235822 0.00611354  548  SER A CA  
4475  C  C   . SER A 548 ? 0.262813  0.339813 0.416578 -0.0101409  0.00282261  0.010025    548  SER A C   
4476  O  O   . SER A 548 ? 0.25649   0.337067 0.412982 -0.0131404  0.0098278   0.0138739   548  SER A O   
4477  C  CB  . SER A 548 ? 0.234325  0.323081 0.369392 -0.0024913  -0.00136703 0.00356454  548  SER A CB  
4478  O  OG  . SER A 548 ? 0.257504  0.352529 0.409143 -0.0034404  -0.00436299 -0.00282228 548  SER A OG  
4479  N  N   . SER A 549 ? 0.268639  0.338889 0.432678 -0.0118336  -0.00021119 0.0090563   549  SER A N   
4480  C  CA  . SER A 549 ? 0.276877  0.343712 0.457179 -0.017873   0.00470101  0.0128144   549  SER A CA  
4481  C  C   . SER A 549 ? 0.317468  0.376844 0.488117 -0.0205676  0.0127904   0.0242802   549  SER A C   
4482  O  O   . SER A 549 ? 0.276014  0.333446 0.457529 -0.0260116  0.0194414   0.0291683   549  SER A O   
4483  C  CB  . SER A 549 ? 0.282843  0.343908 0.478181 -0.0189847  -0.00126037 0.00793962  549  SER A CB  
4484  O  OG  . SER A 549 ? 0.355975  0.406946 0.540986 -0.0167263  -0.00340348 0.0115874   549  SER A OG  
4485  N  N   . ARG A 550 ? 0.304483  0.358999 0.455661 -0.0168715  0.0118479   0.0285243   550  ARG A N   
4486  C  CA  . ARG A 550 ? 0.300683  0.347171 0.440492 -0.0186067  0.0179868   0.039361    550  ARG A CA  
4487  C  C   . ARG A 550 ? 0.282143  0.331679 0.400624 -0.0149146  0.0194234   0.0419029   550  ARG A C   
4488  O  O   . ARG A 550 ? 0.256646  0.311284 0.368545 -0.010456   0.0141573   0.0358973   550  ARG A O   
4489  C  CB  . ARG A 550 ? 0.30775   0.342448 0.444471 -0.0172016  0.0137791   0.0429328   550  ARG A CB  
4490  C  CG  . ARG A 550 ? 0.409863  0.438367 0.567052 -0.0211758  0.0126819   0.0418878   550  ARG A CG  
4491  C  CD  . ARG A 550 ? 0.491104  0.50557  0.643228 -0.0212818  0.012593    0.0505199   550  ARG A CD  
4492  N  NE  . ARG A 550 ? 0.503393  0.514782 0.652202 -0.0157537  0.00369922  0.0451573   550  ARG A NE  
4493  C  CZ  . ARG A 550 ? 0.574217  0.57975  0.709588 -0.0112559  0.00015081  0.0484654   550  ARG A CZ  
4494  N  NH1 . ARG A 550 ? 0.497137  0.495995 0.618849 -0.0113617  0.00380845  0.0590667   550  ARG A NH1 
4495  N  NH2 . ARG A 550 ? 0.497872  0.50452  0.634475 -0.00647573 -0.00742468 0.0404247   550  ARG A NH2 
4496  N  N   . PRO A 551 ? 0.272827  0.319477 0.379707 -0.0166821  0.0266804   0.0505199   551  PRO A N   
4497  C  CA  . PRO A 551 ? 0.262956  0.312931 0.350287 -0.0133429  0.0278732   0.0519416   551  PRO A CA  
4498  C  C   . PRO A 551 ? 0.228814  0.275898 0.30544  -0.00811812 0.0199253   0.0498715   551  PRO A C   
4499  O  O   . PRO A 551 ? 0.220802  0.259368 0.297955 -0.00747909 0.0164101   0.0528194   551  PRO A O   
4500  C  CB  . PRO A 551 ? 0.309522  0.353202 0.386003 -0.0161717  0.035875    0.0624637   551  PRO A CB  
4501  C  CG  . PRO A 551 ? 0.326702  0.367689 0.420144 -0.0220696  0.0416459   0.0656798   551  PRO A CG  
4502  C  CD  . PRO A 551 ? 0.319931  0.359764 0.431555 -0.0220161  0.034211    0.0591328   551  PRO A CD  
4503  N  N   . TRP A 552 ? 0.209904  0.26387  0.277905 -0.00448132 0.0174136   0.0449531   552  TRP A N   
4504  C  CA  . TRP A 552 ? 0.219852  0.272321 0.280312 0.00010615  0.0104501   0.0422576   552  TRP A CA  
4505  C  C   . TRP A 552 ? 0.228341  0.272659 0.276428 0.00135989  0.00976839  0.0495038   552  TRP A C   
4506  O  O   . TRP A 552 ? 0.212496  0.252759 0.260163 0.00432219  0.00385996  0.0485407   552  TRP A O   
4507  C  CB  . TRP A 552 ? 0.202126  0.26276  0.255505 0.00316554  0.0089159   0.0367467   552  TRP A CB  
4508  C  CG  . TRP A 552 ? 0.220614  0.283236 0.26008  0.00333861  0.0133049   0.040195    552  TRP A CG  
4509  C  CD1 . TRP A 552 ? 0.214704  0.283017 0.253991 0.00167581  0.0189574   0.0396174   552  TRP A CD1 
4510  C  CD2 . TRP A 552 ? 0.224028  0.28376  0.248472 0.00580761  0.0116451   0.0432866   552  TRP A CD2 
4511  N  NE1 . TRP A 552 ? 0.253258  0.3217   0.277492 0.00288525  0.0211716   0.0421204   552  TRP A NE1 
4512  C  CE2 . TRP A 552 ? 0.235446  0.298989 0.250376 0.00539508  0.0163857   0.044133    552  TRP A CE2 
4513  C  CE3 . TRP A 552 ? 0.258952  0.313887 0.278053 0.008626    0.00617792  0.0446083   552  TRP A CE3 
4514  C  CZ2 . TRP A 552 ? 0.267208  0.329505 0.267033 0.00741328  0.0155696   0.0461819   552  TRP A CZ2 
4515  C  CZ3 . TRP A 552 ? 0.288025  0.34225  0.293074 0.0106867   0.00514681  0.0469184   552  TRP A CZ3 
4516  C  CH2 . TRP A 552 ? 0.288655  0.346509 0.283918 0.0100086   0.00958749  0.0474809   552  TRP A CH2 
4517  N  N   . GLN A 553 ? 0.23852   0.280406 0.276618 -0.00064941 0.0157154   0.0566406   553  GLN A N   
4518  C  CA  . GLN A 553 ? 0.252787  0.286808 0.277097 0.00096383  0.0144592   0.0638597   553  GLN A CA  
4519  C  C   . GLN A 553 ? 0.274838  0.298466 0.306117 0.00050863  0.0114876   0.0683825   553  GLN A C   
4520  O  O   . GLN A 553 ? 0.269123  0.286869 0.293089 0.00389742  0.00618537  0.0711954   553  GLN A O   
4521  C  CB  . GLN A 553 ? 0.262949  0.29571  0.273183 -0.00088906 0.0214885   0.0707276   553  GLN A CB  
4522  C  CG  . GLN A 553 ? 0.249931  0.29194  0.252223 0.00030239  0.0236807   0.0659123   553  GLN A CG  
4523  C  CD  . GLN A 553 ? 0.255808  0.305303 0.26784  -0.00291266 0.0304101   0.0625371   553  GLN A CD  
4524  O  OE1 . GLN A 553 ? 0.244172  0.295069 0.272661 -0.00531708 0.0310809   0.0602195   553  GLN A OE1 
4525  N  NE2 . GLN A 553 ? 0.230532  0.285807 0.233996 -0.00253105 0.0346018   0.060842    553  GLN A NE2 
4526  N  N   . GLU A 554 ? 0.267338  0.288352 0.3131   -0.00366975 0.0148912   0.0693773   554  GLU A N   
4527  C  CA  . GLU A 554 ? 0.293998  0.304473 0.349093 -0.00457183 0.0122799   0.0731067   554  GLU A CA  
4528  C  C   . GLU A 554 ? 0.276039  0.287032 0.342613 -0.00139726 0.00415313  0.064841    554  GLU A C   
4529  O  O   . GLU A 554 ? 0.281404  0.283613 0.35033  0.00056918  -0.00053396 0.0671328   554  GLU A O   
4530  C  CB  . GLU A 554 ? 0.354905  0.363059 0.424959 -0.0105893  0.0184947   0.0755117   554  GLU A CB  
4531  C  CG  . GLU A 554 ? 0.476614  0.484099 0.538211 -0.0146243  0.0283557   0.0837945   554  GLU A CG  
4532  C  CD  . GLU A 554 ? 0.612226  0.617307 0.690664 -0.0211546  0.0353598   0.0867446   554  GLU A CD  
4533  O  OE1 . GLU A 554 ? 0.660627  0.66383  0.758563 -0.0229165  0.032091    0.082355    554  GLU A OE1 
4534  O  OE2 . GLU A 554 ? 0.678895  0.684425 0.750957 -0.0246475  0.0446402   0.0931925   554  GLU A OE2 
4535  N  N   . VAL A 555 ? 0.26002   0.280672 0.334284 -0.00081552 0.00255179  0.0552611   555  VAL A N   
4536  C  CA  . VAL A 555 ? 0.252867  0.274925 0.333944 0.00295561  -0.00478159 0.0470029   555  VAL A CA  
4537  C  C   . VAL A 555 ? 0.24646   0.267723 0.315557 0.00821441  -0.00959452 0.0472154   555  VAL A C   
4538  O  O   . VAL A 555 ? 0.231481  0.247319 0.305066 0.011103    -0.0148926  0.0458512   555  VAL A O   
4539  C  CB  . VAL A 555 ? 0.234422  0.267124 0.321884 0.0029093   -0.00518898 0.0377445   555  VAL A CB  
4540  C  CG1 . VAL A 555 ? 0.228421  0.262696 0.321033 0.0068585   -0.0120307  0.0291003   555  VAL A CG1 
4541  C  CG2 . VAL A 555 ? 0.220834  0.254944 0.322788 -0.00214482 -0.00132265 0.0369233   555  VAL A CG2 
4542  N  N   . LEU A 556 ? 0.241235  0.267838 0.296321 0.00949     -0.00786176 0.0486402   556  LEU A N   
4543  C  CA  . LEU A 556 ? 0.234235  0.261035 0.278466 0.0139471   -0.0120899  0.0490459   556  LEU A CA  
4544  C  C   . LEU A 556 ? 0.278725  0.294734 0.31983  0.0153183   -0.0148535  0.0565767   556  LEU A C   
4545  O  O   . LEU A 556 ? 0.26922   0.282841 0.312546 0.0193335   -0.0207925  0.0545976   556  LEU A O   
4546  C  CB  . LEU A 556 ? 0.22594   0.259116 0.256422 0.0141625   -0.0092492  0.0499348   556  LEU A CB  
4547  C  CG  . LEU A 556 ? 0.225458  0.261001 0.24727  0.0185211   -0.0140224  0.0483191   556  LEU A CG  
4548  C  CD1 . LEU A 556 ? 0.205625  0.246284 0.235642 0.0214842   -0.0182644  0.0398228   556  LEU A CD1 
4549  C  CD2 . LEU A 556 ? 0.253588  0.295273 0.263157 0.0181329   -0.0109467  0.0483765   556  LEU A CD2 
4550  N  N   . LYS A 557 ? 0.287212  0.296429 0.323557 0.0120553   -0.010304   0.065445    557  LYS A N   
4551  C  CA  . LYS A 557 ? 0.367669  0.365316 0.399037 0.0133628   -0.0127456  0.0741191   557  LYS A CA  
4552  C  C   . LYS A 557 ? 0.342887  0.332702 0.389225 0.0144925   -0.0174279  0.0727366   557  LYS A C   
4553  O  O   . LYS A 557 ? 0.346107  0.330064 0.390913 0.0186875   -0.023421   0.0746646   557  LYS A O   
4554  C  CB  . LYS A 557 ? 0.420154  0.411753 0.44268  0.00922517  -0.00572112 0.0843197   557  LYS A CB  
4555  C  CG  . LYS A 557 ? 0.514848  0.493609 0.529494 0.0109424   -0.00844485 0.0943641   557  LYS A CG  
4556  C  CD  . LYS A 557 ? 0.647247  0.621439 0.648705 0.007091    -0.00044142 0.10446     557  LYS A CD  
4557  C  CE  . LYS A 557 ? 0.805212  0.765484 0.795922 0.00886291  -0.00289777 0.115909    557  LYS A CE  
4558  N  NZ  . LYS A 557 ? 0.857892  0.817686 0.842436 0.0155747   -0.0129429  0.113962    557  LYS A NZ  
4559  N  N   . ASP A 558 ? 0.308877  0.299057 0.370499 0.0111905   -0.0153771  0.068441    558  ASP A N   
4560  C  CA  . ASP A 558 ? 0.342544  0.325757 0.419329 0.0123734   -0.0200865  0.0653284   558  ASP A CA  
4561  C  C   . ASP A 558 ? 0.344409  0.332742 0.423267 0.0182226   -0.0269517  0.0565304   558  ASP A C   
4562  O  O   . ASP A 558 ? 0.380588  0.361898 0.466509 0.0214223   -0.0321657  0.0558355   558  ASP A O   
4563  C  CB  . ASP A 558 ? 0.384306  0.369503 0.477562 0.00806906  -0.0175334  0.0596324   558  ASP A CB  
4564  C  CG  . ASP A 558 ? 0.459988  0.438931 0.55813  0.00172102  -0.0107841  0.0674019   558  ASP A CG  
4565  O  OD1 . ASP A 558 ? 0.496145  0.467354 0.583444 0.00079553  -0.00779604 0.0783576   558  ASP A OD1 
4566  O  OD2 . ASP A 558 ? 0.480962  0.462954 0.593577 -0.0022423  -0.00850832 0.0624963   558  ASP A OD2 
4567  N  N   . MET A 559 ? 0.314251  0.314692 0.38804  0.0195083   -0.0265011  0.0496531   559  MET A N   
4568  C  CA  . MET A 559 ? 0.305956  0.31221  0.382757 0.0243432   -0.0314906  0.0408693   559  MET A CA  
4569  C  C   . MET A 559 ? 0.315557  0.320806 0.383533 0.0289438   -0.0355838  0.0440303   559  MET A C   
4570  O  O   . MET A 559 ? 0.285732  0.288865 0.360478 0.0331956   -0.0407529  0.0404716   559  MET A O   
4571  C  CB  . MET A 559 ? 0.28002   0.298642 0.354798 0.0242118   -0.0296043  0.0328124   559  MET A CB  
4572  C  CG  . MET A 559 ? 0.352211  0.374755 0.434176 0.0284327   -0.0339185  0.0231191   559  MET A CG  
4573  S  SD  . MET A 559 ? 0.408513  0.444327 0.480931 0.0286977   -0.0311382  0.0180794   559  MET A SD  
4574  C  CE  . MET A 559 ? 0.379311  0.420688 0.458388 0.0330141   -0.0343243  0.00665981  559  MET A CE  
4575  N  N   . VAL A 560 ? 0.286257  0.293541 0.34012  0.0282664   -0.0334939  0.0498087   560  VAL A N   
4576  C  CA  . VAL A 560 ? 0.318739  0.328771 0.36417  0.0325447   -0.0376624  0.0503665   560  VAL A CA  
4577  C  C   . VAL A 560 ? 0.347347  0.348116 0.382054 0.0328998   -0.0389232  0.0611792   560  VAL A C   
4578  O  O   . VAL A 560 ? 0.366231  0.367004 0.394708 0.0369514   -0.0440113  0.0627444   560  VAL A O   
4579  C  CB  . VAL A 560 ? 0.299375  0.321421 0.337442 0.0326779   -0.0358107  0.045281    560  VAL A CB  
4580  C  CG1 . VAL A 560 ? 0.292676  0.322853 0.339172 0.0319138   -0.0337486  0.0358569   560  VAL A CG1 
4581  C  CG2 . VAL A 560 ? 0.291438  0.315048 0.316214 0.029286    -0.0308005  0.0505273   560  VAL A CG2 
4582  N  N   . GLY A 561 ? 0.325989  0.318835 0.358648 0.028769    -0.0344223  0.0686952   561  GLY A N   
4583  C  CA  . GLY A 561 ? 0.343214  0.325645 0.364394 0.0291133   -0.0351643  0.0799824   561  GLY A CA  
4584  C  C   . GLY A 561 ? 0.361269  0.347866 0.363893 0.0281147   -0.0319686  0.0839764   561  GLY A C   
4585  O  O   . GLY A 561 ? 0.376065  0.355528 0.365357 0.0292521   -0.0332387  0.0926078   561  GLY A O   
4586  N  N   . LEU A 562 ? 0.354884  0.352499 0.355982 0.0260068   -0.0276827  0.0777829   562  LEU A N   
4587  C  CA  . LEU A 562 ? 0.39673   0.398337 0.381696 0.024705    -0.0238684  0.080436    562  LEU A CA  
4588  C  C   . LEU A 562 ? 0.364406  0.372434 0.353335 0.0198433   -0.0157723  0.0771428   562  LEU A C   
4589  O  O   . LEU A 562 ? 0.339305  0.352748 0.341677 0.0190678   -0.0155067  0.0697785   562  LEU A O   
4590  C  CB  . LEU A 562 ? 0.426012  0.436136 0.406884 0.0287346   -0.0292526  0.0740501   562  LEU A CB  
4591  C  CG  . LEU A 562 ? 0.503478  0.51874  0.468504 0.0280624   -0.0266333  0.0745508   562  LEU A CG  
4592  C  CD1 . LEU A 562 ? 0.473417  0.480094 0.421389 0.0292624   -0.0280779  0.0840906   562  LEU A CD1 
4593  C  CD2 . LEU A 562 ? 0.508027  0.532716 0.474974 0.0310094   -0.0312132  0.0663489   562  LEU A CD2 
4594  N  N   . ASP A 563 ? 0.360965  0.368945 0.338076 0.0169718   -0.00939773 0.0820121   563  ASP A N   
4595  C  CA  . ASP A 563 ? 0.352056  0.365888 0.335353 0.0124676   -0.00163982 0.0791254   563  ASP A CA  
4596  C  C   . ASP A 563 ? 0.341334  0.365785 0.318252 0.0128369   0.00034442  0.0730043   563  ASP A C   
4597  O  O   . ASP A 563 ? 0.3454    0.373968 0.322342 0.00960598  0.00729519  0.0724822   563  ASP A O   
4598  C  CB  . ASP A 563 ? 0.406419  0.413685 0.385134 0.00821652  0.00603648  0.0879629   563  ASP A CB  
4599  C  CG  . ASP A 563 ? 0.501969  0.507979 0.459527 0.0086723   0.00914402  0.0937104   563  ASP A CG  
4600  O  OD1 . ASP A 563 ? 0.486742  0.497306 0.434015 0.0122511   0.00466813  0.0901352   563  ASP A OD1 
4601  O  OD2 . ASP A 563 ? 0.610301  0.61121  0.561943 0.00527637  0.0164119   0.101266    563  ASP A OD2 
4602  N  N   . ALA A 564 ? 0.316545  0.345776 0.290162 0.0166084   -0.00547861 0.0678346   564  ALA A N   
4603  C  CA  . ALA A 564 ? 0.278583  0.316479 0.245851 0.017089    -0.00415891 0.0624673   564  ALA A CA  
4604  C  C   . ALA A 564 ? 0.26138   0.305126 0.234876 0.0202216   -0.010126   0.0549561   564  ALA A C   
4605  O  O   . ALA A 564 ? 0.244586  0.28545  0.221849 0.0230651   -0.0161491  0.0549474   564  ALA A O   
4606  C  CB  . ALA A 564 ? 0.295118  0.330746 0.243842 0.0182899   -0.00425645 0.0668877   564  ALA A CB  
4607  N  N   . LEU A 565 ? 0.244207  0.295861 0.217818 0.0198703   -0.00821513 0.0490377   565  LEU A N   
4608  C  CA  . LEU A 565 ? 0.256485  0.313768 0.233063 0.0224572   -0.0126747  0.0427831   565  LEU A CA  
4609  C  C   . LEU A 565 ? 0.290254  0.345871 0.257618 0.0252379   -0.0179445  0.0445524   565  LEU A C   
4610  O  O   . LEU A 565 ? 0.279122  0.33193  0.234047 0.0249636   -0.0169756  0.0486729   565  LEU A O   
4611  C  CB  . LEU A 565 ? 0.266428  0.330653 0.24168  0.0213031   -0.0090812  0.0379482   565  LEU A CB  
4612  C  CG  . LEU A 565 ? 0.327271  0.394449 0.310976 0.0191037   -0.00460851 0.0354222   565  LEU A CG  
4613  C  CD1 . LEU A 565 ? 0.327745  0.401039 0.30907  0.0190386   -0.00257809 0.0307978   565  LEU A CD1 
4614  C  CD2 . LEU A 565 ? 0.318218  0.385972 0.313477 0.0202699   -0.00781099 0.0320069   565  LEU A CD2 
4615  N  N   . ASP A 566 ? 0.262585  0.320267 0.236224 0.0281066   -0.0236374  0.0411041   566  ASP A N   
4616  C  CA  . ASP A 566 ? 0.268338  0.324967 0.235753 0.0311424   -0.0298725  0.0422934   566  ASP A CA  
4617  C  C   . ASP A 566 ? 0.249555  0.313432 0.226172 0.0330735   -0.0333527  0.0352126   566  ASP A C   
4618  O  O   . ASP A 566 ? 0.23789   0.303679 0.225914 0.03336     -0.0328191  0.0319292   566  ASP A O   
4619  C  CB  . ASP A 566 ? 0.315887  0.364705 0.285211 0.0332478   -0.0341239  0.0476403   566  ASP A CB  
4620  C  CG  . ASP A 566 ? 0.421998  0.469094 0.386214 0.0372608   -0.0421061  0.0492651   566  ASP A CG  
4621  O  OD1 . ASP A 566 ? 0.480736  0.531601 0.436157 0.0377936   -0.0438324  0.0475029   566  ASP A OD1 
4622  O  OD2 . ASP A 566 ? 0.492238  0.534473 0.462355 0.0401063   -0.0471352  0.0516118   566  ASP A OD2 
4623  N  N   . ALA A 567 ? 0.231438  0.299791 0.203224 0.0337915   -0.0356648  0.0323218   567  ALA A N   
4624  C  CA  . ALA A 567 ? 0.233517  0.309044 0.214395 0.0351459   -0.038484   0.0259272   567  ALA A CA  
4625  C  C   . ALA A 567 ? 0.226723  0.302033 0.214928 0.0389975   -0.0456811  0.0256174   567  ALA A C   
4626  O  O   . ALA A 567 ? 0.212819  0.294547 0.211441 0.0400737   -0.0471809  0.020174    567  ALA A O   
4627  C  CB  . ALA A 567 ? 0.239761  0.319749 0.214429 0.034263    -0.0387838  0.0226976   567  ALA A CB  
4628  N  N   . GLN A 568 ? 0.238082  0.306281 0.221226 0.0411903   -0.0500478  0.0313762   568  GLN A N   
4629  C  CA  . GLN A 568 ? 0.273065  0.340856 0.263532 0.0455242   -0.0578033  0.031093    568  GLN A CA  
4630  C  C   . GLN A 568 ? 0.23957   0.311138 0.246929 0.0468273   -0.0573163  0.0261576   568  GLN A C   
4631  O  O   . GLN A 568 ? 0.220865  0.29777  0.23825  0.0497345   -0.0618994  0.0218362   568  GLN A O   
4632  C  CB  . GLN A 568 ? 0.354556  0.412657 0.33671  0.0480751   -0.0628442  0.0389178   568  GLN A CB  
4633  C  CG  . GLN A 568 ? 0.445018  0.501475 0.411249 0.0488816   -0.0667023  0.0419741   568  GLN A CG  
4634  C  CD  . GLN A 568 ? 0.548331  0.612909 0.519821 0.0514068   -0.0734345  0.0357263   568  GLN A CD  
4635  O  OE1 . GLN A 568 ? 0.582502  0.649201 0.565592 0.0551312   -0.0798045  0.0335879   568  GLN A OE1 
4636  N  NE2 . GLN A 568 ? 0.626359  0.696146 0.591538 0.049231    -0.0717166  0.0319428   568  GLN A NE2 
4637  N  N   . PRO A 569 ? 0.215266  0.284012 0.227185 0.0453023   -0.0525135  0.026427    569  PRO A N   
4638  C  CA  . PRO A 569 ? 0.206203  0.278759 0.232784 0.0470056   -0.0522271  0.0208431   569  PRO A CA  
4639  C  C   . PRO A 569 ? 0.179288  0.262206 0.212156 0.0462532   -0.049524   0.0136775   569  PRO A C   
4640  O  O   . PRO A 569 ? 0.1702    0.258149 0.214597 0.0489782   -0.0517931  0.00900356  569  PRO A O   
4641  C  CB  . PRO A 569 ? 0.175436  0.242796 0.202693 0.0447844   -0.0474253  0.022381    569  PRO A CB  
4642  C  CG  . PRO A 569 ? 0.198546  0.256353 0.215296 0.0440722   -0.0488276  0.0309566   569  PRO A CG  
4643  C  CD  . PRO A 569 ? 0.204078  0.26523  0.208755 0.0425745   -0.0482365  0.0320889   569  PRO A CD  
4644  N  N   . LEU A 570 ? 0.15562   0.241339 0.181464 0.0426522   -0.0444818  0.0130623   570  LEU A N   
4645  C  CA  . LEU A 570 ? 0.151547  0.245889 0.182619 0.0415472   -0.0415234  0.00727477  570  LEU A CA  
4646  C  C   . LEU A 570 ? 0.151627  0.251125 0.187037 0.0433318   -0.0467145  0.00493434  570  LEU A C   
4647  O  O   . LEU A 570 ? 0.147473  0.25414  0.194174 0.0442243   -0.0463818  -0.00026278 570  LEU A O   
4648  C  CB  . LEU A 570 ? 0.133996  0.228808 0.156453 0.0377131   -0.03597    0.0078098   570  LEU A CB  
4649  C  CG  . LEU A 570 ? 0.15445   0.256464 0.180719 0.0359845   -0.0322048  0.00303059  570  LEU A CG  
4650  C  CD1 . LEU A 570 ? 0.14092   0.241089 0.159376 0.0329601   -0.0268247  0.00435835  570  LEU A CD1 
4651  C  CD2 . LEU A 570 ? 0.147405  0.253345 0.17385  0.0357794   -0.035477   0.00138781  570  LEU A CD2 
4652  N  N   . LEU A 571 ? 0.159178  0.255549 0.185958 0.0439516   -0.0517137  0.00841482  571  LEU A N   
4653  C  CA  . LEU A 571 ? 0.167316  0.268778 0.198778 0.0460019   -0.0581312  0.00563175  571  LEU A CA  
4654  C  C   . LEU A 571 ? 0.167872  0.27172  0.213135 0.050333    -0.063375   0.00345857  571  LEU A C   
4655  O  O   . LEU A 571 ? 0.169633  0.281722 0.226849 0.0515183   -0.065866   -0.00186556 571  LEU A O   
4656  C  CB  . LEU A 571 ? 0.187391  0.28437  0.205341 0.0466658   -0.0636073  0.009667    571  LEU A CB  
4657  C  CG  . LEU A 571 ? 0.216301  0.311871 0.221343 0.0427478   -0.0585108  0.0106492   571  LEU A CG  
4658  C  CD1 . LEU A 571 ? 0.252932  0.342963 0.241492 0.0435296   -0.0627928  0.0150218   571  LEU A CD1 
4659  C  CD2 . LEU A 571 ? 0.212569  0.31578  0.223699 0.0401567   -0.05551    0.0045623   571  LEU A CD2 
4660  N  N   . LYS A 572 ? 0.171457  0.267915 0.215709 0.0527821   -0.0655161  0.0076281   572  LYS A N   
4661  C  CA  . LYS A 572 ? 0.201794  0.298827 0.259089 0.057386    -0.0704855  0.00591403  572  LYS A CA  
4662  C  C   . LYS A 572 ? 0.185391  0.29058  0.257631 0.0572854   -0.065324   -0.0012613  572  LYS A C   
4663  O  O   . LYS A 572 ? 0.169646  0.281934 0.25593  0.0601578   -0.0683725  -0.00617292 572  LYS A O   
4664  C  CB  . LYS A 572 ? 0.260338  0.346166 0.312568 0.0591609   -0.0724727  0.0122707   572  LYS A CB  
4665  C  CG  . LYS A 572 ? 0.390734  0.475561 0.455987 0.0645597   -0.078768   0.0110354   572  LYS A CG  
4666  C  CD  . LYS A 572 ? 0.550013  0.621954 0.608272 0.065216    -0.0797989  0.0184315   572  LYS A CD  
4667  C  CE  . LYS A 572 ? 0.663255  0.730997 0.733934 0.0704781   -0.085372   0.0181611   572  LYS A CE  
4668  N  NZ  . LYS A 572 ? 0.683072  0.739722 0.750226 0.0691405   -0.0825061  0.0230739   572  LYS A NZ  
4669  N  N   . TYR A 573 ? 0.151654  0.256492 0.2206   0.0539654   -0.0573401  -0.00209741 573  TYR A N   
4670  C  CA  . TYR A 573 ? 0.144148  0.255837 0.224354 0.0540282   -0.0519226  -0.0084471  573  TYR A CA  
4671  C  C   . TYR A 573 ? 0.136427  0.258671 0.22455  0.0528906   -0.0503469  -0.0134574  573  TYR A C   
4672  O  O   . TYR A 573 ? 0.138541  0.268025 0.240453 0.0546985   -0.0487118  -0.0190111  573  TYR A O   
4673  C  CB  . TYR A 573 ? 0.12235   0.230937 0.194204 0.050603    -0.0447089  -0.00756213 573  TYR A CB  
4674  C  CG  . TYR A 573 ? 0.109409  0.223831 0.188007 0.0502854   -0.038214   -0.0134052  573  TYR A CG  
4675  C  CD1 . TYR A 573 ? 0.0989031 0.221211 0.179585 0.0479837   -0.0332807  -0.0167145  573  TYR A CD1 
4676  C  CD2 . TYR A 573 ? 0.105388  0.21656  0.187058 0.0521332   -0.0369687  -0.0152934  573  TYR A CD2 
4677  C  CE1 . TYR A 573 ? 0.103452  0.230243 0.187815 0.0477537   -0.0267789  -0.0212068  573  TYR A CE1 
4678  C  CE2 . TYR A 573 ? 0.105734  0.22184  0.191341 0.0522706   -0.0311388  -0.0208662  573  TYR A CE2 
4679  C  CZ  . TYR A 573 ? 0.106729  0.230466 0.192422 0.0500221   -0.0257862  -0.0233032  573  TYR A CZ  
4680  O  OH  . TYR A 573 ? 0.120931  0.248742 0.207653 0.0500356   -0.0194413  -0.0278637  573  TYR A OH  
4681  N  N   . PHE A 574 ? 0.117483  0.24056  0.197444 0.0496146   -0.0498608  -0.01187    574  PHE A N   
4682  C  CA  . PHE A 574 ? 0.124149  0.25604  0.210881 0.0473254   -0.0473686  -0.0162242  574  PHE A CA  
4683  C  C   . PHE A 574 ? 0.134379  0.271146 0.229355 0.0494141   -0.0553661  -0.0182533  574  PHE A C   
4684  O  O   . PHE A 574 ? 0.13225   0.277175 0.236556 0.0475612   -0.0536495  -0.0226769  574  PHE A O   
4685  C  CB  . PHE A 574 ? 0.118174  0.248827 0.193877 0.042554    -0.0425038  -0.0146561  574  PHE A CB  
4686  C  CG  . PHE A 574 ? 0.116627  0.246189 0.188984 0.0405245   -0.0341313  -0.0147614  574  PHE A CG  
4687  C  CD1 . PHE A 574 ? 0.118591  0.255074 0.200411 0.039751    -0.0281739  -0.0191763  574  PHE A CD1 
4688  C  CD2 . PHE A 574 ? 0.118142  0.240161 0.177917 0.0393737   -0.0321937  -0.010541   574  PHE A CD2 
4689  C  CE1 . PHE A 574 ? 0.118239  0.253378 0.194996 0.0383267   -0.0210559  -0.0191472  574  PHE A CE1 
4690  C  CE2 . PHE A 574 ? 0.110783  0.23202  0.167681 0.0380283   -0.0257135  -0.0110454  574  PHE A CE2 
4691  C  CZ  . PHE A 574 ? 0.105162  0.232646 0.169117 0.0374926   -0.0203183  -0.0151631  574  PHE A CZ  
4692  N  N   . GLN A 575 ? 0.144136  0.276181 0.237085 0.0533618   -0.0639445  -0.0152848  575  GLN A N   
4693  C  CA  . GLN A 575 ? 0.173174  0.308305 0.26976  0.0555837   -0.0731166  -0.0163087  575  GLN A CA  
4694  C  C   . GLN A 575 ? 0.14928   0.296779 0.266178 0.0560777   -0.0739749  -0.0237466  575  GLN A C   
4695  O  O   . GLN A 575 ? 0.142578  0.295181 0.262227 0.0546273   -0.0776022  -0.026437   575  GLN A O   
4696  C  CB  . GLN A 575 ? 0.245336  0.373472 0.339935 0.060903    -0.0814237  -0.0121142  575  GLN A CB  
4697  C  CG  . GLN A 575 ? 0.38404   0.513589 0.479729 0.0643919   -0.0927876  -0.0120844  575  GLN A CG  
4698  C  CD  . GLN A 575 ? 0.513604  0.633831 0.604027 0.0696543   -0.100784   -0.00616567 575  GLN A CD  
4699  O  OE1 . GLN A 575 ? 0.64946   0.762849 0.738734 0.0706092   -0.0976513  -0.00290638 575  GLN A OE1 
4700  N  NE2 . GLN A 575 ? 0.644593  0.76353  0.730665 0.0730447   -0.111375   -0.0043978  575  GLN A NE2 
4701  N  N   . LEU A 576 ? 0.142929  0.29578  0.275085 0.0580428   -0.0705597  -0.0276909  576  LEU A N   
4702  C  CA  . LEU A 576 ? 0.145683  0.311299 0.299346 0.0584429   -0.0701754  -0.035001   576  LEU A CA  
4703  C  C   . LEU A 576 ? 0.136385  0.308458 0.292533 0.0524759   -0.0625655  -0.0380321  576  LEU A C   
4704  O  O   . LEU A 576 ? 0.13167   0.311476 0.299132 0.051499    -0.0659076  -0.0420923  576  LEU A O   
4705  C  CB  . LEU A 576 ? 0.14118   0.310958 0.30877  0.0613024   -0.0655925  -0.0387677  576  LEU A CB  
4706  C  CG  . LEU A 576 ? 0.167499  0.332746 0.339473 0.0678947   -0.0737228  -0.0375528  576  LEU A CG  
4707  C  CD1 . LEU A 576 ? 0.158129  0.326464 0.341363 0.0700362   -0.0670616  -0.041866   576  LEU A CD1 
4708  C  CD2 . LEU A 576 ? 0.181496  0.353253 0.367309 0.0716747   -0.0843551  -0.0404312  576  LEU A CD2 
4709  N  N   . VAL A 577 ? 0.130401  0.29838  0.27527  0.0484517   -0.0530361  -0.0356902  577  VAL A N   
4710  C  CA  . VAL A 577 ? 0.12507   0.297603 0.271726 0.0429372   -0.0458319  -0.037685   577  VAL A CA  
4711  C  C   . VAL A 577 ? 0.133398  0.301519 0.268158 0.0401841   -0.050012   -0.0353848  577  VAL A C   
4712  O  O   . VAL A 577 ? 0.133849  0.306891 0.274931 0.0364596   -0.0479627  -0.0383699  577  VAL A O   
4713  C  CB  . VAL A 577 ? 0.117704  0.288257 0.258262 0.0402836   -0.034431   -0.0364905  577  VAL A CB  
4714  C  CG1 . VAL A 577 ? 0.111957  0.271643 0.231214 0.0386345   -0.032878   -0.0305711  577  VAL A CG1 
4715  C  CG2 . VAL A 577 ? 0.114909  0.292523 0.264122 0.0356085   -0.0257175  -0.0395167  577  VAL A CG2 
4716  N  N   . THR A 578 ? 0.139159  0.297925 0.257018 0.0418524   -0.0552943  -0.0302996  578  THR A N   
4717  C  CA  . THR A 578 ? 0.147526  0.302765 0.254264 0.0400467   -0.0597637  -0.0290121  578  THR A CA  
4718  C  C   . THR A 578 ? 0.156906  0.319821 0.276637 0.0410898   -0.068055   -0.0341741  578  THR A C   
4719  O  O   . THR A 578 ? 0.155462  0.321334 0.277233 0.0376858   -0.068273   -0.0373161  578  THR A O   
4720  C  CB  . THR A 578 ? 0.161416  0.306296 0.249518 0.0424402   -0.0641925  -0.0227804  578  THR A CB  
4721  O  OG1 . THR A 578 ? 0.168734  0.307659 0.247326 0.0408745   -0.056356   -0.0189267  578  THR A OG1 
4722  C  CG2 . THR A 578 ? 0.1747    0.315901 0.249584 0.0411648   -0.0687494  -0.0217417  578  THR A CG2 
4723  N  N   . GLN A 579 ? 0.163962  0.329579 0.292607 0.046076    -0.0755972  -0.0351556  579  GLN A N   
4724  C  CA  . GLN A 579 ? 0.182171  0.355528 0.324248 0.0479015   -0.0849384  -0.0402962  579  GLN A CA  
4725  C  C   . GLN A 579 ? 0.162325  0.347581 0.326738 0.0443708   -0.0793979  -0.0472324  579  GLN A C   
4726  O  O   . GLN A 579 ? 0.166208  0.357048 0.338701 0.0422053   -0.0832691  -0.0518422  579  GLN A O   
4727  C  CB  . GLN A 579 ? 0.212933  0.385041 0.358411 0.0547005   -0.0942082  -0.0387601  579  GLN A CB  
4728  C  CG  . GLN A 579 ? 0.29788   0.479717 0.461676 0.0576947   -0.104451   -0.0448219  579  GLN A CG  
4729  C  CD  . GLN A 579 ? 0.39717   0.576961 0.550448 0.0580953   -0.114747   -0.0451586  579  GLN A CD  
4730  O  OE1 . GLN A 579 ? 0.536427  0.724823 0.704258 0.0594112   -0.123116   -0.0511658  579  GLN A OE1 
4731  N  NE2 . GLN A 579 ? 0.376118  0.544941 0.504478 0.0572671   -0.114678   -0.03921    579  GLN A NE2 
4732  N  N   . TRP A 580 ? 0.137221  0.326421 0.311721 0.0434382   -0.0698433  -0.0482325  580  TRP A N   
4733  C  CA  . TRP A 580 ? 0.128981  0.329544 0.324799 0.0399523   -0.0634499  -0.0542437  580  TRP A CA  
4734  C  C   . TRP A 580 ? 0.130612  0.330271 0.322376 0.0332972   -0.0573274  -0.0545816  580  TRP A C   
4735  O  O   . TRP A 580 ? 0.118117  0.325938 0.326197 0.030165    -0.0573271  -0.0598025  580  TRP A O   
4736  C  CB  . TRP A 580 ? 0.13416   0.337845 0.33754  0.0406028   -0.0534655  -0.0546282  580  TRP A CB  
4737  C  CG  . TRP A 580 ? 0.152639  0.368415 0.378274 0.0373682   -0.0454215  -0.0603815  580  TRP A CG  
4738  C  CD1 . TRP A 580 ? 0.155528  0.383109 0.405435 0.0396846   -0.048128   -0.0665634  580  TRP A CD1 
4739  C  CD2 . TRP A 580 ? 0.150489  0.367522 0.376295 0.0312542   -0.0328517  -0.0600814  580  TRP A CD2 
4740  N  NE1 . TRP A 580 ? 0.158224  0.39478  0.423745 0.0349626   -0.037345   -0.0702288  580  TRP A NE1 
4741  C  CE2 . TRP A 580 ? 0.156366  0.386217 0.406939 0.0297586   -0.0278535  -0.0660041  580  TRP A CE2 
4742  C  CE3 . TRP A 580 ? 0.161109  0.369601 0.368997 0.0270762   -0.025382   -0.0551991  580  TRP A CE3 
4743  C  CZ2 . TRP A 580 ? 0.153941  0.38739  0.410185 0.0239489   -0.0150514  -0.0664028  580  TRP A CZ2 
4744  C  CZ3 . TRP A 580 ? 0.15524   0.36673  0.368088 0.0219619   -0.0135517  -0.0554728  580  TRP A CZ3 
4745  C  CH2 . TRP A 580 ? 0.155984  0.379457 0.392236 0.0201101   -0.00842985 -0.0607357  580  TRP A CH2 
4746  N  N   . LEU A 581 ? 0.123492  0.313176 0.294852 0.0309973   -0.0515263  -0.0491199  581  LEU A N   
4747  C  CA  . LEU A 581 ? 0.131298  0.318724 0.298208 0.0251935   -0.045612   -0.048966   581  LEU A CA  
4748  C  C   . LEU A 581 ? 0.154899  0.341962 0.320388 0.02416     -0.0546046  -0.0518136  581  LEU A C   
4749  O  O   . LEU A 581 ? 0.155814  0.346348 0.330675 0.0195146   -0.0521187  -0.0554641  581  LEU A O   
4750  C  CB  . LEU A 581 ? 0.144953  0.322079 0.291226 0.0239383   -0.0387115  -0.0427839  581  LEU A CB  
4751  C  CG  . LEU A 581 ? 0.141648  0.319386 0.289197 0.0233576   -0.0280313  -0.0409677  581  LEU A CG  
4752  C  CD1 . LEU A 581 ? 0.142656  0.310011 0.269183 0.0241912   -0.0254736  -0.0350538  581  LEU A CD1 
4753  C  CD2 . LEU A 581 ? 0.144084  0.325262 0.300099 0.0177197   -0.0192619  -0.0425655  581  LEU A CD2 
4754  N  N   . GLN A 582 ? 0.154222  0.336777 0.307895 0.0284463   -0.06492    -0.0502424  582  GLN A N   
4755  C  CA  . GLN A 582 ? 0.196191  0.378187 0.346065 0.0282177   -0.0741387  -0.0533247  582  GLN A CA  
4756  C  C   . GLN A 582 ? 0.200788  0.394501 0.374935 0.0279537   -0.0801028  -0.0610421  582  GLN A C   
4757  O  O   . GLN A 582 ? 0.196277  0.393006 0.377705 0.0240655   -0.0813869  -0.0660107  582  GLN A O   
4758  C  CB  . GLN A 582 ? 0.265     0.439498 0.396053 0.033503    -0.0827117  -0.0488244  582  GLN A CB  
4759  C  CG  . GLN A 582 ? 0.4013    0.574109 0.5235   0.0349543   -0.0938617  -0.051284   582  GLN A CG  
4760  C  CD  . GLN A 582 ? 0.498727  0.662834 0.599922 0.0399938   -0.100248   -0.0451261  582  GLN A CD  
4761  O  OE1 . GLN A 582 ? 0.53526   0.690694 0.619299 0.0395342   -0.0942659  -0.0389228  582  GLN A OE1 
4762  N  NE2 . GLN A 582 ? 0.48861   0.655002 0.592016 0.0449446   -0.112274   -0.0464505  582  GLN A NE2 
4763  N  N   . GLU A 583 ? 0.180585  0.381311 0.369518 0.0316962   -0.082692   -0.0625173  583  GLU A N   
4764  C  CA  . GLU A 583 ? 0.196786  0.410106 0.411847 0.0316984   -0.0882323  -0.070296   583  GLU A CA  
4765  C  C   . GLU A 583 ? 0.176287  0.396793 0.409992 0.0249308   -0.0773071  -0.074208   583  GLU A C   
4766  O  O   . GLU A 583 ? 0.181066  0.408198 0.430121 0.0216633   -0.0805606  -0.0804618  583  GLU A O   
4767  C  CB  . GLU A 583 ? 0.226688  0.446817 0.456416 0.0371945   -0.0917364  -0.0714262  583  GLU A CB  
4768  C  CG  . GLU A 583 ? 0.322679  0.537504 0.54044  0.0445238   -0.104378   -0.068353   583  GLU A CG  
4769  C  CD  . GLU A 583 ? 0.390147  0.607825 0.618038 0.0499326   -0.104354   -0.0673279  583  GLU A CD  
4770  O  OE1 . GLU A 583 ? 0.424586  0.647921 0.666268 0.0484645   -0.0939517  -0.0688481  583  GLU A OE1 
4771  O  OE2 . GLU A 583 ? 0.397043  0.610315 0.617511 0.0560355   -0.114955   -0.064707   583  GLU A OE2 
4772  N  N   . GLN A 584 ? 0.16397   0.38234  0.395289 0.0224226   -0.0640287  -0.0703176  584  GLN A N   
4773  C  CA  . GLN A 584 ? 0.161828  0.38541  0.408054 0.0158957   -0.0528303  -0.0726321  584  GLN A CA  
4774  C  C   . GLN A 584 ? 0.158227  0.37613  0.397495 0.0104958   -0.0520962  -0.0730859  584  GLN A C   
4775  O  O   . GLN A 584 ? 0.138441  0.362211 0.395498 0.00531451  -0.0488286  -0.0775883  584  GLN A O   
4776  C  CB  . GLN A 584 ? 0.188357  0.409247 0.428949 0.0148277   -0.0391609  -0.0676695  584  GLN A CB  
4777  C  CG  . GLN A 584 ? 0.195818  0.423548 0.447084 0.0195397   -0.0380359  -0.0687723  584  GLN A CG  
4778  C  CD  . GLN A 584 ? 0.255377  0.497719 0.537029 0.018351    -0.0373215  -0.0759878  584  GLN A CD  
4779  O  OE1 . GLN A 584 ? 0.233339  0.480738 0.52782  0.0125106   -0.0274454  -0.0777278  584  GLN A OE1 
4780  N  NE2 . GLN A 584 ? 0.30318   0.552179 0.597052 0.0237386   -0.048235   -0.0801377  584  GLN A NE2 
4781  N  N   . ASN A 585 ? 0.136871  0.342951 0.350916 0.0112385   -0.0532458  -0.0681465  585  ASN A N   
4782  C  CA  . ASN A 585 ? 0.156237  0.35663  0.364345 0.00635984  -0.051352   -0.0688182  585  ASN A CA  
4783  C  C   . ASN A 585 ? 0.175443  0.380857 0.394496 0.00587852  -0.0627891  -0.0765031  585  ASN A C   
4784  O  O   . ASN A 585 ? 0.178636  0.385108 0.407933 0.00058014  -0.0606628  -0.0805096  585  ASN A O   
4785  C  CB  . ASN A 585 ? 0.136274  0.32415  0.31648  0.00798926  -0.0507606  -0.0626689  585  ASN A CB  
4786  C  CG  . ASN A 585 ? 0.133082  0.315745 0.304314 0.00686298  -0.0387737  -0.0561528  585  ASN A CG  
4787  O  OD1 . ASN A 585 ? 0.135758  0.321617 0.318744 0.00287937  -0.0294023  -0.0562153  585  ASN A OD1 
4788  N  ND2 . ASN A 585 ? 0.122221  0.296059 0.271857 0.00965598  -0.038579   -0.0505416  585  ASN A ND2 
4789  N  N   . GLN A 586 ? 0.208907  0.417119 0.426033 0.0115738   -0.0751705  -0.0785376  586  GLN A N   
4790  C  CA  . GLN A 586 ? 0.278251  0.491992 0.505286 0.0121985   -0.0878183  -0.0862898  586  GLN A CA  
4791  C  C   . GLN A 586 ? 0.27525   0.502073 0.535035 0.00845547  -0.0867752  -0.0936647  586  GLN A C   
4792  O  O   . GLN A 586 ? 0.246886  0.476695 0.518798 0.00411     -0.0894223  -0.100091   586  GLN A O   
4793  C  CB  . GLN A 586 ? 0.345954  0.559611 0.563315 0.0197012   -0.101492   -0.0860317  586  GLN A CB  
4794  C  CG  . GLN A 586 ? 0.49335   0.69413  0.678669 0.0226747   -0.103558   -0.0796663  586  GLN A CG  
4795  C  CD  . GLN A 586 ? 0.63173   0.831214 0.805807 0.0295759   -0.117694   -0.0793203  586  GLN A CD  
4796  O  OE1 . GLN A 586 ? 0.680289  0.888186 0.869452 0.0320335   -0.128522   -0.0854008  586  GLN A OE1 
4797  N  NE2 . GLN A 586 ? 0.629533  0.818295 0.777033 0.0326435   -0.117812   -0.0721646  586  GLN A NE2 
4798  N  N   . GLN A 587 ? 0.282211  0.517298 0.557927 0.010026    -0.0826592  -0.093279   587  GLN A N   
4799  C  CA  . GLN A 587 ? 0.2918    0.540423 0.600214 0.00650513  -0.0807633  -0.100312   587  GLN A CA  
4800  C  C   . GLN A 587 ? 0.285349  0.532587 0.601924 -0.00199726 -0.0683235  -0.100502   587  GLN A C   
4801  O  O   . GLN A 587 ? 0.239733  0.495458 0.580979 -0.00672987 -0.0684216  -0.107247   587  GLN A O   
4802  C  CB  . GLN A 587 ? 0.326796  0.583423 0.648434 0.00954302  -0.075423   -0.099062   587  GLN A CB  
4803  C  CG  . GLN A 587 ? 0.491065  0.754855 0.821218 0.0169192   -0.0895194  -0.102841   587  GLN A CG  
4804  C  CD  . GLN A 587 ? 0.560292  0.826079 0.891494 0.0218005   -0.0848567  -0.0991592  587  GLN A CD  
4805  O  OE1 . GLN A 587 ? 0.6073    0.879717 0.953878 0.0191529   -0.0726823  -0.0996173  587  GLN A OE1 
4806  N  NE2 . GLN A 587 ? 0.56546   0.824576 0.878914 0.0288584   -0.0939426  -0.0952344  587  GLN A NE2 
4807  N  N   . ASN A 588 ? 0.266455  0.502838 0.563138 -0.00393105 -0.057529   -0.092876   588  ASN A N   
4808  C  CA  . ASN A 588 ? 0.26773   0.501996 0.572048 -0.0115969  -0.0454121  -0.0920273  588  ASN A CA  
4809  C  C   . ASN A 588 ? 0.261451  0.488029 0.558253 -0.014859   -0.0502938  -0.0946564  588  ASN A C   
4810  O  O   . ASN A 588 ? 0.286055  0.509115 0.588535 -0.0211688  -0.0415585  -0.0940154  588  ASN A O   
4811  C  CB  . ASN A 588 ? 0.299135  0.525465 0.587492 -0.0125076  -0.0315144  -0.0830977  588  ASN A CB  
4812  C  CG  . ASN A 588 ? 0.345881  0.579661 0.642325 -0.00995781 -0.0247942  -0.0812265  588  ASN A CG  
4813  O  OD1 . ASN A 588 ? 0.395105  0.622713 0.675162 -0.00840289 -0.0169131  -0.074571   588  ASN A OD1 
4814  N  ND2 . ASN A 588 ? 0.327207  0.574262 0.648344 -0.0089217  -0.0283627  -0.0874441  588  ASN A ND2 
4815  N  N   . GLY A 589 ? 0.284067  0.50654  0.56539  -0.0103473  -0.0632716  -0.0967695  589  GLY A N   
4816  C  CA  . GLY A 589 ? 0.263979  0.478852 0.535684 -0.0125481  -0.0684084  -0.100011   589  GLY A CA  
4817  C  C   . GLY A 589 ? 0.299948  0.50128  0.549252 -0.0143065  -0.0592078  -0.0928833  589  GLY A C   
4818  O  O   . GLY A 589 ? 0.292908  0.488653 0.543362 -0.0189877  -0.0565923  -0.0949426  589  GLY A O   
4819  N  N   . GLU A 590 ? 0.241203  0.437196 0.47128  -0.0104686  -0.0545818  -0.0848204  590  GLU A N   
4820  C  CA  . GLU A 590 ? 0.257678  0.441908 0.468747 -0.0119526  -0.0458615  -0.0782035  590  GLU A CA  
4821  C  C   . GLU A 590 ? 0.263024  0.43867  0.454061 -0.00991181 -0.0532251  -0.0795733  590  GLU A C   
4822  O  O   . GLU A 590 ? 0.270585  0.448187 0.45582  -0.00594994 -0.0646241  -0.0833991  590  GLU A O   
4823  C  CB  . GLU A 590 ? 0.239366  0.420292 0.434186 -0.00775072 -0.0410128  -0.0701435  590  GLU A CB  
4824  C  CG  . GLU A 590 ? 0.237295  0.423678 0.445267 -0.00967071 -0.0304756  -0.0671733  590  GLU A CG  
4825  C  CD  . GLU A 590 ? 0.271866  0.458061 0.493146 -0.0163821  -0.0192427  -0.0665101  590  GLU A CD  
4826  O  OE1 . GLU A 590 ? 0.258235  0.437724 0.478305 -0.02058    -0.0165206  -0.0666878  590  GLU A OE1 
4827  O  OE2 . GLU A 590 ? 0.287434  0.481026 0.522079 -0.0172381  -0.0126784  -0.0658288  590  GLU A OE2 
4828  N  N   . VAL A 591 ? 0.296968  0.463068 0.478036 -0.0126774  -0.046596   -0.0768005  591  VAL A N   
4829  C  CA  . VAL A 591 ? 0.325908  0.483364 0.48481  -0.00993535 -0.0511643  -0.0766298  591  VAL A CA  
4830  C  C   . VAL A 591 ? 0.290992  0.442638 0.429578 -0.0062712  -0.0460265  -0.0678176  591  VAL A C   
4831  O  O   . VAL A 591 ? 0.319613  0.468407 0.457939 -0.00795547 -0.0361061  -0.0620073  591  VAL A O   
4832  C  CB  . VAL A 591 ? 0.350643  0.501252 0.511423 -0.0143544  -0.0487261  -0.0802351  591  VAL A CB  
4833  C  CG1 . VAL A 591 ? 0.39021   0.533503 0.529762 -0.0111685  -0.0544164  -0.0821039  591  VAL A CG1 
4834  C  CG2 . VAL A 591 ? 0.393622  0.550846 0.578143 -0.018533   -0.053637   -0.0893254  591  VAL A CG2 
4835  N  N   . LEU A 592 ? 0.259531  0.409421 0.381037 -0.00119559 -0.0528071  -0.0666022  592  LEU A N   
4836  C  CA  . LEU A 592 ? 0.278769  0.423044 0.382758 0.00171493  -0.0478125  -0.0586447  592  LEU A CA  
4837  C  C   . LEU A 592 ? 0.286487  0.421517 0.377172 0.00046524  -0.0435499  -0.0574043  592  LEU A C   
4838  O  O   . LEU A 592 ? 0.319987  0.452736 0.407888 -0.00017885 -0.0482281  -0.0629366  592  LEU A O   
4839  C  CB  . LEU A 592 ? 0.290385  0.435397 0.381744 0.00721514  -0.0554934  -0.0568166  592  LEU A CB  
4840  C  CG  . LEU A 592 ? 0.366623  0.520461 0.471871 0.00926149  -0.0601827  -0.0579493  592  LEU A CG  
4841  C  CD1 . LEU A 592 ? 0.371736  0.523746 0.462633 0.0148293   -0.0660861  -0.0539604  592  LEU A CD1 
4842  C  CD2 . LEU A 592 ? 0.340268  0.498038 0.459609 0.00701596  -0.0508142  -0.0551515  592  LEU A CD2 
4843  N  N   . GLY A 593 ? 0.244786  0.374847 0.328861 0.00011697  -0.0348207  -0.0509161  593  GLY A N   
4844  C  CA  . GLY A 593 ? 0.22515   0.346795 0.298291 -0.000642   -0.0309148  -0.0498561  593  GLY A CA  
4845  C  C   . GLY A 593 ? 0.19459   0.31367  0.280442 -0.00548767 -0.0254331  -0.0516922  593  GLY A C   
4846  O  O   . GLY A 593 ? 0.172172  0.295952 0.274924 -0.00870978 -0.023096   -0.0527482  593  GLY A O   
4847  N  N   . TRP A 594 ? 0.174842  0.286011 0.252795 -0.00597879 -0.0225387  -0.0514936  594  TRP A N   
4848  C  CA  . TRP A 594 ? 0.168827  0.275249 0.256897 -0.0101548  -0.0165287  -0.0514798  594  TRP A CA  
4849  C  C   . TRP A 594 ? 0.192812  0.293686 0.278746 -0.0108545  -0.0197877  -0.0578471  594  TRP A C   
4850  O  O   . TRP A 594 ? 0.217763  0.310999 0.294979 -0.0099564  -0.0161387  -0.055867   594  TRP A O   
4851  C  CB  . TRP A 594 ? 0.168273  0.269229 0.249596 -0.00963527 -0.00801163 -0.0431743  594  TRP A CB  
4852  C  CG  . TRP A 594 ? 0.161599  0.260235 0.225103 -0.00509379 -0.00844173 -0.0393707  594  TRP A CG  
4853  C  CD1 . TRP A 594 ? 0.164701  0.256781 0.217111 -0.00327125 -0.0074772  -0.0389246  594  TRP A CD1 
4854  C  CD2 . TRP A 594 ? 0.166478  0.269635 0.222896 -0.00193382 -0.00973373 -0.0357086  594  TRP A CD2 
4855  N  NE1 . TRP A 594 ? 0.167688  0.260457 0.207288 0.00039407  -0.00771797 -0.0350843  594  TRP A NE1 
4856  C  CE2 . TRP A 594 ? 0.161911  0.260921 0.203391 0.0012164   -0.00938104 -0.0330584  594  TRP A CE2 
4857  C  CE3 . TRP A 594 ? 0.180916  0.291302 0.243547 -0.00145107 -0.0111727  -0.0348388  594  TRP A CE3 
4858  C  CZ2 . TRP A 594 ? 0.161743  0.262894 0.194339 0.00435247  -0.0102862  -0.0291982  594  TRP A CZ2 
4859  C  CZ3 . TRP A 594 ? 0.185337  0.297368 0.238657 0.00210767  -0.012365   -0.0311572  594  TRP A CZ3 
4860  C  CH2 . TRP A 594 ? 0.164788  0.271994 0.203226 0.00477286  -0.0120386  -0.0282798  594  TRP A CH2 
4861  N  N   . PRO A 595 ? 0.20229   0.306857 0.296483 -0.0121916  -0.0270132  -0.0662401  595  PRO A N   
4862  C  CA  . PRO A 595 ? 0.21274   0.312229 0.304149 -0.0124762  -0.0309277  -0.0737519  595  PRO A CA  
4863  C  C   . PRO A 595 ? 0.239098  0.330306 0.339263 -0.016155   -0.0250262  -0.074173   595  PRO A C   
4864  O  O   . PRO A 595 ? 0.229916  0.314991 0.324844 -0.0154658  -0.0264716  -0.0790125  595  PRO A O   
4865  C  CB  . PRO A 595 ? 0.203141  0.309549 0.303837 -0.0133022  -0.0404694  -0.0826817  595  PRO A CB  
4866  C  CG  . PRO A 595 ? 0.196155  0.310653 0.312961 -0.0155241  -0.0391401  -0.0799232  595  PRO A CG  
4867  C  CD  . PRO A 595 ? 0.177001  0.291119 0.283904 -0.0130908  -0.0324553  -0.0697526  595  PRO A CD  
4868  N  N   . GLU A 596 ? 0.228497  0.319251 0.342152 -0.0200019  -0.0183149  -0.0692605  596  GLU A N   
4869  C  CA  . GLU A 596 ? 0.233426  0.31478  0.353779 -0.0231628  -0.0120767  -0.0676115  596  GLU A CA  
4870  C  C   . GLU A 596 ? 0.210037  0.285076 0.316624 -0.0202067  -0.00559518 -0.058758   596  GLU A C   
4871  O  O   . GLU A 596 ? 0.221773  0.294011 0.3323   -0.0220017  0.00151395  -0.0514012  596  GLU A O   
4872  C  CB  . GLU A 596 ? 0.251298  0.334369 0.392559 -0.0290717  -0.00762155 -0.0664519  596  GLU A CB  
4873  C  CG  . GLU A 596 ? 0.284363  0.373962 0.442407 -0.0323454  -0.0146275  -0.0763968  596  GLU A CG  
4874  C  CD  . GLU A 596 ? 0.34804   0.439986 0.531058 -0.0391395  -0.0111303  -0.0778942  596  GLU A CD  
4875  O  OE1 . GLU A 596 ? 0.352355  0.437997 0.541125 -0.0424985  -0.00185583 -0.0710133  596  GLU A OE1 
4876  O  OE2 . GLU A 596 ? 0.363007  0.462991 0.560716 -0.0413064  -0.0177069  -0.0860873  596  GLU A OE2 
4877  N  N   . TYR A 597 ? 0.19934   0.272554 0.289795 -0.0156214  -0.00815852 -0.0596592  597  TYR A N   
4878  C  CA  . TYR A 597 ? 0.199422  0.268895 0.27626  -0.0119916  -0.00372048 -0.0523729  597  TYR A CA  
4879  C  C   . TYR A 597 ? 0.201979  0.261498 0.282174 -0.0131276  0.00237818  -0.0482618  597  TYR A C   
4880  O  O   . TYR A 597 ? 0.224017  0.280623 0.296056 -0.0106589  0.00644284  -0.0412582  597  TYR A O   
4881  C  CB  . TYR A 597 ? 0.18688   0.256498 0.247843 -0.0073695  -0.00732759 -0.0552833  597  TYR A CB  
4882  C  CG  . TYR A 597 ? 0.197021  0.261594 0.258273 -0.00733571 -0.010265   -0.0638365  597  TYR A CG  
4883  C  CD1 . TYR A 597 ? 0.195588  0.251424 0.256068 -0.00645606 -0.00630398 -0.0632646  597  TYR A CD1 
4884  C  CD2 . TYR A 597 ? 0.197392  0.265868 0.259613 -0.00776115 -0.0174404  -0.0728893  597  TYR A CD2 
4885  C  CE1 . TYR A 597 ? 0.208373  0.25926  0.269868 -0.00617045 -0.0087149  -0.0718181  597  TYR A CE1 
4886  C  CE2 . TYR A 597 ? 0.210447  0.27399  0.272923 -0.00767663 -0.0200892  -0.0816137  597  TYR A CE2 
4887  C  CZ  . TYR A 597 ? 0.210144  0.264867 0.272321 -0.00687496 -0.0154201  -0.08121    597  TYR A CZ  
4888  O  OH  . TYR A 597 ? 0.215571  0.265087 0.278734 -0.00652754 -0.0178951  -0.0906648  597  TYR A OH  
4889  N  N   . GLN A 598 ? 0.214208  0.267895 0.305758 -0.0163765  0.00232396  -0.0529303  598  GLN A N   
4890  C  CA  . GLN A 598 ? 0.251593  0.294437 0.346231 -0.0170559  0.00740001  -0.0490903  598  GLN A CA  
4891  C  C   . GLN A 598 ? 0.261913  0.302711 0.366933 -0.0212532  0.0134951   -0.0418905  598  GLN A C   
4892  O  O   . GLN A 598 ? 0.280292  0.311659 0.387247 -0.0219263  0.018178    -0.0367521  598  GLN A O   
4893  C  CB  . GLN A 598 ? 0.267893  0.304191 0.373005 -0.0195     0.00494156  -0.0575197  598  GLN A CB  
4894  C  CG  . GLN A 598 ? 0.295613  0.325035 0.392216 -0.0153682  0.00392927  -0.0609922  598  GLN A CG  
4895  C  CD  . GLN A 598 ? 0.348984  0.370199 0.457173 -0.0177581  0.00225106  -0.0690611  598  GLN A CD  
4896  O  OE1 . GLN A 598 ? 0.326573  0.34981  0.434038 -0.0171099  -0.0032943  -0.0794171  598  GLN A OE1 
4897  N  NE2 . GLN A 598 ? 0.376092  0.387517 0.495217 -0.0206921  0.00688609  -0.0645176  598  GLN A NE2 
4898  N  N   . TRP A 599 ? 0.257776  0.307251 0.369352 -0.0239007  0.0137715   -0.0412105  599  TRP A N   
4899  C  CA  . TRP A 599 ? 0.261545  0.309232 0.384735 -0.0286143  0.0204282   -0.0354929  599  TRP A CA  
4900  C  C   . TRP A 599 ? 0.256529  0.301311 0.368491 -0.0262074  0.0266506   -0.0246861  599  TRP A C   
4901  O  O   . TRP A 599 ? 0.248989  0.299018 0.348302 -0.0219972  0.0253904   -0.0222242  599  TRP A O   
4902  C  CB  . TRP A 599 ? 0.24018   0.299281 0.375053 -0.0318176  0.0188581   -0.0390449  599  TRP A CB  
4903  C  CG  . TRP A 599 ? 0.23855   0.297899 0.385385 -0.0367028  0.0268319   -0.0331685  599  TRP A CG  
4904  C  CD1 . TRP A 599 ? 0.234726  0.290196 0.399374 -0.0428235  0.0303786   -0.0343632  599  TRP A CD1 
4905  C  CD2 . TRP A 599 ? 0.229549  0.293004 0.370762 -0.0358519  0.0328694   -0.0251265  599  TRP A CD2 
4906  N  NE1 . TRP A 599 ? 0.244797  0.302142 0.415114 -0.0460052  0.0388024   -0.0271983  599  TRP A NE1 
4907  C  CE2 . TRP A 599 ? 0.237355  0.29936  0.392781 -0.0416263  0.0405632   -0.0215353  599  TRP A CE2 
4908  C  CE3 . TRP A 599 ? 0.215114  0.282706 0.340727 -0.0308534  0.0327551   -0.0208203  599  TRP A CE3 
4909  C  CZ2 . TRP A 599 ? 0.228231  0.29355  0.381764 -0.0423378  0.0483885   -0.0140996  599  TRP A CZ2 
4910  C  CZ3 . TRP A 599 ? 0.202576  0.273269 0.327006 -0.031447   0.0395906   -0.0141584  599  TRP A CZ3 
4911  C  CH2 . TRP A 599 ? 0.216044  0.285459 0.353149 -0.0368813  0.0474809   -0.0107601  599  TRP A CH2 
4912  N  N   . HIS A 600 ? 0.295574  0.331702 0.412423 -0.0290628  0.0333443   -0.0181234  600  HIS A N   
4913  C  CA  . HIS A 600 ? 0.276176  0.309987 0.383203 -0.0274427  0.0395175   -0.00778482 600  HIS A CA  
4914  C  C   . HIS A 600 ? 0.27088   0.303035 0.389629 -0.0332569  0.0472309   -0.00294099 600  HIS A C   
4915  O  O   . HIS A 600 ? 0.266952  0.295145 0.400844 -0.0382384  0.0483045   -0.0060279  600  HIS A O   
4916  C  CB  . HIS A 600 ? 0.291744  0.313317 0.389271 -0.0241166  0.040688    -0.00242049 600  HIS A CB  
4917  C  CG  . HIS A 600 ? 0.313146  0.336228 0.398696 -0.018189   0.0348725   -0.00571627 600  HIS A CG  
4918  N  ND1 . HIS A 600 ? 0.308019  0.331908 0.396233 -0.0173168  0.0291409   -0.0147455  600  HIS A ND1 
4919  C  CD2 . HIS A 600 ? 0.277257  0.301729 0.348743 -0.0131161  0.0342596   -0.00149464 600  HIS A CD2 
4920  C  CE1 . HIS A 600 ? 0.296767  0.32237  0.372753 -0.0119927  0.0260573   -0.0153818  600  HIS A CE1 
4921  N  NE2 . HIS A 600 ? 0.306381  0.332688 0.373197 -0.0096084  0.0289278   -0.00747646 600  HIS A NE2 
4922  N  N   . PRO A 601 ? 0.2545    0.289655 0.367152 -0.0330452  0.0532572   0.00450735  601  PRO A N   
4923  C  CA  . PRO A 601 ? 0.261199  0.295992 0.385413 -0.0389597  0.061769    0.00886814  601  PRO A CA  
4924  C  C   . PRO A 601 ? 0.293821  0.313298 0.417969 -0.0410073  0.067236    0.0163117   601  PRO A C   
4925  O  O   . PRO A 601 ? 0.296388  0.306988 0.407766 -0.0365083  0.0651241   0.0200106   601  PRO A O   
4926  C  CB  . PRO A 601 ? 0.242039  0.284484 0.355392 -0.0364495  0.0657147   0.0138974   601  PRO A CB  
4927  C  CG  . PRO A 601 ? 0.243551  0.282016 0.336804 -0.0294656  0.0615552   0.0169517   601  PRO A CG  
4928  C  CD  . PRO A 601 ? 0.23258   0.272582 0.328465 -0.0275295  0.0523241   0.00803422  601  PRO A CD  
4929  N  N   . PRO A 602 ? 0.31665   0.331931 0.45522  -0.0476243  0.0743446   0.0191093   602  PRO A N   
4930  C  CA  . PRO A 602 ? 0.347597  0.346883 0.483875 -0.0491851  0.0801706   0.028167    602  PRO A CA  
4931  C  C   . PRO A 602 ? 0.377411  0.373914 0.4952   -0.0461439  0.0866095   0.0395414   602  PRO A C   
4932  O  O   . PRO A 602 ? 0.382129  0.389573 0.491878 -0.0438293  0.0873722   0.0395202   602  PRO A O   
4933  C  CB  . PRO A 602 ? 0.338888  0.336411 0.497751 -0.0577233  0.0858481   0.0268831   602  PRO A CB  
4934  C  CG  . PRO A 602 ? 0.348938  0.363487 0.517999 -0.0604801  0.0872198   0.0215559   602  PRO A CG  
4935  C  CD  . PRO A 602 ? 0.323033  0.348504 0.480935 -0.0538335  0.0775988   0.0145281   602  PRO A CD  
4936  N  N   . LEU A 603 ? 0.401424  0.382829 0.511506 -0.0455627  0.0905446   0.0490445   603  LEU A N   
4937  C  CA  . LEU A 603 ? 0.436061  0.413116 0.528726 -0.0433813  0.0973545   0.0605955   603  LEU A CA  
4938  C  C   . LEU A 603 ? 0.423999  0.404    0.525656 -0.0502753  0.108742    0.0651591   603  LEU A C   
4939  O  O   . LEU A 603 ? 0.393296  0.371063 0.514733 -0.057177   0.112413    0.0631304   603  LEU A O   
4940  C  CB  . LEU A 603 ? 0.49334   0.452263 0.576185 -0.0407321  0.0975662   0.0695858   603  LEU A CB  
4941  C  CG  . LEU A 603 ? 0.501601  0.456878 0.571661 -0.0326683  0.087953    0.0678179   603  LEU A CG  
4942  C  CD1 . LEU A 603 ? 0.518457  0.455737 0.5794   -0.0303564  0.0897299   0.0785384   603  LEU A CD1 
4943  C  CD2 . LEU A 603 ? 0.461483  0.427619 0.515138 -0.0266669  0.0843226   0.0667992   603  LEU A CD2 
4944  N  N   . PRO A 604 ? 0.446211  0.431216 0.534137 -0.0486628  0.114911    0.0711391   604  PRO A N   
4945  C  CA  . PRO A 604 ? 0.476454  0.460699 0.568631 -0.0546472  0.127909    0.078461    604  PRO A CA  
4946  C  C   . PRO A 604 ? 0.549122  0.515431 0.643451 -0.0587533  0.134633    0.0885319   604  PRO A C   
4947  O  O   . PRO A 604 ? 0.552957  0.505618 0.633943 -0.0543395  0.130845    0.0945255   604  PRO A O   
4948  C  CB  . PRO A 604 ? 0.476739  0.465359 0.546191 -0.0495763  0.131357    0.0840549   604  PRO A CB  
4949  C  CG  . PRO A 604 ? 0.427963  0.425449 0.488964 -0.0424501  0.119668    0.0759548   604  PRO A CG  
4950  C  CD  . PRO A 604 ? 0.404243  0.395097 0.471663 -0.0409854  0.109995    0.0711552   604  PRO A CD  
4951  N  N   . ASP A 605 ? 0.62774   0.593536 0.739843 -0.0672631  0.144747    0.0907212   605  ASP A N   
4952  C  CA  . ASP A 605 ? 0.685104  0.632712 0.799087 -0.0715189  0.151981    0.101404    605  ASP A CA  
4953  C  C   . ASP A 605 ? 0.716787  0.653968 0.802146 -0.0665778  0.156942    0.115174    605  ASP A C   
4954  O  O   . ASP A 605 ? 0.729214  0.674941 0.800971 -0.0647489  0.162394    0.117973    605  ASP A O   
4955  C  CB  . ASP A 605 ? 0.779256  0.728675 0.918009 -0.0819532  0.162811    0.101642    605  ASP A CB  
4956  C  CG  . ASP A 605 ? 0.842339  0.801439 1.01051  -0.0869634  0.157043    0.0876982   605  ASP A CG  
4957  O  OD1 . ASP A 605 ? 0.856452  0.806262 1.03443  -0.087538   0.149895    0.0836294   605  ASP A OD1 
4958  O  OD2 . ASP A 605 ? 0.905146  0.881256 1.08621  -0.0898608  0.15923     0.0804513   605  ASP A OD2 
4959  N  N   . ASN A 606 ? 0.737027  0.655981 0.812625 -0.0636104  0.153903    0.122964    606  ASN A N   
4960  C  CA  . ASN A 606 ? 0.900196  0.807977 0.947521 -0.0579326  0.156468    0.136002    606  ASN A CA  
4961  C  C   . ASN A 606 ? 0.844688  0.76461  0.871463 -0.0498608  0.150535    0.132475    606  ASN A C   
4962  O  O   . ASN A 606 ? 0.88759   0.812639 0.899353 -0.0489648  0.157655    0.137424    606  ASN A O   
4963  C  CB  . ASN A 606 ? 1.05907   0.959085 1.10154  -0.0635965  0.17186     0.149057    606  ASN A CB  
4964  C  CG  . ASN A 606 ? 1.06539   0.95066  1.12671  -0.0716209  0.178448    0.154641    606  ASN A CG  
4965  O  OD1 . ASN A 606 ? 1.07231   0.938764 1.12745  -0.0694147  0.175607    0.162575    606  ASN A OD1 
4966  N  ND2 . ASN A 606 ? 0.983283  0.876548 1.0681   -0.0809589  0.187603    0.15099     606  ASN A ND2 
4967  N  N   . TYR A 607 ? 0.742801  0.667843 0.770246 -0.0443144  0.137756    0.123101    607  TYR A N   
4968  C  CA  . TYR A 607 ? 0.704798  0.636834 0.712002 -0.0358252  0.13038     0.12109     607  TYR A CA  
4969  C  C   . TYR A 607 ? 0.686114  0.602761 0.678686 -0.0291034  0.123163    0.127694    607  TYR A C   
4970  O  O   . TYR A 607 ? 0.698157  0.603701 0.70214  -0.030535   0.120399    0.127995    607  TYR A O   
4971  C  CB  . TYR A 607 ? 0.680979  0.629412 0.70054  -0.0348376  0.122009    0.106524    607  TYR A CB  
4972  C  CG  . TYR A 607 ? 0.678854  0.634341 0.68121  -0.0263693  0.113057    0.103001    607  TYR A CG  
4973  C  CD1 . TYR A 607 ? 0.613003  0.580146 0.603982 -0.024235   0.115505    0.101949    607  TYR A CD1 
4974  C  CD2 . TYR A 607 ? 0.67299   0.623503 0.671789 -0.0206118  0.102386    0.100311    607  TYR A CD2 
4975  C  CE1 . TYR A 607 ? 0.576396  0.549105 0.552748 -0.0168922  0.107402    0.0988093   607  TYR A CE1 
4976  C  CE2 . TYR A 607 ? 0.673506  0.630414 0.658331 -0.0134072  0.0946963   0.0972985   607  TYR A CE2 
4977  C  CZ  . TYR A 607 ? 0.65547   0.62308  0.629132 -0.0116813  0.0970085   0.0966743   607  TYR A CZ  
4978  O  OH  . TYR A 607 ? 0.671846  0.645194 0.633465 -0.0048457  0.0889011   0.093203    607  TYR A OH  
4979  N  N   . PRO A 608 ? 0.690958  0.605647 0.658884 -0.0216114  0.119924    0.133259    608  PRO A N   
4980  C  CA  . PRO A 608 ? 0.673706  0.598607 0.625714 -0.0199875  0.12466     0.134611    608  PRO A CA  
4981  C  C   . PRO A 608 ? 0.76765   0.684289 0.701544 -0.0210716  0.135773    0.147679    608  PRO A C   
4982  O  O   . PRO A 608 ? 0.754888  0.675663 0.667709 -0.0162705  0.13616     0.150101    608  PRO A O   
4983  C  CB  . PRO A 608 ? 0.625953  0.554821 0.563876 -0.0107444  0.112245    0.130297    608  PRO A CB  
4984  C  CG  . PRO A 608 ? 0.633433  0.546472 0.569034 -0.0067381  0.105322    0.135369    608  PRO A CG  
4985  C  CD  . PRO A 608 ? 0.648028  0.551598 0.603696 -0.0138267  0.110297    0.136911    608  PRO A CD  
4986  N  N   . GLU A 609 ? 0.85215   0.757624 0.794326 -0.0277607  0.145546    0.155801    609  GLU A N   
4987  C  CA  . GLU A 609 ? 0.904909  0.797085 0.827044 -0.0278216  0.154943    0.170842    609  GLU A CA  
4988  C  C   . GLU A 609 ? 0.836752  0.739445 0.748161 -0.0300382  0.16648     0.172642    609  GLU A C   
4989  O  O   . GLU A 609 ? 0.791557  0.711688 0.717071 -0.0330107  0.168121    0.161855    609  GLU A O   
4990  C  CB  . GLU A 609 ? 1.01702   0.893046 0.95264  -0.0346409  0.162079    0.179255    609  GLU A CB  
4991  C  CG  . GLU A 609 ? 1.13516   0.999861 1.08128  -0.0320623  0.151056    0.177234    609  GLU A CG  
4992  C  CD  . GLU A 609 ? 1.31772   1.17049  1.28617  -0.0403321  0.157256    0.180515    609  GLU A CD  
4993  O  OE1 . GLU A 609 ? 1.32263   1.18005  1.30525  -0.0491457  0.168948    0.18079     609  GLU A OE1 
4994  O  OE2 . GLU A 609 ? 1.44817   1.28668  1.42065  -0.0378252  0.150299    0.182671    609  GLU A OE2 
4995  N  N   . ASP B 2   ? 1.28759   0.732472 0.378832 0.385738    -0.0934181  0.151262    2    ASP B N   
4996  C  CA  . ASP B 2   ? 1.3569    0.776862 0.399594 0.388589    -0.0857921  0.159882    2    ASP B CA  
4997  C  C   . ASP B 2   ? 1.41853   0.774587 0.416457 0.380277    -0.0603033  0.179713    2    ASP B C   
4998  O  O   . ASP B 2   ? 1.38259   0.729892 0.403415 0.353906    -0.0401392  0.182605    2    ASP B O   
4999  C  CB  . ASP B 2   ? 1.32863   0.784208 0.395124 0.369132    -0.0815218  0.150018    2    ASP B CB  
5000  C  CG  . ASP B 2   ? 1.43786   0.865467 0.450058 0.374593    -0.0737311  0.159093    2    ASP B CG  
5001  O  OD1 . ASP B 2   ? 1.47725   0.887194 0.443063 0.40282     -0.0875209  0.163625    2    ASP B OD1 
5002  O  OD2 . ASP B 2   ? 1.4696    0.891546 0.483652 0.351541    -0.0533955  0.162026    2    ASP B OD2 
5003  N  N   . PRO B 3   ? 1.44431   0.755779 0.376846 0.40282     -0.0611436  0.19302     3    PRO B N   
5004  C  CA  . PRO B 3   ? 1.538     0.785229 0.418338 0.396158    -0.0360831  0.212655    3    PRO B CA  
5005  C  C   . PRO B 3   ? 1.55524   0.798644 0.444938 0.362911    -0.00916194 0.21544     3    PRO B C   
5006  O  O   . PRO B 3   ? 1.59772   0.809532 0.487882 0.343228    0.0131658   0.224233    3    PRO B O   
5007  C  CB  . PRO B 3   ? 1.58798   0.804239 0.39988  0.428238    -0.0469946  0.222061    3    PRO B CB  
5008  C  CG  . PRO B 3   ? 1.56487   0.818867 0.393407 0.456851    -0.0795553  0.209412    3    PRO B CG  
5009  C  CD  . PRO B 3   ? 1.49299   0.815371 0.398588 0.436753    -0.0872574  0.188979    3    PRO B CD  
5010  N  N   . GLY B 4   ? 1.57005   0.847688 0.469361 0.356776    -0.0117835  0.206644    4    GLY B N   
5011  C  CA  . GLY B 4   ? 1.53987   0.824868 0.454285 0.327177    0.0106932   0.205892    4    GLY B CA  
5012  C  C   . GLY B 4   ? 1.48447   0.801791 0.464829 0.298612    0.0192079   0.196236    4    GLY B C   
5013  O  O   . GLY B 4   ? 1.49106   0.813787 0.487371 0.273293    0.0389648   0.195662    4    GLY B O   
5014  N  N   . LEU B 5   ? 1.44557   0.78627  0.46424  0.303501    0.00390347  0.188009    5    LEU B N   
5015  C  CA  . LEU B 5   ? 1.39744   0.764637 0.474664 0.279613    0.0103775   0.179776    5    LEU B CA  
5016  C  C   . LEU B 5   ? 1.39899   0.723229 0.467081 0.272755    0.0249484   0.190765    5    LEU B C   
5017  O  O   . LEU B 5   ? 1.31845   0.649776 0.422021 0.247879    0.0391518   0.188081    5    LEU B O   
5018  C  CB  . LEU B 5   ? 1.36625   0.78728  0.492735 0.287057    -0.0138244  0.163025    5    LEU B CB  
5019  C  CG  . LEU B 5   ? 1.37      0.839368 0.517906 0.287564    -0.0268556  0.148962    5    LEU B CG  
5020  C  CD1 . LEU B 5   ? 1.3474    0.863899 0.538488 0.297134    -0.0508003  0.133476    5    LEU B CD1 
5021  C  CD2 . LEU B 5   ? 1.30768   0.796735 0.481263 0.260348    -0.0104126  0.144171    5    LEU B CD2 
5022  N  N   . GLN B 6   ? 1.50289   0.782614 0.522716 0.29597     0.0204079   0.202473    6    GLN B N   
5023  C  CA  . GLN B 6   ? 1.50829   0.743014 0.514048 0.294324    0.0312666   0.212664    6    GLN B CA  
5024  C  C   . GLN B 6   ? 1.53357   0.720658 0.507595 0.274057    0.0612814   0.226315    6    GLN B C   
5025  O  O   . GLN B 6   ? 1.60133   0.771635 0.537688 0.275589    0.0698181   0.233461    6    GLN B O   
5026  C  CB  . GLN B 6   ? 1.62998   0.839897 0.59872  0.328954    0.0127904   0.21826     6    GLN B CB  
5027  C  CG  . GLN B 6   ? 1.64284   0.902578 0.656623 0.342427    -0.0129955  0.202895    6    GLN B CG  
5028  C  CD  . GLN B 6   ? 1.70841   0.962595 0.688569 0.379936    -0.0365091  0.20408     6    GLN B CD  
5029  O  OE1 . GLN B 6   ? 1.66994   0.971153 0.670193 0.39342     -0.0583749  0.191352    6    GLN B OE1 
5030  N  NE2 . GLN B 6   ? 1.76474   0.959831 0.69202  0.397129    -0.0317778  0.219307    6    GLN B NE2 
5031  N  N   . PRO B 7   ? 1.51678   0.68178  0.505644 0.25404     0.0783606   0.229487    7    PRO B N   
5032  C  CA  . PRO B 7   ? 1.53383   0.67196  0.514392 0.225428    0.108396    0.236745    7    PRO B CA  
5033  C  C   . PRO B 7   ? 1.63178   0.702627 0.542778 0.230297    0.126901    0.255596    7    PRO B C   
5034  O  O   . PRO B 7   ? 1.69974   0.729501 0.563846 0.255943    0.118864    0.266012    7    PRO B O   
5035  C  CB  . PRO B 7   ? 1.50046   0.639262 0.520739 0.20575     0.116368    0.232026    7    PRO B CB  
5036  C  CG  . PRO B 7   ? 1.51187   0.641019 0.526568 0.231598    0.0960318   0.23186     7    PRO B CG  
5037  C  CD  . PRO B 7   ? 1.47941   0.644938 0.493604 0.258439    0.0693458   0.225297    7    PRO B CD  
5038  N  N   . GLY B 8   ? 1.63498   0.694657 0.538245 0.206164    0.152114    0.259944    8    GLY B N   
5039  C  CA  . GLY B 8   ? 1.71806   0.714184 0.554282 0.20899     0.171822    0.27796     8    GLY B CA  
5040  C  C   . GLY B 8   ? 1.76117   0.702595 0.581724 0.196248    0.191257    0.287776    8    GLY B C   
5041  O  O   . GLY B 8   ? 1.74574   0.701029 0.608113 0.185836    0.188398    0.27979     8    GLY B O   
5042  N  N   . GLN B 9   ? 1.77467   0.652714 0.533927 0.196513    0.211662    0.304855    9    GLN B N   
5043  C  CA  . GLN B 9   ? 1.85304   0.685011 0.606525 0.173774    0.236605    0.311696    9    GLN B CA  
5044  C  C   . GLN B 9   ? 1.81866   0.677741 0.608297 0.134497    0.262415    0.304866    9    GLN B C   
5045  O  O   . GLN B 9   ? 1.88218   0.767719 0.674344 0.127112    0.268847    0.302345    9    GLN B O   
5046  C  CB  . GLN B 9   ? 2.00957   0.759542 0.686104 0.193098    0.244374    0.331934    9    GLN B CB  
5047  C  CG  . GLN B 9   ? 2.0307    0.768199 0.695007 0.226845    0.21764     0.332989    9    GLN B CG  
5048  C  CD  . GLN B 9   ? 2.11549   0.806253 0.706175 0.263149    0.207817    0.348401    9    GLN B CD  
5049  O  OE1 . GLN B 9   ? 2.11755   0.818006 0.703006 0.295445    0.180162    0.346011    9    GLN B OE1 
5050  N  NE2 . GLN B 9   ? 2.20188   0.843296 0.734958 0.258929    0.230027    0.36388     9    GLN B NE2 
5051  N  N   . PHE B 10  ? 1.82866   0.660031 0.633041 0.109873    0.281514    0.305341    10   PHE B N   
5052  C  CA  . PHE B 10  ? 1.85378   0.698702 0.688388 0.0720435   0.308374    0.299971    10   PHE B CA  
5053  C  C   . PHE B 10  ? 1.92336   0.724855 0.758093 0.0509675   0.327827    0.303011    10   PHE B C   
5054  O  O   . PHE B 10  ? 1.89024   0.681802 0.734585 0.0610231   0.314122    0.300652    10   PHE B O   
5055  C  CB  . PHE B 10  ? 1.77997   0.702524 0.692389 0.0565502   0.297629    0.279607    10   PHE B CB  
5056  C  CG  . PHE B 10  ? 1.74639   0.722799 0.673981 0.0731898   0.276919    0.272078    10   PHE B CG  
5057  C  CD1 . PHE B 10  ? 1.69439   0.692346 0.626908 0.102799    0.245551    0.268017    10   PHE B CD1 
5058  C  CD2 . PHE B 10  ? 1.75167   0.755426 0.686966 0.0593992   0.289472    0.268757    10   PHE B CD2 
5059  C  CE1 . PHE B 10  ? 1.6875    0.732037 0.632099 0.116958    0.22736     0.260642    10   PHE B CE1 
5060  C  CE2 . PHE B 10  ? 1.71192   0.761747 0.659088 0.0746261   0.270756    0.261423    10   PHE B CE2 
5061  C  CZ  . PHE B 10  ? 1.70506   0.774407 0.656724 0.102677    0.239879    0.257328    10   PHE B CZ  
5062  N  N   . SER B 11  ? 1.99244   0.772867 0.820205 0.0205969   0.359885    0.306554    11   SER B N   
5063  C  CA  . SER B 11  ? 2.02836   0.771279 0.860433 -0.00638632 0.382963    0.307421    11   SER B CA  
5064  C  C   . SER B 11  ? 1.97983   0.776165 0.886981 -0.0262884  0.375776    0.287888    11   SER B C   
5065  O  O   . SER B 11  ? 1.8132    0.679164 0.772651 -0.0265665  0.359612    0.273485    11   SER B O   
5066  C  CB  . SER B 11  ? 2.06503   0.774509 0.869731 -0.0331821  0.419055    0.315668    11   SER B CB  
5067  O  OG  . SER B 11  ? 1.97822   0.749717 0.823807 -0.0504504  0.425047    0.30436     11   SER B OG  
5068  N  N   . ALA B 12  ? 2.01339   0.771626 0.921171 -0.0425301  0.388659    0.288116    12   ALA B N   
5069  C  CA  . ALA B 12  ? 1.96826   0.762925 0.937367 -0.05984    0.3826      0.271241    12   ALA B CA  
5070  C  C   . ALA B 12  ? 1.96819   0.775093 0.967919 -0.101429   0.411615    0.26315     12   ALA B C   
5071  O  O   . ALA B 12  ? 2.07944   0.826711 1.05392  -0.12513    0.440159    0.269346    12   ALA B O   
5072  C  CB  . ALA B 12  ? 2.00899   0.752569 0.956653 -0.0490114  0.376987    0.275876    12   ALA B CB  
5073  N  N   . ASP B 13  ? 1.91634   0.797948 0.968387 -0.110745   0.405732    0.249332    13   ASP B N   
5074  C  CA  . ASP B 13  ? 1.92748   0.832457 1.01096  -0.146585   0.431046    0.240615    13   ASP B CA  
5075  C  C   . ASP B 13  ? 1.85574   0.83627  0.983414 -0.145041   0.419178    0.228848    13   ASP B C   
5076  O  O   . ASP B 13  ? 1.82574   0.830328 0.950671 -0.117088   0.39437     0.229769    13   ASP B O   
5077  C  CB  . ASP B 13  ? 2.07358   0.918387 1.10545  -0.162509   0.464548    0.254808    13   ASP B CB  
5078  C  CG  . ASP B 13  ? 2.1191    0.96655  1.11922  -0.154982   0.473178    0.264007    13   ASP B CG  
5079  O  OD1 . ASP B 13  ? 2.03515   0.936399 1.05722  -0.138251   0.452672    0.257894    13   ASP B OD1 
5080  O  OD2 . ASP B 13  ? 2.21923   1.01532  1.17315  -0.166664   0.500988    0.276668    13   ASP B OD2 
5081  N  N   . GLU B 14  ? 1.82286   0.839584 0.990432 -0.175024   0.437356    0.217443    14   GLU B N   
5082  C  CA  . GLU B 14  ? 1.7331    0.825892 0.95433  -0.17723    0.425852    0.202572    14   GLU B CA  
5083  C  C   . GLU B 14  ? 1.70563   0.809733 0.900971 -0.159553   0.422653    0.209635    14   GLU B C   
5084  O  O   . GLU B 14  ? 1.60744   0.762292 0.830689 -0.14455    0.400834    0.201657    14   GLU B O   
5085  C  CB  . GLU B 14  ? 1.69899   0.827756 0.969251 -0.212257   0.445598    0.187938    14   GLU B CB  
5086  C  CG  . GLU B 14  ? 1.62959   0.833244 0.948805 -0.211361   0.434374    0.174178    14   GLU B CG  
5087  C  CD  . GLU B 14  ? 1.56544   0.822731 0.951103 -0.234188   0.434708    0.154505    14   GLU B CD  
5088  O  OE1 . GLU B 14  ? 1.5499    0.786062 0.944392 -0.256056   0.448323    0.150657    14   GLU B OE1 
5089  O  OE2 . GLU B 14  ? 1.45485   0.772579 0.880968 -0.228386   0.420038    0.143208    14   GLU B OE2 
5090  N  N   . ALA B 15  ? 1.77051   0.825628 0.912408 -0.162576   0.445236    0.224091    15   ALA B N   
5091  C  CA  . ALA B 15  ? 1.74171   0.792984 0.845566 -0.146896   0.447144    0.233443    15   ALA B CA  
5092  C  C   . ALA B 15  ? 1.6997    0.746576 0.778571 -0.108774   0.415551    0.239715    15   ALA B C   
5093  O  O   . ALA B 15  ? 1.67224   0.772886 0.775377 -0.0918846  0.393169    0.231454    15   ALA B O   
5094  C  CB  . ALA B 15  ? 1.77771   0.764351 0.8233   -0.157664   0.477966    0.24936     15   ALA B CB  
5095  N  N   . GLY B 16  ? 1.77398   0.755601 0.803543 -0.0952631  0.414292    0.253939    16   GLY B N   
5096  C  CA  . GLY B 16  ? 1.77751   0.749451 0.783633 -0.0598979  0.385062    0.259536    16   GLY B CA  
5097  C  C   . GLY B 16  ? 1.66782   0.708178 0.732406 -0.0508606  0.356569    0.243221    16   GLY B C   
5098  O  O   . GLY B 16  ? 1.60363   0.670646 0.664417 -0.0288212  0.337291    0.242161    16   GLY B O   
5099  N  N   . ALA B 17  ? 1.62394   0.693415 0.742513 -0.0694577  0.355339    0.229946    17   ALA B N   
5100  C  CA  . ALA B 17  ? 1.52541   0.657004 0.699346 -0.062498   0.329855    0.214709    17   ALA B CA  
5101  C  C   . ALA B 17  ? 1.46888   0.657537 0.672015 -0.0648231  0.326608    0.205468    17   ALA B C   
5102  O  O   . ALA B 17  ? 1.3705    0.602986 0.602779 -0.0504769  0.302822    0.19669     17   ALA B O   
5103  C  CB  . ALA B 17  ? 1.50467   0.653198 0.726576 -0.0809781  0.329259    0.202747    17   ALA B CB  
5104  N  N   . GLN B 18  ? 1.47231   0.660168 0.668067 -0.083064   0.350982    0.206965    18   GLN B N   
5105  C  CA  . GLN B 18  ? 1.4693    0.707385 0.688477 -0.0844251  0.349739    0.198604    18   GLN B CA  
5106  C  C   . GLN B 18  ? 1.44043   0.674566 0.622531 -0.0549997  0.333115    0.205689    18   GLN B C   
5107  O  O   . GLN B 18  ? 1.41709   0.698442 0.625638 -0.0451456  0.316197    0.196259    18   GLN B O   
5108  C  CB  . GLN B 18  ? 1.5382    0.774148 0.755894 -0.110584   0.381463    0.198603    18   GLN B CB  
5109  C  CG  . GLN B 18  ? 1.53926   0.808513 0.812805 -0.140726   0.394436    0.184527    18   GLN B CG  
5110  C  CD  . GLN B 18  ? 1.50685   0.84514  0.833265 -0.145629   0.387693    0.16862     18   GLN B CD  
5111  O  OE1 . GLN B 18  ? 1.51351   0.867926 0.833649 -0.147044   0.397965    0.168071    18   GLN B OE1 
5112  N  NE2 . GLN B 18  ? 1.37474   0.753084 0.752005 -0.14719    0.370265    0.155618    18   GLN B NE2 
5113  N  N   . LEU B 19  ? 1.46199   0.637848 0.581725 -0.0409041  0.337851    0.222087    19   LEU B N   
5114  C  CA  . LEU B 19  ? 1.45621   0.620642 0.532904 -0.011788   0.322592    0.230012    19   LEU B CA  
5115  C  C   . LEU B 19  ? 1.40028   0.583474 0.492923 0.0123239   0.289595    0.225059    19   LEU B C   
5116  O  O   . LEU B 19  ? 1.35029   0.565933 0.448796 0.0300507   0.26986     0.219693    19   LEU B O   
5117  C  CB  . LEU B 19  ? 1.52424   0.620293 0.527108 -0.00386466 0.338836    0.249243    19   LEU B CB  
5118  C  CG  . LEU B 19  ? 1.56203   0.64167  0.537601 -0.0206585  0.369145    0.255413    19   LEU B CG  
5119  C  CD1 . LEU B 19  ? 1.65133   0.659586 0.548903 -0.00785892 0.381108    0.275638    19   LEU B CD1 
5120  C  CD2 . LEU B 19  ? 1.51401   0.641785 0.505704 -0.0206501  0.368528    0.246646    19   LEU B CD2 
5121  N  N   . PHE B 20  ? 1.389     0.555312 0.493129 0.0104666   0.284969    0.225154    20   PHE B N   
5122  C  CA  . PHE B 20  ? 1.35952   0.537326 0.476734 0.0318644   0.256806    0.221285    20   PHE B CA  
5123  C  C   . PHE B 20  ? 1.30001   0.54584  0.471443 0.0339109   0.23721     0.205155    20   PHE B C   
5124  O  O   . PHE B 20  ? 1.29938   0.563694 0.467316 0.0570644   0.214336    0.202795    20   PHE B O   
5125  C  CB  . PHE B 20  ? 1.36198   0.512613 0.487497 0.0244693   0.25946     0.222329    20   PHE B CB  
5126  C  CG  . PHE B 20  ? 1.32292   0.491341 0.470776 0.0432489   0.232063    0.216       20   PHE B CG  
5127  C  CD1 . PHE B 20  ? 1.25959   0.482253 0.468363 0.0346691   0.220024    0.200376    20   PHE B CD1 
5128  C  CD2 . PHE B 20  ? 1.36568   0.496635 0.472866 0.0701451   0.218683    0.225583    20   PHE B CD2 
5129  C  CE1 . PHE B 20  ? 1.22736   0.467505 0.456973 0.0508731   0.19645     0.194285    20   PHE B CE1 
5130  C  CE2 . PHE B 20  ? 1.31908   0.4694   0.448851 0.0869904   0.194577    0.218802    20   PHE B CE2 
5131  C  CZ  . PHE B 20  ? 1.26434   0.468812 0.455046 0.0766887   0.184171    0.203282    20   PHE B CZ  
5132  N  N   . ALA B 21  ? 1.27596   0.558077 0.498362 0.00949563  0.24592     0.193576    21   ALA B N   
5133  C  CA  . ALA B 21  ? 1.20195   0.546196 0.47706  0.00749281  0.231456    0.178375    21   ALA B CA  
5134  C  C   . ALA B 21  ? 1.19069   0.55627  0.453139 0.0202681   0.224587    0.177182    21   ALA B C   
5135  O  O   . ALA B 21  ? 1.12349   0.522911 0.405352 0.0347382   0.202523    0.169386    21   ALA B O   
5136  C  CB  . ALA B 21  ? 1.17225   0.543771 0.493306 -0.0210384  0.246716    0.168434    21   ALA B CB  
5137  N  N   . GLN B 22  ? 1.24937   0.594264 0.47775  0.015115    0.24364     0.184609    22   GLN B N   
5138  C  CA  . GLN B 22  ? 1.27242   0.637321 0.487748 0.02748     0.237036    0.18256     22   GLN B CA  
5139  C  C   . GLN B 22  ? 1.30497   0.655479 0.486098 0.0577202   0.213937    0.187787    22   GLN B C   
5140  O  O   . GLN B 22  ? 1.32166   0.704859 0.51376  0.0714698   0.195278    0.179979    22   GLN B O   
5141  C  CB  . GLN B 22  ? 1.28915   0.637321 0.473933 0.0172458   0.261732    0.188707    22   GLN B CB  
5142  C  CG  . GLN B 22  ? 1.26656   0.631424 0.48504  -0.0126846  0.285822    0.182671    22   GLN B CG  
5143  C  CD  . GLN B 22  ? 1.33756   0.67232  0.517311 -0.0238627  0.314341    0.191872    22   GLN B CD  
5144  O  OE1 . GLN B 22  ? 1.37472   0.676427 0.500335 -0.00882581 0.316431    0.203038    22   GLN B OE1 
5145  N  NE2 . GLN B 22  ? 1.34094   0.687547 0.547999 -0.0506814  0.337155    0.186869    22   GLN B NE2 
5146  N  N   . SER B 23  ? 1.34945   0.650758 0.489691 0.068182    0.214958    0.200395    23   SER B N   
5147  C  CA  . SER B 23  ? 1.36851   0.656029 0.478244 0.0978359   0.192236    0.204911    23   SER B CA  
5148  C  C   . SER B 23  ? 1.34226   0.670233 0.498369 0.106233    0.166658    0.192593    23   SER B C   
5149  O  O   . SER B 23  ? 1.34677   0.693276 0.499387 0.12757     0.144334    0.188403    23   SER B O   
5150  C  CB  . SER B 23  ? 1.4065    0.630598 0.463662 0.10597     0.201073    0.221142    23   SER B CB  
5151  O  OG  . SER B 23  ? 1.42299   0.629326 0.434285 0.135355    0.185082    0.227876    23   SER B OG  
5152  N  N   . TYR B 24  ? 1.28762   0.632117 0.488575 0.088771    0.170013    0.185705    24   TYR B N   
5153  C  CA  . TYR B 24  ? 1.23506   0.613151 0.47631  0.0966359   0.147483    0.175224    24   TYR B CA  
5154  C  C   . TYR B 24  ? 1.2227    0.654733 0.497586 0.099353    0.133013    0.162104    24   TYR B C   
5155  O  O   . TYR B 24  ? 1.21076   0.660983 0.48774  0.118675    0.110957    0.157371    24   TYR B O   
5156  C  CB  . TYR B 24  ? 1.18864   0.570393 0.467064 0.0775603   0.154842    0.170882    24   TYR B CB  
5157  C  CG  . TYR B 24  ? 1.14714   0.570564 0.47438  0.0805107   0.135036    0.158307    24   TYR B CG  
5158  C  CD1 . TYR B 24  ? 1.15149   0.567534 0.473073 0.100145    0.116792    0.158977    24   TYR B CD1 
5159  C  CD2 . TYR B 24  ? 1.10205   0.571476 0.479798 0.0642622   0.135122    0.145863    24   TYR B CD2 
5160  C  CE1 . TYR B 24  ? 1.09513   0.548081 0.459966 0.102041    0.100532    0.147736    24   TYR B CE1 
5161  C  CE2 . TYR B 24  ? 1.06403   0.568829 0.482717 0.0672068   0.117988    0.13525     24   TYR B CE2 
5162  C  CZ  . TYR B 24  ? 1.0715    0.567582 0.483581 0.0852668   0.101498    0.136316    24   TYR B CZ  
5163  O  OH  . TYR B 24  ? 1.0353    0.564369 0.485997 0.0876448   0.0862927   0.126243    24   TYR B OH  
5164  N  N   . GLN B 25  ? 1.25011   0.706053 0.550247 0.0794018   0.146771    0.156118    25   GLN B N   
5165  C  CA  . GLN B 25  ? 1.20324   0.709195 0.541257 0.0760485   0.138082    0.142968    25   GLN B CA  
5166  C  C   . GLN B 25  ? 1.27207   0.782817 0.581983 0.0937672   0.12786     0.142801    25   GLN B C   
5167  O  O   . GLN B 25  ? 1.26743   0.8161   0.601909 0.0957726   0.117079    0.131894    25   GLN B O   
5168  C  CB  . GLN B 25  ? 1.17939   0.697934 0.544582 0.0501324   0.159164    0.139238    25   GLN B CB  
5169  C  CG  . GLN B 25  ? 1.22127   0.753932 0.629006 0.0366943   0.158531    0.133255    25   GLN B CG  
5170  C  CD  . GLN B 25  ? 1.20307   0.742056 0.634125 0.0111484   0.180036    0.130414    25   GLN B CD  
5171  O  OE1 . GLN B 25  ? 1.10202   0.676054 0.578972 0.00013983  0.177064    0.119779    25   GLN B OE1 
5172  N  NE2 . GLN B 25  ? 1.16      0.665265 0.559532 0.00163133  0.201847    0.139598    25   GLN B NE2 
5173  N  N   . SER B 26  ? 1.33321   0.802994 0.589586 0.107834    0.130226    0.154932    26   SER B N   
5174  C  CA  . SER B 26  ? 1.3763    0.84302  0.596681 0.1248      0.12307     0.156501    26   SER B CA  
5175  C  C   . SER B 26  ? 1.35685   0.840933 0.580733 0.147653    0.094621    0.150547    26   SER B C   
5176  O  O   . SER B 26  ? 1.3773    0.889004 0.605747 0.156839    0.0811276   0.141821    26   SER B O   
5177  C  CB  . SER B 26  ? 1.3947    0.808264 0.554529 0.130679    0.137829    0.172544    26   SER B CB  
5178  O  OG  . SER B 26  ? 1.50318   0.917153 0.63236  0.138548    0.139448    0.173126    26   SER B OG  
5179  N  N   . SER B 27  ? 1.32235   0.791246 0.546194 0.156072    0.0858889   0.154284    27   SER B N   
5180  C  CA  . SER B 27  ? 1.27393   0.752819 0.492043 0.180421    0.0603703   0.150485    27   SER B CA  
5181  C  C   . SER B 27  ? 1.16422   0.687071 0.439942 0.175138    0.0463477   0.136776    27   SER B C   
5182  O  O   . SER B 27  ? 1.09319   0.644879 0.383052 0.189047    0.0250464   0.12732     27   SER B O   
5183  C  CB  . SER B 27  ? 1.31962   0.752169 0.494681 0.197087    0.0589288   0.163557    27   SER B CB  
5184  O  OG  . SER B 27  ? 1.2903    0.6786   0.413398 0.196565    0.0773401   0.177339    27   SER B OG  
5185  N  N   . ALA B 28  ? 1.1536    0.682314 0.462569 0.153311    0.0599328   0.135233    28   ALA B N   
5186  C  CA  . ALA B 28  ? 1.07643   0.643911 0.439507 0.144953    0.0506425   0.123288    28   ALA B CA  
5187  C  C   . ALA B 28  ? 1.06608   0.677048 0.456941 0.142298    0.0419885   0.110484    28   ALA B C   
5188  O  O   . ALA B 28  ? 1.06765   0.709208 0.487572 0.147928    0.0250374   0.100503    28   ALA B O   
5189  C  CB  . ALA B 28  ? 1.05825   0.619804 0.44574  0.123163    0.067299    0.124773    28   ALA B CB  
5190  N  N   . GLU B 29  ? 1.10747   0.719543 0.487144 0.134574    0.0537839   0.110673    29   GLU B N   
5191  C  CA  . GLU B 29  ? 1.08143   0.728822 0.480089 0.13349     0.0467432   0.0991019   29   GLU B CA  
5192  C  C   . GLU B 29  ? 1.01474   0.678415 0.408772 0.153661    0.0228525   0.0921484   29   GLU B C   
5193  O  O   . GLU B 29  ? 0.971384  0.670436 0.400363 0.152004    0.0109027   0.0798709   29   GLU B O   
5194  C  CB  . GLU B 29  ? 1.19436   0.83388  0.574932 0.123854    0.0649532   0.101884    29   GLU B CB  
5195  C  CG  . GLU B 29  ? 1.26513   0.934804 0.656561 0.124671    0.0590464   0.0906638   29   GLU B CG  
5196  C  CD  . GLU B 29  ? 1.36829   1.04167  0.761759 0.109714    0.0787141   0.0898079   29   GLU B CD  
5197  O  OE1 . GLU B 29  ? 1.33406   1.02855  0.766718 0.0938238   0.0859627   0.0840321   29   GLU B OE1 
5198  O  OE2 . GLU B 29  ? 1.48004   1.13582  0.835651 0.114334    0.087158    0.0946616   29   GLU B OE2 
5199  N  N   . GLN B 30  ? 1.05129   0.688981 0.403636 0.172705    0.0156123   0.0997539   30   GLN B N   
5200  C  CA  . GLN B 30  ? 1.05934   0.711757 0.4026   0.193544    -0.00716192 0.0930225   30   GLN B CA  
5201  C  C   . GLN B 30  ? 1.01192   0.68471  0.388272 0.198668    -0.0229435  0.0864276   30   GLN B C   
5202  O  O   . GLN B 30  ? 0.998287  0.701606 0.39193  0.207629    -0.0413425  0.0747892   30   GLN B O   
5203  C  CB  . GLN B 30  ? 1.12905   0.744286 0.414262 0.213713    -0.00930849 0.104396    30   GLN B CB  
5204  C  CG  . GLN B 30  ? 1.16539   0.794679 0.429453 0.231827    -0.0265111  0.0971786   30   GLN B CG  
5205  C  CD  . GLN B 30  ? 1.25188   0.846145 0.45863  0.25541     -0.0323462  0.107884    30   GLN B CD  
5206  O  OE1 . GLN B 30  ? 1.26762   0.819692 0.434463 0.254841    -0.0156977  0.122701    30   GLN B OE1 
5207  N  NE2 . GLN B 30  ? 1.26463   0.875701 0.46655  0.276669    -0.056052   0.100357    30   GLN B NE2 
5208  N  N   . VAL B 31  ? 0.984966  0.639463 0.36806  0.193195    -0.0152144  0.0936944   31   VAL B N   
5209  C  CA  . VAL B 31  ? 0.948376  0.616684 0.357168 0.199671    -0.0285439  0.0890169   31   VAL B CA  
5210  C  C   . VAL B 31  ? 0.8482    0.556187 0.311421 0.182971    -0.0299408  0.0767882   31   VAL B C   
5211  O  O   . VAL B 31  ? 0.772839  0.511834 0.262451 0.188638    -0.0458632  0.0659171   31   VAL B O   
5212  C  CB  . VAL B 31  ? 0.970802  0.603605 0.364611 0.202092    -0.021255   0.100387    31   VAL B CB  
5213  C  CG1 . VAL B 31  ? 0.919957  0.570877 0.343841 0.208161    -0.0345547  0.0939622   31   VAL B CG1 
5214  C  CG2 . VAL B 31  ? 1.01278   0.60269  0.349381 0.221078    -0.0208954  0.113156    31   VAL B CG2 
5215  N  N   . LEU B 32  ? 0.826627  0.533372 0.305958 0.162283    -0.0126691  0.0784814   32   LEU B N   
5216  C  CA  . LEU B 32  ? 0.747671  0.488484 0.274085 0.146702    -0.0124374  0.0680636   32   LEU B CA  
5217  C  C   . LEU B 32  ? 0.720376  0.492837 0.259631 0.150213    -0.0245788  0.0561226   32   LEU B C   
5218  O  O   . LEU B 32  ? 0.705905  0.507755 0.279227 0.147946    -0.034679   0.0459302   32   LEU B O   
5219  C  CB  . LEU B 32  ? 0.753491  0.485747 0.286276 0.126982    0.00810513  0.0721972   32   LEU B CB  
5220  C  CG  . LEU B 32  ? 0.784728  0.492769 0.317254 0.118441    0.0202694   0.0805384   32   LEU B CG  
5221  C  CD1 . LEU B 32  ? 0.812298  0.508519 0.34217  0.100626    0.0415705   0.0851341   32   LEU B CD1 
5222  C  CD2 . LEU B 32  ? 0.753319  0.481148 0.324266 0.113692    0.0134488   0.0742337   32   LEU B CD2 
5223  N  N   . PHE B 33  ? 0.749425  0.514982 0.261031 0.154684    -0.0225108  0.0570449   33   PHE B N   
5224  C  CA  . PHE B 33  ? 0.751125  0.542152 0.267788 0.160089    -0.0348127  0.0455537   33   PHE B CA  
5225  C  C   . PHE B 33  ? 0.721973  0.533835 0.251487 0.173469    -0.0557949  0.0369479   33   PHE B C   
5226  O  O   . PHE B 33  ? 0.672458  0.514884 0.2329   0.168759    -0.0641124  0.02475     33   PHE B O   
5227  C  CB  . PHE B 33  ? 0.806681  0.585118 0.284674 0.167735    -0.0327504  0.047457    33   PHE B CB  
5228  C  CG  . PHE B 33  ? 0.80851   0.616817 0.297975 0.172331    -0.0474651  0.0329209   33   PHE B CG  
5229  C  CD1 . PHE B 33  ? 0.805303  0.636639 0.325133 0.158107    -0.0435296  0.0232101   33   PHE B CD1 
5230  C  CD2 . PHE B 33  ? 0.83783   0.652648 0.31069  0.190778    -0.0660994  0.0277946   33   PHE B CD2 
5231  C  CE1 . PHE B 33  ? 0.799725  0.656498 0.331085 0.16109     -0.0566626  0.00915624  33   PHE B CE1 
5232  C  CE2 . PHE B 33  ? 0.848017  0.691257 0.333594 0.193335    -0.0795639  0.0129494   33   PHE B CE2 
5233  C  CZ  . PHE B 33  ? 0.804379  0.66761  0.3194   0.177773    -0.0744629  0.00361736  33   PHE B CZ  
5234  N  N   . GLN B 34  ? 0.795533  0.591476 0.300582 0.19077     -0.0645318  0.042542    34   GLN B N   
5235  C  CA  . GLN B 34  ? 0.787874  0.606516 0.303221 0.20571     -0.0853865  0.0330974   34   GLN B CA  
5236  C  C   . GLN B 34  ? 0.739447  0.580789 0.298992 0.198288    -0.0892349  0.0268227   34   GLN B C   
5237  O  O   . GLN B 34  ? 0.662351  0.535154 0.247306 0.201914    -0.103544   0.0144118   34   GLN B O   
5238  C  CB  . GLN B 34  ? 0.895486  0.691109 0.366134 0.229098    -0.0944373  0.0400966   34   GLN B CB  
5239  C  CG  . GLN B 34  ? 1.00275   0.765579 0.454769 0.23622     -0.0889208  0.0533629   34   GLN B CG  
5240  C  CD  . GLN B 34  ? 1.02897   0.80948  0.511373 0.240901    -0.0994086  0.0479612   34   GLN B CD  
5241  O  OE1 . GLN B 34  ? 1.06782   0.874629 0.561022 0.254256    -0.117704   0.037594    34   GLN B OE1 
5242  N  NE2 . GLN B 34  ? 1.02939   0.798037 0.527649 0.229442    -0.087893   0.0537043   34   GLN B NE2 
5243  N  N   . SER B 35  ? 0.760704  0.586764 0.33012  0.187235    -0.0760541  0.0347718   35   SER B N   
5244  C  CA  . SER B 35  ? 0.709757  0.557225 0.32084  0.177578    -0.0772702  0.0287091   35   SER B CA  
5245  C  C   . SER B 35  ? 0.64847   0.523915 0.291379 0.161895    -0.0753411  0.0184433   35   SER B C   
5246  O  O   . SER B 35  ? 0.607268  0.511679 0.27914  0.160815    -0.0853283  0.00739884  35   SER B O   
5247  C  CB  . SER B 35  ? 0.743383  0.56933  0.358336 0.167778    -0.0633156  0.0381956   35   SER B CB  
5248  O  OG  . SER B 35  ? 0.872506  0.667454 0.456101 0.181335    -0.0632969  0.0483426   35   SER B OG  
5249  N  N   . VAL B 36  ? 0.622791  0.48876  0.260781 0.149459    -0.0615553  0.0221095   36   VAL B N   
5250  C  CA  . VAL B 36  ? 0.565775  0.455342 0.236833 0.1343      -0.0583662  0.0134586   36   VAL B CA  
5251  C  C   . VAL B 36  ? 0.552807  0.467027 0.23061  0.140501    -0.072855   0.00084384  36   VAL B C   
5252  O  O   . VAL B 36  ? 0.526309  0.465159 0.234949 0.135066    -0.0790012  -0.00894874 36   VAL B O   
5253  C  CB  . VAL B 36  ? 0.573282  0.453456 0.24097  0.121191    -0.0424202  0.0173465   36   VAL B CB  
5254  C  CG1 . VAL B 36  ? 0.537612  0.44227  0.236817 0.109236    -0.0418208  0.00738354  36   VAL B CG1 
5255  C  CG2 . VAL B 36  ? 0.586491  0.446413 0.25293  0.11272     -0.0280987  0.0276843   36   VAL B CG2 
5256  N  N   . ALA B 37  ? 0.58859   0.495064 0.235338 0.153091    -0.0790853  0.00101361  37   ALA B N   
5257  C  CA  . ALA B 37  ? 0.596654  0.525113 0.245104 0.160179    -0.093671   -0.011656   37   ALA B CA  
5258  C  C   . ALA B 37  ? 0.567188  0.522149 0.242647 0.164901    -0.10838    -0.0217094  37   ALA B C   
5259  O  O   . ALA B 37  ? 0.548751  0.529701 0.248323 0.159477    -0.115429   -0.034681   37   ALA B O   
5260  C  CB  . ALA B 37  ? 0.62172   0.533431 0.226885 0.175782    -0.0983668  -0.00783916 37   ALA B CB  
5261  N  N   . ALA B 38  ? 0.604972  0.553694 0.276752 0.175247    -0.112941   -0.0164253  38   ALA B N   
5262  C  CA  . ALA B 38  ? 0.586042  0.561578 0.282833 0.181181    -0.12667    -0.0264526  38   ALA B CA  
5263  C  C   . ALA B 38  ? 0.529374  0.522385 0.267467 0.165184    -0.121227   -0.0310092  38   ALA B C   
5264  O  O   . ALA B 38  ? 0.494866  0.516883 0.260909 0.162758    -0.129844   -0.0433235  38   ALA B O   
5265  C  CB  . ALA B 38  ? 0.631415  0.592833 0.307127 0.20015     -0.133583   -0.0192912  38   ALA B CB  
5266  N  N   . SER B 39  ? 0.544802  0.520991 0.287492 0.153811    -0.106698   -0.0216023  39   SER B N   
5267  C  CA  . SER B 39  ? 0.521224  0.513363 0.300171 0.139395    -0.101885   -0.0259736  39   SER B CA  
5268  C  C   . SER B 39  ? 0.534776  0.545908 0.332222 0.127706    -0.102011   -0.0365669  39   SER B C   
5269  O  O   . SER B 39  ? 0.466808  0.499947 0.293824 0.120252    -0.104899   -0.0455982  39   SER B O   
5270  C  CB  . SER B 39  ? 0.540434  0.512655 0.319828 0.129549    -0.0872751  -0.0153259  39   SER B CB  
5271  O  OG  . SER B 39  ? 0.573892  0.522131 0.331619 0.138692    -0.0847694  -0.00471841 39   SER B OG  
5272  N  N   . TRP B 40  ? 0.541017  0.542384 0.318466 0.127119    -0.0990026  -0.03581    40   TRP B N   
5273  C  CA  . TRP B 40  ? 0.524598  0.539137 0.315067 0.116941    -0.0983093  -0.0454946  40   TRP B CA  
5274  C  C   . TRP B 40  ? 0.50632   0.547637 0.312118 0.120043    -0.11245    -0.0602044  40   TRP B C   
5275  O  O   . TRP B 40  ? 0.480941  0.538906 0.314286 0.108742    -0.112008   -0.0689163  40   TRP B O   
5276  C  CB  . TRP B 40  ? 0.51704   0.516039 0.281944 0.116924    -0.0921978  -0.0424737  40   TRP B CB  
5277  C  CG  . TRP B 40  ? 0.493589  0.506275 0.270453 0.108834    -0.0936292  -0.0542326  40   TRP B CG  
5278  C  CD1 . TRP B 40  ? 0.509015  0.53575  0.282522 0.113532    -0.10511    -0.0663101  40   TRP B CD1 
5279  C  CD2 . TRP B 40  ? 0.471202  0.484281 0.266184 0.0945749   -0.0833213  -0.0556659  40   TRP B CD2 
5280  N  NE1 . TRP B 40  ? 0.498864  0.532551 0.286621 0.102236    -0.101763   -0.0750321  40   TRP B NE1 
5281  C  CE2 . TRP B 40  ? 0.46895   0.493787 0.269105 0.0913558   -0.0885888  -0.0683604  40   TRP B CE2 
5282  C  CE3 . TRP B 40  ? 0.420895  0.425282 0.22701  0.0851297   -0.0707282  -0.0479153  40   TRP B CE3 
5283  C  CZ2 . TRP B 40  ? 0.468494  0.493763 0.283143 0.0796547   -0.0810192  -0.0725105  40   TRP B CZ2 
5284  C  CZ3 . TRP B 40  ? 0.414146  0.42164  0.235357 0.0744409   -0.064244   -0.052279   40   TRP B CZ3 
5285  C  CH2 . TRP B 40  ? 0.40222   0.418783 0.227125 0.0720645   -0.0691177  -0.0639627  40   TRP B CH2 
5286  N  N   . ALA B 41  ? 0.562138  0.607074 0.349262 0.135487    -0.124794   -0.063062   41   ALA B N   
5287  C  CA  . ALA B 41  ? 0.532889  0.605832 0.333317 0.140592    -0.140008   -0.0780721  41   ALA B CA  
5288  C  C   . ALA B 41  ? 0.512146  0.607329 0.34871  0.133999    -0.141935   -0.0844943  41   ALA B C   
5289  O  O   . ALA B 41  ? 0.51552   0.635245 0.375441 0.127093    -0.147695   -0.0985088  41   ALA B O   
5290  C  CB  . ALA B 41  ? 0.569506  0.640652 0.342821 0.161382    -0.152906   -0.0772514  41   ALA B CB  
5291  N  N   . HIS B 42  ? 0.498315  0.584722 0.338035 0.136717    -0.137274   -0.0748066  42   HIS B N   
5292  C  CA  . HIS B 42  ? 0.489541  0.594424 0.360809 0.131247    -0.137366   -0.0793002  42   HIS B CA  
5293  C  C   . HIS B 42  ? 0.451543  0.557819 0.346435 0.111548    -0.125509   -0.0802723  42   HIS B C   
5294  O  O   . HIS B 42  ? 0.398856  0.527227 0.32098  0.102697    -0.127292   -0.0910249  42   HIS B O   
5295  C  CB  . HIS B 42  ? 0.541011  0.630833 0.403581 0.140576    -0.134758   -0.0676968  42   HIS B CB  
5296  C  CG  . HIS B 42  ? 0.565763  0.669332 0.457312 0.134589    -0.131902   -0.0699352  42   HIS B CG  
5297  N  ND1 . HIS B 42  ? 0.572727  0.663781 0.473711 0.122623    -0.118855   -0.0621784  42   HIS B ND1 
5298  C  CD2 . HIS B 42  ? 0.557655  0.687443 0.470237 0.139619    -0.140492   -0.079565   42   HIS B CD2 
5299  C  CE1 . HIS B 42  ? 0.54501   0.652969 0.470519 0.120217    -0.119296   -0.066781   42   HIS B CE1 
5300  N  NE2 . HIS B 42  ? 0.560167  0.691519 0.493146 0.130445    -0.131807   -0.0770653  42   HIS B NE2 
5301  N  N   . ASP B 43  ? 0.430823  0.513144 0.31469  0.10486     -0.113045   -0.0690688  43   ASP B N   
5302  C  CA  . ASP B 43  ? 0.403967  0.485781 0.308154 0.0886185   -0.102175   -0.0686141  43   ASP B CA  
5303  C  C   . ASP B 43  ? 0.407065  0.50176  0.32422  0.0785253   -0.103398   -0.0804487  43   ASP B C   
5304  O  O   . ASP B 43  ? 0.387195  0.488023 0.325848 0.0662874   -0.0977098  -0.083781   43   ASP B O   
5305  C  CB  . ASP B 43  ? 0.418171  0.475417 0.31026  0.0847028   -0.0897763  -0.0554356  43   ASP B CB  
5306  C  CG  . ASP B 43  ? 0.440584  0.487871 0.330217 0.0895987   -0.0868343  -0.0459961  43   ASP B CG  
5307  O  OD1 . ASP B 43  ? 0.449262  0.506724 0.34294  0.098558    -0.0949186  -0.0488029  43   ASP B OD1 
5308  O  OD2 . ASP B 43  ? 0.488829  0.518152 0.370833 0.0856334   -0.0770913  -0.0365241  43   ASP B OD2 
5309  N  N   . THR B 44  ? 0.409927  0.507241 0.312565 0.0837116   -0.110677   -0.0870581  44   THR B N   
5310  C  CA  . THR B 44  ? 0.41649   0.522893 0.329598 0.0736461   -0.111267   -0.0987824  44   THR B CA  
5311  C  C   . THR B 44  ? 0.463046  0.596895 0.391244 0.0756157   -0.123982   -0.113982   44   THR B C   
5312  O  O   . THR B 44  ? 0.452187  0.594997 0.385589 0.0693865   -0.127401   -0.126017   44   THR B O   
5313  C  CB  . THR B 44  ? 0.440238  0.531562 0.329162 0.0755565   -0.109369   -0.0978723  44   THR B CB  
5314  O  OG1 . THR B 44  ? 0.45229   0.545069 0.319165 0.090584    -0.119796   -0.0983041  44   THR B OG1 
5315  C  CG2 . THR B 44  ? 0.418443  0.48581  0.294083 0.0731943   -0.0963583  -0.0843832  44   THR B CG2 
5316  N  N   . ASN B 45  ? 0.448028  0.595427 0.383019 0.0847155   -0.13107    -0.114096   45   ASN B N   
5317  C  CA  . ASN B 45  ? 0.467266  0.643595 0.415095 0.0900097   -0.144724   -0.128633   45   ASN B CA  
5318  C  C   . ASN B 45  ? 0.476677  0.663384 0.43147  0.101023    -0.149476   -0.125303   45   ASN B C   
5319  O  O   . ASN B 45  ? 0.470596  0.655156 0.405709 0.118488    -0.158614   -0.122021   45   ASN B O   
5320  C  CB  . ASN B 45  ? 0.466206  0.643446 0.390904 0.100417    -0.155669   -0.134727   45   ASN B CB  
5321  C  CG  . ASN B 45  ? 0.464834  0.67496  0.403999 0.104662    -0.170921   -0.152703   45   ASN B CG  
5322  O  OD1 . ASN B 45  ? 0.455819  0.689671 0.426426 0.0950531   -0.171523   -0.163303   45   ASN B OD1 
5323  N  ND2 . ASN B 45  ? 0.471946  0.684282 0.388139 0.118467    -0.18298    -0.156976   45   ASN B ND2 
5324  N  N   . ILE B 46  ? 0.472338  0.666266 0.452008 0.0913985   -0.142021   -0.124703   46   ILE B N   
5325  C  CA  . ILE B 46  ? 0.455968  0.656994 0.443358 0.100277    -0.143735   -0.120762   46   ILE B CA  
5326  C  C   . ILE B 46  ? 0.460523  0.69637  0.464988 0.108771    -0.157649   -0.135668   46   ILE B C   
5327  O  O   . ILE B 46  ? 0.42979   0.690825 0.463341 0.0971958   -0.157389   -0.148458   46   ILE B O   
5328  C  CB  . ILE B 46  ? 0.449993  0.646983 0.456489 0.0873748   -0.130753   -0.115533   46   ILE B CB  
5329  C  CG1 . ILE B 46  ? 0.408443  0.57509  0.401465 0.0784088   -0.117706   -0.102768   46   ILE B CG1 
5330  C  CG2 . ILE B 46  ? 0.473823  0.675453 0.484687 0.0981857   -0.13246    -0.111135   46   ILE B CG2 
5331  C  CD1 . ILE B 46  ? 0.403952  0.566361 0.413063 0.067555    -0.106198   -0.0975712  46   ILE B CD1 
5332  N  N   . THR B 47  ? 0.473049  0.709289 0.458636 0.129307    -0.169217   -0.133652   47   THR B N   
5333  C  CA  . THR B 47  ? 0.452558  0.720927 0.451463 0.142553    -0.183622   -0.145867   47   THR B CA  
5334  C  C   . THR B 47  ? 0.474956  0.731009 0.453675 0.164333    -0.18891    -0.13554    47   THR B C   
5335  O  O   . THR B 47  ? 0.465172  0.68675  0.412603 0.171351    -0.184356   -0.120103   47   THR B O   
5336  C  CB  . THR B 47  ? 0.480725  0.767149 0.474355 0.147674    -0.197583   -0.159529   47   THR B CB  
5337  O  OG1 . THR B 47  ? 0.526921  0.790306 0.481435 0.165383    -0.204161   -0.150105   47   THR B OG1 
5338  C  CG2 . THR B 47  ? 0.451546  0.74349  0.458357 0.127203    -0.192579   -0.169318   47   THR B CG2 
5339  N  N   . ALA B 48  ? 0.538163  0.824339 0.534583 0.176016    -0.199619   -0.145763   48   ALA B N   
5340  C  CA  . ALA B 48  ? 0.513136  0.795071 0.493344 0.20017     -0.208602   -0.140452   48   ALA B CA  
5341  C  C   . ALA B 48  ? 0.552648  0.805459 0.489109 0.216374    -0.214908   -0.1303     48   ALA B C   
5342  O  O   . ALA B 48  ? 0.569352  0.789114 0.479267 0.226479    -0.210167   -0.114616   48   ALA B O   
5343  C  CB  . ALA B 48  ? 0.55735   0.883492 0.563732 0.210594    -0.222611   -0.157812   48   ALA B CB  
5344  N  N   . GLU B 49  ? 0.544977  0.80752  0.473184 0.216695    -0.223771   -0.138999   49   GLU B N   
5345  C  CA  . GLU B 49  ? 0.592176  0.831801 0.478447 0.233179    -0.231365   -0.131836   49   GLU B CA  
5346  C  C   . GLU B 49  ? 0.583478  0.777658 0.440548 0.225892    -0.215972   -0.113084   49   GLU B C   
5347  O  O   . GLU B 49  ? 0.605098  0.767882 0.427341 0.240356    -0.215116   -0.0990091  49   GLU B O   
5348  C  CB  . GLU B 49  ? 0.660664  0.921156 0.547012 0.231114    -0.2422     -0.146486   49   GLU B CB  
5349  C  CG  . GLU B 49  ? 0.793722  1.04116  0.63871  0.254353    -0.255481   -0.143174   49   GLU B CG  
5350  C  CD  . GLU B 49  ? 0.888065  1.15269  0.729769 0.280406    -0.272008   -0.147352   49   GLU B CD  
5351  O  OE1 . GLU B 49  ? 1.02005   1.27277  0.825211 0.301998    -0.283818   -0.144056   49   GLU B OE1 
5352  O  OE2 . GLU B 49  ? 0.858028  1.14764  0.732318 0.279994    -0.273077   -0.153995   49   GLU B OE2 
5353  N  N   . ASN B 50  ? 0.566815  0.758423 0.438963 0.203015    -0.203612   -0.113796   50   ASN B N   
5354  C  CA  . ASN B 50  ? 0.535002  0.689705 0.386472 0.193445    -0.188288   -0.0984725  50   ASN B CA  
5355  C  C   . ASN B 50  ? 0.527722  0.658957 0.371967 0.197886    -0.179695   -0.0839585  50   ASN B C   
5356  O  O   . ASN B 50  ? 0.573747  0.671235 0.385312 0.204465    -0.174178   -0.0698389  50   ASN B O   
5357  C  CB  . ASN B 50  ? 0.51862   0.678141 0.387497 0.171039    -0.179199   -0.104054   50   ASN B CB  
5358  C  CG  . ASN B 50  ? 0.533682  0.709061 0.398703 0.171213    -0.189215   -0.117277   50   ASN B CG  
5359  O  OD1 . ASN B 50  ? 0.533533  0.703051 0.369594 0.187735    -0.199389   -0.116637   50   ASN B OD1 
5360  N  ND2 . ASN B 50  ? 0.493064  0.687433 0.385476 0.153626    -0.186697   -0.129538   50   ASN B ND2 
5361  N  N   . ALA B 51  ? 0.528992  0.678236 0.402176 0.195296    -0.179043   -0.0882253  51   ALA B N   
5362  C  CA  . ALA B 51  ? 0.533153  0.662811 0.401048 0.20097     -0.172529   -0.0767005  51   ALA B CA  
5363  C  C   . ALA B 51  ? 0.549195  0.657779 0.382215 0.225145    -0.180503   -0.0682903  51   ALA B C   
5364  O  O   . ALA B 51  ? 0.531287  0.602387 0.336662 0.228234    -0.171775   -0.053062   51   ALA B O   
5365  C  CB  . ALA B 51  ? 0.545463  0.701836 0.450451 0.195162    -0.171588   -0.0849482  51   ALA B CB  
5366  N  N   . ARG B 52  ? 0.597636  0.729223 0.429334 0.242673    -0.197441   -0.0785272  52   ARG B N   
5367  C  CA  . ARG B 52  ? 0.589571  0.702773 0.386674 0.26836     -0.207182   -0.0716896  52   ARG B CA  
5368  C  C   . ARG B 52  ? 0.631425  0.702917 0.384943 0.270107    -0.200337   -0.0570102  52   ARG B C   
5369  O  O   . ARG B 52  ? 0.628999  0.663816 0.35347  0.279101    -0.194338   -0.042369   52   ARG B O   
5370  C  CB  . ARG B 52  ? 0.659272  0.809382 0.465019 0.286141    -0.227643   -0.0873046  52   ARG B CB  
5371  C  CG  . ARG B 52  ? 0.691379  0.840834 0.486019 0.312776    -0.238804   -0.0859     52   ARG B CG  
5372  C  CD  . ARG B 52  ? 0.768857  0.922526 0.534284 0.339324    -0.258006   -0.0897245  52   ARG B CD  
5373  N  NE  . ARG B 52  ? 0.769395  0.946223 0.536856 0.334719    -0.267068   -0.101773   52   ARG B NE  
5374  C  CZ  . ARG B 52  ? 0.80698   0.960466 0.538733 0.336338    -0.267083   -0.0955216  52   ARG B CZ  
5375  N  NH1 . ARG B 52  ? 0.817811  0.92224  0.50818  0.340713    -0.256743   -0.0761576  52   ARG B NH1 
5376  N  NH2 . ARG B 52  ? 0.794542  0.97357  0.531921 0.332792    -0.276695   -0.109192   52   ARG B NH2 
5377  N  N   . ARG B 53  ? 0.658908  0.735106 0.40892  0.259553    -0.199465   -0.0611834  53   ARG B N   
5378  C  CA  . ARG B 53  ? 0.692246  0.734722 0.402614 0.260697    -0.193375   -0.0498496  53   ARG B CA  
5379  C  C   . ARG B 53  ? 0.670746  0.678401 0.372952 0.247593    -0.1739     -0.0343442  53   ARG B C   
5380  O  O   . ARG B 53  ? 0.68768   0.658072 0.353495 0.255248    -0.167613   -0.0201605  53   ARG B O   
5381  C  CB  . ARG B 53  ? 0.737936  0.795201 0.451221 0.2501      -0.195162   -0.0591638  53   ARG B CB  
5382  C  CG  . ARG B 53  ? 0.785243  0.876442 0.50396  0.263824    -0.215474   -0.0754132  53   ARG B CG  
5383  C  CD  . ARG B 53  ? 0.831758  0.925833 0.535328 0.26049     -0.218968   -0.0817254  53   ARG B CD  
5384  N  NE  . ARG B 53  ? 0.859479  0.998416 0.595204 0.257988    -0.232853   -0.102784   53   ARG B NE  
5385  C  CZ  . ARG B 53  ? 0.901226  1.06147  0.62802  0.273045    -0.251116   -0.115082   53   ARG B CZ  
5386  N  NH1 . ARG B 53  ? 0.927581  1.06726  0.610228 0.294234    -0.259001   -0.107848   53   ARG B NH1 
5387  N  NH2 . ARG B 53  ? 0.889933  1.0922   0.651867 0.266315    -0.26125    -0.135156   53   ARG B NH2 
5388  N  N   . GLN B 54  ? 0.658918  0.679899 0.39619  0.227768    -0.164516   -0.0378103  54   GLN B N   
5389  C  CA  . GLN B 54  ? 0.672597  0.667732 0.409212 0.213196    -0.146898   -0.0260314  54   GLN B CA  
5390  C  C   . GLN B 54  ? 0.65111   0.618593 0.368843 0.225326    -0.144206   -0.0145342  54   GLN B C   
5391  O  O   . GLN B 54  ? 0.683942  0.615507 0.373979 0.224122    -0.133307   -0.00124924 54   GLN B O   
5392  C  CB  . GLN B 54  ? 0.684874  0.70695  0.462692 0.192839    -0.142033   -0.0355669  54   GLN B CB  
5393  C  CG  . GLN B 54  ? 0.741859  0.747142 0.52784  0.174575    -0.124944   -0.0272818  54   GLN B CG  
5394  C  CD  . GLN B 54  ? 0.730837  0.724909 0.52127  0.177448    -0.120794   -0.0209481  54   GLN B CD  
5395  O  OE1 . GLN B 54  ? 0.77805   0.793806 0.592264 0.180197    -0.12664    -0.0283266  54   GLN B OE1 
5396  N  NE2 . GLN B 54  ? 0.682667  0.642434 0.447597 0.178553    -0.111401   -0.00790314 54   GLN B NE2 
5397  N  N   . GLU B 55  ? 0.643928  0.627475 0.375748 0.237291    -0.153822   -0.0200995  55   GLU B N   
5398  C  CA  . GLU B 55  ? 0.687869  0.64622  0.401147 0.252116    -0.153578   -0.0109688  55   GLU B CA  
5399  C  C   . GLU B 55  ? 0.724449  0.647986 0.388944 0.270842    -0.156653   -2.544e-05  55   GLU B C   
5400  O  O   . GLU B 55  ? 0.707632  0.592158 0.347311 0.272829    -0.146612   0.0133566   55   GLU B O   
5401  C  CB  . GLU B 55  ? 0.690359  0.680096 0.43158  0.2622      -0.164878   -0.022092   55   GLU B CB  
5402  C  CG  . GLU B 55  ? 0.692223  0.704287 0.475018 0.242082    -0.156737   -0.0285437  55   GLU B CG  
5403  C  CD  . GLU B 55  ? 0.676105  0.730984 0.496209 0.244449    -0.166031   -0.0436068  55   GLU B CD  
5404  O  OE1 . GLU B 55  ? 0.73996   0.801717 0.558567 0.263423    -0.175721   -0.0465976  55   GLU B OE1 
5405  O  OE2 . GLU B 55  ? 0.637347  0.718118 0.4889   0.226948    -0.162447   -0.0523134  55   GLU B OE2 
5406  N  N   . GLU B 56  ? 0.719455  0.655476 0.368809 0.284244    -0.170067   -0.00575477 56   GLU B N   
5407  C  CA  . GLU B 56  ? 0.748194  0.651364 0.348283 0.302223    -0.173164   0.00453591  56   GLU B CA  
5408  C  C   . GLU B 56  ? 0.769771  0.632701 0.343494 0.28845     -0.154289   0.0191732   56   GLU B C   
5409  O  O   . GLU B 56  ? 0.773445  0.595086 0.31053  0.298242    -0.148287   0.0329285   56   GLU B O   
5410  C  CB  . GLU B 56  ? 0.828902  0.752949 0.416797 0.316216    -0.189718   -0.00467693 56   GLU B CB  
5411  C  CG  . GLU B 56  ? 0.883455  0.824477 0.467555 0.343569    -0.209769   -0.0117576  56   GLU B CG  
5412  C  CD  . GLU B 56  ? 0.986579  0.951083 0.558702 0.359116    -0.228308   -0.0224737  56   GLU B CD  
5413  O  OE1 . GLU B 56  ? 1.02728   0.976462 0.562343 0.385342    -0.240081   -0.0182132  56   GLU B OE1 
5414  O  OE2 . GLU B 56  ? 0.997031  0.995355 0.596426 0.345065    -0.231416   -0.0358198  56   GLU B OE2 
5415  N  N   . ALA B 57  ? 0.741634  0.617061 0.336365 0.26528     -0.14428    0.0156902   57   ALA B N   
5416  C  CA  . ALA B 57  ? 0.763509  0.609344 0.33824  0.251059    -0.126972   0.0266051   57   ALA B CA  
5417  C  C   . ALA B 57  ? 0.773975  0.593173 0.351082 0.240772    -0.111666   0.0369238   57   ALA B C   
5418  O  O   . ALA B 57  ? 0.8161    0.597581 0.363416 0.237481    -0.0983173  0.0497452   57   ALA B O   
5419  C  CB  . ALA B 57  ? 0.718635  0.589191 0.318303 0.23168     -0.122559   0.0180984   57   ALA B CB  
5420  N  N   . ALA B 58  ? 0.751352  0.59127  0.364554 0.235007    -0.113362   0.0304228   58   ALA B N   
5421  C  CA  . ALA B 58  ? 0.726617  0.547337 0.347833 0.224179    -0.100382   0.0372858   58   ALA B CA  
5422  C  C   . ALA B 58  ? 0.764032  0.545294 0.349399 0.240724    -0.0994906  0.0486026   58   ALA B C   
5423  O  O   . ALA B 58  ? 0.806632  0.552102 0.372704 0.232963    -0.0848474  0.0597658   58   ALA B O   
5424  C  CB  . ALA B 58  ? 0.691531  0.544901 0.357147 0.216052    -0.103597   0.026896    58   ALA B CB  
5425  N  N   . LEU B 59  ? 0.787892  0.574329 0.361714 0.264085    -0.115089   0.0456497   59   LEU B N   
5426  C  CA  . LEU B 59  ? 0.850578  0.598494 0.383931 0.284994    -0.117216   0.0561962   59   LEU B CA  
5427  C  C   . LEU B 59  ? 0.891249  0.596215 0.376194 0.287096    -0.107575   0.0700441   59   LEU B C   
5428  O  O   . LEU B 59  ? 0.897031  0.557603 0.351596 0.290765    -0.0977675  0.0825481   59   LEU B O   
5429  C  CB  . LEU B 59  ? 0.86832   0.640757 0.402024 0.310257    -0.13861    0.0473438   59   LEU B CB  
5430  C  CG  . LEU B 59  ? 0.926714  0.72377  0.492893 0.317118    -0.146908   0.0382446   59   LEU B CG  
5431  C  CD1 . LEU B 59  ? 0.901219  0.722916 0.465304 0.344103    -0.16841    0.0292081   59   LEU B CD1 
5432  C  CD2 . LEU B 59  ? 0.93945   0.701727 0.497171 0.317759    -0.136783   0.0472147   59   LEU B CD2 
5433  N  N   . LEU B 60  ? 0.874517  0.590733 0.349074 0.286444    -0.110691   0.0677042   60   LEU B N   
5434  C  CA  . LEU B 60  ? 0.889881  0.568377 0.318979 0.287551    -0.100717   0.0800496   60   LEU B CA  
5435  C  C   . LEU B 60  ? 0.899964  0.553154 0.330071 0.263098    -0.0775163  0.0888175   60   LEU B C   
5436  O  O   . LEU B 60  ? 0.935649  0.543826 0.32672  0.26405     -0.0649735  0.102398    60   LEU B O   
5437  C  CB  . LEU B 60  ? 0.908502  0.609438 0.331832 0.289667    -0.108484   0.0734449   60   LEU B CB  
5438  C  CG  . LEU B 60  ? 0.949649  0.666118 0.356532 0.316529    -0.130686   0.0670025   60   LEU B CG  
5439  C  CD1 . LEU B 60  ? 0.953766  0.684428 0.347591 0.31714     -0.135687   0.0618632   60   LEU B CD1 
5440  C  CD2 . LEU B 60  ? 1.01682   0.695947 0.377904 0.343584    -0.13697    0.0778155   60   LEU B CD2 
5441  N  N   . SER B 61  ? 0.844125  0.5265   0.318889 0.241316    -0.0718003  0.0806617   61   SER B N   
5442  C  CA  . SER B 61  ? 0.866643  0.532251 0.348534 0.218016    -0.0514839  0.0864994   61   SER B CA  
5443  C  C   . SER B 61  ? 0.893034  0.523414 0.363054 0.219028    -0.0433728  0.0951532   61   SER B C   
5444  O  O   . SER B 61  ? 0.964668  0.55816  0.411114 0.209619    -0.026626   0.105771    61   SER B O   
5445  C  CB  . SER B 61  ? 0.802536  0.505981 0.333299 0.197416    -0.048773   0.075921    61   SER B CB  
5446  O  OG  . SER B 61  ? 0.836612  0.567115 0.37481  0.195691    -0.0544997  0.0684862   61   SER B OG  
5447  N  N   . GLN B 62  ? 0.859225  0.501789 0.346853 0.229539    -0.0546003  0.0897324   62   GLN B N   
5448  C  CA  . GLN B 62  ? 0.913593  0.523203 0.391519 0.230888    -0.0475069  0.0965431   62   GLN B CA  
5449  C  C   . GLN B 62  ? 0.955324  0.513269 0.377815 0.246753    -0.04355    0.110564    62   GLN B C   
5450  O  O   . GLN B 62  ? 0.964784  0.480336 0.365457 0.239604    -0.0283541  0.120717    62   GLN B O   
5451  C  CB  . GLN B 62  ? 0.896231  0.533854 0.405288 0.24027     -0.0611533  0.0864729   62   GLN B CB  
5452  C  CG  . GLN B 62  ? 0.882478  0.563693 0.442601 0.221868    -0.0612045  0.0745903   62   GLN B CG  
5453  C  CD  . GLN B 62  ? 0.844792  0.564369 0.434416 0.233467    -0.0776339  0.0625743   62   GLN B CD  
5454  O  OE1 . GLN B 62  ? 0.890602  0.619408 0.469399 0.254547    -0.0923442  0.0595828   62   GLN B OE1 
5455  N  NE2 . GLN B 62  ? 0.876579  0.620793 0.504624 0.219548    -0.0751808  0.0548978   62   GLN B NE2 
5456  N  N   . GLU B 63  ? 0.98379   0.543336 0.380741 0.268648    -0.0570726  0.11124     63   GLU B N   
5457  C  CA  . GLU B 63  ? 1.03274   0.542271 0.373715 0.28668     -0.0547759  0.124934    63   GLU B CA  
5458  C  C   . GLU B 63  ? 1.05382   0.527656 0.366854 0.269223    -0.0330764  0.136507    63   GLU B C   
5459  O  O   . GLU B 63  ? 1.08962   0.513466 0.369403 0.269164    -0.0200288  0.148778    63   GLU B O   
5460  C  CB  . GLU B 63  ? 1.06664   0.588531 0.387477 0.315596    -0.0757816  0.121987    63   GLU B CB  
5461  C  CG  . GLU B 63  ? 1.07612   0.650299 0.440506 0.324257    -0.0952826  0.106006    63   GLU B CG  
5462  C  CD  . GLU B 63  ? 1.16866   0.757338 0.521717 0.355932    -0.118264   0.100678    63   GLU B CD  
5463  O  OE1 . GLU B 63  ? 1.20046   0.794512 0.530387 0.367781    -0.127242   0.100353    63   GLU B OE1 
5464  O  OE2 . GLU B 63  ? 1.12285   0.719221 0.490544 0.369136    -0.127484   0.0960175   63   GLU B OE2 
5465  N  N   . PHE B 64  ? 0.990114  0.490084 0.317881 0.254243    -0.0288866  0.131856    64   PHE B N   
5466  C  CA  . PHE B 64  ? 1.02833   0.506306 0.340082 0.234772    -0.00801997 0.139634    64   PHE B CA  
5467  C  C   . PHE B 64  ? 1.04132   0.499869 0.367994 0.212966    0.0102449   0.142977    64   PHE B C   
5468  O  O   . PHE B 64  ? 1.12201   0.534912 0.415365 0.207025    0.027229    0.154854    64   PHE B O   
5469  C  CB  . PHE B 64  ? 0.992168  0.511226 0.329393 0.221845    -0.00853714 0.130416    64   PHE B CB  
5470  C  CG  . PHE B 64  ? 1.00198   0.503237 0.323525 0.203069    0.0126766   0.137154    64   PHE B CG  
5471  C  CD1 . PHE B 64  ? 1.06078   0.5347   0.334226 0.212545    0.0172916   0.146329    64   PHE B CD1 
5472  C  CD2 . PHE B 64  ? 0.965094  0.475751 0.318443 0.17653     0.0286075   0.134426    64   PHE B CD2 
5473  C  CE1 . PHE B 64  ? 1.08265   0.540652 0.342253 0.19478     0.0383714   0.152246    64   PHE B CE1 
5474  C  CE2 . PHE B 64  ? 0.975925  0.472381 0.317072 0.15934     0.0487013   0.139728    64   PHE B CE2 
5475  C  CZ  . PHE B 64  ? 1.02814   0.499366 0.323641 0.167884    0.0540468   0.148378    64   PHE B CZ  
5476  N  N   . ALA B 65  ? 0.981508  0.47481  0.35753  0.200565    0.00704884  0.132084    65   ALA B N   
5477  C  CA  . ALA B 65  ? 0.986382  0.469392 0.382539 0.179011    0.0223067   0.132388    65   ALA B CA  
5478  C  C   . ALA B 65  ? 1.04227   0.476803 0.408805 0.187754    0.0270882   0.141679    65   ALA B C   
5479  O  O   . ALA B 65  ? 1.11214   0.510965 0.462628 0.172942    0.0459258   0.149361    65   ALA B O   
5480  C  CB  . ALA B 65  ? 0.928159  0.457413 0.378481 0.168708    0.0149903   0.118945    65   ALA B CB  
5481  N  N   . GLU B 66  ? 1.02927   0.460786 0.385763 0.212466    0.0105519   0.141063    66   GLU B N   
5482  C  CA  . GLU B 66  ? 1.10188   0.484985 0.426138 0.225006    0.0133654   0.150012    66   GLU B CA  
5483  C  C   . GLU B 66  ? 1.17608   0.503667 0.445906 0.22535     0.0290441   0.165593    66   GLU B C   
5484  O  O   . GLU B 66  ? 1.19319   0.480151 0.448099 0.211448    0.0471895   0.172923    66   GLU B O   
5485  C  CB  . GLU B 66  ? 1.13277   0.529839 0.454845 0.254876    -0.00938508 0.14565     66   GLU B CB  
5486  C  CG  . GLU B 66  ? 1.25123   0.609529 0.553081 0.269924    -0.0104984  0.150716    66   GLU B CG  
5487  C  CD  . GLU B 66  ? 1.2988    0.662722 0.589451 0.303377    -0.031928   0.148265    66   GLU B CD  
5488  O  OE1 . GLU B 66  ? 1.34616   0.682033 0.624868 0.316049    -0.0333661  0.150809    66   GLU B OE1 
5489  O  OE2 . GLU B 66  ? 1.30703   0.704337 0.601416 0.317473    -0.0476729  0.142919    66   GLU B OE2 
5490  N  N   . ALA B 67  ? 1.19237   0.517846 0.431547 0.240884    0.0223997   0.170292    67   ALA B N   
5491  C  CA  . ALA B 67  ? 1.22188   0.49425  0.403591 0.245542    0.0354426   0.18575     67   ALA B CA  
5492  C  C   . ALA B 67  ? 1.22066   0.473764 0.402761 0.214443    0.0620943   0.190627    67   ALA B C   
5493  O  O   . ALA B 67  ? 1.26477   0.464249 0.412205 0.209278    0.0790727   0.202254    67   ALA B O   
5494  C  CB  . ALA B 67  ? 1.22119   0.506968 0.379468 0.263504    0.0233633   0.186676    67   ALA B CB  
5495  N  N   . TRP B 68  ? 1.15929   0.456529 0.381588 0.193495    0.0660533   0.181116    68   TRP B N   
5496  C  CA  . TRP B 68  ? 1.16808   0.456043 0.39363  0.165399    0.0898011   0.183905    68   TRP B CA  
5497  C  C   . TRP B 68  ? 1.19242   0.470863 0.443707 0.143379    0.103119    0.181177    68   TRP B C   
5498  O  O   . TRP B 68  ? 1.2417    0.483904 0.474281 0.126052    0.125115    0.188683    68   TRP B O   
5499  C  CB  . TRP B 68  ? 1.12122   0.459847 0.377762 0.154885    0.0873723   0.174397    68   TRP B CB  
5500  C  CG  . TRP B 68  ? 1.15823   0.489337 0.376066 0.170475    0.0835075   0.180331    68   TRP B CG  
5501  C  CD1 . TRP B 68  ? 1.1661    0.512879 0.371737 0.196014    0.0620128   0.177866    68   TRP B CD1 
5502  C  CD2 . TRP B 68  ? 1.20144   0.501188 0.381909 0.161538    0.103609    0.1907      68   TRP B CD2 
5503  N  NE1 . TRP B 68  ? 1.18095   0.509976 0.344638 0.203692    0.066391    0.185465    68   TRP B NE1 
5504  C  CE2 . TRP B 68  ? 1.21548   0.51474  0.362078 0.183177    0.0921728   0.19389     68   TRP B CE2 
5505  C  CE3 . TRP B 68  ? 1.214     0.488551 0.388273 0.136758    0.130211    0.196519    68   TRP B CE3 
5506  C  CZ2 . TRP B 68  ? 1.25201   0.523928 0.355947 0.181326    0.107137    0.203685    68   TRP B CZ2 
5507  C  CZ3 . TRP B 68  ? 1.25873   0.507124 0.392567 0.13406     0.1459      0.20611     68   TRP B CZ3 
5508  C  CH2 . TRP B 68  ? 1.2783    0.525419 0.377199 0.156373    0.134372    0.209796    68   TRP B CH2 
5509  N  N   . GLY B 69  ? 1.14341   0.452631 0.435488 0.144351    0.0901218   0.170322    69   GLY B N   
5510  C  CA  . GLY B 69  ? 1.17133   0.471405 0.486022 0.126965    0.0996599   0.166739    69   GLY B CA  
5511  C  C   . GLY B 69  ? 1.28133   0.519932 0.555842 0.134252    0.107636    0.177436    69   GLY B C   
5512  O  O   . GLY B 69  ? 1.3421    0.55131  0.613222 0.114263    0.126364    0.18014     69   GLY B O   
5513  N  N   . GLN B 70  ? 1.36119   0.579817 0.604827 0.163393    0.0932394   0.183032    70   GLN B N   
5514  C  CA  . GLN B 70  ? 1.4608    0.616729 0.660083 0.17447     0.0997386   0.19436     70   GLN B CA  
5515  C  C   . GLN B 70  ? 1.4919    0.596129 0.64526  0.163652    0.122597    0.208395    70   GLN B C   
5516  O  O   . GLN B 70  ? 1.50185   0.553527 0.629334 0.156334    0.138187    0.216134    70   GLN B O   
5517  C  CB  . GLN B 70  ? 1.55322   0.701336 0.725122 0.210897    0.0786789   0.197958    70   GLN B CB  
5518  C  CG  . GLN B 70  ? 1.57448   0.776691 0.792189 0.221825    0.0565003   0.183529    70   GLN B CG  
5519  C  CD  . GLN B 70  ? 1.67486   0.863153 0.871415 0.255285    0.0383202   0.185222    70   GLN B CD  
5520  O  OE1 . GLN B 70  ? 1.75783   0.902673 0.902824 0.276199    0.0372889   0.197226    70   GLN B OE1 
5521  N  NE2 . GLN B 70  ? 1.65142   0.877172 0.887677 0.261041    0.0240051   0.172933    70   GLN B NE2 
5522  N  N   . LYS B 71  ? 1.49631   0.614399 0.638345 0.16261     0.12513     0.211473    71   LYS B N   
5523  C  CA  . LYS B 71  ? 1.52148   0.592358 0.618302 0.153045    0.147379    0.224927    71   LYS B CA  
5524  C  C   . LYS B 71  ? 1.52575   0.597167 0.648845 0.116295    0.171298    0.221092    71   LYS B C   
5525  O  O   . LYS B 71  ? 1.57578   0.59446  0.666476 0.103953    0.192973    0.23103     71   LYS B O   
5526  C  CB  . LYS B 71  ? 1.53385   0.619657 0.608868 0.165244    0.141821    0.228707    71   LYS B CB  
5527  C  CG  . LYS B 71  ? 1.65838   0.686677 0.671348 0.166137    0.160737    0.245505    71   LYS B CG  
5528  C  CD  . LYS B 71  ? 1.7217    0.690275 0.673813 0.194887    0.155584    0.259825    71   LYS B CD  
5529  C  CE  . LYS B 71  ? 1.80952   0.721162 0.704068 0.189144    0.17896     0.276141    71   LYS B CE  
5530  N  NZ  . LYS B 71  ? 1.90214   0.773193 0.733623 0.222786    0.168936    0.289543    71   LYS B NZ  
5531  N  N   . ALA B 72  ? 1.4668    0.597131 0.648709 0.0994734   0.166861    0.206193    72   ALA B N   
5532  C  CA  . ALA B 72  ? 1.45878   0.599243 0.670596 0.0656866   0.187166    0.20039     72   ALA B CA  
5533  C  C   . ALA B 72  ? 1.51882   0.629262 0.736762 0.0535392   0.195801    0.198836    72   ALA B C   
5534  O  O   . ALA B 72  ? 1.52702   0.614646 0.743818 0.0280287   0.218426    0.200039    72   ALA B O   
5535  C  CB  . ALA B 72  ? 1.35558   0.564718 0.623894 0.0542532   0.178988    0.185662    72   ALA B CB  
5536  N  N   . LYS B 73  ? 1.53353   0.64358  0.756855 0.0723632   0.177866    0.195713    73   LYS B N   
5537  C  CA  . LYS B 73  ? 1.57351   0.646412 0.792604 0.0670243   0.184054    0.195631    73   LYS B CA  
5538  C  C   . LYS B 73  ? 1.64665   0.644411 0.805441 0.0689739   0.201998    0.211756    73   LYS B C   
5539  O  O   . LYS B 73  ? 1.72874   0.69468  0.88321  0.0449257   0.223433    0.21297     73   LYS B O   
5540  C  CB  . LYS B 73  ? 1.59123   0.681878 0.827095 0.0894937   0.160548    0.188859    73   LYS B CB  
5541  C  CG  . LYS B 73  ? 1.53468   0.696524 0.830325 0.0839021   0.145873    0.172955    73   LYS B CG  
5542  C  CD  . LYS B 73  ? 1.51495   0.687499 0.826781 0.101467    0.127543    0.165996    73   LYS B CD  
5543  C  CE  . LYS B 73  ? 1.47687   0.70743  0.819449 0.115672    0.106143    0.15754     73   LYS B CE  
5544  N  NZ  . LYS B 73  ? 1.48467   0.709505 0.819016 0.143095    0.0885547   0.156823    73   LYS B NZ  
5545  N  N   . GLU B 74  ? 1.6731    0.642498 0.78468  0.0972491   0.193565    0.223884    74   GLU B N   
5546  C  CA  . GLU B 74  ? 1.74017   0.635239 0.788411 0.10238     0.209855    0.240868    74   GLU B CA  
5547  C  C   . GLU B 74  ? 1.75048   0.625639 0.790531 0.0703136   0.239395    0.245184    74   GLU B C   
5548  O  O   . GLU B 74  ? 1.79294   0.613413 0.807892 0.055918    0.259786    0.251714    74   GLU B O   
5549  C  CB  . GLU B 74  ? 1.81889   0.695662 0.818315 0.13489     0.197868    0.253046    74   GLU B CB  
5550  C  CG  . GLU B 74  ? 1.92279   0.754836 0.883919 0.166328    0.185097    0.260714    74   GLU B CG  
5551  C  CD  . GLU B 74  ? 1.95467   0.819581 0.910384 0.199708    0.158293    0.259919    74   GLU B CD  
5552  O  OE1 . GLU B 74  ? 1.94936   0.804832 0.869772 0.209083    0.159907    0.269154    74   GLU B OE1 
5553  O  OE2 . GLU B 74  ? 1.91889   0.822448 0.908454 0.214398    0.136448    0.248853    74   GLU B OE2 
5554  N  N   . LEU B 75  ? 1.71333   0.632175 0.773624 0.0594829   0.24213     0.241288    75   LEU B N   
5555  C  CA  . LEU B 75  ? 1.7264    0.625238 0.770335 0.0345012   0.269676    0.24731     75   LEU B CA  
5556  C  C   . LEU B 75  ? 1.73521   0.655613 0.826614 -0.00213725 0.286157    0.235024    75   LEU B C   
5557  O  O   . LEU B 75  ? 1.8024    0.680627 0.874954 -0.0243182  0.311721    0.240227    75   LEU B O   
5558  C  CB  . LEU B 75  ? 1.67389   0.605899 0.713928 0.0404066   0.266532    0.248857    75   LEU B CB  
5559  C  CG  . LEU B 75  ? 1.71095   0.613663 0.694164 0.0732966   0.255648    0.262656    75   LEU B CG  
5560  C  CD1 . LEU B 75  ? 1.65794   0.601086 0.646271 0.0741898   0.253464    0.260678    75   LEU B CD1 
5561  C  CD2 . LEU B 75  ? 1.79557   0.6161   0.710719 0.0762234   0.27545     0.28118     75   LEU B CD2 
5562  N  N   . TYR B 76  ? 1.67114   0.656191 0.82279  -0.00810568 0.27152     0.218608    76   TYR B N   
5563  C  CA  . TYR B 76  ? 1.67991   0.702208 0.880217 -0.0410761  0.284889    0.205764    76   TYR B CA  
5564  C  C   . TYR B 76  ? 1.71704   0.753788 0.957875 -0.0519416  0.279081    0.192802    76   TYR B C   
5565  O  O   . TYR B 76  ? 1.67585   0.729536 0.949795 -0.0807934  0.293057    0.182958    76   TYR B O   
5566  C  CB  . TYR B 76  ? 1.62082   0.706472 0.852392 -0.039887   0.275625    0.19854     76   TYR B CB  
5567  C  CG  . TYR B 76  ? 1.60196   0.667871 0.788855 -0.0298792  0.283178    0.211356    76   TYR B CG  
5568  C  CD1 . TYR B 76  ? 1.6532    0.672732 0.803196 -0.0460869  0.310944    0.221843    76   TYR B CD1 
5569  C  CD2 . TYR B 76  ? 1.54728   0.636852 0.725276 -0.00353924 0.26277     0.213223    76   TYR B CD2 
5570  C  CE1 . TYR B 76  ? 1.68817   0.686803 0.793421 -0.0361323  0.318433    0.234108    76   TYR B CE1 
5571  C  CE2 . TYR B 76  ? 1.56658   0.63682  0.701218 0.00653213  0.269005    0.224481    76   TYR B CE2 
5572  C  CZ  . TYR B 76  ? 1.65066   0.674944 0.747705 -0.00916336 0.296845    0.235339    76   TYR B CZ  
5573  O  OH  . TYR B 76  ? 1.65746   0.660705 0.708591 0.00096546  0.303961    0.246869    76   TYR B OH  
5574  N  N   . GLU B 77  ? 1.77291   0.804596 1.01148  -0.0287814  0.258584    0.192047    77   GLU B N   
5575  C  CA  . GLU B 77  ? 1.79971   0.848381 1.07609  -0.0356371  0.250523    0.179236    77   GLU B CA  
5576  C  C   . GLU B 77  ? 1.84819   0.864964 1.12692  -0.0661757  0.27423     0.176187    77   GLU B C   
5577  O  O   . GLU B 77  ? 1.78158   0.834416 1.10686  -0.0867142  0.27529     0.1616      77   GLU B O   
5578  C  CB  . GLU B 77  ? 1.84165   0.874972 1.10397  -0.00598394 0.229702    0.181273    77   GLU B CB  
5579  C  CG  . GLU B 77  ? 1.81753   0.887966 1.12701  -0.00849028 0.215656    0.165912    77   GLU B CG  
5580  C  CD  . GLU B 77  ? 1.81255   0.956212 1.17008  -0.00479197 0.197463    0.154359    77   GLU B CD  
5581  O  OE1 . GLU B 77  ? 1.80353   0.967809 1.17218  0.0165545   0.176643    0.150419    77   GLU B OE1 
5582  O  OE2 . GLU B 77  ? 1.78001   0.959985 1.16403  -0.0232696  0.204571    0.148997    77   GLU B OE2 
5583  N  N   . PRO B 78  ? 1.90906   0.857839 1.13812  -0.0709158  0.29424     0.189186    78   PRO B N   
5584  C  CA  . PRO B 78  ? 1.95429   0.875093 1.18636  -0.104266   0.320193    0.185845    78   PRO B CA  
5585  C  C   . PRO B 78  ? 1.90839   0.879921 1.1879   -0.136041   0.332669    0.17305     78   PRO B C   
5586  O  O   . PRO B 78  ? 1.87475   0.86513  1.19237  -0.157237   0.335942    0.15894     78   PRO B O   
5587  C  CB  . PRO B 78  ? 1.98417   0.8294   1.14942  -0.100909   0.339951    0.205045    78   PRO B CB  
5588  C  CG  . PRO B 78  ? 1.98229   0.8022   1.1086   -0.0612589  0.319414    0.216454    78   PRO B CG  
5589  C  CD  . PRO B 78  ? 1.98388   0.877174 1.15052  -0.0444892  0.293005    0.207311    78   PRO B CD  
5590  N  N   . ILE B 79  ? 1.83138   0.82824  1.10999  -0.137533   0.337835    0.176878    79   ILE B N   
5591  C  CA  . ILE B 79  ? 1.74712   0.76258  1.04636  -0.169298   0.360807    0.171169    79   ILE B CA  
5592  C  C   . ILE B 79  ? 1.67802   0.770366 1.02638  -0.17318    0.351493    0.159483    79   ILE B C   
5593  O  O   . ILE B 79  ? 1.60221   0.717875 0.974387 -0.198934   0.368919    0.152385    79   ILE B O   
5594  C  CB  . ILE B 79  ? 1.79249   0.75168  1.03677  -0.174423   0.38561     0.187779    79   ILE B CB  
5595  C  CG1 . ILE B 79  ? 1.76559   0.712275 0.966942 -0.142268   0.373779    0.202883    79   ILE B CG1 
5596  C  CG2 . ILE B 79  ? 1.84124   0.726691 1.049    -0.185352   0.403735    0.194823    79   ILE B CG2 
5597  C  CD1 . ILE B 79  ? 1.81882   0.708869 0.961621 -0.145094   0.397631    0.220156    79   ILE B CD1 
5598  N  N   . TRP B 80  ? 1.63964   0.7716   1.00448  -0.148625   0.324889    0.156643    80   TRP B N   
5599  C  CA  . TRP B 80  ? 1.68318   0.877109 1.08067  -0.147167   0.316705    0.149705    80   TRP B CA  
5600  C  C   . TRP B 80  ? 1.66235   0.913131 1.121    -0.169336   0.316617    0.131152    80   TRP B C   
5601  O  O   . TRP B 80  ? 1.56859   0.862862 1.05252  -0.177364   0.319846    0.125195    80   TRP B O   
5602  C  CB  . TRP B 80  ? 1.67963   0.895231 1.07294  -0.114886   0.289709    0.152677    80   TRP B CB  
5603  C  CG  . TRP B 80  ? 1.66505   0.908715 1.09076  -0.103939   0.266663    0.142684    80   TRP B CG  
5604  C  CD1 . TRP B 80  ? 1.68291   0.89683  1.08994  -0.0858248  0.254209    0.146626    80   TRP B CD1 
5605  C  CD2 . TRP B 80  ? 1.60272   0.909594 1.08358  -0.10917    0.253492    0.127284    80   TRP B CD2 
5606  N  NE1 . TRP B 80  ? 1.61208   0.866861 1.05906  -0.0804114  0.235128    0.134643    80   TRP B NE1 
5607  C  CE2 . TRP B 80  ? 1.59312   0.9038   1.08454  -0.0944686  0.234273    0.123101    80   TRP B CE2 
5608  C  CE3 . TRP B 80  ? 1.54723   0.90651  1.06805  -0.123804   0.256209    0.116786    80   TRP B CE3 
5609  C  CZ2 . TRP B 80  ? 1.54086   0.903934 1.0793   -0.094924   0.218717    0.109564    80   TRP B CZ2 
5610  C  CZ3 . TRP B 80  ? 1.52655   0.93664  1.09328  -0.12303    0.239852    0.103584    80   TRP B CZ3 
5611  C  CH2 . TRP B 80  ? 1.51385   0.924961 1.08839  -0.109188   0.221701    0.100363    80   TRP B CH2 
5612  N  N   . GLN B 81  ? 1.71298   0.963727 1.19453  -0.177853   0.312206    0.121646    81   GLN B N   
5613  C  CA  . GLN B 81  ? 1.63676   0.940074 1.17448  -0.197253   0.310422    0.103584    81   GLN B CA  
5614  C  C   . GLN B 81  ? 1.65908   0.964456 1.2088   -0.229063   0.336881    0.0982596   81   GLN B C   
5615  O  O   . GLN B 81  ? 1.6233    0.976885 1.22004  -0.245969   0.337261    0.082903    81   GLN B O   
5616  C  CB  . GLN B 81  ? 1.5873    0.892853 1.1455   -0.195796   0.296776    0.0941738   81   GLN B CB  
5617  C  CG  . GLN B 81  ? 1.57254   0.904464 1.14033  -0.168084   0.268865    0.0933599   81   GLN B CG  
5618  C  CD  . GLN B 81  ? 1.51727   0.869861 1.11751  -0.169404   0.255148    0.0804085   81   GLN B CD  
5619  O  OE1 . GLN B 81  ? 1.51578   0.830766 1.10069  -0.168472   0.255507    0.0810937   81   GLN B OE1 
5620  N  NE2 . GLN B 81  ? 1.406     0.817496 1.04954  -0.170271   0.242622    0.0686307   81   GLN B NE2 
5621  N  N   . GLN B 82  ? 1.62656   0.881351 1.13344  -0.236259   0.358845    0.110898    82   GLN B N   
5622  C  CA  . GLN B 82  ? 1.62406   0.870484 1.13715  -0.268368   0.38707     0.106628    82   GLN B CA  
5623  C  C   . GLN B 82  ? 1.6166    0.866386 1.11218  -0.271557   0.403293    0.114548    82   GLN B C   
5624  O  O   . GLN B 82  ? 1.6708    0.904388 1.16098  -0.29668    0.430038    0.11442     82   GLN B O   
5625  C  CB  . GLN B 82  ? 1.70455   0.884366 1.18581  -0.279652   0.401766    0.112064    82   GLN B CB  
5626  C  CG  . GLN B 82  ? 1.66695   0.851319 1.1735   -0.281062   0.387663    0.100331    82   GLN B CG  
5627  C  CD  . GLN B 82  ? 1.69942   0.815414 1.1613   -0.268812   0.386479    0.111194    82   GLN B CD  
5628  O  OE1 . GLN B 82  ? 1.77117   0.826887 1.19469  -0.280608   0.408299    0.120418    82   GLN B OE1 
5629  N  NE2 . GLN B 82  ? 1.63276   0.75697  1.09897  -0.24466    0.361267    0.109983    82   GLN B NE2 
5630  N  N   . PHE B 83  ? 1.54847   0.820171 1.03596  -0.247074   0.387832    0.120535    83   PHE B N   
5631  C  CA  . PHE B 83  ? 1.52796   0.81292  1.00498  -0.248646   0.400327    0.125371    83   PHE B CA  
5632  C  C   . PHE B 83  ? 1.46872   0.820338 1.00253  -0.267055   0.403934    0.108069    83   PHE B C   
5633  O  O   . PHE B 83  ? 1.419     0.819331 0.994957 -0.260821   0.38355     0.095924    83   PHE B O   
5634  C  CB  . PHE B 83  ? 1.50304   0.797222 0.959018 -0.217228   0.380903    0.13426     83   PHE B CB  
5635  C  CG  . PHE B 83  ? 1.54127   0.775658 0.938032 -0.193832   0.375461    0.15208     83   PHE B CG  
5636  C  CD1 . PHE B 83  ? 1.60685   0.774688 0.958347 -0.202491   0.396033    0.164029    83   PHE B CD1 
5637  C  CD2 . PHE B 83  ? 1.51317   0.758227 0.899483 -0.162952   0.349829    0.156434    83   PHE B CD2 
5638  C  CE1 . PHE B 83  ? 1.64578   0.758415 0.941502 -0.178732   0.390066    0.180457    83   PHE B CE1 
5639  C  CE2 . PHE B 83  ? 1.57083   0.764514 0.904319 -0.140004   0.343537    0.171664    83   PHE B CE2 
5640  C  CZ  . PHE B 83  ? 1.66714   0.794478 0.95463  -0.146912   0.363243    0.183946    83   PHE B CZ  
5641  N  N   . THR B 84  ? 1.48877   0.842277 1.02182  -0.288172   0.429829    0.107366    84   THR B N   
5642  C  CA  . THR B 84  ? 1.48374   0.899094 1.06902  -0.306439   0.436289    0.0907919   84   THR B CA  
5643  C  C   . THR B 84  ? 1.43545   0.904667 1.04347  -0.28551    0.415193    0.0863264   84   THR B C   
5644  O  O   . THR B 84  ? 1.39961   0.924332 1.05814  -0.289312   0.404035    0.0707652   84   THR B O   
5645  C  CB  . THR B 84  ? 1.53515   0.93808  1.11027  -0.331894   0.469813    0.0921348   84   THR B CB  
5646  O  OG1 . THR B 84  ? 1.56972   0.952814 1.102    -0.31539    0.474105    0.106867    84   THR B OG1 
5647  C  CG2 . THR B 84  ? 1.5268    0.87451  1.07948  -0.355016   0.492707    0.0960674   84   THR B CG2 
5648  N  N   . ASP B 85  ? 1.43649   0.888012 1.00598  -0.263114   0.40953     0.0997062   85   ASP B N   
5649  C  CA  . ASP B 85  ? 1.38739   0.881726 0.970946 -0.242194   0.390165    0.0969195   85   ASP B CA  
5650  C  C   . ASP B 85  ? 1.38858   0.906919 0.998066 -0.225638   0.360294    0.0904991   85   ASP B C   
5651  O  O   . ASP B 85  ? 1.44286   0.928491 1.02615  -0.209059   0.346725    0.0991487   85   ASP B O   
5652  C  CB  . ASP B 85  ? 1.36882   0.834028 0.90201  -0.225766   0.394667    0.11206     85   ASP B CB  
5653  C  CG  . ASP B 85  ? 1.33484   0.825037 0.865347 -0.198279   0.371448    0.113408    85   ASP B CG  
5654  O  OD1 . ASP B 85  ? 1.28718   0.824265 0.859116 -0.191408   0.351548    0.101886    85   ASP B OD1 
5655  O  OD2 . ASP B 85  ? 1.30099   0.761713 0.785818 -0.183358   0.373121    0.126114    85   ASP B OD2 
5656  N  N   . PRO B 86  ? 1.33175   0.90807  0.993256 -0.228935   0.349065    0.074949    86   PRO B N   
5657  C  CA  . PRO B 86  ? 1.25167   0.850571 0.935783 -0.213003   0.32169     0.0693919   86   PRO B CA  
5658  C  C   . PRO B 86  ? 1.20158   0.804891 0.868838 -0.184633   0.300901    0.0761806   86   PRO B C   
5659  O  O   . PRO B 86  ? 1.19524   0.79641  0.864158 -0.169886   0.280876    0.0766667   86   PRO B O   
5660  C  CB  . PRO B 86  ? 1.20078   0.858045 0.941891 -0.226234   0.319098    0.0512776   86   PRO B CB  
5661  C  CG  . PRO B 86  ? 1.21538   0.892202 0.962538 -0.238707   0.339052    0.0483877   86   PRO B CG  
5662  C  CD  . PRO B 86  ? 1.28112   0.903534 0.981058 -0.247026   0.362038    0.0620153   86   PRO B CD  
5663  N  N   . GLN B 87  ? 1.16123   0.771482 0.813071 -0.177721   0.306076    0.0804697   87   GLN B N   
5664  C  CA  . GLN B 87  ? 1.1194    0.735108 0.754933 -0.152489   0.287921    0.0856416   87   GLN B CA  
5665  C  C   . GLN B 87  ? 1.12279   0.689658 0.712484 -0.135332   0.28007     0.0995334   87   GLN B C   
5666  O  O   . GLN B 87  ? 0.994811  0.568506 0.585009 -0.115925   0.257995    0.0999295   87   GLN B O   
5667  C  CB  . GLN B 87  ? 1.13646   0.77261  0.767416 -0.148866   0.294358    0.0852816   87   GLN B CB  
5668  C  CG  . GLN B 87  ? 1.10466   0.795384 0.77647  -0.142255   0.279212    0.0729705   87   GLN B CG  
5669  C  CD  . GLN B 87  ? 1.13157   0.842371 0.799803 -0.138758   0.28608     0.0713931   87   GLN B CD  
5670  O  OE1 . GLN B 87  ? 1.11746   0.809177 0.749901 -0.124391   0.283993    0.0799844   87   GLN B OE1 
5671  N  NE2 . GLN B 87  ? 1.14365   0.8949   0.849686 -0.151088   0.293719    0.0594224   87   GLN B NE2 
5672  N  N   . LEU B 88  ? 1.21212   0.730386 0.763133 -0.142947   0.298809    0.110375    88   LEU B N   
5673  C  CA  . LEU B 88  ? 1.23517   0.700113 0.740174 -0.129033   0.294988    0.123949    88   LEU B CA  
5674  C  C   . LEU B 88  ? 1.15698   0.615103 0.676367 -0.125776   0.280789    0.120695    88   LEU B C   
5675  O  O   . LEU B 88  ? 1.09654   0.538374 0.596501 -0.104431   0.26352     0.126511    88   LEU B O   
5676  C  CB  . LEU B 88  ? 1.27178   0.686943 0.737642 -0.143067   0.321833    0.134614    88   LEU B CB  
5677  C  CG  . LEU B 88  ? 1.36917   0.743873 0.776918 -0.127806   0.327542    0.150279    88   LEU B CG  
5678  C  CD1 . LEU B 88  ? 1.37696   0.690903 0.745857 -0.140952   0.350647    0.16146     88   LEU B CD1 
5679  C  CD2 . LEU B 88  ? 1.31452   0.680371 0.695753 -0.0961607  0.302965    0.157261    88   LEU B CD2 
5680  N  N   . ARG B 89  ? 1.16383   0.632104 0.714849 -0.147242   0.289309    0.111324    89   ARG B N   
5681  C  CA  . ARG B 89  ? 1.18997   0.654197 0.757297 -0.14667    0.277546    0.106411    89   ARG B CA  
5682  C  C   . ARG B 89  ? 1.15456   0.654463 0.744804 -0.126543   0.250111    0.100765    89   ARG B C   
5683  O  O   . ARG B 89  ? 1.1179    0.599677 0.696606 -0.111621   0.23597     0.104125    89   ARG B O   
5684  C  CB  . ARG B 89  ? 1.23958   0.721279 0.843747 -0.174261   0.290575    0.0941133   89   ARG B CB  
5685  C  CG  . ARG B 89  ? 1.35502   0.788556 0.934366 -0.194015   0.315039    0.0995297   89   ARG B CG  
5686  C  CD  . ARG B 89  ? 1.39994   0.83965  1.01138  -0.216209   0.320562    0.0871721   89   ARG B CD  
5687  N  NE  . ARG B 89  ? 1.44461   0.933361 1.10163  -0.237958   0.329641    0.0724052   89   ARG B NE  
5688  C  CZ  . ARG B 89  ? 1.37707   0.924012 1.07952  -0.236102   0.315164    0.0592057   89   ARG B CZ  
5689  N  NH1 . ARG B 89  ? 1.42257   0.987402 1.13535  -0.215905   0.290537    0.0575514   89   ARG B NH1 
5690  N  NH2 . ARG B 89  ? 1.32408   0.910988 1.06179  -0.254755   0.325894    0.0472664   89   ARG B NH2 
5691  N  N   . ARG B 90  ? 1.1124    0.662485 0.73514  -0.126419   0.243434    0.091876    90   ARG B N   
5692  C  CA  . ARG B 90  ? 1.15294   0.736553 0.794552 -0.107896   0.219586    0.0872411   90   ARG B CA  
5693  C  C   . ARG B 90  ? 1.15257   0.711743 0.756275 -0.0833845  0.20758     0.0982262   90   ARG B C   
5694  O  O   . ARG B 90  ? 1.08774   0.6462   0.693147 -0.0688794  0.190182    0.0979491   90   ARG B O   
5695  C  CB  . ARG B 90  ? 1.12323   0.757728 0.798122 -0.110702   0.216728    0.0776982   90   ARG B CB  
5696  C  CG  . ARG B 90  ? 1.11774   0.789987 0.838976 -0.128231   0.219519    0.0639018   90   ARG B CG  
5697  C  CD  . ARG B 90  ? 1.0655    0.783742 0.81272  -0.124136   0.21327     0.0563717   90   ARG B CD  
5698  N  NE  . ARG B 90  ? 1.12458   0.880036 0.911833 -0.123911   0.198862    0.0449974   90   ARG B NE  
5699  C  CZ  . ARG B 90  ? 1.10601   0.877039 0.902323 -0.107893   0.178668    0.0432997   90   ARG B CZ  
5700  N  NH1 . ARG B 90  ? 1.07388   0.879701 0.905937 -0.109802   0.169021    0.0328796   90   ARG B NH1 
5701  N  NH2 . ARG B 90  ? 1.08021   0.83335  0.850362 -0.0901018  0.168243    0.05145     90   ARG B NH2 
5702  N  N   . ILE B 91  ? 1.08083   0.62073  0.650355 -0.0786094  0.216868    0.10728     91   ILE B N   
5703  C  CA  . ILE B 91  ? 1.06194   0.584218 0.597157 -0.0544051  0.203876    0.116107    91   ILE B CA  
5704  C  C   . ILE B 91  ? 1.07205   0.550095 0.578322 -0.0444005  0.199803    0.124487    91   ILE B C   
5705  O  O   . ILE B 91  ? 1.06999   0.55108  0.573341 -0.0248639  0.180431    0.124832    91   ILE B O   
5706  C  CB  . ILE B 91  ? 1.12615   0.636019 0.627982 -0.0504149  0.21422     0.123807    91   ILE B CB  
5707  C  CG1 . ILE B 91  ? 1.06324   0.616951 0.593343 -0.0596114  0.219172    0.114837    91   ILE B CG1 
5708  C  CG2 . ILE B 91  ? 1.16662   0.659793 0.633607 -0.0237709  0.1979      0.13165     91   ILE B CG2 
5709  C  CD1 . ILE B 91  ? 1.08331   0.622159 0.589493 -0.0701963  0.241983    0.120196    91   ILE B CD1 
5710  N  N   . ILE B 92  ? 1.09553   0.533016 0.581771 -0.057653   0.217851    0.130444    92   ILE B N   
5711  C  CA  . ILE B 92  ? 1.18737   0.576071 0.638402 -0.0456887  0.215118    0.139989    92   ILE B CA  
5712  C  C   . ILE B 92  ? 1.21049   0.611691 0.688651 -0.0407606  0.199035    0.132328    92   ILE B C   
5713  O  O   . ILE B 92  ? 1.24834   0.633526 0.708258 -0.0195497  0.184236    0.13675     92   ILE B O   
5714  C  CB  . ILE B 92  ? 1.27804   0.612853 0.694193 -0.0600439  0.239513    0.149658    92   ILE B CB  
5715  C  CG1 . ILE B 92  ? 1.3198    0.633702 0.697068 -0.0592552  0.254396    0.160244    92   ILE B CG1 
5716  C  CG2 . ILE B 92  ? 1.28889   0.573576 0.674353 -0.0488884  0.236185    0.15756     92   ILE B CG2 
5717  C  CD1 . ILE B 92  ? 1.32289   0.627987 0.664998 -0.0303449  0.238871    0.168814    92   ILE B CD1 
5718  N  N   . GLY B 93  ? 1.15378   0.584012 0.674698 -0.0596218  0.201916    0.120496    93   GLY B N   
5719  C  CA  . GLY B 93  ? 1.15043   0.599687 0.700494 -0.0554343  0.186286    0.111766    93   GLY B CA  
5720  C  C   . GLY B 93  ? 1.13978   0.618527 0.699465 -0.0325193  0.162624    0.109396    93   GLY B C   
5721  O  O   . GLY B 93  ? 1.18237   0.654984 0.741827 -0.0192415  0.149329    0.108639    93   GLY B O   
5722  N  N   . ALA B 94  ? 1.0544    0.565127 0.622971 -0.0284402  0.158045    0.10752     94   ALA B N   
5723  C  CA  . ALA B 94  ? 1.02072   0.560226 0.598348 -0.00895366 0.137331    0.104606    94   ALA B CA  
5724  C  C   . ALA B 94  ? 1.01551   0.523104 0.552966 0.0141269   0.128491    0.114467    94   ALA B C   
5725  O  O   . ALA B 94  ? 0.967208  0.481456 0.509686 0.0296766   0.112071    0.112217    94   ALA B O   
5726  C  CB  . ALA B 94  ? 0.944488  0.520095 0.53751  -0.0113514  0.136656    0.10027     94   ALA B CB  
5727  N  N   . VAL B 95  ? 1.12376   0.594566 0.620188 0.0158606   0.140635    0.125438    95   VAL B N   
5728  C  CA  . VAL B 95  ? 1.09492   0.533216 0.547572 0.0387721   0.133349    0.135812    95   VAL B CA  
5729  C  C   . VAL B 95  ? 1.07973   0.490586 0.521645 0.0504909   0.125699    0.138299    95   VAL B C   
5730  O  O   . VAL B 95  ? 1.03072   0.438761 0.458426 0.0737832   0.109298    0.140325    95   VAL B O   
5731  C  CB  . VAL B 95  ? 1.15725   0.55665  0.567053 0.0342295   0.152067    0.14751     95   VAL B CB  
5732  C  CG1 . VAL B 95  ? 1.19543   0.564674 0.557942 0.0604486   0.142687    0.158092    95   VAL B CG1 
5733  C  CG2 . VAL B 95  ? 1.1677    0.595727 0.590782 0.0211996   0.161432    0.143824    95   VAL B CG2 
5734  N  N   . ARG B 96  ? 1.10842   0.499114 0.55726  0.0341429   0.137996    0.137378    96   ARG B N   
5735  C  CA  . ARG B 96  ? 1.1413    0.499057 0.577139 0.0420353   0.134995    0.139883    96   ARG B CA  
5736  C  C   . ARG B 96  ? 1.1009    0.494616 0.576195 0.0468761   0.118139    0.128261    96   ARG B C   
5737  O  O   . ARG B 96  ? 1.137     0.509115 0.608297 0.0517186   0.115571    0.127892    96   ARG B O   
5738  C  CB  . ARG B 96  ? 1.23817   0.559716 0.663639 0.0187373   0.158383    0.143243    96   ARG B CB  
5739  C  CG  . ARG B 96  ? 1.3551    0.642591 0.777054 0.0123349   0.164242    0.142585    96   ARG B CG  
5740  C  CD  . ARG B 96  ? 1.35392   0.672949 0.823589 -0.010797   0.167761    0.128786    96   ARG B CD  
5741  N  NE  . ARG B 96  ? 1.3166    0.679612 0.823066 -0.0015789  0.147899    0.118024    96   ARG B NE  
5742  C  CZ  . ARG B 96  ? 1.27323   0.628755 0.781264 0.0116      0.136159    0.115366    96   ARG B CZ  
5743  N  NH1 . ARG B 96  ? 1.21938   0.616448 0.755923 0.0229353   0.118046    0.107371    96   ARG B NH1 
5744  N  NH2 . ARG B 96  ? 1.31112   0.616206 0.790049 0.0145192   0.142864    0.121062    96   ARG B NH2 
5745  N  N   . THR B 97  ? 1.05038   0.496504 0.561469 0.0462961   0.107091    0.119003    97   THR B N   
5746  C  CA  . THR B 97  ? 1.00072   0.48191  0.546072 0.0530447   0.090563    0.108799    97   THR B CA  
5747  C  C   . THR B 97  ? 0.947798  0.4453   0.486049 0.0776809   0.0719473   0.109273    97   THR B C   
5748  O  O   . THR B 97  ? 0.926414  0.451786 0.472361 0.0794602   0.0670985   0.107214    97   THR B O   
5749  C  CB  . THR B 97  ? 0.938781  0.465157 0.528861 0.0345119   0.0918727   0.0978324   97   THR B CB  
5750  O  OG1 . THR B 97  ? 0.992065  0.50241  0.588393 0.0135372   0.107445    0.096238    97   THR B OG1 
5751  C  CG2 . THR B 97  ? 0.910684  0.472558 0.535073 0.0397632   0.0766359   0.0876879   97   THR B CG2 
5752  N  N   . LEU B 98  ? 0.94431   0.425881 0.469331 0.0966675   0.0613059   0.110863    98   LEU B N   
5753  C  CA  . LEU B 98  ? 0.952847  0.443513 0.464295 0.121403    0.0448232   0.112237    98   LEU B CA  
5754  C  C   . LEU B 98  ? 0.937624  0.479036 0.487211 0.127333    0.0281784   0.100667    98   LEU B C   
5755  O  O   . LEU B 98  ? 0.965549  0.525491 0.511375 0.14234     0.0157337   0.0994464   98   LEU B O   
5756  C  CB  . LEU B 98  ? 1.01631   0.464263 0.491088 0.141793    0.0412423   0.120068    98   LEU B CB  
5757  C  CG  . LEU B 98  ? 1.06716   0.464619 0.491211 0.146152    0.0526591   0.134026    98   LEU B CG  
5758  C  CD1 . LEU B 98  ? 1.0872    0.458446 0.507131 0.119746    0.0755479   0.137943    98   LEU B CD1 
5759  C  CD2 . LEU B 98  ? 1.09402   0.453061 0.484087 0.170379    0.0455859   0.140637    98   LEU B CD2 
5760  N  N   . GLY B 99  ? 0.90001   0.462595 0.48444  0.116375    0.0277023   0.0919876   99   GLY B N   
5761  C  CA  . GLY B 99  ? 0.804039  0.413281 0.423886 0.120124    0.0139906   0.0814254   99   GLY B CA  
5762  C  C   . GLY B 99  ? 0.778045  0.389978 0.391223 0.144313    -0.00148116 0.0798447   99   GLY B C   
5763  O  O   . GLY B 99  ? 0.821218  0.400005 0.411351 0.155723    -0.0011716  0.0847262   99   GLY B O   
5764  N  N   . SER B 100 ? 0.726354  0.376134 0.357485 0.152744    -0.0146644  0.0730808   100  SER B N   
5765  C  CA  . SER B 100 ? 0.738263  0.397141 0.366875 0.175685    -0.0300343  0.0698012   100  SER B CA  
5766  C  C   . SER B 100 ? 0.847901  0.472131 0.43303  0.195966    -0.0333855  0.0791516   100  SER B C   
5767  O  O   . SER B 100 ? 0.885927  0.51458  0.464667 0.217925    -0.046712   0.0769605   100  SER B O   
5768  C  CB  . SER B 100 ? 0.700498  0.4072   0.357226 0.178615    -0.0424408  0.0599265   100  SER B CB  
5769  O  OG  . SER B 100 ? 0.724387  0.437553 0.368684 0.180309    -0.0447968  0.0618648   100  SER B OG  
5770  N  N   . ALA B 101 ? 0.874828  0.466378 0.429981 0.189199    -0.0214566  0.0892292   101  ALA B N   
5771  C  CA  . ALA B 101 ? 0.935155  0.487178 0.443425 0.207635    -0.0224309  0.0999054   101  ALA B CA  
5772  C  C   . ALA B 101 ? 0.973134  0.484729 0.461306 0.216588    -0.019021   0.105211    101  ALA B C   
5773  O  O   . ALA B 101 ? 1.0434    0.520866 0.492517 0.236815    -0.022477   0.113503    101  ALA B O   
5774  C  CB  . ALA B 101 ? 0.949928  0.476945 0.431607 0.1959      -0.00820319 0.109289    101  ALA B CB  
5775  N  N   . ASN B 102 ? 0.945501  0.457595 0.457386 0.201059    -0.0112735  0.100857    102  ASN B N   
5776  C  CA  . ASN B 102 ? 0.97413   0.446126 0.468234 0.20663     -0.00632351 0.104871    102  ASN B CA  
5777  C  C   . ASN B 102 ? 0.956476  0.44553  0.459898 0.230133    -0.0231391  0.0982447   102  ASN B C   
5778  O  O   . ASN B 102 ? 0.991249  0.447005 0.475221 0.242467    -0.022788   0.101489    102  ASN B O   
5779  C  CB  . ASN B 102 ? 0.979388  0.448009 0.49628  0.182857    0.00642068  0.100724    102  ASN B CB  
5780  C  CG  . ASN B 102 ? 1.02301   0.462074 0.524054 0.161226    0.0254682   0.108122    102  ASN B CG  
5781  O  OD1 . ASN B 102 ? 1.03522   0.42534  0.495707 0.165419    0.0344926   0.119088    102  ASN B OD1 
5782  N  ND2 . ASN B 102 ? 0.954162  0.423131 0.486475 0.138349    0.031961    0.102145    102  ASN B ND2 
5783  N  N   . LEU B 103 ? 0.885208  0.424689 0.41734  0.2362      -0.0370795  0.0888072   103  LEU B N   
5784  C  CA  . LEU B 103 ? 0.891379  0.452641 0.436907 0.257262    -0.0524441  0.0808772   103  LEU B CA  
5785  C  C   . LEU B 103 ? 0.974779  0.513013 0.482392 0.286235    -0.062752   0.0872819   103  LEU B C   
5786  O  O   . LEU B 103 ? 0.993034  0.519247 0.474705 0.289235    -0.0623429  0.0945161   103  LEU B O   
5787  C  CB  . LEU B 103 ? 0.843645  0.464839 0.430437 0.254772    -0.0636056  0.0684274   103  LEU B CB  
5788  C  CG  . LEU B 103 ? 0.819451  0.468896 0.447055 0.231355    -0.0569379  0.0601559   103  LEU B CG  
5789  C  CD1 . LEU B 103 ? 0.785262  0.4854   0.445263 0.223654    -0.0637608  0.0512874   103  LEU B CD1 
5790  C  CD2 . LEU B 103 ? 0.806107  0.457917 0.448772 0.237547    -0.0591816  0.0538644   103  LEU B CD2 
5791  N  N   . PRO B 104 ? 1.00554   0.541681 0.510715 0.309144    -0.0732757  0.0837305   104  PRO B N   
5792  C  CA  . PRO B 104 ? 1.0514    0.578897 0.527564 0.340343    -0.0876073  0.0867349   104  PRO B CA  
5793  C  C   . PRO B 104 ? 1.00905   0.593132 0.512164 0.343304    -0.101647   0.0766982   104  PRO B C   
5794  O  O   . PRO B 104 ? 0.895379  0.518045 0.437394 0.322926    -0.0991889  0.0681952   104  PRO B O   
5795  C  CB  . PRO B 104 ? 1.06026   0.580121 0.537436 0.361157    -0.0947121  0.0824787   104  PRO B CB  
5796  C  CG  . PRO B 104 ? 1.01876   0.563349 0.538605 0.33986     -0.0876072  0.0728671   104  PRO B CG  
5797  C  CD  . PRO B 104 ? 0.984366  0.527352 0.514098 0.30725     -0.0722294  0.0760749   104  PRO B CD  
5798  N  N   . LEU B 105 ? 1.04559   0.632128 0.526252 0.369691    -0.116514   0.0775109   105  LEU B N   
5799  C  CA  . LEU B 105 ? 1.02043   0.649876 0.513335 0.375243    -0.130056   0.0700511   105  LEU B CA  
5800  C  C   . LEU B 105 ? 0.970944  0.661474 0.515496 0.37394     -0.141002   0.052859    105  LEU B C   
5801  O  O   . LEU B 105 ? 0.935906  0.664436 0.508532 0.358042    -0.142031   0.0453168   105  LEU B O   
5802  C  CB  . LEU B 105 ? 1.10085   0.712131 0.551405 0.404913    -0.142987   0.0758474   105  LEU B CB  
5803  C  CG  . LEU B 105 ? 1.17405   0.721622 0.568253 0.40758     -0.131525   0.0939148   105  LEU B CG  
5804  C  CD1 . LEU B 105 ? 1.24605   0.772209 0.595308 0.441       -0.145338   0.0999654   105  LEU B CD1 
5805  C  CD2 . LEU B 105 ? 1.18866   0.732781 0.579426 0.381863    -0.118308   0.0990257   105  LEU B CD2 
5806  N  N   . ALA B 106 ? 0.977389  0.677217 0.534916 0.389647    -0.148105   0.0463521   106  ALA B N   
5807  C  CA  . ALA B 106 ? 0.922589  0.68102  0.528729 0.388206    -0.157343   0.0297811   106  ALA B CA  
5808  C  C   . ALA B 106 ? 0.893621  0.670758 0.53656  0.356636    -0.144145   0.0253807   106  ALA B C   
5809  O  O   . ALA B 106 ? 0.846488  0.672561 0.529131 0.347141    -0.148502   0.0130441   106  ALA B O   
5810  C  CB  . ALA B 106 ? 0.911992  0.675629 0.52277  0.412645    -0.166746   0.0237606   106  ALA B CB  
5811  N  N   . LYS B 107 ? 0.873845  0.611964 0.503758 0.340567    -0.127954   0.0349353   107  LYS B N   
5812  C  CA  . LYS B 107 ? 0.830057  0.586369 0.493609 0.312583    -0.116661   0.0304407   107  LYS B CA  
5813  C  C   . LYS B 107 ? 0.834121  0.601308 0.501847 0.292803    -0.111759   0.0323793   107  LYS B C   
5814  O  O   . LYS B 107 ? 0.775669  0.574699 0.476972 0.273377    -0.10817    0.0252836   107  LYS B O   
5815  C  CB  . LYS B 107 ? 0.838689  0.55618  0.492534 0.303034    -0.102708   0.0368016   107  LYS B CB  
5816  C  CG  . LYS B 107 ? 0.846     0.565125 0.50821  0.318942    -0.107366   0.0307279   107  LYS B CG  
5817  C  CD  . LYS B 107 ? 0.934605  0.607311 0.579084 0.312687    -0.0944301  0.0375847   107  LYS B CD  
5818  C  CE  . LYS B 107 ? 0.990615  0.659852 0.640712 0.327848    -0.0974607  0.0317165   107  LYS B CE  
5819  N  NZ  . LYS B 107 ? 0.980468  0.63745  0.642626 0.306368    -0.0839373  0.0307347   107  LYS B NZ  
5820  N  N   . ARG B 108 ? 0.861979  0.600046 0.493079 0.298856    -0.111151   0.0423635   108  ARG B N   
5821  C  CA  . ARG B 108 ? 0.869307  0.612954 0.497626 0.283631    -0.106668   0.0449914   108  ARG B CA  
5822  C  C   . ARG B 108 ? 0.805849  0.601192 0.463116 0.285013    -0.119328   0.0324768   108  ARG B C   
5823  O  O   . ARG B 108 ? 0.756204  0.573687 0.43542  0.265248    -0.114583   0.028458    108  ARG B O   
5824  C  CB  . ARG B 108 ? 0.915991  0.623464 0.497747 0.29512     -0.106537   0.0565197   108  ARG B CB  
5825  C  CG  . ARG B 108 ? 0.964959  0.624887 0.521014 0.280415    -0.0881593  0.0693949   108  ARG B CG  
5826  C  CD  . ARG B 108 ? 1.02865   0.656648 0.538675 0.2932      -0.0887809  0.0800262   108  ARG B CD  
5827  N  NE  . ARG B 108 ? 1.08884   0.663165 0.566379 0.284572    -0.071546   0.0934685   108  ARG B NE  
5828  C  CZ  . ARG B 108 ? 1.16868   0.703379 0.598939 0.296653    -0.0691786  0.105209    108  ARG B CZ  
5829  N  NH1 . ARG B 108 ? 1.13738   0.683633 0.550397 0.31537     -0.0827005  0.104535    108  ARG B NH1 
5830  N  NH2 . ARG B 108 ? 1.25841   0.742203 0.658451 0.289218    -0.0529342  0.117175    108  ARG B NH2 
5831  N  N   . GLN B 109 ? 0.811639  0.623481 0.466905 0.309074    -0.135163   0.0264367   109  GLN B N   
5832  C  CA  . GLN B 109 ? 0.797089  0.659956 0.481333 0.313646    -0.149024   0.0123518   109  GLN B CA  
5833  C  C   . GLN B 109 ? 0.736032  0.631027 0.464984 0.293393    -0.143041   0.00306083  109  GLN B C   
5834  O  O   . GLN B 109 ? 0.65652   0.568196 0.402665 0.273494    -0.137805   0.00027756  109  GLN B O   
5835  C  CB  . GLN B 109 ? 0.890713  0.765845 0.568505 0.3436      -0.166186   0.00654595  109  GLN B CB  
5836  C  CG  . GLN B 109 ? 0.910201  0.816709 0.588372 0.355293    -0.18213    -0.0019083  109  GLN B CG  
5837  C  CD  . GLN B 109 ? 0.974403  0.875389 0.626896 0.388773    -0.198372   -0.00217147 109  GLN B CD  
5838  O  OE1 . GLN B 109 ? 0.962711  0.88434  0.631821 0.404871    -0.20761    -0.0105552  109  GLN B OE1 
5839  N  NE2 . GLN B 109 ? 0.981022  0.853632 0.591204 0.400745    -0.201995   0.00705618  109  GLN B NE2 
5840  N  N   . GLN B 110 ? 0.741984  0.637747 0.484344 0.297907    -0.141614   0.00028344  110  GLN B N   
5841  C  CA  . GLN B 110 ? 0.676762  0.605247 0.460412 0.283443    -0.137747   -0.00964411 110  GLN B CA  
5842  C  C   . GLN B 110 ? 0.601411  0.530102 0.399171 0.254872    -0.124378   -0.00734326 110  GLN B C   
5843  O  O   . GLN B 110 ? 0.563012  0.526284 0.393301 0.241667    -0.12387    -0.0164488  110  GLN B O   
5844  C  CB  . GLN B 110 ? 0.707464  0.628428 0.496666 0.292483    -0.135994   -0.0111083  110  GLN B CB  
5845  C  CG  . GLN B 110 ? 0.733901  0.698172 0.566193 0.283889    -0.136074   -0.0241743  110  GLN B CG  
5846  C  CD  . GLN B 110 ? 0.813312  0.77438  0.652584 0.293966    -0.134769   -0.0273113  110  GLN B CD  
5847  O  OE1 . GLN B 110 ? 0.816876  0.763972 0.638114 0.317642    -0.142227   -0.0262298  110  GLN B OE1 
5848  N  NE2 . GLN B 110 ? 0.771432  0.745535 0.63618  0.27697     -0.125471   -0.0315742  110  GLN B NE2 
5849  N  N   . TYR B 111 ? 0.62134   0.511149 0.395009 0.245524    -0.113068   0.00451116  111  TYR B N   
5850  C  CA  . TYR B 111 ? 0.597781  0.486196 0.382339 0.220559    -0.10083    0.00700354  111  TYR B CA  
5851  C  C   . TYR B 111 ? 0.588772  0.499296 0.380292 0.212736    -0.104068   0.0034836   111  TYR B C   
5852  O  O   . TYR B 111 ? 0.549515  0.482516 0.366973 0.195458    -0.0997498  -0.00177957 111  TYR B O   
5853  C  CB  . TYR B 111 ? 0.630743  0.472433 0.383379 0.216364    -0.0898071  0.0200052   111  TYR B CB  
5854  C  CG  . TYR B 111 ? 0.667551  0.502546 0.425986 0.192352    -0.0765799  0.023823    111  TYR B CG  
5855  C  CD1 . TYR B 111 ? 0.646503  0.477708 0.420444 0.177882    -0.0670035  0.0232859   111  TYR B CD1 
5856  C  CD2 . TYR B 111 ? 0.668823  0.500711 0.415842 0.185265    -0.0737957  0.0276596   111  TYR B CD2 
5857  C  CE1 . TYR B 111 ? 0.664692  0.491288 0.444083 0.157461    -0.0558425  0.026123    111  TYR B CE1 
5858  C  CE2 . TYR B 111 ? 0.672829  0.49914  0.425028 0.164873    -0.0617004  0.0307863   111  TYR B CE2 
5859  C  CZ  . TYR B 111 ? 0.692039  0.517276 0.461736 0.151092    -0.0531837  0.0296943   111  TYR B CZ  
5860  O  OH  . TYR B 111 ? 0.680578  0.502076 0.455808 0.132397    -0.0421878  0.0320487   111  TYR B OH  
5861  N  N   . ASN B 112 ? 0.600111  0.502845 0.366792 0.226277    -0.111809   0.00625028  112  ASN B N   
5862  C  CA  . ASN B 112 ? 0.580648  0.50088  0.349542 0.220212    -0.115156   0.0027776   112  ASN B CA  
5863  C  C   . ASN B 112 ? 0.528743  0.495983 0.335063 0.217214    -0.123533   -0.0118847  112  ASN B C   
5864  O  O   . ASN B 112 ? 0.518917  0.504421 0.344124 0.200795    -0.119953   -0.0165798  112  ASN B O   
5865  C  CB  . ASN B 112 ? 0.606981  0.507087 0.338577 0.235259    -0.121109   0.00895893  112  ASN B CB  
5866  C  CG  . ASN B 112 ? 0.668856  0.520187 0.362105 0.236274    -0.110539   0.0239155   112  ASN B CG  
5867  O  OD1 . ASN B 112 ? 0.657745  0.491608 0.353244 0.219146    -0.0963366  0.0297023   112  ASN B OD1 
5868  N  ND2 . ASN B 112 ? 0.689894  0.517819 0.346068 0.255394    -0.116572   0.030426    112  ASN B ND2 
5869  N  N   . ALA B 113 ? 0.519626  0.505985 0.339144 0.231169    -0.132756   -0.0193625  113  ALA B N   
5870  C  CA  . ALA B 113 ? 0.487868  0.52006  0.343707 0.22853     -0.140061   -0.034176   113  ALA B CA  
5871  C  C   . ALA B 113 ? 0.477791  0.524873 0.365285 0.208332    -0.129685   -0.0380788  113  ALA B C   
5872  O  O   . ALA B 113 ? 0.453951  0.533973 0.369773 0.19814     -0.131155   -0.0485207  113  ALA B O   
5873  C  CB  . ALA B 113 ? 0.506524  0.554787 0.366474 0.250462    -0.152249   -0.0410609  113  ALA B CB  
5874  N  N   . LEU B 114 ? 0.477862  0.5009   0.360659 0.202757    -0.11922    -0.0303819  114  LEU B N   
5875  C  CA  . LEU B 114 ? 0.4686    0.507865 0.380259 0.185491    -0.110769   -0.034843   114  LEU B CA  
5876  C  C   . LEU B 114 ? 0.439184  0.479888 0.356942 0.165411    -0.103396   -0.0334129  114  LEU B C   
5877  O  O   . LEU B 114 ? 0.398164  0.463226 0.341673 0.152983    -0.100984   -0.0406695  114  LEU B O   
5878  C  CB  . LEU B 114 ? 0.472381  0.490597 0.3808   0.184466    -0.102513   -0.0294265  114  LEU B CB  
5879  C  CG  . LEU B 114 ? 0.480408  0.507268 0.394741 0.201182    -0.108376   -0.0346696  114  LEU B CG  
5880  C  CD1 . LEU B 114 ? 0.517361  0.508883 0.414962 0.200991    -0.0998624  -0.0259816  114  LEU B CD1 
5881  C  CD2 . LEU B 114 ? 0.437808  0.502887 0.387644 0.193597    -0.107925   -0.0462723  114  LEU B CD2 
5882  N  N   . LEU B 115 ? 0.495175  0.508252 0.388001 0.163035    -0.0992328  -0.0239096  115  LEU B N   
5883  C  CA  . LEU B 115 ? 0.51589   0.527045 0.409313 0.147273    -0.0928777  -0.0218475  115  LEU B CA  
5884  C  C   . LEU B 115 ? 0.490944  0.533068 0.401208 0.144819    -0.100224   -0.0323753  115  LEU B C   
5885  O  O   . LEU B 115 ? 0.429194  0.483664 0.356652 0.129739    -0.0953359  -0.0360634  115  LEU B O   
5886  C  CB  . LEU B 115 ? 0.5218    0.501304 0.383287 0.14953     -0.0891487  -0.0113415  115  LEU B CB  
5887  C  CG  . LEU B 115 ? 0.57932   0.525393 0.42365  0.147882    -0.0795878  -0.00101322 115  LEU B CG  
5888  C  CD1 . LEU B 115 ? 0.599633  0.516803 0.415798 0.145181    -0.0728373  0.00870844  115  LEU B CD1 
5889  C  CD2 . LEU B 115 ? 0.588965  0.538203 0.453697 0.132983    -0.0705144  -0.00172116 115  LEU B CD2 
5890  N  N   . SER B 116 ? 0.460472  0.515432 0.365843 0.160291    -0.112498   -0.0379988  116  SER B N   
5891  C  CA  . SER B 116 ? 0.415831  0.498988 0.334668 0.15847     -0.120391   -0.048899   116  SER B CA  
5892  C  C   . SER B 116 ? 0.388553  0.504401 0.343025 0.14993     -0.120361   -0.0603195  116  SER B C   
5893  O  O   . SER B 116 ? 0.354329  0.485568 0.325467 0.135851    -0.117809   -0.0666387  116  SER B O   
5894  C  CB  . SER B 116 ? 0.487047  0.572082 0.386581 0.178411    -0.133852   -0.0510537  116  SER B CB  
5895  O  OG  . SER B 116 ? 0.477838  0.596872 0.395644 0.17881     -0.143821   -0.0648403  116  SER B OG  
5896  N  N   . GLN B 117 ? 0.359534  0.483446 0.325229 0.157066    -0.121245   -0.0624767  117  GLN B N   
5897  C  CA  . GLN B 117 ? 0.340713  0.49471  0.339218 0.148437    -0.119304   -0.0728486  117  GLN B CA  
5898  C  C   . GLN B 117 ? 0.314304  0.459543 0.322548 0.128732    -0.105615   -0.0685344  117  GLN B C   
5899  O  O   . GLN B 117 ? 0.297732  0.463049 0.32775  0.115911    -0.102519   -0.0760808  117  GLN B O   
5900  C  CB  . GLN B 117 ? 0.377154  0.547156 0.387984 0.161209    -0.123659   -0.0783354  117  GLN B CB  
5901  C  CG  . GLN B 117 ? 0.448499  0.643017 0.462138 0.179242    -0.13886    -0.0883197  117  GLN B CG  
5902  C  CD  . GLN B 117 ? 0.550836  0.756227 0.572065 0.195411    -0.143126   -0.0921137  117  GLN B CD  
5903  O  OE1 . GLN B 117 ? 0.599279  0.797148 0.626898 0.191462    -0.134201   -0.0888455  117  GLN B OE1 
5904  N  NE2 . GLN B 117 ? 0.572483  0.796401 0.592927 0.214919    -0.157198   -0.0996977  117  GLN B NE2 
5905  N  N   . MET B 118 ? 0.324674  0.440696 0.317189 0.126441    -0.097572   -0.0571581  118  MET B N   
5906  C  CA  . MET B 118 ? 0.312037  0.421296 0.313173 0.109305    -0.0859413  -0.0536374  118  MET B CA  
5907  C  C   . MET B 118 ? 0.314796  0.425307 0.317437 0.0965941   -0.0833368  -0.0544712  118  MET B C   
5908  O  O   . MET B 118 ? 0.337489  0.457854 0.356675 0.0834497   -0.0774485  -0.0579019  118  MET B O   
5909  C  CB  . MET B 118 ? 0.308546  0.387405 0.292196 0.10882     -0.0787582  -0.0424405  118  MET B CB  
5910  C  CG  . MET B 118 ? 0.346981  0.420697 0.328664 0.119967    -0.0796799  -0.0416211  118  MET B CG  
5911  S  SD  . MET B 118 ? 0.371351  0.414325 0.340792 0.113168    -0.0689922  -0.0316329  118  MET B SD  
5912  C  CE  . MET B 118 ? 0.348876  0.358096 0.286087 0.119132    -0.0689425  -0.0211597  118  MET B CE  
5913  N  N   . SER B 119 ? 0.320323  0.419007 0.304037 0.100956    -0.0871382  -0.0511237  119  SER B N   
5914  C  CA  . SER B 119 ? 0.346053  0.445172 0.329105 0.0909083   -0.085344   -0.0526338  119  SER B CA  
5915  C  C   . SER B 119 ? 0.332946  0.460485 0.337893 0.0853418   -0.0896574  -0.0652838  119  SER B C   
5916  O  O   . SER B 119 ? 0.281316  0.412363 0.296866 0.0717921   -0.0840577  -0.0680362  119  SER B O   
5917  C  CB  . SER B 119 ? 0.395224  0.478205 0.352368 0.0992921   -0.0894987  -0.0477504  119  SER B CB  
5918  O  OG  . SER B 119 ? 0.508188  0.594962 0.465204 0.0915872   -0.0893486  -0.0514561  119  SER B OG  
5919  N  N   . ARG B 120 ? 0.31738   0.465432 0.32917  0.0961281   -0.0997745  -0.0736487  120  ARG B N   
5920  C  CA  . ARG B 120 ? 0.32421   0.502334 0.358481 0.0910327   -0.104565   -0.0874783  120  ARG B CA  
5921  C  C   . ARG B 120 ? 0.308657  0.49868  0.367286 0.0777013   -0.095555   -0.0911114  120  ARG B C   
5922  O  O   . ARG B 120 ? 0.339959  0.541662 0.413622 0.0645874   -0.0923058  -0.0983549  120  ARG B O   
5923  C  CB  . ARG B 120 ? 0.344658  0.547357 0.385224 0.105862    -0.117612   -0.0972706  120  ARG B CB  
5924  C  CG  . ARG B 120 ? 0.381201  0.618132 0.450083 0.0972045   -0.120786   -0.113157   120  ARG B CG  
5925  C  CD  . ARG B 120 ? 0.462491  0.731989 0.545292 0.110037    -0.133549   -0.125978   120  ARG B CD  
5926  N  NE  . ARG B 120 ? 0.501565  0.770574 0.584623 0.122749    -0.133767   -0.121742   120  ARG B NE  
5927  C  CZ  . ARG B 120 ? 0.549015  0.825649 0.650247 0.11686     -0.125273   -0.12234    120  ARG B CZ  
5928  N  NH1 . ARG B 120 ? 0.492639  0.788641 0.619724 0.0997752   -0.117847   -0.130755   120  ARG B NH1 
5929  N  NH2 . ARG B 120 ? 0.597772  0.862983 0.690589 0.128998    -0.124461   -0.115336   120  ARG B NH2 
5930  N  N   . ILE B 121 ? 0.282957  0.470451 0.345077 0.0815      -0.0916435  -0.0870115  121  ILE B N   
5931  C  CA  . ILE B 121 ? 0.263433  0.462399 0.346576 0.069998    -0.082905   -0.0904895  121  ILE B CA  
5932  C  C   . ILE B 121 ? 0.231176  0.41301  0.311208 0.0544943   -0.0726413  -0.0847556  121  ILE B C   
5933  O  O   . ILE B 121 ? 0.242885  0.435315 0.338795 0.0419045   -0.0668798  -0.0903486  121  ILE B O   
5934  C  CB  . ILE B 121 ? 0.289449  0.485465 0.373556 0.0774013   -0.0799676  -0.0864848  121  ILE B CB  
5935  C  CG1 . ILE B 121 ? 0.333331  0.550677 0.424865 0.0932815   -0.0898291  -0.0942371  121  ILE B CG1 
5936  C  CG2 . ILE B 121 ? 0.262963  0.462996 0.362295 0.0640906   -0.0684925  -0.0870361  121  ILE B CG2 
5937  C  CD1 . ILE B 121 ? 0.358479  0.566159 0.444205 0.103989    -0.0881675  -0.0890546  121  ILE B CD1 
5938  N  N   . TYR B 122 ? 0.244072  0.399428 0.303826 0.0556593   -0.0698398  -0.0737692  122  TYR B N   
5939  C  CA  . TYR B 122 ? 0.216291  0.355801 0.272948 0.0431693   -0.0605033  -0.0680505  122  TYR B CA  
5940  C  C   . TYR B 122 ? 0.22445   0.370083 0.286453 0.0340862   -0.0608311  -0.0745617  122  TYR B C   
5941  O  O   . TYR B 122 ? 0.224203  0.371107 0.296333 0.0219926   -0.053785   -0.076823   122  TYR B O   
5942  C  CB  . TYR B 122 ? 0.215705  0.329486 0.251719 0.0463059   -0.0579752  -0.0567396  122  TYR B CB  
5943  C  CG  . TYR B 122 ? 0.216774  0.317339 0.251228 0.0349592   -0.0492481  -0.0518279  122  TYR B CG  
5944  C  CD1 . TYR B 122 ? 0.220789  0.316865 0.2601   0.0298204   -0.0420876  -0.0481827  122  TYR B CD1 
5945  C  CD2 . TYR B 122 ? 0.214789  0.308836 0.243318 0.0300865   -0.0485603  -0.0519211  122  TYR B CD2 
5946  C  CE1 . TYR B 122 ? 0.20955   0.294237 0.246363 0.0214936   -0.03537    -0.0439722  122  TYR B CE1 
5947  C  CE2 . TYR B 122 ? 0.216075  0.299278 0.243694 0.021487    -0.0413426  -0.0483055  122  TYR B CE2 
5948  C  CZ  . TYR B 122 ? 0.239244  0.317536 0.270578 0.0177503   -0.0350244  -0.0439005  122  TYR B CZ  
5949  O  OH  . TYR B 122 ? 0.23842   0.305678 0.267251 0.0114378   -0.0287673  -0.0398481  122  TYR B OH  
5950  N  N   . SER B 123 ? 0.256253  0.403443 0.309159 0.040354    -0.0688984  -0.0774627  123  SER B N   
5951  C  CA  . SER B 123 ? 0.291882  0.437914 0.343295 0.0330319   -0.0692529  -0.0820447  123  SER B CA  
5952  C  C   . SER B 123 ? 0.322873  0.493467 0.393875 0.0269882   -0.0728663  -0.0959677  123  SER B C   
5953  O  O   . SER B 123 ? 0.324344  0.494012 0.396539 0.0186297   -0.0721086  -0.101395   123  SER B O   
5954  C  CB  . SER B 123 ? 0.317617  0.452033 0.347643 0.0417514   -0.0752384  -0.0787592  123  SER B CB  
5955  O  OG  . SER B 123 ? 0.326318  0.437152 0.340906 0.0413972   -0.0685717  -0.0672412  123  SER B OG  
5956  N  N   . THR B 124 ? 0.308331  0.500989 0.39514  0.0307973   -0.0763963  -0.102518   124  THR B N   
5957  C  CA  . THR B 124 ? 0.331333  0.55009  0.440801 0.0225229   -0.0780192  -0.116853   124  THR B CA  
5958  C  C   . THR B 124 ? 0.331071  0.559031 0.460353 0.0113342   -0.0678186  -0.119181   124  THR B C   
5959  O  O   . THR B 124 ? 0.323807  0.573908 0.473656 0.00250046  -0.0671929  -0.131402   124  THR B O   
5960  C  CB  . THR B 124 ? 0.350102  0.594475 0.465798 0.0346577   -0.091442   -0.127116   124  THR B CB  
5961  O  OG1 . THR B 124 ? 0.36245   0.612756 0.480967 0.0454493   -0.0925096  -0.123512   124  THR B OG1 
5962  C  CG2 . THR B 124 ? 0.333844  0.569308 0.4279   0.0457909   -0.101593   -0.125587   124  THR B CG2 
5963  N  N   . ALA B 125 ? 0.311495  0.522965 0.434786 0.0105353   -0.0592347  -0.108347   125  ALA B N   
5964  C  CA  . ALA B 125 ? 0.295133  0.514151 0.434048 0.00104881  -0.0492514  -0.110017   125  ALA B CA  
5965  C  C   . ALA B 125 ? 0.304248  0.516862 0.448846 -0.0162614  -0.0400076  -0.112983   125  ALA B C   
5966  O  O   . ALA B 125 ? 0.27593   0.467181 0.406232 -0.0194837  -0.0384143  -0.107599   125  ALA B O   
5967  C  CB  . ALA B 125 ? 0.319115  0.52089  0.447221 0.00561391  -0.0436016  -0.0980896  125  ALA B CB  
5968  N  N   . LYS B 126 ? 0.293526  0.524757 0.458846 -0.0271854  -0.0338676  -0.122301   126  LYS B N   
5969  C  CA  . LYS B 126 ? 0.330827  0.553335 0.500564 -0.0445572  -0.0236947  -0.125224   126  LYS B CA  
5970  C  C   . LYS B 126 ? 0.311628  0.533586 0.489015 -0.0534726  -0.0104993  -0.122823   126  LYS B C   
5971  O  O   . LYS B 126 ? 0.36935   0.606573 0.555018 -0.0473333  -0.0104158  -0.123365   126  LYS B O   
5972  C  CB  . LYS B 126 ? 0.38528   0.629781 0.572754 -0.0532696  -0.0274887  -0.141182   126  LYS B CB  
5973  C  CG  . LYS B 126 ? 0.477555  0.730982 0.660518 -0.0430854  -0.0422654  -0.146928   126  LYS B CG  
5974  C  CD  . LYS B 126 ? 0.560024  0.794932 0.73124  -0.0497634  -0.0428144  -0.148064   126  LYS B CD  
5975  C  CE  . LYS B 126 ? 0.626624  0.847969 0.775995 -0.0360668  -0.0527285  -0.141683   126  LYS B CE  
5976  N  NZ  . LYS B 126 ? 0.591811  0.832985 0.741199 -0.0206745  -0.0665074  -0.145889   126  LYS B NZ  
5977  N  N   . VAL B 127 ? 0.296285  0.499318 0.4692   -0.06722    0.00081897  -0.120158   127  VAL B N   
5978  C  CA  . VAL B 127 ? 0.331879  0.532387 0.509993 -0.0775205  0.0147524   -0.118424   127  VAL B CA  
5979  C  C   . VAL B 127 ? 0.383296  0.596679 0.579918 -0.0950712  0.0219993   -0.131271   127  VAL B C   
5980  O  O   . VAL B 127 ? 0.397399  0.600925 0.59133  -0.10253    0.0211621   -0.135297   127  VAL B O   
5981  C  CB  . VAL B 127 ? 0.315825  0.48162  0.471227 -0.0786587  0.023112    -0.104101   127  VAL B CB  
5982  C  CG1 . VAL B 127 ? 0.317268  0.477724 0.474519 -0.0895534  0.0382846   -0.10201    127  VAL B CG1 
5983  C  CG2 . VAL B 127 ? 0.333317  0.489048 0.473059 -0.0628965  0.0159807   -0.093239   127  VAL B CG2 
5984  N  N   . CYS B 128 ? 0.443849  0.67919  0.659348 -0.101959   0.0297724   -0.138138   128  CYS B N   
5985  C  CA  . CYS B 128 ? 0.525208  0.780638 0.763717 -0.118975   0.036747    -0.152732   128  CYS B CA  
5986  C  C   . CYS B 128 ? 0.559425  0.805083 0.799014 -0.133859   0.0557858   -0.150018   128  CYS B C   
5987  O  O   . CYS B 128 ? 0.581503  0.823793 0.814664 -0.128102   0.0612563   -0.141777   128  CYS B O   
5988  C  CB  . CYS B 128 ? 0.58663   0.885658 0.852151 -0.114099   0.0309836   -0.165564   128  CYS B CB  
5989  S  SG  . CYS B 128 ? 0.734396  1.05491  1.00328  -0.0950901  0.00807711  -0.172052   128  CYS B SG  
5990  N  N   . LEU B 129 ? 0.619265  0.861252 0.867228 -0.153363   0.0661361   -0.157978   129  LEU B N   
5991  C  CA  . LEU B 129 ? 0.694349  0.944564 0.955486 -0.169495   0.0836106   -0.162549   129  LEU B CA  
5992  C  C   . LEU B 129 ? 0.795859  1.08565  1.09138  -0.182105   0.0831042   -0.183458   129  LEU B C   
5993  O  O   . LEU B 129 ? 0.837001  1.16543  1.1535   -0.172319   0.0740394   -0.192333   129  LEU B O   
5994  C  CB  . LEU B 129 ? 0.684812  0.894138 0.924912 -0.183485   0.100669    -0.152799   129  LEU B CB  
5995  C  CG  . LEU B 129 ? 0.743087  0.951697 0.985455 -0.19481    0.119948    -0.150611   129  LEU B CG  
5996  C  CD1 . LEU B 129 ? 0.739712  0.899546 0.947279 -0.195455   0.130206    -0.133127   129  LEU B CD1 
5997  C  CD2 . LEU B 129 ? 0.718219  0.947803 0.987222 -0.218117   0.133582    -0.16654    129  LEU B CD2 
5998  N  N   . CYS B 136 ? 0.461066  0.701523 0.697194 -0.138771   0.0114927   -0.184268   136  CYS B N   
5999  C  CA  . CYS B 136 ? 0.500347  0.732166 0.720887 -0.120946   0.00817404  -0.168468   136  CYS B CA  
6000  C  C   . CYS B 136 ? 0.442935  0.641379 0.63498  -0.110913   0.00423964  -0.155128   136  CYS B C   
6001  O  O   . CYS B 136 ? 0.474357  0.669571 0.659777 -0.107319   -0.00476209 -0.159168   136  CYS B O   
6002  C  CB  . CYS B 136 ? 0.511091  0.776713 0.743948 -0.105729   -0.00518651 -0.173635   136  CYS B CB  
6003  S  SG  . CYS B 136 ? 0.764803  1.06753  1.02911  -0.114006   0.00246316  -0.184731   136  CYS B SG  
6004  N  N   . TRP B 137 ? 0.415082  0.591463 0.590826 -0.105227   0.0104131   -0.139752   137  TRP B N   
6005  C  CA  . TRP B 137 ? 0.379556  0.525508 0.530164 -0.0966287  0.00848675  -0.12711    137  TRP B CA  
6006  C  C   . TRP B 137 ? 0.356615  0.508953 0.499021 -0.0782412  -0.00337526 -0.120765   137  TRP B C   
6007  O  O   . TRP B 137 ? 0.327832  0.492236 0.474661 -0.0710287  -0.00442628 -0.117285   137  TRP B O   
6008  C  CB  . TRP B 137 ? 0.391357  0.510882 0.528563 -0.10003    0.0210251   -0.114575   137  TRP B CB  
6009  C  CG  . TRP B 137 ? 0.458756  0.560673 0.595563 -0.116887   0.0337022   -0.117597   137  TRP B CG  
6010  C  CD1 . TRP B 137 ? 0.487886  0.5855   0.628629 -0.127702   0.0343827   -0.127701   137  TRP B CD1 
6011  C  CD2 . TRP B 137 ? 0.499996  0.582444 0.629042 -0.124492   0.0480259   -0.109797   137  TRP B CD2 
6012  N  NE1 . TRP B 137 ? 0.553026  0.62915  0.689884 -0.142394   0.0488685   -0.126857   137  TRP B NE1 
6013  C  CE2 . TRP B 137 ? 0.525631  0.591307 0.654111 -0.140316   0.0575491   -0.115363   137  TRP B CE2 
6014  C  CE3 . TRP B 137 ? 0.516103  0.592662 0.637196 -0.119311   0.0536714   -0.0989798  137  TRP B CE3 
6015  C  CZ2 . TRP B 137 ? 0.567798  0.609127 0.686424 -0.150746   0.073096    -0.109358   137  TRP B CZ2 
6016  C  CZ3 . TRP B 137 ? 0.547113  0.601628 0.658534 -0.128992   0.0682514   -0.0933796  137  TRP B CZ3 
6017  C  CH2 . TRP B 137 ? 0.581787  0.617931 0.691127 -0.144224   0.0780368   -0.0979133  137  TRP B CH2 
6018  N  N   . SER B 138 ? 0.330776  0.47118  0.458865 -0.0709551  -0.0107697  -0.118295   138  SER B N   
6019  C  CA  . SER B 138 ? 0.328068  0.467925 0.444198 -0.0548388  -0.0199128  -0.110755   138  SER B CA  
6020  C  C   . SER B 138 ? 0.288393  0.400848 0.385877 -0.050798   -0.0144294  -0.0963969  138  SER B C   
6021  O  O   . SER B 138 ? 0.272402  0.365256 0.363733 -0.0585498  -0.00591773 -0.0931369  138  SER B O   
6022  C  CB  . SER B 138 ? 0.374947  0.517911 0.485297 -0.0497975  -0.0300789  -0.116791   138  SER B CB  
6023  O  OG  . SER B 138 ? 0.460141  0.580036 0.559025 -0.0558559  -0.0255568  -0.115517   138  SER B OG  
6024  N  N   . LEU B 139 ? 0.27428   0.385741 0.362879 -0.0384327  -0.019502   -0.0884586  139  LEU B N   
6025  C  CA  . LEU B 139 ? 0.291567  0.381925 0.364853 -0.0337957  -0.0156804  -0.076171   139  LEU B CA  
6026  C  C   . LEU B 139 ? 0.307851  0.379291 0.369218 -0.0356973  -0.0142869  -0.0747832  139  LEU B C   
6027  O  O   . LEU B 139 ? 0.349372  0.402657 0.403446 -0.0390214  -0.00721668 -0.0691546  139  LEU B O   
6028  C  CB  . LEU B 139 ? 0.264712  0.358194 0.331181 -0.0213143  -0.0220816  -0.0701991  139  LEU B CB  
6029  C  CG  . LEU B 139 ? 0.292048  0.367238 0.344364 -0.0164156  -0.0193183  -0.059026   139  LEU B CG  
6030  C  CD1 . LEU B 139 ? 0.277654  0.344067 0.330272 -0.0212712  -0.0109881  -0.0539776  139  LEU B CD1 
6031  C  CD2 . LEU B 139 ? 0.239334  0.318224 0.286399 -0.00584947 -0.024946   -0.0546427  139  LEU B CD2 
6032  N  N   . ASP B 140 ? 0.318549  0.394457 0.377108 -0.0326017  -0.0213547  -0.0804013  140  ASP B N   
6033  C  CA  . ASP B 140 ? 0.349799  0.409234 0.396177 -0.0324197  -0.0208752  -0.0798477  140  ASP B CA  
6034  C  C   . ASP B 140 ? 0.348194  0.414173 0.401047 -0.039792   -0.0233987  -0.0924571  140  ASP B C   
6035  O  O   . ASP B 140 ? 0.345393  0.42883  0.402768 -0.0361713  -0.0317376  -0.0994295  140  ASP B O   
6036  C  CB  . ASP B 140 ? 0.373832  0.430832 0.407565 -0.0209393  -0.0263704  -0.0740927  140  ASP B CB  
6037  C  CG  . ASP B 140 ? 0.535503  0.57704  0.555906 -0.0188687  -0.025517   -0.0730322  140  ASP B CG  
6038  O  OD1 . ASP B 140 ? 0.514468  0.547403 0.535094 -0.0257476  -0.0223929  -0.0785898  140  ASP B OD1 
6039  O  OD2 . ASP B 140 ? 0.493469  0.53089  0.50295  -0.0106165  -0.0273209  -0.0670951  140  ASP B OD2 
6040  N  N   . PRO B 141 ? 0.346891  0.398743 0.399386 -0.0496983  -0.0169039  -0.0962909  141  PRO B N   
6041  C  CA  . PRO B 141 ? 0.357458  0.385477 0.400844 -0.0518437  -0.00773117 -0.0876947  141  PRO B CA  
6042  C  C   . PRO B 141 ? 0.357076  0.379949 0.406631 -0.0605449  0.00157805  -0.0850555  141  PRO B C   
6043  O  O   . PRO B 141 ? 0.361746  0.364112 0.400964 -0.0600783  0.00831484  -0.0768735  141  PRO B O   
6044  C  CB  . PRO B 141 ? 0.372383  0.385203 0.408295 -0.0558914  -0.00681368 -0.094126   141  PRO B CB  
6045  C  CG  . PRO B 141 ? 0.379186  0.408741 0.428781 -0.0651918  -0.0103457  -0.108568   141  PRO B CG  
6046  C  CD  . PRO B 141 ? 0.370321  0.426794 0.429126 -0.0583982  -0.0187635  -0.109642   141  PRO B CD  
6047  N  N   . ASP B 142 ? 0.320527  0.362471 0.386367 -0.0679275  0.00213456  -0.0921752  142  ASP B N   
6048  C  CA  . ASP B 142 ? 0.316548  0.351957 0.388061 -0.0797206  0.012936    -0.0925564  142  ASP B CA  
6049  C  C   . ASP B 142 ? 0.314389  0.340226 0.378406 -0.0752612  0.0186913   -0.0802471  142  ASP B C   
6050  O  O   . ASP B 142 ? 0.327237  0.329542 0.380257 -0.0790087  0.027441    -0.0743029  142  ASP B O   
6051  C  CB  . ASP B 142 ? 0.337402  0.398995 0.43017  -0.0887116  0.0127142   -0.103997   142  ASP B CB  
6052  C  CG  . ASP B 142 ? 0.383966  0.457831 0.485422 -0.0935944  0.00616588  -0.11794    142  ASP B CG  
6053  O  OD1 . ASP B 142 ? 0.404706  0.458165 0.496711 -0.0984751  0.00878901  -0.120126   142  ASP B OD1 
6054  O  OD2 . ASP B 142 ? 0.381607  0.484352 0.497756 -0.091198   -0.00194058 -0.126395   142  ASP B OD2 
6055  N  N   . LEU B 143 ? 0.276051  0.31933  0.345189 -0.067228   0.0137606   -0.0771119  143  LEU B N   
6056  C  CA  . LEU B 143 ? 0.294064  0.329953 0.355818 -0.0621582  0.0178355   -0.0664923  143  LEU B CA  
6057  C  C   . LEU B 143 ? 0.28062   0.295531 0.324426 -0.0535027  0.0169342   -0.0567195  143  LEU B C   
6058  O  O   . LEU B 143 ? 0.307233  0.305546 0.340754 -0.0530974  0.0231512   -0.0491941  143  LEU B O   
6059  C  CB  . LEU B 143 ? 0.283645  0.342316 0.355065 -0.0555379  0.0122308   -0.0670452  143  LEU B CB  
6060  C  CG  . LEU B 143 ? 0.288948  0.371286 0.379944 -0.0629541  0.0134213   -0.0773167  143  LEU B CG  
6061  C  CD1 . LEU B 143 ? 0.280439  0.384517 0.379369 -0.0531227  0.00592802  -0.0782568  143  LEU B CD1 
6062  C  CD2 . LEU B 143 ? 0.320416  0.398709 0.415935 -0.0745971  0.0257585   -0.0778509  143  LEU B CD2 
6063  N  N   . THR B 144 ? 0.284638  0.300746 0.324215 -0.0462177  0.00938644  -0.0571253  144  THR B N   
6064  C  CA  . THR B 144 ? 0.273709  0.272558 0.298895 -0.0390293  0.00900679  -0.0501562  144  THR B CA  
6065  C  C   . THR B 144 ? 0.284054  0.259325 0.299697 -0.0437464  0.0165885   -0.0483525  144  THR B C   
6066  O  O   . THR B 144 ? 0.285537  0.246905 0.290562 -0.0388183  0.0195207   -0.0404691  144  THR B O   
6067  C  CB  . THR B 144 ? 0.27981   0.282642 0.302038 -0.0330092  0.00174105  -0.0529574  144  THR B CB  
6068  O  OG1 . THR B 144 ? 0.256881  0.277734 0.285223 -0.0281577  -0.00400661 -0.0527692  144  THR B OG1 
6069  C  CG2 . THR B 144 ? 0.276621  0.266047 0.286484 -0.0249583  0.00177618  -0.0461246  144  THR B CG2 
6070  N  N   . ASN B 145 ? 0.30105   0.27065  0.319429 -0.052834   0.0195954   -0.0559019  145  ASN B N   
6071  C  CA  . ASN B 145 ? 0.351618  0.294291 0.358064 -0.0564571  0.026969    -0.0539399  145  ASN B CA  
6072  C  C   . ASN B 145 ? 0.367371  0.299069 0.369684 -0.061226   0.0360537   -0.0480141  145  ASN B C   
6073  O  O   . ASN B 145 ? 0.413403  0.321638 0.400194 -0.0575382  0.0408327   -0.0407355  145  ASN B O   
6074  C  CB  . ASN B 145 ? 0.413993  0.350914 0.423474 -0.0659162  0.0283666   -0.0643571  145  ASN B CB  
6075  C  CG  . ASN B 145 ? 0.468462  0.405479 0.473543 -0.05912    0.0211813   -0.0682416  145  ASN B CG  
6076  O  OD1 . ASN B 145 ? 0.519203  0.452696 0.515507 -0.0476904  0.0178374   -0.0617677  145  ASN B OD1 
6077  N  ND2 . ASN B 145 ? 0.43853   0.379712 0.449259 -0.0661143  0.0190587   -0.0794144  145  ASN B ND2 
6078  N  N   . ILE B 146 ? 0.364511  0.312781 0.37967  -0.0688156  0.038683    -0.0513664  146  ILE B N   
6079  C  CA  . ILE B 146 ? 0.354619  0.294176 0.365196 -0.0732516  0.0480143   -0.0457538  146  ILE B CA  
6080  C  C   . ILE B 146 ? 0.351554  0.28499  0.349501 -0.0607944  0.0458043   -0.0347943  146  ILE B C   
6081  O  O   . ILE B 146 ? 0.377451  0.288402 0.359592 -0.0593631  0.0521013   -0.0276425  146  ILE B O   
6082  C  CB  . ILE B 146 ? 0.340371  0.302471 0.368501 -0.0825614  0.0513968   -0.0518786  146  ILE B CB  
6083  C  CG1 . ILE B 146 ? 0.3573    0.324783 0.398317 -0.0966151  0.0550432   -0.0635561  146  ILE B CG1 
6084  C  CG2 . ILE B 146 ? 0.372189  0.324303 0.392683 -0.0858242  0.0617733   -0.0450096  146  ILE B CG2 
6085  C  CD1 . ILE B 146 ? 0.352909  0.348789 0.414807 -0.104322   0.0568773   -0.0712884  146  ILE B CD1 
6086  N  N   . LEU B 147 ? 0.340869  0.293314 0.344817 -0.0518021  0.0369403   -0.0337576  147  LEU B N   
6087  C  CA  . LEU B 147 ? 0.314626  0.265617 0.309948 -0.0417151  0.0346624   -0.0253049  147  LEU B CA  
6088  C  C   . LEU B 147 ? 0.339742  0.269828 0.319153 -0.0338589  0.0339253   -0.0196934  147  LEU B C   
6089  O  O   . LEU B 147 ? 0.332935  0.253282 0.300672 -0.0275884  0.0352745   -0.0125249  147  LEU B O   
6090  C  CB  . LEU B 147 ? 0.279116  0.252334 0.283949 -0.0350471  0.0260664   -0.0262129  147  LEU B CB  
6091  C  CG  . LEU B 147 ? 0.279118  0.268662 0.292733 -0.0364887  0.0269091   -0.0269347  147  LEU B CG  
6092  C  CD1 . LEU B 147 ? 0.281208  0.262286 0.28385  -0.0324941  0.0305014   -0.0195074  147  LEU B CD1 
6093  C  CD2 . LEU B 147 ? 0.286696  0.284149 0.311722 -0.0478758  0.0330581   -0.0338328  147  LEU B CD2 
6094  N  N   . ALA B 148 ? 0.330892  0.253913 0.309312 -0.0340177  0.0320653   -0.0236302  148  ALA B N   
6095  C  CA  . ALA B 148 ? 0.374471  0.281824 0.340385 -0.0247775  0.030104    -0.019906   148  ALA B CA  
6096  C  C   . ALA B 148 ? 0.412612  0.290859 0.362316 -0.0258963  0.0378706   -0.0159002  148  ALA B C   
6097  O  O   . ALA B 148 ? 0.427673  0.293164 0.364281 -0.0156712  0.036957    -0.00970985 148  ALA B O   
6098  C  CB  . ALA B 148 ? 0.345433  0.256844 0.315412 -0.0232657  0.0252761   -0.0258652  148  ALA B CB  
6099  N  N   . SER B 149 ? 0.431162  0.299195 0.381523 -0.0381166  0.0456447   -0.0194975  149  SER B N   
6100  C  CA  . SER B 149 ? 0.478924  0.314497 0.412328 -0.0402617  0.0536731   -0.0168092  149  SER B CA  
6101  C  C   . SER B 149 ? 0.491991  0.314269 0.41932  -0.0506163  0.0648611   -0.0139253  149  SER B C   
6102  O  O   . SER B 149 ? 0.541027  0.332273 0.449224 -0.0505193  0.0724541   -0.00876505 149  SER B O   
6103  C  CB  . SER B 149 ? 0.524706  0.352775 0.461113 -0.0459892  0.0539025   -0.0250645  149  SER B CB  
6104  O  OG  . SER B 149 ? 0.540628  0.383884 0.493322 -0.0605451  0.0565961   -0.0334652  149  SER B OG  
6105  N  N   . SER B 150 ? 0.437852  0.281767 0.379581 -0.0588253  0.0666675   -0.0167784  150  SER B N   
6106  C  CA  . SER B 150 ? 0.460786  0.292668 0.395942 -0.0683186  0.0785274   -0.0137309  150  SER B CA  
6107  C  C   . SER B 150 ? 0.48184   0.301779 0.397882 -0.0570207  0.0793158   -0.00237483 150  SER B C   
6108  O  O   . SER B 150 ? 0.468904  0.306461 0.388305 -0.0462588  0.0704602   0.00017772  150  SER B O   
6109  C  CB  . SER B 150 ? 0.435534  0.294893 0.392354 -0.0800176  0.0809091   -0.021177   150  SER B CB  
6110  O  OG  . SER B 150 ? 0.466389  0.315912 0.417163 -0.0893402  0.0936239   -0.0182265  150  SER B OG  
6111  N  N   . ARG B 151 ? 0.509933  0.298725 0.404538 -0.0594422  0.090023    0.00427192  151  ARG B N   
6112  C  CA  . ARG B 151 ? 0.53435   0.311097 0.408452 -0.0487262  0.0910224   0.0147487   151  ARG B CA  
6113  C  C   . ARG B 151 ? 0.584587  0.357778 0.454425 -0.0595793  0.103521    0.0169636   151  ARG B C   
6114  O  O   . ARG B 151 ? 0.61159   0.364535 0.458112 -0.054133   0.108935    0.0260647   151  ARG B O   
6115  C  CB  . ARG B 151 ? 0.598179  0.340086 0.445424 -0.0371508  0.0912698   0.0224965   151  ARG B CB  
6116  C  CG  . ARG B 151 ? 0.572971  0.320349 0.424163 -0.0246415  0.0792712   0.0203503   151  ARG B CG  
6117  C  CD  . ARG B 151 ? 0.547523  0.327711 0.413302 -0.0145727  0.0665199   0.0189251   151  ARG B CD  
6118  N  NE  . ARG B 151 ? 0.582397  0.36095  0.446362 -0.00197643 0.0578469   0.0183454   151  ARG B NE  
6119  C  CZ  . ARG B 151 ? 0.600866  0.404549 0.483412 0.00017399  0.0491535   0.0122916   151  ARG B CZ  
6120  N  NH1 . ARG B 151 ? 0.634815  0.436185 0.514622 0.0114417   0.0429487   0.0118333   151  ARG B NH1 
6121  N  NH2 . ARG B 151 ? 0.560346  0.391598 0.463038 -0.0075262  0.0466066   0.00706441  151  ARG B NH2 
6122  N  N   . SER B 152 ? 0.548408  0.342132 0.440672 -0.07461    0.108158    0.00810031  152  SER B N   
6123  C  CA  . SER B 152 ? 0.550127  0.347114 0.444111 -0.086455   0.120524    0.00783502  152  SER B CA  
6124  C  C   . SER B 152 ? 0.496389  0.328242 0.406462 -0.081835   0.113719    0.00549839  152  SER B C   
6125  O  O   . SER B 152 ? 0.441175  0.302844 0.375829 -0.0828144  0.105236    -0.00293778 152  SER B O   
6126  C  CB  . SER B 152 ? 0.590041  0.389698 0.500398 -0.105626   0.129747    -0.00190576 152  SER B CB  
6127  O  OG  . SER B 152 ? 0.570301  0.400069 0.502077 -0.115259   0.13379     -0.00867798 152  SER B OG  
6128  N  N   . TYR B 153 ? 0.483283  0.308713 0.376612 -0.0754642  0.117077    0.0133202   153  TYR B N   
6129  C  CA  . TYR B 153 ? 0.448768  0.302162 0.352549 -0.0692324  0.110711    0.0119892   153  TYR B CA  
6130  C  C   . TYR B 153 ? 0.425842  0.309932 0.359054 -0.0811741  0.113076    0.00106442  153  TYR B C   
6131  O  O   . TYR B 153 ? 0.393108  0.30446  0.344598 -0.0759703  0.102411    -0.00416666 153  TYR B O   
6132  C  CB  . TYR B 153 ? 0.443358  0.282267 0.323192 -0.0644228  0.117758    0.0206879   153  TYR B CB  
6133  C  CG  . TYR B 153 ? 0.413907  0.279483 0.302593 -0.0568512  0.110419    0.018907    153  TYR B CG  
6134  C  CD1 . TYR B 153 ? 0.393808  0.284972 0.302579 -0.0651362  0.114976    0.0116667   153  TYR B CD1 
6135  C  CD2 . TYR B 153 ? 0.389922  0.256068 0.268301 -0.0412573  0.0984598   0.0233465   153  TYR B CD2 
6136  C  CE1 . TYR B 153 ? 0.376666  0.289453 0.29201  -0.057426   0.10836     0.00981205  153  TYR B CE1 
6137  C  CE2 . TYR B 153 ? 0.378515  0.267234 0.264986 -0.0351907  0.0917711   0.0208181   153  TYR B CE2 
6138  C  CZ  . TYR B 153 ? 0.371682  0.281615 0.274895 -0.0429148  0.0970317   0.0145609   153  TYR B CZ  
6139  O  OH  . TYR B 153 ? 0.371286  0.30025  0.280203 -0.035444   0.0898579   0.012172    153  TYR B OH  
6140  N  N   . ALA B 154 ? 0.447504  0.326737 0.385101 -0.0970059  0.127089    -0.00270502 154  ALA B N   
6141  C  CA  . ALA B 154 ? 0.43178   0.342103 0.396665 -0.108126   0.131154    -0.0133227  154  ALA B CA  
6142  C  C   . ALA B 154 ? 0.407466  0.340805 0.39814  -0.110381   0.120771    -0.0239256  154  ALA B C   
6143  O  O   . ALA B 154 ? 0.366165  0.331561 0.379533 -0.110479   0.115811    -0.0319369  154  ALA B O   
6144  C  CB  . ALA B 154 ? 0.450397  0.350151 0.413352 -0.125384   0.150119    -0.0149947  154  ALA B CB  
6145  N  N   . MET B 155 ? 0.431206  0.347293 0.416967 -0.111517   0.117654    -0.0241647  155  MET B N   
6146  C  CA  . MET B 155 ? 0.424747  0.360028 0.431736 -0.113669   0.108104    -0.0343289  155  MET B CA  
6147  C  C   . MET B 155 ? 0.371319  0.322962 0.382269 -0.0976947  0.0918679   -0.0329686  155  MET B C   
6148  O  O   . MET B 155 ? 0.350216  0.32897  0.381579 -0.0968487  0.0834215   -0.041288   155  MET B O   
6149  C  CB  . MET B 155 ? 0.473165  0.38251  0.471004 -0.119005   0.110137    -0.0349825  155  MET B CB  
6150  C  CG  . MET B 155 ? 0.49022   0.41648  0.505987 -0.11994    0.0996343   -0.0452291  155  MET B CG  
6151  S  SD  . MET B 155 ? 0.577509  0.537598 0.625651 -0.136627   0.103139    -0.0615877  155  MET B SD  
6152  C  CE  . MET B 155 ? 0.577347  0.579749 0.646017 -0.125867   0.0910921   -0.0656738  155  MET B CE  
6153  N  N   . LEU B 156 ? 0.369552  0.304127 0.360286 -0.0850508  0.0877104   -0.0227134  156  LEU B N   
6154  C  CA  . LEU B 156 ? 0.332913  0.280048 0.32564  -0.07093    0.0738618   -0.0208658  156  LEU B CA  
6155  C  C   . LEU B 156 ? 0.311141  0.284918 0.317438 -0.0686558  0.0713821   -0.0239376  156  LEU B C   
6156  O  O   . LEU B 156 ? 0.270668  0.265065 0.290616 -0.0634144  0.0615211   -0.0284748  156  LEU B O   
6157  C  CB  . LEU B 156 ? 0.323219  0.249139 0.293138 -0.0591101  0.071186    -0.0104825  156  LEU B CB  
6158  C  CG  . LEU B 156 ? 0.341699  0.240657 0.296585 -0.0574834  0.0720432   -0.0069617  156  LEU B CG  
6159  C  CD1 . LEU B 156 ? 0.361764  0.241328 0.293413 -0.0453524  0.0707908   0.00319184  156  LEU B CD1 
6160  C  CD2 . LEU B 156 ? 0.323547  0.236123 0.29095  -0.0530955  0.0609004   -0.0122953  156  LEU B CD2 
6161  N  N   . LEU B 157 ? 0.323857  0.295721 0.325526 -0.0732516  0.0816347   -0.0218583  157  LEU B N   
6162  C  CA  . LEU B 157 ? 0.314918  0.309732 0.327513 -0.0708923  0.0810783   -0.0248567  157  LEU B CA  
6163  C  C   . LEU B 157 ? 0.299576  0.322365 0.338616 -0.076763   0.0784829   -0.0362656  157  LEU B C   
6164  O  O   . LEU B 157 ? 0.301028  0.345473 0.352364 -0.0700578  0.0707205   -0.0401947  157  LEU B O   
6165  C  CB  . LEU B 157 ? 0.357751  0.344199 0.359062 -0.0754082  0.0940925   -0.020956   157  LEU B CB  
6166  C  CG  . LEU B 157 ? 0.350977  0.359492 0.361282 -0.0721116  0.094732    -0.0240586  157  LEU B CG  
6167  C  CD1 . LEU B 157 ? 0.344221  0.360731 0.353843 -0.0580284  0.0811342   -0.022327   157  LEU B CD1 
6168  C  CD2 . LEU B 157 ? 0.379137  0.378623 0.375642 -0.0759923  0.108392    -0.020014   157  LEU B CD2 
6169  N  N   . PHE B 158 ? 0.332378  0.355067 0.380279 -0.0898296  0.0859053   -0.0423295  158  PHE B N   
6170  C  CA  . PHE B 158 ? 0.319217  0.371659 0.393494 -0.0959258  0.0840266   -0.0545809  158  PHE B CA  
6171  C  C   . PHE B 158 ? 0.297771  0.361448 0.380113 -0.0876032  0.0688448   -0.0583848  158  PHE B C   
6172  O  O   . PHE B 158 ? 0.290558  0.380134 0.38979  -0.0835073  0.0614284   -0.0655657  158  PHE B O   
6173  C  CB  . PHE B 158 ? 0.373919  0.417456 0.451799 -0.113016   0.0963377   -0.0593723  158  PHE B CB  
6174  C  CG  . PHE B 158 ? 0.381317  0.457091 0.488264 -0.120532   0.0936077   -0.0739772  158  PHE B CG  
6175  C  CD1 . PHE B 158 ? 0.406966  0.509902 0.532574 -0.125017   0.0992953   -0.0813447  158  PHE B CD1 
6176  C  CD2 . PHE B 158 ? 0.399064  0.479501 0.514379 -0.121673   0.0845582   -0.0808392  158  PHE B CD2 
6177  C  CE1 . PHE B 158 ? 0.447177  0.583009 0.600846 -0.130353   0.0954396   -0.0957676  158  PHE B CE1 
6178  C  CE2 . PHE B 158 ? 0.425849  0.538124 0.567338 -0.126665   0.0800284   -0.0949299  158  PHE B CE2 
6179  C  CZ  . PHE B 158 ? 0.445349  0.585815 0.606552 -0.130952   0.0853221   -0.1025     158  PHE B CZ  
6180  N  N   . ALA B 159 ? 0.280265  0.323445 0.348828 -0.083907   0.0641119   -0.053268   159  ALA B N   
6181  C  CA  . ALA B 159 ? 0.267808  0.319322 0.340444 -0.0752339  0.0506697   -0.0555821  159  ALA B CA  
6182  C  C   . ALA B 159 ? 0.251952  0.312762 0.322577 -0.0615136  0.0418591   -0.051347   159  ALA B C   
6183  O  O   . ALA B 159 ? 0.226399  0.305203 0.30746  -0.05568    0.0327447   -0.0562153  159  ALA B O   
6184  C  CB  . ALA B 159 ? 0.265527  0.292747 0.32381  -0.0750653  0.0495664   -0.0515597  159  ALA B CB  
6185  N  N   . TRP B 160 ? 0.263082  0.310178 0.318859 -0.0561348  0.0444566   -0.0424245  160  TRP B N   
6186  C  CA  . TRP B 160 ? 0.231251  0.282659 0.28283  -0.0445047  0.0372698   -0.0382221  160  TRP B CA  
6187  C  C   . TRP B 160 ? 0.205097  0.279527 0.271083 -0.0427689  0.0364564   -0.0440284  160  TRP B C   
6188  O  O   . TRP B 160 ? 0.181437  0.267576 0.253185 -0.0350581  0.0279699   -0.0462157  160  TRP B O   
6189  C  CB  . TRP B 160 ? 0.232251  0.264702 0.265223 -0.040698   0.0409415   -0.029056   160  TRP B CB  
6190  C  CG  . TRP B 160 ? 0.226908  0.261982 0.255091 -0.0300595  0.0336265   -0.0254665  160  TRP B CG  
6191  C  CD1 . TRP B 160 ? 0.202071  0.230464 0.22361  -0.0231673  0.0261569   -0.0218514  160  TRP B CD1 
6192  C  CD2 . TRP B 160 ? 0.218074  0.265105 0.250268 -0.0258466  0.0329704   -0.0268784  160  TRP B CD2 
6193  N  NE1 . TRP B 160 ? 0.195184  0.228117 0.21486  -0.0162528  0.0218992   -0.0203018  160  TRP B NE1 
6194  C  CE2 . TRP B 160 ? 0.212793  0.25639  0.238465 -0.0172729  0.0254711   -0.0233972  160  TRP B CE2 
6195  C  CE3 . TRP B 160 ? 0.240301  0.300211 0.280728 -0.028613   0.038715    -0.0311204  160  TRP B CE3 
6196  C  CZ2 . TRP B 160 ? 0.212277  0.262503 0.23832  -0.0115706  0.023125    -0.0240292  160  TRP B CZ2 
6197  C  CZ3 . TRP B 160 ? 0.244479  0.311952 0.285186 -0.0215258  0.0360503   -0.0316467  160  TRP B CZ3 
6198  C  CH2 . TRP B 160 ? 0.227742  0.289058 0.260609 -0.0132156  0.0282423   -0.0280635  160  TRP B CH2 
6199  N  N   . GLU B 161 ? 0.228321  0.308545 0.299401 -0.0497495  0.0461414   -0.0465936  161  GLU B N   
6200  C  CA  . GLU B 161 ? 0.230637  0.333849 0.315937 -0.0473881  0.0463652   -0.0527182  161  GLU B CA  
6201  C  C   . GLU B 161 ? 0.221742  0.348159 0.327173 -0.0480354  0.0400865   -0.0629061  161  GLU B C   
6202  O  O   . GLU B 161 ? 0.222359  0.364384 0.335511 -0.038672   0.0320456   -0.0663478  161  GLU B O   
6203  C  CB  . GLU B 161 ? 0.253514  0.357934 0.340191 -0.0566315  0.0600725   -0.0538901  161  GLU B CB  
6204  C  CG  . GLU B 161 ? 0.311682  0.44332  0.416555 -0.0558426  0.0622659   -0.0622942  161  GLU B CG  
6205  C  CD  . GLU B 161 ? 0.353257  0.485553 0.458043 -0.0654569  0.0776815   -0.06306    161  GLU B CD  
6206  O  OE1 . GLU B 161 ? 0.398838  0.523623 0.503806 -0.0785692  0.0877754   -0.0639299  161  GLU B OE1 
6207  O  OE2 . GLU B 161 ? 0.368597  0.507733 0.47194  -0.0597751  0.0802287   -0.0628283  161  GLU B OE2 
6208  N  N   . GLY B 162 ? 0.223294  0.351065 0.3362   -0.0586668  0.0434699   -0.0680934  162  GLY B N   
6209  C  CA  . GLY B 162 ? 0.209798  0.361007 0.341693 -0.0592781  0.0365062   -0.0789553  162  GLY B CA  
6210  C  C   . GLY B 162 ? 0.207701  0.359137 0.334551 -0.0462936  0.0225718   -0.0770711  162  GLY B C   
6211  O  O   . GLY B 162 ? 0.198554  0.370858 0.336978 -0.0389693  0.0148668   -0.0834067  162  GLY B O   
6212  N  N   . TRP B 163 ? 0.196227  0.324451 0.305361 -0.0430882  0.0196813   -0.0685465  163  TRP B N   
6213  C  CA  . TRP B 163 ? 0.18254   0.309999 0.286199 -0.0324143  0.00813961  -0.0668829  163  TRP B CA  
6214  C  C   . TRP B 163 ? 0.174938  0.30721  0.276124 -0.0206431  0.00343159  -0.0638003  163  TRP B C   
6215  O  O   . TRP B 163 ? 0.159242  0.302094 0.263718 -0.0117261  -0.00535836 -0.0668039  163  TRP B O   
6216  C  CB  . TRP B 163 ? 0.193406  0.297139 0.280212 -0.0317756  0.00708434  -0.0592234  163  TRP B CB  
6217  C  CG  . TRP B 163 ? 0.196927  0.299923 0.277382 -0.0213117  -0.00292697 -0.0570853  163  TRP B CG  
6218  C  CD1 . TRP B 163 ? 0.206678  0.298892 0.275372 -0.0133573  -0.00559453 -0.0494365  163  TRP B CD1 
6219  C  CD2 . TRP B 163 ? 0.218109  0.332902 0.303687 -0.0176723  -0.0113559  -0.0634276  163  TRP B CD2 
6220  N  NE1 . TRP B 163 ? 0.225828  0.319981 0.291025 -0.005965   -0.0137162  -0.0498071  163  TRP B NE1 
6221  C  CE2 . TRP B 163 ? 0.225705  0.333226 0.299817 -0.00746779 -0.0177988  -0.0579087  163  TRP B CE2 
6222  C  CE3 . TRP B 163 ? 0.230734  0.361446 0.328916 -0.0223586  -0.0139894  -0.0736861  163  TRP B CE3 
6223  C  CZ2 . TRP B 163 ? 0.231651  0.345038 0.303645 -0.00073426 -0.0264456  -0.0610043  163  TRP B CZ2 
6224  C  CZ3 . TRP B 163 ? 0.242662  0.381349 0.339827 -0.0150403  -0.0239556  -0.0776079  163  TRP B CZ3 
6225  C  CH2 . TRP B 163 ? 0.218085  0.34721  0.30108  -0.00395602 -0.0298904  -0.0707773  163  TRP B CH2 
6226  N  N   . HIS B 164 ? 0.158379  0.279468 0.250679 -0.0198662  0.00895885  -0.0572061  164  HIS B N   
6227  C  CA  . HIS B 164 ? 0.158561  0.280028 0.246442 -0.00974523 0.00536168  -0.0542449  164  HIS B CA  
6228  C  C   . HIS B 164 ? 0.156659  0.301115 0.259755 -0.00561971 0.0038739   -0.062293   164  HIS B C   
6229  O  O   . HIS B 164 ? 0.148745  0.296832 0.250726 0.00498527  -0.00305838 -0.0626113  164  HIS B O   
6230  C  CB  . HIS B 164 ? 0.142975  0.25     0.219142 -0.0105253  0.0116186   -0.0473905  164  HIS B CB  
6231  C  CG  . HIS B 164 ? 0.155496  0.24327  0.217223 -0.00931223 0.00907631  -0.0400439  164  HIS B CG  
6232  N  ND1 . HIS B 164 ? 0.158698  0.234433 0.214469 -0.0153668  0.0120227   -0.0372256  164  HIS B ND1 
6233  C  CD2 . HIS B 164 ? 0.157997  0.237364 0.210789 -0.00225259 0.00391618  -0.0356183  164  HIS B CD2 
6234  C  CE1 . HIS B 164 ? 0.15725   0.220217 0.202008 -0.0111041  0.00822     -0.0315914  164  HIS B CE1 
6235  N  NE2 . HIS B 164 ? 0.16449   0.229893 0.207786 -0.00395503 0.00354653  -0.0306427  164  HIS B NE2 
6236  N  N   . ASN B 165 ? 0.173738  0.332304 0.290077 -0.0138805  0.0111546   -0.0685538  165  ASN B N   
6237  C  CA  . ASN B 165 ? 0.208237  0.392832 0.342054 -0.00979919 0.00978141  -0.0777678  165  ASN B CA  
6238  C  C   . ASN B 165 ? 0.231784  0.432269 0.37528  -0.00388652 -0.0011991  -0.0848108  165  ASN B C   
6239  O  O   . ASN B 165 ? 0.242993  0.455991 0.391056 0.00801715  -0.00831121 -0.0883159  165  ASN B O   
6240  C  CB  . ASN B 165 ? 0.219788  0.417897 0.367075 -0.0212184  0.021428    -0.0836817  165  ASN B CB  
6241  C  CG  . ASN B 165 ? 0.228185  0.41377  0.364895 -0.0237228  0.0316753   -0.0775766  165  ASN B CG  
6242  O  OD1 . ASN B 165 ? 0.237078  0.408599 0.359369 -0.0154137  0.0291467   -0.0707172  165  ASN B OD1 
6243  N  ND2 . ASN B 165 ? 0.213886  0.403625 0.356718 -0.0358849  0.0437812   -0.0803151  165  ASN B ND2 
6244  N  N   . ALA B 166 ? 0.227541  0.427472 0.373382 -0.0114026  -0.00288304 -0.0875088  166  ALA B N   
6245  C  CA  . ALA B 166 ? 0.202674  0.419937 0.357942 -0.00665657 -0.0132102  -0.0957504  166  ALA B CA  
6246  C  C   . ALA B 166 ? 0.203621  0.409854 0.343668 0.00769303  -0.0241139  -0.0900645  166  ALA B C   
6247  O  O   . ALA B 166 ? 0.186426  0.407907 0.331556 0.0181797   -0.0335425  -0.0956329  166  ALA B O   
6248  C  CB  . ALA B 166 ? 0.22158   0.436411 0.379578 -0.018566   -0.0118645  -0.0995274  166  ALA B CB  
6249  N  N   . ALA B 167 ? 0.178711  0.358373 0.299384 0.00866808  -0.0229751  -0.0791538  167  ALA B N   
6250  C  CA  . ALA B 167 ? 0.195563  0.363585 0.301388 0.0203977   -0.0316361  -0.073863   167  ALA B CA  
6251  C  C   . ALA B 167 ? 0.220443  0.383744 0.320244 0.0311506   -0.0327318  -0.0698344  167  ALA B C   
6252  O  O   . ALA B 167 ? 0.259264  0.423809 0.354019 0.0432633   -0.0407431  -0.0702067  167  ALA B O   
6253  C  CB  . ALA B 167 ? 0.206627  0.350472 0.295883 0.016524    -0.0300199  -0.0652514  167  ALA B CB  
6254  N  N   . GLY B 168 ? 0.215151  0.370194 0.312812 0.0272259   -0.0247783  -0.0656377  168  GLY B N   
6255  C  CA  . GLY B 168 ? 0.20817   0.352496 0.296549 0.0355531   -0.024793   -0.060907   168  GLY B CA  
6256  C  C   . GLY B 168 ? 0.213059  0.375502 0.312133 0.045135    -0.0274789  -0.0678215  168  GLY B C   
6257  O  O   . GLY B 168 ? 0.238393  0.394496 0.329288 0.0572966   -0.0332824  -0.0662176  168  GLY B O   
6258  N  N   . ILE B 169 ? 0.209842  0.393572 0.326441 0.0398328   -0.022462   -0.0754286  169  ILE B N   
6259  C  CA  . ILE B 169 ? 0.239537  0.442697 0.368069 0.0490119   -0.0236058  -0.0827175  169  ILE B CA  
6260  C  C   . ILE B 169 ? 0.245416  0.456347 0.373664 0.064318    -0.0356137  -0.0862769  169  ILE B C   
6261  O  O   . ILE B 169 ? 0.239231  0.443614 0.359914 0.0775716   -0.0391442  -0.0848332  169  ILE B O   
6262  C  CB  . ILE B 169 ? 0.223346  0.451336 0.372953 0.0394243   -0.0154008  -0.0914864  169  ILE B CB  
6263  C  CG1 . ILE B 169 ? 0.211922  0.42747  0.355902 0.0284259   -0.0031295  -0.086404   169  ILE B CG1 
6264  C  CG2 . ILE B 169 ? 0.216824  0.472334 0.383438 0.0499702   -0.0182207  -0.101711   169  ILE B CG2 
6265  C  CD1 . ILE B 169 ? 0.21037   0.443955 0.370944 0.015274    0.00758537  -0.0930245  169  ILE B CD1 
6266  N  N   . PRO B 170 ? 0.223788  0.447937 0.35879  0.0640699   -0.0425641  -0.0913932  170  PRO B N   
6267  C  CA  . PRO B 170 ? 0.228004  0.459658 0.360481 0.0799723   -0.0548452  -0.0948157  170  PRO B CA  
6268  C  C   . PRO B 170 ? 0.226249  0.428771 0.332863 0.0905396   -0.0607196  -0.0847436  170  PRO B C   
6269  O  O   . PRO B 170 ? 0.228091  0.431032 0.328023 0.106577    -0.0694749  -0.0857665  170  PRO B O   
6270  C  CB  . PRO B 170 ? 0.213469  0.467203 0.359509 0.0747889   -0.0602969  -0.103742   170  PRO B CB  
6271  C  CG  . PRO B 170 ? 0.19929   0.447668 0.349513 0.0552963   -0.0502141  -0.102141   170  PRO B CG  
6272  C  CD  . PRO B 170 ? 0.195219  0.427534 0.3399   0.049056    -0.0389783  -0.0949045  170  PRO B CD  
6273  N  N   . LEU B 171 ? 0.208486  0.38503  0.299935 0.081937    -0.0553767  -0.0750019  171  LEU B N   
6274  C  CA  . LEU B 171 ? 0.227111  0.375853 0.294952 0.0888377   -0.0587605  -0.065622   171  LEU B CA  
6275  C  C   . LEU B 171 ? 0.228142  0.360604 0.285587 0.0976651   -0.0570592  -0.0613402  171  LEU B C   
6276  O  O   . LEU B 171 ? 0.251917  0.365827 0.291694 0.108206    -0.0616843  -0.0562995  171  LEU B O   
6277  C  CB  . LEU B 171 ? 0.233162  0.36303  0.291219 0.0760092   -0.0530691  -0.0580488  171  LEU B CB  
6278  C  CG  . LEU B 171 ? 0.270039  0.405204 0.32916  0.0699945   -0.0559854  -0.059871   171  LEU B CG  
6279  C  CD1 . LEU B 171 ? 0.27092   0.388079 0.321862 0.0578533   -0.0491367  -0.0527785  171  LEU B CD1 
6280  C  CD2 . LEU B 171 ? 0.260938  0.390434 0.305952 0.0829777   -0.0654419  -0.0586821  171  LEU B CD2 
6281  N  N   . LYS B 172 ? 0.22986   0.368646 0.297253 0.0936411   -0.0502471  -0.0638169  172  LYS B N   
6282  C  CA  . LYS B 172 ? 0.267269  0.387272 0.323578 0.0989095   -0.0471028  -0.0597194  172  LYS B CA  
6283  C  C   . LYS B 172 ? 0.285019  0.398987 0.332256 0.117247    -0.0543682  -0.0605409  172  LYS B C   
6284  O  O   . LYS B 172 ? 0.287106  0.373427 0.314793 0.122375    -0.0546632  -0.0537173  172  LYS B O   
6285  C  CB  . LYS B 172 ? 0.265608  0.39693  0.33427  0.0939898   -0.0393451  -0.0640625  172  LYS B CB  
6286  C  CG  . LYS B 172 ? 0.299852  0.408553 0.354763 0.0974223   -0.0358999  -0.0597955  172  LYS B CG  
6287  C  CD  . LYS B 172 ? 0.345679  0.463902 0.40966  0.0933676   -0.0281377  -0.0640322  172  LYS B CD  
6288  C  CE  . LYS B 172 ? 0.399467  0.492705 0.44758  0.0964113   -0.0258065  -0.0602004  172  LYS B CE  
6289  N  NZ  . LYS B 172 ? 0.409018  0.505902 0.46048  0.0919826   -0.0182166  -0.0631385  172  LYS B NZ  
6290  N  N   . PRO B 173 ? 0.297058  0.436324 0.358091 0.128023    -0.0601829  -0.0693269  173  PRO B N   
6291  C  CA  . PRO B 173 ? 0.321254  0.454443 0.372184 0.148039    -0.0682486  -0.0701265  173  PRO B CA  
6292  C  C   . PRO B 173 ? 0.338605  0.447442 0.365864 0.155355    -0.0747923  -0.0622977  173  PRO B C   
6293  O  O   . PRO B 173 ? 0.370044  0.45357  0.377766 0.166892    -0.0765357  -0.057134   173  PRO B O   
6294  C  CB  . PRO B 173 ? 0.327872  0.49881  0.401734 0.157152    -0.0736971  -0.0824615  173  PRO B CB  
6295  C  CG  . PRO B 173 ? 0.322073  0.517493 0.416885 0.139254    -0.0688337  -0.0875671  173  PRO B CG  
6296  C  CD  . PRO B 173 ? 0.274807  0.448877 0.361562 0.121747    -0.0585995  -0.0792442  173  PRO B CD  
6297  N  N   . LEU B 174 ? 0.326347  0.440022 0.3535   0.147854    -0.0772633  -0.0610786  174  LEU B N   
6298  C  CA  . LEU B 174 ? 0.346395  0.437808 0.350197 0.153497    -0.0823409  -0.0536354  174  LEU B CA  
6299  C  C   . LEU B 174 ? 0.339543  0.395671 0.323518 0.145405    -0.0745444  -0.0427633  174  LEU B C   
6300  O  O   . LEU B 174 ? 0.370708  0.398973 0.330936 0.153778    -0.0760016  -0.0355546  174  LEU B O   
6301  C  CB  . LEU B 174 ? 0.34885   0.458005 0.360967 0.145146    -0.0855623  -0.0569111  174  LEU B CB  
6302  C  CG  . LEU B 174 ? 0.382521  0.524161 0.409619 0.154907    -0.0958591  -0.0678624  174  LEU B CG  
6303  C  CD1 . LEU B 174 ? 0.401024  0.57307  0.453466 0.158303    -0.0960618  -0.0786605  174  LEU B CD1 
6304  C  CD2 . LEU B 174 ? 0.405189  0.560611 0.4388   0.144671    -0.0982281  -0.0713682  174  LEU B CD2 
6305  N  N   . TYR B 175 ? 0.29996   0.357329 0.293429 0.128635    -0.0659766  -0.0417967  175  TYR B N   
6306  C  CA  . TYR B 175 ? 0.317199  0.34608  0.295503 0.12002     -0.0589519  -0.0332493  175  TYR B CA  
6307  C  C   . TYR B 175 ? 0.33795   0.344015 0.303159 0.128329    -0.0570889  -0.0305046  175  TYR B C   
6308  O  O   . TYR B 175 ? 0.356317  0.33384  0.302084 0.127571    -0.054331   -0.0232611  175  TYR B O   
6309  C  CB  . TYR B 175 ? 0.295536  0.332021 0.286645 0.10244     -0.0513397  -0.0335274  175  TYR B CB  
6310  C  CG  . TYR B 175 ? 0.284861  0.296865 0.261464 0.0935847   -0.0460521  -0.0255524  175  TYR B CG  
6311  C  CD1 . TYR B 175 ? 0.269394  0.277317 0.239305 0.0887392   -0.0465082  -0.0218173  175  TYR B CD1 
6312  C  CD2 . TYR B 175 ? 0.287319  0.281879 0.257886 0.0898784   -0.0404409  -0.022858   175  TYR B CD2 
6313  C  CE1 . TYR B 175 ? 0.304305  0.292572 0.26281  0.0807263   -0.0410395  -0.0154333  175  TYR B CE1 
6314  C  CE2 . TYR B 175 ? 0.31042   0.28621  0.270693 0.0808095   -0.035454   -0.0170623  175  TYR B CE2 
6315  C  CZ  . TYR B 175 ? 0.297752  0.271065 0.252615 0.0761993   -0.035436   -0.0132764  175  TYR B CZ  
6316  O  OH  . TYR B 175 ? 0.316634  0.273107 0.26207  0.0679209   -0.0300907  -0.00817896 175  TYR B OH  
6317  N  N   . GLU B 176 ? 0.3563    0.373838 0.33152  0.136167    -0.0580051  -0.0366527  176  GLU B N   
6318  C  CA  . GLU B 176 ? 0.398136  0.391029 0.359338 0.144061    -0.0559365  -0.0344163  176  GLU B CA  
6319  C  C   . GLU B 176 ? 0.440711  0.410728 0.378927 0.159927    -0.0618743  -0.0295605  176  GLU B C   
6320  O  O   . GLU B 176 ? 0.436204  0.372916 0.353664 0.161471    -0.0584304  -0.0232957  176  GLU B O   
6321  C  CB  . GLU B 176 ? 0.417855  0.427454 0.392743 0.152307    -0.0562838  -0.0425617  176  GLU B CB  
6322  C  CG  . GLU B 176 ? 0.450274  0.487296 0.448394 0.139979    -0.0511429  -0.0486002  176  GLU B CG  
6323  C  CD  . GLU B 176 ? 0.58862   0.641954 0.599186 0.148612    -0.0502639  -0.0569018  176  GLU B CD  
6324  O  OE1 . GLU B 176 ? 0.593357  0.633341 0.593587 0.163998    -0.0532318  -0.0577968  176  GLU B OE1 
6325  O  OE2 . GLU B 176 ? 0.585079  0.664009 0.615147 0.140009    -0.0459976  -0.0625539  176  GLU B OE2 
6326  N  N   . ASP B 177 ? 0.459175  0.446586 0.400129 0.171541    -0.0708147  -0.0326316  177  ASP B N   
6327  C  CA  . ASP B 177 ? 0.477087  0.443538 0.393957 0.188596    -0.0775571  -0.0278146  177  ASP B CA  
6328  C  C   . ASP B 177 ? 0.482652  0.421136 0.377367 0.180634    -0.0738621  -0.0176932  177  ASP B C   
6329  O  O   . ASP B 177 ? 0.489782  0.393518 0.357997 0.187876    -0.0724822  -0.0101922  177  ASP B O   
6330  C  CB  . ASP B 177 ? 0.520894  0.516969 0.447821 0.202103    -0.0887959  -0.0348213  177  ASP B CB  
6331  C  CG  . ASP B 177 ? 0.566402  0.586592 0.511644 0.214131    -0.0925691  -0.0447594  177  ASP B CG  
6332  O  OD1 . ASP B 177 ? 0.606277  0.612815 0.549738 0.215245    -0.086949   -0.0446504  177  ASP B OD1 
6333  O  OD2 . ASP B 177 ? 0.611079  0.665274 0.573987 0.220746    -0.100355   -0.0534657  177  ASP B OD2 
6334  N  N   . PHE B 178 ? 0.43676   0.390005 0.342631 0.164991    -0.0711771  -0.0177618  178  PHE B N   
6335  C  CA  . PHE B 178 ? 0.444182  0.376089 0.332357 0.156509    -0.0669988  -0.00939823 178  PHE B CA  
6336  C  C   . PHE B 178 ? 0.449301  0.349256 0.324333 0.147883    -0.0570948  -0.00298276 178  PHE B C   
6337  O  O   . PHE B 178 ? 0.469088  0.33812  0.319216 0.149801    -0.054048   0.00495727  178  PHE B O   
6338  C  CB  . PHE B 178 ? 0.424858  0.37973  0.32853  0.142748    -0.0662532  -0.0118376  178  PHE B CB  
6339  C  CG  . PHE B 178 ? 0.458531  0.392163 0.349843 0.129325    -0.0578822  -0.0041508  178  PHE B CG  
6340  C  CD1 . PHE B 178 ? 0.488315  0.401941 0.355925 0.133256    -0.0581911  0.00268953  178  PHE B CD1 
6341  C  CD2 . PHE B 178 ? 0.49318   0.42663  0.395761 0.11364     -0.0494657  -0.00405123 178  PHE B CD2 
6342  C  CE1 . PHE B 178 ? 0.525285  0.421064 0.38317  0.120494    -0.0492389  0.00899321  178  PHE B CE1 
6343  C  CE2 . PHE B 178 ? 0.516224  0.432764 0.409676 0.101857    -0.0418151  0.00180746  178  PHE B CE2 
6344  C  CZ  . PHE B 178 ? 0.529205  0.427035 0.400934 0.104938    -0.0411653  0.00823225  178  PHE B CZ  
6345  N  N   . THR B 179 ? 0.397618  0.305018 0.289006 0.13768     -0.0516431  -0.00683228 179  THR B N   
6346  C  CA  . THR B 179 ? 0.404744  0.285601 0.286606 0.127656    -0.0426954  -0.00263455 179  THR B CA  
6347  C  C   . THR B 179 ? 0.424413  0.271009 0.281766 0.140003    -0.0423759  0.00168791  179  THR B C   
6348  O  O   . THR B 179 ? 0.440626  0.256747 0.279053 0.134436    -0.0359108  0.00829216  179  THR B O   
6349  C  CB  . THR B 179 ? 0.381501  0.277488 0.283605 0.117549    -0.0386529  -0.00860201 179  THR B CB  
6350  O  OG1 . THR B 179 ? 0.379768  0.302218 0.299888 0.10684     -0.0385447  -0.0110034  179  THR B OG1 
6351  C  CG2 . THR B 179 ? 0.397845  0.268546 0.291334 0.108444    -0.0307944  -0.00646719 179  THR B CG2 
6352  N  N   . ALA B 180 ? 0.442994  0.294633 0.301511 0.156415    -0.0486241  -0.00264133 180  ALA B N   
6353  C  CA  . ALA B 180 ? 0.489211  0.307878 0.324612 0.170356    -0.048819   0.00067193  180  ALA B CA  
6354  C  C   . ALA B 180 ? 0.528209  0.318613 0.334213 0.177842    -0.0498319  0.0100273   180  ALA B C   
6355  O  O   . ALA B 180 ? 0.550706  0.301715 0.332493 0.177357    -0.0434497  0.0166753   180  ALA B O   
6356  C  CB  . ALA B 180 ? 0.513724  0.350801 0.358692 0.188758    -0.0570339  -0.00667707 180  ALA B CB  
6357  N  N   . LEU B 181 ? 0.538422  0.347399 0.345196 0.183407    -0.0569717  0.0105578   181  LEU B N   
6358  C  CA  . LEU B 181 ? 0.571901  0.355238 0.34847  0.192677    -0.0587642  0.0192436   181  LEU B CA  
6359  C  C   . LEU B 181 ? 0.592814  0.35392  0.357335 0.174365    -0.0475263  0.0268738   181  LEU B C   
6360  O  O   . LEU B 181 ? 0.62192   0.344522 0.357022 0.176435    -0.0419207  0.0355256   181  LEU B O   
6361  C  CB  . LEU B 181 ? 0.577889  0.390405 0.360246 0.202812    -0.069972   0.0159809   181  LEU B CB  
6362  C  CG  . LEU B 181 ? 0.602668  0.435242 0.392059 0.224705    -0.082359   0.00875187  181  LEU B CG  
6363  C  CD1 . LEU B 181 ? 0.612745  0.482431 0.416335 0.229657    -0.0928879  0.00243415  181  LEU B CD1 
6364  C  CD2 . LEU B 181 ? 0.645872  0.444081 0.403525 0.24698     -0.0863492  0.0144406   181  LEU B CD2 
6365  N  N   . SER B 182 ? 0.53619   0.322188 0.323863 0.156138    -0.043693   0.0234056   182  SER B N   
6366  C  CA  . SER B 182 ? 0.538032  0.30922  0.318528 0.138923    -0.0333874  0.0290638   182  SER B CA  
6367  C  C   . SER B 182 ? 0.565807  0.302294 0.33341  0.131166    -0.0229922  0.0327748   182  SER B C   
6368  O  O   . SER B 182 ? 0.574667  0.281067 0.320084 0.125422    -0.0146436  0.0403884   182  SER B O   
6369  C  CB  . SER B 182 ? 0.515627  0.320661 0.324426 0.123096    -0.0321161  0.0236848   182  SER B CB  
6370  O  OG  . SER B 182 ? 0.524265  0.317717 0.329246 0.106544    -0.0219152  0.0278731   182  SER B OG  
6371  N  N   . ASN B 183 ? 0.545791  0.28628  0.327179 0.130311    -0.0228656  0.0267821   183  ASN B N   
6372  C  CA  . ASN B 183 ? 0.573388  0.282538 0.34462  0.122191    -0.0135663  0.0282762   183  ASN B CA  
6373  C  C   . ASN B 183 ? 0.631893  0.296938 0.368225 0.13512     -0.0116541  0.0360171   183  ASN B C   
6374  O  O   . ASN B 183 ? 0.659705  0.290977 0.378519 0.124992    -0.00104347 0.0411761   183  ASN B O   
6375  C  CB  . ASN B 183 ? 0.557947  0.280294 0.348672 0.120986    -0.0148808  0.0196646   183  ASN B CB  
6376  C  CG  . ASN B 183 ? 0.542975  0.292165 0.359887 0.102365    -0.0113704  0.0141485   183  ASN B CG  
6377  O  OD1 . ASN B 183 ? 0.558605  0.31128  0.378158 0.0886536   -0.00625318 0.0168366   183  ASN B OD1 
6378  N  ND2 . ASN B 183 ? 0.528669  0.296907 0.364104 0.102513    -0.0139486  0.00637224  183  ASN B ND2 
6379  N  N   A GLU B 184 ? 0.654196  0.319097 0.380801 0.157363    -0.021554   0.0362081   184  GLU B N   
6380  N  N   B GLU B 184 ? 0.65504   0.321995 0.382092 0.157424    -0.0219793  0.0363289   184  GLU B N   
6381  C  CA  A GLU B 184 ? 0.724594  0.346681 0.415653 0.173368    -0.0212309  0.0438318   184  GLU B CA  
6382  C  CA  B GLU B 184 ? 0.726584  0.354853 0.420163 0.176172    -0.0235833  0.0429347   184  GLU B CA  
6383  C  C   A GLU B 184 ? 0.762238  0.359118 0.427592 0.167344    -0.0141496  0.0541912   184  GLU B C   
6384  C  C   B GLU B 184 ? 0.766358  0.370089 0.430473 0.177591    -0.0202292  0.0535996   184  GLU B C   
6385  O  O   A GLU B 184 ? 0.781594  0.334364 0.419623 0.163992    -0.00429356 0.0615275   184  GLU B O   
6386  O  O   B GLU B 184 ? 0.816524  0.381888 0.447235 0.191628    -0.0196862  0.061175    184  GLU B O   
6387  C  CB  A GLU B 184 ? 0.735231  0.37447  0.425419 0.198819    -0.035601   0.0411756   184  GLU B CB  
6388  C  CB  B GLU B 184 ? 0.731624  0.37878  0.427678 0.201159    -0.0378318  0.0388632   184  GLU B CB  
6389  C  CG  A GLU B 184 ? 0.804508  0.402461 0.457405 0.220915    -0.0382795  0.0484919   184  GLU B CG  
6390  C  CG  B GLU B 184 ? 0.726256  0.391822 0.444159 0.20695     -0.0418828  0.0289516   184  GLU B CG  
6391  C  CD  A GLU B 184 ? 0.819374  0.43528  0.472295 0.248343    -0.0534497  0.0444575   184  GLU B CD  
6392  C  CD  B GLU B 184 ? 0.733541  0.412593 0.451584 0.233417    -0.0546187  0.0244555   184  GLU B CD  
6393  O  OE1 A GLU B 184 ? 0.776895  0.437089 0.461949 0.250636    -0.0612561  0.0341009   184  GLU B OE1 
6394  O  OE1 B GLU B 184 ? 0.782312  0.426144 0.47311  0.250762    -0.0558529  0.0287711   184  GLU B OE1 
6395  O  OE2 A GLU B 184 ? 0.885399  0.469987 0.504737 0.267981    -0.0572545  0.0517745   184  GLU B OE2 
6396  O  OE2 B GLU B 184 ? 0.692257  0.416224 0.4373   0.237046    -0.0630333  0.0163086   184  GLU B OE2 
6397  N  N   . ALA B 185 ? 0.749621  0.375568 0.425085 0.164276    -0.0181813  0.054072    185  ALA B N   
6398  C  CA  . ALA B 185 ? 0.786736  0.39462  0.438066 0.161705    -0.0132089  0.0630906   185  ALA B CA  
6399  C  C   . ALA B 185 ? 0.810267  0.394785 0.457112 0.138705    0.00319554  0.0668733   185  ALA B C   
6400  O  O   . ALA B 185 ? 0.86186   0.404956 0.47667  0.13838     0.0121979   0.0760097   185  ALA B O   
6401  C  CB  . ALA B 185 ? 0.753764  0.402662 0.423375 0.160667    -0.0207313  0.0593159   185  ALA B CB  
6402  N  N   . TYR B 186 ? 0.744407  0.354475 0.422714 0.119879    0.0072727   0.0594989   186  TYR B N   
6403  C  CA  . TYR B 186 ? 0.764704  0.362992 0.444153 0.0972891   0.0215489   0.0613132   186  TYR B CA  
6404  C  C   . TYR B 186 ? 0.813324  0.373487 0.47989  0.090551    0.0313759   0.0623748   186  TYR B C   
6405  O  O   . TYR B 186 ? 0.834012  0.370543 0.48961  0.0747755   0.0448538   0.0662972   186  TYR B O   
6406  C  CB  . TYR B 186 ? 0.742532  0.381889 0.456405 0.080471    0.0222442   0.0541257   186  TYR B CB  
6407  C  CG  . TYR B 186 ? 0.72961   0.392324 0.446016 0.0826932   0.0180898   0.0558241   186  TYR B CG  
6408  C  CD1 . TYR B 186 ? 0.785149  0.433054 0.484265 0.0750852   0.0274294   0.0625391   186  TYR B CD1 
6409  C  CD2 . TYR B 186 ? 0.693974  0.391373 0.427971 0.0927918   0.00539497  0.0505172   186  TYR B CD2 
6410  C  CE1 . TYR B 186 ? 0.768292  0.436051 0.467956 0.0777444   0.0237046   0.0635054   186  TYR B CE1 
6411  C  CE2 . TYR B 186 ? 0.707279  0.424396 0.443119 0.0941972   0.00167186  0.0510592   186  TYR B CE2 
6412  C  CZ  . TYR B 186 ? 0.744191  0.445987 0.462025 0.0874896   0.0103682   0.0575604   186  TYR B CZ  
6413  O  OH  . TYR B 186 ? 0.72959   0.450129 0.447955 0.089914    0.00632887  0.0573899   186  TYR B OH  
6414  N  N   . LYS B 187 ? 0.830968  0.384837 0.498642 0.102221    0.0252275   0.0583498   187  LYS B N   
6415  C  CA  . LYS B 187 ? 0.89322   0.408737 0.547369 0.0973732   0.0337437   0.0583906   187  LYS B CA  
6416  C  C   . LYS B 187 ? 0.937037  0.400147 0.549836 0.100686    0.0432168   0.0699568   187  LYS B C   
6417  O  O   . LYS B 187 ? 0.963482  0.392078 0.563947 0.0870634   0.0560766   0.0715471   187  LYS B O   
6418  C  CB  . LYS B 187 ? 0.94181   0.460301 0.602877 0.112006    0.0248729   0.0517983   187  LYS B CB  
6419  C  CG  . LYS B 187 ? 1.01365   0.569162 0.71154  0.0992734   0.0229889   0.0402593   187  LYS B CG  
6420  C  CD  . LYS B 187 ? 1.08464   0.64893  0.793756 0.110625    0.015648    0.0320952   187  LYS B CD  
6421  C  CE  . LYS B 187 ? 1.18462   0.704328 0.872415 0.114058    0.021297    0.032145    187  LYS B CE  
6422  N  NZ  . LYS B 187 ? 1.18051   0.713655 0.883002 0.122433    0.0151804   0.0225981   187  LYS B NZ  
6423  N  N   . GLN B 188 ? 0.936463  0.394034 0.527483 0.117754    0.0373443   0.0778177   188  GLN B N   
6424  C  CA  . GLN B 188 ? 1.01152   0.418339 0.559238 0.123394    0.0457552   0.089972    188  GLN B CA  
6425  C  C   . GLN B 188 ? 1.03808   0.435016 0.578862 0.101775    0.0609922   0.0953116   188  GLN B C   
6426  O  O   . GLN B 188 ? 1.10553   0.456831 0.610135 0.101603    0.0717795   0.105469    188  GLN B O   
6427  C  CB  . GLN B 188 ? 1.02999   0.432222 0.555177 0.153106    0.0321551   0.0951803   188  GLN B CB  
6428  C  CG  . GLN B 188 ? 1.05186   0.46251  0.587398 0.171175    0.0200764   0.0881055   188  GLN B CG  
6429  C  CD  . GLN B 188 ? 1.0862    0.499766 0.604864 0.201462    0.00497309  0.0909429   188  GLN B CD  
6430  O  OE1 . GLN B 188 ? 1.16167   0.53184  0.640208 0.217601    0.00583751  0.100568    188  GLN B OE1 
6431  N  NE2 . GLN B 188 ? 1.05592   0.520254 0.604552 0.20959     -0.0089146  0.0822851   188  GLN B NE2 
6432  N  N   . ASP B 189 ? 0.968828  0.406106 0.543156 0.08323     0.0630809   0.0884396   189  ASP B N   
6433  C  CA  . ASP B 189 ? 1.0039    0.434464 0.575271 0.0619162   0.0783937   0.0918166   189  ASP B CA  
6434  C  C   . ASP B 189 ? 1.01717   0.444061 0.60748  0.0379315   0.0900806   0.0847179   189  ASP B C   
6435  O  O   . ASP B 189 ? 1.05549   0.481833 0.649993 0.0175364   0.103466    0.0849705   189  ASP B O   
6436  C  CB  . ASP B 189 ? 1.02978   0.502553 0.619513 0.0590089   0.0740181   0.0901088   189  ASP B CB  
6437  C  CG  . ASP B 189 ? 1.09554   0.581246 0.67439  0.0830725   0.0589524   0.0933054   189  ASP B CG  
6438  O  OD1 . ASP B 189 ? 1.15394   0.611912 0.706335 0.102775    0.0530695   0.0984657   189  ASP B OD1 
6439  O  OD2 . ASP B 189 ? 1.04283   0.567315 0.640919 0.0825727   0.0524258   0.0895891   189  ASP B OD2 
6440  N  N   . GLY B 190 ? 0.984376  0.410106 0.586377 0.0406698   0.0849124   0.0775888   190  GLY B N   
6441  C  CA  . GLY B 190 ? 0.987688  0.406694 0.604738 0.0193308   0.0949629   0.0699627   190  GLY B CA  
6442  C  C   . GLY B 190 ? 0.931124  0.401992 0.592016 0.00936512  0.0879687   0.0573901   190  GLY B C   
6443  O  O   . GLY B 190 ? 0.930437  0.403922 0.608285 -0.0081375  0.0941012   0.0490801   190  GLY B O   
6444  N  N   . PHE B 191 ? 0.903782  0.414678 0.581717 0.0209812   0.0749102   0.0557243   191  PHE B N   
6445  C  CA  . PHE B 191 ? 0.808948  0.366997 0.52483  0.0143867   0.0675668   0.0451226   191  PHE B CA  
6446  C  C   . PHE B 191 ? 0.818831  0.38307  0.544029 0.0256587   0.0575113   0.0384736   191  PHE B C   
6447  O  O   . PHE B 191 ? 0.844489  0.400557 0.556146 0.0460089   0.0490379   0.0418052   191  PHE B O   
6448  C  CB  . PHE B 191 ? 0.7698    0.365007 0.49807  0.0216      0.0589386   0.0463449   191  PHE B CB  
6449  C  CG  . PHE B 191 ? 0.729807  0.323766 0.452013 0.00986562  0.0690104   0.0513972   191  PHE B CG  
6450  C  CD1 . PHE B 191 ? 0.700774  0.310823 0.443621 -0.0113046  0.0777995   0.0457501   191  PHE B CD1 
6451  C  CD2 . PHE B 191 ? 0.786569  0.362638 0.481368 0.0205173   0.0699563   0.0613077   191  PHE B CD2 
6452  C  CE1 . PHE B 191 ? 0.715819  0.326349 0.454275 -0.0219705  0.0879473   0.0496226   191  PHE B CE1 
6453  C  CE2 . PHE B 191 ? 0.802383  0.375571 0.489804 0.00931126  0.0807664   0.0658307   191  PHE B CE2 
6454  C  CZ  . PHE B 191 ? 0.771111  0.362581 0.481515 -0.0120696  0.0900178   0.0597919   191  PHE B CZ  
6455  N  N   . THR B 192 ? 0.768819  0.352033 0.518843 0.0130171   0.0577776   0.0283073   192  THR B N   
6456  C  CA  . THR B 192 ? 0.749781  0.341876 0.510155 0.0221278   0.0492137   0.0209922   192  THR B CA  
6457  C  C   . THR B 192 ? 0.692446  0.317704 0.464353 0.0391003   0.0360377   0.0207764   192  THR B C   
6458  O  O   . THR B 192 ? 0.686866  0.308923 0.454011 0.0557001   0.0286265   0.0196334   192  THR B O   
6459  C  CB  . THR B 192 ? 0.793671  0.400563 0.576697 0.00429131  0.0524064   0.0102121   192  THR B CB  
6460  O  OG1 . THR B 192 ? 0.895024  0.50686  0.683079 0.0157564   0.044374    0.00423573  192  THR B OG1 
6461  C  CG2 . THR B 192 ? 0.706179  0.356022 0.517134 -0.00714764 0.0505174   0.0057184   192  THR B CG2 
6462  N  N   . ASP B 193 ? 0.637071  0.293064 0.422864 0.0356041   0.0335346   0.0220017   193  ASP B N   
6463  C  CA  . ASP B 193 ? 0.591124  0.276708 0.386884 0.0495859   0.0223493   0.0218221   193  ASP B CA  
6464  C  C   . ASP B 193 ? 0.553801  0.260199 0.356062 0.0440828   0.0227874   0.0250952   193  ASP B C   
6465  O  O   . ASP B 193 ? 0.571003  0.273835 0.374105 0.0290762   0.0315591   0.0263442   193  ASP B O   
6466  C  CB  . ASP B 193 ? 0.557722  0.272427 0.377849 0.0503617   0.0157476   0.0126708   193  ASP B CB  
6467  C  CG  . ASP B 193 ? 0.55716   0.294545 0.399608 0.0325291   0.0191055   0.0066378   193  ASP B CG  
6468  O  OD1 . ASP B 193 ? 0.54193   0.302778 0.395792 0.0274162   0.0183218   0.00774955  193  ASP B OD1 
6469  O  OD2 . ASP B 193 ? 0.566274  0.298543 0.414454 0.0246492   0.0218822   0.00029097  193  ASP B OD2 
6470  N  N   . THR B 194 ? 0.543484  0.273886 0.35243  0.0557359   0.0133916   0.0251842   194  THR B N   
6471  C  CA  . THR B 194 ? 0.540928  0.290502 0.354725 0.0526294   0.0127044   0.027633    194  THR B CA  
6472  C  C   . THR B 194 ? 0.529552  0.2999   0.364335 0.0349449   0.0178514   0.0234511   194  THR B C   
6473  O  O   . THR B 194 ? 0.55705   0.330185 0.389547 0.0284027   0.0224434   0.0265389   194  THR B O   
6474  C  CB  . THR B 194 ? 0.501564  0.278755 0.325719 0.0651391   0.00145666  0.0252411   194  THR B CB  
6475  O  OG1 . THR B 194 ? 0.542188  0.300804 0.347791 0.0821047   -0.00353243 0.0280871   194  THR B OG1 
6476  C  CG2 . THR B 194 ? 0.502642  0.293867 0.326518 0.0642397   0.00027939  0.0279157   194  THR B CG2 
6477  N  N   . GLY B 195 ? 0.495265  0.282614 0.350312 0.0290573   0.0161406   0.0161477   195  GLY B N   
6478  C  CA  . GLY B 195 ? 0.43432   0.243426 0.309275 0.0148551   0.019208    0.0116398   195  GLY B CA  
6479  C  C   . GLY B 195 ? 0.474143  0.26576  0.342641 0.00083697  0.0302123   0.0130659   195  GLY B C   
6480  O  O   . GLY B 195 ? 0.450534  0.256301 0.328354 -0.00875528 0.0342897   0.0124631   195  GLY B O   
6481  N  N   . ALA B 196 ? 0.476749  0.236165 0.328131 -2.658e-05  0.0356993   0.0150268   196  ALA B N   
6482  C  CA  . ALA B 196 ? 0.514854  0.255613 0.360301 -0.0153904  0.0477401   0.0155817   196  ALA B CA  
6483  C  C   . ALA B 196 ? 0.521044  0.253114 0.352201 -0.0167823  0.0542171   0.0232852   196  ALA B C   
6484  O  O   . ALA B 196 ? 0.559342  0.292871 0.394914 -0.0312789  0.0638609   0.0225147   196  ALA B O   
6485  C  CB  . ALA B 196 ? 0.551443  0.256068 0.380083 -0.0164518  0.0528727   0.0157994   196  ALA B CB  
6486  N  N   . TYR B 197 ? 0.523827  0.247416 0.337659 -0.00143188 0.0489752   0.0300348   197  TYR B N   
6487  C  CA  . TYR B 197 ? 0.565183  0.28034  0.362203 7.05e-05    0.0536523   0.0374793   197  TYR B CA  
6488  C  C   . TYR B 197 ? 0.536475  0.28734  0.354726 -0.00567003 0.0520764   0.0339689   197  TYR B C   
6489  O  O   . TYR B 197 ? 0.520302  0.27292  0.339342 -0.0169095  0.0614267   0.0348523   197  TYR B O   
6490  C  CB  . TYR B 197 ? 0.592125  0.294985 0.368247 0.0203736   0.0449696   0.0434345   197  TYR B CB  
6491  C  CG  . TYR B 197 ? 0.629901  0.331079 0.390114 0.0246687   0.0465274   0.0499501   197  TYR B CG  
6492  C  CD1 . TYR B 197 ? 0.669818  0.348666 0.412308 0.0148191   0.0598612   0.0557193   197  TYR B CD1 
6493  C  CD2 . TYR B 197 ? 0.619068  0.342463 0.383002 0.037171    0.0354319   0.0494004   197  TYR B CD2 
6494  C  CE1 . TYR B 197 ? 0.704099  0.381465 0.430712 0.0187153   0.0619168   0.0613629   197  TYR B CE1 
6495  C  CE2 . TYR B 197 ? 0.678526  0.400931 0.427487 0.0408852   0.0365512   0.0542746   197  TYR B CE2 
6496  C  CZ  . TYR B 197 ? 0.709104  0.408525 0.438903 0.0320446   0.0497583   0.0604074   197  TYR B CZ  
6497  O  OH  . TYR B 197 ? 0.803359  0.500805 0.516256 0.0360372   0.0514974   0.0651595   197  TYR B OH  
6498  N  N   . TRP B 198 ? 0.512442  0.292032 0.349212 0.00135179  0.0409253   0.0291945   198  TRP B N   
6499  C  CA  . TRP B 198 ? 0.466935  0.277924 0.322387 -0.0020672  0.0384173   0.0258376   198  TRP B CA  
6500  C  C   . TRP B 198 ? 0.460254  0.28181  0.331897 -0.018636   0.0467947   0.0211445   198  TRP B C   
6501  O  O   . TRP B 198 ? 0.470207  0.302921 0.346015 -0.0242131  0.0515319   0.0213368   198  TRP B O   
6502  C  CB  . TRP B 198 ? 0.449185  0.285149 0.321843 0.00603431  0.0266939   0.0209339   198  TRP B CB  
6503  C  CG  . TRP B 198 ? 0.426264  0.263401 0.289642 0.021354    0.0177257   0.0234651   198  TRP B CG  
6504  C  CD1 . TRP B 198 ? 0.464487  0.281611 0.303999 0.031149    0.0171717   0.0296887   198  TRP B CD1 
6505  C  CD2 . TRP B 198 ? 0.40398   0.265061 0.282475 0.0285554   0.00783851  0.018998    198  TRP B CD2 
6506  N  NE1 . TRP B 198 ? 0.461842  0.291555 0.302544 0.0442103   0.00660063  0.0284043   198  TRP B NE1 
6507  C  CE2 . TRP B 198 ? 0.412045  0.268848 0.277207 0.0419581   0.00139657  0.0217495   198  TRP B CE2 
6508  C  CE3 . TRP B 198 ? 0.367902  0.253044 0.268918 0.0247694   0.00428424  0.0129159   198  TRP B CE3 
6509  C  CZ2 . TRP B 198 ? 0.395729  0.27329  0.271945 0.0502292   -0.00797941 0.0176533   198  TRP B CZ2 
6510  C  CZ3 . TRP B 198 ? 0.35341   0.255988 0.263078 0.0327402   -0.00390545 0.010048    198  TRP B CZ3 
6511  C  CH2 . TRP B 198 ? 0.377939  0.277914 0.276797 0.0445813   -0.00976383 0.0118836   198  TRP B CH2 
6512  N  N   . ARG B 199 ? 0.451931  0.270383 0.332589 -0.0262407  0.0486381   0.0161677   199  ARG B N   
6513  C  CA  . ARG B 199 ? 0.446019  0.27692  0.344039 -0.0417603  0.0552868   0.00986     199  ARG B CA  
6514  C  C   . ARG B 199 ? 0.510619  0.321799 0.396112 -0.0529064  0.0691237   0.0133289   199  ARG B C   
6515  O  O   . ARG B 199 ? 0.492535  0.319676 0.392193 -0.0646987  0.0757091   0.00913177  199  ARG B O   
6516  C  CB  . ARG B 199 ? 0.435151  0.266927 0.344544 -0.0472036  0.0533306   0.00257913  199  ARG B CB  
6517  C  CG  . ARG B 199 ? 0.401112  0.255529 0.324995 -0.0387669  0.0415694   -0.00181983 199  ARG B CG  
6518  C  CD  . ARG B 199 ? 0.403373  0.262165 0.339082 -0.0454365  0.0402929   -0.0100106  199  ARG B CD  
6519  N  NE  . ARG B 199 ? 0.450248  0.278962 0.369952 -0.0434956  0.0423633   -0.00884951 199  ARG B NE  
6520  C  CZ  . ARG B 199 ? 0.463453  0.280743 0.373363 -0.03118    0.0364445   -0.00705872 199  ARG B CZ  
6521  N  NH1 . ARG B 199 ? 0.485738  0.273546 0.381059 -0.0313193  0.040153    -0.00682585 199  ARG B NH1 
6522  N  NH2 . ARG B 199 ? 0.395264  0.229541 0.309891 -0.0191612  0.0275847   -0.00603966 199  ARG B NH2 
6523  N  N   . SER B 200 ? 0.558179  0.334727 0.416554 -0.0487322  0.0739153   0.0209695   200  SER B N   
6524  C  CA  . SER B 200 ? 0.626099  0.380465 0.46974  -0.0600531  0.0887397   0.0250324   200  SER B CA  
6525  C  C   . SER B 200 ? 0.649652  0.422    0.497466 -0.0635945  0.0938522   0.0263468   200  SER B C   
6526  O  O   . SER B 200 ? 0.671774  0.441202 0.521061 -0.0779075  0.106965    0.0253331   200  SER B O   
6527  C  CB  . SER B 200 ? 0.639451  0.351203 0.449486 -0.0530967  0.0929539   0.0342294   200  SER B CB  
6528  O  OG  . SER B 200 ? 0.64425   0.352487 0.437044 -0.0354561  0.0849864   0.0413502   200  SER B OG  
6529  N  N   . TRP B 201 ? 0.631814  0.42479  0.483957 -0.0515891  0.0838758   0.0272246   201  TRP B N   
6530  C  CA  . TRP B 201 ? 0.647311  0.455252 0.500175 -0.0517054  0.0872014   0.0286319   201  TRP B CA  
6531  C  C   . TRP B 201 ? 0.627671  0.462423 0.506189 -0.0656389  0.093687    0.0208153   201  TRP B C   
6532  O  O   . TRP B 201 ? 0.764632  0.609522 0.643484 -0.067951   0.0995588   0.0213856   201  TRP B O   
6533  C  CB  . TRP B 201 ? 0.603161  0.429895 0.459456 -0.0371789  0.0741532   0.0288248   201  TRP B CB  
6534  C  CG  . TRP B 201 ? 0.58136   0.388252 0.414098 -0.0219998  0.0668637   0.0354651   201  TRP B CG  
6535  C  CD1 . TRP B 201 ? 0.66458   0.43775  0.467911 -0.0178264  0.0718017   0.0433143   201  TRP B CD1 
6536  C  CD2 . TRP B 201 ? 0.591955  0.412952 0.429729 -0.00852378 0.0528047   0.0340147   201  TRP B CD2 
6537  N  NE1 . TRP B 201 ? 0.704855  0.472261 0.494989 -0.00116225 0.0605635   0.046525    201  TRP B NE1 
6538  C  CE2 . TRP B 201 ? 0.630197  0.427851 0.442468 0.00398758  0.0490536   0.04041     201  TRP B CE2 
6539  C  CE3 . TRP B 201 ? 0.516144  0.366504 0.377007 -0.0059951  0.0435089   0.0277993   201  TRP B CE3 
6540  C  CZ2 . TRP B 201 ? 0.621254  0.42795  0.433467 0.0183427   0.0360443   0.0395639   201  TRP B CZ2 
6541  C  CZ3 . TRP B 201 ? 0.535556  0.391996 0.395097 0.00675873  0.0320633   0.0276188   201  TRP B CZ3 
6542  C  CH2 . TRP B 201 ? 0.563812  0.400711 0.400891 0.0185502   0.0281638   0.0328147   201  TRP B CH2 
6543  N  N   . TYR B 202 ? 0.564676  0.412452 0.464537 -0.0736391  0.0919187   0.0129361   202  TYR B N   
6544  C  CA  . TYR B 202 ? 0.510626  0.387578 0.436835 -0.0849357  0.0958186   0.00420631  202  TYR B CA  
6545  C  C   . TYR B 202 ? 0.570879  0.436733 0.498472 -0.102709   0.11047     0.00124291  202  TYR B C   
6546  O  O   . TYR B 202 ? 0.578939  0.469875 0.529501 -0.113497   0.114918    -0.00713171 202  TYR B O   
6547  C  CB  . TYR B 202 ? 0.445599  0.347329 0.394513 -0.0813452  0.0834147   -0.00337503 202  TYR B CB  
6548  C  CG  . TYR B 202 ? 0.400934  0.316777 0.350606 -0.0666704  0.0721601   -0.00101937 202  TYR B CG  
6549  C  CD1 . TYR B 202 ? 0.379593  0.321226 0.343221 -0.0655631  0.0712997   -0.00423564 202  TYR B CD1 
6550  C  CD2 . TYR B 202 ? 0.39877   0.30175  0.335105 -0.0542401  0.0632181   0.00391776  202  TYR B CD2 
6551  C  CE1 . TYR B 202 ? 0.3553    0.30733  0.318976 -0.0535278  0.0620538   -0.00258544 202  TYR B CE1 
6552  C  CE2 . TYR B 202 ? 0.366268  0.282066 0.304006 -0.0427317  0.0540571   0.00521519  202  TYR B CE2 
6553  C  CZ  . TYR B 202 ? 0.369306  0.30877  0.320682 -0.0430314  0.0536215   0.00189096  202  TYR B CZ  
6554  O  OH  . TYR B 202 ? 0.334328  0.285166 0.287257 -0.0333647  0.0459093   0.00244112  202  TYR B OH  
6555  N  N   . ASN B 203 ? 0.646074  0.474664 0.549622 -0.105482   0.117671    0.00749312  203  ASN B N   
6556  C  CA  . ASN B 203 ? 0.685524  0.496523 0.587697 -0.123248   0.131775    0.00472246  203  ASN B CA  
6557  C  C   . ASN B 203 ? 0.672699  0.513338 0.60758  -0.136858   0.132012    -0.00858277 203  ASN B C   
6558  O  O   . ASN B 203 ? 0.641542  0.49856  0.59096  -0.150419   0.142679    -0.01408    203  ASN B O   
6559  C  CB  . ASN B 203 ? 0.709983  0.517496 0.606544 -0.134961   0.148612    0.00687626  203  ASN B CB  
6560  C  CG  . ASN B 203 ? 0.7767    0.544253 0.63495  -0.127731   0.154819    0.0200706   203  ASN B CG  
6561  O  OD1 . ASN B 203 ? 0.82641   0.595611 0.672198 -0.111966   0.146851    0.0263812   203  ASN B OD1 
6562  N  ND2 . ASN B 203 ? 0.817622  0.548968 0.656566 -0.138489   0.168204    0.0238765   203  ASN B ND2 
6563  N  N   . SER B 204 ? 0.68037   0.528246 0.626138 -0.13271    0.120231    -0.0141108  204  SER B N   
6564  C  CA  . SER B 204 ? 0.713696  0.589629 0.688762 -0.143917   0.118439    -0.027316   204  SER B CA  
6565  C  C   . SER B 204 ? 0.772805  0.632011 0.744404 -0.143892   0.112506    -0.0306976  204  SER B C   
6566  O  O   . SER B 204 ? 0.763785  0.616742 0.726378 -0.128848   0.100972    -0.026572   204  SER B O   
6567  C  CB  . SER B 204 ? 0.723683  0.640888 0.72175  -0.135701   0.107324    -0.0325578  204  SER B CB  
6568  O  OG  . SER B 204 ? 0.789707  0.73506  0.815346 -0.146595   0.106311    -0.0457553  204  SER B OG  
6569  N  N   . PRO B 205 ? 0.782821  0.632189 0.759929 -0.161127   0.121412    -0.038289   205  PRO B N   
6570  C  CA  . PRO B 205 ? 0.772872  0.60493  0.746386 -0.162343   0.11672     -0.0429481  205  PRO B CA  
6571  C  C   . PRO B 205 ? 0.725293  0.59068  0.71989  -0.154379   0.100817    -0.051507   205  PRO B C   
6572  O  O   . PRO B 205 ? 0.781668  0.636327 0.768036 -0.144128   0.0915779   -0.050632   205  PRO B O   
6573  C  CB  . PRO B 205 ? 0.765173  0.585323 0.744321 -0.185424   0.131016    -0.0512569  205  PRO B CB  
6574  C  CG  . PRO B 205 ? 0.797693  0.619322 0.775366 -0.194832   0.145649    -0.0469584  205  PRO B CG  
6575  C  CD  . PRO B 205 ? 0.792416  0.64746  0.780221 -0.181069   0.137062    -0.0437557  205  PRO B CD  
6576  N  N   . THR B 206 ? 0.650515  0.556161 0.670964 -0.157683   0.0976076   -0.0594101  206  THR B N   
6577  C  CA  . THR B 206 ? 0.601472  0.536442 0.639406 -0.150254   0.0830612   -0.06747    206  THR B CA  
6578  C  C   . THR B 206 ? 0.553518  0.505401 0.590743 -0.131754   0.0722874   -0.0605539  206  THR B C   
6579  O  O   . THR B 206 ? 0.509944  0.492936 0.564636 -0.126926   0.0628731   -0.0668278  206  THR B O   
6580  C  CB  . THR B 206 ? 0.581467  0.549973 0.647943 -0.164136   0.0846454   -0.0818095  206  THR B CB  
6581  O  OG1 . THR B 206 ? 0.577943  0.557817 0.64865  -0.166246   0.0927529   -0.0777302  206  THR B OG1 
6582  C  CG2 . THR B 206 ? 0.627326  0.582028 0.69743  -0.182932   0.0929697   -0.0914865  206  THR B CG2 
6583  N  N   . PHE B 207 ? 0.516796  0.447902 0.533349 -0.121313   0.0734145   -0.0481695  207  PHE B N   
6584  C  CA  . PHE B 207 ? 0.508547  0.452936 0.523495 -0.105637   0.0648313   -0.041841   207  PHE B CA  
6585  C  C   . PHE B 207 ? 0.462563  0.423573 0.485646 -0.0953765  0.0511434   -0.0456597  207  PHE B C   
6586  O  O   . PHE B 207 ? 0.460055  0.448221 0.496778 -0.0902704  0.0448578   -0.048396   207  PHE B O   
6587  C  CB  . PHE B 207 ? 0.467449  0.385404 0.457908 -0.0956646  0.0664812   -0.0295017  207  PHE B CB  
6588  C  CG  . PHE B 207 ? 0.434955  0.366379 0.424198 -0.0819985  0.0594425   -0.023856   207  PHE B CG  
6589  C  CD1 . PHE B 207 ? 0.395673  0.351981 0.398191 -0.0827676  0.060382    -0.025857   207  PHE B CD1 
6590  C  CD2 . PHE B 207 ? 0.436268  0.356082 0.411905 -0.0683883  0.05189     -0.0175064  207  PHE B CD2 
6591  C  CE1 . PHE B 207 ? 0.379067  0.344591 0.379193 -0.0709824  0.0545088   -0.0212339  207  PHE B CE1 
6592  C  CE2 . PHE B 207 ? 0.422132  0.353451 0.397039 -0.05763    0.0461484   -0.0133538  207  PHE B CE2 
6593  C  CZ  . PHE B 207 ? 0.403984  0.356984 0.390599 -0.0592135  0.0474873   -0.0152061  207  PHE B CZ  
6594  N  N   . GLU B 208 ? 0.49208   0.435278 0.505236 -0.0918661  0.0471555   -0.0456418  208  GLU B N   
6595  C  CA  . GLU B 208 ? 0.467101  0.422107 0.484213 -0.0820209  0.0356938   -0.0483651  208  GLU B CA  
6596  C  C   . GLU B 208 ? 0.482314  0.466501 0.519762 -0.0867676  0.0306588   -0.059253   208  GLU B C   
6597  O  O   . GLU B 208 ? 0.460261  0.46511  0.504681 -0.0779648  0.0227321   -0.0594885  208  GLU B O   
6598  C  CB  . GLU B 208 ? 0.51884   0.449918 0.521282 -0.0766836  0.0331779   -0.0467317  208  GLU B CB  
6599  C  CG  . GLU B 208 ? 0.513654  0.424626 0.497877 -0.0658562  0.0336689   -0.035854   208  GLU B CG  
6600  C  CD  . GLU B 208 ? 0.583158  0.474299 0.554198 -0.0573458  0.0299925   -0.0343972  208  GLU B CD  
6601  O  OE1 . GLU B 208 ? 0.577115  0.480892 0.552404 -0.0489384  0.0219727   -0.0363112  208  GLU B OE1 
6602  O  OE2 . GLU B 208 ? 0.614399  0.476485 0.569908 -0.0585541  0.0355895   -0.0312757  208  GLU B OE2 
6603  N  N   . ASP B 209 ? 0.461163  0.446413 0.507331 -0.100469   0.0353004   -0.0683896  209  ASP B N   
6604  C  CA  . ASP B 209 ? 0.469348  0.484125 0.536106 -0.106173   0.0306034   -0.0805634  209  ASP B CA  
6605  C  C   . ASP B 209 ? 0.416894  0.461139 0.498594 -0.103471   0.0292405   -0.0811234  209  ASP B C   
6606  O  O   . ASP B 209 ? 0.409357  0.478246 0.501614 -0.0966702  0.019907    -0.0860438  209  ASP B O   
6607  C  CB  . ASP B 209 ? 0.557897  0.567524 0.631995 -0.123609   0.037842    -0.0905995  209  ASP B CB  
6608  C  CG  . ASP B 209 ? 0.674989  0.65578  0.734976 -0.126067   0.038391    -0.0921532  209  ASP B CG  
6609  O  OD1 . ASP B 209 ? 0.761708  0.734446 0.810187 -0.113123   0.0308383   -0.0877879  209  ASP B OD1 
6610  O  OD2 . ASP B 209 ? 0.773374  0.738797 0.833416 -0.140932   0.0471244   -0.0977057  209  ASP B OD2 
6611  N  N   . ASP B 210 ? 0.401217  0.441696 0.482143 -0.107928   0.0386982   -0.076034   210  ASP B N   
6612  C  CA  . ASP B 210 ? 0.388993  0.455107 0.482675 -0.104741   0.0386776   -0.0763226  210  ASP B CA  
6613  C  C   . ASP B 210 ? 0.340404  0.414445 0.429527 -0.0877527  0.0287638   -0.0702085  210  ASP B C   
6614  O  O   . ASP B 210 ? 0.319696  0.420124 0.422161 -0.0823489  0.0224316   -0.0750294  210  ASP B O   
6615  C  CB  . ASP B 210 ? 0.414206  0.470246 0.503202 -0.111426   0.0513668   -0.0707422  210  ASP B CB  
6616  C  CG  . ASP B 210 ? 0.495763  0.548365 0.592465 -0.130236   0.0632579   -0.0778014  210  ASP B CG  
6617  O  OD1 . ASP B 210 ? 0.489487  0.550898 0.598185 -0.138598   0.0607044   -0.0886419  210  ASP B OD1 
6618  O  OD2 . ASP B 210 ? 0.569983  0.610704 0.66     -0.136866   0.0753746   -0.0727921  210  ASP B OD2 
6619  N  N   . LEU B 211 ? 0.307652  0.358848 0.378014 -0.0794127  0.0278128   -0.0599644  211  LEU B N   
6620  C  CA  . LEU B 211 ? 0.299079  0.354571 0.364208 -0.065079   0.0194732   -0.0544465  211  LEU B CA  
6621  C  C   . LEU B 211 ? 0.307534  0.377388 0.378794 -0.0597189  0.00936173  -0.0603902  211  LEU B C   
6622  O  O   . LEU B 211 ? 0.273917  0.358942 0.348896 -0.0505274  0.00292531  -0.0600258  211  LEU B O   
6623  C  CB  . LEU B 211 ? 0.32404   0.352988 0.369953 -0.0595072  0.0201018   -0.0452935  211  LEU B CB  
6624  C  CG  . LEU B 211 ? 0.343956  0.357041 0.378527 -0.0601119  0.0277639   -0.0374514  211  LEU B CG  
6625  C  CD1 . LEU B 211 ? 0.359613  0.349045 0.37652  -0.0533401  0.0260674   -0.0305046  211  LEU B CD1 
6626  C  CD2 . LEU B 211 ? 0.313773  0.339912 0.351455 -0.0544329  0.0275655   -0.034375   211  LEU B CD2 
6627  N  N   . GLU B 212 ? 0.333357  0.395379 0.402836 -0.0647172  0.00806483  -0.0654742  212  GLU B N   
6628  C  CA  . GLU B 212 ? 0.329481  0.40276  0.401516 -0.0595153  -0.00131436 -0.0712524  212  GLU B CA  
6629  C  C   . GLU B 212 ? 0.316426  0.419741 0.405921 -0.0602178  -0.00591695 -0.0802314  212  GLU B C   
6630  O  O   . GLU B 212 ? 0.314748  0.431346 0.404784 -0.0504697  -0.0144896  -0.0814811  212  GLU B O   
6631  C  CB  . GLU B 212 ? 0.37452   0.431789 0.440614 -0.0658033  -0.00051639 -0.0757995  212  GLU B CB  
6632  C  CG  . GLU B 212 ? 0.467628  0.534788 0.53393  -0.0607463  -0.00979872 -0.0824227  212  GLU B CG  
6633  C  CD  . GLU B 212 ? 0.671902  0.721282 0.731105 -0.0666301  -0.00857416 -0.0874309  212  GLU B CD  
6634  O  OE1 . GLU B 212 ? 0.748805  0.776909 0.793511 -0.0613555  -0.00732139 -0.0810667  212  GLU B OE1 
6635  O  OE2 . GLU B 212 ? 0.768563  0.825393 0.837107 -0.0765417  -0.00877286 -0.0984792  212  GLU B OE2 
6636  N  N   . HIS B 213 ? 0.330361  0.44466  0.433977 -0.0716811  -5.68e-06   -0.0869732  213  HIS B N   
6637  C  CA  . HIS B 213 ? 0.35189   0.498327 0.474847 -0.0721964  -0.0044194  -0.0969548  213  HIS B CA  
6638  C  C   . HIS B 213 ? 0.312306  0.471739 0.437325 -0.0605949  -0.00690138 -0.0916502  213  HIS B C   
6639  O  O   . HIS B 213 ? 0.29506   0.476472 0.427959 -0.0522504  -0.0152895  -0.0965307  213  HIS B O   
6640  C  CB  . HIS B 213 ? 0.432217  0.589265 0.57203  -0.0886977  0.00381656  -0.106524   213  HIS B CB  
6641  C  CG  . HIS B 213 ? 0.565953  0.714273 0.706728 -0.100755   0.00498964  -0.115011   213  HIS B CG  
6642  N  ND1 . HIS B 213 ? 0.659971  0.804434 0.809464 -0.118402   0.0156772   -0.121174   213  HIS B ND1 
6643  C  CD2 . HIS B 213 ? 0.632391  0.77404  0.765926 -0.0983204  -0.00247454 -0.11898    213  HIS B CD2 
6644  C  CE1 . HIS B 213 ? 0.638718  0.773357 0.786342 -0.126405   0.0143588   -0.128774   213  HIS B CE1 
6645  N  NE2 . HIS B 213 ? 0.595917  0.72968  0.734138 -0.114037   0.00306745  -0.127897   213  HIS B NE2 
6646  N  N   . LEU B 214 ? 0.290249  0.434985 0.406943 -0.059565   0.00022406  -0.0819899  214  LEU B N   
6647  C  CA  . LEU B 214 ? 0.292121  0.444198 0.407685 -0.0482176  -0.00188612 -0.0764882  214  LEU B CA  
6648  C  C   . LEU B 214 ? 0.251972  0.40057  0.356677 -0.0346513  -0.0116215  -0.0722802  214  LEU B C   
6649  O  O   . LEU B 214 ? 0.221344  0.386144 0.330471 -0.0248984  -0.0181118  -0.0741888  214  LEU B O   
6650  C  CB  . LEU B 214 ? 0.288269  0.422561 0.393752 -0.0490835  0.00667531  -0.0670303  214  LEU B CB  
6651  C  CG  . LEU B 214 ? 0.341312  0.481948 0.456521 -0.0598507  0.0173472   -0.0699886  214  LEU B CG  
6652  C  CD1 . LEU B 214 ? 0.34207   0.461266 0.441641 -0.0581644  0.0240299   -0.0595354  214  LEU B CD1 
6653  C  CD2 . LEU B 214 ? 0.30837   0.480642 0.442678 -0.0567041  0.0155147   -0.0777     214  LEU B CD2 
6654  N  N   . TYR B 215 ? 0.232507  0.358521 0.321711 -0.0333259  -0.0118088  -0.065853   215  TYR B N   
6655  C  CA  . TYR B 215 ? 0.231654  0.353498 0.3101   -0.0220022  -0.0192044  -0.0618623  215  TYR B CA  
6656  C  C   . TYR B 215 ? 0.249498  0.389773 0.333367 -0.0169377  -0.0281934  -0.0696245  215  TYR B C   
6657  O  O   . TYR B 215 ? 0.270543  0.414516 0.348603 -0.00559681 -0.0339769  -0.066865   215  TYR B O   
6658  C  CB  . TYR B 215 ? 0.2372    0.335878 0.301072 -0.0222655  -0.0176683  -0.0559235  215  TYR B CB  
6659  C  CG  . TYR B 215 ? 0.274348  0.369049 0.327736 -0.0111225  -0.0225214  -0.0503061  215  TYR B CG  
6660  C  CD1 . TYR B 215 ? 0.304112  0.394954 0.353734 -0.00568466 -0.0208007  -0.0435719  215  TYR B CD1 
6661  C  CD2 . TYR B 215 ? 0.263213  0.358191 0.310151 -0.0064404  -0.0282428  -0.0522627  215  TYR B CD2 
6662  C  CE1 . TYR B 215 ? 0.374599  0.460566 0.414844 0.0029977   -0.0239402  -0.0387735  215  TYR B CE1 
6663  C  CE2 . TYR B 215 ? 0.290401  0.381051 0.326959 0.00292029  -0.0311457  -0.0468796  215  TYR B CE2 
6664  C  CZ  . TYR B 215 ? 0.321201  0.406601 0.354668 0.00706255  -0.0286167  -0.0400442  215  TYR B CZ  
6665  O  OH  . TYR B 215 ? 0.343159  0.422424 0.366341 0.0148755   -0.0301771  -0.0348743  215  TYR B OH  
6666  N  N   . GLN B 216 ? 0.246971  0.396532 0.339542 -0.024815   -0.0297192  -0.0792658  216  GLN B N   
6667  C  CA  . GLN B 216 ? 0.287846  0.455194 0.383821 -0.0190302  -0.0395221  -0.0872606  216  GLN B CA  
6668  C  C   . GLN B 216 ? 0.279634  0.470743 0.385932 -0.0103223  -0.0445708  -0.0904223  216  GLN B C   
6669  O  O   . GLN B 216 ? 0.286923  0.486486 0.387932 0.00136686  -0.0535389  -0.0916077  216  GLN B O   
6670  C  CB  . GLN B 216 ? 0.356368  0.534383 0.463767 -0.0301297  -0.0405283  -0.0995798  216  GLN B CB  
6671  C  CG  . GLN B 216 ? 0.493344  0.648537 0.590227 -0.0376219  -0.0369752  -0.0988149  216  GLN B CG  
6672  C  CD  . GLN B 216 ? 0.611108  0.775308 0.718961 -0.0493861  -0.037767   -0.112065   216  GLN B CD  
6673  O  OE1 . GLN B 216 ? 0.690981  0.881082 0.816274 -0.0528862  -0.0409842  -0.122502   216  GLN B OE1 
6674  N  NE2 . GLN B 216 ? 0.596703  0.74012  0.695143 -0.055644   -0.0347778  -0.112624   216  GLN B NE2 
6675  N  N   . GLN B 217 ? 0.274739  0.475807 0.394237 -0.0147743  -0.038642   -0.091506   217  GLN B N   
6676  C  CA  . GLN B 217 ? 0.295497  0.520055 0.4255   -0.00519061 -0.0434225  -0.095246   217  GLN B CA  
6677  C  C   . GLN B 217 ? 0.254909  0.466458 0.370185 0.00843164  -0.0447085  -0.0844479  217  GLN B C   
6678  O  O   . GLN B 217 ? 0.244029  0.468481 0.36038  0.0210062   -0.0512171  -0.0857748  217  GLN B O   
6679  C  CB  . GLN B 217 ? 0.319105  0.560732 0.468216 -0.0125114  -0.0362015  -0.100177   217  GLN B CB  
6680  C  CG  . GLN B 217 ? 0.418912  0.676139 0.586398 -0.0281986  -0.0325377  -0.112012   217  GLN B CG  
6681  C  CD  . GLN B 217 ? 0.498058  0.767256 0.681332 -0.0365468  -0.022252   -0.114609   217  GLN B CD  
6682  O  OE1 . GLN B 217 ? 0.50855   0.80542  0.708023 -0.0311988  -0.0245277  -0.121384   217  GLN B OE1 
6683  N  NE2 . GLN B 217 ? 0.460636  0.708363 0.637885 -0.0487026  -0.0106352  -0.108976   217  GLN B NE2 
6684  N  N   . LEU B 218 ? 0.242573  0.428228 0.34408  0.00600628  -0.0384323  -0.0742312  218  LEU B N   
6685  C  CA  . LEU B 218 ? 0.21836   0.390584 0.306984 0.0163658   -0.0383408  -0.0648479  218  LEU B CA  
6686  C  C   . LEU B 218 ? 0.21689   0.375852 0.287923 0.0249975   -0.0442368  -0.0599824  218  LEU B C   
6687  O  O   . LEU B 218 ? 0.198986  0.349789 0.259484 0.0351655   -0.0458401  -0.0539782  218  LEU B O   
6688  C  CB  . LEU B 218 ? 0.210996  0.364745 0.294476 0.00988143  -0.0291998  -0.0574283  218  LEU B CB  
6689  C  CG  . LEU B 218 ? 0.226514  0.387991 0.322563 0.00086746  -0.0213022  -0.0603293  218  LEU B CG  
6690  C  CD1 . LEU B 218 ? 0.238525  0.377978 0.324703 -0.00546411 -0.0135472  -0.0527943  218  LEU B CD1 
6691  C  CD2 . LEU B 218 ? 0.280052  0.453406 0.381185 0.0100075   -0.0219501  -0.0607529  218  LEU B CD2 
6692  N  N   . GLU B 219 ? 0.237278  0.391075 0.303344 0.0204724   -0.0461612  -0.0620401  219  GLU B N   
6693  C  CA  . GLU B 219 ? 0.234605  0.373797 0.282471 0.0273614   -0.0495202  -0.0567924  219  GLU B CA  
6694  C  C   . GLU B 219 ? 0.262736  0.406907 0.30149  0.0417634   -0.0571863  -0.0559868  219  GLU B C   
6695  O  O   . GLU B 219 ? 0.272033  0.399026 0.294015 0.0484693   -0.0563872  -0.0478519  219  GLU B O   
6696  C  CB  . GLU B 219 ? 0.274603  0.409379 0.319404 0.0205656   -0.0501746  -0.0606476  219  GLU B CB  
6697  C  CG  . GLU B 219 ? 0.367831  0.487263 0.393591 0.0267152   -0.0517399  -0.0552101  219  GLU B CG  
6698  C  CD  . GLU B 219 ? 0.518903  0.633665 0.540284 0.0214384   -0.0523571  -0.0595658  219  GLU B CD  
6699  O  OE1 . GLU B 219 ? 0.516698  0.639029 0.549943 0.0124957   -0.0519144  -0.067147   219  GLU B OE1 
6700  O  OE2 . GLU B 219 ? 0.680821  0.783632 0.687006 0.0254546   -0.0523822  -0.0558902  219  GLU B OE2 
6701  N  N   . PRO B 220 ? 0.263313  0.43017  0.311443 0.0473144   -0.0648425  -0.0644681  220  PRO B N   
6702  C  CA  . PRO B 220 ? 0.268085  0.438675 0.305296 0.0632534   -0.0730465  -0.0635132  220  PRO B CA  
6703  C  C   . PRO B 220 ? 0.253803  0.411162 0.282807 0.0715479   -0.0697015  -0.0546902  220  PRO B C   
6704  O  O   . PRO B 220 ? 0.26735   0.410056 0.277098 0.0822217   -0.0720691  -0.0482322  220  PRO B O   
6705  C  CB  . PRO B 220 ? 0.274237  0.476451 0.328279 0.0672401   -0.0817834  -0.075891   220  PRO B CB  
6706  C  CG  . PRO B 220 ? 0.291763  0.50529  0.364908 0.0501859   -0.0774496  -0.0842024  220  PRO B CG  
6707  C  CD  . PRO B 220 ? 0.265154  0.45554  0.334636 0.0387657   -0.0660618  -0.075954   220  PRO B CD  
6708  N  N   . LEU B 221 ? 0.229674  0.390642 0.271851 0.0663226   -0.0636429  -0.0545897  221  LEU B N   
6709  C  CA  . LEU B 221 ? 0.227645  0.375425 0.262705 0.0730221   -0.0599661  -0.0473921  221  LEU B CA  
6710  C  C   . LEU B 221 ? 0.220027  0.339308 0.23655  0.0710041   -0.054691   -0.0373801  221  LEU B C   
6711  O  O   . LEU B 221 ? 0.237612  0.341341 0.238805 0.0803002   -0.0548671  -0.0310701  221  LEU B O   
6712  C  CB  . LEU B 221 ? 0.226849  0.381911 0.277708 0.0660211   -0.0532927  -0.0492499  221  LEU B CB  
6713  C  CG  . LEU B 221 ? 0.250677  0.433153 0.319068 0.0715276   -0.0570494  -0.0580585  221  LEU B CG  
6714  C  CD1 . LEU B 221 ? 0.248119  0.455428 0.331742 0.0663114   -0.0620769  -0.0687134  221  LEU B CD1 
6715  C  CD2 . LEU B 221 ? 0.223636  0.407936 0.302759 0.0655781   -0.04847    -0.0578901  221  LEU B CD2 
6716  N  N   . TYR B 222 ? 0.194253  0.306518 0.212663 0.0587053   -0.0494511  -0.0362939  222  TYR B N   
6717  C  CA  . TYR B 222 ? 0.192147  0.281325 0.195794 0.0565026   -0.0444706  -0.0282153  222  TYR B CA  
6718  C  C   . TYR B 222 ? 0.210518  0.289994 0.19622  0.063608    -0.0479417  -0.0251415  222  TYR B C   
6719  O  O   . TYR B 222 ? 0.216852  0.27742  0.187155 0.0672086   -0.0446787  -0.0179482  222  TYR B O   
6720  C  CB  . TYR B 222 ? 0.181102  0.267119 0.190391 0.0439908   -0.0395582  -0.0287584  222  TYR B CB  
6721  C  CG  . TYR B 222 ? 0.183548  0.249836 0.180229 0.0421739   -0.0347311  -0.021765   222  TYR B CG  
6722  C  CD1 . TYR B 222 ? 0.187342  0.242534 0.181428 0.041962    -0.0300544  -0.0168873  222  TYR B CD1 
6723  C  CD2 . TYR B 222 ? 0.193694  0.253817 0.182162 0.0402736   -0.0345066  -0.0210628  222  TYR B CD2 
6724  C  CE1 . TYR B 222 ? 0.186962  0.226966 0.172146 0.0392949   -0.0254717  -0.0119209  222  TYR B CE1 
6725  C  CE2 . TYR B 222 ? 0.197262  0.242402 0.176834 0.038001    -0.0292215  -0.0156531  222  TYR B CE2 
6726  C  CZ  . TYR B 222 ? 0.192553  0.228336 0.171027 0.037374    -0.0248562  -0.0112551  222  TYR B CZ  
6727  O  OH  . TYR B 222 ? 0.19059   0.214737 0.163556 0.0336667   -0.0194999  -0.00751031 222  TYR B OH  
6728  N  N   . LEU B 223 ? 0.214934  0.307008 0.201827 0.0650923   -0.0541669  -0.0310754  223  LEU B N   
6729  C  CA  . LEU B 223 ? 0.241642  0.323922 0.209157 0.0719031   -0.0571116  -0.0282142  223  LEU B CA  
6730  C  C   . LEU B 223 ? 0.270057  0.343052 0.221834 0.085872    -0.0599778  -0.023006   223  LEU B C   
6731  O  O   . LEU B 223 ? 0.268649  0.321548 0.20019  0.0896392   -0.0569028  -0.0157634  223  LEU B O   
6732  C  CB  . LEU B 223 ? 0.27508   0.373229 0.245835 0.0718215   -0.0642327  -0.0366582  223  LEU B CB  
6733  C  CG  . LEU B 223 ? 0.298264  0.39835  0.278668 0.0585671   -0.0605108  -0.0408061  223  LEU B CG  
6734  C  CD1 . LEU B 223 ? 0.316075  0.429669 0.297815 0.0584252   -0.0675906  -0.0499685  223  LEU B CD1 
6735  C  CD2 . LEU B 223 ? 0.292533  0.371783 0.262749 0.0533265   -0.0521197  -0.0332557  223  LEU B CD2 
6736  N  N   . ASN B 224 ? 0.267628  0.354877 0.22883  0.0933778   -0.065134   -0.0269165  224  ASN B N   
6737  C  CA  . ASN B 224 ? 0.30811   0.386092 0.254083 0.10868     -0.0686135  -0.0224489  224  ASN B CA  
6738  C  C   . ASN B 224 ? 0.294532  0.34846  0.23181  0.107305    -0.0600075  -0.013816   224  ASN B C   
6739  O  O   . ASN B 224 ? 0.328894  0.361417 0.244472 0.11581     -0.0588142  -0.00663588 224  ASN B O   
6740  C  CB  . ASN B 224 ? 0.308572  0.410608 0.268146 0.11827     -0.0768727  -0.0301044  224  ASN B CB  
6741  C  CG  . ASN B 224 ? 0.336414  0.454356 0.292066 0.126583    -0.0875631  -0.0364279  224  ASN B CG  
6742  O  OD1 . ASN B 224 ? 0.365962  0.473469 0.299875 0.141323    -0.0929724  -0.0324025  224  ASN B OD1 
6743  N  ND2 . ASN B 224 ? 0.312065  0.45407  0.287329 0.11753     -0.090644   -0.0464989  224  ASN B ND2 
6744  N  N   . LEU B 225 ? 0.272355  0.328208 0.224959 0.0961844   -0.0536813  -0.0145918  225  LEU B N   
6745  C  CA  . LEU B 225 ? 0.261505  0.295645 0.206151 0.094688    -0.0462626  -0.0078094  225  LEU B CA  
6746  C  C   . LEU B 225 ? 0.267892  0.280517 0.196374 0.0891784   -0.0401663  -0.00117088 225  LEU B C   
6747  O  O   . LEU B 225 ? 0.28248   0.272804 0.195436 0.092035    -0.0355024  0.00526924  225  LEU B O   
6748  C  CB  . LEU B 225 ? 0.245288  0.286703 0.208442 0.084136    -0.0412545  -0.0105376  225  LEU B CB  
6749  C  CG  . LEU B 225 ? 0.243498  0.264044 0.20005  0.0801165   -0.0336859  -0.00508109 225  LEU B CG  
6750  C  CD1 . LEU B 225 ? 0.260367  0.272721 0.209252 0.0926729   -0.0352584  -0.00364066 225  LEU B CD1 
6751  C  CD2 . LEU B 225 ? 0.236129  0.263698 0.208291 0.069596    -0.0293406  -0.00781233 225  LEU B CD2 
6752  N  N   . HIS B 226 ? 0.250446  0.26963  0.18485  0.0794301   -0.0387008  -0.0033256  226  HIS B N   
6753  C  CA  . HIS B 226 ? 0.264388  0.268362 0.186673 0.0737383   -0.0327529  0.00129599  226  HIS B CA  
6754  C  C   . HIS B 226 ? 0.29109   0.278974 0.188608 0.0834973   -0.0333992  0.0067324   226  HIS B C   
6755  O  O   . HIS B 226 ? 0.314844  0.282363 0.198765 0.0809909   -0.0259275  0.0129225   226  HIS B O   
6756  C  CB  . HIS B 226 ? 0.236013  0.253381 0.169022 0.065157    -0.0333989  -0.00370906 226  HIS B CB  
6757  C  CG  . HIS B 226 ? 0.237127  0.244779 0.161358 0.0595999   -0.02794    -0.0011238  226  HIS B CG  
6758  N  ND1 . HIS B 226 ? 0.248814  0.248977 0.154739 0.0651348   -0.0286013  0.00114585  226  HIS B ND1 
6759  C  CD2 . HIS B 226 ? 0.22343   0.228464 0.154604 0.0495837   -0.0214963  -0.00079926 226  HIS B CD2 
6760  C  CE1 . HIS B 226 ? 0.255453  0.24906  0.158182 0.0579415   -0.0217832  0.00266113  226  HIS B CE1 
6761  N  NE2 . HIS B 226 ? 0.229307  0.226926 0.148165 0.0489115   -0.0179815  0.00113114  226  HIS B NE2 
6762  N  N   . ALA B 227 ? 0.315232  0.31258  0.206399 0.0937301   -0.0419449  0.00397531  227  ALA B N   
6763  C  CA  . ALA B 227 ? 0.340291  0.32177  0.204656 0.104612    -0.0433435  0.00935829  227  ALA B CA  
6764  C  C   . ALA B 227 ? 0.373942  0.333091 0.222546 0.113362    -0.0405566  0.0165491   227  ALA B C   
6765  O  O   . ALA B 227 ? 0.38286   0.316627 0.208671 0.114832    -0.0339869  0.0243348   227  ALA B O   
6766  C  CB  . ALA B 227 ? 0.339453  0.339624 0.202983 0.114741    -0.0550077  0.00316069  227  ALA B CB  
6767  N  N   . PHE B 228 ? 0.379429  0.34701  0.240376 0.118249    -0.044398   0.0136779   228  PHE B N   
6768  C  CA  . PHE B 228 ? 0.410383  0.356017 0.257421 0.127043    -0.0418443  0.0195334   228  PHE B CA  
6769  C  C   . PHE B 228 ? 0.411025  0.333034 0.253319 0.115293    -0.0295818  0.0252068   228  PHE B C   
6770  O  O   . PHE B 228 ? 0.429571  0.323218 0.249145 0.119153    -0.0239762  0.0326269   228  PHE B O   
6771  C  CB  . PHE B 228 ? 0.425984  0.389886 0.291787 0.132737    -0.0476547  0.0134606   228  PHE B CB  
6772  C  CG  . PHE B 228 ? 0.480909  0.424299 0.335162 0.142775    -0.0457029  0.0177986   228  PHE B CG  
6773  C  CD1 . PHE B 228 ? 0.529491  0.461432 0.362695 0.161737    -0.0517206  0.0211523   228  PHE B CD1 
6774  C  CD2 . PHE B 228 ? 0.49679   0.432569 0.360704 0.134166    -0.0385069  0.0178491   228  PHE B CD2 
6775  C  CE1 . PHE B 228 ? 0.556959  0.467871 0.378524 0.171888    -0.0498347  0.0249183   228  PHE B CE1 
6776  C  CE2 . PHE B 228 ? 0.541415  0.457213 0.394209 0.143537    -0.0367027  0.0209116   228  PHE B CE2 
6777  C  CZ  . PHE B 228 ? 0.54189   0.444857 0.373827 0.162356    -0.0421519  0.0244736   228  PHE B CZ  
6778  N  N   . VAL B 229 ? 0.378153  0.311038 0.241208 0.100368    -0.0249923  0.0215144   229  VAL B N   
6779  C  CA  . VAL B 229 ? 0.358575  0.27384  0.220265 0.0885793   -0.0143772  0.0249698   229  VAL B CA  
6780  C  C   . VAL B 229 ? 0.371318  0.272846 0.217877 0.0829296   -0.00750142 0.0296468   229  VAL B C   
6781  O  O   . VAL B 229 ? 0.390165  0.268163 0.223767 0.0782866   0.00167564  0.0348546   229  VAL B O   
6782  C  CB  . VAL B 229 ? 0.334158  0.267357 0.221617 0.0762259   -0.0130221  0.0191006   229  VAL B CB  
6783  C  CG1 . VAL B 229 ? 0.328773  0.24962  0.217509 0.0632656   -0.00335992 0.020832    229  VAL B CG1 
6784  C  CG2 . VAL B 229 ? 0.324766  0.267857 0.224728 0.0809342   -0.0172501  0.0151333   229  VAL B CG2 
6785  N  N   . ARG B 230 ? 0.350742  0.267047 0.199633 0.081912    -0.0108388  0.0271166   230  ARG B N   
6786  C  CA  . ARG B 230 ? 0.352458  0.255819 0.185248 0.0777146   -0.0036899  0.0314005   230  ARG B CA  
6787  C  C   . ARG B 230 ? 0.38643   0.26092  0.188154 0.0872927   -0.00017543 0.0398497   230  ARG B C   
6788  O  O   . ARG B 230 ? 0.389691  0.243128 0.176162 0.0812619   0.0105895   0.0454018   230  ARG B O   
6789  C  CB  . ARG B 230 ? 0.337038  0.258362 0.172    0.0790994   -0.00934584 0.0272255   230  ARG B CB  
6790  C  CG  . ARG B 230 ? 0.347973  0.260889 0.171811 0.0722717   -0.00077996 0.0298084   230  ARG B CG  
6791  C  CD  . ARG B 230 ? 0.330044  0.260763 0.156654 0.0731578   -0.00623344 0.0243816   230  ARG B CD  
6792  N  NE  . ARG B 230 ? 0.332285  0.273187 0.15413  0.0858943   -0.018501   0.0214094   230  ARG B NE  
6793  C  CZ  . ARG B 230 ? 0.320952  0.283142 0.154178 0.0859668   -0.0262662  0.0135979   230  ARG B CZ  
6794  N  NH1 . ARG B 230 ? 0.301463  0.272025 0.14638  0.0756034   -0.0223243  0.00957747  230  ARG B NH1 
6795  N  NH2 . ARG B 230 ? 0.321687  0.296802 0.155369 0.0961838   -0.0377019  0.00919802  230  ARG B NH2 
6796  N  N   . ARG B 231 ? 0.408348  0.282817 0.200444 0.102811    -0.009447   0.0404363   231  ARG B N   
6797  C  CA  . ARG B 231 ? 0.468854  0.314692 0.228586 0.115296    -0.0078995  0.0487898   231  ARG B CA  
6798  C  C   . ARG B 231 ? 0.500672  0.317991 0.252328 0.110154    0.00265726  0.0543223   231  ARG B C   
6799  O  O   . ARG B 231 ? 0.531449  0.319029 0.257782 0.109674    0.0119369   0.06214     231  ARG B O   
6800  C  CB  . ARG B 231 ? 0.486532  0.340137 0.240094 0.134619    -0.0211381  0.0472454   231  ARG B CB  
6801  C  CG  . ARG B 231 ? 0.559833  0.378311 0.277222 0.148212    -0.0184951  0.0570652   231  ARG B CG  
6802  C  CD  . ARG B 231 ? 0.615907  0.413093 0.302596 0.149327    -0.0122669  0.064517    231  ARG B CD  
6803  N  NE  . ARG B 231 ? 0.631035  0.449404 0.314655 0.157595    -0.0227678  0.0603288   231  ARG B NE  
6804  C  CZ  . ARG B 231 ? 0.657607  0.462964 0.312826 0.163066    -0.0211865  0.0652785   231  ARG B CZ  
6805  N  NH1 . ARG B 231 ? 0.689237  0.457636 0.313715 0.162096    -0.00869395 0.0759664   231  ARG B NH1 
6806  N  NH2 . ARG B 231 ? 0.632631  0.461864 0.290482 0.168183    -0.0312652  0.0589735   231  ARG B NH2 
6807  N  N   . ALA B 232 ? 0.499058  0.324634 0.271527 0.106153    0.00153578  0.0498695   232  ALA B N   
6808  C  CA  . ALA B 232 ? 0.529652  0.328726 0.295555 0.100959    0.0108511   0.0535105   232  ALA B CA  
6809  C  C   . ALA B 232 ? 0.515848  0.305858 0.284637 0.0822623   0.0239663   0.0545369   232  ALA B C   
6810  O  O   . ALA B 232 ? 0.565939  0.325573 0.316766 0.077936    0.0345871   0.0601981   232  ALA B O   
6811  C  CB  . ALA B 232 ? 0.525514  0.337077 0.312059 0.10235     0.00580473  0.0476012   232  ALA B CB  
6812  N  N   . LEU B 233 ? 0.473476  0.28879  0.263251 0.0711543   0.0240045   0.0490879   233  LEU B N   
6813  C  CA  . LEU B 233 ? 0.461825  0.273128 0.256903 0.0544273   0.0357453   0.0487646   233  LEU B CA  
6814  C  C   . LEU B 233 ? 0.498648  0.290322 0.268084 0.0543044   0.0442628   0.0556563   233  LEU B C   
6815  O  O   . LEU B 233 ? 0.510072  0.287389 0.275028 0.0420545   0.0570046   0.0576475   233  LEU B O   
6816  C  CB  . LEU B 233 ? 0.439428  0.283402 0.261896 0.0460675   0.0320344   0.0411304   233  LEU B CB  
6817  C  CG  . LEU B 233 ? 0.416234  0.278917 0.264052 0.0430538   0.0261308   0.0344034   233  LEU B CG  
6818  C  CD1 . LEU B 233 ? 0.378067  0.270149 0.248227 0.0378049   0.0214104   0.027975    233  LEU B CD1 
6819  C  CD2 . LEU B 233 ? 0.462841  0.312682 0.315374 0.0312152   0.0352823   0.0335221   233  LEU B CD2 
6820  N  N   . HIS B 234 ? 0.519897  0.314445 0.274118 0.0669663   0.0373462   0.0582072   234  HIS B N   
6821  C  CA  . HIS B 234 ? 0.551437  0.324477 0.276232 0.0690905   0.0452266   0.0655807   234  HIS B CA  
6822  C  C   . HIS B 234 ? 0.600579  0.33346  0.296725 0.0729983   0.0535154   0.0745352   234  HIS B C   
6823  O  O   . HIS B 234 ? 0.594587  0.303969 0.272327 0.0651636   0.067244    0.0802312   234  HIS B O   
6824  C  CB  . HIS B 234 ? 0.563607  0.348585 0.277003 0.0834811   0.0342237   0.0655092   234  HIS B CB  
6825  C  CG  . HIS B 234 ? 0.643713  0.408708 0.324952 0.0872961   0.0410793   0.0726755   234  HIS B CG  
6826  N  ND1 . HIS B 234 ? 0.70156   0.439842 0.348336 0.102962    0.0391789   0.0809798   234  HIS B ND1 
6827  C  CD2 . HIS B 234 ? 0.64887   0.415603 0.325406 0.0785704   0.0500004   0.0729398   234  HIS B CD2 
6828  C  CE1 . HIS B 234 ? 0.73399   0.457581 0.354484 0.103485    0.0467376   0.0865148   234  HIS B CE1 
6829  N  NE2 . HIS B 234 ? 0.708062  0.449118 0.346705 0.0883687   0.0538158   0.0815266   234  HIS B NE2 
6830  N  N   . ARG B 235 ? 0.622258  0.346082 0.312288 0.0862739   0.0454316   0.075965    235  ARG B N   
6831  C  CA  . ARG B 235 ? 0.6859    0.36866  0.348408 0.0905512   0.053306    0.0841879   235  ARG B CA  
6832  C  C   . ARG B 235 ? 0.707808  0.375681 0.378245 0.0702398   0.0686564   0.083523    235  ARG B C   
6833  O  O   . ARG B 235 ? 0.737168  0.371143 0.382635 0.0652864   0.0820108   0.0908235   235  ARG B O   
6834  C  CB  . ARG B 235 ? 0.716251  0.394755 0.377117 0.106698    0.0425842   0.0837533   235  ARG B CB  
6835  C  CG  . ARG B 235 ? 0.789845  0.470325 0.431271 0.129567    0.0297973   0.0868053   235  ARG B CG  
6836  C  CD  . ARG B 235 ? 0.862184  0.545642 0.508927 0.144837    0.0189589   0.0841301   235  ARG B CD  
6837  N  NE  . ARG B 235 ? 0.929347  0.643524 0.585336 0.161211    0.00214632  0.0788132   235  ARG B NE  
6838  C  CZ  . ARG B 235 ? 0.997345  0.713625 0.633552 0.178425    -0.00712046 0.0813072   235  ARG B CZ  
6839  N  NH1 . ARG B 235 ? 0.968445  0.717048 0.620729 0.190863    -0.0223806  0.0737802   235  ARG B NH1 
6840  N  NH2 . ARG B 235 ? 1.0566    0.743313 0.656797 0.183568    -0.00129317 0.0907841   235  ARG B NH2 
6841  N  N   . ARG B 236 ? 0.697507  0.391299 0.402558 0.0580707   0.0669303   0.0743108   236  ARG B N   
6842  C  CA  . ARG B 236 ? 0.709786  0.395139 0.426808 0.0392876   0.0789948   0.0712036   236  ARG B CA  
6843  C  C   . ARG B 236 ? 0.702546  0.393017 0.422692 0.0237078   0.0909063   0.0708004   236  ARG B C   
6844  O  O   . ARG B 236 ? 0.767965  0.436031 0.480041 0.0109228   0.105223    0.0728322   236  ARG B O   
6845  C  CB  . ARG B 236 ? 0.67149   0.380719 0.421265 0.0326473   0.073045    0.0614912   236  ARG B CB  
6846  C  CG  . ARG B 236 ? 0.679371  0.394848 0.449977 0.0119241   0.0825708   0.0548956   236  ARG B CG  
6847  C  CD  . ARG B 236 ? 0.789263  0.470883 0.548354 0.00180905  0.0950765   0.0562969   236  ARG B CD  
6848  N  NE  . ARG B 236 ? 0.838689  0.501687 0.585381 0.0159637   0.0883802   0.0586686   236  ARG B NE  
6849  C  CZ  . ARG B 236 ? 0.935065  0.59557  0.692385 0.0145313   0.0858013   0.0531056   236  ARG B CZ  
6850  N  NH1 . ARG B 236 ? 0.892815  0.554888 0.666146 -0.00316448 0.0930918   0.046007    236  ARG B NH1 
6851  N  NH2 . ARG B 236 ? 0.883872  0.539392 0.634476 0.031361    0.0762156   0.0542498   236  ARG B NH2 
6852  N  N   . TYR B 237 ? 0.674566  0.395037 0.408109 0.023559    0.0858993   0.0671789   237  TYR B N   
6853  C  CA  . TYR B 237 ? 0.635818  0.366999 0.380701 0.00706524  0.097187    0.0639477   237  TYR B CA  
6854  C  C   . TYR B 237 ? 0.681181  0.402882 0.401855 0.0101412   0.103791    0.0702753   237  TYR B C   
6855  O  O   . TYR B 237 ? 0.682621  0.408452 0.408285 -0.00342714 0.115933    0.0685508   237  TYR B O   
6856  C  CB  . TYR B 237 ? 0.599617  0.371354 0.379901 4.555e-05   0.090955    0.0538081   237  TYR B CB  
6857  C  CG  . TYR B 237 ? 0.563852  0.347469 0.369356 -0.0059706  0.0864955   0.0466106   237  TYR B CG  
6858  C  CD1 . TYR B 237 ? 0.56406   0.343206 0.380765 -0.022068   0.0969346   0.0424792   237  TYR B CD1 
6859  C  CD2 . TYR B 237 ? 0.520494  0.319245 0.337434 0.00423219  0.0723855   0.043589    237  TYR B CD2 
6860  C  CE1 . TYR B 237 ? 0.541175  0.330733 0.378774 -0.0268376  0.0922575   0.0354346   237  TYR B CE1 
6861  C  CE2 . TYR B 237 ? 0.503346  0.311725 0.340659 -0.00088606 0.0689405   0.0372463   237  TYR B CE2 
6862  C  CZ  . TYR B 237 ? 0.518621  0.321723 0.36521  -0.0158188  0.0783833   0.0332624   237  TYR B CZ  
6863  O  OH  . TYR B 237 ? 0.510648  0.322696 0.375534 -0.0204485  0.0745198   0.0264117   237  TYR B OH  
6864  N  N   . GLY B 238 ? 0.681183  0.393739 0.377602 0.0279431   0.0954335   0.0763831   238  GLY B N   
6865  C  CA  . GLY B 238 ? 0.708336  0.40783  0.37641  0.0321703   0.101861    0.0830133   238  GLY B CA  
6866  C  C   . GLY B 238 ? 0.707404  0.438763 0.387124 0.0348634   0.0947319   0.0776038   238  GLY B C   
6867  O  O   . GLY B 238 ? 0.642727  0.405749 0.354396 0.0301823   0.0875589   0.06865     238  GLY B O   
6868  N  N   . ASP B 239 ? 0.762352  0.483431 0.414124 0.0425416   0.0971924   0.083041    239  ASP B N   
6869  C  CA  . ASP B 239 ? 0.739521  0.486274 0.396996 0.0457552   0.0914414   0.078039    239  ASP B CA  
6870  C  C   . ASP B 239 ? 0.68255   0.450074 0.364663 0.0289306   0.101397    0.0711195   239  ASP B C   
6871  O  O   . ASP B 239 ? 0.674569  0.466846 0.368761 0.0298772   0.0963438   0.0648645   239  ASP B O   
6872  C  CB  . ASP B 239 ? 0.842415  0.568721 0.460619 0.0550391   0.0960929   0.0857784   239  ASP B CB  
6873  C  CG  . ASP B 239 ? 0.932859  0.664592 0.534355 0.0751584   0.0794498   0.0861934   239  ASP B CG  
6874  O  OD1 . ASP B 239 ? 0.978529  0.73132  0.600469 0.0820915   0.0638039   0.0801304   239  ASP B OD1 
6875  O  OD2 . ASP B 239 ? 1.00456   0.720628 0.572581 0.0836313   0.0823347   0.0919698   239  ASP B OD2 
6876  N  N   . ARG B 240 ? 0.680762  0.437662 0.368736 0.0135467   0.116535    0.0718426   240  ARG B N   
6877  C  CA  . ARG B 240 ? 0.671984  0.452233 0.384263 -0.00072808 0.125132    0.0642615   240  ARG B CA  
6878  C  C   . ARG B 240 ? 0.614133  0.428755 0.364923 -0.00248752 0.112628    0.0538636   240  ARG B C   
6879  O  O   . ARG B 240 ? 0.577117  0.417516 0.346552 -0.00569808 0.111501    0.0466862   240  ARG B O   
6880  C  CB  . ARG B 240 ? 0.774525  0.536551 0.484961 -0.0173498  0.144297    0.0664924   240  ARG B CB  
6881  C  CG  . ARG B 240 ? 0.831591  0.618381 0.569395 -0.0334764  0.154926    0.0578203   240  ARG B CG  
6882  C  CD  . ARG B 240 ? 0.954135  0.726299 0.695004 -0.0519214  0.173563    0.057972    240  ARG B CD  
6883  N  NE  . ARG B 240 ? 1.00203   0.805028 0.778207 -0.0671787  0.180293    0.0468361   240  ARG B NE  
6884  C  CZ  . ARG B 240 ? 0.935598  0.763464 0.724986 -0.0717107  0.186279    0.0406562   240  ARG B CZ  
6885  N  NH1 . ARG B 240 ? 0.882966  0.708991 0.651865 -0.0630343  0.187753    0.0443372   240  ARG B NH1 
6886  N  NH2 . ARG B 240 ? 0.861041  0.716341 0.684441 -0.0845415  0.190639    0.0300202   240  ARG B NH2 
6887  N  N   . TYR B 241 ? 0.560751  0.3742   0.321948 0.00026921  0.10354     0.0531975   241  TYR B N   
6888  C  CA  . TYR B 241 ? 0.520636  0.362482 0.316714 -0.00378365 0.0947178   0.0440893   241  TYR B CA  
6889  C  C   . TYR B 241 ? 0.477595  0.331628 0.278137 0.00947694  0.0774405   0.0423636   241  TYR B C   
6890  O  O   . TYR B 241 ? 0.483436  0.360551 0.309437 0.00791978  0.069444    0.0353976   241  TYR B O   
6891  C  CB  . TYR B 241 ? 0.528724  0.363316 0.337548 -0.0138916  0.099325    0.0426386   241  TYR B CB  
6892  C  CG  . TYR B 241 ? 0.551056  0.383933 0.36683  -0.0305913  0.115793    0.0402846   241  TYR B CG  
6893  C  CD1 . TYR B 241 ? 0.542373  0.402158 0.379735 -0.0381728  0.119151    0.0326763   241  TYR B CD1 
6894  C  CD2 . TYR B 241 ? 0.625057  0.429064 0.425505 -0.038621   0.12839     0.0452463   241  TYR B CD2 
6895  C  CE1 . TYR B 241 ? 0.59863   0.46057  0.44491  -0.0535039  0.134232    0.0292447   241  TYR B CE1 
6896  C  CE2 . TYR B 241 ? 0.673323  0.476898 0.481861 -0.0556325  0.144336    0.0420317   241  TYR B CE2 
6897  C  CZ  . TYR B 241 ? 0.685691  0.520638 0.518907 -0.0631859  0.146943    0.0334997   241  TYR B CZ  
6898  O  OH  . TYR B 241 ? 0.739823  0.577991 0.583473 -0.0800358  0.162705    0.0291048   241  TYR B OH  
6899  N  N   . ILE B 242 ? 0.489448  0.327143 0.265374 0.0223895   0.0718867   0.048579    242  ILE B N   
6900  C  CA  . ILE B 242 ? 0.47923   0.330621 0.261263 0.0342565   0.0558827   0.0458479   242  ILE B CA  
6901  C  C   . ILE B 242 ? 0.491245  0.342671 0.252782 0.0452687   0.0510379   0.0475784   242  ILE B C   
6902  O  O   . ILE B 242 ? 0.534887  0.363074 0.266253 0.0509144   0.05646     0.055069    242  ILE B O   
6903  C  CB  . ILE B 242 ? 0.509428  0.346838 0.286306 0.0413137   0.050492    0.0492521   242  ILE B CB  
6904  C  CG1 . ILE B 242 ? 0.486598  0.321842 0.281855 0.0300674   0.0556588   0.04693     242  ILE B CG1 
6905  C  CG2 . ILE B 242 ? 0.48528   0.339242 0.26855  0.0538596   0.0346015   0.0458005   242  ILE B CG2 
6906  C  CD1 . ILE B 242 ? 0.459357  0.323426 0.287303 0.0243565   0.0489816   0.0381752   242  ILE B CD1 
6907  N  N   . ASN B 243 ? 0.437799  0.314059 0.214883 0.0475759   0.0416049   0.0403881   243  ASN B N   
6908  C  CA  . ASN B 243 ? 0.440474  0.321747 0.202577 0.057795    0.0344232   0.0392723   243  ASN B CA  
6909  C  C   . ASN B 243 ? 0.423349  0.313226 0.188593 0.069479    0.0191097   0.0370095   243  ASN B C   
6910  O  O   . ASN B 243 ? 0.402984  0.312932 0.193766 0.0669835   0.0115566   0.0303531   243  ASN B O   
6911  C  CB  . ASN B 243 ? 0.431267  0.333001 0.208286 0.0518113   0.0350476   0.0317531   243  ASN B CB  
6912  C  CG  . ASN B 243 ? 0.443345  0.349237 0.203643 0.0611102   0.0287673   0.0295238   243  ASN B CG  
6913  O  OD1 . ASN B 243 ? 0.453907  0.353373 0.196359 0.072885    0.020552    0.0319947   243  ASN B OD1 
6914  N  ND2 . ASN B 243 ? 0.456388  0.374156 0.222565 0.0568879   0.0315632   0.0239107   243  ASN B ND2 
6915  N  N   . LEU B 244 ? 0.444634  0.31958  0.183405 0.0826443   0.0147474   0.0423712   244  LEU B N   
6916  C  CA  . LEU B 244 ? 0.444824  0.32985  0.186257 0.0950128   0.00018544  0.0395399   244  LEU B CA  
6917  C  C   . LEU B 244 ? 0.425502  0.33835  0.182445 0.0968149   -0.0111261  0.0296478   244  LEU B C   
6918  O  O   . LEU B 244 ? 0.416137  0.343884 0.184975 0.103221    -0.0225048  0.0248618   244  LEU B O   
6919  C  CB  . LEU B 244 ? 0.493876  0.356864 0.201489 0.110399    -0.00238134 0.0472037   244  LEU B CB  
6920  C  CG  . LEU B 244 ? 0.520623  0.355558 0.216381 0.110244    0.00611252  0.0559952   244  LEU B CG  
6921  C  CD1 . LEU B 244 ? 0.560605  0.365509 0.214819 0.125104    0.00708213  0.0657726   244  LEU B CD1 
6922  C  CD2 . LEU B 244 ? 0.496592  0.340591 0.215369 0.110289    0.00042597  0.0527321   244  LEU B CD2 
6923  N  N   . ARG B 245 ? 0.423891  0.344134 0.182762 0.0902001   -0.00726046 0.0258403   245  ARG B N   
6924  C  CA  . ARG B 245 ? 0.414637  0.359154 0.18934  0.090165    -0.0171004  0.015653    245  ARG B CA  
6925  C  C   . ARG B 245 ? 0.382057  0.339229 0.182633 0.0765737   -0.0121372  0.0101585   245  ARG B C   
6926  O  O   . ARG B 245 ? 0.38704   0.358767 0.196186 0.0749319   -0.0168546  0.00235275  245  ARG B O   
6927  C  CB  . ARG B 245 ? 0.454426  0.396338 0.204289 0.0982254   -0.0198985  0.0145612   245  ARG B CB  
6928  C  CG  . ARG B 245 ? 0.542555  0.478044 0.269916 0.114559    -0.0296603  0.0175973   245  ARG B CG  
6929  C  CD  . ARG B 245 ? 0.652906  0.583497 0.350663 0.124616    -0.0331334  0.0172887   245  ARG B CD  
6930  N  NE  . ARG B 245 ? 0.725265  0.635702 0.402916 0.119228    -0.0181314  0.0242486   245  ARG B NE  
6931  C  CZ  . ARG B 245 ? 0.854609  0.758542 0.507414 0.123086    -0.0153044  0.0244415   245  ARG B CZ  
6932  N  NH1 . ARG B 245 ? 0.799201  0.713409 0.439776 0.134204    -0.0279278  0.0182175   245  ARG B NH1 
6933  N  NH2 . ARG B 245 ? 0.864829  0.753577 0.506199 0.11512     0.00057633  0.0298958   245  ARG B NH2 
6934  N  N   . GLY B 246 ? 0.34909   0.299305 0.159371 0.0675169   -0.0024736  0.0139443   246  GLY B N   
6935  C  CA  . GLY B 246 ? 0.332106  0.292953 0.163811 0.0564089   0.00247276  0.00932995  246  GLY B CA  
6936  C  C   . GLY B 246 ? 0.306289  0.273076 0.161067 0.0503041   0.0018637   0.00849947  246  GLY B C   
6937  O  O   . GLY B 246 ? 0.299449  0.26202  0.154181 0.0540693   -0.00158907 0.011315    246  GLY B O   
6938  N  N   . PRO B 247 ? 0.298501  0.275161 0.173036 0.0416313   0.00491402  0.00436529  247  PRO B N   
6939  C  CA  . PRO B 247 ? 0.27683   0.258335 0.170677 0.0365836   0.00411246  0.00369977  247  PRO B CA  
6940  C  C   . PRO B 247 ? 0.276888  0.244743 0.166408 0.0332582   0.0118185   0.00956253  247  PRO B C   
6941  O  O   . PRO B 247 ? 0.300412  0.257559 0.177702 0.0309387   0.0204691   0.013056    247  PRO B O   
6942  C  CB  . PRO B 247 ? 0.263495  0.255729 0.17372  0.0297801   0.00639678  -0.00136459 247  PRO B CB  
6943  C  CG  . PRO B 247 ? 0.283588  0.279701 0.186418 0.0326754   0.00470924  -0.00514312 247  PRO B CG  
6944  C  CD  . PRO B 247 ? 0.291455  0.274919 0.170042 0.0376302   0.00861353  -9.901e-05  247  PRO B CD  
6945  N  N   . ILE B 248 ? 0.269296  0.237647 0.169404 0.0319441   0.00958036  0.0098905   248  ILE B N   
6946  C  CA  . ILE B 248 ? 0.277783  0.232617 0.174987 0.0281265   0.0163308   0.0141352   248  ILE B CA  
6947  C  C   . ILE B 248 ? 0.275577  0.237325 0.188231 0.0177312   0.02274     0.0109705   248  ILE B C   
6948  O  O   . ILE B 248 ? 0.265154  0.2416   0.194345 0.0156672   0.0185236   0.00609405  248  ILE B O   
6949  C  CB  . ILE B 248 ? 0.257143  0.211948 0.160476 0.0315726   0.0105661   0.0142047   248  ILE B CB  
6950  C  CG1 . ILE B 248 ? 0.268725  0.220356 0.159159 0.0433721   0.00314142  0.0161334   248  ILE B CG1 
6951  C  CG2 . ILE B 248 ? 0.270611  0.211859 0.173442 0.0265414   0.0171459   0.0169101   248  ILE B CG2 
6952  C  CD1 . ILE B 248 ? 0.252074  0.209561 0.152903 0.0470378   -0.0029803  0.0142928   248  ILE B CD1 
6953  N  N   . PRO B 249 ? 0.294479  0.246464 0.202356 0.011087    0.0330044   0.0131579   249  PRO B N   
6954  C  CA  . PRO B 249 ? 0.281061  0.242549 0.206137 0.00139601  0.0383569   0.00883198  249  PRO B CA  
6955  C  C   . PRO B 249 ? 0.254969  0.223288 0.196046 -0.0005777  0.0330939   0.00575595  249  PRO B C   
6956  O  O   . PRO B 249 ? 0.265517  0.223375 0.201387 0.00172189  0.031188    0.00839654  249  PRO B O   
6957  C  CB  . PRO B 249 ? 0.293711  0.240042 0.208107 -0.00530677 0.0504303   0.0122171   249  PRO B CB  
6958  C  CG  . PRO B 249 ? 0.315834  0.248785 0.206144 0.00149292  0.0523392   0.0178406   249  PRO B CG  
6959  C  CD  . PRO B 249 ? 0.316688  0.247914 0.201938 0.0122199   0.0406185   0.0195494   249  PRO B CD  
6960  N  N   . ALA B 250 ? 0.228168  0.213372 0.186849 -0.00340094 0.0303947   0.00020557  250  ALA B N   
6961  C  CA  . ALA B 250 ? 0.218828  0.212305 0.190049 -0.00251183 0.0232862   -0.00266371 250  ALA B CA  
6962  C  C   . ALA B 250 ? 0.224813  0.213556 0.200872 -0.00788442 0.0257228   -0.00356379 250  ALA B C   
6963  O  O   . ALA B 250 ? 0.240263  0.233429 0.223703 -0.00674726 0.0203081   -0.00548819 250  ALA B O   
6964  C  CB  . ALA B 250 ? 0.195563  0.205092 0.180192 -0.00285736 0.0203756   -0.00765873 250  ALA B CB  
6965  N  N   . HIS B 251 ? 0.232435  0.210917 0.203096 -0.0139295  0.0341818   -0.00235832 251  HIS B N   
6966  C  CA  . HIS B 251 ? 0.24042   0.214632 0.216802 -0.0210309  0.037475    -0.00491833 251  HIS B CA  
6967  C  C   . HIS B 251 ? 0.250507  0.202649 0.211992 -0.0192233  0.0394089   -0.00010708 251  HIS B C   
6968  O  O   . HIS B 251 ? 0.2623    0.207456 0.226251 -0.0248918  0.0422654   -0.00231121 251  HIS B O   
6969  C  CB  . HIS B 251 ? 0.249531  0.228845 0.233735 -0.0313277  0.046462    -0.00893511 251  HIS B CB  
6970  C  CG  . HIS B 251 ? 0.277495  0.24244  0.247325 -0.0347234  0.0568501   -0.00446093 251  HIS B CG  
6971  N  ND1 . HIS B 251 ? 0.289162  0.249881 0.24551  -0.027883   0.0568184   0.00044216  251  HIS B ND1 
6972  C  CD2 . HIS B 251 ? 0.307384  0.259953 0.272377 -0.0440632  0.0677902   -0.00403592 251  HIS B CD2 
6973  C  CE1 . HIS B 251 ? 0.322019  0.268389 0.264707 -0.0322726  0.06748     0.00415922  251  HIS B CE1 
6974  N  NE2 . HIS B 251 ? 0.345826  0.28705  0.294141 -0.0428785  0.0750888   0.0015566   251  HIS B NE2 
6975  N  N   . LEU B 252 ? 0.258817  0.200383 0.205056 -0.0106     0.0371062   0.00566162  252  LEU B N   
6976  C  CA  . LEU B 252 ? 0.274855  0.1927   0.203391 -0.00728023 0.0400896   0.0109793   252  LEU B CA  
6977  C  C   . LEU B 252 ? 0.278925  0.195372 0.206357 0.00170448  0.0318523   0.0115442   252  LEU B C   
6978  O  O   . LEU B 252 ? 0.302823  0.200522 0.215373 0.00738224  0.0327154   0.0157388   252  LEU B O   
6979  C  CB  . LEU B 252 ? 0.296908  0.203678 0.206558 -0.0022274  0.0433505   0.0170479   252  LEU B CB  
6980  C  CG  . LEU B 252 ? 0.309265  0.212553 0.21517  -0.0110266  0.0542957   0.0176032   252  LEU B CG  
6981  C  CD1 . LEU B 252 ? 0.332387  0.220166 0.213814 -0.0041199  0.0574249   0.0247323   252  LEU B CD1 
6982  C  CD2 . LEU B 252 ? 0.323334  0.212903 0.229722 -0.0222585  0.0642161   0.0165717   252  LEU B CD2 
6983  N  N   . LEU B 253 ? 0.281341  0.216383 0.223827 0.00315435  0.0245727   0.00723015  253  LEU B N   
6984  C  CA  . LEU B 253 ? 0.275043  0.212512 0.217327 0.0119265   0.0173479   0.00749156  253  LEU B CA  
6985  C  C   . LEU B 253 ? 0.282288  0.220588 0.232931 0.0093195   0.0162659   0.00361581  253  LEU B C   
6986  O  O   . LEU B 253 ? 0.284698  0.227707 0.237925 0.0153279   0.011184    0.00264133  253  LEU B O   
6987  C  CB  . LEU B 253 ? 0.270919  0.226406 0.220421 0.0160625   0.0108287   0.00612741  253  LEU B CB  
6988  C  CG  . LEU B 253 ? 0.287029  0.240368 0.225312 0.0209934   0.0104197   0.00940846  253  LEU B CG  
6989  C  CD1 . LEU B 253 ? 0.254324  0.225096 0.20202  0.0204627   0.00636816  0.00627249  253  LEU B CD1 
6990  C  CD2 . LEU B 253 ? 0.295327  0.241069 0.221357 0.0320955   0.00606898  0.0125179   253  LEU B CD2 
6991  N  N   . GLY B 254 ? 0.262925  0.19796  0.218175 0.00016961  0.0211849   0.00061051  254  GLY B N   
6992  C  CA  . GLY B 254 ? 0.283432  0.213225 0.241517 -0.00220351 0.0212414   -0.00303368 254  GLY B CA  
6993  C  C   . GLY B 254 ? 0.26875   0.217059 0.242086 -0.00592457 0.017081    -0.00896488 254  GLY B C   
6994  O  O   . GLY B 254 ? 0.289297  0.235846 0.265302 -0.00787399 0.016334    -0.0129704  254  GLY B O   
6995  N  N   . ASP B 255 ? 0.246601  0.210864 0.228073 -0.00651097 0.0146006   -0.00959705 255  ASP B N   
6996  C  CA  . ASP B 255 ? 0.250573  0.230865 0.243191 -0.00717474 0.00975639  -0.0137976  255  ASP B CA  
6997  C  C   . ASP B 255 ? 0.229167  0.221725 0.229518 -0.010514   0.0102212   -0.0153054  255  ASP B C   
6998  O  O   . ASP B 255 ? 0.230095  0.221852 0.226843 -0.00926872 0.012193    -0.0121594  255  ASP B O   
6999  C  CB  . ASP B 255 ? 0.273472  0.258328 0.264873 0.00034903  0.00477769  -0.0117205  255  ASP B CB  
7000  C  CG  . ASP B 255 ? 0.307392  0.305579 0.306312 0.00096481  0.00041943  -0.0140954  255  ASP B CG  
7001  O  OD1 . ASP B 255 ? 0.284494  0.290644 0.286829 0.0014795   -0.00103951 -0.013435   255  ASP B OD1 
7002  O  OD2 . ASP B 255 ? 0.377718  0.376253 0.377012 0.00166193  -0.0012411  -0.0163457  255  ASP B OD2 
7003  N  N   . MET B 256 ? 0.207934  0.212333 0.218256 -0.0136575  0.00799152  -0.0205402  256  MET B N   
7004  C  CA  . MET B 256 ? 0.201888  0.219382 0.220798 -0.015654   0.008185    -0.0230938  256  MET B CA  
7005  C  C   . MET B 256 ? 0.203245  0.224802 0.220186 -0.00982262 0.00567943  -0.0196213  256  MET B C   
7006  O  O   . MET B 256 ? 0.222983  0.250484 0.243041 -0.0106479  0.00782633  -0.0202504  256  MET B O   
7007  C  CB  . MET B 256 ? 0.213355  0.243933 0.242157 -0.0167437  0.0038147   -0.0294337  256  MET B CB  
7008  C  CG  . MET B 256 ? 0.239612  0.28588  0.278911 -0.017477   0.00339079  -0.033435   256  MET B CG  
7009  S  SD  . MET B 256 ? 0.220134  0.267364 0.264824 -0.0269335  0.0128732   -0.0359607  256  MET B SD  
7010  C  CE  . MET B 256 ? 0.235701  0.2885   0.289713 -0.0345309  0.0122288   -0.0446008  256  MET B CE  
7011  N  N   . TRP B 257 ? 0.178874  0.198003 0.191444 -0.00454237 0.00163199  -0.0169193  257  TRP B N   
7012  C  CA  . TRP B 257 ? 0.187099  0.210029 0.198845 -0.00029456 -0.00095305 -0.0150207  257  TRP B CA  
7013  C  C   . TRP B 257 ? 0.175136  0.191128 0.179191 0.00245466  -0.00023292 -0.0111276  257  TRP B C   
7014  O  O   . TRP B 257 ? 0.179644  0.198402 0.182921 0.00524805  -0.00244791 -0.0103506  257  TRP B O   
7015  C  CB  . TRP B 257 ? 0.185647  0.212523 0.199014 0.00275817  -0.00558443 -0.0157013  257  TRP B CB  
7016  C  CG  . TRP B 257 ? 0.180656  0.214728 0.19974  0.00199684  -0.00750848 -0.0196782  257  TRP B CG  
7017  C  CD1 . TRP B 257 ? 0.199213  0.241501 0.223679 0.00304112  -0.00856018 -0.022275   257  TRP B CD1 
7018  C  CD2 . TRP B 257 ? 0.191738  0.226413 0.212102 0.00019611  -0.00860436 -0.0226251  257  TRP B CD2 
7019  N  NE1 . TRP B 257 ? 0.194693  0.244414 0.224434 0.0026335   -0.011075   -0.0267651  257  TRP B NE1 
7020  C  CE2 . TRP B 257 ? 0.190876  0.235934 0.217936 0.00042347  -0.0112241  -0.0272256  257  TRP B CE2 
7021  C  CE3 . TRP B 257 ? 0.20031   0.228212 0.216603 -0.00078878 -0.0080346  -0.0224752  257  TRP B CE3 
7022  C  CZ2 . TRP B 257 ? 0.202185  0.251698 0.232049 -0.00103701 -0.0136788  -0.0320203  257  TRP B CZ2 
7023  C  CZ3 . TRP B 257 ? 0.232952  0.263236 0.251095 -0.00260593 -0.00973488 -0.0270391  257  TRP B CZ3 
7024  C  CH2 . TRP B 257 ? 0.213048  0.254546 0.238105 -0.00309569 -0.0127253  -0.0319396  257  TRP B CH2 
7025  N  N   . ALA B 258 ? 0.181256  0.187909 0.179342 0.00204416  0.00241563  -0.00927036 258  ALA B N   
7026  C  CA  . ALA B 258 ? 0.213141  0.213404 0.202776 0.00672387  0.00191353  -0.00581948 258  ALA B CA  
7027  C  C   . ALA B 258 ? 0.201193  0.206901 0.193402 0.0107457   -0.00269152 -0.0062286  258  ALA B C   
7028  O  O   . ALA B 258 ? 0.215941  0.223324 0.205324 0.0147654   -0.00487286 -0.0052042  258  ALA B O   
7029  C  CB  . ALA B 258 ? 0.198293  0.197902 0.182377 0.00788743  0.00339123  -0.00405803 258  ALA B CB  
7030  N  N   . GLN B 259 ? 0.18934   0.198186 0.186496 0.00959532  -0.00389351 -0.00815863 259  GLN B N   
7031  C  CA  . GLN B 259 ? 0.209428  0.224398 0.209517 0.0118698   -0.00663944 -0.00870896 259  GLN B CA  
7032  C  C   . GLN B 259 ? 0.248977  0.261872 0.247018 0.0157039   -0.00691495 -0.0084544  259  GLN B C   
7033  O  O   . GLN B 259 ? 0.306917  0.326361 0.307876 0.0179737   -0.00847312 -0.00920989 259  GLN B O   
7034  C  CB  . GLN B 259 ? 0.210741  0.229409 0.21475  0.0095718   -0.00737053 -0.0104122  259  GLN B CB  
7035  C  CG  . GLN B 259 ? 0.25868   0.274268 0.261843 0.0088391   -0.00675246 -0.0118511  259  GLN B CG  
7036  C  CD  . GLN B 259 ? 0.335966  0.355008 0.340334 0.00803179  -0.00831162 -0.0133666  259  GLN B CD  
7037  O  OE1 . GLN B 259 ? 0.3115    0.333476 0.317915 0.00717     -0.0094993  -0.0141712  259  GLN B OE1 
7038  N  NE2 . GLN B 259 ? 0.355059  0.373628 0.357092 0.00923281  -0.00825532 -0.0138056  259  GLN B NE2 
7039  N  N   . SER B 260 ? 0.247341  0.251467 0.241057 0.0161867   -0.00503481 -0.00812561 260  SER B N   
7040  C  CA  . SER B 260 ? 0.314042  0.314544 0.304149 0.0219019   -0.00538671 -0.00770567 260  SER B CA  
7041  C  C   . SER B 260 ? 0.301322  0.28679  0.28213  0.023118    -0.00278068 -0.0055813  260  SER B C   
7042  O  O   . SER B 260 ? 0.299413  0.278606 0.279206 0.0173228   0.00021016  -0.00589296 260  SER B O   
7043  C  CB  . SER B 260 ? 0.387755  0.391349 0.380911 0.0226892   -0.00528897 -0.0101593  260  SER B CB  
7044  O  OG  . SER B 260 ? 0.367806  0.363971 0.358835 0.0190193   -0.00345451 -0.0116298  260  SER B OG  
7045  N  N   . TRP B 261 ? 0.240192  0.220522 0.214339 0.0306827   -0.00386402 -0.003707   261  TRP B N   
7046  C  CA  . TRP B 261 ? 0.255025  0.21814  0.216544 0.0327458   -0.00106579 -0.00014346 261  TRP B CA  
7047  C  C   . TRP B 261 ? 0.261724  0.21062  0.21592  0.0376234   0.00045074  -0.00011228 261  TRP B C   
7048  O  O   . TRP B 261 ? 0.276629  0.208555 0.217551 0.0423871   0.00231811  0.00343159  261  TRP B O   
7049  C  CB  . TRP B 261 ? 0.238451  0.202932 0.193211 0.0395475   -0.00391246 0.00276566  261  TRP B CB  
7050  C  CG  . TRP B 261 ? 0.224876  0.201602 0.185342 0.0354419   -0.00536929 0.0020853   261  TRP B CG  
7051  C  CD1 . TRP B 261 ? 0.216705  0.200987 0.186009 0.0272923   -0.00399435 8.89e-05    261  TRP B CD1 
7052  C  CD2 . TRP B 261 ? 0.237936  0.219274 0.193565 0.0405671   -0.00880344 0.00315414  261  TRP B CD2 
7053  N  NE1 . TRP B 261 ? 0.205174  0.197595 0.175784 0.0269965   -0.00591638 -0.00018425 261  TRP B NE1 
7054  C  CE2 . TRP B 261 ? 0.220396  0.211219 0.182635 0.0344562   -0.00878381 0.00143953  261  TRP B CE2 
7055  C  CE3 . TRP B 261 ? 0.260153  0.238555 0.205746 0.0508166   -0.0125288  0.00490047  261  TRP B CE3 
7056  C  CZ2 . TRP B 261 ? 0.228786  0.225583 0.187942 0.0370415   -0.0118087  0.00101071  261  TRP B CZ2 
7057  C  CZ3 . TRP B 261 ? 0.279773  0.26609  0.22263  0.0537713   -0.0164092  0.00434453  261  TRP B CZ3 
7058  C  CH2 . TRP B 261 ? 0.246973  0.241712 0.196332 0.0463672   -0.0156886  0.00231778  261  TRP B CH2 
7059  N  N   . GLU B 262 ? 0.255157  0.20939  0.216    0.0375409   -0.00019932 -0.00389585 262  GLU B N   
7060  C  CA  . GLU B 262 ? 0.287169  0.227316 0.240144 0.0438413   0.00107338  -0.00440957 262  GLU B CA  
7061  C  C   . GLU B 262 ? 0.298797  0.215302 0.240719 0.039247    0.0064756   -0.00303714 262  GLU B C   
7062  O  O   . GLU B 262 ? 0.307654  0.205491 0.237783 0.0455818   0.00823226  -0.00162207 262  GLU B O   
7063  C  CB  . GLU B 262 ? 0.326398  0.274161 0.286624 0.0436548   0.00072253  -0.0093223  262  GLU B CB  
7064  C  CG  . GLU B 262 ? 0.408728  0.358712 0.374244 0.0330539   0.00250963  -0.0124095  262  GLU B CG  
7065  C  CD  . GLU B 262 ? 0.524779  0.493047 0.500657 0.0276063   0.0003799   -0.0129766  262  GLU B CD  
7066  O  OE1 . GLU B 262 ? 0.407124  0.38654  0.387327 0.0288589   -0.00185539 -0.0108653  262  GLU B OE1 
7067  O  OE2 . GLU B 262 ? 0.525359  0.495556 0.504146 0.0219292   0.00084212  -0.0162541  262  GLU B OE2 
7068  N  N   . ASN B 263 ? 0.284493  0.201138 0.23032  0.0280462   0.00956375  -0.00404603 263  ASN B N   
7069  C  CA  . ASN B 263 ? 0.344054  0.239903 0.281601 0.0215179   0.0157155   -0.00402094 263  ASN B CA  
7070  C  C   . ASN B 263 ? 0.376229  0.252187 0.297962 0.0246514   0.0196845   0.00225414  263  ASN B C   
7071  O  O   . ASN B 263 ? 0.389701  0.243207 0.301328 0.0203703   0.0258988   0.00284961  263  ASN B O   
7072  C  CB  . ASN B 263 ? 0.347767  0.250902 0.294974 0.00861427  0.0183263   -0.00782864 263  ASN B CB  
7073  C  CG  . ASN B 263 ? 0.377846  0.294023 0.335601 0.00613566  0.0149327   -0.0141057  263  ASN B CG  
7074  O  OD1 . ASN B 263 ? 0.407625  0.342537 0.376088 0.00325252  0.0117079   -0.0160986  263  ASN B OD1 
7075  N  ND2 . ASN B 263 ? 0.336826  0.241683 0.289763 0.00807273  0.0156852   -0.0171809  263  ASN B ND2 
7076  N  N   . ILE B 264 ? 0.362103  0.244214 0.279898 0.0321802   0.0164127   0.00670904  264  ILE B N   
7077  C  CA  . ILE B 264 ? 0.383594  0.244089 0.282326 0.0367981   0.0200674   0.0131402   264  ILE B CA  
7078  C  C   . ILE B 264 ? 0.410186  0.262639 0.297611 0.0525431   0.0155137   0.0157995   264  ILE B C   
7079  O  O   . ILE B 264 ? 0.437104  0.275224 0.30747  0.0603085   0.0159385   0.0216181   264  ILE B O   
7080  C  CB  . ILE B 264 ? 0.409469  0.278742 0.307335 0.0346662   0.0202541   0.0162916   264  ILE B CB  
7081  C  CG1 . ILE B 264 ? 0.374588  0.26847  0.282452 0.041154    0.0119142   0.0148432   264  ILE B CG1 
7082  C  CG2 . ILE B 264 ? 0.392336  0.266273 0.299177 0.0200439   0.026212    0.0138224   264  ILE B CG2 
7083  C  CD1 . ILE B 264 ? 0.430999  0.330319 0.334576 0.0409473   0.0117297   0.0176481   264  ILE B CD1 
7084  N  N   . TYR B 265 ? 0.375269  0.236768 0.271105 0.0580079   0.0113358   0.0114203   265  TYR B N   
7085  C  CA  . TYR B 265 ? 0.398767  0.25477  0.285977 0.0740312   0.00699343  0.0125448   265  TYR B CA  
7086  C  C   . TYR B 265 ? 0.4418    0.262521 0.304542 0.0804022   0.0116549   0.0181886   265  TYR B C   
7087  O  O   . TYR B 265 ? 0.4587    0.27122  0.307191 0.0949403   0.00800578  0.0224908   265  TYR B O   
7088  C  CB  . TYR B 265 ? 0.380824  0.248751 0.280571 0.07608     0.00474242  0.00612954  265  TYR B CB  
7089  C  CG  . TYR B 265 ? 0.412857  0.275488 0.305045 0.0930477   0.00103018  0.00605757  265  TYR B CG  
7090  C  CD1 . TYR B 265 ? 0.394134  0.27657  0.291192 0.104742    -0.00615641 0.0057517   265  TYR B CD1 
7091  C  CD2 . TYR B 265 ? 0.46173   0.3011   0.343238 0.0974873   0.00447965  0.00507602  265  TYR B CD2 
7092  C  CE1 . TYR B 265 ? 0.41782   0.299083 0.310071 0.121402    -0.0101953  0.00458331  265  TYR B CE1 
7093  C  CE2 . TYR B 265 ? 0.47419   0.308967 0.348831 0.114715    0.00091184  0.00453715  265  TYR B CE2 
7094  C  CZ  . TYR B 265 ? 0.458059  0.315309 0.338911 0.127       -0.00662128 0.00419385  265  TYR B CZ  
7095  O  OH  . TYR B 265 ? 0.516007  0.371693 0.391641 0.145054    -0.0107112  0.00281301  265  TYR B OH  
7096  N  N   . ASP B 266 ? 0.461735  0.260388 0.318515 0.0703139   0.0195612   0.0178161   266  ASP B N   
7097  C  CA  . ASP B 266 ? 0.561333  0.322264 0.393379 0.0752584   0.0254003   0.0231493   266  ASP B CA  
7098  C  C   . ASP B 266 ? 0.602227  0.35024  0.415753 0.079317    0.0271802   0.031616    266  ASP B C   
7099  O  O   . ASP B 266 ? 0.587297  0.306444 0.376416 0.0904293   0.0289877   0.0378231   266  ASP B O   
7100  C  CB  . ASP B 266 ? 0.625489  0.365926 0.456183 0.061085    0.0342981   0.0199067   266  ASP B CB  
7101  C  CG  . ASP B 266 ? 0.697547  0.445302 0.538441 0.0419226   0.0403694   0.0181944   266  ASP B CG  
7102  O  OD1 . ASP B 266 ? 0.710011  0.482005 0.561737 0.0392688   0.0371956   0.0189045   266  ASP B OD1 
7103  O  OD2 . ASP B 266 ? 0.744943  0.47509  0.583805 0.0295194   0.0482885   0.0153249   266  ASP B OD2 
7104  N  N   . MET B 267 ? 0.560812  0.329073 0.383834 0.0717392   0.0264783   0.0320415   267  MET B N   
7105  C  CA  . MET B 267 ? 0.597583  0.353673 0.402103 0.0747272   0.028944    0.0394947   267  MET B CA  
7106  C  C   . MET B 267 ? 0.606068  0.376444 0.40624  0.0919034   0.0185169   0.0414486   267  MET B C   
7107  O  O   . MET B 267 ? 0.661454  0.418228 0.440895 0.0989703   0.0190272   0.0480587   267  MET B O   
7108  C  CB  . MET B 267 ? 0.619696  0.389874 0.434453 0.0596824   0.0334635   0.0387296   267  MET B CB  
7109  C  CG  . MET B 267 ? 0.7129    0.463166 0.523973 0.0434512   0.045869    0.0389903   267  MET B CG  
7110  S  SD  . MET B 267 ? 0.917331  0.68569  0.736519 0.031424    0.0501614   0.0392033   267  MET B SD  
7111  C  CE  . MET B 267 ? 0.653153  0.462774 0.506957 0.0242634   0.042658    0.0295246   267  MET B CE  
7112  N  N   . VAL B 268 ? 0.536634  0.334897 0.355796 0.0982164   0.0093915   0.0353628   268  VAL B N   
7113  C  CA  . VAL B 268 ? 0.541738  0.359959 0.361664 0.111725    -0.00071323 0.0351766   268  VAL B CA  
7114  C  C   . VAL B 268 ? 0.575383  0.39819  0.395836 0.128747    -0.0082576  0.0325545   268  VAL B C   
7115  O  O   . VAL B 268 ? 0.566554  0.408343 0.389466 0.141143    -0.0175056  0.0309023   268  VAL B O   
7116  C  CB  . VAL B 268 ? 0.517593  0.371012 0.360549 0.10369     -0.00527982 0.0298912   268  VAL B CB  
7117  C  CG1 . VAL B 268 ? 0.51382   0.364626 0.359169 0.0870602   0.00245971  0.0311821   268  VAL B CG1 
7118  C  CG2 . VAL B 268 ? 0.492481  0.371451 0.360879 0.100577    -0.00902277 0.0220716   268  VAL B CG2 
7119  N  N   . VAL B 269 ? 0.576486  0.384075 0.396095 0.12903     -0.0044229  0.0310409   269  VAL B N   
7120  C  CA  . VAL B 269 ? 0.635306  0.449455 0.458483 0.144448    -0.010576   0.0271526   269  VAL B CA  
7121  C  C   . VAL B 269 ? 0.65262   0.460612 0.457395 0.165928    -0.0180746  0.0310894   269  VAL B C   
7122  O  O   . VAL B 269 ? 0.695818  0.470539 0.472809 0.172464    -0.0147044  0.0388916   269  VAL B O   
7123  C  CB  . VAL B 269 ? 0.623845  0.415337 0.443269 0.142059    -0.00412635 0.0255071   269  VAL B CB  
7124  C  CG1 . VAL B 269 ? 0.693196  0.443887 0.489625 0.134717    0.00590212  0.0320281   269  VAL B CG1 
7125  C  CG2 . VAL B 269 ? 0.701797  0.492183 0.518168 0.161238    -0.00939735 0.022727    269  VAL B CG2 
7126  N  N   . PRO B 270 ? 0.652795  0.493225 0.4723   0.177465    -0.0284371  0.0254637   270  PRO B N   
7127  C  CA  . PRO B 270 ? 0.665589  0.50795  0.471006 0.19837     -0.0378251  0.0274333   270  PRO B CA  
7128  C  C   . PRO B 270 ? 0.753671  0.566792 0.533998 0.219336    -0.0395229  0.031782    270  PRO B C   
7129  O  O   . PRO B 270 ? 0.761906  0.563463 0.520045 0.233783    -0.044648   0.0371872   270  PRO B O   
7130  C  CB  . PRO B 270 ? 0.650603  0.53966  0.484752 0.20247     -0.0475494  0.017502    270  PRO B CB  
7131  C  CG  . PRO B 270 ? 0.616328  0.525138 0.475279 0.179694    -0.0421954  0.0130873   270  PRO B CG  
7132  C  CD  . PRO B 270 ? 0.649909  0.529448 0.501344 0.169582    -0.0316185  0.0163824   270  PRO B CD  
7133  N  N   . PHE B 271 ? 0.728383  0.533025 0.512965 0.222759    -0.036537   0.0284815   271  PHE B N   
7134  C  CA  . PHE B 271 ? 0.737659  0.509572 0.498159 0.241561    -0.0364013  0.032187    271  PHE B CA  
7135  C  C   . PHE B 271 ? 0.770793  0.50882  0.523599 0.228377    -0.0240724  0.0341133   271  PHE B C   
7136  O  O   . PHE B 271 ? 0.728207  0.472621 0.495067 0.227372    -0.0224216  0.0274291   271  PHE B O   
7137  C  CB  . PHE B 271 ? 0.708788  0.512371 0.48718  0.259419    -0.0463214  0.023316    271  PHE B CB  
7138  C  CG  . PHE B 271 ? 0.702623  0.542442 0.490922 0.270186    -0.0586583  0.0198518   271  PHE B CG  
7139  C  CD1 . PHE B 271 ? 0.737413  0.563979 0.500298 0.291796    -0.0666641  0.0251306   271  PHE B CD1 
7140  C  CD2 . PHE B 271 ? 0.64408   0.530555 0.466064 0.259354    -0.0624915  0.0107988   271  PHE B CD2 
7141  C  CE1 . PHE B 271 ? 0.737673  0.599225 0.509927 0.301659    -0.0789806  0.0205805   271  PHE B CE1 
7142  C  CE2 . PHE B 271 ? 0.637679  0.557536 0.469536 0.268061    -0.0737791  0.00623385  271  PHE B CE2 
7143  C  CZ  . PHE B 271 ? 0.655035  0.563924 0.462791 0.289197    -0.08255    0.0105924   271  PHE B CZ  
7144  N  N   . PRO B 272 ? 0.859398  0.563554 0.591634 0.216092    -0.0147176  0.0422754   272  PRO B N   
7145  C  CA  . PRO B 272 ? 0.898509  0.576596 0.628691 0.197096    -0.00228715 0.0425582   272  PRO B CA  
7146  C  C   . PRO B 272 ? 0.995645  0.640632 0.715391 0.197661    0.00480893  0.0411212   272  PRO B C   
7147  O  O   . PRO B 272 ? 1.00352   0.641597 0.731679 0.178546    0.0131273   0.0378355   272  PRO B O   
7148  C  CB  . PRO B 272 ? 0.906992  0.560776 0.617478 0.185734    0.00540532  0.0514934   272  PRO B CB  
7149  C  CG  . PRO B 272 ? 0.958815  0.605683 0.646344 0.206656    -0.00202359 0.0583986   272  PRO B CG  
7150  C  CD  . PRO B 272 ? 0.889719  0.585077 0.603036 0.217572    -0.0155939  0.0503805   272  PRO B CD  
7151  N  N   . ASP B 273 ? 1.05584   0.679101 0.755943 0.220073    0.00133993  0.0432772   273  ASP B N   
7152  C  CA  . ASP B 273 ? 1.13619   0.72128  0.820277 0.224531    0.00775853  0.0426923   273  ASP B CA  
7153  C  C   . ASP B 273 ? 1.13063   0.740234 0.838075 0.228884    0.00405901  0.0315618   273  ASP B C   
7154  O  O   . ASP B 273 ? 1.13206   0.713762 0.830409 0.229617    0.00981372  0.0288449   273  ASP B O   
7155  C  CB  . ASP B 273 ? 1.22918   0.785627 0.882776 0.252238    0.00304664  0.0492504   273  ASP B CB  
7156  C  CG  . ASP B 273 ? 1.21277   0.811551 0.881024 0.272747    -0.0115908  0.0453628   273  ASP B CG  
7157  O  OD1 . ASP B 273 ? 1.2293    0.861858 0.912668 0.266241    -0.0167328  0.0451527   273  ASP B OD1 
7158  O  OD2 . ASP B 273 ? 1.223     0.82457  0.891356 0.293259    -0.0174577  0.0408818   273  ASP B OD2 
7159  N  N   . LYS B 274 ? 0.9893    0.64898  0.724773 0.232701    -0.00509343 0.0250512   274  LYS B N   
7160  C  CA  . LYS B 274 ? 0.890143  0.577394 0.647589 0.239213    -0.00882738 0.0147452   274  LYS B CA  
7161  C  C   . LYS B 274 ? 0.895027  0.582884 0.666402 0.217017    -0.00068549 0.00895048  274  LYS B C   
7162  O  O   . LYS B 274 ? 0.973793  0.646025 0.740501 0.198005    0.00618084  0.012507    274  LYS B O   
7163  C  CB  . LYS B 274 ? 0.819117  0.560008 0.604382 0.242738    -0.0182891  0.00942004  274  LYS B CB  
7164  C  CG  . LYS B 274 ? 0.865607  0.618812 0.644428 0.264028    -0.0287224  0.0121128   274  LYS B CG  
7165  C  CD  . LYS B 274 ? 0.933207  0.689664 0.710364 0.289636    -0.0346142  0.00707462  274  LYS B CD  
7166  C  CE  . LYS B 274 ? 0.932306  0.734473 0.728473 0.302359    -0.0463019  0.00205816  274  LYS B CE  
7167  N  NZ  . LYS B 274 ? 0.987797  0.806644 0.793119 0.323824    -0.051582   -0.00614144 274  LYS B NZ  
7168  N  N   . PRO B 275 ? 0.899463  0.607023 0.688542 0.218378    -0.00116578 -0.00054393 275  PRO B N   
7169  C  CA  . PRO B 275 ? 0.873493  0.580899 0.673325 0.19827     0.00580621  -0.0063579  275  PRO B CA  
7170  C  C   . PRO B 275 ? 0.80998   0.540936 0.626209 0.177042    0.00654863  -0.00517477 275  PRO B C   
7171  O  O   . PRO B 275 ? 0.759148  0.521577 0.588973 0.178583    0.00062294  -0.00412392 275  PRO B O   
7172  C  CB  . PRO B 275 ? 0.882872  0.617082 0.70047  0.206522    0.00335564  -0.0163489  275  PRO B CB  
7173  C  CG  . PRO B 275 ? 0.94852   0.682026 0.757711 0.233673    -0.00302758 -0.0156645  275  PRO B CG  
7174  C  CD  . PRO B 275 ? 0.929303  0.662022 0.729142 0.239157    -0.00828435 -0.00671086 275  PRO B CD  
7175  N  N   . ASN B 276 ? 0.76458   0.479181 0.578935 0.157754    0.0137486   -0.00593202 276  ASN B N   
7176  C  CA  . ASN B 276 ? 0.754935  0.488807 0.583935 0.137713    0.015088    -0.00569617 276  ASN B CA  
7177  C  C   . ASN B 276 ? 0.69189   0.465756 0.546284 0.13329     0.0116274   -0.0131829  276  ASN B C   
7178  O  O   . ASN B 276 ? 0.660761  0.434529 0.519651 0.129707    0.0141034   -0.020123   276  ASN B O   
7179  C  CB  . ASN B 276 ? 0.780385  0.484598 0.599646 0.120614    0.0235954   -0.00571115 276  ASN B CB  
7180  C  CG  . ASN B 276 ? 0.794262  0.517446 0.62831  0.100707    0.0250849   -0.00607732 276  ASN B CG  
7181  O  OD1 . ASN B 276 ? 0.76379   0.515032 0.610058 0.10029     0.0203847   -0.00376256 276  ASN B OD1 
7182  N  ND2 . ASN B 276 ? 0.839738  0.548328 0.673169 0.0844019   0.0313931   -0.00969558 276  ASN B ND2 
7183  N  N   . LEU B 277 ? 0.636619  0.442915 0.505969 0.133371    0.00636327  -0.0118637  277  LEU B N   
7184  C  CA  . LEU B 277 ? 0.607308  0.450029 0.499001 0.129612    0.00386943  -0.0179442  277  LEU B CA  
7185  C  C   . LEU B 277 ? 0.59141   0.441195 0.492331 0.109947    0.00707724  -0.0198824  277  LEU B C   
7186  O  O   . LEU B 277 ? 0.639271  0.514541 0.555548 0.105129    0.00614369  -0.0242743  277  LEU B O   
7187  C  CB  . LEU B 277 ? 0.566347  0.440335 0.471013 0.136232    -0.00247539 -0.0169474  277  LEU B CB  
7188  C  CG  . LEU B 277 ? 0.634829  0.513889 0.536755 0.157358    -0.0075475  -0.0178664  277  LEU B CG  
7189  C  CD1 . LEU B 277 ? 0.580263  0.491882 0.4966   0.160389    -0.0140122  -0.0179123  277  LEU B CD1 
7190  C  CD2 . LEU B 277 ? 0.605979  0.490345 0.512861 0.166601    -0.00619622 -0.0252907  277  LEU B CD2 
7191  N  N   . ASP B 278 ? 0.594876  0.423515 0.486607 0.0988615   0.01088     -0.0165478  278  ASP B N   
7192  C  CA  . ASP B 278 ? 0.591233  0.425725 0.491401 0.0817631   0.0134952   -0.0199541  278  ASP B CA  
7193  C  C   . ASP B 278 ? 0.593964  0.406958 0.486139 0.079132    0.0176852   -0.0257238  278  ASP B C   
7194  O  O   . ASP B 278 ? 0.65908   0.441207 0.535936 0.0788501   0.0218303   -0.0238501  278  ASP B O   
7195  C  CB  . ASP B 278 ? 0.651627  0.482927 0.551399 0.0697162   0.0152397   -0.0152544  278  ASP B CB  
7196  C  CG  . ASP B 278 ? 0.748369  0.578664 0.653622 0.0528754   0.0185998   -0.0194426  278  ASP B CG  
7197  O  OD1 . ASP B 278 ? 0.70879   0.548077 0.621038 0.0492469   0.0179651   -0.0262029  278  ASP B OD1 
7198  O  OD2 . ASP B 278 ? 0.800997  0.621161 0.702795 0.0436416   0.0220681   -0.0165129  278  ASP B OD2 
7199  N  N   . VAL B 279 ? 0.516812  0.345153 0.418097 0.0770935   0.0169595   -0.0327237  279  VAL B N   
7200  C  CA  . VAL B 279 ? 0.485513  0.297423 0.379613 0.0775425   0.0198704   -0.0398179  279  VAL B CA  
7201  C  C   . VAL B 279 ? 0.459566  0.265125 0.354836 0.0606681   0.0222405   -0.0444487  279  VAL B C   
7202  O  O   . VAL B 279 ? 0.460912  0.256477 0.352174 0.0575823   0.0240117   -0.0519842  279  VAL B O   
7203  C  CB  . VAL B 279 ? 0.484145  0.316048 0.3854   0.0866622   0.0181383   -0.045124   279  VAL B CB  
7204  C  CG1 . VAL B 279 ? 0.51577   0.356484 0.418237 0.103391    0.0156535   -0.0419692  279  VAL B CG1 
7205  C  CG2 . VAL B 279 ? 0.431825  0.292539 0.346987 0.0782178   0.0164451   -0.0477807  279  VAL B CG2 
7206  N  N   . THR B 280 ? 0.459952  0.273253 0.361591 0.0496511   0.021945    -0.0408778  280  THR B N   
7207  C  CA  . THR B 280 ? 0.455259  0.267461 0.360864 0.0341543   0.0234279   -0.0462515  280  THR B CA  
7208  C  C   . THR B 280 ? 0.487887  0.268579 0.381102 0.0300551   0.0285114   -0.0512188  280  THR B C   
7209  O  O   . THR B 280 ? 0.482564  0.262447 0.377011 0.0236885   0.0285088   -0.060112   280  THR B O   
7210  C  CB  . THR B 280 ? 0.472084  0.292765 0.384753 0.0240544   0.0236809   -0.041602   280  THR B CB  
7211  O  OG1 . THR B 280 ? 0.457168  0.306705 0.381684 0.0261854   0.0188863   -0.0387738  280  THR B OG1 
7212  C  CG2 . THR B 280 ? 0.472463  0.291844 0.390086 0.00849982  0.025502    -0.0484331  280  THR B CG2 
7213  N  N   . SER B 281 ? 0.535803  0.288685 0.41563  0.0331188   0.0330955   -0.0456664  281  SER B N   
7214  C  CA  . SER B 281 ? 0.605833  0.325868 0.473645 0.0258405   0.0393126   -0.0505867  281  SER B CA  
7215  C  C   . SER B 281 ? 0.613294  0.321835 0.473943 0.0334881   0.0390353   -0.0584607  281  SER B C   
7216  O  O   . SER B 281 ? 0.611429  0.303825 0.468392 0.023671    0.0422616   -0.0669808  281  SER B O   
7217  C  CB  . SER B 281 ? 0.668715  0.356386 0.520284 0.0265879   0.0457295   -0.0427078  281  SER B CB  
7218  O  OG  . SER B 281 ? 0.714919  0.393035 0.554712 0.0459057   0.04382     -0.03626    281  SER B OG  
7219  N  N   . THR B 282 ? 0.58149   0.299705 0.441073 0.050482    0.0353921   -0.0566148  282  THR B N   
7220  C  CA  . THR B 282 ? 0.571447  0.285283 0.426459 0.0588876   0.0349595   -0.0646572  282  THR B CA  
7221  C  C   . THR B 282 ? 0.529812  0.266512 0.396091 0.0492328   0.0321486   -0.0739547  282  THR B C   
7222  O  O   . THR B 282 ? 0.543614  0.268236 0.403958 0.0470261   0.0335316   -0.0832548  282  THR B O   
7223  C  CB  . THR B 282 ? 0.572436  0.297197 0.427041 0.0787643   0.0320326   -0.0607506  282  THR B CB  
7224  O  OG1 . THR B 282 ? 0.615315  0.3201   0.458212 0.089648    0.0331528   -0.0523105  282  THR B OG1 
7225  C  CG2 . THR B 282 ? 0.560141  0.282373 0.41053  0.088656    0.0323915   -0.0692727  282  THR B CG2 
7226  N  N   . MET B 283 ? 0.505873  0.275181 0.38692  0.0445338   0.0278625   -0.0718054  283  MET B N   
7227  C  CA  . MET B 283 ? 0.473481  0.26287  0.362373 0.0366449   0.0247111   -0.0795967  283  MET B CA  
7228  C  C   . MET B 283 ? 0.505186  0.280767 0.392489 0.0214899   0.0261776   -0.0878004  283  MET B C   
7229  O  O   . MET B 283 ? 0.518848  0.295221 0.404201 0.0182207   0.0248231   -0.0977059  283  MET B O   
7230  C  CB  . MET B 283 ? 0.442805  0.26345  0.345661 0.0328279   0.0205016   -0.0745097  283  MET B CB  
7231  C  CG  . MET B 283 ? 0.426564  0.265407 0.333889 0.0449792   0.0189905   -0.0681467  283  MET B CG  
7232  S  SD  . MET B 283 ? 0.425176  0.295772 0.346966 0.0401198   0.0149718   -0.062136   283  MET B SD  
7233  C  CE  . MET B 283 ? 0.394052  0.279587 0.31696  0.0348106   0.0123513   -0.0701906  283  MET B CE  
7234  N  N   . LEU B 284 ? 0.534497  0.298865 0.423144 0.0115619   0.0291496   -0.084227   284  LEU B N   
7235  C  CA  . LEU B 284 ? 0.567169  0.319751 0.456646 -0.00441058 0.0315666   -0.0928076  284  LEU B CA  
7236  C  C   . LEU B 284 ? 0.586918  0.30427  0.460744 -0.00261821 0.0367272   -0.0986523  284  LEU B C   
7237  O  O   . LEU B 284 ? 0.58294   0.294538 0.455944 -0.0112187  0.0366954   -0.110226   284  LEU B O   
7238  C  CB  . LEU B 284 ? 0.600149  0.348926 0.494373 -0.0145158  0.0353472   -0.0864219  284  LEU B CB  
7239  C  CG  . LEU B 284 ? 0.582244  0.364658 0.492167 -0.0173703  0.030452    -0.081931   284  LEU B CG  
7240  C  CD1 . LEU B 284 ? 0.58414   0.362622 0.495577 -0.0209881  0.034521    -0.0723428  284  LEU B CD1 
7241  C  CD2 . LEU B 284 ? 0.55116   0.353495 0.47283  -0.0290006  0.0260674   -0.0930258  284  LEU B CD2 
7242  N  N   . GLN B 285 ? 0.617084  0.310378 0.477777 0.00920293  0.040767    -0.0910338  285  GLN B N   
7243  C  CA  . GLN B 285 ? 0.673209  0.328517 0.5167   0.0120214   0.0461527   -0.0962111  285  GLN B CA  
7244  C  C   . GLN B 285 ? 0.665221  0.327178 0.507503 0.0163143   0.0428235   -0.107752   285  GLN B C   
7245  O  O   . GLN B 285 ? 0.690844  0.331692 0.525857 0.00889912  0.0456119   -0.118157   285  GLN B O   
7246  C  CB  . GLN B 285 ? 0.714769  0.341983 0.542206 0.0264096   0.0502805   -0.0859546  285  GLN B CB  
7247  C  CG  . GLN B 285 ? 0.849969  0.435873 0.65716  0.0334244   0.055466    -0.0905861  285  GLN B CG  
7248  C  CD  . GLN B 285 ? 0.921148  0.511778 0.723431 0.053989    0.0520418   -0.0923618  285  GLN B CD  
7249  O  OE1 . GLN B 285 ? 0.998654  0.581176 0.79593  0.0557279   0.0523651   -0.103041   285  GLN B OE1 
7250  N  NE2 . GLN B 285 ? 0.932052  0.537262 0.736262 0.0699053   0.0488182   -0.0827262  285  GLN B NE2 
7251  N  N   . GLN B 286 ? 0.642544  0.334144 0.491813 0.0271596   0.0373522   -0.106346   286  GLN B N   
7252  C  CA  . GLN B 286 ? 0.641383  0.340413 0.487451 0.033812    0.035018    -0.115812   286  GLN B CA  
7253  C  C   . GLN B 286 ? 0.613755  0.334257 0.468365 0.021198    0.0303839   -0.125449   286  GLN B C   
7254  O  O   . GLN B 286 ? 0.60929   0.334143 0.459037 0.0248637   0.0285381   -0.134561   286  GLN B O   
7255  C  CB  . GLN B 286 ? 0.621846  0.343146 0.470874 0.0506379   0.0326528   -0.110623   286  GLN B CB  
7256  C  CG  . GLN B 286 ? 0.658284  0.362485 0.498727 0.0673227   0.0356472   -0.103781   286  GLN B CG  
7257  C  CD  . GLN B 286 ? 0.645582  0.376842 0.493076 0.0824184   0.0334268   -0.0995453  286  GLN B CD  
7258  O  OE1 . GLN B 286 ? 0.602221  0.364591 0.460886 0.079741    0.0304865   -0.0995973  286  GLN B OE1 
7259  N  NE2 . GLN B 286 ? 0.646103  0.365795 0.487066 0.0987391   0.035029    -0.0958893  286  GLN B NE2 
7260  N  N   . GLY B 287 ? 0.578887  0.314632 0.445702 0.00775599  0.0280619   -0.123787   287  GLY B N   
7261  C  CA  . GLY B 287 ? 0.563682  0.320347 0.437867 -0.00222415 0.0224864   -0.133681   287  GLY B CA  
7262  C  C   . GLY B 287 ? 0.528739  0.319222 0.40933  0.00446667  0.0164623   -0.130507   287  GLY B C   
7263  O  O   . GLY B 287 ? 0.518415  0.322738 0.398611 0.00194038  0.0116603   -0.139149   287  GLY B O   
7264  N  N   . TRP B 288 ? 0.490196  0.294448 0.376407 0.0120683   0.0164923   -0.118275   288  TRP B N   
7265  C  CA  . TRP B 288 ? 0.468866  0.302413 0.360477 0.0162375   0.0118497   -0.115373   288  TRP B CA  
7266  C  C   . TRP B 288 ? 0.457185  0.308991 0.358076 0.0047701   0.00614869  -0.118795   288  TRP B C   
7267  O  O   . TRP B 288 ? 0.445565  0.293902 0.354147 -0.00555563 0.00652587  -0.118786   288  TRP B O   
7268  C  CB  . TRP B 288 ? 0.45089   0.294928 0.34845  0.0242689   0.0132365   -0.102392   288  TRP B CB  
7269  C  CG  . TRP B 288 ? 0.448803  0.285039 0.339724 0.0383329   0.0171364   -0.0996749  288  TRP B CG  
7270  C  CD1 . TRP B 288 ? 0.47993   0.290813 0.361612 0.0445316   0.0212286   -0.101509   288  TRP B CD1 
7271  C  CD2 . TRP B 288 ? 0.427866  0.283715 0.321966 0.0482461   0.0173993   -0.0947942  288  TRP B CD2 
7272  N  NE1 . TRP B 288 ? 0.47626   0.291954 0.35619  0.0589297   0.0231865   -0.0984764  288  TRP B NE1 
7273  C  CE2 . TRP B 288 ? 0.441409  0.285619 0.32994  0.0605338   0.0212579   -0.094687   288  TRP B CE2 
7274  C  CE3 . TRP B 288 ? 0.401226  0.282439 0.302175 0.0476488   0.0152128   -0.0907064  288  TRP B CE3 
7275  C  CZ2 . TRP B 288 ? 0.423587  0.284542 0.315743 0.0714219   0.0229727   -0.0917754  288  TRP B CZ2 
7276  C  CZ3 . TRP B 288 ? 0.400407  0.295006 0.303443 0.0571523   0.0178131   -0.0872117  288  TRP B CZ3 
7277  C  CH2 . TRP B 288 ? 0.396947  0.283251 0.296778 0.0684897   0.0216523   -0.0883603  288  TRP B CH2 
7278  N  N   . GLN B 289 ? 0.433931  0.305397 0.333571 0.00738169  0.00121244  -0.121419   289  GLN B N   
7279  C  CA  . GLN B 289 ? 0.451676  0.34323  0.359187 0.0003614   -0.00531894 -0.12344    289  GLN B CA  
7280  C  C   . GLN B 289 ? 0.420393  0.331819 0.328357 0.00779921  -0.00752595 -0.114832   289  GLN B C   
7281  O  O   . GLN B 289 ? 0.41908   0.329508 0.321795 0.0168994   -0.00358516 -0.10916    289  GLN B O   
7282  C  CB  . GLN B 289 ? 0.487296  0.38157  0.388885 -0.00363766 -0.0106391  -0.137272   289  GLN B CB  
7283  C  CG  . GLN B 289 ? 0.597685  0.473155 0.500279 -0.0140031  -0.00868807 -0.147895   289  GLN B CG  
7284  C  CD  . GLN B 289 ? 0.636431  0.514171 0.553913 -0.0262095  -0.00813748 -0.146879   289  GLN B CD  
7285  O  OE1 . GLN B 289 ? 0.675249  0.571488 0.603303 -0.0271967  -0.0107855  -0.139916   289  GLN B OE1 
7286  N  NE2 . GLN B 289 ? 0.725402  0.583309 0.643296 -0.0362195  -0.00402403 -0.154655   289  GLN B NE2 
7287  N  N   . ALA B 290 ? 0.378639  0.307723 0.292917 0.00386525  -0.0135093  -0.114572   290  ALA B N   
7288  C  CA  . ALA B 290 ? 0.382466  0.327277 0.295784 0.0100416   -0.0153141  -0.106223   290  ALA B CA  
7289  C  C   . ALA B 290 ? 0.398302  0.342677 0.297023 0.0188044   -0.0135428  -0.107017   290  ALA B C   
7290  O  O   . ALA B 290 ? 0.363378  0.312329 0.260415 0.0247816   -0.00975711 -0.0985587  290  ALA B O   
7291  C  CB  . ALA B 290 ? 0.362484  0.324157 0.281088 0.00649805  -0.02292    -0.107792   290  ALA B CB  
7292  N  N   . THR B 291 ? 0.415193  0.354345 0.303572 0.018854    -0.0158229  -0.117944   291  THR B N   
7293  C  CA  . THR B 291 ? 0.458024  0.397983 0.330822 0.0270442   -0.0140827  -0.119257   291  THR B CA  
7294  C  C   . THR B 291 ? 0.442722  0.373697 0.313664 0.0336645   -0.00514803 -0.114801   291  THR B C   
7295  O  O   . THR B 291 ? 0.436324  0.37404  0.301258 0.0401477   -0.00115375 -0.10947    291  THR B O   
7296  C  CB  . THR B 291 ? 0.503329  0.439946 0.365577 0.0252328   -0.019394   -0.133168   291  THR B CB  
7297  O  OG1 . THR B 291 ? 0.572855  0.513393 0.418499 0.0336295   -0.0181157  -0.132379   291  THR B OG1 
7298  C  CG2 . THR B 291 ? 0.516757  0.434675 0.377339 0.0230409   -0.0156991  -0.141955   291  THR B CG2 
7299  N  N   . HIS B 292 ? 0.433447  0.349751 0.309755 0.0322955   -0.00170634 -0.116579   292  HIS B N   
7300  C  CA  . HIS B 292 ? 0.433589  0.342748 0.308769 0.0404629   0.00560769  -0.113037   292  HIS B CA  
7301  C  C   . HIS B 292 ? 0.396511  0.318459 0.281278 0.0434569   0.00832875  -0.101037   292  HIS B C   
7302  O  O   . HIS B 292 ? 0.382358  0.310257 0.26557  0.0508602   0.0135616   -0.0979018  292  HIS B O   
7303  C  CB  . HIS B 292 ? 0.487837  0.376729 0.365902 0.0395614   0.00824113  -0.115348   292  HIS B CB  
7304  C  CG  . HIS B 292 ? 0.579151  0.451738 0.448712 0.0353447   0.00675114  -0.127736   292  HIS B CG  
7305  N  ND1 . HIS B 292 ? 0.592423  0.460834 0.466849 0.0237777   0.00246269  -0.132957   292  HIS B ND1 
7306  C  CD2 . HIS B 292 ? 0.60365   0.464307 0.460613 0.0404087   0.00898718  -0.13706    292  HIS B CD2 
7307  C  CE1 . HIS B 292 ? 0.620338  0.47366  0.485968 0.0211122   0.00219227  -0.145148   292  HIS B CE1 
7308  N  NE2 . HIS B 292 ? 0.636121  0.483777 0.490135 0.0314988   0.00586149  -0.147786   292  HIS B NE2 
7309  N  N   . MET B 293 ? 0.357307  0.284592 0.252624 0.03716     0.00495583  -0.095278   293  MET B N   
7310  C  CA  . MET B 293 ? 0.331761  0.269537 0.236839 0.0387959   0.00690348  -0.0848074  293  MET B CA  
7311  C  C   . MET B 293 ? 0.323201  0.275367 0.223843 0.0419348   0.00848501  -0.0811575  293  MET B C   
7312  O  O   . MET B 293 ? 0.30628   0.265497 0.211039 0.0463111   0.0134482   -0.0759503  293  MET B O   
7313  C  CB  . MET B 293 ? 0.327162  0.267932 0.24223  0.0310076   0.00261529  -0.080824   293  MET B CB  
7314  C  CG  . MET B 293 ? 0.342499  0.267215 0.261517 0.0280053   0.00382595  -0.0821265  293  MET B CG  
7315  S  SD  . MET B 293 ? 0.379857  0.306501 0.308997 0.0168729   -7.286e-05  -0.080996   293  MET B SD  
7316  C  CE  . MET B 293 ? 0.286704  0.226117 0.224986 0.0196468   0.00072248  -0.0688794  293  MET B CE  
7317  N  N   . PHE B 294 ? 0.310788  0.267446 0.203324 0.0393173   0.00412979  -0.0837443  294  PHE B N   
7318  C  CA  . PHE B 294 ? 0.308215  0.274017 0.191858 0.0422704   0.0061441   -0.0800397  294  PHE B CA  
7319  C  C   . PHE B 294 ? 0.309314  0.273746 0.183219 0.0488572   0.0134514   -0.083101   294  PHE B C   
7320  O  O   . PHE B 294 ? 0.301074  0.273328 0.173222 0.0511256   0.019338    -0.0777713  294  PHE B O   
7321  C  CB  . PHE B 294 ? 0.314707  0.283584 0.189197 0.0400247   -0.0011064  -0.0824623  294  PHE B CB  
7322  C  CG  . PHE B 294 ? 0.307047  0.282508 0.191755 0.0356126   -0.00604661 -0.0766067  294  PHE B CG  
7323  C  CD1 . PHE B 294 ? 0.317452  0.291859 0.21357  0.0299409   -0.0111227  -0.079935   294  PHE B CD1 
7324  C  CD2 . PHE B 294 ? 0.304697  0.286401 0.186948 0.0369103   -0.00474753 -0.0681512  294  PHE B CD2 
7325  C  CE1 . PHE B 294 ? 0.296888  0.278486 0.202833 0.0265106   -0.0148747  -0.0749749  294  PHE B CE1 
7326  C  CE2 . PHE B 294 ? 0.298074  0.284823 0.18962  0.0337848   -0.00881718 -0.0630532  294  PHE B CE2 
7327  C  CZ  . PHE B 294 ? 0.298974  0.286581 0.202785 0.0290093   -0.0139229  -0.0666026  294  PHE B CZ  
7328  N  N   . ARG B 295 ? 0.322477  0.277151 0.188965 0.0514354   0.0135414   -0.0922835  295  ARG B N   
7329  C  CA  . ARG B 295 ? 0.338186  0.292303 0.194566 0.0584178   0.0207164   -0.0960978  295  ARG B CA  
7330  C  C   . ARG B 295 ? 0.335576  0.293783 0.204233 0.0629937   0.0276638   -0.0922896  295  ARG B C   
7331  O  O   . ARG B 295 ? 0.333107  0.299155 0.199734 0.067966    0.0353149   -0.0917965  295  ARG B O   
7332  C  CB  . ARG B 295 ? 0.356211  0.297547 0.201349 0.0609628   0.019475    -0.107801   295  ARG B CB  
7333  C  CG  . ARG B 295 ? 0.366738  0.307513 0.19824  0.0577083   0.0123177   -0.113318   295  ARG B CG  
7334  C  CD  . ARG B 295 ? 0.377814  0.326595 0.193822 0.0617476   0.0160276   -0.110188   295  ARG B CD  
7335  N  NE  . ARG B 295 ? 0.386973  0.334318 0.184628 0.0620254   0.00945717  -0.116636   295  ARG B NE  
7336  C  CZ  . ARG B 295 ? 0.412547  0.362357 0.19052  0.0666533   0.012497    -0.115629   295  ARG B CZ  
7337  N  NH1 . ARG B 295 ? 0.412968  0.366289 0.186886 0.0705131   0.0237259   -0.109879   295  ARG B NH1 
7338  N  NH2 . ARG B 295 ? 0.428441  0.37698  0.189974 0.0675417   0.00436831  -0.121889   295  ARG B NH2 
7339  N  N   . VAL B 296 ? 0.335044  0.288089 0.216203 0.0616805   0.0250336   -0.0903665  296  VAL B N   
7340  C  CA  . VAL B 296 ? 0.341754  0.299288 0.234091 0.0675802   0.0299168   -0.087339   296  VAL B CA  
7341  C  C   . VAL B 296 ? 0.316771  0.291831 0.218832 0.0655804   0.0327844   -0.0790475  296  VAL B C   
7342  O  O   . VAL B 296 ? 0.322975  0.309348 0.230603 0.0704522   0.039256    -0.0785172  296  VAL B O   
7343  C  CB  . VAL B 296 ? 0.355732  0.300169 0.255008 0.0677354   0.0263935   -0.087097   296  VAL B CB  
7344  C  CG1 . VAL B 296 ? 0.365173  0.31793  0.278023 0.0720708   0.0281761   -0.0807738  296  VAL B CG1 
7345  C  CG2 . VAL B 296 ? 0.372659  0.297892 0.262113 0.0714495   0.0265315   -0.0959721  296  VAL B CG2 
7346  N  N   . ALA B 297 ? 0.303173  0.281224 0.20723  0.0582775   0.0284516   -0.0734702  297  ALA B N   
7347  C  CA  . ALA B 297 ? 0.286443  0.278082 0.19734  0.0553787   0.0314189   -0.0661727  297  ALA B CA  
7348  C  C   . ALA B 297 ? 0.293195  0.291665 0.194076 0.0566434   0.0388524   -0.0666965  297  ALA B C   
7349  O  O   . ALA B 297 ? 0.290222  0.300667 0.198334 0.0573371   0.0459902   -0.0644113  297  ALA B O   
7350  C  CB  . ALA B 297 ? 0.276005  0.266834 0.188207 0.0484571   0.0252906   -0.0609597  297  ALA B CB  
7351  N  N   . GLU B 298 ? 0.305346  0.296418 0.18887  0.0570003   0.0376995   -0.070556   298  GLU B N   
7352  C  CA  . GLU B 298 ? 0.321124  0.316147 0.191357 0.0582447   0.0452538   -0.0703677  298  GLU B CA  
7353  C  C   . GLU B 298 ? 0.329383  0.332436 0.204325 0.0638417   0.0549003   -0.0743721  298  GLU B C   
7354  O  O   . GLU B 298 ? 0.326484  0.339612 0.201121 0.0629335   0.0642638   -0.0718563  298  GLU B O   
7355  C  CB  . GLU B 298 ? 0.346817  0.331132 0.197148 0.0598113   0.040514    -0.0761642  298  GLU B CB  
7356  C  CG  . GLU B 298 ? 0.393481  0.378399 0.223926 0.0618053   0.0476166   -0.0758916  298  GLU B CG  
7357  C  CD  . GLU B 298 ? 0.451462  0.426749 0.260262 0.065105    0.0428451   -0.0833271  298  GLU B CD  
7358  O  OE1 . GLU B 298 ? 0.453984  0.422949 0.261395 0.0681311   0.039471    -0.092697   298  GLU B OE1 
7359  O  OE2 . GLU B 298 ? 0.510731  0.483958 0.301177 0.0651271   0.0434085   -0.0797809  298  GLU B OE2 
7360  N  N   . GLU B 299 ? 0.326679  0.324345 0.204599 0.0698248   0.0531983   -0.0813543  299  GLU B N   
7361  C  CA  . GLU B 299 ? 0.33999   0.345014 0.221257 0.0771514   0.0615336   -0.0865035  299  GLU B CA  
7362  C  C   . GLU B 299 ? 0.327631  0.350617 0.229561 0.0772545   0.0664988   -0.082497   299  GLU B C   
7363  O  O   . GLU B 299 ? 0.323951  0.360631 0.230822 0.0812821   0.0758395   -0.0856041  299  GLU B O   
7364  C  CB  . GLU B 299 ? 0.363996  0.355514 0.241954 0.0840949   0.0577574   -0.0946746  299  GLU B CB  
7365  C  CG  . GLU B 299 ? 0.400965  0.39642  0.275509 0.0935872   0.0661556   -0.102399   299  GLU B CG  
7366  C  CD  . GLU B 299 ? 0.42853   0.439274 0.322835 0.100197    0.0707901   -0.102157   299  GLU B CD  
7367  O  OE1 . GLU B 299 ? 0.43668   0.445947 0.344002 0.100805    0.0648125   -0.0987024  299  GLU B OE1 
7368  O  OE2 . GLU B 299 ? 0.441167  0.466452 0.337932 0.105105    0.0804095   -0.105814   299  GLU B OE2 
7369  N  N   . PHE B 300 ? 0.310737  0.334652 0.225611 0.0735687   0.0601172   -0.0770759  300  PHE B N   
7370  C  CA  . PHE B 300 ? 0.315506  0.357555 0.249476 0.0725388   0.063625    -0.0737077  300  PHE B CA  
7371  C  C   . PHE B 300 ? 0.310728  0.363915 0.242337 0.065691    0.0726486   -0.0704366  300  PHE B C   
7372  O  O   . PHE B 300 ? 0.303391  0.373511 0.24491  0.0668521   0.0815159   -0.0728455  300  PHE B O   
7373  C  CB  . PHE B 300 ? 0.312736  0.3529   0.258215 0.0694434   0.055229    -0.0684144  300  PHE B CB  
7374  C  CG  . PHE B 300 ? 0.322248  0.380579 0.288079 0.0720169   0.0566939   -0.0678963  300  PHE B CG  
7375  C  CD1 . PHE B 300 ? 0.347418  0.424075 0.323333 0.066249    0.0634032   -0.0660422  300  PHE B CD1 
7376  C  CD2 . PHE B 300 ? 0.32158   0.379021 0.295623 0.0810185   0.0520879   -0.0703521  300  PHE B CD2 
7377  C  CE1 . PHE B 300 ? 0.35094   0.447399 0.347299 0.0684015   0.0641016   -0.0674029  300  PHE B CE1 
7378  C  CE2 . PHE B 300 ? 0.310848  0.386964 0.303156 0.0848203   0.0520772   -0.0707036  300  PHE B CE2 
7379  C  CZ  . PHE B 300 ? 0.310343  0.407722 0.314989 0.0784681   0.0578032   -0.0700121  300  PHE B CZ  
7380  N  N   . PHE B 301 ? 0.324791  0.36768  0.242357 0.0587944   0.0706552   -0.0652625  301  PHE B N   
7381  C  CA  . PHE B 301 ? 0.345652  0.392259 0.255276 0.0522265   0.0791823   -0.0608492  301  PHE B CA  
7382  C  C   . PHE B 301 ? 0.362875  0.415298 0.263769 0.0555129   0.0908618   -0.0657801  301  PHE B C   
7383  O  O   . PHE B 301 ? 0.361434  0.427643 0.269928 0.051416    0.101646    -0.0648995  301  PHE B O   
7384  C  CB  . PHE B 301 ? 0.360064  0.391691 0.252604 0.0473178   0.0737315   -0.0548081  301  PHE B CB  
7385  C  CG  . PHE B 301 ? 0.36209   0.392892 0.265541 0.0419254   0.0665544   -0.0486871  301  PHE B CG  
7386  C  CD1 . PHE B 301 ? 0.369109  0.405377 0.278063 0.034748    0.0720605   -0.0428448  301  PHE B CD1 
7387  C  CD2 . PHE B 301 ? 0.36007   0.384349 0.268386 0.0434553   0.0553484   -0.0492374  301  PHE B CD2 
7388  C  CE1 . PHE B 301 ? 0.350661  0.385357 0.268359 0.0302713   0.0656878   -0.0378849  301  PHE B CE1 
7389  C  CE2 . PHE B 301 ? 0.379245  0.403386 0.296933 0.0387893   0.0496086   -0.0439234  301  PHE B CE2 
7390  C  CZ  . PHE B 301 ? 0.355253  0.38493  0.277855 0.0327381   0.0544485   -0.038448   301  PHE B CZ  
7391  N  N   . THR B 302 ? 0.367859  0.40989  0.252767 0.0621284   0.0892059   -0.0714944  302  THR B N   
7392  C  CA  . THR B 302 ? 0.388188  0.43364  0.261197 0.0658538   0.100082    -0.0765171  302  THR B CA  
7393  C  C   . THR B 302 ? 0.375568  0.439699 0.268637 0.0714563   0.106962    -0.0828139  302  THR B C   
7394  O  O   . THR B 302 ? 0.387948  0.462411 0.278374 0.0723042   0.119213    -0.0860504  302  THR B O   
7395  C  CB  . THR B 302 ? 0.418397  0.447581 0.268765 0.0716044   0.0954269   -0.081994   302  THR B CB  
7396  O  OG1 . THR B 302 ? 0.393679  0.417519 0.252702 0.0776671   0.0866042   -0.0878272  302  THR B OG1 
7397  C  CG2 . THR B 302 ? 0.428758  0.443038 0.260418 0.0670679   0.0877558   -0.0766132  302  THR B CG2 
7398  N  N   . SER B 303 ? 0.358856  0.427922 0.271401 0.0756034   0.0994974   -0.0844496  303  SER B N   
7399  C  CA  . SER B 303 ? 0.362019  0.450029 0.29355  0.0831857   0.104711    -0.0909182  303  SER B CA  
7400  C  C   . SER B 303 ? 0.358956  0.470728 0.3078   0.0760895   0.114614    -0.088962   303  SER B C   
7401  O  O   . SER B 303 ? 0.369783  0.501935 0.331814 0.0805849   0.123353    -0.0953819  303  SER B O   
7402  C  CB  . SER B 303 ? 0.350041  0.43591  0.295288 0.0906183   0.0942281   -0.0925423  303  SER B CB  
7403  O  OG  . SER B 303 ? 0.360628  0.456639 0.322982 0.0845729   0.0903902   -0.0867863  303  SER B OG  
7404  N  N   . LEU B 304 ? 0.343079  0.452053 0.29151  0.0648031   0.113751    -0.080854   304  LEU B N   
7405  C  CA  . LEU B 304 ? 0.348883  0.475566 0.311679 0.0549223   0.122649    -0.0782077  304  LEU B CA  
7406  C  C   . LEU B 304 ? 0.386396  0.510026 0.331765 0.0477088   0.13665     -0.0760723  304  LEU B C   
7407  O  O   . LEU B 304 ? 0.39458   0.528756 0.347896 0.0373946   0.146241    -0.073396   304  LEU B O   
7408  C  CB  . LEU B 304 ? 0.315706  0.436138 0.283688 0.0465551   0.114515    -0.0703708  304  LEU B CB  
7409  C  CG  . LEU B 304 ? 0.300923  0.423094 0.284344 0.0522242   0.101302    -0.0710145  304  LEU B CG  
7410  C  CD1 . LEU B 304 ? 0.2987    0.416589 0.286591 0.0431742   0.0956618   -0.0638498  304  LEU B CD1 
7411  C  CD2 . LEU B 304 ? 0.293514  0.441458 0.301752 0.0583118   0.103479    -0.0781897  304  LEU B CD2 
7412  N  N   . GLU B 305 ? 0.416101  0.52314  0.336095 0.0524708   0.137467    -0.076938   305  GLU B N   
7413  C  CA  . GLU B 305 ? 0.459295  0.557822 0.355621 0.0472875   0.149341    -0.0738574  305  GLU B CA  
7414  C  C   . GLU B 305 ? 0.467682  0.549688 0.350298 0.0375538   0.147149    -0.0632321  305  GLU B C   
7415  O  O   . GLU B 305 ? 0.505253  0.581158 0.37171  0.0307783   0.158616    -0.058541   305  GLU B O   
7416  C  CB  . GLU B 305 ? 0.512191  0.632032 0.417883 0.0446366   0.167273    -0.078831   305  GLU B CB  
7417  C  CG  . GLU B 305 ? 0.605279  0.740334 0.522957 0.0569385   0.168118    -0.0899538  305  GLU B CG  
7418  C  CD  . GLU B 305 ? 0.748611  0.894933 0.659528 0.0583318   0.185418    -0.0959259  305  GLU B CD  
7419  O  OE1 . GLU B 305 ? 0.794444  0.968669 0.72969  0.0574337   0.195703    -0.102108   305  GLU B OE1 
7420  O  OE2 . GLU B 305 ? 0.885118  1.01311  0.766142 0.0608029   0.188317    -0.0950783  305  GLU B OE2 
7421  N  N   . LEU B 306 ? 0.449047  0.521657 0.335668 0.0376687   0.132566    -0.0593541  306  LEU B N   
7422  C  CA  . LEU B 306 ? 0.450597  0.503585 0.318769 0.0323558   0.127819    -0.0503248  306  LEU B CA  
7423  C  C   . LEU B 306 ? 0.461262  0.495745 0.301537 0.0393989   0.121313    -0.0509995  306  LEU B C   
7424  O  O   . LEU B 306 ? 0.47473   0.511253 0.3105   0.0468964   0.121864    -0.058475   306  LEU B O   
7425  C  CB  . LEU B 306 ? 0.418624  0.472423 0.304674 0.0296317   0.115992    -0.0470357  306  LEU B CB  
7426  C  CG  . LEU B 306 ? 0.421803  0.494753 0.335145 0.0227902   0.121087    -0.0474276  306  LEU B CG  
7427  C  CD1 . LEU B 306 ? 0.393385  0.464342 0.319797 0.0219753   0.107985    -0.0446027  306  LEU B CD1 
7428  C  CD2 . LEU B 306 ? 0.455894  0.527993 0.364086 0.0116229   0.134457    -0.0423056  306  LEU B CD2 
7429  N  N   . SER B 307 ? 0.464193  0.481208 0.285351 0.0374744   0.115357    -0.0439662  307  SER B N   
7430  C  CA  . SER B 307 ? 0.511241  0.512324 0.303692 0.0437065   0.109961    -0.0447434  307  SER B CA  
7431  C  C   . SER B 307 ? 0.46908   0.466946 0.266479 0.0495418   0.0938126   -0.0501009  307  SER B C   
7432  O  O   . SER B 307 ? 0.440009  0.440447 0.255479 0.0473517   0.0848444   -0.0485423  307  SER B O   
7433  C  CB  . SER B 307 ? 0.547135  0.531592 0.31587  0.0408628   0.110229    -0.0354744  307  SER B CB  
7434  O  OG  . SER B 307 ? 0.642972  0.628645 0.406984 0.0341813   0.127144    -0.0308863  307  SER B OG  
7435  N  N   . PRO B 308 ? 0.47422   0.465692 0.254398 0.0564629   0.0906297   -0.0569054  308  PRO B N   
7436  C  CA  . PRO B 308 ? 0.465389  0.450534 0.24512  0.0604308   0.0756936   -0.0622633  308  PRO B CA  
7437  C  C   . PRO B 308 ? 0.45479   0.43014  0.222486 0.0589175   0.0658863   -0.0562063  308  PRO B C   
7438  O  O   . PRO B 308 ? 0.468966  0.438592 0.222212 0.0568786   0.0710073   -0.0482253  308  PRO B O   
7439  C  CB  . PRO B 308 ? 0.473066  0.453559 0.234013 0.0673858   0.0772234   -0.0714755  308  PRO B CB  
7440  C  CG  . PRO B 308 ? 0.514523  0.493733 0.255052 0.0673037   0.0911496   -0.0675585  308  PRO B CG  
7441  C  CD  . PRO B 308 ? 0.493074  0.482676 0.252191 0.060046    0.101839    -0.0601827  308  PRO B CD  
7442  N  N   . MET B 309 ? 0.43359   0.406864 0.207873 0.0598875   0.0522903   -0.0600879  309  MET B N   
7443  C  CA  . MET B 309 ? 0.442553  0.408904 0.204841 0.0605321   0.0416184   -0.0570044  309  MET B CA  
7444  C  C   . MET B 309 ? 0.469467  0.427604 0.201097 0.0667918   0.040038    -0.0606412  309  MET B C   
7445  O  O   . MET B 309 ? 0.478821  0.436722 0.204021 0.0703394   0.0408127   -0.0697175  309  MET B O   
7446  C  CB  . MET B 309 ? 0.424861  0.393863 0.204324 0.0591049   0.0286283   -0.0618893  309  MET B CB  
7447  C  CG  . MET B 309 ? 0.404458  0.380357 0.211914 0.0539196   0.0294971   -0.0587707  309  MET B CG  
7448  S  SD  . MET B 309 ? 0.425702  0.402351 0.237625 0.0494135   0.031885    -0.0464996  309  MET B SD  
7449  C  CE  . MET B 309 ? 0.416184  0.398491 0.231763 0.0475824   0.0483975   -0.044399   309  MET B CE  
7450  N  N   . PRO B 310 ? 0.489098  0.43891  0.198451 0.0691637   0.0388996   -0.0535157  310  PRO B N   
7451  C  CA  . PRO B 310 ? 0.506443  0.447656 0.183038 0.0765805   0.036456    -0.0564935  310  PRO B CA  
7452  C  C   . PRO B 310 ? 0.498328  0.441655 0.172807 0.0807345   0.0198821   -0.066583   310  PRO B C   
7453  O  O   . PRO B 310 ? 0.477853  0.427801 0.1747   0.0772548   0.0106314   -0.0689101  310  PRO B O   
7454  C  CB  . PRO B 310 ? 0.524309  0.454547 0.18055  0.0778952   0.0396563   -0.0442307  310  PRO B CB  
7455  C  CG  . PRO B 310 ? 0.497391  0.431674 0.177967 0.0724761   0.0352183   -0.0383307  310  PRO B CG  
7456  C  CD  . PRO B 310 ? 0.477915  0.424733 0.191317 0.0656884   0.0393905   -0.0425616  310  PRO B CD  
7457  N  N   . PRO B 311 ? 0.518742  0.457344 0.166874 0.087719    0.015797    -0.0735091  311  PRO B N   
7458  C  CA  . PRO B 311 ? 0.519843  0.462183 0.165559 0.0911667   -0.00055583 -0.0845451  311  PRO B CA  
7459  C  C   . PRO B 311 ? 0.508883  0.455502 0.162059 0.0916756   -0.0136766  -0.0814477  311  PRO B C   
7460  O  O   . PRO B 311 ? 0.493532  0.449276 0.166472 0.0885231   -0.0245137  -0.0896781  311  PRO B O   
7461  C  CB  . PRO B 311 ? 0.553502  0.487969 0.161516 0.100175    -0.00101826 -0.0883509  311  PRO B CB  
7462  C  CG  . PRO B 311 ? 0.568778  0.497543 0.167682 0.099329    0.0172234   -0.083934   311  PRO B CG  
7463  C  CD  . PRO B 311 ? 0.541697  0.471621 0.160202 0.0923596   0.0271284   -0.0713118  311  PRO B CD  
7464  N  N   . GLU B 312 ? 0.526284  0.465638 0.164061 0.0953441   -0.0115934  -0.0695188  312  GLU B N   
7465  C  CA  . GLU B 312 ? 0.535617  0.477896 0.178358 0.0976776   -0.0229883  -0.0654576  312  GLU B CA  
7466  C  C   . GLU B 312 ? 0.494637  0.447295 0.174699 0.0888107   -0.0248888  -0.0656853  312  GLU B C   
7467  O  O   . GLU B 312 ? 0.479718  0.440982 0.171291 0.089625    -0.0373119  -0.0692678  312  GLU B O   
7468  C  CB  . GLU B 312 ? 0.579707  0.508183 0.201276 0.101932    -0.0167366  -0.0508532  312  GLU B CB  
7469  C  CG  . GLU B 312 ? 0.654217  0.569199 0.233848 0.111677    -0.0143723  -0.0487939  312  GLU B CG  
7470  C  CD  . GLU B 312 ? 0.706817  0.613147 0.268702 0.110223    0.00183411  -0.047492   312  GLU B CD  
7471  O  OE1 . GLU B 312 ? 0.691873  0.602666 0.273755 0.101518    0.013998    -0.0477767  312  GLU B OE1 
7472  O  OE2 . GLU B 312 ? 0.772995  0.668065 0.298699 0.118816    0.00268619  -0.046241   312  GLU B OE2 
7473  N  N   . PHE B 313 ? 0.459449  0.412414 0.158024 0.0809606   -0.0128496  -0.0624746  313  PHE B N   
7474  C  CA  . PHE B 313 ? 0.43137   0.39286  0.16291  0.0731535   -0.0141067  -0.0625828  313  PHE B CA  
7475  C  C   . PHE B 313 ? 0.428422  0.398484 0.175303 0.0705323   -0.0235851  -0.0755907  313  PHE B C   
7476  O  O   . PHE B 313 ? 0.416016  0.393796 0.181171 0.0673237   -0.0317606  -0.0775997  313  PHE B O   
7477  C  CB  . PHE B 313 ? 0.412659  0.373671 0.159401 0.0668073   -0.00033177 -0.0570782  313  PHE B CB  
7478  C  CG  . PHE B 313 ? 0.387179  0.356178 0.165206 0.0599767   -0.00221812 -0.0586867  313  PHE B CG  
7479  C  CD1 . PHE B 313 ? 0.37672   0.348891 0.167563 0.0575207   -0.00338972 -0.0680306  313  PHE B CD1 
7480  C  CD2 . PHE B 313 ? 0.367488  0.338589 0.159301 0.056565    -0.00257871 -0.0508637  313  PHE B CD2 
7481  C  CE1 . PHE B 313 ? 0.357606  0.334152 0.173211 0.0519606   -0.00457428 -0.0686524  313  PHE B CE1 
7482  C  CE2 . PHE B 313 ? 0.351549  0.329078 0.169136 0.0509179   -0.00403544 -0.052082   313  PHE B CE2 
7483  C  CZ  . PHE B 313 ? 0.351412  0.331324 0.180272 0.048719    -0.00504805 -0.0605908  313  PHE B CZ  
7484  N  N   . TRP B 314 ? 0.446148  0.414209 0.185648 0.0713574   -0.0217553  -0.084912   314  TRP B N   
7485  C  CA  . TRP B 314 ? 0.450167  0.423041 0.203696 0.067414    -0.0289595  -0.097711   314  TRP B CA  
7486  C  C   . TRP B 314 ? 0.470762  0.450813 0.218313 0.07032     -0.043753   -0.105769   314  TRP B C   
7487  O  O   . TRP B 314 ? 0.451304  0.439245 0.21753  0.0648839   -0.0515082  -0.113781   314  TRP B O   
7488  C  CB  . TRP B 314 ? 0.456327  0.423136 0.202595 0.068035    -0.0227805  -0.106054   314  TRP B CB  
7489  C  CG  . TRP B 314 ? 0.436047  0.399522 0.19239  0.0658854   -0.00921435 -0.0994435  314  TRP B CG  
7490  C  CD1 . TRP B 314 ? 0.447773  0.407656 0.190486 0.0694942   0.00219958  -0.0937838  314  TRP B CD1 
7491  C  CD2 . TRP B 314 ? 0.414459  0.379559 0.19689  0.0599949   -0.00574231 -0.0973544  314  TRP B CD2 
7492  N  NE1 . TRP B 314 ? 0.431989  0.393716 0.192567 0.0663173   0.0117741   -0.0893838  314  TRP B NE1 
7493  C  CE2 . TRP B 314 ? 0.409438  0.37371  0.193327 0.061265    0.00667903  -0.0911019  314  TRP B CE2 
7494  C  CE3 . TRP B 314 ? 0.398737  0.365952 0.202349 0.0539467   -0.0115205  -0.100326   314  TRP B CE3 
7495  C  CZ2 . TRP B 314 ? 0.39188   0.358093 0.197063 0.0581442   0.0118516   -0.0882776  314  TRP B CZ2 
7496  C  CZ3 . TRP B 314 ? 0.388058  0.354243 0.210396 0.0506237   -0.00546636 -0.0963092  314  TRP B CZ3 
7497  C  CH2 . TRP B 314 ? 0.377768  0.343873 0.200726 0.0533739   0.00529589  -0.0904431  314  TRP B CH2 
7498  N  N   . GLU B 315 ? 0.508836  0.486223 0.229294 0.0791535   -0.0472242  -0.104001   315  GLU B N   
7499  C  CA  . GLU B 315 ? 0.559633  0.545442 0.271466 0.0843016   -0.0623593  -0.112659   315  GLU B CA  
7500  C  C   . GLU B 315 ? 0.541607  0.537553 0.270017 0.0836956   -0.0704805  -0.108614   315  GLU B C   
7501  O  O   . GLU B 315 ? 0.571312  0.580468 0.310135 0.0830201   -0.0827732  -0.11887    315  GLU B O   
7502  C  CB  . GLU B 315 ? 0.630664  0.609113 0.305677 0.0958103   -0.063885   -0.110395   315  GLU B CB  
7503  C  CG  . GLU B 315 ? 0.746724  0.718573 0.403965 0.0974322   -0.0593801  -0.119012   315  GLU B CG  
7504  C  CD  . GLU B 315 ? 0.814801  0.79278  0.488748 0.0905889   -0.0643597  -0.135489   315  GLU B CD  
7505  O  OE1 . GLU B 315 ? 0.843984  0.833222 0.522272 0.090813    -0.0786114  -0.146834   315  GLU B OE1 
7506  O  OE2 . GLU B 315 ? 0.833978  0.80561  0.517561 0.0849387   -0.0540623  -0.137413   315  GLU B OE2 
7507  N  N   . GLY B 316 ? 0.516318  0.507229 0.249317 0.0831979   -0.0632634  -0.0947592  316  GLY B N   
7508  C  CA  . GLY B 316 ? 0.50787   0.505721 0.247272 0.0865248   -0.0712829  -0.0901084  316  GLY B CA  
7509  C  C   . GLY B 316 ? 0.480611  0.484824 0.251745 0.0773216   -0.0685408  -0.0870968  316  GLY B C   
7510  O  O   . GLY B 316 ? 0.453075  0.465817 0.233961 0.0791695   -0.0757823  -0.0858029  316  GLY B O   
7511  N  N   . SER B 317 ? 0.452692  0.452745 0.238618 0.0685742   -0.0582585  -0.0860524  317  SER B N   
7512  C  CA  . SER B 317 ? 0.426233  0.430053 0.238144 0.0609794   -0.0548026  -0.0816297  317  SER B CA  
7513  C  C   . SER B 317 ? 0.411222  0.427961 0.244847 0.0548354   -0.0631141  -0.0927462  317  SER B C   
7514  O  O   . SER B 317 ? 0.404912  0.425477 0.236625 0.0536802   -0.0684418  -0.1045     317  SER B O   
7515  C  CB  . SER B 317 ? 0.412448  0.408322 0.23205  0.0551997   -0.0421855  -0.0771389  317  SER B CB  
7516  O  OG  . SER B 317 ? 0.447001  0.43375  0.25201  0.058604    -0.0331253  -0.0668111  317  SER B OG  
7517  N  N   . MET B 318 ? 0.389451  0.412353 0.24429  0.0497665   -0.0630067  -0.0894349  318  MET B N   
7518  C  CA  . MET B 318 ? 0.396476  0.429903 0.273699 0.0414958   -0.0671923  -0.0989266  318  MET B CA  
7519  C  C   . MET B 318 ? 0.38469   0.410229 0.276962 0.032993    -0.0570313  -0.0948183  318  MET B C   
7520  O  O   . MET B 318 ? 0.348936  0.373203 0.249166 0.0321356   -0.0524431  -0.085246   318  MET B O   
7521  C  CB  . MET B 318 ? 0.406681  0.454425 0.295554 0.0432952   -0.0749409  -0.0987063  318  MET B CB  
7522  C  CG  . MET B 318 ? 0.446145  0.507912 0.358211 0.0344833   -0.0792976  -0.109665   318  MET B CG  
7523  S  SD  . MET B 318 ? 0.509933  0.586966 0.439302 0.0359341   -0.0835567  -0.106026   318  MET B SD  
7524  C  CE  . MET B 318 ? 0.490744  0.55835  0.435996 0.0268017   -0.0711858  -0.0963917  318  MET B CE  
7525  N  N   . LEU B 319 ? 0.395303  0.414548 0.289991 0.0275253   -0.0538952  -0.102313   319  LEU B N   
7526  C  CA  . LEU B 319 ? 0.39727   0.405406 0.29995  0.0226294   -0.0440876  -0.0978782  319  LEU B CA  
7527  C  C   . LEU B 319 ? 0.403593  0.413051 0.325305 0.0128164   -0.0440578  -0.103498   319  LEU B C   
7528  O  O   . LEU B 319 ? 0.403091  0.402789 0.331521 0.00899748  -0.0369146  -0.0998363  319  LEU B O   
7529  C  CB  . LEU B 319 ? 0.413133  0.409134 0.302574 0.0252727   -0.0383025  -0.100014   319  LEU B CB  
7530  C  CG  . LEU B 319 ? 0.413696  0.407428 0.282282 0.0339612   -0.0365449  -0.0957681  319  LEU B CG  
7531  C  CD1 . LEU B 319 ? 0.477777  0.461357 0.335213 0.0360445   -0.0307864  -0.100539   319  LEU B CD1 
7532  C  CD2 . LEU B 319 ? 0.401734  0.395109 0.270465 0.0365844   -0.0308071  -0.0829428  319  LEU B CD2 
7533  N  N   . GLU B 320 ? 0.413179  0.43498  0.343303 0.00881846  -0.0518213  -0.112663   320  GLU B N   
7534  C  CA  . GLU B 320 ? 0.442717  0.467    0.39128  -0.00199042 -0.0508164  -0.118614   320  GLU B CA  
7535  C  C   . GLU B 320 ? 0.435294  0.48028  0.396459 -0.00293291 -0.0585261  -0.121898   320  GLU B C   
7536  O  O   . GLU B 320 ? 0.387513  0.444201 0.341173 0.00471875  -0.0670832  -0.124287   320  GLU B O   
7537  C  CB  . GLU B 320 ? 0.511089  0.53139  0.457836 -0.00784758 -0.0529067  -0.132813   320  GLU B CB  
7538  C  CG  . GLU B 320 ? 0.58072   0.579155 0.523319 -0.0116353  -0.0440607  -0.133004   320  GLU B CG  
7539  C  CD  . GLU B 320 ? 0.673171  0.664773 0.609362 -0.0156423  -0.0462264  -0.14735    320  GLU B CD  
7540  O  OE1 . GLU B 320 ? 0.675066  0.680386 0.614215 -0.0188562  -0.0547391  -0.159672   320  GLU B OE1 
7541  O  OE2 . GLU B 320 ? 0.657862  0.629996 0.585325 -0.0146816  -0.0394744  -0.146717   320  GLU B OE2 
7542  N  N   . LYS B 321 ? 0.422314  0.471783 0.401673 -0.0114602  -0.0553875  -0.122119   321  LYS B N   
7543  C  CA  . LYS B 321 ? 0.413669  0.485207 0.407565 -0.0129115  -0.0622816  -0.127627   321  LYS B CA  
7544  C  C   . LYS B 321 ? 0.429878  0.515263 0.427575 -0.0163657  -0.0709221  -0.144124   321  LYS B C   
7545  O  O   . LYS B 321 ? 0.452604  0.531209 0.454421 -0.026386   -0.0679258  -0.153395   321  LYS B O   
7546  C  CB  . LYS B 321 ? 0.436698  0.509551 0.448676 -0.0223811  -0.0554455  -0.125288   321  LYS B CB  
7547  C  CG  . LYS B 321 ? 0.454992  0.553178 0.483823 -0.0231973  -0.061753   -0.131138   321  LYS B CG  
7548  C  CD  . LYS B 321 ? 0.524514  0.623644 0.568048 -0.0299892  -0.0539497  -0.125811   321  LYS B CD  
7549  C  CE  . LYS B 321 ? 0.498471  0.623508 0.558823 -0.0291914  -0.0593164  -0.130899   321  LYS B CE  
7550  N  NZ  . LYS B 321 ? 0.531603  0.655399 0.604098 -0.0362681  -0.0502458  -0.125788   321  LYS B NZ  
7551  N  N   . PRO B 322 ? 0.430355  0.53464  0.425559 -0.00771627 -0.0822587  -0.148856   322  PRO B N   
7552  C  CA  . PRO B 322 ? 0.501333  0.621219 0.499169 -0.00949689 -0.0922207  -0.165607   322  PRO B CA  
7553  C  C   . PRO B 322 ? 0.525936  0.660257 0.549568 -0.0243188  -0.0912346  -0.178361   322  PRO B C   
7554  O  O   . PRO B 322 ? 0.562239  0.706256 0.602844 -0.0283011  -0.0878887  -0.175188   322  PRO B O   
7555  C  CB  . PRO B 322 ? 0.497758  0.635576 0.487935 0.00487406  -0.104704   -0.166001   322  PRO B CB  
7556  C  CG  . PRO B 322 ? 0.447114  0.576724 0.43053  0.0135773   -0.100351   -0.1488     322  PRO B CG  
7557  C  CD  . PRO B 322 ? 0.412812  0.52239  0.39986  0.00525884  -0.0864312  -0.138547   322  PRO B CD  
7558  N  N   . ALA B 323 ? 0.557889  0.692261 0.583529 -0.0329678  -0.0931601  -0.192879   323  ALA B N   
7559  C  CA  . ALA B 323 ? 0.678476  0.821188 0.726981 -0.0502557  -0.0896189  -0.206023   323  ALA B CA  
7560  C  C   . ALA B 323 ? 0.717351  0.896123 0.78462  -0.0513522  -0.101688   -0.222024   323  ALA B C   
7561  O  O   . ALA B 323 ? 0.677191  0.867878 0.765448 -0.0666019  -0.0998461  -0.236021   323  ALA B O   
7562  C  CB  . ALA B 323 ? 0.650591  0.771678 0.691261 -0.0600036  -0.084405   -0.213936   323  ALA B CB  
7563  N  N   . ASP B 324 ? 0.80163   0.99808  0.861869 -0.035113   -0.11366    -0.220006   324  ASP B N   
7564  C  CA  . ASP B 324 ? 0.863281  1.09378  0.9359   -0.0320238  -0.128182   -0.236623   324  ASP B CA  
7565  C  C   . ASP B 324 ? 0.911056  1.16787  1.00447  -0.028509   -0.131071   -0.235517   324  ASP B C   
7566  O  O   . ASP B 324 ? 0.983633  1.2669   1.07986  -0.016816   -0.144987   -0.242851   324  ASP B O   
7567  C  CB  . ASP B 324 ? 0.899312  1.13155  0.94679  -0.0148861  -0.141384   -0.23792    324  ASP B CB  
7568  C  CG  . ASP B 324 ? 0.972562  1.18775  0.994986 0.00243538  -0.140556   -0.217996   324  ASP B CG  
7569  O  OD1 . ASP B 324 ? 0.913201  1.12175  0.941148 0.00295617  -0.132436   -0.204294   324  ASP B OD1 
7570  O  OD2 . ASP B 324 ? 1.03472   1.24212  1.0314   0.014547    -0.147231   -0.216517   324  ASP B OD2 
7571  N  N   . GLY B 325 ? 0.921794  1.17134  1.02882  -0.037842   -0.118195   -0.226992   325  GLY B N   
7572  C  CA  . GLY B 325 ? 0.900612  1.17195  1.02612  -0.0344798  -0.118705   -0.224541   325  GLY B CA  
7573  C  C   . GLY B 325 ? 0.838876  1.11448  0.948114 -0.0121962  -0.128706   -0.214453   325  GLY B C   
7574  O  O   . GLY B 325 ? 0.82977   1.13396  0.947245 -0.00213602 -0.141271   -0.223053   325  GLY B O   
7575  N  N   . ARG B 326 ? 0.694352  0.940662 0.779625 -0.00423846 -0.123076   -0.19654    326  ARG B N   
7576  C  CA  . ARG B 326 ? 0.626232  0.870854 0.693207 0.0155188   -0.130531   -0.185887   326  ARG B CA  
7577  C  C   . ARG B 326 ? 0.590178  0.81464  0.65288  0.0162725   -0.118976   -0.167947   326  ARG B C   
7578  O  O   . ARG B 326 ? 0.611208  0.812005 0.66817  0.00755804  -0.107519   -0.159993   326  ARG B O   
7579  C  CB  . ARG B 326 ? 0.598814  0.832361 0.637831 0.0262189   -0.138677   -0.185957   326  ARG B CB  
7580  C  CG  . ARG B 326 ? 0.597604  0.816984 0.61065  0.0445953   -0.141673   -0.170722   326  ARG B CG  
7581  C  CD  . ARG B 326 ? 0.646246  0.846248 0.627026 0.0538807   -0.144636   -0.166089   326  ARG B CD  
7582  N  NE  . ARG B 326 ? 0.687195  0.874555 0.662885 0.0430272   -0.139528   -0.17163    326  ARG B NE  
7583  C  CZ  . ARG B 326 ? 0.672517  0.8369   0.622584 0.0466929   -0.135691   -0.164942   326  ARG B CZ  
7584  N  NH1 . ARG B 326 ? 0.653725  0.799928 0.582184 0.0571489   -0.131837   -0.149267   326  ARG B NH1 
7585  N  NH2 . ARG B 326 ? 0.674361  0.832671 0.621467 0.0384719   -0.134004   -0.174048   326  ARG B NH2 
7586  N  N   . GLU B 327 ? 0.528347  0.763155 0.594838 0.0267673   -0.122276   -0.1627     327  GLU B N   
7587  C  CA  . GLU B 327 ? 0.517752  0.735526 0.580697 0.0279622   -0.112497   -0.147228   327  GLU B CA  
7588  C  C   . GLU B 327 ? 0.501902  0.691937 0.534965 0.0375146   -0.111051   -0.133252   327  GLU B C   
7589  O  O   . GLU B 327 ? 0.505422  0.69541  0.520419 0.0507474   -0.120523   -0.133125   327  GLU B O   
7590  C  CB  . GLU B 327 ? 0.550375  0.7888   0.627052 0.0363469   -0.116979   -0.148209   327  GLU B CB  
7591  C  CG  . GLU B 327 ? 0.62819   0.89509  0.737037 0.0247727   -0.115524   -0.161942   327  GLU B CG  
7592  C  CD  . GLU B 327 ? 0.750506  1.0112   0.874262 0.010767    -0.10089    -0.157264   327  GLU B CD  
7593  O  OE1 . GLU B 327 ? 0.753974  1.03927  0.903228 0.00319609  -0.0991915  -0.167562   327  GLU B OE1 
7594  O  OE2 . GLU B 327 ? 0.775251  1.00811  0.885809 0.00728249  -0.0910148  -0.144073   327  GLU B OE2 
7595  N  N   . VAL B 328 ? 0.405881  0.57277  0.433493 0.0302744   -0.098976   -0.122419   328  VAL B N   
7596  C  CA  . VAL B 328 ? 0.398631  0.540942 0.401498 0.0372854   -0.095487   -0.109403   328  VAL B CA  
7597  C  C   . VAL B 328 ? 0.347268  0.47722  0.352828 0.0351131   -0.0858264  -0.09724    328  VAL B C   
7598  O  O   . VAL B 328 ? 0.327157  0.463496 0.351105 0.0258778   -0.0804612  -0.0994007  328  VAL B O   
7599  C  CB  . VAL B 328 ? 0.435957  0.562238 0.427075 0.031322    -0.0909732  -0.109902   328  VAL B CB  
7600  C  CG1 . VAL B 328 ? 0.449112  0.584846 0.432552 0.0350861   -0.101      -0.121464   328  VAL B CG1 
7601  C  CG2 . VAL B 328 ? 0.480358  0.601197 0.48631  0.0161907   -0.0811821  -0.112019   328  VAL B CG2 
7602  N  N   . VAL B 329 ? 0.34528   0.45853  0.332096 0.0436638   -0.0839908  -0.0854539  329  VAL B N   
7603  C  CA  . VAL B 329 ? 0.353432  0.450956 0.338619 0.040744    -0.0742654  -0.0739584  329  VAL B CA  
7604  C  C   . VAL B 329 ? 0.377476  0.462199 0.360871 0.0313077   -0.0661735  -0.0725324  329  VAL B C   
7605  O  O   . VAL B 329 ? 0.369546  0.443692 0.337012 0.0339084   -0.0657806  -0.0708261  329  VAL B O   
7606  C  CB  . VAL B 329 ? 0.33798   0.420177 0.302967 0.050976    -0.0739068  -0.0630348  329  VAL B CB  
7607  C  CG1 . VAL B 329 ? 0.312424  0.380922 0.278626 0.0462441   -0.0640397  -0.0531951  329  VAL B CG1 
7608  C  CG2 . VAL B 329 ? 0.33535   0.425488 0.29637  0.0633551   -0.0826128  -0.0636123  329  VAL B CG2 
7609  N  N   . CYS B 330 ? 0.365756  0.451012 0.364235 0.021399    -0.0596127  -0.0731582  330  CYS B N   
7610  C  CA  . CYS B 330 ? 0.413278  0.486186 0.410523 0.0135944   -0.0524816  -0.0724508  330  CYS B CA  
7611  C  C   . CYS B 330 ? 0.40415   0.46079  0.390426 0.0159235   -0.0459329  -0.0614355  330  CYS B C   
7612  O  O   . CYS B 330 ? 0.435118  0.481279 0.413695 0.0144716   -0.0421407  -0.0605099  330  CYS B O   
7613  C  CB  . CYS B 330 ? 0.459552  0.536838 0.473729 0.00268448  -0.0480788  -0.0776931  330  CYS B CB  
7614  S  SG  . CYS B 330 ? 0.623621  0.71209  0.645386 -0.00398013 -0.0530497  -0.093053   330  CYS B SG  
7615  N  N   . HIS B 331 ? 0.342065  0.397586 0.328369 0.0195262   -0.0446594  -0.054151   331  HIS B N   
7616  C  CA  . HIS B 331 ? 0.298822  0.341788 0.279046 0.0196889   -0.0380483  -0.0451145  331  HIS B CA  
7617  C  C   . HIS B 331 ? 0.290209  0.324097 0.254656 0.0233178   -0.0369994  -0.0430099  331  HIS B C   
7618  O  O   . HIS B 331 ? 0.289552  0.324136 0.242699 0.0295708   -0.0418522  -0.043803   331  HIS B O   
7619  C  CB  . HIS B 331 ? 0.294604  0.33743  0.274235 0.0241084   -0.038397   -0.0390884  331  HIS B CB  
7620  C  CG  . HIS B 331 ? 0.317736  0.350573 0.295003 0.0223088   -0.0317371  -0.0317323  331  HIS B CG  
7621  N  ND1 . HIS B 331 ? 0.388668  0.421262 0.375694 0.0174495   -0.0273825  -0.0298606  331  HIS B ND1 
7622  C  CD2 . HIS B 331 ? 0.337951  0.361405 0.303692 0.0245929   -0.0286043  -0.0265009  331  HIS B CD2 
7623  C  CE1 . HIS B 331 ? 0.377085  0.402    0.359488 0.0173155   -0.0228899  -0.0244403  331  HIS B CE1 
7624  N  NE2 . HIS B 331 ? 0.345719  0.365556 0.316247 0.0210155   -0.0231383  -0.0225008  331  HIS B NE2 
7625  N  N   . ALA B 332 ? 0.251961  0.277698 0.214756 0.0201895   -0.0307304  -0.0408007  332  ALA B N   
7626  C  CA  . ALA B 332 ? 0.262281  0.281142 0.211379 0.023048    -0.0286608  -0.0403625  332  ALA B CA  
7627  C  C   . ALA B 332 ? 0.270609  0.284166 0.207314 0.0280044   -0.0270293  -0.0333252  332  ALA B C   
7628  O  O   . ALA B 332 ? 0.265242  0.276765 0.205635 0.0271818   -0.0239611  -0.0275232  332  ALA B O   
7629  C  CB  . ALA B 332 ? 0.259906  0.272712 0.211642 0.0197804   -0.0220268  -0.0398805  332  ALA B CB  
7630  N  N   . SER B 333 ? 0.276604  0.286045 0.197007 0.0327077   -0.0281202  -0.0338093  333  SER B N   
7631  C  CA  . SER B 333 ? 0.296038  0.296957 0.201792 0.0367684   -0.0250704  -0.0265754  333  SER B CA  
7632  C  C   . SER B 333 ? 0.294403  0.288536 0.180818 0.040393    -0.0226825  -0.0267345  333  SER B C   
7633  O  O   . SER B 333 ? 0.284819  0.281928 0.167844 0.0413722   -0.0257448  -0.0334502  333  SER B O   
7634  C  CB  . SER B 333 ? 0.318612  0.3199   0.220873 0.0420499   -0.0312459  -0.0243506  333  SER B CB  
7635  O  OG  . SER B 333 ? 0.332402  0.340102 0.229319 0.0474385   -0.040169   -0.0306036  333  SER B OG  
7636  N  N   . ALA B 334 ? 0.304054  0.288475 0.17851  0.0411157   -0.0157002  -0.0196226  334  ALA B N   
7637  C  CA  . ALA B 334 ? 0.338849  0.315516 0.194062 0.0435188   -0.0103088  -0.0183881  334  ALA B CA  
7638  C  C   . ALA B 334 ? 0.372322  0.336798 0.205601 0.0495658   -0.0108069  -0.0119247  334  ALA B C   
7639  O  O   . ALA B 334 ? 0.361149  0.31991  0.196156 0.0484664   -0.00867994 -0.00603455 334  ALA B O   
7640  C  CB  . ALA B 334 ? 0.303856  0.279339 0.164085 0.0378694   0.00107041  -0.0157387  334  ALA B CB  
7641  N  N   . TRP B 335 ? 0.40617   0.364671 0.217082 0.0558618   -0.0124188  -0.0128301  335  TRP B N   
7642  C  CA  . TRP B 335 ? 0.445717  0.392568 0.232371 0.0648668   -0.0166395  -0.00812929 335  TRP B CA  
7643  C  C   . TRP B 335 ? 0.481505  0.413326 0.240983 0.0669477   -0.00757395 -0.00298369 335  TRP B C   
7644  O  O   . TRP B 335 ? 0.473244  0.408067 0.225902 0.0673156   -0.0058287  -0.007838   335  TRP B O   
7645  C  CB  . TRP B 335 ? 0.459143  0.415892 0.243401 0.0725596   -0.0305637  -0.0161742  335  TRP B CB  
7646  C  CG  . TRP B 335 ? 0.487008  0.458434 0.296106 0.0707884   -0.0389105  -0.0211764  335  TRP B CG  
7647  C  CD1 . TRP B 335 ? 0.467975  0.451873 0.303329 0.0623234   -0.0383709  -0.0265857  335  TRP B CD1 
7648  C  CD2 . TRP B 335 ? 0.48785   0.462431 0.295998 0.0786498   -0.0487946  -0.021189   335  TRP B CD2 
7649  N  NE1 . TRP B 335 ? 0.470812  0.465319 0.321574 0.0631783   -0.0461471  -0.0296767  335  TRP B NE1 
7650  C  CE2 . TRP B 335 ? 0.452729  0.443443 0.288739 0.0732599   -0.0528838  -0.0270773  335  TRP B CE2 
7651  C  CE3 . TRP B 335 ? 0.508495  0.473264 0.293635 0.0906214   -0.054435   -0.0168718  335  TRP B CE3 
7652  C  CZ2 . TRP B 335 ? 0.458693  0.458787 0.302616 0.0788834   -0.0620524  -0.0296323  335  TRP B CZ2 
7653  C  CZ3 . TRP B 335 ? 0.491118  0.464641 0.284079 0.0973992   -0.0644854  -0.0192727  335  TRP B CZ3 
7654  C  CH2 . TRP B 335 ? 0.468946  0.46097  0.291858 0.0913099   -0.0679279  -0.0258345  335  TRP B CH2 
7655  N  N   . ASP B 336 ? 0.507616  0.422116 0.251585 0.0675225   -0.00057527 0.00674093  336  ASP B N   
7656  C  CA  . ASP B 336 ? 0.529291  0.425265 0.242863 0.0698775   0.0089202   0.0133817   336  ASP B CA  
7657  C  C   . ASP B 336 ? 0.58079   0.461983 0.2657   0.0828407   0.00061092  0.0178167   336  ASP B C   
7658  O  O   . ASP B 336 ? 0.568753  0.442683 0.254113 0.0860597   -0.0032299  0.0223592   336  ASP B O   
7659  C  CB  . ASP B 336 ? 0.545328  0.429664 0.260104 0.0603623   0.0240876   0.021197    336  ASP B CB  
7660  C  CG  . ASP B 336 ? 0.588537  0.453793 0.274032 0.0596332   0.037587    0.0280442   336  ASP B CG  
7661  O  OD1 . ASP B 336 ? 0.593233  0.449766 0.251087 0.0688414   0.0345556   0.0286848   336  ASP B OD1 
7662  O  OD2 . ASP B 336 ? 0.657107  0.517363 0.348092 0.0492746   0.0515714   0.0320733   336  ASP B OD2 
7663  N  N   . PHE B 337 ? 0.590747  0.467623 0.250092 0.0913702   -0.0027841  0.0160009   337  PHE B N   
7664  C  CA  . PHE B 337 ? 0.629753  0.494491 0.261059 0.105999    -0.0128955  0.0192587   337  PHE B CA  
7665  C  C   . PHE B 337 ? 0.655488  0.489606 0.250377 0.109165    -0.00136404 0.0317987   337  PHE B C   
7666  O  O   . PHE B 337 ? 0.715113  0.534634 0.280725 0.122626    -0.00832952 0.0360112   337  PHE B O   
7667  C  CB  . PHE B 337 ? 0.628259  0.505425 0.250221 0.115132    -0.0253943  0.00957426  337  PHE B CB  
7668  C  CG  . PHE B 337 ? 0.576469  0.480464 0.229086 0.114626    -0.0394999  -0.00270246 337  PHE B CG  
7669  C  CD1 . PHE B 337 ? 0.539162  0.459958 0.223719 0.102364    -0.0360357  -0.00970949 337  PHE B CD1 
7670  C  CD2 . PHE B 337 ? 0.575146  0.48777  0.224041 0.126546    -0.0559238  -0.00780672 337  PHE B CD2 
7671  C  CE1 . PHE B 337 ? 0.507459  0.449821 0.217739 0.100859    -0.0473217  -0.0205159  337  PHE B CE1 
7672  C  CE2 . PHE B 337 ? 0.543159  0.481415 0.221475 0.124271    -0.0673666  -0.0198702  337  PHE B CE2 
7673  C  CZ  . PHE B 337 ? 0.508464  0.46027  0.216793 0.110765    -0.0624437  -0.0259204  337  PHE B CZ  
7674  N  N   . TYR B 338 ? 0.685965  0.50994  0.282068 0.0970836   0.0162574   0.0376529   338  TYR B N   
7675  C  CA  . TYR B 338 ? 0.782415  0.575754 0.345362 0.097053    0.0300618   0.0496593   338  TYR B CA  
7676  C  C   . TYR B 338 ? 0.849037  0.628257 0.370572 0.109264    0.0285561   0.0519311   338  TYR B C   
7677  O  O   . TYR B 338 ? 0.858888  0.612475 0.34628  0.11988     0.0275035   0.0608568   338  TYR B O   
7678  C  CB  . TYR B 338 ? 0.794367  0.567151 0.350737 0.0994798   0.0300408   0.0585516   338  TYR B CB  
7679  C  CG  . TYR B 338 ? 0.763504  0.550222 0.358692 0.0887216   0.0301566   0.0555982   338  TYR B CG  
7680  C  CD1 . TYR B 338 ? 0.776544  0.560519 0.386185 0.0728717   0.0460515   0.0581753   338  TYR B CD1 
7681  C  CD2 . TYR B 338 ? 0.767487  0.572176 0.385595 0.0939852   0.0147025   0.0492626   338  TYR B CD2 
7682  C  CE1 . TYR B 338 ? 0.782083  0.580438 0.426398 0.0634137   0.045593    0.0545117   338  TYR B CE1 
7683  C  CE2 . TYR B 338 ? 0.73827   0.555701 0.389958 0.0842927   0.0153482   0.0463849   338  TYR B CE2 
7684  C  CZ  . TYR B 338 ? 0.750172  0.563739 0.413836 0.0695209   0.0303231   0.049174    338  TYR B CZ  
7685  O  OH  . TYR B 338 ? 0.776527  0.601736 0.470859 0.0603503   0.0310068   0.0463147   338  TYR B OH  
7686  N  N   . ASN B 339 ? 0.881415  0.676521 0.404765 0.108882    0.0276245   0.0435336   339  ASN B N   
7687  C  CA  . ASN B 339 ? 0.891189  0.675819 0.377276 0.118294    0.0282425   0.0439657   339  ASN B CA  
7688  C  C   . ASN B 339 ? 0.906727  0.692503 0.392295 0.1071      0.0463837   0.0432715   339  ASN B C   
7689  O  O   . ASN B 339 ? 0.870685  0.646641 0.32476  0.112672    0.0510662   0.0440699   339  ASN B O   
7690  C  CB  . ASN B 339 ? 0.942909  0.752662 0.440015 0.123377    0.0142784   0.0300223   339  ASN B CB  
7691  C  CG  . ASN B 339 ? 0.943471  0.76197  0.439222 0.137191    -0.00741006 0.024619    339  ASN B CG  
7692  O  OD1 . ASN B 339 ? 0.952291  0.755171 0.430955 0.146665    -0.0126412  0.0323282   339  ASN B OD1 
7693  N  ND2 . ASN B 339 ? 0.865155  0.708481 0.379533 0.138352    -0.0198464  0.0109767   339  ASN B ND2 
7694  N  N   . ARG B 340 ? 0.836879  0.638832 0.359387 0.0925277   0.0547681   0.0397074   340  ARG B N   
7695  C  CA  . ARG B 340 ? 0.874353  0.686063 0.405362 0.0828961   0.0691434   0.0355487   340  ARG B CA  
7696  C  C   . ARG B 340 ? 0.855925  0.687556 0.39337  0.0880316   0.0594163   0.0228575   340  ARG B C   
7697  O  O   . ARG B 340 ? 0.905486  0.74553  0.448006 0.0825597   0.0699113   0.0181462   340  ARG B O   
7698  C  CB  . ARG B 340 ? 0.918998  0.706797 0.415757 0.0801631   0.0885862   0.0451258   340  ARG B CB  
7699  C  CG  . ARG B 340 ? 0.976269  0.738753 0.460687 0.0748831   0.0994262   0.0579041   340  ARG B CG  
7700  C  CD  . ARG B 340 ? 1.02049   0.762767 0.479815 0.0667323   0.122937    0.066066    340  ARG B CD  
7701  N  NE  . ARG B 340 ? 1.20851   0.935637 0.624508 0.0769103   0.12607     0.0685149   340  ARG B NE  
7702  C  CZ  . ARG B 340 ? 1.22985   0.934677 0.604673 0.0928187   0.116471    0.0744227   340  ARG B CZ  
7703  N  NH1 . ARG B 340 ? 1.24714   0.941165 0.617131 0.101982    0.102148    0.0788382   340  ARG B NH1 
7704  N  NH2 . ARG B 340 ? 1.2788    0.972922 0.616564 0.100529    0.121023    0.0753831   340  ARG B NH2 
7705  N  N   . LYS B 341 ? 0.815823  0.655785 0.354936 0.0979438   0.0398505   0.0164974   341  LYS B N   
7706  C  CA  . LYS B 341 ? 0.828054  0.683514 0.368937 0.103425    0.0290596   0.00395869  341  LYS B CA  
7707  C  C   . LYS B 341 ? 0.7707    0.648642 0.349142 0.100895    0.0148402   -0.00595621 341  LYS B C   
7708  O  O   . LYS B 341 ? 0.732941  0.626197 0.330541 0.0965985   0.0140309   -0.016039   341  LYS B O   
7709  C  CB  . LYS B 341 ? 0.90359   0.749234 0.407612 0.118779    0.0168636   0.00320097  341  LYS B CB  
7710  C  CG  . LYS B 341 ? 1.0167    0.841397 0.475892 0.124835    0.0275043   0.00935189  341  LYS B CG  
7711  C  CD  . LYS B 341 ? 1.10888   0.922977 0.532096 0.142073    0.0122831   0.0100826   341  LYS B CD  
7712  C  CE  . LYS B 341 ? 1.14234   0.942196 0.520652 0.151496    0.0160979   0.0106107   341  LYS B CE  
7713  N  NZ  . LYS B 341 ? 1.16441   0.932531 0.498725 0.158728    0.0248765   0.0257551   341  LYS B NZ  
7714  N  N   . ASP B 342 ? 0.711744  0.590598 0.298647 0.104336    0.00362392  -0.00351435 342  ASP B N   
7715  C  CA  . ASP B 342 ? 0.673892  0.57364  0.293646 0.102148    -0.00948425 -0.0131145  342  ASP B CA  
7716  C  C   . ASP B 342 ? 0.616722  0.523495 0.270594 0.0907899   -0.0036364  -0.0103541  342  ASP B C   
7717  O  O   . ASP B 342 ? 0.595028  0.491892 0.248674 0.0894491   0.00013082  -0.00115112 342  ASP B O   
7718  C  CB  . ASP B 342 ? 0.688707  0.592387 0.301386 0.113342    -0.027384   -0.0163457  342  ASP B CB  
7719  C  CG  . ASP B 342 ? 0.767412  0.670677 0.352062 0.124456    -0.036459   -0.0230672  342  ASP B CG  
7720  O  OD1 . ASP B 342 ? 0.772383  0.656768 0.32031  0.133769    -0.033921   -0.0151199  342  ASP B OD1 
7721  O  OD2 . ASP B 342 ? 0.777426  0.697892 0.376471 0.123056    -0.0450372  -0.0362406  342  ASP B OD2 
7722  N  N   . PHE B 343 ? 0.560761  0.483927 0.242669 0.0835388   -0.00409917 -0.0190852  343  PHE B N   
7723  C  CA  . PHE B 343 ? 0.522641  0.454854 0.237238 0.0736824   -7.965e-05  -0.0184834  343  PHE B CA  
7724  C  C   . PHE B 343 ? 0.482086  0.430933 0.220892 0.071387    -0.00980311 -0.029664   343  PHE B C   
7725  O  O   . PHE B 343 ? 0.466355  0.419234 0.200684 0.0729405   -0.0121017  -0.0382252  343  PHE B O   
7726  C  CB  . PHE B 343 ? 0.534462  0.465798 0.253977 0.0662191   0.0155416   -0.0165692  343  PHE B CB  
7727  C  CG  . PHE B 343 ? 0.564485  0.479311 0.258215 0.0666031   0.0282138   -0.00718565 343  PHE B CG  
7728  C  CD1 . PHE B 343 ? 0.561414  0.466373 0.255714 0.0622655   0.0350102   0.00249273  343  PHE B CD1 
7729  C  CD2 . PHE B 343 ? 0.609953  0.517692 0.27757  0.0708145   0.0341016   -0.00827104 343  PHE B CD2 
7730  C  CE1 . PHE B 343 ? 0.595368  0.482696 0.265229 0.0610972   0.048102    0.0111957   343  PHE B CE1 
7731  C  CE2 . PHE B 343 ? 0.6317    0.522596 0.274012 0.0702961   0.0473797   0.00087265  343  PHE B CE2 
7732  C  CZ  . PHE B 343 ? 0.618049  0.498225 0.261715 0.0649254   0.054732    0.0107424   343  PHE B CZ  
7733  N  N   . ARG B 344 ? 0.438447  0.395567 0.200822 0.067875    -0.0155863  -0.0300113  344  ARG B N   
7734  C  CA  . ARG B 344 ? 0.403566  0.37419  0.184943 0.0659075   -0.0250824  -0.040397   344  ARG B CA  
7735  C  C   . ARG B 344 ? 0.380386  0.358137 0.190268 0.0583539   -0.0238823  -0.039142   344  ARG B C   
7736  O  O   . ARG B 344 ? 0.379744  0.35347  0.193484 0.0566455   -0.0195856  -0.0309222  344  ARG B O   
7737  C  CB  . ARG B 344 ? 0.417958  0.394439 0.19375  0.0729633   -0.0393027  -0.0451346  344  ARG B CB  
7738  C  CG  . ARG B 344 ? 0.443706  0.414975 0.189963 0.0824783   -0.0442702  -0.0479399  344  ARG B CG  
7739  C  CD  . ARG B 344 ? 0.455245  0.435661 0.199373 0.0903099   -0.0595663  -0.0530731  344  ARG B CD  
7740  N  NE  . ARG B 344 ? 0.493681  0.468305 0.206487 0.100596    -0.064554   -0.0555729  344  ARG B NE  
7741  C  CZ  . ARG B 344 ? 0.519555  0.501426 0.221709 0.110631    -0.0786935  -0.0612343  344  ARG B CZ  
7742  N  NH1 . ARG B 344 ? 0.504448  0.500291 0.226802 0.111206    -0.0881549  -0.0645395  344  ARG B NH1 
7743  N  NH2 . ARG B 344 ? 0.532004  0.507563 0.20298  0.120682    -0.083077   -0.0633221  344  ARG B NH2 
7744  N  N   . ILE B 345 ? 0.370675  0.35746  0.198522 0.053893    -0.0275523  -0.0475883  345  ILE B N   
7745  C  CA  . ILE B 345 ? 0.335909  0.329003 0.188589 0.0474626   -0.0275328  -0.0470784  345  ILE B CA  
7746  C  C   . ILE B 345 ? 0.333778  0.337113 0.196597 0.0470897   -0.0384906  -0.0553999  345  ILE B C   
7747  O  O   . ILE B 345 ? 0.337392  0.343727 0.194024 0.0487388   -0.0439932  -0.0641425  345  ILE B O   
7748  C  CB  . ILE B 345 ? 0.313109  0.305646 0.178111 0.0418493   -0.0198592  -0.0487932  345  ILE B CB  
7749  C  CG1 . ILE B 345 ? 0.310076  0.29774  0.172795 0.0409022   -0.00900212 -0.0404405  345  ILE B CG1 
7750  C  CG2 . ILE B 345 ? 0.285127  0.283456 0.172744 0.0359637   -0.0222839  -0.0514047  345  ILE B CG2 
7751  C  CD1 . ILE B 345 ? 0.286967  0.27547  0.158729 0.0382703   -0.00174493 -0.0428923  345  ILE B CD1 
7752  N  N   . LYS B 346 ? 0.322478  0.331824 0.200807 0.0447045   -0.0411551  -0.0531781  346  LYS B N   
7753  C  CA  . LYS B 346 ? 0.341107  0.362647 0.233941 0.0423923   -0.0495094  -0.0612962  346  LYS B CA  
7754  C  C   . LYS B 346 ? 0.314346  0.337142 0.227981 0.0338111   -0.0443169  -0.0606164  346  LYS B C   
7755  O  O   . LYS B 346 ? 0.314974  0.336829 0.23523  0.0330173   -0.0410843  -0.0532945  346  LYS B O   
7756  C  CB  . LYS B 346 ? 0.344273  0.372058 0.234265 0.0492109   -0.0572261  -0.0591885  346  LYS B CB  
7757  C  CG  . LYS B 346 ? 0.343452  0.387211 0.252883 0.0462462   -0.0644709  -0.0671005  346  LYS B CG  
7758  C  CD  . LYS B 346 ? 0.35009   0.399722 0.259612 0.0536371   -0.0703025  -0.0635644  346  LYS B CD  
7759  C  CE  . LYS B 346 ? 0.371324  0.413206 0.28576  0.0520951   -0.0632402  -0.0532398  346  LYS B CE  
7760  N  NZ  . LYS B 346 ? 0.350384  0.395429 0.284594 0.0414522   -0.0574772  -0.0550231  346  LYS B NZ  
7761  N  N   . GLN B 347 ? 0.301244  0.324135 0.222921 0.0278442   -0.0432668  -0.0680338  347  GLN B N   
7762  C  CA  . GLN B 347 ? 0.308892  0.329311 0.246294 0.0206754   -0.0376531  -0.0665067  347  GLN B CA  
7763  C  C   . GLN B 347 ? 0.324573  0.349307 0.272814 0.0138613   -0.0406704  -0.0767981  347  GLN B C   
7764  O  O   . GLN B 347 ? 0.330247  0.353874 0.272    0.0135908   -0.0434497  -0.0852261  347  GLN B O   
7765  C  CB  . GLN B 347 ? 0.292293  0.301726 0.225668 0.0207623   -0.029026   -0.0614647  347  GLN B CB  
7766  C  CG  . GLN B 347 ? 0.293053  0.298525 0.239637 0.0153409   -0.024198   -0.0598196  347  GLN B CG  
7767  C  CD  . GLN B 347 ? 0.308338  0.306195 0.252006 0.0175609   -0.0170034  -0.0549179  347  GLN B CD  
7768  O  OE1 . GLN B 347 ? 0.293721  0.291078 0.228063 0.0219375   -0.0143666  -0.0516859  347  GLN B OE1 
7769  N  NE2 . GLN B 347 ? 0.306471  0.298845 0.258093 0.014761    -0.0135584  -0.0542987  347  GLN B NE2 
7770  N  N   . CYS B 348 ? 0.296579  0.326185 0.260628 0.00792971  -0.0398206  -0.0767407  348  CYS B N   
7771  C  CA  . CYS B 348 ? 0.314843  0.346521 0.289852 -0.00077027 -0.0402273  -0.0862362  348  CYS B CA  
7772  C  C   . CYS B 348 ? 0.323077  0.338256 0.29785  -0.00532369 -0.0320377  -0.084425   348  CYS B C   
7773  O  O   . CYS B 348 ? 0.307088  0.318073 0.291101 -0.0109867  -0.0272078  -0.0818596  348  CYS B O   
7774  C  CB  . CYS B 348 ? 0.324995  0.370007 0.316395 -0.00559143 -0.0422134  -0.0882884  348  CYS B CB  
7775  S  SG  . CYS B 348 ? 0.363534  0.428826 0.354357 0.00205761  -0.0537487  -0.093073   348  CYS B SG  
7776  N  N   . THR B 349 ? 0.333438  0.33851  0.295762 -0.00145337 -0.0302607  -0.085181   349  THR B N   
7777  C  CA  . THR B 349 ? 0.342496  0.331879 0.301514 -0.00110056 -0.0227316  -0.0809937  349  THR B CA  
7778  C  C   . THR B 349 ? 0.325393  0.30457  0.291099 -0.00965585 -0.019351   -0.0862237  349  THR B C   
7779  O  O   . THR B 349 ? 0.338731  0.317314 0.304568 -0.0146259  -0.0218187  -0.0963499  349  THR B O   
7780  C  CB  . THR B 349 ? 0.345972  0.327924 0.29104  0.00448753  -0.0216763  -0.0837939  349  THR B CB  
7781  O  OG1 . THR B 349 ? 0.330593  0.321326 0.267729 0.0110555   -0.0244599  -0.0797936  349  THR B OG1 
7782  C  CG2 . THR B 349 ? 0.361659  0.330116 0.30377  0.00752089  -0.0144051  -0.0792609  349  THR B CG2 
7783  N  N   . ARG B 350 ? 0.314567  0.283836 0.283368 -0.0106696  -0.0133648  -0.0793178  350  ARG B N   
7784  C  CA  . ARG B 350 ? 0.348869  0.301167 0.31843  -0.0168359  -0.00789756 -0.0815675  350  ARG B CA  
7785  C  C   . ARG B 350 ? 0.342936  0.277499 0.301839 -0.010023   -0.00317423 -0.0782601  350  ARG B C   
7786  O  O   . ARG B 350 ? 0.324642  0.263096 0.280003 -0.00163173 -0.00298642 -0.072167   350  ARG B O   
7787  C  CB  . ARG B 350 ? 0.323225  0.276889 0.301539 -0.0211022  -0.00474382 -0.075202   350  ARG B CB  
7788  C  CG  . ARG B 350 ? 0.361025  0.331112 0.351479 -0.0290135  -0.00830434 -0.0811853  350  ARG B CG  
7789  C  CD  . ARG B 350 ? 0.363919  0.338874 0.363486 -0.0328189  -0.00512749 -0.0754341  350  ARG B CD  
7790  N  NE  . ARG B 350 ? 0.392896  0.375834 0.391994 -0.0248263  -0.00669155 -0.0660136  350  ARG B NE  
7791  C  CZ  . ARG B 350 ? 0.371615  0.344209 0.365026 -0.0200272  -0.00279991 -0.0574175  350  ARG B CZ  
7792  N  NH1 . ARG B 350 ? 0.438468  0.392119 0.425891 -0.0216497  0.00289098  -0.0559231  350  ARG B NH1 
7793  N  NH2 . ARG B 350 ? 0.350543  0.330686 0.343232 -0.0131734  -0.00475867 -0.0508107  350  ARG B NH2 
7794  N  N   . VAL B 351 ? 0.375011  0.289668 0.329211 -0.013681   0.00110888  -0.0825067  351  VAL B N   
7795  C  CA  . VAL B 351 ? 0.394075  0.290958 0.33776  -0.00565362 0.00525409  -0.0800221  351  VAL B CA  
7796  C  C   . VAL B 351 ? 0.396348  0.283002 0.339536 -0.00251705 0.00966797  -0.0703666  351  VAL B C   
7797  O  O   . VAL B 351 ? 0.397722  0.264495 0.336969 -0.00677522 0.0143795   -0.0701524  351  VAL B O   
7798  C  CB  . VAL B 351 ? 0.435973  0.313604 0.371972 -0.00950628 0.00741574  -0.0897706  351  VAL B CB  
7799  C  CG1 . VAL B 351 ? 0.455844  0.314077 0.380186 0.00074214  0.0116201   -0.0875408  351  VAL B CG1 
7800  C  CG2 . VAL B 351 ? 0.421691  0.310908 0.356888 -0.0117613  0.00196674  -0.10023    351  VAL B CG2 
7801  N  N   . THR B 352 ? 0.364765  0.263989 0.31057  0.00515165  0.00831765  -0.0625431  352  THR B N   
7802  C  CA  . THR B 352 ? 0.366744  0.259867 0.311544 0.0101441   0.0109117   -0.0538485  352  THR B CA  
7803  C  C   . THR B 352 ? 0.345806  0.249269 0.290266 0.0214778   0.00965214  -0.0500208  352  THR B C   
7804  O  O   . THR B 352 ? 0.348914  0.266756 0.295577 0.0230064   0.00740066  -0.052478   352  THR B O   
7805  C  CB  . THR B 352 ? 0.373799  0.275532 0.326489 0.00392489  0.0106278   -0.0488736  352  THR B CB  
7806  O  OG1 . THR B 352 ? 0.344193  0.268437 0.304338 0.00550263  0.00624793  -0.0474352  352  THR B OG1 
7807  C  CG2 . THR B 352 ? 0.357485  0.254843 0.314136 -0.00854001 0.0124508   -0.0535745  352  THR B CG2 
7808  N  N   . MET B 353 ? 0.352075  0.248607 0.293365 0.0295182   0.0112812   -0.0443903  353  MET B N   
7809  C  CA  . MET B 353 ? 0.373443  0.283863 0.317889 0.039359    0.0100617   -0.0415069  353  MET B CA  
7810  C  C   . MET B 353 ? 0.357495  0.290689 0.312118 0.0360245   0.00737789  -0.038286   353  MET B C   
7811  O  O   . MET B 353 ? 0.348609  0.296126 0.306767 0.0391637   0.00698166  -0.0390909  353  MET B O   
7812  C  CB  . MET B 353 ? 0.407838  0.308323 0.347546 0.0491981   0.0109495   -0.0368057  353  MET B CB  
7813  C  CG  . MET B 353 ? 0.445554  0.363191 0.390815 0.05977     0.00955254  -0.0359955  353  MET B CG  
7814  S  SD  . MET B 353 ? 0.505292  0.412814 0.444549 0.0729912   0.00861244  -0.0311258  353  MET B SD  
7815  C  CE  . MET B 353 ? 0.51082   0.443481 0.460429 0.0840931   0.00731396  -0.0343133  353  MET B CE  
7816  N  N   . ASP B 354 ? 0.362478  0.298484 0.321294 0.0290773   0.00623581  -0.0350968  354  ASP B N   
7817  C  CA  . ASP B 354 ? 0.371117  0.325781 0.338134 0.0266742   0.00383593  -0.032262   354  ASP B CA  
7818  C  C   . ASP B 354 ? 0.327455  0.29135  0.295602 0.0226927   0.00221969  -0.0361847  354  ASP B C   
7819  O  O   . ASP B 354 ? 0.292744  0.269308 0.263919 0.0236316   0.00138062  -0.0344828  354  ASP B O   
7820  C  CB  . ASP B 354 ? 0.466689  0.422241 0.437323 0.0217599   0.00318707  -0.0282092  354  ASP B CB  
7821  C  CG  . ASP B 354 ? 0.694972  0.646293 0.666724 0.0125738   0.00344902  -0.0312253  354  ASP B CG  
7822  O  OD1 . ASP B 354 ? 0.676548  0.611821 0.643258 0.00964256  0.00641492  -0.0329235  354  ASP B OD1 
7823  O  OD2 . ASP B 354 ? 0.693951  0.657877 0.671652 0.00830814  0.00087825  -0.0323995  354  ASP B OD2 
7824  N  N   . GLN B 355 ? 0.31493   0.271588 0.279579 0.0181806   0.0017931   -0.0417027  355  GLN B N   
7825  C  CA  . GLN B 355 ? 0.30197   0.266331 0.264946 0.0162314   -0.00068271 -0.0461403  355  GLN B CA  
7826  C  C   . GLN B 355 ? 0.28644   0.25262  0.24352  0.0226385   0.00105631  -0.0477311  355  GLN B C   
7827  O  O   . GLN B 355 ? 0.276193  0.251233 0.230741 0.0231305   -1.782e-05  -0.048076   355  GLN B O   
7828  C  CB  . GLN B 355 ? 0.307217  0.264516 0.268876 0.00971798  -0.00205842 -0.0531919  355  GLN B CB  
7829  C  CG  . GLN B 355 ? 0.320074  0.283474 0.290009 0.0026078   -0.00396457 -0.0525145  355  GLN B CG  
7830  C  CD  . GLN B 355 ? 0.305625  0.284524 0.278102 0.00214109  -0.00898588 -0.0538404  355  GLN B CD  
7831  O  OE1 . GLN B 355 ? 0.305108  0.28699  0.274545 0.0010174   -0.0123414  -0.0605503  355  GLN B OE1 
7832  N  NE2 . GLN B 355 ? 0.272442  0.259963 0.248296 0.00445899  -0.00968309 -0.0474857  355  GLN B NE2 
7833  N  N   . LEU B 356 ? 0.308288  0.264747 0.261673 0.0279979   0.00414788  -0.0491492  356  LEU B N   
7834  C  CA  . LEU B 356 ? 0.293116  0.253484 0.242562 0.0347417   0.006802    -0.0509549  356  LEU B CA  
7835  C  C   . LEU B 356 ? 0.271144  0.24738  0.226534 0.0367451   0.00806904  -0.0458368  356  LEU B C   
7836  O  O   . LEU B 356 ? 0.2709    0.254986 0.223067 0.0377204   0.0100619   -0.0467517  356  LEU B O   
7837  C  CB  . LEU B 356 ? 0.312316  0.260278 0.25785  0.0417671   0.00964421  -0.0533547  356  LEU B CB  
7838  C  CG  . LEU B 356 ? 0.325609  0.278753 0.267776 0.0493421   0.013041    -0.0567118  356  LEU B CG  
7839  C  CD1 . LEU B 356 ? 0.345043  0.298073 0.278573 0.0468327   0.0130481   -0.0626693  356  LEU B CD1 
7840  C  CD2 . LEU B 356 ? 0.354883  0.29269  0.292989 0.0571592   0.0148642   -0.0589934  356  LEU B CD2 
7841  N  N   A SER B 357 ? 0.252016  0.23219  0.215095 0.0368436   0.00741428  -0.0407379  357  SER B N   
7842  N  N   B SER B 357 ? 0.256714  0.236828 0.219822 0.036495    0.00726031  -0.0406625  357  SER B N   
7843  C  CA  A SER B 357 ? 0.253933  0.248417 0.223775 0.0362017   0.00810049  -0.0365961  357  SER B CA  
7844  C  CA  B SER B 357 ? 0.247018  0.241394 0.217033 0.0360825   0.00797719  -0.0364584  357  SER B CA  
7845  C  C   A SER B 357 ? 0.235179  0.234377 0.203074 0.0304118   0.00668423  -0.0350948  357  SER B C   
7846  C  C   B SER B 357 ? 0.2349    0.234072 0.202806 0.0304293   0.00668644  -0.0351011  357  SER B C   
7847  O  O   A SER B 357 ? 0.236976  0.243977 0.204226 0.0302353   0.00937476  -0.0338026  357  SER B O   
7848  O  O   B SER B 357 ? 0.23396   0.240957 0.201223 0.0303544   0.00944742  -0.0338724  357  SER B O   
7849  C  CB  A SER B 357 ? 0.261637  0.25828  0.238861 0.0371555   0.0065208   -0.032412   357  SER B CB  
7850  C  CB  B SER B 357 ? 0.243336  0.239832 0.22057  0.0364893   0.00627181  -0.0321876  357  SER B CB  
7851  O  OG  A SER B 357 ? 0.271752  0.267002 0.249698 0.0452539   0.00784902  -0.0337752  357  SER B OG  
7852  O  OG  B SER B 357 ? 0.241378  0.251935 0.226049 0.03859     0.00790875  -0.0306919  357  SER B OG  
7853  N  N   . THR B 358 ? 0.228044  0.222377 0.194718 0.0259419   0.00285665  -0.0354087  358  THR B N   
7854  C  CA  . THR B 358 ? 0.232711  0.231324 0.196557 0.022713    0.00049271  -0.0344405  358  THR B CA  
7855  C  C   . THR B 358 ? 0.228399  0.226683 0.181705 0.0247851   0.00176189  -0.0374867  358  THR B C   
7856  O  O   . THR B 358 ? 0.22432   0.225928 0.17238  0.024612    0.00214226  -0.03502    358  THR B O   
7857  C  CB  . THR B 358 ? 0.272012  0.268291 0.237733 0.0184727   -0.00411784 -0.036212   358  THR B CB  
7858  O  OG1 . THR B 358 ? 0.25626   0.253494 0.230016 0.0169111   -0.00394774 -0.0322777  358  THR B OG1 
7859  C  CG2 . THR B 358 ? 0.289732  0.291591 0.252454 0.0174977   -0.00756893 -0.0352929  358  THR B CG2 
7860  N  N   . VAL B 359 ? 0.224705  0.216741 0.172681 0.0265848   0.0020124   -0.0431433  359  VAL B N   
7861  C  CA  . VAL B 359 ? 0.244852  0.236272 0.180994 0.0291107   0.0033215   -0.0466036  359  VAL B CA  
7862  C  C   . VAL B 359 ? 0.241767  0.238926 0.175842 0.0318904   0.00982106  -0.0433697  359  VAL B C   
7863  O  O   . VAL B 359 ? 0.243098  0.241513 0.167274 0.032132    0.0114187   -0.041963   359  VAL B O   
7864  C  CB  . VAL B 359 ? 0.246226  0.228855 0.17797  0.0307132   0.00316872  -0.0540192  359  VAL B CB  
7865  C  CG1 . VAL B 359 ? 0.268269  0.249958 0.187128 0.0346729   0.005839    -0.0582691  359  VAL B CG1 
7866  C  CG2 . VAL B 359 ? 0.260634  0.239305 0.193038 0.0257523   -0.00295421 -0.0586688  359  VAL B CG2 
7867  N  N   . HIS B 360 ? 0.223641  0.224716 0.167151 0.0338726   0.0136517   -0.0421105  360  HIS B N   
7868  C  CA  . HIS B 360 ? 0.238656  0.248764 0.184333 0.0351351   0.0203327   -0.0401188  360  HIS B CA  
7869  C  C   . HIS B 360 ? 0.22988   0.24446  0.177051 0.0303592   0.0210974   -0.0342368  360  HIS B C   
7870  O  O   . HIS B 360 ? 0.238246  0.254825 0.178708 0.0292007   0.0264522   -0.0325839  360  HIS B O   
7871  C  CB  . HIS B 360 ? 0.223979  0.240625 0.18189  0.0389339   0.0227108   -0.0409527  360  HIS B CB  
7872  C  CG  . HIS B 360 ? 0.235118  0.247595 0.189487 0.0454598   0.0246241   -0.0467493  360  HIS B CG  
7873  N  ND1 . HIS B 360 ? 0.245444  0.244842 0.195852 0.0472742   0.0205153   -0.0498031  360  HIS B ND1 
7874  C  CD2 . HIS B 360 ? 0.244784  0.263074 0.197783 0.0503286   0.0307244   -0.0505886  360  HIS B CD2 
7875  C  CE1 . HIS B 360 ? 0.256697  0.252447 0.203204 0.0536867   0.0234611   -0.0550375  360  HIS B CE1 
7876  N  NE2 . HIS B 360 ? 0.253094  0.261294 0.201391 0.0561804   0.0295411   -0.0557665  360  HIS B NE2 
7877  N  N   . HIS B 361 ? 0.242702  0.256701 0.19669  0.027521    0.0162129   -0.0312015  361  HIS B N   
7878  C  CA  . HIS B 361 ? 0.233204  0.249151 0.187988 0.0234374   0.0166171   -0.0260575  361  HIS B CA  
7879  C  C   . HIS B 361 ? 0.242135  0.251473 0.181319 0.023343    0.0163521   -0.0247067  361  HIS B C   
7880  O  O   . HIS B 361 ? 0.252068  0.260561 0.185049 0.0215175   0.0216514   -0.021192   361  HIS B O   
7881  C  CB  . HIS B 361 ? 0.232024  0.247321 0.194776 0.0214137   0.0108462   -0.0240471  361  HIS B CB  
7882  C  CG  . HIS B 361 ? 0.217355  0.232205 0.17933  0.0180781   0.0104977   -0.019487   361  HIS B CG  
7883  N  ND1 . HIS B 361 ? 0.223309  0.24341  0.193735 0.0151662   0.013331    -0.0171453  361  HIS B ND1 
7884  C  CD2 . HIS B 361 ? 0.232887  0.242111 0.186075 0.0178749   0.00752842  -0.0174282  361  HIS B CD2 
7885  C  CE1 . HIS B 361 ? 0.230357  0.245844 0.196331 0.0126154   0.0129976   -0.013538   361  HIS B CE1 
7886  N  NE2 . HIS B 361 ? 0.243187  0.2517   0.197941 0.0150448   0.00946037  -0.0132781  361  HIS B NE2 
7887  N  N   . GLU B 362 ? 0.248329  0.252643 0.180444 0.025342    0.0104585   -0.0278687  362  GLU B N   
7888  C  CA  . GLU B 362 ? 0.274054  0.273006 0.190367 0.0270589   0.00814095  -0.0271095  362  GLU B CA  
7889  C  C   . GLU B 362 ? 0.287614  0.283917 0.189904 0.0292239   0.0148474   -0.0275063  362  GLU B C   
7890  O  O   . GLU B 362 ? 0.294712  0.285456 0.182638 0.0299893   0.017119    -0.0235251  362  GLU B O   
7891  C  CB  . GLU B 362 ? 0.295739  0.293186 0.208589 0.0287129   -0.00043899 -0.0319675  362  GLU B CB  
7892  C  CG  . GLU B 362 ? 0.308113  0.308907 0.234162 0.0260286   -0.00599003 -0.0317914  362  GLU B CG  
7893  C  CD  . GLU B 362 ? 0.330758  0.331892 0.258456 0.0253293   -0.00650184 -0.0256035  362  GLU B CD  
7894  O  OE1 . GLU B 362 ? 0.33913   0.335847 0.253777 0.0280371   -0.00636488 -0.0225462  362  GLU B OE1 
7895  O  OE2 . GLU B 362 ? 0.330361  0.334444 0.270181 0.0226314   -0.0069154  -0.0237988  362  GLU B OE2 
7896  N  N   . MET B 363 ? 0.266232  0.264916 0.170591 0.0309421   0.0181417   -0.0324633  363  MET B N   
7897  C  CA  . MET B 363 ? 0.291497  0.288651 0.182526 0.0332871   0.0252242   -0.0337382  363  MET B CA  
7898  C  C   . MET B 363 ? 0.284058  0.285122 0.177362 0.0299705   0.0351568   -0.0287417  363  MET B C   
7899  O  O   . MET B 363 ? 0.293935  0.291618 0.172659 0.0304252   0.0422632   -0.0274706  363  MET B O   
7900  C  CB  . MET B 363 ? 0.298367  0.297208 0.19225  0.0366584   0.0265541   -0.0410193  363  MET B CB  
7901  C  CG  . MET B 363 ? 0.35201   0.349272 0.230529 0.0400306   0.0335639   -0.04393    363  MET B CG  
7902  S  SD  . MET B 363 ? 0.379857  0.374136 0.25577  0.0454076   0.03232     -0.0541425  363  MET B SD  
7903  C  CE  . MET B 363 ? 0.394292  0.380702 0.263853 0.0444499   0.0196998   -0.0576835  363  MET B CE  
7904  N  N   . GLY B 364 ? 0.271136  0.279348 0.182203 0.0262473   0.0360105   -0.0265277  364  GLY B N   
7905  C  CA  . GLY B 364 ? 0.274263  0.287286 0.190568 0.0211556   0.0444498   -0.0227206  364  GLY B CA  
7906  C  C   . GLY B 364 ? 0.31231   0.313315 0.211528 0.0187922   0.0463487   -0.0164821  364  GLY B C   
7907  O  O   . GLY B 364 ? 0.315958  0.314393 0.20675  0.0155869   0.0561815   -0.0138552  364  GLY B O   
7908  N  N   . HIS B 365 ? 0.295903  0.288964 0.189178 0.0208401   0.037249    -0.0142906  365  HIS B N   
7909  C  CA  . HIS B 365 ? 0.316975  0.296917 0.192679 0.0208931   0.0376556   -0.00816105 365  HIS B CA  
7910  C  C   . HIS B 365 ? 0.340464  0.311751 0.192319 0.0250581   0.0411414   -0.00783488 365  HIS B C   
7911  O  O   . HIS B 365 ? 0.360471  0.320815 0.195786 0.023591    0.0487361   -0.00229659 365  HIS B O   
7912  C  CB  . HIS B 365 ? 0.308557  0.284347 0.183572 0.0242103   0.0262734   -0.00713564 365  HIS B CB  
7913  C  CG  . HIS B 365 ? 0.3102    0.291145 0.203811 0.0205734   0.0229989   -0.0062135  365  HIS B CG  
7914  N  ND1 . HIS B 365 ? 0.334016  0.313379 0.233038 0.0148892   0.0293268   -0.002374   365  HIS B ND1 
7915  C  CD2 . HIS B 365 ? 0.289954  0.277155 0.197075 0.0212946   0.0148713   -0.00893775 365  HIS B CD2 
7916  C  CE1 . HIS B 365 ? 0.323034  0.307605 0.237266 0.013191    0.0244024   -0.00292816 365  HIS B CE1 
7917  N  NE2 . HIS B 365 ? 0.297234  0.285873 0.21542  0.0172001   0.0160379   -0.00626149 365  HIS B NE2 
7918  N  N   . ILE B 366 ? 0.333879  0.308493 0.182484 0.0300822   0.0359063   -0.0138852  366  ILE B N   
7919  C  CA  . ILE B 366 ? 0.349169  0.31612  0.173758 0.0348289   0.038377    -0.0146697  366  ILE B CA  
7920  C  C   . ILE B 366 ? 0.378826  0.346127 0.198116 0.0315229   0.0527968   -0.0133394  366  ILE B C   
7921  O  O   . ILE B 366 ? 0.403081  0.358719 0.198622 0.0326964   0.0593772   -0.00895586 366  ILE B O   
7922  C  CB  . ILE B 366 ? 0.353474  0.324674 0.177309 0.0398466   0.030424    -0.023178   366  ILE B CB  
7923  C  CG1 . ILE B 366 ? 0.342851  0.315327 0.172055 0.042115    0.0168728   -0.0257422  366  ILE B CG1 
7924  C  CG2 . ILE B 366 ? 0.363658  0.327298 0.161158 0.0449203   0.0337279   -0.0245683  366  ILE B CG2 
7925  C  CD1 . ILE B 366 ? 0.372688  0.336025 0.181209 0.0474294   0.0108756   -0.0218928  366  ILE B CD1 
7926  N  N   . GLN B 367 ? 0.353124  0.333832 0.192686 0.0283419   0.0579333   -0.0176571  367  GLN B N   
7927  C  CA  . GLN B 367 ? 0.382104  0.367274 0.220538 0.0248088   0.0721277   -0.0176469  367  GLN B CA  
7928  C  C   . GLN B 367 ? 0.416003  0.392375 0.246223 0.018012    0.0815168   -0.00968935 367  GLN B C   
7929  O  O   . GLN B 367 ? 0.430199  0.399621 0.242922 0.0161337   0.0932005   -0.00698605 367  GLN B O   
7930  C  CB  . GLN B 367 ? 0.358656  0.361873 0.224091 0.0231859   0.07423     -0.0234309  367  GLN B CB  
7931  C  CG  . GLN B 367 ? 0.360889  0.373916 0.228027 0.0218029   0.0878368   -0.0267951  367  GLN B CG  
7932  C  CD  . GLN B 367 ? 0.400584  0.408068 0.246973 0.0278885   0.0910653   -0.0303863  367  GLN B CD  
7933  O  OE1 . GLN B 367 ? 0.420897  0.425063 0.2524   0.025725    0.10297     -0.0283948  367  GLN B OE1 
7934  N  NE2 . GLN B 367 ? 0.380996  0.386974 0.225348 0.0350125   0.0817806   -0.0362187  367  GLN B NE2 
7935  N  N   . TYR B 368 ? 0.41235   0.388255 0.255258 0.0134586   0.0778825   -0.00610879 368  TYR B N   
7936  C  CA  . TYR B 368 ? 0.42327   0.387893 0.258542 0.00642425  0.0862866   0.0010366   368  TYR B CA  
7937  C  C   . TYR B 368 ? 0.459654  0.402312 0.260587 0.0109211   0.0880959   0.00728997  368  TYR B C   
7938  O  O   . TYR B 368 ? 0.491407  0.424003 0.276377 0.00648956  0.10141     0.0115751   368  TYR B O   
7939  C  CB  . TYR B 368 ? 0.412085  0.375556 0.261008 0.00374898  0.0784846   0.00345129  368  TYR B CB  
7940  C  CG  . TYR B 368 ? 0.418671  0.384465 0.280555 -0.00694137 0.0877341   0.00528065  368  TYR B CG  
7941  C  CD1 . TYR B 368 ? 0.463087  0.419443 0.312832 -0.0143873  0.102507    0.00909834  368  TYR B CD1 
7942  C  CD2 . TYR B 368 ? 0.399125  0.376356 0.285042 -0.0101962  0.0820577   0.00263922  368  TYR B CD2 
7943  C  CE1 . TYR B 368 ? 0.468192  0.427724 0.33177  -0.0258355  0.111357    0.00924409  368  TYR B CE1 
7944  C  CE2 . TYR B 368 ? 0.401807  0.382118 0.300071 -0.0202559  0.0895098   0.00288793  368  TYR B CE2 
7945  C  CZ  . TYR B 368 ? 0.437778  0.409577 0.325895 -0.0286716  0.104176    0.00579052  368  TYR B CZ  
7946  O  OH  . TYR B 368 ? 0.426468  0.402589 0.329204 -0.0401305  0.111558    0.0045093   368  TYR B OH  
7947  N  N   . TYR B 369 ? 0.447561  0.383466 0.237016 0.0198652   0.0748724   0.00735337  369  TYR B N   
7948  C  CA  . TYR B 369 ? 0.499096  0.414746 0.255865 0.0264707   0.073282    0.0131154   369  TYR B CA  
7949  C  C   . TYR B 369 ? 0.543824  0.455067 0.27848  0.0290132   0.0822215   0.0123263   369  TYR B C   
7950  O  O   . TYR B 369 ? 0.581402  0.472984 0.285461 0.0323259   0.086529    0.0189848   369  TYR B O   
7951  C  CB  . TYR B 369 ? 0.484098  0.39883  0.234339 0.0366655   0.0565829   0.0106193   369  TYR B CB  
7952  C  CG  . TYR B 369 ? 0.456466  0.377451 0.226378 0.0371574   0.0446691   0.00954037  369  TYR B CG  
7953  C  CD1 . TYR B 369 ? 0.444808  0.361342 0.22465  0.031448    0.0475341   0.0145057   369  TYR B CD1 
7954  C  CD2 . TYR B 369 ? 0.436398  0.367128 0.213571 0.0431172   0.0310059   0.00299673  369  TYR B CD2 
7955  C  CE1 . TYR B 369 ? 0.432395  0.354736 0.22867  0.0325147   0.0371843   0.0131635   369  TYR B CE1 
7956  C  CE2 . TYR B 369 ? 0.425394  0.362078 0.219294 0.0434799   0.0211869   0.00187838  369  TYR B CE2 
7957  C  CZ  . TYR B 369 ? 0.415694  0.347951 0.218245 0.0387322   0.0243944   0.00727294  369  TYR B CZ  
7958  O  OH  . TYR B 369 ? 0.420775  0.358874 0.239216 0.0390743   0.0159359   0.00612449  369  TYR B OH  
7959  N  N   . LEU B 370 ? 0.521252  0.449077 0.268988 0.0290266   0.0839482   0.00418839  370  LEU B N   
7960  C  CA  . LEU B 370 ? 0.558533  0.484315 0.287273 0.0315032   0.09312     0.00208304  370  LEU B CA  
7961  C  C   . LEU B 370 ? 0.566255  0.490717 0.294499 0.0219104   0.112297    0.00604101  370  LEU B C   
7962  O  O   . LEU B 370 ? 0.593965  0.507445 0.296945 0.0222417   0.123538    0.00910494  370  LEU B O   
7963  C  CB  . LEU B 370 ? 0.532373  0.474809 0.274813 0.0353885   0.0887732   -0.00853047 370  LEU B CB  
7964  C  CG  . LEU B 370 ? 0.511189  0.456101 0.256287 0.0428666   0.0712516   -0.0143543  370  LEU B CG  
7965  C  CD1 . LEU B 370 ? 0.485088  0.444616 0.247551 0.0441853   0.0701921   -0.0244394  370  LEU B CD1 
7966  C  CD2 . LEU B 370 ? 0.564108  0.495358 0.277092 0.0515384   0.0645311   -0.0136395  370  LEU B CD2 
7967  N  N   . GLN B 371 ? 0.541787  0.478176 0.298051 0.0129055   0.116467    0.00541467  371  GLN B N   
7968  C  CA  . GLN B 371 ? 0.566127  0.506355 0.32781  0.0022255   0.134719    0.0067838   371  GLN B CA  
7969  C  C   . GLN B 371 ? 0.607523  0.523262 0.346903 -0.00370969 0.143601    0.0172149   371  GLN B C   
7970  O  O   . GLN B 371 ? 0.591416  0.502967 0.322048 -0.0115241  0.161002    0.0195128   371  GLN B O   
7971  C  CB  . GLN B 371 ? 0.528117  0.493435 0.328378 -0.00506478 0.136811    0.00033288  371  GLN B CB  
7972  C  CG  . GLN B 371 ? 0.517369  0.504924 0.336364 0.00076266  0.13285     -0.0096979  371  GLN B CG  
7973  C  CD  . GLN B 371 ? 0.558879  0.551745 0.367241 0.00285331  0.144799    -0.0139052  371  GLN B CD  
7974  O  OE1 . GLN B 371 ? 0.57278   0.563296 0.372185 -0.00430574 0.161353    -0.0114332  371  GLN B OE1 
7975  N  NE2 . GLN B 371 ? 0.566231  0.565154 0.37433  0.0125401   0.137087    -0.0206571  371  GLN B NE2 
7976  N  N   . TYR B 372 ? 0.578947  0.477573 0.307617 0.00026963  0.132732    0.0233204   372  TYR B N   
7977  C  CA  . TYR B 372 ? 0.623214  0.495427 0.329548 -0.00481999 0.141778    0.0334274   372  TYR B CA  
7978  C  C   . TYR B 372 ? 0.657083  0.502172 0.322249 0.0069198   0.13628     0.0409924   372  TYR B C   
7979  O  O   . TYR B 372 ? 0.697299  0.516351 0.340762 0.0068309   0.138902    0.050151    372  TYR B O   
7980  C  CB  . TYR B 372 ? 0.566106  0.440954 0.296479 -0.0125888  0.138637    0.034079    372  TYR B CB  
7981  C  CG  . TYR B 372 ? 0.537664  0.41481  0.278414 -0.00461422 0.119234    0.0330983   372  TYR B CG  
7982  C  CD1 . TYR B 372 ? 0.534369  0.400261 0.253998 0.0086044   0.106096    0.0354569   372  TYR B CD1 
7983  C  CD2 . TYR B 372 ? 0.506969  0.398575 0.278952 -0.0106912  0.114621    0.0293052   372  TYR B CD2 
7984  C  CE1 . TYR B 372 ? 0.537543  0.408288 0.269224 0.0147793   0.0898028   0.0336374   372  TYR B CE1 
7985  C  CE2 . TYR B 372 ? 0.490131  0.38437  0.271683 -0.0041758  0.0986225   0.0282655   372  TYR B CE2 
7986  C  CZ  . TYR B 372 ? 0.498939  0.382988 0.260918 0.00813263  0.0868311   0.030437    372  TYR B CZ  
7987  O  OH  . TYR B 372 ? 0.503184  0.391027 0.275352 0.0138119   0.0724173   0.0289801   372  TYR B OH  
7988  N  N   . LYS B 373 ? 0.655446  0.505572 0.308331 0.0179116   0.128081    0.0368425   373  LYS B N   
7989  C  CA  . LYS B 373 ? 0.692298  0.52178  0.309739 0.0310373   0.118658    0.0419275   373  LYS B CA  
7990  C  C   . LYS B 373 ? 0.747241  0.547877 0.324479 0.0302961   0.134248    0.0519673   373  LYS B C   
7991  O  O   . LYS B 373 ? 0.783997  0.561833 0.328046 0.0410565   0.127906    0.0587098   373  LYS B O   
7992  C  CB  . LYS B 373 ? 0.687964  0.530997 0.302333 0.0416532   0.106931    0.0334438   373  LYS B CB  
7993  C  CG  . LYS B 373 ? 0.72656   0.569312 0.320931 0.0430554   0.11807     0.0309994   373  LYS B CG  
7994  C  CD  . LYS B 373 ? 0.720591  0.589778 0.339948 0.0444968   0.111843    0.0184417   373  LYS B CD  
7995  C  CE  . LYS B 373 ? 0.731668  0.602642 0.331685 0.0536559   0.108276    0.0120344   373  LYS B CE  
7996  N  NZ  . LYS B 373 ? 0.781277  0.64173  0.356623 0.0509309   0.126905    0.0160202   373  LYS B NZ  
7997  N  N   . ASP B 374 ? 0.757596  0.559081 0.337392 0.0180029   0.154534    0.0529008   374  ASP B N   
7998  C  CA  . ASP B 374 ? 0.850493  0.622633 0.38994  0.0164609   0.171061    0.0627887   374  ASP B CA  
7999  C  C   . ASP B 374 ? 0.866968  0.616673 0.402858 0.00590734  0.18165     0.0719307   374  ASP B C   
8000  O  O   . ASP B 374 ? 0.891712  0.619283 0.403271 -0.00166017 0.200715    0.0794498   374  ASP B O   
8001  C  CB  . ASP B 374 ? 0.857846  0.639744 0.394099 0.010049    0.188916    0.0590724   374  ASP B CB  
8002  C  CG  . ASP B 374 ? 0.914922  0.713111 0.447196 0.0213633   0.180024    0.050427    374  ASP B CG  
8003  O  OD1 . ASP B 374 ? 0.922543  0.707066 0.425345 0.0357779   0.167132    0.0525628   374  ASP B OD1 
8004  O  OD2 . ASP B 374 ? 0.942216  0.767122 0.501473 0.0161253   0.185471    0.0408755   374  ASP B OD2 
8005  N  N   . LEU B 375 ? 0.829604  0.583393 0.388227 0.00534324  0.16965     0.0711426   375  LEU B N   
8006  C  CA  . LEU B 375 ? 0.840283  0.573661 0.39856  -0.00495032 0.17855     0.0781739   375  LEU B CA  
8007  C  C   . LEU B 375 ? 0.898756  0.59863  0.422651 0.00794626  0.168834    0.0881497   375  LEU B C   
8008  O  O   . LEU B 375 ? 0.862307  0.564582 0.376214 0.0243951   0.150519    0.0869332   375  LEU B O   
8009  C  CB  . LEU B 375 ? 0.80125   0.557247 0.404755 -0.0157479  0.175027    0.0713343   375  LEU B CB  
8010  C  CG  . LEU B 375 ? 0.768449  0.555587 0.407757 -0.0301341  0.186457    0.0620601   375  LEU B CG  
8011  C  CD1 . LEU B 375 ? 0.722223  0.520902 0.396273 -0.0419129  0.185806    0.0581952   375  LEU B CD1 
8012  C  CD2 . LEU B 375 ? 0.777783  0.557417 0.400391 -0.0396723  0.209138    0.0645145   375  LEU B CD2 
8013  N  N   . PRO B 376 ? 0.976734  0.643821 0.480595 0.00064421  0.181896    0.0979094   376  PRO B N   
8014  C  CA  . PRO B 376 ? 1.03352   0.669934 0.514118 0.0110125   0.172588    0.106462    376  PRO B CA  
8015  C  C   . PRO B 376 ? 0.990691  0.650567 0.506337 0.0158664   0.152527    0.0989977   376  PRO B C   
8016  O  O   . PRO B 376 ? 0.989457  0.670028 0.543093 0.00304573  0.154562    0.0923779   376  PRO B O   
8017  C  CB  . PRO B 376 ? 1.09839   0.705378 0.569236 -0.00538921 0.193754    0.11404     376  PRO B CB  
8018  C  CG  . PRO B 376 ? 1.08126   0.717037 0.587199 -0.0255601  0.209129    0.105521    376  PRO B CG  
8019  C  CD  . PRO B 376 ? 1.05036   0.707518 0.552306 -0.0181808  0.207259    0.100742    376  PRO B CD  
8020  N  N   . VAL B 377 ? 0.97687   0.63469  0.479065 0.0346722   0.13332     0.0995655   377  VAL B N   
8021  C  CA  . VAL B 377 ? 1.00847   0.689503 0.540159 0.0416453   0.113373    0.0922038   377  VAL B CA  
8022  C  C   . VAL B 377 ? 0.986771  0.676661 0.55326  0.0282129   0.116126    0.0888854   377  VAL B C   
8023  O  O   . VAL B 377 ? 0.919323  0.64162  0.523528 0.0231541   0.109701    0.0793888   377  VAL B O   
8024  C  CB  . VAL B 377 ? 1.04209   0.705217 0.546112 0.0621027   0.0971613   0.097049    377  VAL B CB  
8025  C  CG1 . VAL B 377 ? 1.05012   0.722594 0.535972 0.07652     0.0865293   0.0941196   377  VAL B CG1 
8026  C  CG2 . VAL B 377 ? 1.13814   0.755452 0.601643 0.0657663   0.106353    0.110218    377  VAL B CG2 
8027  N  N   . SER B 378 ? 1.03417   0.693869 0.586587 0.0223633   0.126053    0.0965313   378  SER B N   
8028  C  CA  . SER B 378 ? 1.02427   0.688343 0.605006 0.0115718   0.126943    0.0933567   378  SER B CA  
8029  C  C   . SER B 378 ? 0.974992  0.667405 0.592374 -0.00736155 0.137502    0.0850185   378  SER B C   
8030  O  O   . SER B 378 ? 0.994916  0.698598 0.640875 -0.0165892  0.136642    0.0799997   378  SER B O   
8031  C  CB  . SER B 378 ? 1.10845   0.729645 0.661594 0.00903505  0.137009    0.103318    378  SER B CB  
8032  O  OG  . SER B 378 ? 1.14227   0.737108 0.659729 0.0289733   0.126513    0.111118    378  SER B OG  
8033  N  N   . LEU B 379 ? 0.88919   0.594207 0.505874 -0.0123126  0.147021    0.0828852   379  LEU B N   
8034  C  CA  . LEU B 379 ? 0.846121  0.583186 0.500311 -0.0271028  0.154178    0.0735153   379  LEU B CA  
8035  C  C   . LEU B 379 ? 0.74543   0.519261 0.42529  -0.0195519  0.139735    0.0640591   379  LEU B C   
8036  O  O   . LEU B 379 ? 0.726026  0.528231 0.436584 -0.028543   0.143332    0.0558464   379  LEU B O   
8037  C  CB  . LEU B 379 ? 0.938303  0.668316 0.581458 -0.0401265  0.176427    0.0756848   379  LEU B CB  
8038  C  CG  . LEU B 379 ? 0.979663  0.671542 0.597572 -0.0507138  0.193953    0.0847888   379  LEU B CG  
8039  C  CD1 . LEU B 379 ? 0.975671  0.670868 0.592935 -0.0662989  0.216546    0.0838892   379  LEU B CD1 
8040  C  CD2 . LEU B 379 ? 0.957744  0.647131 0.597594 -0.0603925  0.192636    0.0822487   379  LEU B CD2 
8041  N  N   . ARG B 380 ? 0.682573  0.45547  0.349642 -0.00311509 0.123725    0.0648111   380  ARG B N   
8042  C  CA  . ARG B 380 ? 0.667507  0.470007 0.353506 0.00405554  0.110946    0.056301    380  ARG B CA  
8043  C  C   . ARG B 380 ? 0.587509  0.407636 0.303359 0.0056137   0.0966491   0.0507178   380  ARG B C   
8044  O  O   . ARG B 380 ? 0.567365  0.390849 0.281575 0.0173262   0.0813989   0.0493558   380  ARG B O   
8045  C  CB  . ARG B 380 ? 0.678396  0.474286 0.337661 0.0200363   0.100472    0.0578982   380  ARG B CB  
8046  C  CG  . ARG B 380 ? 0.704035  0.484942 0.331228 0.0211731   0.112656    0.062461    380  ARG B CG  
8047  C  CD  . ARG B 380 ? 0.729051  0.505492 0.331645 0.0384927   0.0984828   0.0626226   380  ARG B CD  
8048  N  NE  . ARG B 380 ? 0.820771  0.572265 0.382301 0.04182     0.10978     0.0702588   380  ARG B NE  
8049  C  CZ  . ARG B 380 ? 0.846152  0.583799 0.373221 0.0561411   0.103002    0.0734305   380  ARG B CZ  
8050  N  NH1 . ARG B 380 ? 0.809447  0.559577 0.338902 0.0694249   0.0833946   0.0678427   380  ARG B NH1 
8051  N  NH2 . ARG B 380 ? 0.91388   0.624336 0.402712 0.0566361   0.116868    0.0822164   380  ARG B NH2 
8052  N  N   . ARG B 381 ? 0.610842  0.44142  0.352793 -0.00672535 0.102484    0.0474392   381  ARG B N   
8053  C  CA  . ARG B 381 ? 0.582822  0.430618 0.353575 -0.00703127 0.0912896   0.041953    381  ARG B CA  
8054  C  C   . ARG B 381 ? 0.536932  0.40957  0.336987 -0.0185467  0.0985326   0.0347596   381  ARG B C   
8055  O  O   . ARG B 381 ? 0.547193  0.418522 0.341565 -0.0256681  0.112137    0.0353461   381  ARG B O   
8056  C  CB  . ARG B 381 ? 0.629268  0.456586 0.395734 -0.0113226  0.0936725   0.0466006   381  ARG B CB  
8057  C  CG  . ARG B 381 ? 0.727371  0.538071 0.475972 0.00240854  0.081248    0.0510758   381  ARG B CG  
8058  C  CD  . ARG B 381 ? 0.887604  0.670669 0.623998 -0.00062571 0.0860532   0.056945    381  ARG B CD  
8059  N  NE  . ARG B 381 ? 1.03224   0.783493 0.729243 0.00919382  0.0879773   0.0662601   381  ARG B NE  
8060  C  CZ  . ARG B 381 ? 1.14631   0.885972 0.826974 0.0249374   0.0753656   0.0694168   381  ARG B CZ  
8061  N  NH1 . ARG B 381 ? 1.08101   0.834464 0.781437 0.0301268   0.0625725   0.064623    381  ARG B NH1 
8062  N  NH2 . ARG B 381 ? 1.17705   0.891542 0.820949 0.0359449   0.0758023   0.0771956   381  ARG B NH2 
8063  N  N   . GLY B 382 ? 0.513867  0.407888 0.343361 -0.0201645  0.0903167   0.0282642   382  GLY B N   
8064  C  CA  . GLY B 382 ? 0.458482  0.37528  0.314711 -0.0302518  0.0970063   0.0214914   382  GLY B CA  
8065  C  C   . GLY B 382 ? 0.502772  0.409902 0.362191 -0.0433602  0.108296    0.0228305   382  GLY B C   
8066  O  O   . GLY B 382 ? 0.556739  0.438862 0.398676 -0.0431454  0.108767    0.0289665   382  GLY B O   
8067  N  N   . ALA B 383 ? 0.477165  0.403871 0.358517 -0.0542403  0.117117    0.0165399   383  ALA B N   
8068  C  CA  . ALA B 383 ? 0.526824  0.449234 0.416185 -0.0688676  0.128187    0.0152639   383  ALA B CA  
8069  C  C   . ALA B 383 ? 0.529259  0.445906 0.426725 -0.0692945  0.118922    0.0146585   383  ALA B C   
8070  O  O   . ALA B 383 ? 0.527492  0.424969 0.418005 -0.0779214  0.125768    0.0170332   383  ALA B O   
8071  C  CB  . ALA B 383 ? 0.481495  0.434443 0.398592 -0.0779727  0.135547    0.00608758  383  ALA B CB  
8072  N  N   . ASN B 384 ? 0.471176  0.403879 0.383004 -0.0603248  0.104111    0.0110941   384  ASN B N   
8073  C  CA  . ASN B 384 ? 0.467816  0.391885 0.379472 -0.0552041  0.0929302   0.0123405   384  ASN B CA  
8074  C  C   . ASN B 384 ? 0.440956  0.375577 0.354213 -0.0415582  0.0791276   0.0119723   384  ASN B C   
8075  O  O   . ASN B 384 ? 0.410347  0.35957  0.327866 -0.0379955  0.0787458   0.00963533  384  ASN B O   
8076  C  CB  . ASN B 384 ? 0.43823   0.372609 0.371624 -0.0649422  0.0931005   0.00595566  384  ASN B CB  
8077  C  CG  . ASN B 384 ? 0.40569   0.373036 0.367439 -0.0647468  0.0868549   -0.00272486 384  ASN B CG  
8078  O  OD1 . ASN B 384 ? 0.393618  0.373022 0.359692 -0.0543982  0.0770753   -0.00346958 384  ASN B OD1 
8079  N  ND2 . ASN B 384 ? 0.395769  0.377462 0.376662 -0.0759656  0.0921616   -0.00973278 384  ASN B ND2 
8080  N  N   . PRO B 385 ? 0.410445  0.337651 0.319928 -0.0336792  0.0681015   0.0138223   385  PRO B N   
8081  C  CA  . PRO B 385 ? 0.379593  0.316597 0.290889 -0.022514   0.0564498   0.0129053   385  PRO B CA  
8082  C  C   . PRO B 385 ? 0.335967  0.299308 0.270571 -0.0225514  0.0521236   0.00615348  385  PRO B C   
8083  O  O   . PRO B 385 ? 0.316623  0.287312 0.250708 -0.0157073  0.0470587   0.00510946  385  PRO B O   
8084  C  CB  . PRO B 385 ? 0.367758  0.294094 0.275566 -0.0174508  0.04805     0.014746    385  PRO B CB  
8085  C  CG  . PRO B 385 ? 0.396403  0.296231 0.285112 -0.0215238  0.0563874   0.0203121   385  PRO B CG  
8086  C  CD  . PRO B 385 ? 0.41226   0.320368 0.314604 -0.0351645  0.0671797   0.0165207   385  PRO B CD  
8087  N  N   . GLY B 386 ? 0.317217  0.293077 0.270391 -0.0300077  0.0543156   0.00144701  386  GLY B N   
8088  C  CA  . GLY B 386 ? 0.306758  0.306649 0.280966 -0.0297023  0.0509216   -0.00489884 386  GLY B CA  
8089  C  C   . GLY B 386 ? 0.328976  0.34037  0.305479 -0.0289133  0.0562473   -0.0070847  386  GLY B C   
8090  O  O   . GLY B 386 ? 0.291553  0.317545 0.277911 -0.0233158  0.0512526   -0.0106641  386  GLY B O   
8091  N  N   . PHE B 387 ? 0.346466  0.349957 0.312816 -0.0345221  0.0672806   -0.00496714 387  PHE B N   
8092  C  CA  . PHE B 387 ? 0.328402  0.342062 0.295329 -0.0340515  0.0740561   -0.00721616 387  PHE B CA  
8093  C  C   . PHE B 387 ? 0.308533  0.316843 0.262236 -0.0234034  0.0676882   -0.00509689 387  PHE B C   
8094  O  O   . PHE B 387 ? 0.295707  0.317752 0.257045 -0.0186482  0.0659914   -0.00930538 387  PHE B O   
8095  C  CB  . PHE B 387 ? 0.356819  0.360655 0.311951 -0.0424291  0.0886861   -0.00467815 387  PHE B CB  
8096  C  CG  . PHE B 387 ? 0.37707   0.39521  0.351026 -0.0547592  0.0982419   -0.0101849  387  PHE B CG  
8097  C  CD1 . PHE B 387 ? 0.372512  0.39126  0.357996 -0.0614998  0.0959049   -0.0123586  387  PHE B CD1 
8098  C  CD2 . PHE B 387 ? 0.395251  0.429101 0.377418 -0.0594919  0.109182    -0.0146393  387  PHE B CD2 
8099  C  CE1 . PHE B 387 ? 0.383085  0.417356 0.387709 -0.073504   0.1039      -0.0191075  387  PHE B CE1 
8100  C  CE2 . PHE B 387 ? 0.429167  0.479855 0.431612 -0.0716222  0.118015    -0.0212511  387  PHE B CE2 
8101  C  CZ  . PHE B 387 ? 0.414265  0.465568 0.428397 -0.0788854  0.114953    -0.0237863  387  PHE B CZ  
8102  N  N   . HIS B 388 ? 0.311266  0.300108 0.246016 -0.0192441  0.063421    0.00060709  388  HIS B N   
8103  C  CA  . HIS B 388 ? 0.320472  0.304529 0.242058 -0.00996607 0.0572057   0.00165624  388  HIS B CA  
8104  C  C   . HIS B 388 ? 0.309823  0.307608 0.246597 -0.00464152 0.0471175   -0.00300452 388  HIS B C   
8105  O  O   . HIS B 388 ? 0.296075  0.298865 0.231403 0.00045794  0.0450338   -0.00585358 388  HIS B O   
8106  C  CB  . HIS B 388 ? 0.355272  0.318082 0.255199 -0.00609423 0.05397     0.00788451  388  HIS B CB  
8107  C  CG  . HIS B 388 ? 0.371084  0.323697 0.248353 -0.00038129 0.0555633   0.0103525   388  HIS B CG  
8108  N  ND1 . HIS B 388 ? 0.360463  0.321201 0.236477 0.00588345  0.0508779   0.00639516  388  HIS B ND1 
8109  C  CD2 . HIS B 388 ? 0.400983  0.33403  0.253626 -0.00019171 0.0622399   0.0164259   388  HIS B CD2 
8110  C  CE1 . HIS B 388 ? 0.409187  0.357434 0.261184 0.0100746   0.0535494   0.00938792  388  HIS B CE1 
8111  N  NE2 . HIS B 388 ? 0.422773  0.354055 0.259697 0.00664659  0.0609266   0.0159093   388  HIS B NE2 
8112  N  N   . GLU B 389 ? 0.29564   0.298715 0.246369 -0.0062366  0.0418489   -0.0040975  389  GLU B N   
8113  C  CA  . GLU B 389 ? 0.275561  0.287662 0.237353 -0.00139124 0.0329807   -0.0072932  389  GLU B CA  
8114  C  C   . GLU B 389 ? 0.264092  0.292473 0.240637 -0.00098448 0.0348859   -0.0123612  389  GLU B C   
8115  O  O   . GLU B 389 ? 0.281474  0.314656 0.263634 0.00399381  0.0290446   -0.0147992  389  GLU B O   
8116  C  CB  . GLU B 389 ? 0.266085  0.277783 0.235736 -0.00274576 0.0274825   -0.00661755 389  GLU B CB  
8117  C  CG  . GLU B 389 ? 0.271734  0.268087 0.227642 -0.0011741  0.0247232   -0.00222487 389  GLU B CG  
8118  C  CD  . GLU B 389 ? 0.285259  0.276502 0.229538 0.00565332  0.0194134   -0.0016714  389  GLU B CD  
8119  O  OE1 . GLU B 389 ? 0.313972  0.292472 0.242684 0.00842289  0.0186207   0.00196299  389  GLU B OE1 
8120  O  OE2 . GLU B 389 ? 0.271339  0.270367 0.220956 0.00872662  0.0156026   -0.00519627 389  GLU B OE2 
8121  N  N   . ALA B 390 ? 0.247229  0.283934 0.230023 -0.00596931 0.0432833   -0.0142395  390  ALA B N   
8122  C  CA  . ALA B 390 ? 0.247211  0.30223  0.246634 -0.00437948 0.0438468   -0.0198296  390  ALA B CA  
8123  C  C   . ALA B 390 ? 0.273177  0.332465 0.268949 0.00042396  0.0477691   -0.0226045  390  ALA B C   
8124  O  O   . ALA B 390 ? 0.291482  0.364059 0.298704 0.00500228  0.0468201   -0.027365   390  ALA B O   
8125  C  CB  . ALA B 390 ? 0.236352  0.302392 0.248491 -0.0124658  0.0499946   -0.0222975  390  ALA B CB  
8126  N  N   . ILE B 391 ? 0.288874  0.336832 0.267681 8.571e-05   0.052593    -0.0199604  391  ILE B N   
8127  C  CA  . ILE B 391 ? 0.294702  0.347919 0.269802 0.00297909  0.0591826   -0.0232494  391  ILE B CA  
8128  C  C   . ILE B 391 ? 0.280006  0.335366 0.256925 0.0119719   0.0523376   -0.0270499  391  ILE B C   
8129  O  O   . ILE B 391 ? 0.260457  0.328312 0.247048 0.0159207   0.0548564   -0.0321605  391  ILE B O   
8130  C  CB  . ILE B 391 ? 0.30899   0.347802 0.26194  0.00145844  0.0656732   -0.0193876  391  ILE B CB  
8131  C  CG1 . ILE B 391 ? 0.334882  0.368123 0.284292 -0.00793271 0.0742567   -0.0152222  391  ILE B CG1 
8132  C  CG2 . ILE B 391 ? 0.322623  0.366854 0.270382 0.00522544  0.0725329   -0.0234579  391  ILE B CG2 
8133  C  CD1 . ILE B 391 ? 0.321441  0.372693 0.29014  -0.0153924  0.0832148   -0.0195379  391  ILE B CD1 
8134  N  N   . GLY B 392 ? 0.252431  0.295092 0.219615 0.0152715   0.0441237   -0.0250361  392  GLY B N   
8135  C  CA  . GLY B 392 ? 0.241956  0.28325  0.208652 0.0222653   0.0391643   -0.0289522  392  GLY B CA  
8136  C  C   . GLY B 392 ? 0.240881  0.289707 0.223093 0.0250782   0.03427     -0.030791   392  GLY B C   
8137  O  O   . GLY B 392 ? 0.226209  0.276257 0.210891 0.0314157   0.0328257   -0.0346335  392  GLY B O   
8138  N  N   . ASP B 393 ? 0.225907  0.278198 0.216736 0.020999    0.0317605   -0.0280417  393  ASP B N   
8139  C  CA  . ASP B 393 ? 0.234758  0.293999 0.23802  0.0241729   0.0269754   -0.0294056  393  ASP B CA  
8140  C  C   . ASP B 393 ? 0.22298   0.298546 0.237983 0.0279894   0.0309985   -0.034234   393  ASP B C   
8141  O  O   . ASP B 393 ? 0.232508  0.311449 0.25282  0.0353785   0.0272635   -0.0367229  393  ASP B O   
8142  C  CB  . ASP B 393 ? 0.248515  0.309271 0.258004 0.0194499   0.0235975   -0.026494   393  ASP B CB  
8143  C  CG  . ASP B 393 ? 0.31165   0.359326 0.313708 0.018295    0.0176709   -0.0228333  393  ASP B CG  
8144  O  OD1 . ASP B 393 ? 0.298988  0.336319 0.289994 0.0189329   0.0165872   -0.0221023  393  ASP B OD1 
8145  O  OD2 . ASP B 393 ? 0.325559  0.374785 0.333322 0.0169387   0.0140098   -0.021485   393  ASP B OD2 
8146  N  N   . VAL B 394 ? 0.222403  0.307609 0.24068  0.023343    0.0390348   -0.0357004  394  VAL B N   
8147  C  CA  . VAL B 394 ? 0.22684   0.331499 0.258744 0.0265758   0.0436437   -0.0415711  394  VAL B CA  
8148  C  C   . VAL B 394 ? 0.244423  0.346949 0.271719 0.0365133   0.0435527   -0.0451711  394  VAL B C   
8149  O  O   . VAL B 394 ? 0.236581  0.349375 0.273762 0.0448053   0.0408348   -0.0492788  394  VAL B O   
8150  C  CB  . VAL B 394 ? 0.252812  0.36709  0.288244 0.0177968   0.054298    -0.0426366  394  VAL B CB  
8151  C  CG1 . VAL B 394 ? 0.267664  0.404923 0.318285 0.0206567   0.0606606   -0.0499832  394  VAL B CG1 
8152  C  CG2 . VAL B 394 ? 0.269035  0.385491 0.311398 0.00855864  0.0537242   -0.0404103  394  VAL B CG2 
8153  N  N   . LEU B 395 ? 0.243551  0.332325 0.254857 0.0364787   0.046273    -0.0441043  395  LEU B N   
8154  C  CA  . LEU B 395 ? 0.262273  0.347316 0.268085 0.045514    0.0465708   -0.0484413  395  LEU B CA  
8155  C  C   . LEU B 395 ? 0.258068  0.333007 0.263478 0.0523643   0.0376254   -0.0481475  395  LEU B C   
8156  O  O   . LEU B 395 ? 0.265644  0.342467 0.273823 0.0618517   0.0368405   -0.0522889  395  LEU B O   
8157  C  CB  . LEU B 395 ? 0.296464  0.367552 0.28363  0.0438798   0.0497493   -0.0478647  395  LEU B CB  
8158  C  CG  . LEU B 395 ? 0.335649  0.414902 0.319044 0.0414718   0.0608089   -0.0499868  395  LEU B CG  
8159  C  CD1 . LEU B 395 ? 0.329399  0.412335 0.313678 0.03129     0.0663416   -0.0455274  395  LEU B CD1 
8160  C  CD2 . LEU B 395 ? 0.349831  0.413644 0.31241  0.0436786   0.0615255   -0.0507887  395  LEU B CD2 
8161  N  N   . ALA B 396 ? 0.238566  0.301321 0.239112 0.0478155   0.0315767   -0.0432543  396  ALA B N   
8162  C  CA  . ALA B 396 ? 0.250388  0.301389 0.248786 0.0526904   0.0246913   -0.0424296  396  ALA B CA  
8163  C  C   . ALA B 396 ? 0.242936  0.30425  0.252895 0.0598271   0.0219573   -0.0435781  396  ALA B C   
8164  O  O   . ALA B 396 ? 0.263036  0.314176 0.269107 0.0674516   0.0183474   -0.0440454  396  ALA B O   
8165  C  CB  . ALA B 396 ? 0.215629  0.255722 0.209478 0.0462753   0.0197839   -0.0376469  396  ALA B CB  
8166  N  N   . LEU B 397 ? 0.244227  0.324437 0.267321 0.0574687   0.0232972   -0.0441726  397  LEU B N   
8167  C  CA  . LEU B 397 ? 0.251916  0.345097 0.286266 0.0658611   0.0197301   -0.046746   397  LEU B CA  
8168  C  C   . LEU B 397 ? 0.272079  0.369843 0.307731 0.0776957   0.0216842   -0.052295   397  LEU B C   
8169  O  O   . LEU B 397 ? 0.299305  0.39658  0.33619  0.0886186   0.0168641   -0.0534429  397  LEU B O   
8170  C  CB  . LEU B 397 ? 0.264183  0.379837 0.314253 0.0601299   0.021213    -0.0485057  397  LEU B CB  
8171  C  CG  . LEU B 397 ? 0.257365  0.368591 0.306946 0.0506707   0.0182271   -0.0437722  397  LEU B CG  
8172  C  CD1 . LEU B 397 ? 0.261432  0.394001 0.326418 0.0437804   0.021211    -0.0470199  397  LEU B CD1 
8173  C  CD2 . LEU B 397 ? 0.284407  0.387925 0.330947 0.0571554   0.0100282   -0.0413765  397  LEU B CD2 
8174  N  N   . SER B 398 ? 0.254307  0.357108 0.289193 0.0765593   0.0290028   -0.0559513  398  SER B N   
8175  C  CA  . SER B 398 ? 0.261307  0.367513 0.296556 0.0884592   0.0312878   -0.0618131  398  SER B CA  
8176  C  C   . SER B 398 ? 0.262096  0.340737 0.280125 0.0941911   0.0280813   -0.0604539  398  SER B C   
8177  O  O   . SER B 398 ? 0.279522  0.353024 0.29572  0.106537    0.0255648   -0.0629813  398  SER B O   
8178  C  CB  . SER B 398 ? 0.2722    0.390915 0.310074 0.0852754   0.0409839   -0.0663188  398  SER B CB  
8179  O  OG  . SER B 398 ? 0.27863   0.425362 0.335066 0.0819122   0.0455034   -0.0699122  398  SER B OG  
8180  N  N   . VAL B 399 ? 0.253627  0.314416 0.258903 0.085363    0.0282795   -0.0570589  399  VAL B N   
8181  C  CA  . VAL B 399 ? 0.282163  0.31785  0.272246 0.0884293   0.0262131   -0.0573987  399  VAL B CA  
8182  C  C   . VAL B 399 ? 0.283293  0.305151 0.270614 0.0943576   0.0200326   -0.0543188  399  VAL B C   
8183  O  O   . VAL B 399 ? 0.294748  0.298764 0.272506 0.102132    0.019313    -0.0561995  399  VAL B O   
8184  C  CB  . VAL B 399 ? 0.286934  0.31039  0.26627  0.0773343   0.0265466   -0.0553667  399  VAL B CB  
8185  C  CG1 . VAL B 399 ? 0.317068  0.315855 0.283625 0.0777338   0.0233686   -0.0560668  399  VAL B CG1 
8186  C  CG2 . VAL B 399 ? 0.274316  0.305506 0.249917 0.0745886   0.0330917   -0.0587741  399  VAL B CG2 
8187  N  N   . SER B 400 ? 0.283161  0.310529 0.276649 0.0905735   0.0159968   -0.0494461  400  SER B N   
8188  C  CA  . SER B 400 ? 0.303033  0.31395  0.290022 0.0947236   0.010908    -0.0454346  400  SER B CA  
8189  C  C   . SER B 400 ? 0.3278    0.34235  0.317017 0.110286    0.00825455  -0.0471539  400  SER B C   
8190  O  O   . SER B 400 ? 0.36031   0.357034 0.339953 0.116686    0.00464427  -0.0437208  400  SER B O   
8191  C  CB  . SER B 400 ? 0.328554  0.343359 0.319416 0.0856507   0.00782167  -0.0400686  400  SER B CB  
8192  O  OG  . SER B 400 ? 0.345569  0.383336 0.34981  0.0887674   0.00613493  -0.0408331  400  SER B OG  
8193  N  N   . THR B 401 ? 0.296     0.333571 0.297263 0.116946    0.0101731   -0.0525175  401  THR B N   
8194  C  CA  . THR B 401 ? 0.327595  0.37185  0.332257 0.133519    0.00677734  -0.0552829  401  THR B CA  
8195  C  C   . THR B 401 ? 0.372426  0.38825  0.360157 0.144357    0.00681313  -0.0556928  401  THR B C   
8196  O  O   . THR B 401 ? 0.385673  0.388443 0.365525 0.141499    0.0115596   -0.0585077  401  THR B O   
8197  C  CB  . THR B 401 ? 0.303151  0.37962  0.325759 0.139311    0.00950736  -0.0627278  401  THR B CB  
8198  O  OG1 . THR B 401 ? 0.303708  0.381187 0.325166 0.137535    0.0170119   -0.0676146  401  THR B OG1 
8199  C  CG2 . THR B 401 ? 0.285716  0.389043 0.325314 0.128763    0.009604    -0.0628679  401  THR B CG2 
8200  N  N   . PRO B 402 ? 0.390583  0.39555  0.371193 0.158012    0.00152238  -0.0533698  402  PRO B N   
8201  C  CA  . PRO B 402 ? 0.403831  0.378557 0.366586 0.169758    0.00196812  -0.0535581  402  PRO B CA  
8202  C  C   . PRO B 402 ? 0.416967  0.396514 0.381942 0.177641    0.00663778  -0.0616734  402  PRO B C   
8203  O  O   . PRO B 402 ? 0.437862  0.390512 0.388022 0.178877    0.00988974  -0.063137   402  PRO B O   
8204  C  CB  . PRO B 402 ? 0.424582  0.396838 0.382935 0.185707    -0.00491842 -0.05043    402  PRO B CB  
8205  C  CG  . PRO B 402 ? 0.401123  0.388928 0.367856 0.175957    -0.00881908 -0.0458062  402  PRO B CG  
8206  C  CD  . PRO B 402 ? 0.359708  0.376905 0.345907 0.161808    -0.00509796 -0.0498861  402  PRO B CD  
8207  N  N   . GLU B 403 ? 0.404866  0.418962 0.388568 0.182623    0.00747424  -0.0676881  403  GLU B N   
8208  C  CA  . GLU B 403 ? 0.432464  0.453863 0.419061 0.191577    0.0125212   -0.0759512  403  GLU B CA  
8209  C  C   . GLU B 403 ? 0.389424  0.404141 0.371371 0.177444    0.0198334   -0.0781078  403  GLU B C   
8210  O  O   . GLU B 403 ? 0.386024  0.388226 0.359091 0.182891    0.0240837   -0.0833795  403  GLU B O   
8211  C  CB  . GLU B 403 ? 0.479821  0.542361 0.489359 0.199482    0.0125375   -0.0825732  403  GLU B CB  
8212  C  CG  . GLU B 403 ? 0.668867  0.736508 0.679608 0.213876    0.0170768   -0.0914101  403  GLU B CG  
8213  C  CD  . GLU B 403 ? 0.849975  0.95591  0.882194 0.2276      0.017421    -0.10032    403  GLU B CD  
8214  O  OE1 . GLU B 403 ? 0.880044  0.986018 0.910648 0.2406      0.0213809   -0.107522   403  GLU B OE1 
8215  O  OE2 . GLU B 403 ? 0.950711  1.08728  1.00189  0.225506    0.0138462   -0.101053   403  GLU B OE2 
8216  N  N   . HIS B 404 ? 0.352388  0.376438 0.339925 0.160053    0.0211019   -0.0745471  404  HIS B N   
8217  C  CA  . HIS B 404 ? 0.340266  0.358161 0.321598 0.147623    0.0268071   -0.0761117  404  HIS B CA  
8218  C  C   . HIS B 404 ? 0.352041  0.333742 0.313784 0.144005    0.0253711   -0.0738305  404  HIS B C   
8219  O  O   . HIS B 404 ? 0.351236  0.320634 0.303176 0.142127    0.0291651   -0.0783915  404  HIS B O   
8220  C  CB  . HIS B 404 ? 0.30698   0.340932 0.296992 0.131223    0.0278681   -0.0721892  404  HIS B CB  
8221  C  CG  . HIS B 404 ? 0.316516  0.346904 0.299212 0.12193     0.0336647   -0.0745745  404  HIS B CG  
8222  N  ND1 . HIS B 404 ? 0.329104  0.377203 0.316973 0.124115    0.0408327   -0.0804757  404  HIS B ND1 
8223  C  CD2 . HIS B 404 ? 0.310468  0.322263 0.280284 0.111881    0.0333505   -0.0727178  404  HIS B CD2 
8224  C  CE1 . HIS B 404 ? 0.339339  0.377693 0.315273 0.116132    0.0445498   -0.0814542  404  HIS B CE1 
8225  N  NE2 . HIS B 404 ? 0.322561  0.340308 0.288409 0.108743    0.0394115   -0.0770044  404  HIS B NE2 
8226  N  N   . LEU B 405 ? 0.347512  0.313695 0.304092 0.14117     0.0203492   -0.0671212  405  LEU B N   
8227  C  CA  . LEU B 405 ? 0.369415  0.30217  0.309237 0.13613     0.0198392   -0.065179   405  LEU B CA  
8228  C  C   . LEU B 405 ? 0.40416   0.315207 0.331451 0.148887    0.0219446   -0.0706005  405  LEU B C   
8229  O  O   . LEU B 405 ? 0.408809  0.29863  0.324217 0.143929    0.0245593   -0.0743506  405  LEU B O   
8230  C  CB  . LEU B 405 ? 0.371907  0.292091 0.307941 0.133734    0.0154282   -0.0572788  405  LEU B CB  
8231  C  CG  . LEU B 405 ? 0.368075  0.304247 0.313795 0.120025    0.0135227   -0.0522759  405  LEU B CG  
8232  C  CD1 . LEU B 405 ? 0.36009   0.287483 0.302585 0.120614    0.00943649  -0.0450211  405  LEU B CD1 
8233  C  CD2 . LEU B 405 ? 0.361066  0.290226 0.30305  0.104616    0.0156334   -0.0533442  405  LEU B CD2 
8234  N  N   . HIS B 406 ? 0.414788  0.332036 0.345002 0.166179    0.0204865   -0.0719249  406  HIS B N   
8235  C  CA  . HIS B 406 ? 0.449742  0.346728 0.36793  0.180474    0.0226508   -0.0776149  406  HIS B CA  
8236  C  C   . HIS B 406 ? 0.452922  0.358774 0.372509 0.178802    0.0284279   -0.0864219  406  HIS B C   
8237  O  O   . HIS B 406 ? 0.460993  0.342094 0.366233 0.181344    0.03126     -0.0915858  406  HIS B O   
8238  C  CB  . HIS B 406 ? 0.474332  0.379483 0.39632  0.201104    0.0189826   -0.0775158  406  HIS B CB  
8239  C  CG  . HIS B 406 ? 0.51629   0.40362  0.427199 0.218109    0.021262    -0.0840196  406  HIS B CG  
8240  N  ND1 . HIS B 406 ? 0.563492  0.407536 0.451936 0.222549    0.0216547   -0.0824665  406  HIS B ND1 
8241  C  CD2 . HIS B 406 ? 0.544951  0.450305 0.463451 0.231558    0.0239503   -0.0924504  406  HIS B CD2 
8242  C  CE1 . HIS B 406 ? 0.604309  0.438647 0.485859 0.239399    0.0238826   -0.0896209  406  HIS B CE1 
8243  N  NE2 . HIS B 406 ? 0.581842  0.454326 0.481967 0.245653    0.0251487   -0.0959138  406  HIS B NE2 
8244  N  N   . LYS B 407 ? 0.450213  0.390192 0.385783 0.173696    0.0308307   -0.0884056  407  LYS B N   
8245  C  CA  . LYS B 407 ? 0.477509  0.426072 0.412405 0.172525    0.0372212   -0.0962959  407  LYS B CA  
8246  C  C   . LYS B 407 ? 0.487995  0.415328 0.40866  0.158689    0.038582    -0.0975073  407  LYS B C   
8247  O  O   . LYS B 407 ? 0.519087  0.439337 0.430872 0.161131    0.0428092   -0.105069   407  LYS B O   
8248  C  CB  . LYS B 407 ? 0.506271  0.492877 0.458685 0.168022    0.04139     -0.0978675  407  LYS B CB  
8249  C  CG  . LYS B 407 ? 0.587295  0.600669 0.555151 0.18285     0.0430487   -0.102484   407  LYS B CG  
8250  C  CD  . LYS B 407 ? 0.614656  0.666198 0.603118 0.175447    0.046465    -0.10238    407  LYS B CD  
8251  C  CE  . LYS B 407 ? 0.685292  0.761928 0.689455 0.192105    0.0471825   -0.108744   407  LYS B CE  
8252  N  NZ  . LYS B 407 ? 0.729546  0.845516 0.757045 0.186674    0.0502939   -0.110305   407  LYS B NZ  
8253  N  N   . ILE B 408 ? 0.459976  0.379868 0.379224 0.144586    0.0349814   -0.0911312  408  ILE B N   
8254  C  CA  . ILE B 408 ? 0.458947  0.363826 0.36751  0.13122     0.0351797   -0.0931551  408  ILE B CA  
8255  C  C   . ILE B 408 ? 0.481164  0.351104 0.376364 0.129293    0.0328538   -0.0929423  408  ILE B C   
8256  O  O   . ILE B 408 ? 0.49036   0.349512 0.38047  0.116194    0.0314228   -0.0931999  408  ILE B O   
8257  C  CB  . ILE B 408 ? 0.419785  0.3427   0.336265 0.116552    0.0336275   -0.0879956  408  ILE B CB  
8258  C  CG1 . ILE B 408 ? 0.392216  0.317265 0.31677  0.111878    0.0289258   -0.0789793  408  ILE B CG1 
8259  C  CG2 . ILE B 408 ? 0.405776  0.357643 0.331474 0.118046    0.0382459   -0.0895809  408  ILE B CG2 
8260  C  CD1 . ILE B 408 ? 0.390357  0.326389 0.319987 0.0975349   0.0268549   -0.0742747  408  ILE B CD1 
8261  N  N   . GLY B 409 ? 0.492292  0.345245 0.382281 0.142219    0.0325018   -0.0921142  409  GLY B N   
8262  C  CA  . GLY B 409 ? 0.518905  0.333662 0.392728 0.142979    0.0326218   -0.0931343  409  GLY B CA  
8263  C  C   . GLY B 409 ? 0.52979   0.330312 0.401711 0.131374    0.0300506   -0.0854204  409  GLY B C   
8264  O  O   . GLY B 409 ? 0.581879  0.351294 0.440978 0.126166    0.0314789   -0.0869631  409  GLY B O   
8265  N  N   . LEU B 410 ? 0.492757  0.314615 0.376856 0.127494    0.0270094   -0.0776991  410  LEU B N   
8266  C  CA  . LEU B 410 ? 0.477932  0.289345 0.360938 0.117251    0.0251185   -0.0703029  410  LEU B CA  
8267  C  C   . LEU B 410 ? 0.502617  0.302957 0.380874 0.128955    0.0234224   -0.0628601  410  LEU B C   
8268  O  O   . LEU B 410 ? 0.499473  0.291993 0.37587  0.121975    0.0223933   -0.0560476  410  LEU B O   
8269  C  CB  . LEU B 410 ? 0.422801  0.262569 0.320252 0.105131    0.0226791   -0.066694   410  LEU B CB  
8270  C  CG  . LEU B 410 ? 0.422997  0.272467 0.323028 0.0927034   0.0231751   -0.0723491  410  LEU B CG  
8271  C  CD1 . LEU B 410 ? 0.376946  0.253821 0.290112 0.0842035   0.0206674   -0.0676441  410  LEU B CD1 
8272  C  CD2 . LEU B 410 ? 0.421252  0.24515  0.311637 0.0815762   0.0239998   -0.0759515  410  LEU B CD2 
8273  N  N   . LEU B 411 ? 0.532201  0.334778 0.409031 0.147278    0.0227373   -0.0640224  411  LEU B N   
8274  C  CA  . LEU B 411 ? 0.58056   0.373775 0.451502 0.159942    0.0197783   -0.0569409  411  LEU B CA  
8275  C  C   . LEU B 411 ? 0.64201   0.425532 0.50519  0.181415    0.0198211   -0.0608745  411  LEU B C   
8276  O  O   . LEU B 411 ? 0.639756  0.444643 0.512648 0.188223    0.0206348   -0.0679434  411  LEU B O   
8277  C  CB  . LEU B 411 ? 0.555291  0.384222 0.443652 0.159813    0.0152066   -0.0524854  411  LEU B CB  
8278  C  CG  . LEU B 411 ? 0.589373  0.413842 0.472846 0.169999    0.0106701   -0.0446248  411  LEU B CG  
8279  C  CD1 . LEU B 411 ? 0.593085  0.391053 0.463549 0.158972    0.0118286   -0.0369179  411  LEU B CD1 
8280  C  CD2 . LEU B 411 ? 0.535577  0.400935 0.439317 0.171481    0.0060151   -0.0439463  411  LEU B CD2 
8281  N  N   . ASP B 412 ? 0.80392   0.555424 0.648994 0.192962    0.0192796   -0.0562328  412  ASP B N   
8282  C  CA  . ASP B 412 ? 0.912632  0.65644  0.750349 0.216521    0.018136    -0.0595196  412  ASP B CA  
8283  C  C   . ASP B 412 ? 0.969722  0.744645 0.819805 0.231836    0.0113791   -0.0566171  412  ASP B C   
8284  O  O   . ASP B 412 ? 1.00477   0.784216 0.85556  0.228517    0.00754879  -0.0488034  412  ASP B O   
8285  C  CB  . ASP B 412 ? 1.02847   0.721283 0.839825 0.222025    0.0221848   -0.0594038  412  ASP B CB  
8286  C  CG  . ASP B 412 ? 1.17725   0.856046 0.985434 0.207948    0.0281531   -0.067734   412  ASP B CG  
8287  O  OD1 . ASP B 412 ? 1.19398   0.897032 1.01413  0.209836    0.0289067   -0.0763294  412  ASP B OD1 
8288  O  OD2 . ASP B 412 ? 1.29993   0.946152 1.09466  0.194051    0.0321514   -0.0660175  412  ASP B OD2 
8289  N  N   . ARG B 413 ? 0.920223  0.71901  0.781376 0.24757     0.0101996   -0.0640771  413  ARG B N   
8290  C  CA  . ARG B 413 ? 0.859166  0.701698 0.741496 0.257305    0.00466739  -0.0654582  413  ARG B CA  
8291  C  C   . ARG B 413 ? 0.816711  0.654701 0.692376 0.266129    -0.002542   -0.0567994  413  ARG B C   
8292  O  O   . ARG B 413 ? 0.798254  0.599193 0.650572 0.277871    -0.00365802 -0.0518165  413  ARG B O   
8293  C  CB  . ARG B 413 ? 0.881781  0.74172  0.772127 0.276736    0.00514152  -0.0751041  413  ARG B CB  
8294  C  CG  . ARG B 413 ? 0.958582  0.855905 0.86623  0.293798    -0.00187504 -0.0770622  413  ARG B CG  
8295  C  CD  . ARG B 413 ? 0.956494  0.906269 0.894727 0.283791    -0.00154679 -0.0819768  413  ARG B CD  
8296  N  NE  . ARG B 413 ? 1.04193   1.01207  0.992921 0.281903    0.0057313   -0.0918827  413  ARG B NE  
8297  C  CZ  . ARG B 413 ? 1.08602   1.05726  1.0363   0.300042    0.00795432  -0.100135   413  ARG B CZ  
8298  N  NH1 . ARG B 413 ? 1.07688   1.06884  1.03897  0.29608     0.0154897   -0.108836   413  ARG B NH1 
8299  N  NH2 . ARG B 413 ? 1.12461   1.07532  1.061    0.323018    0.00294284  -0.0996658  413  ARG B NH2 
8300  N  N   . VAL B 414 ? 0.779328  0.652283 0.673288 0.259936    -0.00706946 -0.0548298  414  VAL B N   
8301  C  CA  . VAL B 414 ? 0.807039  0.676019 0.693259 0.267952    -0.0142858  -0.0470947  414  VAL B CA  
8302  C  C   . VAL B 414 ? 0.808532  0.704611 0.704702 0.292098    -0.021847   -0.051958   414  VAL B C   
8303  O  O   . VAL B 414 ? 0.800273  0.730289 0.717705 0.296209    -0.0210136  -0.0613454  414  VAL B O   
8304  C  CB  . VAL B 414 ? 0.811541  0.696655 0.707016 0.249757    -0.0161874  -0.0415332  414  VAL B CB  
8305  C  CG1 . VAL B 414 ? 0.741652  0.604148 0.62972  0.226547    -0.00926184 -0.037677   414  VAL B CG1 
8306  C  CG2 . VAL B 414 ? 0.783162  0.719746 0.708713 0.245231    -0.0189455  -0.047625   414  VAL B CG2 
8307  N  N   . THR B 415 ? 0.829658  0.711877 0.710353 0.308323    -0.0291502  -0.045913   415  THR B N   
8308  C  CA  . THR B 415 ? 0.874682  0.789498 0.768155 0.330897    -0.0379856  -0.0516236  415  THR B CA  
8309  C  C   . THR B 415 ? 0.77101   0.731876 0.69036  0.320107    -0.0428787  -0.0537159  415  THR B C   
8310  O  O   . THR B 415 ? 0.798819  0.752639 0.712716 0.306473    -0.0438251  -0.0464634  415  THR B O   
8311  C  CB  . THR B 415 ? 0.951009  0.837097 0.8185   0.358557    -0.0450095  -0.046931   415  THR B CB  
8312  O  OG1 . THR B 415 ? 0.99311   0.877042 0.850384 0.362022    -0.05281    -0.0390423  415  THR B OG1 
8313  C  CG2 . THR B 415 ? 0.9613    0.790881 0.797936 0.363437    -0.0382986  -0.0424666  415  THR B CG2 
8314  N  N   . ASN B 416 ? 0.727041  0.734666 0.675225 0.324671    -0.0446259  -0.0644557  416  ASN B N   
8315  C  CA  . ASN B 416 ? 0.65852   0.713384 0.634243 0.316175    -0.0489492  -0.0691123  416  ASN B CA  
8316  C  C   . ASN B 416 ? 0.686055  0.748408 0.656099 0.333152    -0.0615524  -0.0667231  416  ASN B C   
8317  O  O   . ASN B 416 ? 0.656635  0.754826 0.643941 0.349481    -0.0691078  -0.0752596  416  ASN B O   
8318  C  CB  . ASN B 416 ? 0.643966  0.742404 0.649495 0.318911    -0.0459507  -0.0820563  416  ASN B CB  
8319  C  CG  . ASN B 416 ? 0.633187  0.778995 0.669364 0.303811    -0.0465439  -0.08796    416  ASN B CG  
8320  O  OD1 . ASN B 416 ? 0.640666  0.783626 0.67632  0.285241    -0.0463093  -0.0821807  416  ASN B OD1 
8321  N  ND2 . ASN B 416 ? 0.628659  0.817785 0.691884 0.311084    -0.0465238  -0.0999702  416  ASN B ND2 
8322  N  N   . ASP B 417 ? 0.69506   0.725326 0.641101 0.329186    -0.0639362  -0.0556138  417  ASP B N   
8323  C  CA  . ASP B 417 ? 0.689086  0.726349 0.627697 0.343521    -0.0757973  -0.0529314  417  ASP B CA  
8324  C  C   . ASP B 417 ? 0.678476  0.727654 0.623863 0.322641    -0.0767128  -0.0493306  417  ASP B C   
8325  O  O   . ASP B 417 ? 0.624378  0.667526 0.574607 0.298519    -0.0679652  -0.0467459  417  ASP B O   
8326  C  CB  . ASP B 417 ? 0.734525  0.723327 0.635364 0.363554    -0.0787503  -0.0435532  417  ASP B CB  
8327  C  CG  . ASP B 417 ? 0.793954  0.731152 0.665631 0.34872     -0.0707543  -0.0308761  417  ASP B CG  
8328  O  OD1 . ASP B 417 ? 0.733117  0.671274 0.613852 0.322365    -0.0629987  -0.0292602  417  ASP B OD1 
8329  O  OD2 . ASP B 417 ? 0.830433  0.726359 0.669759 0.364015    -0.0722828  -0.0226739  417  ASP B OD2 
8330  N  N   . THR B 418 ? 0.666968  0.73277  0.611594 0.333141    -0.0879104  -0.0495498  418  THR B N   
8331  C  CA  . THR B 418 ? 0.643511  0.724673 0.596209 0.315286    -0.0897909  -0.048024   418  THR B CA  
8332  C  C   . THR B 418 ? 0.596407  0.634983 0.524313 0.299091    -0.082693   -0.0354531  418  THR B C   
8333  O  O   . THR B 418 ? 0.541614  0.590355 0.481056 0.276964    -0.0786593  -0.0350134  418  THR B O   
8334  C  CB  . THR B 418 ? 0.674645  0.784108 0.631549 0.331403    -0.104091   -0.0525638  418  THR B CB  
8335  O  OG1 . THR B 418 ? 0.749837  0.817865 0.669189 0.348955    -0.108446   -0.0419291  418  THR B OG1 
8336  C  CG2 . THR B 418 ? 0.597289  0.751056 0.58062  0.348232    -0.111049   -0.0663035  418  THR B CG2 
8337  N  N   . GLU B 419 ? 0.595654  0.586873 0.490748 0.308975    -0.0801236  -0.0258584  419  GLU B N   
8338  C  CA  . GLU B 419 ? 0.624536  0.576006 0.497577 0.292594    -0.0719126  -0.0148578  419  GLU B CA  
8339  C  C   . GLU B 419 ? 0.60388   0.549958 0.488589 0.268912    -0.0600339  -0.0157693  419  GLU B C   
8340  O  O   . GLU B 419 ? 0.571078  0.509174 0.454649 0.248909    -0.0547782  -0.0112197  419  GLU B O   
8341  C  CB  . GLU B 419 ? 0.694618  0.59417  0.529392 0.30639     -0.0700039  -0.00458677 419  GLU B CB  
8342  C  CG  . GLU B 419 ? 0.81843   0.714087 0.632992 0.329912    -0.0814092  -0.00082103 419  GLU B CG  
8343  C  CD  . GLU B 419 ? 0.920045  0.762021 0.694072 0.346824    -0.0794266  0.00950845  419  GLU B CD  
8344  O  OE1 . GLU B 419 ? 0.98331   0.787563 0.743716 0.337138    -0.0681163  0.0143891   419  GLU B OE1 
8345  O  OE2 . GLU B 419 ? 1.0302    0.867345 0.785174 0.369964    -0.0893708  0.0124693   419  GLU B OE2 
8346  N  N   . SER B 420 ? 0.611479  0.559598 0.505004 0.272294    -0.0558039  -0.0215597  420  SER B N   
8347  C  CA  . SER B 420 ? 0.58115   0.528219 0.486218 0.251552    -0.0457959  -0.0237689  420  SER B CA  
8348  C  C   . SER B 420 ? 0.503011  0.490654 0.436744 0.234678    -0.0458764  -0.0293186  420  SER B C   
8349  O  O   . SER B 420 ? 0.495477  0.478337 0.432671 0.214304    -0.0395066  -0.0271112  420  SER B O   
8350  C  CB  . SER B 420 ? 0.601529  0.545615 0.509984 0.260077    -0.0418772  -0.0298909  420  SER B CB  
8351  O  OG  . SER B 420 ? 0.657045  0.563115 0.538439 0.278106    -0.0424281  -0.0254072  420  SER B OG  
8352  N  N   . ASP B 421 ? 0.514361  0.541812 0.468816 0.243369    -0.0528878  -0.0371477  421  ASP B N   
8353  C  CA  . ASP B 421 ? 0.518984  0.583109 0.499121 0.227615    -0.0530474  -0.0424236  421  ASP B CA  
8354  C  C   . ASP B 421 ? 0.482891  0.53426  0.453527 0.21348     -0.0531341  -0.0350038  421  ASP B C   
8355  O  O   . ASP B 421 ? 0.46379   0.516251 0.441956 0.193493    -0.0468493  -0.0340159  421  ASP B O   
8356  C  CB  . ASP B 421 ? 0.600804  0.708456 0.603352 0.238465    -0.0612695  -0.0521545  421  ASP B CB  
8357  C  CG  . ASP B 421 ? 0.724137  0.866207 0.754451 0.235703    -0.0569436  -0.0630075  421  ASP B CG  
8358  O  OD1 . ASP B 421 ? 0.772437  0.910417 0.80824  0.219161    -0.0471163  -0.0628905  421  ASP B OD1 
8359  O  OD2 . ASP B 421 ? 0.752866  0.925607 0.798392 0.250999    -0.0632506  -0.0717901  421  ASP B OD2 
8360  N  N   . ILE B 422 ? 0.482041  0.519613 0.434174 0.224874    -0.060015   -0.0295994  422  ILE B N   
8361  C  CA  . ILE B 422 ? 0.472547  0.501484 0.416246 0.212896    -0.0603115  -0.0235279  422  ILE B CA  
8362  C  C   . ILE B 422 ? 0.443769  0.4416   0.375848 0.195832    -0.0501643  -0.0164405  422  ILE B C   
8363  O  O   . ILE B 422 ? 0.404088  0.408244 0.343844 0.178401    -0.0471285  -0.015549   422  ILE B O   
8364  C  CB  . ILE B 422 ? 0.500565  0.518635 0.423314 0.228625    -0.0689751  -0.0186662  422  ILE B CB  
8365  C  CG1 . ILE B 422 ? 0.536862  0.592302 0.47445  0.243627    -0.0806676  -0.0273571  422  ILE B CG1 
8366  C  CG2 . ILE B 422 ? 0.500171  0.505705 0.412374 0.214719    -0.0669572  -0.0121006  422  ILE B CG2 
8367  C  CD1 . ILE B 422 ? 0.503069  0.601597 0.473604 0.229597    -0.081538   -0.0373493  422  ILE B CD1 
8368  N  N   . ASN B 423 ? 0.451591  0.415938 0.365192 0.200928    -0.0451625  -0.011986   423  ASN B N   
8369  C  CA  . ASN B 423 ? 0.450686  0.386508 0.353964 0.184917    -0.0359108  -0.00660016 423  ASN B CA  
8370  C  C   . ASN B 423 ? 0.413699  0.368165 0.338564 0.167082    -0.0305948  -0.0118034  423  ASN B C   
8371  O  O   . ASN B 423 ? 0.402387  0.35142  0.328168 0.150312    -0.0260697  -0.00909317 423  ASN B O   
8372  C  CB  . ASN B 423 ? 0.498793  0.398869 0.382959 0.191611    -0.0307418  -0.00372183 423  ASN B CB  
8373  C  CG  . ASN B 423 ? 0.537733  0.400375 0.391482 0.200824    -0.0304925  0.00528527  423  ASN B CG  
8374  O  OD1 . ASN B 423 ? 0.527223  0.390477 0.372643 0.202322    -0.0342357  0.00997836  423  ASN B OD1 
8375  N  ND2 . ASN B 423 ? 0.559175  0.38726  0.394753 0.206357    -0.0253678  0.00771767  423  ASN B ND2 
8376  N  N   . TYR B 424 ? 0.403753  0.380915 0.345539 0.171367    -0.0310525  -0.0194194  424  TYR B N   
8377  C  CA  . TYR B 424 ? 0.382153  0.375153 0.341326 0.156237    -0.0255583  -0.0240427  424  TYR B CA  
8378  C  C   . TYR B 424 ? 0.336957  0.354831 0.311569 0.143835    -0.0272678  -0.0250938  424  TYR B C   
8379  O  O   . TYR B 424 ? 0.323546  0.339491 0.301667 0.12779     -0.0227163  -0.0236939  424  TYR B O   
8380  C  CB  . TYR B 424 ? 0.374142  0.382994 0.345274 0.16365     -0.0239294  -0.0317117  424  TYR B CB  
8381  C  CG  . TYR B 424 ? 0.343224  0.370949 0.331283 0.14848     -0.0182941  -0.036185   424  TYR B CG  
8382  C  CD1 . TYR B 424 ? 0.350607  0.360556 0.332188 0.135683    -0.0121719  -0.0341636  424  TYR B CD1 
8383  C  CD2 . TYR B 424 ? 0.331006  0.393787 0.340619 0.146823    -0.0189059  -0.0426168  424  TYR B CD2 
8384  C  CE1 . TYR B 424 ? 0.341989  0.366731 0.335373 0.1235      -0.00740699 -0.0375617  424  TYR B CE1 
8385  C  CE2 . TYR B 424 ? 0.327652  0.403681 0.34912  0.133502    -0.0125852  -0.0458091  424  TYR B CE2 
8386  C  CZ  . TYR B 424 ? 0.334003  0.39017  0.346056 0.12224     -0.00717533 -0.0426779  424  TYR B CZ  
8387  O  OH  . TYR B 424 ? 0.304135  0.371035 0.324391 0.110181    -0.00142483 -0.0449777  424  TYR B OH  
8388  N  N   . LEU B 425 ? 0.334211  0.375068 0.317585 0.151741    -0.0342107  -0.0280889  425  LEU B N   
8389  C  CA  . LEU B 425 ? 0.314383  0.379411 0.313269 0.140322    -0.0358385  -0.0305995  425  LEU B CA  
8390  C  C   . LEU B 425 ? 0.31717   0.364844 0.304345 0.130151    -0.0351124  -0.023756   425  LEU B C   
8391  O  O   . LEU B 425 ? 0.282728  0.339906 0.279143 0.116174    -0.0331003  -0.0243145  425  LEU B O   
8392  C  CB  . LEU B 425 ? 0.323224  0.418783 0.335747 0.150187    -0.0437061  -0.0371724  425  LEU B CB  
8393  C  CG  . LEU B 425 ? 0.327922  0.451791 0.361461 0.15355     -0.0422407  -0.0463644  425  LEU B CG  
8394  C  CD1 . LEU B 425 ? 0.346211  0.500932 0.393431 0.165888    -0.0507923  -0.0540664  425  LEU B CD1 
8395  C  CD2 . LEU B 425 ? 0.302663  0.439142 0.35173  0.135938    -0.0342852  -0.0494174  425  LEU B CD2 
8396  N  N   . LEU B 426 ? 0.334375  0.354851 0.300011 0.137421    -0.0359765  -0.0171966  426  LEU B N   
8397  C  CA  . LEU B 426 ? 0.334458  0.338784 0.28836  0.128553    -0.0344028  -0.010934   426  LEU B CA  
8398  C  C   . LEU B 426 ? 0.316762  0.307595 0.271016 0.113414    -0.026343   -0.0090452  426  LEU B C   
8399  O  O   . LEU B 426 ? 0.288738  0.282084 0.246735 0.101076    -0.0243568  -0.00779955 426  LEU B O   
8400  C  CB  . LEU B 426 ? 0.370216  0.348418 0.299546 0.141021    -0.0364318  -0.00442606 426  LEU B CB  
8401  C  CG  . LEU B 426 ? 0.38601   0.347582 0.300287 0.134714    -0.0347722  0.00222715  426  LEU B CG  
8402  C  CD1 . LEU B 426 ? 0.384863  0.324148 0.293939 0.121255    -0.025469   0.0057533   426  LEU B CD1 
8403  C  CD2 . LEU B 426 ? 0.359207  0.343525 0.284903 0.126898    -0.0383321  -0.00031632 426  LEU B CD2 
8404  N  N   . LYS B 427 ? 0.316311  0.292679 0.266109 0.114955    -0.0221035  -0.00937582 427  LYS B N   
8405  C  CA  . LYS B 427 ? 0.318733  0.286043 0.270358 0.100986    -0.0156678  -0.00925184 427  LYS B CA  
8406  C  C   . LYS B 427 ? 0.275146  0.267185 0.245429 0.0904089   -0.015148   -0.0134648  427  LYS B C   
8407  O  O   . LYS B 427 ? 0.2589    0.248879 0.231019 0.0783077   -0.0124617  -0.0121198  427  LYS B O   
8408  C  CB  . LYS B 427 ? 0.347204  0.296223 0.291111 0.105172    -0.0118545  -0.0105212  427  LYS B CB  
8409  C  CG  . LYS B 427 ? 0.363479  0.300551 0.306663 0.0913749   -0.00596605 -0.0110426  427  LYS B CG  
8410  C  CD  . LYS B 427 ? 0.411505  0.330793 0.346791 0.0959806   -0.00267737 -0.0136999  427  LYS B CD  
8411  C  CE  . LYS B 427 ? 0.445752  0.351208 0.378135 0.0827799   0.00214646  -0.0145165  427  LYS B CE  
8412  N  NZ  . LYS B 427 ? 0.497148  0.425391 0.444412 0.0733737   0.00176476  -0.0178029  427  LYS B NZ  
8413  N  N   . MET B 428 ? 0.257792  0.272791 0.241475 0.0952988   -0.0173511  -0.0187032  428  MET B N   
8414  C  CA  . MET B 428 ? 0.256165  0.292672 0.256021 0.0855682   -0.0156044  -0.0225987  428  MET B CA  
8415  C  C   . MET B 428 ? 0.255053  0.300365 0.259192 0.0785889   -0.0182095  -0.0212135  428  MET B C   
8416  O  O   . MET B 428 ? 0.242592  0.292676 0.25272  0.0673549   -0.015618   -0.02138    428  MET B O   
8417  C  CB  . MET B 428 ? 0.255914  0.314647 0.26911  0.0922505   -0.0159587  -0.0290731  428  MET B CB  
8418  C  CG  . MET B 428 ? 0.301913  0.352658 0.311526 0.0978277   -0.0120234  -0.0314053  428  MET B CG  
8419  S  SD  . MET B 428 ? 0.339744  0.37468  0.34325  0.085034    -0.0054675  -0.0299565  428  MET B SD  
8420  C  CE  . MET B 428 ? 0.266385  0.322138 0.283664 0.0719109   -0.00322445 -0.0312678  428  MET B CE  
8421  N  N   . ALA B 429 ? 0.239952  0.284886 0.238521 0.0859075   -0.023461   -0.0195903  429  ALA B N   
8422  C  CA  . ALA B 429 ? 0.221889  0.273773 0.222875 0.0797132   -0.0259365  -0.0188906  429  ALA B CA  
8423  C  C   . ALA B 429 ? 0.22782   0.261571 0.219763 0.0700645   -0.0220931  -0.0137627  429  ALA B C   
8424  O  O   . ALA B 429 ? 0.214818  0.255274 0.212708 0.0610075   -0.0214872  -0.0143003  429  ALA B O   
8425  C  CB  . ALA B 429 ? 0.236423  0.290851 0.230846 0.0905578   -0.032612   -0.0185164  429  ALA B CB  
8426  N  N   . LEU B 430 ? 0.237756  0.24895  0.215745 0.0720669   -0.0193683  -0.00940014 430  LEU B N   
8427  C  CA  . LEU B 430 ? 0.260655  0.257048 0.232008 0.062749    -0.0152711  -0.00572835 430  LEU B CA  
8428  C  C   . LEU B 430 ? 0.258607  0.261644 0.240181 0.0521364   -0.0122062  -0.00809511 430  LEU B C   
8429  O  O   . LEU B 430 ? 0.237757  0.239385 0.22026  0.0438692   -0.0105952  -0.00698505 430  LEU B O   
8430  C  CB  . LEU B 430 ? 0.283069  0.254814 0.239483 0.0659831   -0.0118667  -0.0021536  430  LEU B CB  
8431  C  CG  . LEU B 430 ? 0.315644  0.273116 0.255693 0.0763083   -0.01371    0.00227254  430  LEU B CG  
8432  C  CD1 . LEU B 430 ? 0.337578  0.266694 0.261781 0.0784229   -0.00876333 0.00574303  430  LEU B CD1 
8433  C  CD2 . LEU B 430 ? 0.31954   0.277379 0.254647 0.0727146   -0.0142487  0.00526975  430  LEU B CD2 
8434  N  N   . GLU B 431 ? 0.26024   0.270623 0.248606 0.0533717   -0.0113693  -0.0115202  431  GLU B N   
8435  C  CA  . GLU B 431 ? 0.282557  0.297797 0.277481 0.0449478   -0.00859005 -0.0134182  431  GLU B CA  
8436  C  C   . GLU B 431 ? 0.253644  0.286114 0.259283 0.040375    -0.00939284 -0.0153824  431  GLU B C   
8437  O  O   . GLU B 431 ? 0.246905  0.279309 0.254038 0.0329839   -0.00815936 -0.0147259  431  GLU B O   
8438  C  CB  . GLU B 431 ? 0.303766  0.315057 0.297326 0.0482923   -0.00625262 -0.0158904  431  GLU B CB  
8439  C  CG  . GLU B 431 ? 0.375765  0.391556 0.373345 0.0409314   -0.00363903 -0.0177929  431  GLU B CG  
8440  C  CD  . GLU B 431 ? 0.466474  0.48033  0.462317 0.045007    -0.00123539 -0.0210357  431  GLU B CD  
8441  O  OE1 . GLU B 431 ? 0.418457  0.43871  0.416996 0.0408714   0.00104974  -0.0228649  431  GLU B OE1 
8442  O  OE2 . GLU B 431 ? 0.462611  0.468018 0.453293 0.052755    -0.00142004 -0.0216608  431  GLU B OE2 
8443  N  N   . LYS B 432 ? 0.208599  0.255678 0.22172  0.0447866   -0.0114901  -0.0182325  432  LYS B N   
8444  C  CA  . LYS B 432 ? 0.196648  0.259824 0.220992 0.0394473   -0.0107153  -0.0214129  432  LYS B CA  
8445  C  C   . LYS B 432 ? 0.208034  0.277709 0.235247 0.0375617   -0.01434    -0.0218661  432  LYS B C   
8446  O  O   . LYS B 432 ? 0.231602  0.30298  0.262024 0.029609    -0.0127934  -0.0220844  432  LYS B O   
8447  C  CB  . LYS B 432 ? 0.198963  0.277965 0.232946 0.0439978   -0.00989646 -0.0262907  432  LYS B CB  
8448  C  CG  . LYS B 432 ? 0.224742  0.298195 0.25556  0.0465224   -0.00583041 -0.0268509  432  LYS B CG  
8449  C  CD  . LYS B 432 ? 0.227659  0.295692 0.256075 0.0377038   -0.00087679 -0.0257116  432  LYS B CD  
8450  C  CE  . LYS B 432 ? 0.235195  0.297947 0.258899 0.0403134   0.00299317  -0.0271293  432  LYS B CE  
8451  N  NZ  . LYS B 432 ? 0.245504  0.304372 0.265536 0.0321819   0.00673861  -0.0258353  432  LYS B NZ  
8452  N  N   A ILE B 433 ? 0.187077  0.258773 0.211379 0.0453788   -0.019156   -0.0220743  433  ILE B N   
8453  N  N   B ILE B 433 ? 0.190509  0.262216 0.214807 0.0454995   -0.0191531  -0.0220881  433  ILE B N   
8454  C  CA  A ILE B 433 ? 0.174873  0.253488 0.200874 0.0440732   -0.0230926  -0.0235043  433  ILE B CA  
8455  C  CA  B ILE B 433 ? 0.181391  0.259537 0.206769 0.044786    -0.0232965  -0.023351   433  ILE B CA  
8456  C  C   A ILE B 433 ? 0.177058  0.240829 0.193197 0.03973     -0.0221772  -0.0189973  433  ILE B C   
8457  C  C   B ILE B 433 ? 0.180033  0.24379  0.196271 0.0397032   -0.0220868  -0.0190001  433  ILE B C   
8458  O  O   A ILE B 433 ? 0.174157  0.241632 0.193061 0.034217    -0.0228     -0.0203924  433  ILE B O   
8459  O  O   B ILE B 433 ? 0.177336  0.245042 0.196842 0.0338438   -0.0224883  -0.0204756  433  ILE B O   
8460  C  CB  A ILE B 433 ? 0.176357  0.263237 0.201029 0.0550117   -0.0293968  -0.0256816  433  ILE B CB  
8461  C  CB  B ILE B 433 ? 0.186647  0.269349 0.207954 0.056365    -0.0294017  -0.0243937  433  ILE B CB  
8462  C  CG1 A ILE B 433 ? 0.164288  0.270312 0.202029 0.0596347   -0.0303273  -0.0316481  433  ILE B CG1 
8463  C  CG1 B ILE B 433 ? 0.182638  0.283852 0.215853 0.0622052   -0.0310704  -0.030139   433  ILE B CG1 
8464  C  CG2 A ILE B 433 ? 0.173303  0.26673  0.197752 0.0537651   -0.034044   -0.0277821  433  ILE B CG2 
8465  C  CG2 B ILE B 433 ? 0.185333  0.273794 0.205468 0.0556212   -0.0340886  -0.0260903  433  ILE B CG2 
8466  C  CD1 A ILE B 433 ? 0.167378  0.284186 0.204791 0.0727855   -0.0376809  -0.034731   433  ILE B CD1 
8467  C  CD1 B ILE B 433 ? 0.174041  0.294794 0.224346 0.0529502   -0.0291217  -0.0363914  433  ILE B CD1 
8468  N  N   . ALA B 434 ? 0.174684  0.222131 0.179841 0.0420181   -0.0203524  -0.0143601  434  ALA B N   
8469  C  CA  . ALA B 434 ? 0.19895   0.235162 0.196758 0.037522    -0.0186436  -0.0110136  434  ALA B CA  
8470  C  C   . ALA B 434 ? 0.192029  0.230109 0.196113 0.0285795   -0.015971   -0.0118672  434  ALA B C   
8471  O  O   . ALA B 434 ? 0.207143  0.243364 0.209585 0.0251748   -0.0158842  -0.0113596  434  ALA B O   
8472  C  CB  . ALA B 434 ? 0.214274  0.233293 0.200854 0.0395205   -0.015831   -0.0068088  434  ALA B CB  
8473  N  N   . PHE B 435 ? 0.170599  0.212294 0.18072  0.0258313   -0.0138903  -0.0133163  435  PHE B N   
8474  C  CA  . PHE B 435 ? 0.164081  0.205103 0.177034 0.0192375   -0.0115215  -0.0134523  435  PHE B CA  
8475  C  C   . PHE B 435 ? 0.172205  0.220432 0.190547 0.0152196   -0.0121339  -0.0157507  435  PHE B C   
8476  O  O   . PHE B 435 ? 0.176064  0.219902 0.193207 0.0111126   -0.0111304  -0.0150832  435  PHE B O   
8477  C  CB  . PHE B 435 ? 0.176013  0.21764  0.190864 0.0183767   -0.00881338 -0.0141483  435  PHE B CB  
8478  C  CG  . PHE B 435 ? 0.171435  0.210161 0.185752 0.0129288   -0.00684238 -0.0135419  435  PHE B CG  
8479  C  CD1 . PHE B 435 ? 0.176482  0.207334 0.186009 0.0118984   -0.00701834 -0.0119323  435  PHE B CD1 
8480  C  CD2 . PHE B 435 ? 0.172395  0.215872 0.190424 0.0092501   -0.00467626 -0.0148201  435  PHE B CD2 
8481  C  CE1 . PHE B 435 ? 0.189131  0.217211 0.196626 0.00921561  -0.00630391 -0.0114049  435  PHE B CE1 
8482  C  CE2 . PHE B 435 ? 0.184427  0.221637 0.198401 0.00568792  -0.002669   -0.0133639  435  PHE B CE2 
8483  C  CZ  . PHE B 435 ? 0.172733  0.202247 0.180868 0.00673081  -0.0042156  -0.0115076  435  PHE B CZ  
8484  N  N   . LEU B 436 ? 0.177357  0.236697 0.201668 0.0167773   -0.0140914  -0.0191298  436  LEU B N   
8485  C  CA  . LEU B 436 ? 0.185463  0.251581 0.216263 0.0110648   -0.0136633  -0.0225968  436  LEU B CA  
8486  C  C   . LEU B 436 ? 0.173126  0.232491 0.199796 0.00803646  -0.0145016  -0.0221245  436  LEU B C   
8487  O  O   . LEU B 436 ? 0.156511  0.211888 0.184058 0.00242968  -0.0118547  -0.022564   436  LEU B O   
8488  C  CB  . LEU B 436 ? 0.184924  0.266803 0.224228 0.0132918   -0.016684   -0.027831   436  LEU B CB  
8489  C  CG  . LEU B 436 ? 0.17516   0.267009 0.221743 0.0153923   -0.014714   -0.0299128  436  LEU B CG  
8490  C  CD1 . LEU B 436 ? 0.183931  0.294076 0.239577 0.0198332   -0.0194871  -0.0359432  436  LEU B CD1 
8491  C  CD2 . LEU B 436 ? 0.178547  0.270574 0.229609 0.00759259  -0.00810204 -0.0304824  436  LEU B CD2 
8492  N  N   . PRO B 437 ? 0.171474  0.228958 0.192801 0.0117772   -0.017731   -0.0216272  437  PRO B N   
8493  C  CA  . PRO B 437 ? 0.171342  0.223598 0.189234 0.00918579  -0.0179574  -0.0221624  437  PRO B CA  
8494  C  C   . PRO B 437 ? 0.169248  0.21137  0.183922 0.00698951  -0.0147111  -0.0188781  437  PRO B C   
8495  O  O   . PRO B 437 ? 0.188493  0.225966 0.20232  0.00415786  -0.0138106  -0.0197391  437  PRO B O   
8496  C  CB  . PRO B 437 ? 0.188624  0.240019 0.199185 0.0144878   -0.0209025  -0.0214688  437  PRO B CB  
8497  C  CG  . PRO B 437 ? 0.189403  0.240176 0.196917 0.0201049   -0.021325   -0.0185184  437  PRO B CG  
8498  C  CD  . PRO B 437 ? 0.183211  0.242361 0.199926 0.0190934   -0.0209176  -0.0206816  437  PRO B CD  
8499  N  N   . PHE B 438 ? 0.15228   0.190756 0.164894 0.00873393  -0.0133006  -0.0157252  438  PHE B N   
8500  C  CA  . PHE B 438 ? 0.156121  0.187766 0.166256 0.00757936  -0.0116348  -0.0138856  438  PHE B CA  
8501  C  C   . PHE B 438 ? 0.166748  0.196012 0.177947 0.00474628  -0.00988988 -0.0138458  438  PHE B C   
8502  O  O   . PHE B 438 ? 0.177047  0.200517 0.185669 0.00392858  -0.00938728 -0.0135237  438  PHE B O   
8503  C  CB  . PHE B 438 ? 0.14674   0.176039 0.155055 0.0093199   -0.0107816  -0.0117939  438  PHE B CB  
8504  C  CG  . PHE B 438 ? 0.175212  0.201148 0.182783 0.00853022  -0.0100809  -0.0113044  438  PHE B CG  
8505  C  CD1 . PHE B 438 ? 0.19546   0.221111 0.202669 0.00875486  -0.00995081 -0.0118316  438  PHE B CD1 
8506  C  CD2 . PHE B 438 ? 0.175495  0.200052 0.182689 0.00826491  -0.00976333 -0.0109828  438  PHE B CD2 
8507  C  CE1 . PHE B 438 ? 0.200871  0.226978 0.209503 0.00894157  -0.0100059  -0.0126102  438  PHE B CE1 
8508  C  CE2 . PHE B 438 ? 0.202678  0.226438 0.20943  0.00873114  -0.0105135  -0.0115178  438  PHE B CE2 
8509  C  CZ  . PHE B 438 ? 0.190823  0.21636  0.19932  0.00917275  -0.0108729  -0.0125838  438  PHE B CZ  
8510  N  N   . GLY B 439 ? 0.163588  0.196916 0.177662 0.00383316  -0.00861143 -0.0142643  439  GLY B N   
8511  C  CA  . GLY B 439 ? 0.163927  0.19465  0.177747 0.00029062  -0.0054541  -0.0141502  439  GLY B CA  
8512  C  C   . GLY B 439 ? 0.191697  0.218648 0.205618 -0.00388281 -0.00437323 -0.0158021  439  GLY B C   
8513  O  O   . GLY B 439 ? 0.190905  0.20846  0.199624 -0.00597827 -0.0016413  -0.0141881  439  GLY B O   
8514  N  N   . TYR B 440 ? 0.173502  0.206801 0.192203 -0.00502858 -0.00636872 -0.0193347  440  TYR B N   
8515  C  CA  . TYR B 440 ? 0.185242  0.214354 0.204249 -0.00979613 -0.00536503 -0.0222503  440  TYR B CA  
8516  C  C   . TYR B 440 ? 0.202134  0.220324 0.214028 -0.00736925 -0.00650168 -0.0209183  440  TYR B C   
8517  O  O   . TYR B 440 ? 0.232836  0.239975 0.24048  -0.0101591  -0.00414936 -0.021076   440  TYR B O   
8518  C  CB  . TYR B 440 ? 0.195297  0.236938 0.221666 -0.0107851  -0.00839962 -0.0276087  440  TYR B CB  
8519  C  CG  . TYR B 440 ? 0.229978  0.270471 0.259373 -0.0175041  -0.00737489 -0.0329206  440  TYR B CG  
8520  C  CD1 . TYR B 440 ? 0.290243  0.320649 0.318287 -0.0244264  -0.00176661 -0.0328423  440  TYR B CD1 
8521  C  CD2 . TYR B 440 ? 0.263428  0.31142  0.295598 -0.0171792  -0.0117055  -0.0382769  440  TYR B CD2 
8522  C  CE1 . TYR B 440 ? 0.297717  0.32503  0.328439 -0.0320488  0.00013271  -0.0383191  440  TYR B CE1 
8523  C  CE2 . TYR B 440 ? 0.279709  0.327344 0.315528 -0.0243044  -0.0109721  -0.0446936  440  TYR B CE2 
8524  C  CZ  . TYR B 440 ? 0.287103  0.323729 0.322613 -0.0322725  -0.00473609 -0.0448009  440  TYR B CZ  
8525  O  OH  . TYR B 440 ? 0.298918  0.332176 0.337105 -0.0403084  -0.00323832 -0.0514279  440  TYR B OH  
8526  N  N   . LEU B 441 ? 0.18486   0.205144 0.19496  -0.00217472 -0.00937063 -0.0197829  441  LEU B N   
8527  C  CA  . LEU B 441 ? 0.179253  0.193146 0.185068 -3.785e-05  -0.0102398  -0.0205373  441  LEU B CA  
8528  C  C   . LEU B 441 ? 0.188488  0.19333  0.189278 0.00293294  -0.0093298  -0.0176583  441  LEU B C   
8529  O  O   . LEU B 441 ? 0.182886  0.18032  0.17977  0.0050615   -0.00946858 -0.0186075  441  LEU B O   
8530  C  CB  . LEU B 441 ? 0.181491  0.201906 0.187219 0.00362774  -0.0123623  -0.0208661  441  LEU B CB  
8531  C  CG  . LEU B 441 ? 0.177828  0.200331 0.183175 0.00672474  -0.0120378  -0.0176347  441  LEU B CG  
8532  C  CD1 . LEU B 441 ? 0.185877  0.204768 0.189651 0.00923812  -0.011444   -0.0172638  441  LEU B CD1 
8533  C  CD2 . LEU B 441 ? 0.170076  0.197369 0.173851 0.00861587  -0.0128543  -0.0177019  441  LEU B CD2 
8534  N  N   . VAL B 442 ? 0.172352  0.178337 0.172741 0.00439878  -0.00905004 -0.0146693  442  VAL B N   
8535  C  CA  . VAL B 442 ? 0.186853  0.187304 0.182624 0.00874     -0.00977729 -0.0127546  442  VAL B CA  
8536  C  C   . VAL B 442 ? 0.196971  0.183484 0.185059 0.00919518  -0.00839468 -0.0119156  442  VAL B C   
8537  O  O   . VAL B 442 ? 0.224947  0.205842 0.208993 0.0143953   -0.00989401 -0.0121199  442  VAL B O   
8538  C  CB  . VAL B 442 ? 0.186359  0.190045 0.181812 0.00993195  -0.0101648  -0.0106529  442  VAL B CB  
8539  C  CG1 . VAL B 442 ? 0.194924  0.193915 0.184848 0.0152834   -0.0121524  -0.00959228 442  VAL B CG1 
8540  C  CG2 . VAL B 442 ? 0.168852  0.182504 0.170162 0.00985573  -0.0110711  -0.0114969  442  VAL B CG2 
8541  N  N   . ASP B 443 ? 0.198442  0.17851  0.183851 0.0040537   -0.00497102 -0.0109477  443  ASP B N   
8542  C  CA  . ASP B 443 ? 0.220525  0.183323 0.196158 0.00368098  -0.00231065 -0.00948599 443  ASP B CA  
8543  C  C   . ASP B 443 ? 0.225813  0.183149 0.202347 0.00089327  -0.00168385 -0.0133184  443  ASP B C   
8544  O  O   . ASP B 443 ? 0.257147  0.198497 0.224655 0.00341937  -0.00072148 -0.0126843  443  ASP B O   
8545  C  CB  . ASP B 443 ? 0.253323  0.208424 0.223212 -0.00094385 0.00263517  -0.00651841 443  ASP B CB  
8546  C  CG  . ASP B 443 ? 0.26857   0.219395 0.229242 0.00493105  0.001749    -0.00213939 443  ASP B CG  
8547  O  OD1 . ASP B 443 ? 0.27065   0.226074 0.231069 0.01255     -0.00343769 -0.00208701 443  ASP B OD1 
8548  O  OD2 . ASP B 443 ? 0.286206  0.229556 0.239679 0.00177522  0.00644875  0.0006882   443  ASP B OD2 
8549  N  N   . GLN B 444 ? 0.215821  0.185285 0.201444 -0.00245672 -0.00302695 -0.017516   444  GLN B N   
8550  C  CA  . GLN B 444 ? 0.227182  0.191585 0.211991 -0.00317894 -0.00360413 -0.0219578  444  GLN B CA  
8551  C  C   . GLN B 444 ? 0.234794  0.194907 0.214918 0.00547988  -0.00601265 -0.0215841  444  GLN B C   
8552  O  O   . GLN B 444 ? 0.257974  0.203943 0.231188 0.00757027  -0.00518891 -0.022934   444  GLN B O   
8553  C  CB  . GLN B 444 ? 0.238812  0.218018 0.232182 -0.00641266 -0.00573004 -0.0265857  444  GLN B CB  
8554  C  CG  . GLN B 444 ? 0.310421  0.294151 0.30974  -0.0149719  -0.00349144 -0.0292966  444  GLN B CG  
8555  C  CD  . GLN B 444 ? 0.397865  0.394185 0.40386  -0.0172263  -0.00672041 -0.0355429  444  GLN B CD  
8556  O  OE1 . GLN B 444 ? 0.453598  0.445087 0.457184 -0.0181656  -0.00778293 -0.04028    444  GLN B OE1 
8557  N  NE2 . GLN B 444 ? 0.378446  0.390626 0.391517 -0.0167094  -0.00883238 -0.0357029  444  GLN B NE2 
8558  N  N   . TRP B 445 ? 0.216507  0.188139 0.20035  0.0105902   -0.00849894 -0.0200278  445  TRP B N   
8559  C  CA  . TRP B 445 ? 0.218576  0.189587 0.200423 0.0186258   -0.0103489  -0.0205018  445  TRP B CA  
8560  C  C   . TRP B 445 ? 0.238189  0.193928 0.210469 0.0240375   -0.0103771  -0.0177552  445  TRP B C   
8561  O  O   . TRP B 445 ? 0.243177  0.187758 0.209267 0.0295907   -0.0106761  -0.0192045  445  TRP B O   
8562  C  CB  . TRP B 445 ? 0.203711  0.190825 0.192753 0.0210125   -0.0120341  -0.0199651  445  TRP B CB  
8563  C  CG  . TRP B 445 ? 0.22667   0.217621 0.216868 0.0286424   -0.0135197  -0.0217996  445  TRP B CG  
8564  C  CD1 . TRP B 445 ? 0.227012  0.221794 0.219076 0.0312132   -0.0128946  -0.0255831  445  TRP B CD1 
8565  C  CD2 . TRP B 445 ? 0.228271  0.220488 0.217799 0.0353879   -0.0159881  -0.0208045  445  TRP B CD2 
8566  N  NE1 . TRP B 445 ? 0.226972  0.227077 0.221558 0.0387898   -0.014259   -0.0272558  445  TRP B NE1 
8567  C  CE2 . TRP B 445 ? 0.232016  0.23155  0.225632 0.0416732   -0.0167878  -0.0246226  445  TRP B CE2 
8568  C  CE3 . TRP B 445 ? 0.240723  0.229952 0.226425 0.0371272   -0.0177901  -0.0176137  445  TRP B CE3 
8569  C  CZ2 . TRP B 445 ? 0.231166  0.236184 0.226553 0.0501433   -0.0200253  -0.0259222  445  TRP B CZ2 
8570  C  CZ3 . TRP B 445 ? 0.236259  0.229642 0.221801 0.0456591   -0.0214887  -0.0185455  445  TRP B CZ3 
8571  C  CH2 . TRP B 445 ? 0.243694  0.245624 0.23481  0.0522098   -0.0229336  -0.022859   445  TRP B CH2 
8572  N  N   . ARG B 446 ? 0.242764  0.196132 0.21171  0.0233467   -0.00999759 -0.0136048  446  ARG B N   
8573  C  CA  . ARG B 446 ? 0.271931  0.211165 0.229302 0.0304714   -0.0108266  -0.0103678  446  ARG B CA  
8574  C  C   . ARG B 446 ? 0.285145  0.200548 0.230397 0.0283915   -0.00690804 -0.00914842 446  ARG B C   
8575  O  O   . ARG B 446 ? 0.304204  0.204568 0.238458 0.0367253   -0.00797583 -0.00780275 446  ARG B O   
8576  C  CB  . ARG B 446 ? 0.268119  0.212241 0.223759 0.031292    -0.0118957  -0.00677628 446  ARG B CB  
8577  C  CG  . ARG B 446 ? 0.314155  0.246948 0.256554 0.0398856   -0.0140431  -0.00309605 446  ARG B CG  
8578  C  CD  . ARG B 446 ? 0.282885  0.231643 0.230635 0.0410404   -0.0172534  -0.0030704  446  ARG B CD  
8579  N  NE  . ARG B 446 ? 0.256826  0.210475 0.208462 0.0319838   -0.0136511  -0.00197141 446  ARG B NE  
8580  C  CZ  . ARG B 446 ? 0.271624  0.232649 0.222998 0.0326845   -0.0152296  -0.00122923 446  ARG B CZ  
8581  N  NH1 . ARG B 446 ? 0.241899  0.205749 0.188857 0.0412299   -0.0205323  -0.00161269 446  ARG B NH1 
8582  N  NH2 . ARG B 446 ? 0.250085  0.216503 0.205928 0.0254587   -0.0119275  -0.00096418 446  ARG B NH2 
8583  N  N   . TRP B 447 ? 0.293049  0.204539 0.240192 0.0175458   -0.00230286 -0.0101546  447  TRP B N   
8584  C  CA  . TRP B 447 ? 0.312967  0.201235 0.249824 0.0138368   0.00222493  -0.0104894  447  TRP B CA  
8585  C  C   . TRP B 447 ? 0.319992  0.201467 0.255097 0.0190472   0.00035076  -0.0148563  447  TRP B C   
8586  O  O   . TRP B 447 ? 0.351724  0.209003 0.273632 0.0215055   0.00281017  -0.0139797  447  TRP B O   
8587  C  CB  . TRP B 447 ? 0.32194   0.210718 0.264429 0.00010752  0.00745366  -0.0130927  447  TRP B CB  
8588  C  CG  . TRP B 447 ? 0.306807  0.200208 0.250257 -0.00543558 0.0109253   -0.00945649 447  TRP B CG  
8589  C  CD1 . TRP B 447 ? 0.317037  0.20459  0.250795 -0.00028924 0.0113679   -0.00340503 447  TRP B CD1 
8590  C  CD2 . TRP B 447 ? 0.308422  0.215741 0.263722 -0.0162055  0.0139782   -0.0125048  447  TRP B CD2 
8591  N  NE1 . TRP B 447 ? 0.311161  0.206364 0.248985 -0.00767988 0.0154602   -0.002239   447  TRP B NE1 
8592  C  CE2 . TRP B 447 ? 0.309405  0.217667 0.261364 -0.0172218  0.0171288   -0.00781471 447  TRP B CE2 
8593  C  CE3 . TRP B 447 ? 0.313531  0.234159 0.281868 -0.0238923  0.0136597   -0.0192923  447  TRP B CE3 
8594  C  CZ2 . TRP B 447 ? 0.303474  0.225671 0.265715 -0.0256888  0.0207231   -0.00975106 447  TRP B CZ2 
8595  C  CZ3 . TRP B 447 ? 0.327376  0.262868 0.306436 -0.0319118  0.0163013   -0.0213932  447  TRP B CZ3 
8596  C  CH2 . TRP B 447 ? 0.310904  0.247435 0.287485 -0.0325832  0.0200052   -0.0166557  447  TRP B CH2 
8597  N  N   . GLY B 448 ? 0.301519  0.201483 0.248088 0.0201157   -0.00295404 -0.019667   448  GLY B N   
8598  C  CA  . GLY B 448 ? 0.291374  0.18551  0.235677 0.0254161   -0.00409827 -0.0243898  448  GLY B CA  
8599  C  C   . GLY B 448 ? 0.30099   0.191247 0.239332 0.0393985   -0.00727976 -0.0225404  448  GLY B C   
8600  O  O   . GLY B 448 ? 0.326301  0.202799 0.25722  0.0463152   -0.00739493 -0.0249     448  GLY B O   
8601  N  N   . VAL B 449 ? 0.284456  0.188617 0.226941 0.0442732   -0.0103723  -0.0193016  449  VAL B N   
8602  C  CA  . VAL B 449 ? 0.301343  0.204847 0.239595 0.0578747   -0.0143212  -0.0186168  449  VAL B CA  
8603  C  C   . VAL B 449 ? 0.336865  0.211569 0.256054 0.0633399   -0.0132186  -0.0139807  449  VAL B C   
8604  O  O   . VAL B 449 ? 0.380339  0.240892 0.2903   0.0738595   -0.0145623  -0.0149266  449  VAL B O   
8605  C  CB  . VAL B 449 ? 0.272687  0.199025 0.220637 0.0609646   -0.0182819  -0.0176514  449  VAL B CB  
8606  C  CG1 . VAL B 449 ? 0.28788   0.21332  0.230347 0.0754585   -0.0233415  -0.0171361  449  VAL B CG1 
8607  C  CG2 . VAL B 449 ? 0.255407  0.206415 0.21973  0.0568123   -0.018386   -0.0220813  449  VAL B CG2 
8608  N  N   . PHE B 450 ? 0.35305   0.217609 0.264609 0.0571073   -0.0103605  -0.00862108 450  PHE B N   
8609  C  CA  . PHE B 450 ? 0.389518  0.22382  0.27981  0.0621239   -0.00813472 -0.00321985 450  PHE B CA  
8610  C  C   . PHE B 450 ? 0.417176  0.224732 0.297193 0.0596144   -0.00334338 -0.00505444 450  PHE B C   
8611  O  O   . PHE B 450 ? 0.468846  0.250138 0.330498 0.0692984   -0.00305857 -0.00203446 450  PHE B O   
8612  C  CB  . PHE B 450 ? 0.39624   0.222775 0.279853 0.0526113   -0.00321949 0.00231719  450  PHE B CB  
8613  C  CG  . PHE B 450 ? 0.406512  0.247781 0.290748 0.0578638   -0.00751988 0.00568923  450  PHE B CG  
8614  C  CD1 . PHE B 450 ? 0.439014  0.277045 0.312923 0.0734282   -0.013731   0.00783895  450  PHE B CD1 
8615  C  CD2 . PHE B 450 ? 0.384427  0.241978 0.278626 0.047797    -0.0055742  0.00612015  450  PHE B CD2 
8616  C  CE1 . PHE B 450 ? 0.4407    0.293214 0.315243 0.0776897   -0.0182639  0.00963914  450  PHE B CE1 
8617  C  CE2 . PHE B 450 ? 0.399652  0.26845  0.292878 0.0521783   -0.00918271 0.0085491   450  PHE B CE2 
8618  C  CZ  . PHE B 450 ? 0.420404  0.287306 0.304186 0.0666279   -0.0157082  0.00995408  450  PHE B CZ  
8619  N  N   . SER B 451 ? 0.395122  0.207296 0.285197 0.0471453   0.00026191  -0.0101746  451  SER B N   
8620  C  CA  . SER B 451 ? 0.426635  0.213929 0.307742 0.0435193   0.00469345  -0.013457   451  SER B CA  
8621  C  C   . SER B 451 ? 0.447404  0.232019 0.327183 0.0556284   0.00100204  -0.0184425  451  SER B C   
8622  O  O   . SER B 451 ? 0.465367  0.224152 0.3337   0.0559717   0.00422958  -0.0208945  451  SER B O   
8623  C  CB  . SER B 451 ? 0.439388  0.233241 0.331263 0.0267976   0.00891154  -0.0185322  451  SER B CB  
8624  O  OG  . SER B 451 ? 0.414353  0.234744 0.322681 0.0263478   0.00474341  -0.0250248  451  SER B OG  
8625  N  N   . GLY B 452 ? 0.444142  0.254186 0.335135 0.0655217   -0.00506205 -0.020424   452  GLY B N   
8626  C  CA  . GLY B 452 ? 0.454235  0.267229 0.347282 0.076143    -0.00771659 -0.026425   452  GLY B CA  
8627  C  C   . GLY B 452 ? 0.444908  0.275066 0.351516 0.067863    -0.00668201 -0.0340005  452  GLY B C   
8628  O  O   . GLY B 452 ? 0.430626  0.268162 0.340838 0.075725    -0.00825461 -0.0395041  452  GLY B O   
8629  N  N   . ARG B 453 ? 0.419853  0.258938 0.334228 0.0530335   -0.00435388 -0.0345471  453  ARG B N   
8630  C  CA  . ARG B 453 ? 0.43729   0.291909 0.361845 0.0465472   -0.00425232 -0.0414764  453  ARG B CA  
8631  C  C   . ARG B 453 ? 0.382569  0.265878 0.31942  0.052707    -0.00749339 -0.0425786  453  ARG B C   
8632  O  O   . ARG B 453 ? 0.368446  0.261728 0.309738 0.0526185   -0.00735431 -0.0483125  453  ARG B O   
8633  C  CB  . ARG B 453 ? 0.468256  0.329297 0.399238 0.0310858   -0.00227006 -0.042439   453  ARG B CB  
8634  C  CG  . ARG B 453 ? 0.625386  0.459805 0.546596 0.0225205   0.00219983  -0.044407   453  ARG B CG  
8635  C  CD  . ARG B 453 ? 0.826819  0.671296 0.757168 0.00728283  0.00364776  -0.0487916  453  ARG B CD  
8636  N  NE  . ARG B 453 ? 0.997285  0.819332 0.921264 -0.00319673 0.00837622  -0.0533283  453  ARG B NE  
8637  C  CZ  . ARG B 453 ? 0.972444  0.799441 0.903877 -0.0177483  0.010794    -0.0574064  453  ARG B CZ  
8638  N  NH1 . ARG B 453 ? 0.893951  0.747374 0.838906 -0.0226931  0.0085762   -0.0568814  453  ARG B NH1 
8639  N  NH2 . ARG B 453 ? 0.964642  0.769762 0.890193 -0.0274167  0.0157103   -0.0625034  453  ARG B NH2 
8640  N  N   . THR B 454 ? 0.349322  0.245428 0.291169 0.0563616   -0.00976266 -0.0374016  454  THR B N   
8641  C  CA  . THR B 454 ? 0.303212  0.225451 0.257139 0.0609632   -0.0120065  -0.038313   454  THR B CA  
8642  C  C   . THR B 454 ? 0.310186  0.233265 0.262528 0.0749144   -0.015182   -0.0375038  454  THR B C   
8643  O  O   . THR B 454 ? 0.288866  0.215236 0.241223 0.0774396   -0.017768   -0.033017   454  THR B O   
8644  C  CB  . THR B 454 ? 0.295217  0.233678 0.257859 0.0524793   -0.012317   -0.034605   454  THR B CB  
8645  O  OG1 . THR B 454 ? 0.268476  0.206747 0.232309 0.0417361   -0.0102579  -0.0362908  454  THR B OG1 
8646  C  CG2 . THR B 454 ? 0.27493   0.238196 0.249635 0.0552183   -0.0134965  -0.035692   454  THR B CG2 
8647  N  N   . PRO B 455 ? 0.313675  0.237161 0.265756 0.0848936   -0.0154906  -0.042709   455  PRO B N   
8648  C  CA  . PRO B 455 ? 0.316064  0.245336 0.269258 0.0998333   -0.0193028  -0.0436128  455  PRO B CA  
8649  C  C   . PRO B 455 ? 0.29172   0.253556 0.262456 0.0995304   -0.020734   -0.0453843  455  PRO B C   
8650  O  O   . PRO B 455 ? 0.265218  0.241475 0.244909 0.0889984   -0.0178279  -0.0460472  455  PRO B O   
8651  C  CB  . PRO B 455 ? 0.331987  0.252603 0.280711 0.109059    -0.0180052  -0.0499138  455  PRO B CB  
8652  C  CG  . PRO B 455 ? 0.328802  0.254691 0.281572 0.097911    -0.0136221  -0.0538465  455  PRO B CG  
8653  C  CD  . PRO B 455 ? 0.310237  0.229397 0.260695 0.0832988   -0.0124845  -0.0488974  455  PRO B CD  
8654  N  N   . PRO B 456 ? 0.299916  0.274347 0.275898 0.111026    -0.0252995  -0.046576   456  PRO B N   
8655  C  CA  . PRO B 456 ? 0.271416  0.277749 0.265789 0.109694    -0.0260831  -0.0499164  456  PRO B CA  
8656  C  C   . PRO B 456 ? 0.254178  0.278729 0.26059  0.103935    -0.0204641  -0.0553701  456  PRO B C   
8657  O  O   . PRO B 456 ? 0.232266  0.275261 0.250017 0.0948846   -0.0180115  -0.0556579  456  PRO B O   
8658  C  CB  . PRO B 456 ? 0.303639  0.318114 0.300336 0.126877    -0.0321648  -0.0534078  456  PRO B CB  
8659  C  CG  . PRO B 456 ? 0.328506  0.312281 0.30439  0.134007    -0.0356954  -0.0473044  456  PRO B CG  
8660  C  CD  . PRO B 456 ? 0.331562  0.289258 0.295189 0.126207    -0.02996    -0.045329   456  PRO B CD  
8661  N  N   . SER B 457 ? 0.258836  0.274321 0.259894 0.108192    -0.0175804  -0.0592302  457  SER B N   
8662  C  CA  . SER B 457 ? 0.26239   0.293153 0.271598 0.104544    -0.0117214  -0.0646416  457  SER B CA  
8663  C  C   . SER B 457 ? 0.248198  0.275608 0.254428 0.0896192   -0.00768556 -0.0613074  457  SER B C   
8664  O  O   . SER B 457 ? 0.247355  0.288072 0.258972 0.0844818   -0.00247133 -0.0640115  457  SER B O   
8665  C  CB  . SER B 457 ? 0.294952  0.315221 0.297189 0.115032    -0.0102769  -0.0703634  457  SER B CB  
8666  O  OG  . SER B 457 ? 0.319149  0.312186 0.305712 0.109555    -0.00952481 -0.0677769  457  SER B OG  
8667  N  N   . ARG B 458 ? 0.235096  0.246655 0.233173 0.0827292   -0.00993121 -0.0552547  458  ARG B N   
8668  C  CA  . ARG B 458 ? 0.228309  0.23934  0.224806 0.070279    -0.00727029 -0.0525873  458  ARG B CA  
8669  C  C   . ARG B 458 ? 0.218202  0.232079 0.217687 0.0629989   -0.0091979  -0.0466993  458  ARG B C   
8670  O  O   . ARG B 458 ? 0.220906  0.229487 0.216721 0.0543098   -0.00835025 -0.043907   458  ARG B O   
8671  C  CB  . ARG B 458 ? 0.236408  0.2261   0.220385 0.0669821   -0.00703365 -0.0529509  458  ARG B CB  
8672  C  CG  . ARG B 458 ? 0.262528  0.251214 0.243024 0.0715631   -0.00409506 -0.0596493  458  ARG B CG  
8673  C  CD  . ARG B 458 ? 0.277501  0.247675 0.246792 0.0648124   -0.00410759 -0.0609414  458  ARG B CD  
8674  N  NE  . ARG B 458 ? 0.30631   0.25241  0.266359 0.0667453   -0.00602959 -0.0604196  458  ARG B NE  
8675  C  CZ  . ARG B 458 ? 0.337978  0.267582 0.290127 0.0751996   -0.00598697 -0.0639639  458  ARG B CZ  
8676  N  NH1 . ARG B 458 ? 0.336698  0.273242 0.290277 0.0846869   -0.0045312  -0.0694679  458  ARG B NH1 
8677  N  NH2 . ARG B 458 ? 0.363933  0.268382 0.305758 0.0739931   -0.00665194 -0.0622498  458  ARG B NH2 
8678  N  N   . TYR B 459 ? 0.211285  0.231835 0.215999 0.0673958   -0.0124981  -0.0452446  459  TYR B N   
8679  C  CA  . TYR B 459 ? 0.199536  0.22182  0.205868 0.0607238   -0.0141231  -0.0402914  459  TYR B CA  
8680  C  C   . TYR B 459 ? 0.183705  0.217502 0.19617  0.0509851   -0.0105227  -0.0394939  459  TYR B C   
8681  O  O   . TYR B 459 ? 0.177447  0.205126 0.186369 0.044118    -0.0106659  -0.0354657  459  TYR B O   
8682  C  CB  . TYR B 459 ? 0.20694   0.242246 0.221023 0.0661889   -0.017824   -0.0410092  459  TYR B CB  
8683  C  CG  . TYR B 459 ? 0.228642  0.251282 0.233896 0.0753771   -0.0230772  -0.0388814  459  TYR B CG  
8684  C  CD1 . TYR B 459 ? 0.246266  0.245047 0.237299 0.0784559   -0.023079   -0.0365008  459  TYR B CD1 
8685  C  CD2 . TYR B 459 ? 0.259527  0.294701 0.270426 0.0819888   -0.0279587  -0.0402673  459  TYR B CD2 
8686  C  CE1 . TYR B 459 ? 0.286081  0.270033 0.265932 0.0879272   -0.0270904  -0.0338775  459  TYR B CE1 
8687  C  CE2 . TYR B 459 ? 0.264859  0.287888 0.265016 0.0924794   -0.0333186  -0.0380859  459  TYR B CE2 
8688  C  CZ  . TYR B 459 ? 0.284712  0.280669 0.268233 0.0954474   -0.0324255  -0.0341878  459  TYR B CZ  
8689  O  OH  . TYR B 459 ? 0.352482  0.332982 0.322335 0.106687    -0.0369001  -0.0313507  459  TYR B OH  
8690  N  N   . ASN B 460 ? 0.173001  0.223064 0.194252 0.0504928   -0.00685101 -0.0431831  460  ASN B N   
8691  C  CA  . ASN B 460 ? 0.16045   0.217386 0.18448  0.0415245   -0.00274297 -0.0414339  460  ASN B CA  
8692  C  C   . ASN B 460 ? 0.16907   0.217437 0.183863 0.0378178   0.00011067  -0.040564   460  ASN B C   
8693  O  O   . ASN B 460 ? 0.159112  0.204817 0.170456 0.0315043   0.00101778  -0.0369994  460  ASN B O   
8694  C  CB  . ASN B 460 ? 0.161488  0.237347 0.197366 0.040507    0.00151535  -0.045358   460  ASN B CB  
8695  C  CG  . ASN B 460 ? 0.166103  0.24798  0.207334 0.0325424   0.00293202  -0.0430287  460  ASN B CG  
8696  O  OD1 . ASN B 460 ? 0.196743  0.274981 0.237801 0.0318561   -0.00164327 -0.0404434  460  ASN B OD1 
8697  N  ND2 . ASN B 460 ? 0.159037  0.246938 0.202432 0.0261315   0.00983978  -0.0434352  460  ASN B ND2 
8698  N  N   . PHE B 461 ? 0.169306  0.214609 0.179959 0.0425132   0.00147213  -0.0445248  461  PHE B N   
8699  C  CA  . PHE B 461 ? 0.182251  0.219026 0.182737 0.0400343   0.00284625  -0.0450196  461  PHE B CA  
8700  C  C   . PHE B 461 ? 0.186648  0.211311 0.181182 0.0356248   -0.00128056 -0.0415898  461  PHE B C   
8701  O  O   . PHE B 461 ? 0.185711  0.209727 0.175756 0.0308745   -0.00099337 -0.0399269  461  PHE B O   
8702  C  CB  . PHE B 461 ? 0.206287  0.239757 0.202995 0.0467602   0.00403912  -0.0507857  461  PHE B CB  
8703  C  CG  . PHE B 461 ? 0.211816  0.235281 0.197054 0.0456147   0.00433144  -0.0534413  461  PHE B CG  
8704  C  CD1 . PHE B 461 ? 0.217451  0.245811 0.197125 0.0427035   0.00813215  -0.0539361  461  PHE B CD1 
8705  C  CD2 . PHE B 461 ? 0.228274  0.236651 0.207244 0.0476902   0.00101561  -0.0559409  461  PHE B CD2 
8706  C  CE1 . PHE B 461 ? 0.222693  0.243169 0.190946 0.042253    0.00724213  -0.0571955  461  PHE B CE1 
8707  C  CE2 . PHE B 461 ? 0.240016  0.240494 0.209301 0.0462693   0.00091636  -0.0601998  461  PHE B CE2 
8708  C  CZ  . PHE B 461 ? 0.239143  0.24711  0.203462 0.0440146   0.00353102  -0.0611099  461  PHE B CZ  
8709  N  N   . ASP B 462 ? 0.187355  0.202298 0.181046 0.0375222   -0.00479222 -0.0408257  462  ASP B N   
8710  C  CA  . ASP B 462 ? 0.192697  0.197367 0.182209 0.0323735   -0.00730484 -0.0383911  462  ASP B CA  
8711  C  C   . ASP B 462 ? 0.180998  0.191229 0.174611 0.0274887   -0.00805699 -0.0336027  462  ASP B C   
8712  O  O   . ASP B 462 ? 0.166035  0.173962 0.157773 0.0225889   -0.00906267 -0.0324628  462  ASP B O   
8713  C  CB  . ASP B 462 ? 0.222275  0.211968 0.207392 0.0349481   -0.00906957 -0.0385407  462  ASP B CB  
8714  C  CG  . ASP B 462 ? 0.28368   0.262204 0.261912 0.0374825   -0.00843126 -0.0437358  462  ASP B CG  
8715  O  OD1 . ASP B 462 ? 0.298948  0.283107 0.276029 0.0372728   -0.00705209 -0.047475   462  ASP B OD1 
8716  O  OD2 . ASP B 462 ? 0.322779  0.28576  0.295354 0.0403432   -0.0089732  -0.0441532  462  ASP B OD2 
8717  N  N   . TRP B 463 ? 0.168755  0.187064 0.168458 0.0291294   -0.00776427 -0.0317955  463  TRP B N   
8718  C  CA  . TRP B 463 ? 0.164532  0.187906 0.16762  0.0247344   -0.00790106 -0.0281106  463  TRP B CA  
8719  C  C   . TRP B 463 ? 0.158269  0.185496 0.159413 0.0208747   -0.00571405 -0.0272811  463  TRP B C   
8720  O  O   . TRP B 463 ? 0.149411  0.174094 0.148174 0.0177092   -0.00707607 -0.0251981  463  TRP B O   
8721  C  CB  . TRP B 463 ? 0.164834  0.196928 0.175078 0.0268581   -0.00808409 -0.0280397  463  TRP B CB  
8722  C  CG  . TRP B 463 ? 0.165318  0.201807 0.178776 0.0222159   -0.00774313 -0.0252878  463  TRP B CG  
8723  C  CD1 . TRP B 463 ? 0.173285  0.217628 0.190932 0.0189743   -0.00443882 -0.0255818  463  TRP B CD1 
8724  C  CD2 . TRP B 463 ? 0.178937  0.210793 0.190853 0.0204185   -0.0100706  -0.0222751  463  TRP B CD2 
8725  N  NE1 . TRP B 463 ? 0.172629  0.21652  0.191325 0.0155173   -0.00503797 -0.0231778  463  TRP B NE1 
8726  C  CE2 . TRP B 463 ? 0.177166  0.214612 0.19277  0.0168797   -0.0087239  -0.0213492  463  TRP B CE2 
8727  C  CE3 . TRP B 463 ? 0.206305  0.228863 0.213351 0.0211249   -0.0122534  -0.0204303  463  TRP B CE3 
8728  C  CZ2 . TRP B 463 ? 0.197474  0.232266 0.212148 0.0150273   -0.0102046  -0.0190661  463  TRP B CZ2 
8729  C  CZ3 . TRP B 463 ? 0.197078  0.218161 0.203413 0.0188935   -0.0130431  -0.0178629  463  TRP B CZ3 
8730  C  CH2 . TRP B 463 ? 0.190633  0.218402 0.200971 0.016412    -0.0124004  -0.0174615  463  TRP B CH2 
8731  N  N   . TRP B 464 ? 0.155871  0.188577 0.15679  0.0219546   -0.00219623 -0.0292017  464  TRP B N   
8732  C  CA  . TRP B 464 ? 0.156681  0.190312 0.152332 0.0192874   0.00042067  -0.0275002  464  TRP B CA  
8733  C  C   . TRP B 464 ? 0.15335   0.181518 0.140565 0.0195515   -0.00200159 -0.0285758  464  TRP B C   
8734  O  O   . TRP B 464 ? 0.15002   0.177507 0.132009 0.0183186   -0.00240702 -0.0262383  464  TRP B O   
8735  C  CB  . TRP B 464 ? 0.16383   0.204063 0.160221 0.0192304   0.00652959  -0.0287531  464  TRP B CB  
8736  C  CG  . TRP B 464 ? 0.168258  0.214752 0.173425 0.0162288   0.00859282  -0.027515   464  TRP B CG  
8737  C  CD1 . TRP B 464 ? 0.170269  0.226469 0.186125 0.0172227   0.00949638  -0.0307485  464  TRP B CD1 
8738  C  CD2 . TRP B 464 ? 0.171287  0.214654 0.175026 0.011988    0.00936878  -0.0234998  464  TRP B CD2 
8739  N  NE1 . TRP B 464 ? 0.172978  0.232851 0.194719 0.0128329   0.0104825   -0.0295074  464  TRP B NE1 
8740  C  CE2 . TRP B 464 ? 0.181353  0.232179 0.19531  0.00941771  0.0109334   -0.0249159  464  TRP B CE2 
8741  C  CE3 . TRP B 464 ? 0.194332  0.229563 0.18894  0.0109852   0.00851526  -0.0195046  464  TRP B CE3 
8742  C  CZ2 . TRP B 464 ? 0.179848  0.228203 0.194645 0.00480858  0.0122618   -0.0225061  464  TRP B CZ2 
8743  C  CZ3 . TRP B 464 ? 0.196065  0.228326 0.191008 0.00772945  0.00988798  -0.0164546  464  TRP B CZ3 
8744  C  CH2 . TRP B 464 ? 0.19208   0.229796 0.196645 0.00428083  0.0119143   -0.0179792  464  TRP B CH2 
8745  N  N   . TYR B 465 ? 0.164086  0.188317 0.149444 0.0216083   -0.0036611  -0.0326403  465  TYR B N   
8746  C  CA  . TYR B 465 ? 0.172413  0.192316 0.151741 0.0206722   -0.00690521 -0.0353508  465  TYR B CA  
8747  C  C   . TYR B 465 ? 0.16945   0.189585 0.15173  0.0171918   -0.0102659  -0.032861   465  TYR B C   
8748  O  O   . TYR B 465 ? 0.16523   0.188103 0.143733 0.0166703   -0.0125273  -0.032974   465  TYR B O   
8749  C  CB  . TYR B 465 ? 0.187175  0.199686 0.165273 0.021901    -0.00813745 -0.0404261  465  TYR B CB  
8750  C  CG  . TYR B 465 ? 0.200083  0.20925  0.174489 0.0187772   -0.0117159  -0.0443159  465  TYR B CG  
8751  C  CD1 . TYR B 465 ? 0.211976  0.222967 0.178452 0.0200459   -0.0126653  -0.0485538  465  TYR B CD1 
8752  C  CD2 . TYR B 465 ? 0.2085    0.21416  0.187425 0.0142363   -0.0139248  -0.0442157  465  TYR B CD2 
8753  C  CE1 . TYR B 465 ? 0.230844  0.241577 0.195272 0.0170532   -0.0169194  -0.053602   465  TYR B CE1 
8754  C  CE2 . TYR B 465 ? 0.237309  0.243208 0.21564  0.010161    -0.0169704  -0.0490639  465  TYR B CE2 
8755  C  CZ  . TYR B 465 ? 0.239909  0.249031 0.211671 0.0116485   -0.019047   -0.0542144  465  TYR B CZ  
8756  O  OH  . TYR B 465 ? 0.255719  0.268133 0.228193 0.00767308  -0.0231062  -0.0602579  465  TYR B OH  
8757  N  N   . LEU B 466 ? 0.163063  0.181083 0.151564 0.0157112   -0.010621   -0.0307516  466  LEU B N   
8758  C  CA  . LEU B 466 ? 0.169098  0.187524 0.161007 0.012298    -0.0127306  -0.0291201  466  LEU B CA  
8759  C  C   . LEU B 466 ? 0.159674  0.18367  0.152112 0.0125735   -0.0125071  -0.0252196  466  LEU B C   
8760  O  O   . LEU B 466 ? 0.146208  0.173414 0.139022 0.011691    -0.0147319  -0.0250932  466  LEU B O   
8761  C  CB  . LEU B 466 ? 0.167671  0.18017  0.162907 0.0112168   -0.0122275  -0.0276485  466  LEU B CB  
8762  C  CG  . LEU B 466 ? 0.198722  0.201196 0.191194 0.0102406   -0.0122183  -0.0311147  466  LEU B CG  
8763  C  CD1 . LEU B 466 ? 0.21648   0.209892 0.208214 0.0110522   -0.0111661  -0.0282704  466  LEU B CD1 
8764  C  CD2 . LEU B 466 ? 0.199413  0.202143 0.192868 0.00475527  -0.0135079  -0.0346654  466  LEU B CD2 
8765  N  N   . ARG B 467 ? 0.172919  0.19807  0.1659   0.0138297   -0.00966787 -0.0225982  467  ARG B N   
8766  C  CA  . ARG B 467 ? 0.181493  0.208259 0.173169 0.013643    -0.00855042 -0.0190554  467  ARG B CA  
8767  C  C   . ARG B 467 ? 0.202388  0.228965 0.185515 0.0156908   -0.00929354 -0.0187958  467  ARG B C   
8768  O  O   . ARG B 467 ? 0.203751  0.230407 0.184628 0.0168674   -0.0110456  -0.0167094  467  ARG B O   
8769  C  CB  . ARG B 467 ? 0.189389  0.217305 0.183609 0.012987    -0.00462986 -0.0175455  467  ARG B CB  
8770  C  CG  . ARG B 467 ? 0.189272  0.21865  0.190893 0.0125905   -0.00560784 -0.0182207  467  ARG B CG  
8771  C  CD  . ARG B 467 ? 0.197152  0.226355 0.201384 0.0109173   -0.0061247  -0.0159419  467  ARG B CD  
8772  N  NE  . ARG B 467 ? 0.201011  0.232158 0.206766 0.00905725  -0.00268043 -0.0154064  467  ARG B NE  
8773  C  CZ  . ARG B 467 ? 0.211338  0.241033 0.218188 0.0069086   -0.00183761 -0.0140252  467  ARG B CZ  
8774  N  NH1 . ARG B 467 ? 0.185731  0.211849 0.190462 0.00745091  -0.00391968 -0.0121928  467  ARG B NH1 
8775  N  NH2 . ARG B 467 ? 0.202953  0.234824 0.212997 0.00385646  0.00176689  -0.0150978  467  ARG B NH2 
8776  N  N   . THR B 468 ? 0.191703  0.217693 0.16875  0.0172319   -0.00789284 -0.0208189  468  THR B N   
8777  C  CA  . THR B 468 ? 0.200715  0.225755 0.1667   0.0203077   -0.00915003 -0.0207162  468  THR B CA  
8778  C  C   . THR B 468 ? 0.197127  0.226177 0.16422  0.0210997   -0.0156195  -0.0243362  468  THR B C   
8779  O  O   . THR B 468 ? 0.192691  0.223398 0.154935 0.0242625   -0.0187066  -0.0230724  468  THR B O   
8780  C  CB  . THR B 468 ? 0.22212   0.245578 0.179957 0.0218065   -0.00532177 -0.0223409  468  THR B CB  
8781  O  OG1 . THR B 468 ? 0.228765  0.251723 0.189479 0.0197695   0.00131204  -0.0199473  468  THR B OG1 
8782  C  CG2 . THR B 468 ? 0.236096  0.257292 0.179052 0.0259483   -0.00677378 -0.0220901  468  THR B CG2 
8783  N  N   . LYS B 469 ? 0.182685  0.21309  0.155769 0.0184459   -0.0175264  -0.0292735  469  LYS B N   
8784  C  CA  . LYS B 469 ? 0.196694  0.232118 0.172882 0.0170841   -0.0227425  -0.0343648  469  LYS B CA  
8785  C  C   . LYS B 469 ? 0.189843  0.231128 0.172051 0.017007    -0.0251419  -0.0324423  469  LYS B C   
8786  O  O   . LYS B 469 ? 0.193076  0.241743 0.174272 0.0195002   -0.0299065  -0.0351627  469  LYS B O   
8787  C  CB  . LYS B 469 ? 0.208392  0.240686 0.191228 0.0122193   -0.0224219  -0.0388275  469  LYS B CB  
8788  C  CG  . LYS B 469 ? 0.226234  0.264005 0.214651 0.00817206  -0.026443   -0.045102   469  LYS B CG  
8789  C  CD  . LYS B 469 ? 0.224568  0.2549   0.216553 0.00248145  -0.0248825  -0.0497032  469  LYS B CD  
8790  C  CE  . LYS B 469 ? 0.260131  0.298335 0.25946  -0.00311562 -0.0280685  -0.0563698  469  LYS B CE  
8791  N  NZ  . LYS B 469 ? 0.2959    0.323772 0.297659 -0.0100635  -0.0252532  -0.0605343  469  LYS B NZ  
8792  N  N   . TYR B 470 ? 0.168972  0.207999 0.157649 0.0147268   -0.0222241  -0.0286363  470  TYR B N   
8793  C  CA  . TYR B 470 ? 0.182491  0.227202 0.178447 0.0138424   -0.0236829  -0.0280938  470  TYR B CA  
8794  C  C   . TYR B 470 ? 0.181091  0.224636 0.172609 0.0185516   -0.0232343  -0.0230323  470  TYR B C   
8795  O  O   . TYR B 470 ? 0.196481  0.246186 0.188396 0.0221851   -0.0266476  -0.0237639  470  TYR B O   
8796  C  CB  . TYR B 470 ? 0.167732  0.209214 0.171186 0.00883941  -0.02057    -0.0271903  470  TYR B CB  
8797  C  CG  . TYR B 470 ? 0.178482  0.220284 0.186304 0.00368224  -0.0210144  -0.0325133  470  TYR B CG  
8798  C  CD1 . TYR B 470 ? 0.174897  0.226523 0.189716 0.00079758  -0.0234296  -0.0374554  470  TYR B CD1 
8799  C  CD2 . TYR B 470 ? 0.184314  0.21647  0.189576 0.00159653  -0.0187816  -0.033324   470  TYR B CD2 
8800  C  CE1 . TYR B 470 ? 0.190959  0.241987 0.210063 -0.00570171 -0.022953   -0.0432407  470  TYR B CE1 
8801  C  CE2 . TYR B 470 ? 0.209272  0.237887 0.216681 -0.00365708 -0.018427   -0.0383084  470  TYR B CE2 
8802  C  CZ  . TYR B 470 ? 0.209625  0.247341 0.224159 -0.00827328 -0.0201093  -0.0433166  470  TYR B CZ  
8803  O  OH  . TYR B 470 ? 0.221875  0.255718 0.239192 -0.0151746  -0.0189054  -0.0489837  470  TYR B OH  
8804  N  N   . GLN B 471 ? 0.173523  0.209263 0.16078  0.0187413   -0.0190656  -0.0185843  471  GLN B N   
8805  C  CA  . GLN B 471 ? 0.169612  0.201084 0.15261  0.0216653   -0.0175471  -0.0140646  471  GLN B CA  
8806  C  C   . GLN B 471 ? 0.182735  0.208597 0.152324 0.0263821   -0.0170876  -0.011656   471  GLN B C   
8807  O  O   . GLN B 471 ? 0.215998  0.236419 0.179068 0.0302381   -0.0167002  -0.00814223 471  GLN B O   
8808  C  CB  . GLN B 471 ? 0.163913  0.189806 0.149366 0.0184801   -0.0129118  -0.0111886  471  GLN B CB  
8809  C  CG  . GLN B 471 ? 0.154838  0.183701 0.149611 0.0154087   -0.0131654  -0.0121855  471  GLN B CG  
8810  C  CD  . GLN B 471 ? 0.158708  0.18363  0.155201 0.0131182   -0.00992483 -0.0104493  471  GLN B CD  
8811  O  OE1 . GLN B 471 ? 0.156456  0.181849 0.155373 0.0112484   -0.00874309 -0.0115742  471  GLN B OE1 
8812  N  NE2 . GLN B 471 ? 0.135733  0.156999 0.130797 0.013779    -0.00873421 -0.00847214 471  GLN B NE2 
8813  N  N   . GLY B 472 ? 0.186692  0.212044 0.150281 0.0266243   -0.0166934  -0.0133127  472  GLY B N   
8814  C  CA  . GLY B 472 ? 0.2025    0.22097  0.150212 0.0314642   -0.0154775  -0.0104468  472  GLY B CA  
8815  C  C   . GLY B 472 ? 0.219819  0.22737  0.161808 0.0294512   -0.0079613  -0.00507467 472  GLY B C   
8816  O  O   . GLY B 472 ? 0.220773  0.218224 0.149772 0.0332757   -0.00603507 -0.0004925  472  GLY B O   
8817  N  N   . ILE B 473 ? 0.216469  0.225763 0.167983 0.0233553   -0.00352047 -0.00611442 473  ILE B N   
8818  C  CA  . ILE B 473 ? 0.221293  0.22421  0.171886 0.0193118   0.00383117  -0.0032684  473  ILE B CA  
8819  C  C   . ILE B 473 ? 0.233396  0.240227 0.185779 0.0164214   0.00841883  -0.00580983 473  ILE B C   
8820  O  O   . ILE B 473 ? 0.237088  0.250884 0.194245 0.0173032   0.00525801  -0.00989971 473  ILE B O   
8821  C  CB  . ILE B 473 ? 0.218166  0.222577 0.18057  0.015348    0.00422563  -0.00340587 473  ILE B CB  
8822  C  CG1 . ILE B 473 ? 0.215537  0.229841 0.191333 0.0133464   0.00102254  -0.0074557  473  ILE B CG1 
8823  C  CG2 . ILE B 473 ? 0.243372  0.242676 0.202788 0.0186745   0.00120558  -0.0009408  473  ILE B CG2 
8824  C  CD1 . ILE B 473 ? 0.196715  0.211794 0.181161 0.0102859   0.00130523  -0.00749629 473  ILE B CD1 
8825  N  N   . CYS B 474 ? 0.246402  0.249111 0.196469 0.0124985   0.0162887   -0.00410767 474  CYS B N   
8826  C  CA  . CYS B 474 ? 0.238546  0.247686 0.192246 0.0100537   0.0213874   -0.00736878 474  CYS B CA  
8827  C  C   . CYS B 474 ? 0.233689  0.246093 0.197821 0.00344307  0.0276479   -0.00827352 474  CYS B C   
8828  O  O   . CYS B 474 ? 0.243868  0.248582 0.206102 0.00023759  0.0302259   -0.00529823 474  CYS B O   
8829  C  CB  . CYS B 474 ? 0.267561  0.270326 0.204546 0.0122013   0.026355    -0.00558723 474  CYS B CB  
8830  S  SG  . CYS B 474 ? 0.291463  0.276359 0.21075  0.0108202   0.0337234   0.00185205  474  CYS B SG  
8831  N  N   . PRO B 475 ? 0.2389    0.263119 0.214557 0.00139771  0.0302706   -0.0131572  475  PRO B N   
8832  C  CA  . PRO B 475 ? 0.230955  0.262264 0.219339 -0.00492013 0.0350901   -0.0157255  475  PRO B CA  
8833  C  C   . PRO B 475 ? 0.262213  0.285648 0.24118  -0.0104129  0.0459394   -0.0131139  475  PRO B C   
8834  O  O   . PRO B 475 ? 0.268627  0.287966 0.235628 -0.00854131 0.0503757   -0.0116413  475  PRO B O   
8835  C  CB  . PRO B 475 ? 0.224889  0.272126 0.226878 -0.00308067 0.0339465   -0.0220863  475  PRO B CB  
8836  C  CG  . PRO B 475 ? 0.235951  0.280875 0.228174 0.00254868  0.0329048   -0.0222806  475  PRO B CG  
8837  C  CD  . PRO B 475 ? 0.225958  0.257978 0.20416  0.00561301  0.027866    -0.0173867  475  PRO B CD  
8838  N  N   . PRO B 476 ? 0.259374  0.278674 0.241892 -0.0177092  0.0510182   -0.0125042  476  PRO B N   
8839  C  CA  . PRO B 476 ? 0.284523  0.292338 0.256289 -0.0242776  0.0627854   -0.00943604 476  PRO B CA  
8840  C  C   . PRO B 476 ? 0.299585  0.322127 0.283137 -0.0308538  0.0720377   -0.0151591  476  PRO B C   
8841  O  O   . PRO B 476 ? 0.3401    0.354676 0.315758 -0.0376955  0.0837897   -0.0133174  476  PRO B O   
8842  C  CB  . PRO B 476 ? 0.276551  0.274312 0.249753 -0.0299492  0.0637709   -0.00801236 476  PRO B CB  
8843  C  CG  . PRO B 476 ? 0.261473  0.276449 0.255467 -0.0295865  0.0550726   -0.0142686  476  PRO B CG  
8844  C  CD  . PRO B 476 ? 0.246042  0.269167 0.240801 -0.0200194  0.0459091   -0.0147081  476  PRO B CD  
8845  N  N   . VAL B 477 ? 0.289187  0.332785 0.2914   -0.0287402  0.0672892   -0.0222047  477  VAL B N   
8846  C  CA  . VAL B 477 ? 0.286603  0.347145 0.300262 -0.0324294  0.0754275   -0.0284478  477  VAL B CA  
8847  C  C   . VAL B 477 ? 0.281768  0.353871 0.299291 -0.0224755  0.0684489   -0.0318849  477  VAL B C   
8848  O  O   . VAL B 477 ? 0.24815   0.318148 0.265188 -0.0151905  0.0572559   -0.030913   477  VAL B O   
8849  C  CB  . VAL B 477 ? 0.309816  0.388048 0.346193 -0.0408419  0.0784981   -0.0361092  477  VAL B CB  
8850  C  CG1 . VAL B 477 ? 0.321578  0.388548 0.354875 -0.0534852  0.0892267   -0.0344902  477  VAL B CG1 
8851  C  CG2 . VAL B 477 ? 0.287468  0.375894 0.337456 -0.0358853  0.0656029   -0.0397407  477  VAL B CG2 
8852  N  N   . THR B 478 ? 0.259138  0.342309 0.279823 -0.0223902  0.0758275   -0.0361091  478  THR B N   
8853  C  CA  . THR B 478 ? 0.264975  0.358004 0.289105 -0.0127878  0.0702743   -0.0403249  478  THR B CA  
8854  C  C   . THR B 478 ? 0.234048  0.340702 0.27628  -0.00809533 0.0599721   -0.0454177  478  THR B C   
8855  O  O   . THR B 478 ? 0.217334  0.336771 0.275716 -0.0130212  0.0606757   -0.0496273  478  THR B O   
8856  C  CB  . THR B 478 ? 0.307922  0.413824 0.336038 -0.0143905  0.0814744   -0.0455352  478  THR B CB  
8857  O  OG1 . THR B 478 ? 0.324997  0.41255  0.330214 -0.0170274  0.0891132   -0.0388355  478  THR B OG1 
8858  C  CG2 . THR B 478 ? 0.330966  0.444928 0.360836 -0.00360229 0.0764329   -0.0503537  478  THR B CG2 
8859  N  N   . ARG B 479 ? 0.224543  0.32689  0.262604 0.00123889  0.0502595   -0.0449836  479  ARG B N   
8860  C  CA  . ARG B 479 ? 0.203875  0.315938 0.254807 0.00752099  0.0410646   -0.049109   479  ARG B CA  
8861  C  C   . ARG B 479 ? 0.201466  0.319255 0.253261 0.0168825   0.0395581   -0.0538502  479  ARG B C   
8862  O  O   . ARG B 479 ? 0.209261  0.31829  0.248191 0.0188266   0.0425186   -0.0525034  479  ARG B O   
8863  C  CB  . ARG B 479 ? 0.189771  0.287212 0.232719 0.0101791   0.0313962   -0.0438106  479  ARG B CB  
8864  C  CG  . ARG B 479 ? 0.194388  0.280767 0.230577 0.00271128  0.0331098   -0.0380522  479  ARG B CG  
8865  C  CD  . ARG B 479 ? 0.188134  0.284653 0.237327 -0.00484737 0.0368637   -0.0409164  479  ARG B CD  
8866  N  NE  . ARG B 479 ? 0.176142  0.282605 0.237675 -0.00166521 0.0288433   -0.0446729  479  ARG B NE  
8867  C  CZ  . ARG B 479 ? 0.190014  0.312727 0.267569 -0.00600566 0.0300526   -0.0507975  479  ARG B CZ  
8868  N  NH1 . ARG B 479 ? 0.169117  0.297312 0.253711 -0.00333642 0.021895    -0.0530994  479  ARG B NH1 
8869  N  NH2 . ARG B 479 ? 0.187276  0.320233 0.273016 -0.0139019  0.0398566   -0.0547899  479  ARG B NH2 
8870  N  N   . ASN B 480 ? 0.184595  0.316103 0.250045 0.0235307   0.0346729   -0.0596585  480  ASN B N   
8871  C  CA  . ASN B 480 ? 0.187636  0.319614 0.251325 0.0342422   0.0317253   -0.0634957  480  ASN B CA  
8872  C  C   . ASN B 480 ? 0.18702   0.31799  0.254897 0.042452    0.0211504   -0.0642114  480  ASN B C   
8873  O  O   . ASN B 480 ? 0.175155  0.302725 0.244121 0.0393202   0.0163069   -0.0608335  480  ASN B O   
8874  C  CB  . ASN B 480 ? 0.218794  0.370115 0.293163 0.0359944   0.0399127   -0.0711106  480  ASN B CB  
8875  C  CG  . ASN B 480 ? 0.230145  0.405657 0.326266 0.0338036   0.0407576   -0.077266   480  ASN B CG  
8876  O  OD1 . ASN B 480 ? 0.201718  0.381945 0.305613 0.0383292   0.0318082   -0.0785184  480  ASN B OD1 
8877  N  ND2 . ASN B 480 ? 0.281193  0.472448 0.386705 0.0267382   0.0518128   -0.081631   480  ASN B ND2 
8878  N  N   . GLU B 481 ? 0.205681  0.337517 0.273821 0.0536319   0.0177113   -0.0683657  481  GLU B N   
8879  C  CA  . GLU B 481 ? 0.231932  0.357014 0.298795 0.0622473   0.00792152  -0.0674995  481  GLU B CA  
8880  C  C   . GLU B 481 ? 0.249378  0.394491 0.332303 0.0659023   0.00362146  -0.0720248  481  GLU B C   
8881  O  O   . GLU B 481 ? 0.264707  0.403246 0.344185 0.0736696   -0.00480646 -0.0706266  481  GLU B O   
8882  C  CB  . GLU B 481 ? 0.260595  0.374088 0.318641 0.0737197   0.00534737  -0.0696548  481  GLU B CB  
8883  C  CG  . GLU B 481 ? 0.268752  0.358153 0.30914  0.0705745   0.00574989  -0.0650549  481  GLU B CG  
8884  C  CD  . GLU B 481 ? 0.252129  0.324899 0.283917 0.065031    0.00084721  -0.0577467  481  GLU B CD  
8885  O  OE1 . GLU B 481 ? 0.248024  0.321892 0.28325  0.0649765   -0.00392414 -0.0549667  481  GLU B OE1 
8886  O  OE2 . GLU B 481 ? 0.2344    0.293825 0.255596 0.0602649   0.00221198  -0.0552802  481  GLU B OE2 
8887  N  N   . THR B 482 ? 0.235993  0.405152 0.335716 0.0605521   0.00918372  -0.0778151  482  THR B N   
8888  C  CA  . THR B 482 ? 0.240681  0.429124 0.355896 0.0616507   0.00398746  -0.0824606  482  THR B CA  
8889  C  C   . THR B 482 ? 0.246259  0.423561 0.355833 0.0531651   0.00066915  -0.0762751  482  THR B C   
8890  O  O   . THR B 482 ? 0.24592   0.428512 0.359606 0.0565993   -0.00700472 -0.0775279  482  THR B O   
8891  C  CB  . THR B 482 ? 0.25121   0.469169 0.387673 0.0558542   0.0113063   -0.0913045  482  THR B CB  
8892  O  OG1 . THR B 482 ? 0.225016  0.451671 0.364889 0.0660527   0.0136286   -0.0968627  482  THR B OG1 
8893  C  CG2 . THR B 482 ? 0.251449  0.491842 0.405473 0.0565528   0.00507948  -0.0979044  482  THR B CG2 
8894  N  N   . HIS B 483 ? 0.212218  0.373968 0.31131  0.0429171   0.00631924  -0.0698377  483  HIS B N   
8895  C  CA  . HIS B 483 ? 0.215576  0.365376 0.30826  0.0356415   0.00381609  -0.0639626  483  HIS B CA  
8896  C  C   . HIS B 483 ? 0.212761  0.342088 0.290506 0.0423599   -0.00381808 -0.0579016  483  HIS B C   
8897  O  O   . HIS B 483 ? 0.223092  0.341165 0.291661 0.0487083   -0.00452246 -0.05643    483  HIS B O   
8898  C  CB  . HIS B 483 ? 0.197701  0.337859 0.283626 0.0240399   0.0123353   -0.0593461  483  HIS B CB  
8899  C  CG  . HIS B 483 ? 0.200107  0.356823 0.29801  0.01661     0.0218608   -0.0646108  483  HIS B CG  
8900  N  ND1 . HIS B 483 ? 0.201774  0.357465 0.295225 0.0147851   0.0306373   -0.0646203  483  HIS B ND1 
8901  C  CD2 . HIS B 483 ? 0.195598  0.36999  0.309375 0.0097095   0.0246549   -0.0704268  483  HIS B CD2 
8902  C  CE1 . HIS B 483 ? 0.204654  0.375885 0.310247 0.00653795  0.0395764   -0.0694931  483  HIS B CE1 
8903  N  NE2 . HIS B 483 ? 0.194564  0.377835 0.313772 0.00272976  0.0360991   -0.0734842  483  HIS B NE2 
8904  N  N   . PHE B 484 ? 0.188351  0.313217 0.263938 0.0406131   -0.00898928 -0.0551781  484  PHE B N   
8905  C  CA  . PHE B 484 ? 0.181022  0.286793 0.242597 0.0448738   -0.0145684  -0.0492446  484  PHE B CA  
8906  C  C   . PHE B 484 ? 0.170045  0.267942 0.22738  0.0358606   -0.0137869  -0.0445959  484  PHE B C   
8907  O  O   . PHE B 484 ? 0.178028  0.278908 0.236987 0.0359193   -0.0181707  -0.0450611  484  PHE B O   
8908  C  CB  . PHE B 484 ? 0.199462  0.311507 0.263193 0.0555308   -0.022521   -0.0522951  484  PHE B CB  
8909  C  CG  . PHE B 484 ? 0.209925  0.301171 0.257574 0.0603098   -0.0275999  -0.046012   484  PHE B CG  
8910  C  CD1 . PHE B 484 ? 0.210565  0.281255 0.245401 0.0589414   -0.0251493  -0.0405811  484  PHE B CD1 
8911  C  CD2 . PHE B 484 ? 0.211418  0.304007 0.256439 0.0656378   -0.0343582  -0.0460556  484  PHE B CD2 
8912  C  CE1 . PHE B 484 ? 0.230042  0.281751 0.250888 0.0614668   -0.027978   -0.0351945  484  PHE B CE1 
8913  C  CE2 . PHE B 484 ? 0.2192    0.291131 0.247577 0.0692469   -0.0373176  -0.0397436  484  PHE B CE2 
8914  C  CZ  . PHE B 484 ? 0.235759  0.287101 0.252497 0.0667012   -0.033565   -0.0342508  484  PHE B CZ  
8915  N  N   . ASP B 485 ? 0.170286  0.258617 0.221611 0.0292243   -0.00854554 -0.0407009  485  ASP B N   
8916  C  CA  . ASP B 485 ? 0.173869  0.255871 0.221961 0.0211617   -0.00659693 -0.0369318  485  ASP B CA  
8917  C  C   . ASP B 485 ? 0.195623  0.265481 0.235013 0.0228507   -0.0114543  -0.0325629  485  ASP B C   
8918  O  O   . ASP B 485 ? 0.193109  0.261536 0.232226 0.0187727   -0.0119535  -0.0312761  485  ASP B O   
8919  C  CB  . ASP B 485 ? 0.173393  0.250052 0.216985 0.0153987   -3.772e-05  -0.0344821  485  ASP B CB  
8920  C  CG  . ASP B 485 ? 0.171448  0.260934 0.223966 0.0118197   0.00643268  -0.038924   485  ASP B CG  
8921  O  OD1 . ASP B 485 ? 0.164833  0.267596 0.229004 0.00975839  0.00643503  -0.0436621  485  ASP B OD1 
8922  O  OD2 . ASP B 485 ? 0.181633  0.268212 0.229282 0.0106659   0.0116487   -0.0380412  485  ASP B OD2 
8923  N  N   . ALA B 486 ? 0.209891  0.269986 0.241598 0.0283546   -0.0141502  -0.03052    486  ALA B N   
8924  C  CA  . ALA B 486 ? 0.204356  0.253068 0.22763  0.029552    -0.0174462  -0.0266313  486  ALA B CA  
8925  C  C   . ALA B 486 ? 0.206999  0.26197  0.232502 0.033001    -0.021992   -0.028404   486  ALA B C   
8926  O  O   . ALA B 486 ? 0.182097  0.231199 0.202207 0.0315479   -0.0234073  -0.0257784  486  ALA B O   
8927  C  CB  . ALA B 486 ? 0.208138  0.244548 0.222853 0.0347434   -0.0187156  -0.0250492  486  ALA B CB  
8928  N  N   . GLY B 487 ? 0.183846  0.251814 0.21713  0.0383398   -0.0246377  -0.0335244  487  GLY B N   
8929  C  CA  . GLY B 487 ? 0.177825  0.253677 0.212964 0.0428708   -0.0304543  -0.0363588  487  GLY B CA  
8930  C  C   . GLY B 487 ? 0.18314   0.268187 0.225679 0.035088    -0.0296414  -0.0390406  487  GLY B C   
8931  O  O   . GLY B 487 ? 0.207779  0.296254 0.248958 0.0373587   -0.0345424  -0.0408888  487  GLY B O   
8932  N  N   . ALA B 488 ? 0.16486   0.249706 0.21162  0.0260346   -0.0233767  -0.0383982  488  ALA B N   
8933  C  CA  . ALA B 488 ? 0.171235  0.260055 0.222823 0.0182109   -0.0215832  -0.0405148  488  ALA B CA  
8934  C  C   . ALA B 488 ? 0.166252  0.2404   0.207228 0.0155034   -0.0211786  -0.0352222  488  ALA B C   
8935  O  O   . ALA B 488 ? 0.170558  0.244068 0.213246 0.00940865  -0.0191154  -0.0363553  488  ALA B O   
8936  C  CB  . ALA B 488 ? 0.180713  0.275651 0.240989 0.010429    -0.0144819  -0.0428136  488  ALA B CB  
8937  N  N   . LYS B 489 ? 0.176699  0.239258 0.207058 0.0199922   -0.0228094  -0.0301527  489  LYS B N   
8938  C  CA  . LYS B 489 ? 0.190565  0.242386 0.212304 0.018203    -0.0224003  -0.0262104  489  LYS B CA  
8939  C  C   . LYS B 489 ? 0.198636  0.248022 0.212691 0.0242208   -0.0274339  -0.02599    489  LYS B C   
8940  O  O   . LYS B 489 ? 0.209852  0.255377 0.218554 0.0304856   -0.0297109  -0.0244349  489  LYS B O   
8941  C  CB  . LYS B 489 ? 0.180506  0.222033 0.196641 0.0173893   -0.0191986  -0.0212284  489  LYS B CB  
8942  C  CG  . LYS B 489 ? 0.19991   0.231744 0.207816 0.0167468   -0.0184845  -0.0173555  489  LYS B CG  
8943  C  CD  . LYS B 489 ? 0.210805  0.24303  0.220271 0.0124682   -0.0165283  -0.0177325  489  LYS B CD  
8944  C  CE  . LYS B 489 ? 0.24983   0.275584 0.252967 0.0122664   -0.015374   -0.0150604  489  LYS B CE  
8945  N  NZ  . LYS B 489 ? 0.256408  0.282511 0.260517 0.0100215   -0.0143729  -0.0166141  489  LYS B NZ  
8946  N  N   . PHE B 490 ? 0.19759   0.246825 0.208767 0.0228334   -0.0288213  -0.0272183  490  PHE B N   
8947  C  CA  . PHE B 490 ? 0.212438  0.259541 0.214037 0.028928    -0.033756   -0.027415   490  PHE B CA  
8948  C  C   . PHE B 490 ? 0.221035  0.256073 0.209878 0.0353355   -0.0343569  -0.0220045  490  PHE B C   
8949  O  O   . PHE B 490 ? 0.220625  0.255778 0.203437 0.0434842   -0.0393785  -0.0226309  490  PHE B O   
8950  C  CB  . PHE B 490 ? 0.225861  0.268985 0.22258  0.0254438   -0.0325764  -0.0275703  490  PHE B CB  
8951  C  CG  . PHE B 490 ? 0.252725  0.291494 0.236121 0.0316229   -0.0366565  -0.0270639  490  PHE B CG  
8952  C  CD1 . PHE B 490 ? 0.261121  0.286243 0.230812 0.0338197   -0.033803   -0.0207728  490  PHE B CD1 
8953  C  CD2 . PHE B 490 ? 0.254762  0.303364 0.238911 0.035063    -0.0430864  -0.03326    490  PHE B CD2 
8954  C  CE1 . PHE B 490 ? 0.293483  0.312532 0.24795  0.0396943   -0.0365676  -0.0196064  490  PHE B CE1 
8955  C  CE2 . PHE B 490 ? 0.292436  0.336443 0.261514 0.0420573   -0.047472   -0.0327391  490  PHE B CE2 
8956  C  CZ  . PHE B 490 ? 0.289536  0.31751  0.242507 0.0445088   -0.0437803  -0.0253215  490  PHE B CZ  
8957  N  N   . HIS B 491 ? 0.200817  0.224554 0.184734 0.0319182   -0.0291614  -0.0168677  491  HIS B N   
8958  C  CA  . HIS B 491 ? 0.214027  0.223327 0.184291 0.0352969   -0.0278112  -0.0117524  491  HIS B CA  
8959  C  C   . HIS B 491 ? 0.223133  0.227501 0.190667 0.0412381   -0.0295947  -0.0108524  491  HIS B C   
8960  O  O   . HIS B 491 ? 0.240985  0.231132 0.194611 0.0458739   -0.0293731  -0.00691111 491  HIS B O   
8961  C  CB  . HIS B 491 ? 0.212506  0.214914 0.183109 0.0283892   -0.0213508  -0.00844091 491  HIS B CB  
8962  C  CG  . HIS B 491 ? 0.196408  0.201293 0.167485 0.0243162   -0.0191024  -0.0088161  491  HIS B CG  
8963  N  ND1 . HIS B 491 ? 0.190916  0.205448 0.171939 0.0213365   -0.0197537  -0.0123399  491  HIS B ND1 
8964  C  CD2 . HIS B 491 ? 0.202972  0.201751 0.165838 0.0230028   -0.0157994  -0.00657329 491  HIS B CD2 
8965  C  CE1 . HIS B 491 ? 0.196061  0.209727 0.174924 0.0190742   -0.017517   -0.0123907  491  HIS B CE1 
8966  N  NE2 . HIS B 491 ? 0.201383  0.206972 0.170078 0.0200549   -0.0150292  -0.00914639 491  HIS B NE2 
8967  N  N   . VAL B 492 ? 0.212969  0.227515 0.192447 0.0412819   -0.0306436  -0.0144477  492  VAL B N   
8968  C  CA  . VAL B 492 ? 0.226239  0.237338 0.204089 0.0478545   -0.032332   -0.0147022  492  VAL B CA  
8969  C  C   . VAL B 492 ? 0.245867  0.260933 0.218932 0.0586539   -0.0393285  -0.0168894  492  VAL B C   
8970  O  O   . VAL B 492 ? 0.272181  0.272299 0.230119 0.0662685   -0.0408946  -0.0131627  492  VAL B O   
8971  C  CB  . VAL B 492 ? 0.215743  0.236491 0.20687  0.0443822   -0.0301264  -0.0179881  492  VAL B CB  
8972  C  CG1 . VAL B 492 ? 0.215054  0.234349 0.205664 0.0522204   -0.0319467  -0.0196508  492  VAL B CG1 
8973  C  CG2 . VAL B 492 ? 0.196049  0.209999 0.187425 0.0360205   -0.024503   -0.0152574  492  VAL B CG2 
8974  N  N   . PRO B 493 ? 0.245801  0.28034  0.230513 0.0603062   -0.0439371  -0.0232476  493  PRO B N   
8975  C  CA  . PRO B 493 ? 0.270409  0.31145  0.250988 0.0715743   -0.0520031  -0.026436   493  PRO B CA  
8976  C  C   . PRO B 493 ? 0.302623  0.330128 0.263945 0.075985    -0.0544499  -0.0220802  493  PRO B C   
8977  O  O   . PRO B 493 ? 0.332402  0.355797 0.281906 0.0879199   -0.0605891  -0.0216583  493  PRO B O   
8978  C  CB  . PRO B 493 ? 0.235724  0.302647 0.23563  0.068305    -0.0550631  -0.035417   493  PRO B CB  
8979  C  CG  . PRO B 493 ? 0.211988  0.278256 0.218946 0.0545785   -0.0478829  -0.0343779  493  PRO B CG  
8980  C  CD  . PRO B 493 ? 0.211503  0.262713 0.213461 0.0519782   -0.0417789  -0.0282708  493  PRO B CD  
8981  N  N   . ASN B 494 ? 0.304697  0.324802 0.261673 0.0672413   -0.0494258  -0.0187867  494  ASN B N   
8982  C  CA  . ASN B 494 ? 0.317049  0.326409 0.256599 0.0698386   -0.0503261  -0.0154126  494  ASN B CA  
8983  C  C   . ASN B 494 ? 0.346617  0.3314   0.268562 0.0700039   -0.044277   -0.00690686 494  ASN B C   
8984  O  O   . ASN B 494 ? 0.359078  0.331335 0.265065 0.07005     -0.041812   -0.00263137 494  ASN B O   
8985  C  CB  . ASN B 494 ? 0.344001  0.362437 0.289972 0.0615994   -0.0489805  -0.0186988  494  ASN B CB  
8986  C  CG  . ASN B 494 ? 0.37431   0.414049 0.332912 0.0631721   -0.0561314  -0.0277917  494  ASN B CG  
8987  O  OD1 . ASN B 494 ? 0.431196  0.474583 0.3811   0.0712888   -0.0633425  -0.0306118  494  ASN B OD1 
8988  N  ND2 . ASN B 494 ? 0.316382  0.370588 0.294748 0.0558321   -0.0544629  -0.0329891  494  ASN B ND2 
8989  N  N   . VAL B 495 ? 0.331427  0.308901 0.256433 0.0689152   -0.0408487  -0.00489269 495  VAL B N   
8990  C  CA  . VAL B 495 ? 0.349303  0.303114 0.259397 0.0681311   -0.0348493  0.00184472  495  VAL B CA  
8991  C  C   . VAL B 495 ? 0.400416  0.345197 0.303137 0.0594132   -0.0276737  0.00588481  495  VAL B C   
8992  O  O   . VAL B 495 ? 0.409497  0.334909 0.292367 0.0616936   -0.0243102  0.0115204   495  VAL B O   
8993  C  CB  . VAL B 495 ? 0.411763  0.349187 0.301742 0.0815533   -0.0390094  0.00529367  495  VAL B CB  
8994  C  CG1 . VAL B 495 ? 0.446413  0.357596 0.32316  0.0794847   -0.0318046  0.0113548   495  VAL B CG1 
8995  C  CG2 . VAL B 495 ? 0.396222  0.34876  0.295776 0.0922051   -0.0476408  -0.0004965  495  VAL B CG2 
8996  N  N   . THR B 496 ? 0.331731  0.28956  0.249418 0.0497779   -0.0246575  0.00313418  496  THR B N   
8997  C  CA  . THR B 496 ? 0.342169  0.293548 0.255159 0.0419732   -0.0173869  0.00611625  496  THR B CA  
8998  C  C   . THR B 496 ? 0.303414  0.254187 0.227127 0.0331483   -0.0115982  0.00613017  496  THR B C   
8999  O  O   . THR B 496 ? 0.311834  0.276196 0.251422 0.0303678   -0.0134152  0.00225584  496  THR B O   
9000  C  CB  . THR B 496 ? 0.346998  0.31308  0.267705 0.0390726   -0.0186795  0.00243422  496  THR B CB  
9001  O  OG1 . THR B 496 ? 0.402693  0.372367 0.315794 0.0475066   -0.0258102  0.00040946  496  THR B OG1 
9002  C  CG2 . THR B 496 ? 0.330021  0.292298 0.24724  0.0322657   -0.0112426  0.00448285  496  THR B CG2 
9003  N  N   . PRO B 497 ? 0.31132   0.247006 0.226691 0.028147    -0.0044059  0.00989772  497  PRO B N   
9004  C  CA  . PRO B 497 ? 0.309681  0.246939 0.23626  0.0193411   0.000364    0.00838184  497  PRO B CA  
9005  C  C   . PRO B 497 ? 0.273599  0.229293 0.21609  0.0135059   0.00097065  0.00478694  497  PRO B C   
9006  O  O   . PRO B 497 ? 0.264704  0.226697 0.206386 0.0141924   0.00078642  0.00454694  497  PRO B O   
9007  C  CB  . PRO B 497 ? 0.322484  0.241497 0.236869 0.0137173   0.00888712  0.0123032   497  PRO B CB  
9008  C  CG  . PRO B 497 ? 0.347974  0.249534 0.240183 0.0225924   0.00765993  0.0173881   497  PRO B CG  
9009  C  CD  . PRO B 497 ? 0.349128  0.265208 0.243142 0.0300814   5.235e-05   0.0154284   497  PRO B CD  
9010  N  N   . TYR B 498 ? 0.243477  0.206121 0.198437 0.0087206   0.00150732  0.0019042   498  TYR B N   
9011  C  CA  . TYR B 498 ? 0.222004  0.200995 0.190804 0.00557297  0.00070902  -0.00137614 498  TYR B CA  
9012  C  C   . TYR B 498 ? 0.220866  0.203919 0.196687 -0.00206742 0.00585744  -0.00298698 498  TYR B C   
9013  O  O   . TYR B 498 ? 0.225237  0.22071  0.209967 -0.00339621 0.00576369  -0.00518368 498  TYR B O   
9014  C  CB  . TYR B 498 ? 0.193243  0.180212 0.170606 0.00806799  -0.00416766 -0.00402872 498  TYR B CB  
9015  C  CG  . TYR B 498 ? 0.180432  0.179966 0.165789 0.00840982  -0.00621005 -0.00592197 498  TYR B CG  
9016  C  CD1 . TYR B 498 ? 0.178861  0.180352 0.161221 0.0119905   -0.00864495 -0.0059509  498  TYR B CD1 
9017  C  CD2 . TYR B 498 ? 0.168579  0.176406 0.162642 0.00537215  -0.00554681 -0.0078237  498  TYR B CD2 
9018  C  CE1 . TYR B 498 ? 0.177676  0.187419 0.166046 0.0115952   -0.00976306 -0.00796825 498  TYR B CE1 
9019  C  CE2 . TYR B 498 ? 0.164318  0.179357 0.162705 0.00652711  -0.00693602 -0.00885943 498  TYR B CE2 
9020  C  CZ  . TYR B 498 ? 0.175183  0.190127 0.170731 0.00894969  -0.00843558 -0.008899   498  TYR B CZ  
9021  O  OH  . TYR B 498 ? 0.172298  0.191395 0.17113  0.00924013  -0.0090856  -0.0102994  498  TYR B OH  
9022  N  N   . ILE B 499 ? 0.230156  0.203692 0.203232 -0.00697221 0.00997595  -0.00282951 499  ILE B N   
9023  C  CA  . ILE B 499 ? 0.218889  0.200004 0.202092 -0.0149973  0.0140029   -0.00640904 499  ILE B CA  
9024  C  C   . ILE B 499 ? 0.239997  0.228626 0.225723 -0.0182129  0.0190499   -0.00652956 499  ILE B C   
9025  O  O   . ILE B 499 ? 0.212459  0.215833 0.210824 -0.0220249  0.020188    -0.0107129  499  ILE B O   
9026  C  CB  . ILE B 499 ? 0.23339   0.201717 0.213266 -0.0212081  0.0181793   -0.00727191 499  ILE B CB  
9027  C  CG1 . ILE B 499 ? 0.225751  0.207042 0.220138 -0.0295243  0.0200951   -0.0135211  499  ILE B CG1 
9028  C  CG2 . ILE B 499 ? 0.246166  0.196437 0.211529 -0.0239129  0.0255129   -0.00271098 499  ILE B CG2 
9029  C  CD1 . ILE B 499 ? 0.214633  0.210361 0.219408 -0.0261338  0.0128439   -0.0176532  499  ILE B CD1 
9030  N  N   . ARG B 500 ? 0.236599  0.216572 0.210088 -0.0151578  0.0212313   -0.00244538 500  ARG B N   
9031  C  CA  . ARG B 500 ? 0.23795   0.224019 0.21136  -0.0166638  0.0260859   -0.00248944 500  ARG B CA  
9032  C  C   . ARG B 500 ? 0.219613  0.224238 0.206135 -0.0138158  0.0221227   -0.00629574 500  ARG B C   
9033  O  O   . ARG B 500 ? 0.213476  0.228177 0.206421 -0.0164404  0.0265401   -0.00870414 500  ARG B O   
9034  C  CB  . ARG B 500 ? 0.24989   0.223391 0.205696 -0.0113319  0.0265518   0.00219546  500  ARG B CB  
9035  C  CG  . ARG B 500 ? 0.265805  0.240475 0.219673 -0.00278991 0.0173515   0.00246041  500  ARG B CG  
9036  C  CD  . ARG B 500 ? 0.293992  0.258107 0.230501 0.00374641  0.0156985   0.00586621  500  ARG B CD  
9037  N  NE  . ARG B 500 ? 0.3071    0.251751 0.227836 0.00352013  0.019665    0.0105448   500  ARG B NE  
9038  C  CZ  . ARG B 500 ? 0.360964  0.291848 0.26225  0.0100401   0.018657    0.0145999   500  ARG B CZ  
9039  N  NH1 . ARG B 500 ? 0.328924  0.265999 0.225832 0.0164576   0.0135128   0.0134826   500  ARG B NH1 
9040  N  NH2 . ARG B 500 ? 0.364074  0.274058 0.249714 0.0104106   0.0224501   0.0193793   500  ARG B NH2 
9041  N  N   . TYR B 501 ? 0.199048  0.207278 0.188793 -0.00840025 0.0146558   -0.00687217 501  TYR B N   
9042  C  CA  . TYR B 501 ? 0.201288  0.222446 0.199936 -0.0052436  0.0117084   -0.00960888 501  TYR B CA  
9043  C  C   . TYR B 501 ? 0.193531  0.226985 0.205183 -0.00776257 0.0111934   -0.0135072  501  TYR B C   
9044  O  O   . TYR B 501 ? 0.188899  0.233797 0.207999 -0.00620093 0.0115084   -0.0162325  501  TYR B O   
9045  C  CB  . TYR B 501 ? 0.198511  0.218407 0.195731 0.00013481  0.00536296  -0.00904201 501  TYR B CB  
9046  C  CG  . TYR B 501 ? 0.219433  0.230787 0.205393 0.00323399  0.00456498  -0.00681973 501  TYR B CG  
9047  C  CD1 . TYR B 501 ? 0.226108  0.23781  0.207222 0.00482104  0.00652469  -0.00715912 501  TYR B CD1 
9048  C  CD2 . TYR B 501 ? 0.204445  0.208487 0.184563 0.00548014  0.00130072  -0.00516732 501  TYR B CD2 
9049  C  CE1 . TYR B 501 ? 0.220595  0.225502 0.190557 0.0082377   0.00467071  -0.00602063 501  TYR B CE1 
9050  C  CE2 . TYR B 501 ? 0.21527   0.213526 0.185246 0.00950385  -0.00073096 -0.00395405 501  TYR B CE2 
9051  C  CZ  . TYR B 501 ? 0.234401  0.233319 0.199171 0.0107351   0.00058533  -0.00450619 501  TYR B CZ  
9052  O  OH  . TYR B 501 ? 0.249957  0.244369 0.204548 0.0154282   -0.00300476 -0.00420722 501  TYR B OH  
9053  N  N   . PHE B 502 ? 0.194388  0.22595  0.208454 -0.0107014  0.00979084  -0.0144128  502  PHE B N   
9054  C  CA  . PHE B 502 ? 0.195421  0.240048 0.2215   -0.0135634  0.00912848  -0.0192914  502  PHE B CA  
9055  C  C   . PHE B 502 ? 0.209199  0.262504 0.242473 -0.0196951  0.0157299   -0.0224866  502  PHE B C   
9056  O  O   . PHE B 502 ? 0.203841  0.27356  0.248382 -0.0187789  0.0150119   -0.02694    502  PHE B O   
9057  C  CB  . PHE B 502 ? 0.208985  0.248408 0.234888 -0.0166588  0.00718719  -0.0205554  502  PHE B CB  
9058  C  CG  . PHE B 502 ? 0.223438  0.277492 0.261331 -0.0193863  0.00515001  -0.026813   502  PHE B CG  
9059  C  CD1 . PHE B 502 ? 0.212007  0.276254 0.253817 -0.0130761  -0.00109242 -0.0285471  502  PHE B CD1 
9060  C  CD2 . PHE B 502 ? 0.234042  0.291949 0.278778 -0.0281289  0.00963647  -0.0313037  502  PHE B CD2 
9061  C  CE1 . PHE B 502 ? 0.231358  0.309874 0.28279  -0.0141399  -0.00430324 -0.0347946  502  PHE B CE1 
9062  C  CE2 . PHE B 502 ? 0.250568  0.324358 0.307477 -0.030692   0.00678886  -0.0385344  502  PHE B CE2 
9063  C  CZ  . PHE B 502 ? 0.245299  0.330602 0.30557  -0.0227866  -0.00082289 -0.0403582  502  PHE B CZ  
9064  N  N   . VAL B 503 ? 0.213634  0.255956 0.240051 -0.0257222  0.0226092   -0.0203783  503  VAL B N   
9065  C  CA  . VAL B 503 ? 0.230035  0.279545 0.262318 -0.032863   0.0310176   -0.023148   503  VAL B CA  
9066  C  C   . VAL B 503 ? 0.223296  0.284972 0.259394 -0.027987   0.032272    -0.0241645  503  VAL B C   
9067  O  O   . VAL B 503 ? 0.227778  0.307775 0.277814 -0.0302808  0.0348881   -0.0298197  503  VAL B O   
9068  C  CB  . VAL B 503 ? 0.240055  0.269859 0.258816 -0.0392913  0.0391132   -0.0188701  503  VAL B CB  
9069  C  CG1 . VAL B 503 ? 0.253462  0.288491 0.275603 -0.0473258  0.0500242   -0.0207991  503  VAL B CG1 
9070  C  CG2 . VAL B 503 ? 0.24702   0.265729 0.264237 -0.0446317  0.0385797   -0.0195975  503  VAL B CG2 
9071  N  N   A SER B 504 ? 0.221575  0.274063 0.246072 -0.0211504  0.0302408   -0.0197019  504  SER B N   
9072  N  N   B SER B 504 ? 0.215041  0.267579 0.239706 -0.0209304  0.0297964   -0.0197191  504  SER B N   
9073  C  CA  A SER B 504 ? 0.222413  0.282756 0.247809 -0.0158465  0.0312823   -0.0207783  504  SER B CA  
9074  C  CA  B SER B 504 ? 0.211363  0.270485 0.235797 -0.015871   0.0312411   -0.0204229  504  SER B CA  
9075  C  C   A SER B 504 ? 0.21505   0.292529 0.254045 -0.0104588  0.0260425   -0.025521   504  SER B C   
9076  C  C   B SER B 504 ? 0.209028  0.283688 0.245318 -0.00941915 0.0255785   -0.0245802  504  SER B C   
9077  O  O   A SER B 504 ? 0.20023   0.291588 0.247568 -0.00866836 0.0289632   -0.0295088  504  SER B O   
9078  O  O   B SER B 504 ? 0.207855  0.293002 0.249165 -0.00626737 0.0280931   -0.0275248  504  SER B O   
9079  C  CB  A SER B 504 ? 0.235618  0.283326 0.247197 -0.00958044 0.0280013   -0.016584   504  SER B CB  
9080  C  CB  B SER B 504 ? 0.212035  0.256333 0.220429 -0.0110391  0.0298272   -0.0156417  504  SER B CB  
9081  O  OG  A SER B 504 ? 0.276654  0.331436 0.289738 -0.00402506 0.028056    -0.0187431  504  SER B OG  
9082  O  OG  B SER B 504 ? 0.199483  0.239603 0.205789 -0.00537816 0.021546    -0.0143437  504  SER B OG  
9083  N  N   . PHE B 505 ? 0.205905  0.28159  0.245699 -0.00694776 0.0184158   -0.0249431  505  PHE B N   
9084  C  CA  . PHE B 505 ? 0.221621  0.308093 0.268578 0.00041918  0.0126901   -0.0277247  505  PHE B CA  
9085  C  C   . PHE B 505 ? 0.231367  0.338336 0.294044 -0.00152525 0.0136753   -0.0342884  505  PHE B C   
9086  O  O   . PHE B 505 ? 0.263247  0.382701 0.332694 0.00536933  0.0118487   -0.0376476  505  PHE B O   
9087  C  CB  . PHE B 505 ? 0.209751  0.288132 0.251443 0.00475453  0.0055615   -0.0251065  505  PHE B CB  
9088  C  CG  . PHE B 505 ? 0.249143  0.315203 0.280481 0.00972194  0.00384973  -0.0214047  505  PHE B CG  
9089  C  CD1 . PHE B 505 ? 0.218975  0.274453 0.2415   0.00748657  0.00667547  -0.0186642  505  PHE B CD1 
9090  C  CD2 . PHE B 505 ? 0.262883  0.327117 0.292414 0.0164402   -0.00065605 -0.0209645  505  PHE B CD2 
9091  C  CE1 . PHE B 505 ? 0.280237  0.326335 0.294948 0.010978    0.0044606   -0.0168005  505  PHE B CE1 
9092  C  CE2 . PHE B 505 ? 0.270745  0.322762 0.29151  0.0189344   -0.00149142 -0.018377   505  PHE B CE2 
9093  C  CZ  . PHE B 505 ? 0.313062  0.357397 0.327681 0.0158234   0.00078631  -0.0169422  505  PHE B CZ  
9094  N  N   . VAL B 506 ? 0.222411  0.332506 0.290692 -0.0108517  0.0170556   -0.0366184  506  VAL B N   
9095  C  CA  . VAL B 506 ? 0.246169  0.378125 0.331595 -0.0150162  0.0191988   -0.0444088  506  VAL B CA  
9096  C  C   . VAL B 506 ? 0.2544    0.3937   0.344193 -0.0190236  0.0288963   -0.04633    506  VAL B C   
9097  O  O   . VAL B 506 ? 0.275225  0.435993 0.379049 -0.0163272  0.029884    -0.0526704  506  VAL B O   
9098  C  CB  . VAL B 506 ? 0.258845  0.390472 0.348974 -0.0252566  0.0201076   -0.0473529  506  VAL B CB  
9099  C  CG1 . VAL B 506 ? 0.264888  0.421112 0.37497  -0.0320989  0.0234457   -0.0570154  506  VAL B CG1 
9100  C  CG2 . VAL B 506 ? 0.252621  0.377821 0.337796 -0.0209239  0.0110439   -0.046095   506  VAL B CG2 
9101  N  N   . LEU B 507 ? 0.259539  0.381568 0.336834 -0.0249183  0.0362534   -0.0411496  507  LEU B N   
9102  C  CA  . LEU B 507 ? 0.281564  0.408053 0.360072 -0.0299415  0.0470157   -0.0424086  507  LEU B CA  
9103  C  C   . LEU B 507 ? 0.267288  0.402698 0.346719 -0.0200942  0.0467674   -0.0436967  507  LEU B C   
9104  O  O   . LEU B 507 ? 0.273129  0.425985 0.363786 -0.021842   0.0535197   -0.0491397  507  LEU B O   
9105  C  CB  . LEU B 507 ? 0.339709  0.441143 0.399286 -0.0359102  0.0532969   -0.0351629  507  LEU B CB  
9106  C  CG  . LEU B 507 ? 0.370597  0.469302 0.42546  -0.0436696  0.0665565   -0.034611   507  LEU B CG  
9107  C  CD1 . LEU B 507 ? 0.382144  0.488471 0.448974 -0.0575678  0.0751574   -0.0395054  507  LEU B CD1 
9108  C  CD2 . LEU B 507 ? 0.4029    0.472825 0.432618 -0.0430636  0.068442    -0.0255851  507  LEU B CD2 
9109  N  N   . GLN B 508 ? 0.225859  0.350952 0.295239 -0.00998484 0.0393757   -0.0398669  508  GLN B N   
9110  C  CA  . GLN B 508 ? 0.233128  0.362265 0.300825 -0.00069717 0.0395213   -0.041157   508  GLN B CA  
9111  C  C   . GLN B 508 ? 0.232501  0.386572 0.318294 0.00537597  0.0377501   -0.0488403  508  GLN B C   
9112  O  O   . GLN B 508 ? 0.211008  0.374362 0.300031 0.0100784   0.042174    -0.0522491  508  GLN B O   
9113  C  CB  . GLN B 508 ? 0.213723  0.324621 0.266741 0.00708019  0.0325994   -0.0360751  508  GLN B CB  
9114  C  CG  . GLN B 508 ? 0.194235  0.305209 0.250176 0.0133955   0.0228733   -0.0358928  508  GLN B CG  
9115  C  CD  . GLN B 508 ? 0.221549  0.312798 0.26283  0.0174191   0.018348    -0.0308119  508  GLN B CD  
9116  O  OE1 . GLN B 508 ? 0.24059   0.328565 0.279176 0.025445    0.0146071   -0.0311688  508  GLN B OE1 
9117  N  NE2 . GLN B 508 ? 0.230103  0.307666 0.26147  0.0120111   0.0190905   -0.0264956  508  GLN B NE2 
9118  N  N   . PHE B 509 ? 0.225424  0.391253 0.322818 0.00577182  0.0312342   -0.0521832  509  PHE B N   
9119  C  CA  . PHE B 509 ? 0.229222  0.421017 0.344295 0.0126746   0.0281354   -0.0602304  509  PHE B CA  
9120  C  C   . PHE B 509 ? 0.223873  0.438909 0.356652 0.00387417  0.0372738   -0.0678321  509  PHE B C   
9121  O  O   . PHE B 509 ? 0.225854  0.462186 0.3715   0.0104152   0.0384878   -0.0745051  509  PHE B O   
9122  C  CB  . PHE B 509 ? 0.207908  0.40528  0.327652 0.0177788   0.0172094   -0.0618006  509  PHE B CB  
9123  C  CG  . PHE B 509 ? 0.213929  0.390832 0.317117 0.0282167   0.00999709  -0.0551912  509  PHE B CG  
9124  C  CD1 . PHE B 509 ? 0.219598  0.398944 0.321284 0.042042    0.00615048  -0.0563716  509  PHE B CD1 
9125  C  CD2 . PHE B 509 ? 0.187395  0.341372 0.275977 0.0239183   0.00830694  -0.0479728  509  PHE B CD2 
9126  C  CE1 . PHE B 509 ? 0.205024  0.362876 0.290559 0.0500581   0.00098846  -0.0503324  509  PHE B CE1 
9127  C  CE2 . PHE B 509 ? 0.194624  0.33131  0.26971  0.0317841   0.00311197  -0.0427869  509  PHE B CE2 
9128  C  CZ  . PHE B 509 ? 0.206168  0.3437   0.279281 0.044053    -0.00010736 -0.0437927  509  PHE B CZ  
9129  N  N   . GLN B 510 ? 0.246582  0.456096 0.379026 -0.0107027  0.0444752   -0.0667803  510  GLN B N   
9130  C  CA  . GLN B 510 ? 0.264787  0.492827 0.41237  -0.02196    0.0556263   -0.0734777  510  GLN B CA  
9131  C  C   . GLN B 510 ? 0.279957  0.506831 0.421755 -0.0204791  0.0658156   -0.0724662  510  GLN B C   
9132  O  O   . GLN B 510 ? 0.240385  0.491594 0.398613 -0.0220753  0.0729812   -0.0802944  510  GLN B O   
9133  C  CB  . GLN B 510 ? 0.263545  0.479865 0.408177 -0.0385118  0.0626576   -0.0716494  510  GLN B CB  
9134  C  CG  . GLN B 510 ? 0.278113  0.497089 0.429691 -0.0418257  0.0540458   -0.0744378  510  GLN B CG  
9135  C  CD  . GLN B 510 ? 0.291449  0.495888 0.438944 -0.0577813  0.0611532   -0.0730675  510  GLN B CD  
9136  O  OE1 . GLN B 510 ? 0.304909  0.483864 0.435739 -0.0586232  0.0578408   -0.0658493  510  GLN B OE1 
9137  N  NE2 . GLN B 510 ? 0.293419  0.514461 0.456918 -0.0706277  0.0712383   -0.0807331  510  GLN B NE2 
9138  N  N   . PHE B 511 ? 0.292432  0.491619 0.410947 -0.0185171  0.0670064   -0.0634174  511  PHE B N   
9139  C  CA  . PHE B 511 ? 0.30085   0.495085 0.409301 -0.0162224  0.0757003   -0.0619128  511  PHE B CA  
9140  C  C   . PHE B 511 ? 0.278222  0.488534 0.394812 -0.00204576 0.0717224   -0.0673183  511  PHE B C   
9141  O  O   . PHE B 511 ? 0.283433  0.508567 0.406819 -0.00126553 0.0805424   -0.072432   511  PHE B O   
9142  C  CB  . PHE B 511 ? 0.300316  0.462926 0.38241  -0.0142005  0.0735374   -0.0521492  511  PHE B CB  
9143  C  CG  . PHE B 511 ? 0.349127  0.491692 0.417011 -0.0259205  0.080245    -0.0458558  511  PHE B CG  
9144  C  CD1 . PHE B 511 ? 0.365808  0.515435 0.443704 -0.0389784  0.0882515   -0.0485121  511  PHE B CD1 
9145  C  CD2 . PHE B 511 ? 0.371797  0.487768 0.416148 -0.0233009  0.0776384   -0.0376788  511  PHE B CD2 
9146  C  CE1 . PHE B 511 ? 0.376164  0.503263 0.438556 -0.0485881  0.094146    -0.0421632  511  PHE B CE1 
9147  C  CE2 . PHE B 511 ? 0.384629  0.480827 0.414063 -0.0316826  0.082905    -0.0316219  511  PHE B CE2 
9148  C  CZ  . PHE B 511 ? 0.392439  0.49263  0.429951 -0.0441044  0.0914684   -0.033423   511  PHE B CZ  
9149  N  N   . HIS B 512 ? 0.236753  0.442774 0.351511 0.00928816  0.0591516   -0.0661103  512  HIS B N   
9150  C  CA  . HIS B 512 ? 0.240078  0.454544 0.358162 0.0244017   0.0542314   -0.0699144  512  HIS B CA  
9151  C  C   . HIS B 512 ? 0.247357  0.496824 0.390607 0.0271358   0.0564845   -0.0805692  512  HIS B C   
9152  O  O   . HIS B 512 ? 0.232347  0.494164 0.38063  0.0349501   0.0608219   -0.0856625  512  HIS B O   
9153  C  CB  . HIS B 512 ? 0.221038  0.421693 0.331268 0.033727    0.0411864   -0.0658145  512  HIS B CB  
9154  C  CG  . HIS B 512 ? 0.224361  0.426216 0.333328 0.0498889   0.0355589   -0.0681641  512  HIS B CG  
9155  N  ND1 . HIS B 512 ? 0.235536  0.425615 0.332796 0.0564505   0.0389929   -0.0675199  512  HIS B ND1 
9156  C  CD2 . HIS B 512 ? 0.231958  0.445224 0.349262 0.0615548   0.0269533   -0.0717279  512  HIS B CD2 
9157  C  CE1 . HIS B 512 ? 0.235667  0.426668 0.333229 0.0711528   0.0327292   -0.0699702  512  HIS B CE1 
9158  N  NE2 . HIS B 512 ? 0.230307  0.43518  0.339413 0.075082    0.0252811   -0.0721595  512  HIS B NE2 
9159  N  N   . GLU B 513 ? 0.251569  0.518736 0.411576 0.0212287   0.0531501   -0.0850351  513  GLU B N   
9160  C  CA  . GLU B 513 ? 0.24968   0.554228 0.43639  0.0233314   0.0544463   -0.0967753  513  GLU B CA  
9161  C  C   . GLU B 513 ? 0.233835  0.55217  0.429473 0.0123217   0.0704655   -0.101384   513  GLU B C   
9162  O  O   . GLU B 513 ? 0.252128  0.596975 0.464072 0.0180537   0.0748315   -0.110139   513  GLU B O   
9163  C  CB  . GLU B 513 ? 0.276889  0.597219 0.478838 0.0186335   0.0467107   -0.101481   513  GLU B CB  
9164  C  CG  . GLU B 513 ? 0.320045  0.68299  0.55258  0.0188138   0.0473799   -0.11536    513  GLU B CG  
9165  C  CD  . GLU B 513 ? 0.384807  0.760596 0.62967  0.0135326   0.0385899   -0.120195   513  GLU B CD  
9166  O  OE1 . GLU B 513 ? 0.384573  0.756412 0.632112 -0.0043093  0.0451185   -0.120287   513  GLU B OE1 
9167  O  OE2 . GLU B 513 ? 0.429637  0.816416 0.678905 0.0272194   0.0251033   -0.123488   513  GLU B OE2 
9168  N  N   . ALA B 514 ? 0.231371  0.53281  0.416772 -0.00367916 0.0801575   -0.0959786  514  ALA B N   
9169  C  CA  . ALA B 514 ? 0.249432  0.560877 0.439909 -0.0141507  0.096811    -0.0994387  514  ALA B CA  
9170  C  C   . ALA B 514 ? 0.269062  0.575202 0.447858 -0.00338351 0.101649    -0.0983223  514  ALA B C   
9171  O  O   . ALA B 514 ? 0.278183  0.605617 0.469061 -0.00500155 0.11279     -0.105428   514  ALA B O   
9172  C  CB  . ALA B 514 ? 0.266252  0.554561 0.44231  -0.0315465  0.106572    -0.0923114  514  ALA B CB  
9173  N  N   . LEU B 515 ? 0.27324   0.550545 0.428223 0.00609199  0.0944287   -0.0898717  515  LEU B N   
9174  C  CA  . LEU B 515 ? 0.289282  0.556739 0.429671 0.015162    0.0986924   -0.0886788  515  LEU B CA  
9175  C  C   . LEU B 515 ? 0.276505  0.567181 0.432004 0.0311467   0.094733    -0.0975442  515  LEU B C   
9176  O  O   . LEU B 515 ? 0.277912  0.580519 0.436409 0.0344099   0.104431    -0.102833   515  LEU B O   
9177  C  CB  . LEU B 515 ? 0.277372  0.508612 0.389142 0.0187678   0.0928261   -0.0785548  515  LEU B CB  
9178  C  CG  . LEU B 515 ? 0.303981  0.512335 0.397111 0.00528254  0.0998072   -0.0703769  515  LEU B CG  
9179  C  CD1 . LEU B 515 ? 0.317593  0.494096 0.384625 0.00954266  0.0928548   -0.061791   515  LEU B CD1 
9180  C  CD2 . LEU B 515 ? 0.362243  0.575996 0.452212 -0.00293227 0.116679    -0.0722023  515  LEU B CD2 
9181  N  N   . CYS B 516 ? 0.273504  0.570423 0.437695 0.0412749   0.0810103   -0.0992289  516  CYS B N   
9182  C  CA  . CYS B 516 ? 0.302025  0.618213 0.478658 0.0589071   0.0747195   -0.106856   516  CYS B CA  
9183  C  C   . CYS B 516 ? 0.327986  0.685778 0.533803 0.0569382   0.0822427   -0.11907    516  CYS B C   
9184  O  O   . CYS B 516 ? 0.355706  0.731666 0.570982 0.0705161   0.0831118   -0.126652   516  CYS B O   
9185  C  CB  . CYS B 516 ? 0.340366  0.652377 0.517427 0.0691376   0.0587686   -0.105043   516  CYS B CB  
9186  S  SG  . CYS B 516 ? 0.413152  0.678196 0.557436 0.0723643   0.051329    -0.092125   516  CYS B SG  
9187  N  N   . LYS B 517 ? 0.317386  0.689431 0.537014 0.0395584   0.0887718   -0.121409   517  LYS B N   
9188  C  CA  . LYS B 517 ? 0.341487  0.754219 0.59024  0.0341792   0.0984436   -0.133888   517  LYS B CA  
9189  C  C   . LYS B 517 ? 0.342564  0.75567  0.586044 0.0284665   0.116156    -0.134965   517  LYS B C   
9190  O  O   . LYS B 517 ? 0.362936  0.805186 0.623897 0.0350633   0.122478    -0.145083   517  LYS B O   
9191  C  CB  . LYS B 517 ? 0.350948  0.780153 0.618213 0.0177884   0.0985783   -0.137786   517  LYS B CB  
9192  C  CG  . LYS B 517 ? 0.375892  0.852569 0.678196 0.0127818   0.106339    -0.153028   517  LYS B CG  
9193  C  CD  . LYS B 517 ? 0.415566  0.914527 0.740753 -0.00052884 0.10323     -0.160268   517  LYS B CD  
9194  C  CE  . LYS B 517 ? 0.438432  0.983674 0.797251 -0.0076959  0.11531     -0.175699   517  LYS B CE  
9195  N  NZ  . LYS B 517 ? 0.476835  1.0482   0.861358 -0.0221735  0.113722    -0.185403   517  LYS B NZ  
9196  N  N   . GLU B 518 ? 0.337667  0.71946  0.556795 0.0165024   0.124572    -0.124943   518  GLU B N   
9197  C  CA  . GLU B 518 ? 0.366181  0.744436 0.575354 0.0114993   0.14118     -0.124821   518  GLU B CA  
9198  C  C   . GLU B 518 ? 0.394335  0.770822 0.595487 0.0310856   0.138184    -0.127247   518  GLU B C   
9199  O  O   . GLU B 518 ? 0.398732  0.793602 0.607228 0.0330479   0.15017     -0.134373   518  GLU B O   
9200  C  CB  . GLU B 518 ? 0.408221  0.752357 0.591634 -0.0041686  0.148507    -0.113221   518  GLU B CB  
9201  C  CG  . GLU B 518 ? 0.443607  0.775456 0.60796  -0.00925871 0.165122    -0.110359   518  GLU B CG  
9202  C  CD  . GLU B 518 ? 0.50606   0.858658 0.683979 -0.025705   0.185365    -0.116059   518  GLU B CD  
9203  O  OE1 . GLU B 518 ? 0.44877   0.791173 0.60893  -0.0284349  0.199714    -0.11374    518  GLU B OE1 
9204  O  OE2 . GLU B 518 ? 0.49408   0.871949 0.698967 -0.0361687  0.187113    -0.122959   518  GLU B OE2 
9205  N  N   . ALA B 519 ? 0.399179  0.7554   0.587124 0.0456095   0.122696    -0.12246    519  ALA B N   
9206  C  CA  . ALA B 519 ? 0.387153  0.736896 0.565688 0.0645311   0.118725    -0.124672   519  ALA B CA  
9207  C  C   . ALA B 519 ? 0.388231  0.775605 0.593406 0.0785079   0.11806     -0.137594   519  ALA B C   
9208  O  O   . ALA B 519 ? 0.427652  0.815109 0.628026 0.0932682   0.119328    -0.141825   519  ALA B O   
9209  C  CB  . ALA B 519 ? 0.342231  0.659829 0.500724 0.0741766   0.103395    -0.116426   519  ALA B CB  
9210  N  N   . GLY B 520 ? 0.366779  0.786688 0.600192 0.0750548   0.115262    -0.144715   520  GLY B N   
9211  C  CA  . GLY B 520 ? 0.358039  0.816903 0.618595 0.0896544   0.112623    -0.157797   520  GLY B CA  
9212  C  C   . GLY B 520 ? 0.354197  0.806392 0.611897 0.110656    0.0937378   -0.157108   520  GLY B C   
9213  O  O   . GLY B 520 ? 0.33953   0.818068 0.614162 0.127855    0.089236    -0.166877   520  GLY B O   
9214  N  N   . TYR B 521 ? 0.322849  0.740081 0.558872 0.109616    0.0830761   -0.1457     521  TYR B N   
9215  C  CA  . TYR B 521 ? 0.33953   0.744703 0.56842  0.12777     0.0663074   -0.143207   521  TYR B CA  
9216  C  C   . TYR B 521 ? 0.3743    0.81101  0.627704 0.130506    0.0563844   -0.149875   521  TYR B C   
9217  O  O   . TYR B 521 ? 0.349013  0.80229  0.617174 0.113324    0.0599533   -0.151889   521  TYR B O   
9218  C  CB  . TYR B 521 ? 0.329939  0.691178 0.530541 0.121778    0.0599323   -0.12943    521  TYR B CB  
9219  C  CG  . TYR B 521 ? 0.321405  0.666299 0.511911 0.137934    0.0441019   -0.125462   521  TYR B CG  
9220  C  CD1 . TYR B 521 ? 0.362628  0.692936 0.540896 0.158014    0.0393948   -0.12594    521  TYR B CD1 
9221  C  CD2 . TYR B 521 ? 0.342471  0.686883 0.535492 0.133382    0.0344538   -0.121792   521  TYR B CD2 
9222  C  CE1 . TYR B 521 ? 0.387106  0.700649 0.554455 0.172545    0.0260331   -0.121815   521  TYR B CE1 
9223  C  CE2 . TYR B 521 ? 0.345304  0.674623 0.527529 0.14779     0.0209673   -0.117815   521  TYR B CE2 
9224  C  CZ  . TYR B 521 ? 0.374466  0.686915 0.542884 0.167017    0.0171088   -0.117223   521  TYR B CZ  
9225  O  OH  . TYR B 521 ? 0.396832  0.691542 0.552368 0.17952     0.00478698  -0.11216    521  TYR B OH  
9226  N  N   . GLU B 522 ? 0.437596  0.879009 0.692483 0.152282    0.043136    -0.152758   522  GLU B N   
9227  C  CA  . GLU B 522 ? 0.456492  0.935714 0.737396 0.158453    0.0338204   -0.162261   522  GLU B CA  
9228  C  C   . GLU B 522 ? 0.462954  0.926443 0.731104 0.174752    0.0159173   -0.157284   522  GLU B C   
9229  O  O   . GLU B 522 ? 0.513648  1.0061   0.799847 0.181926    0.00598971  -0.164697   522  GLU B O   
9230  C  CB  . GLU B 522 ? 0.520664  1.04255  0.827917 0.171832    0.0372201   -0.177054   522  GLU B CB  
9231  C  CG  . GLU B 522 ? 0.561317  1.11881  0.895298 0.152534    0.0531132   -0.186606   522  GLU B CG  
9232  C  CD  . GLU B 522 ? 0.662481  1.27399  1.03153  0.165127    0.0517556   -0.20385    522  GLU B CD  
9233  O  OE1 . GLU B 522 ? 0.674327  1.30089  1.05097  0.172418    0.0619021   -0.210881   522  GLU B OE1 
9234  O  OE2 . GLU B 522 ? 0.665984  1.30547  1.05473  0.168391    0.0401666   -0.210902   522  GLU B OE2 
9235  N  N   . GLY B 523 ? 0.485087  0.903075 0.721812 0.180151    0.011769    -0.145074   523  GLY B N   
9236  C  CA  . GLY B 523 ? 0.409193  0.809252 0.631172 0.194441    -0.00346841 -0.139424   523  GLY B CA  
9237  C  C   . GLY B 523 ? 0.365478  0.751901 0.580419 0.178523    -0.00788623 -0.131717   523  GLY B C   
9238  O  O   . GLY B 523 ? 0.336862  0.734078 0.563047 0.15751     -0.00073472 -0.132671   523  GLY B O   
9239  N  N   . PRO B 524 ? 0.331778  0.690781 0.525541 0.188051    -0.0189668  -0.123334   524  PRO B N   
9240  C  CA  . PRO B 524 ? 0.338635  0.68115  0.522807 0.173901    -0.0224803  -0.1155     524  PRO B CA  
9241  C  C   . PRO B 524 ? 0.335768  0.654024 0.509172 0.152955    -0.0112192  -0.107841   524  PRO B C   
9242  O  O   . PRO B 524 ? 0.342458  0.636898 0.500826 0.154105    -0.00495082 -0.103333   524  PRO B O   
9243  C  CB  . PRO B 524 ? 0.357148  0.669613 0.516235 0.189908    -0.0339276  -0.10715    524  PRO B CB  
9244  C  CG  . PRO B 524 ? 0.37986   0.696912 0.537639 0.214415    -0.0379864  -0.111817   524  PRO B CG  
9245  C  CD  . PRO B 524 ? 0.355372  0.694968 0.531367 0.212423    -0.0272388  -0.120583   524  PRO B CD  
9246  N  N   . LEU B 525 ? 0.298634  0.624705 0.480471 0.134344    -0.0088208  -0.107506   525  LEU B N   
9247  C  CA  . LEU B 525 ? 0.336348  0.640121 0.507461 0.115195    0.00017866  -0.100057   525  LEU B CA  
9248  C  C   . LEU B 525 ? 0.339093  0.600802 0.481646 0.118476    -0.00088592 -0.088912   525  LEU B C   
9249  O  O   . LEU B 525 ? 0.355337  0.59987  0.487901 0.110448    0.00762829  -0.0850383  525  LEU B O   
9250  C  CB  . LEU B 525 ? 0.334076  0.644794 0.512851 0.0986572   -0.00056496 -0.0997864  525  LEU B CB  
9251  C  CG  . LEU B 525 ? 0.363869  0.659708 0.536948 0.0785259   0.010334    -0.0946438  525  LEU B CG  
9252  C  CD1 . LEU B 525 ? 0.366251  0.672332 0.546804 0.07252     0.0235139   -0.0986153  525  LEU B CD1 
9253  C  CD2 . LEU B 525 ? 0.369412  0.675472 0.55289  0.0636507   0.00969542  -0.0965841  525  LEU B CD2 
9254  N  N   . HIS B 526 ? 0.31491   0.559535 0.44346  0.129946    -0.0109087  -0.0840266  526  HIS B N   
9255  C  CA  . HIS B 526 ? 0.315478  0.520853 0.418803 0.128575    -0.0106984  -0.0737958  526  HIS B CA  
9256  C  C   . HIS B 526 ? 0.319452  0.506659 0.410039 0.140605    -0.00821985 -0.0731367  526  HIS B C   
9257  O  O   . HIS B 526 ? 0.306589  0.46109  0.376349 0.141836    -0.00882966 -0.0659946  526  HIS B O   
9258  C  CB  . HIS B 526 ? 0.319435  0.509158 0.409803 0.133927    -0.0202436  -0.0678646  526  HIS B CB  
9259  C  CG  . HIS B 526 ? 0.357131  0.553847 0.446639 0.154508    -0.0288422  -0.0709597  526  HIS B CG  
9260  N  ND1 . HIS B 526 ? 0.370727  0.601855 0.47944  0.161083    -0.0349213  -0.0794593  526  HIS B ND1 
9261  C  CD2 . HIS B 526 ? 0.380239  0.552898 0.450901 0.169956    -0.0327336  -0.0666602  526  HIS B CD2 
9262  C  CE1 . HIS B 526 ? 0.386554  0.61564  0.4879   0.182125    -0.0429674  -0.0803284  526  HIS B CE1 
9263  N  NE2 . HIS B 526 ? 0.408731  0.600267 0.485678 0.187674    -0.0413413  -0.0719704  526  HIS B NE2 
9264  N  N   . GLN B 527 ? 0.312279  0.52143  0.416013 0.149931    -0.00554875 -0.0814527  527  GLN B N   
9265  C  CA  . GLN B 527 ? 0.338282  0.532612 0.43129  0.163147    -0.00321033 -0.0825924  527  GLN B CA  
9266  C  C   . GLN B 527 ? 0.324654  0.529872 0.425534 0.15503     0.00826344  -0.0875321  527  GLN B C   
9267  O  O   . GLN B 527 ? 0.362802  0.559916 0.457191 0.164279    0.0120144   -0.0903163  527  GLN B O   
9268  C  CB  . GLN B 527 ? 0.38218   0.586783 0.478235 0.186089    -0.010917   -0.0875182  527  GLN B CB  
9269  C  CG  . GLN B 527 ? 0.415053  0.592999 0.491048 0.197585    -0.0207078  -0.0801554  527  GLN B CG  
9270  C  CD  . GLN B 527 ? 0.472868  0.658353 0.548574 0.222633    -0.0288363  -0.0844787  527  GLN B CD  
9271  O  OE1 . GLN B 527 ? 0.467158  0.683948 0.561804 0.232355    -0.0286195  -0.0943126  527  GLN B OE1 
9272  N  NE2 . GLN B 527 ? 0.525743  0.682505 0.579225 0.234378    -0.0360447  -0.0772698  527  GLN B NE2 
9273  N  N   . CYS B 528 ? 0.287455  0.510578 0.401401 0.138132    0.0143484   -0.0889265  528  CYS B N   
9274  C  CA  . CYS B 528 ? 0.30007   0.531982 0.418926 0.129162    0.0262485   -0.0925702  528  CYS B CA  
9275  C  C   . CYS B 528 ? 0.291508  0.490004 0.387485 0.122344    0.0307381   -0.0858563  528  CYS B C   
9276  O  O   . CYS B 528 ? 0.284486  0.461912 0.368322 0.113279    0.0276324   -0.0781033  528  CYS B O   
9277  C  CB  . CYS B 528 ? 0.334422  0.589831 0.470475 0.112381    0.0315414   -0.0947406  528  CYS B CB  
9278  S  SG  . CYS B 528 ? 0.460396  0.71521  0.593719 0.096631    0.0473226   -0.0948996  528  CYS B SG  
9279  N  N   . ASP B 529 ? 0.277883  0.475503 0.369991 0.12594     0.0384919   -0.0900166  529  ASP B N   
9280  C  CA  . ASP B 529 ? 0.281395  0.453514 0.353956 0.119276    0.0437458   -0.0862445  529  ASP B CA  
9281  C  C   . ASP B 529 ? 0.27024   0.459439 0.348953 0.111597    0.0560518   -0.0908889  529  ASP B C   
9282  O  O   . ASP B 529 ? 0.269543  0.477624 0.358369 0.120542    0.0610291   -0.0988182  529  ASP B O   
9283  C  CB  . ASP B 529 ? 0.298896  0.448377 0.355991 0.133328    0.0412094   -0.0875165  529  ASP B CB  
9284  C  CG  . ASP B 529 ? 0.305882  0.427055 0.34167  0.127377    0.0444449   -0.0847229  529  ASP B CG  
9285  O  OD1 . ASP B 529 ? 0.309237  0.426184 0.340292 0.113156    0.047143    -0.08044    529  ASP B OD1 
9286  O  OD2 . ASP B 529 ? 0.319462  0.422823 0.342989 0.137338    0.0441591   -0.0874758  529  ASP B OD2 
9287  N  N   . ILE B 530 ? 0.251598  0.434575 0.324005 0.0958064   0.0612215   -0.0860343  530  ILE B N   
9288  C  CA  . ILE B 530 ? 0.269766  0.466123 0.34515  0.0870148   0.0739122   -0.0889477  530  ILE B CA  
9289  C  C   . ILE B 530 ? 0.274785  0.452695 0.329892 0.0895551   0.0793337   -0.0893985  530  ILE B C   
9290  O  O   . ILE B 530 ? 0.285141  0.470242 0.337748 0.0832598   0.0905847   -0.0912857  530  ILE B O   
9291  C  CB  . ILE B 530 ? 0.268749  0.466492 0.34545  0.0696451   0.078015    -0.0836406  530  ILE B CB  
9292  C  CG1 . ILE B 530 ? 0.275409  0.442461 0.330597 0.0632252   0.0729893   -0.0745797  530  ILE B CG1 
9293  C  CG2 . ILE B 530 ? 0.269655  0.489239 0.368482 0.0666222   0.0735851   -0.0854742  530  ILE B CG2 
9294  C  CD1 . ILE B 530 ? 0.290087  0.453647 0.340625 0.0479412   0.0790759   -0.0693343  530  ILE B CD1 
9295  N  N   . TYR B 531 ? 0.273237  0.426387 0.312823 0.097494    0.0718069   -0.0876325  531  TYR B N   
9296  C  CA  . TYR B 531 ? 0.282821  0.418036 0.303065 0.100829    0.0755677   -0.0897079  531  TYR B CA  
9297  C  C   . TYR B 531 ? 0.295244  0.449354 0.321031 0.106007    0.0867258   -0.0978305  531  TYR B C   
9298  O  O   . TYR B 531 ? 0.302034  0.475392 0.343639 0.116783    0.0873564   -0.104388   531  TYR B O   
9299  C  CB  . TYR B 531 ? 0.294669  0.408436 0.305255 0.112745    0.0670421   -0.090811   531  TYR B CB  
9300  C  CG  . TYR B 531 ? 0.308363  0.398783 0.297623 0.115488    0.0684639   -0.0934204  531  TYR B CG  
9301  C  CD1 . TYR B 531 ? 0.314248  0.389854 0.287277 0.104736    0.0692365   -0.0897897  531  TYR B CD1 
9302  C  CD2 . TYR B 531 ? 0.324774  0.407096 0.309549 0.129619    0.0680691   -0.0999916  531  TYR B CD2 
9303  C  CE1 . TYR B 531 ? 0.329683  0.38521  0.283617 0.107095    0.0692513   -0.0933814  531  TYR B CE1 
9304  C  CE2 . TYR B 531 ? 0.354606  0.415262 0.319818 0.13154     0.0693917   -0.103666   531  TYR B CE2 
9305  C  CZ  . TYR B 531 ? 0.351552  0.398948 0.301775 0.119697    0.0692499   -0.100405   531  TYR B CZ  
9306  O  OH  . TYR B 531 ? 0.373073  0.400885 0.304396 0.121383    0.0696822   -0.105258   531  TYR B OH  
9307  N  N   . ARG B 532 ? 0.304117  0.451532 0.314856 0.0996596   0.0953024   -0.0977485  532  ARG B N   
9308  C  CA  . ARG B 532 ? 0.319561  0.480756 0.330503 0.104292    0.107183    -0.105372   532  ARG B CA  
9309  C  C   . ARG B 532 ? 0.32327   0.517178 0.355685 0.0982321   0.117921    -0.108451   532  ARG B C   
9310  O  O   . ARG B 532 ? 0.330097  0.540091 0.366564 0.102395    0.128825    -0.115764   532  ARG B O   
9311  C  CB  . ARG B 532 ? 0.331043  0.490343 0.342421 0.121816    0.104584    -0.113446   532  ARG B CB  
9312  C  CG  . ARG B 532 ? 0.341006  0.467965 0.326267 0.124773    0.100417    -0.113091   532  ARG B CG  
9313  C  CD  . ARG B 532 ? 0.365503  0.485654 0.348942 0.141677    0.0980071   -0.120842   532  ARG B CD  
9314  N  NE  . ARG B 532 ? 0.388713  0.477795 0.347334 0.142753    0.0948086   -0.121885   532  ARG B NE  
9315  C  CZ  . ARG B 532 ? 0.406681  0.475967 0.356744 0.154461    0.0898123   -0.126541   532  ARG B CZ  
9316  N  NH1 . ARG B 532 ? 0.39643   0.472293 0.358592 0.168712    0.0874805   -0.130306   532  ARG B NH1 
9317  N  NH2 . ARG B 532 ? 0.419346  0.461516 0.347966 0.151745    0.0869324   -0.127641   532  ARG B NH2 
9318  N  N   . SER B 533 ? 0.333265  0.537907 0.380012 0.0881013   0.115689    -0.103931   533  SER B N   
9319  C  CA  . SER B 533 ? 0.335492  0.56983  0.402437 0.0789488   0.126791    -0.107206   533  SER B CA  
9320  C  C   . SER B 533 ? 0.3493    0.573828 0.400322 0.0636653   0.138477    -0.101612   533  SER B C   
9321  O  O   . SER B 533 ? 0.348818  0.556136 0.389703 0.0535182   0.134531    -0.0929164  533  SER B O   
9322  C  CB  . SER B 533 ? 0.343128  0.595201 0.43384  0.0755997   0.119374    -0.106914   533  SER B CB  
9323  O  OG  . SER B 533 ? 0.336746  0.617563 0.447785 0.0645668   0.130674    -0.111163   533  SER B OG  
9324  N  N   . THR B 534 ? 0.37006   0.603382 0.416374 0.0633889   0.152819    -0.10646    534  THR B N   
9325  C  CA  . THR B 534 ? 0.413131  0.638793 0.44341  0.0498293   0.166574    -0.101691   534  THR B CA  
9326  C  C   . THR B 534 ? 0.409875  0.651509 0.457848 0.0340412   0.173678    -0.0995922  534  THR B C   
9327  O  O   . THR B 534 ? 0.431077  0.654783 0.462743 0.021844    0.178172    -0.0912351  534  THR B O   
9328  C  CB  . THR B 534 ? 0.469986  0.69893  0.487668 0.0535116   0.180904    -0.107082   534  THR B CB  
9329  O  OG1 . THR B 534 ? 0.446479  0.710405 0.490496 0.0568657   0.190648    -0.117659   534  THR B OG1 
9330  C  CG2 . THR B 534 ? 0.498324  0.70795  0.495906 0.0679322   0.173672    -0.109546   534  THR B CG2 
9331  N  N   . LYS B 535 ? 0.41533   0.688971 0.495707 0.0346584   0.173469    -0.107252   535  LYS B N   
9332  C  CA  . LYS B 535 ? 0.428702  0.719478 0.528764 0.0191762   0.179339    -0.107282   535  LYS B CA  
9333  C  C   . LYS B 535 ? 0.408389  0.678884 0.502766 0.012735    0.166904    -0.0981671  535  LYS B C   
9334  O  O   . LYS B 535 ? 0.432676  0.691407 0.519123 -0.00223964 0.173299    -0.0917461  535  LYS B O   
9335  C  CB  . LYS B 535 ? 0.439895  0.772673 0.577276 0.0234903   0.179681    -0.119566   535  LYS B CB  
9336  C  CG  . LYS B 535 ? 0.473155  0.832463 0.621441 0.0281352   0.194361    -0.130114   535  LYS B CG  
9337  C  CD  . LYS B 535 ? 0.512321  0.918026 0.699328 0.0240465   0.201839    -0.142557   535  LYS B CD  
9338  C  CE  . LYS B 535 ? 0.565046  0.994408 0.780304 0.0323075   0.186002    -0.14873    535  LYS B CE  
9339  N  NZ  . LYS B 535 ? 0.561064  0.985011 0.772907 0.0553178   0.170007    -0.150363   535  LYS B NZ  
9340  N  N   . ALA B 536 ? 0.357256  0.621422 0.453813 0.0242899   0.14964     -0.0973125  536  ALA B N   
9341  C  CA  . ALA B 536 ? 0.354196  0.59797  0.443216 0.019125    0.138289    -0.0887353  536  ALA B CA  
9342  C  C   . ALA B 536 ? 0.368393  0.578216 0.425536 0.0132173   0.140589    -0.0785792  536  ALA B C   
9343  O  O   . ALA B 536 ? 0.391005  0.588572 0.441694 0.00155355  0.142079    -0.0719685  536  ALA B O   
9344  C  CB  . ALA B 536 ? 0.34799   0.588933 0.441578 0.0328638   0.121355    -0.0894023  536  ALA B CB  
9345  N  N   . GLY B 537 ? 0.377471  0.572968 0.414007 0.021226    0.142131    -0.0781361  537  GLY B N   
9346  C  CA  . GLY B 537 ? 0.366409  0.532882 0.371958 0.0171995   0.144562    -0.0699818  537  GLY B CA  
9347  C  C   . GLY B 537 ? 0.393978  0.557995 0.392319 0.00250143  0.1597      -0.0657966  537  GLY B C   
9348  O  O   . GLY B 537 ? 0.414873  0.556077 0.395181 -0.00397497 0.157897    -0.0570124  537  GLY B O   
9349  N  N   . ALA B 538 ? 0.400428  0.587419 0.412482 -0.00237981 0.174974    -0.0723091  538  ALA B N   
9350  C  CA  . ALA B 538 ? 0.428803  0.614745 0.435149 -0.0175177  0.192602    -0.0694272  538  ALA B CA  
9351  C  C   . ALA B 538 ? 0.422723  0.604416 0.437959 -0.0303659  0.190429    -0.0646123  538  ALA B C   
9352  O  O   . ALA B 538 ? 0.435597  0.592563 0.429223 -0.0394947  0.195662    -0.0556752  538  ALA B O   
9353  C  CB  . ALA B 538 ? 0.425276  0.643341 0.452568 -0.0201582  0.20828     -0.0797097  538  ALA B CB  
9354  N  N   . LYS B 539 ? 0.408572  0.612709 0.453749 -0.0297525  0.181786    -0.0705976  539  LYS B N   
9355  C  CA  . LYS B 539 ? 0.415788  0.617386 0.470923 -0.0408612  0.178136    -0.0676427  539  LYS B CA  
9356  C  C   . LYS B 539 ? 0.452697  0.620724 0.484319 -0.038854   0.165892    -0.0568322  539  LYS B C   
9357  O  O   . LYS B 539 ? 0.465303  0.615698 0.486937 -0.0498593  0.169485    -0.0502798  539  LYS B O   
9358  C  CB  . LYS B 539 ? 0.399583  0.632686 0.489056 -0.0364798  0.168585    -0.0771554  539  LYS B CB  
9359  C  CG  . LYS B 539 ? 0.39917   0.629665 0.498718 -0.0455768  0.161479    -0.075082   539  LYS B CG  
9360  C  CD  . LYS B 539 ? 0.407663  0.675203 0.543212 -0.04524    0.157039    -0.0865107  539  LYS B CD  
9361  C  CE  . LYS B 539 ? 0.430785  0.724764 0.58636  -0.0585854  0.174342    -0.0950234  539  LYS B CE  
9362  N  NZ  . LYS B 539 ? 0.426321  0.701865 0.572258 -0.077787   0.185422    -0.0895092  539  LYS B NZ  
9363  N  N   . LEU B 540 ? 0.439888  0.598885 0.463262 -0.0248563  0.151427    -0.0554094  540  LEU B N   
9364  C  CA  . LEU B 540 ? 0.42775   0.558211 0.430385 -0.0225416  0.140316    -0.0464403  540  LEU B CA  
9365  C  C   . LEU B 540 ? 0.467767  0.572057 0.439106 -0.026982   0.149185    -0.0384105  540  LEU B C   
9366  O  O   . LEU B 540 ? 0.49115   0.574478 0.448618 -0.0321469  0.147001    -0.030739   540  LEU B O   
9367  C  CB  . LEU B 540 ? 0.407415  0.534539 0.408364 -0.00827395 0.125061    -0.0476013  540  LEU B CB  
9368  C  CG  . LEU B 540 ? 0.418438  0.522794 0.405527 -0.00559563 0.111786    -0.0405091  540  LEU B CG  
9369  C  CD1 . LEU B 540 ? 0.403546  0.509829 0.403875 -0.0128396  0.106966    -0.0384394  540  LEU B CD1 
9370  C  CD2 . LEU B 540 ? 0.385612  0.491284 0.375583 0.00701839  0.0997941   -0.0439028  540  LEU B CD2 
9371  N  N   . ARG B 541 ? 0.497861  0.603088 0.456992 -0.0245275  0.159804    -0.0402784  541  ARG B N   
9372  C  CA  . ARG B 541 ? 0.525375  0.604653 0.450986 -0.0266205  0.167586    -0.0325424  541  ARG B CA  
9373  C  C   . ARG B 541 ? 0.530093  0.596787 0.449083 -0.041076   0.178714    -0.0261397  541  ARG B C   
9374  O  O   . ARG B 541 ? 0.576482  0.61475  0.468378 -0.0414152  0.177111    -0.016973   541  ARG B O   
9375  C  CB  . ARG B 541 ? 0.583885  0.666794 0.496559 -0.0216221  0.178024    -0.0361875  541  ARG B CB  
9376  C  CG  . ARG B 541 ? 0.678083  0.731367 0.551293 -0.0185361  0.179976    -0.028247   541  ARG B CG  
9377  C  CD  . ARG B 541 ? 0.707069  0.760685 0.564624 -0.00797457 0.18164     -0.0327658  541  ARG B CD  
9378  N  NE  . ARG B 541 ? 0.760526  0.831518 0.624854 -0.0127321  0.200207    -0.0382157  541  ARG B NE  
9379  C  CZ  . ARG B 541 ? 0.69123   0.788894 0.578117 -0.00805216 0.203291    -0.0486339  541  ARG B CZ  
9380  N  NH1 . ARG B 541 ? 0.593385  0.6988   0.49179  0.003853    0.189012    -0.0545645  541  ARG B NH1 
9381  N  NH2 . ARG B 541 ? 0.671836  0.78729  0.568247 -0.0153368  0.221801    -0.0531132  541  ARG B NH2 
9382  N  N   . LYS B 542 ? 0.54097   0.62854  0.485041 -0.0525128  0.189053    -0.0314847  542  LYS B N   
9383  C  CA  . LYS B 542 ? 0.595284  0.671408 0.534622 -0.0685112  0.202586    -0.0269225  542  LYS B CA  
9384  C  C   . LYS B 542 ? 0.582596  0.638608 0.517053 -0.0704593  0.191073    -0.0202608  542  LYS B C   
9385  O  O   . LYS B 542 ? 0.582734  0.609153 0.491759 -0.0755675  0.19607     -0.0110928  542  LYS B O   
9386  C  CB  . LYS B 542 ? 0.604276  0.711545 0.574335 -0.0807157  0.216655    -0.0365368  542  LYS B CB  
9387  C  CG  . LYS B 542 ? 0.68756   0.785227 0.65569  -0.100119   0.233793    -0.033785   542  LYS B CG  
9388  C  CD  . LYS B 542 ? 0.716904  0.849051 0.71637  -0.112842   0.249434    -0.0450482  542  LYS B CD  
9389  C  CE  . LYS B 542 ? 0.752068  0.90372  0.753229 -0.104323   0.25621     -0.0508851  542  LYS B CE  
9390  N  NZ  . LYS B 542 ? 0.83761   1.01761  0.860315 -0.11704    0.276324    -0.0601633  542  LYS B NZ  
9391  N  N   . VAL B 543 ? 0.534456  0.604473 0.490232 -0.0642142  0.174851    -0.0244872  543  VAL B N   
9392  C  CA  . VAL B 543 ? 0.491459  0.543635 0.441827 -0.0631568  0.162303    -0.0188098  543  VAL B CA  
9393  C  C   . VAL B 543 ? 0.48513   0.506069 0.40082  -0.0546326  0.156604    -0.00919296 543  VAL B C   
9394  O  O   . VAL B 543 ? 0.508621  0.504767 0.406991 -0.0583607  0.156875    -0.00156357 543  VAL B O   
9395  C  CB  . VAL B 543 ? 0.430447  0.50273  0.406861 -0.0566028  0.146376    -0.0248897  543  VAL B CB  
9396  C  CG1 . VAL B 543 ? 0.422073  0.475399 0.39083  -0.0546174  0.133889    -0.0189942  543  VAL B CG1 
9397  C  CG2 . VAL B 543 ? 0.398098  0.499638 0.406606 -0.0657124  0.151821    -0.0341432  543  VAL B CG2 
9398  N  N   . LEU B 544 ? 0.468437  0.490241 0.373912 -0.0425091  0.150441    -0.0101056  544  LEU B N   
9399  C  CA  . LEU B 544 ? 0.473286  0.470659 0.351023 -0.0330909  0.140747    -0.00313892 544  LEU B CA  
9400  C  C   . LEU B 544 ? 0.540001  0.510534 0.383794 -0.0357509  0.151813    0.00528808  544  LEU B C   
9401  O  O   . LEU B 544 ? 0.521001  0.467904 0.341738 -0.0305312  0.14479     0.01254     544  LEU B O   
9402  C  CB  . LEU B 544 ? 0.471846  0.477132 0.348236 -0.0204727  0.130976    -0.00763981 544  LEU B CB  
9403  C  CG  . LEU B 544 ? 0.470895  0.497988 0.375858 -0.0159624  0.119926    -0.0149901  544  LEU B CG  
9404  C  CD1 . LEU B 544 ? 0.497633  0.522938 0.393794 -0.0040281  0.11022     -0.0177538  544  LEU B CD1 
9405  C  CD2 . LEU B 544 ? 0.445862  0.468616 0.360458 -0.0179471  0.109377    -0.0121807  544  LEU B CD2 
9406  N  N   . ARG B 545 ? 0.575362  0.549695 0.414601 -0.042543   0.169045    0.00414427  545  ARG B N   
9407  C  CA  . ARG B 545 ? 0.675287  0.622472 0.478876 -0.0446197  0.181108    0.0125898   545  ARG B CA  
9408  C  C   . ARG B 545 ? 0.707033  0.631696 0.501424 -0.0554166  0.18841     0.0202231   545  ARG B C   
9409  O  O   . ARG B 545 ? 0.736208  0.629932 0.495919 -0.0536708  0.192844    0.0297111   545  ARG B O   
9410  C  CB  . ARG B 545 ? 0.708824  0.667977 0.511729 -0.0498822  0.199203    0.00856931  545  ARG B CB  
9411  C  CG  . ARG B 545 ? 0.74033   0.719189 0.549765 -0.0386865  0.193444    0.0006393   545  ARG B CG  
9412  C  CD  . ARG B 545 ? 0.82794   0.817556 0.634684 -0.043787   0.213016    -0.00320088 545  ARG B CD  
9413  N  NE  . ARG B 545 ? 0.905567  0.867422 0.670318 -0.042022   0.222858    0.00494334  545  ARG B NE  
9414  C  CZ  . ARG B 545 ? 0.934138  0.881221 0.670653 -0.0286725  0.213714    0.00736803  545  ARG B CZ  
9415  N  NH1 . ARG B 545 ? 0.886486  0.8437   0.633229 -0.0170137  0.195344    0.00184636  545  ARG B NH1 
9416  N  NH2 . ARG B 545 ? 0.988734  0.910206 0.685868 -0.0273803  0.22336     0.015104    545  ARG B NH2 
9417  N  N   . ALA B 546 ? 0.710328  0.649895 0.534739 -0.066084   0.189689    0.0156386   546  ALA B N   
9418  C  CA  . ALA B 546 ? 0.704669  0.625474 0.525603 -0.078284   0.197239    0.0205768   546  ALA B CA  
9419  C  C   . ALA B 546 ? 0.749261  0.642859 0.55077  -0.0699394  0.183558    0.0285973   546  ALA B C   
9420  O  O   . ALA B 546 ? 0.805253  0.671979 0.590348 -0.0766304  0.190338    0.0354958   546  ALA B O   
9421  C  CB  . ALA B 546 ? 0.660621  0.60843  0.520709 -0.0904595  0.199606    0.0113997   546  ALA B CB  
9422  N  N   . GLY B 547 ? 0.690877  0.591078 0.494806 -0.0556241  0.164748    0.0272587   547  GLY B N   
9423  C  CA  . GLY B 547 ? 0.632746  0.513083 0.423908 -0.0475929  0.151184    0.0330012   547  GLY B CA  
9424  C  C   . GLY B 547 ? 0.593464  0.467864 0.398077 -0.0583844  0.153531    0.0332723   547  GLY B C   
9425  O  O   . GLY B 547 ? 0.544894  0.443344 0.380886 -0.0671949  0.155067    0.0254189   547  GLY B O   
9426  N  N   . SER B 548 ? 0.651033  0.492557 0.430186 -0.0573132  0.154396    0.0419738   548  SER B N   
9427  C  CA  . SER B 548 ? 0.666658  0.495847 0.452767 -0.0678188  0.158342    0.0427921   548  SER B CA  
9428  C  C   . SER B 548 ? 0.740565  0.541579 0.504383 -0.0801833  0.178509    0.0491315   548  SER B C   
9429  O  O   . SER B 548 ? 0.731515  0.504636 0.482091 -0.0841999  0.181538    0.0543284   548  SER B O   
9430  C  CB  . SER B 548 ? 0.675633  0.487362 0.451316 -0.0571464  0.14399     0.0471462   548  SER B CB  
9431  O  OG  . SER B 548 ? 0.725366  0.510889 0.46428  -0.0446349  0.141729    0.0561215   548  SER B OG  
9432  N  N   . SER B 549 ? 0.742603  0.550639 0.502807 -0.0866818  0.193044    0.0482397   549  SER B N   
9433  C  CA  . SER B 549 ? 0.847346  0.629743 0.586665 -0.100092   0.214645    0.0539544   549  SER B CA  
9434  C  C   . SER B 549 ? 0.845352  0.637566 0.61309  -0.119692   0.224362    0.0469858   549  SER B C   
9435  O  O   . SER B 549 ? 0.957668  0.720388 0.709819 -0.131227   0.237515    0.0519746   549  SER B O   
9436  C  CB  . SER B 549 ? 0.846143  0.637499 0.576817 -0.102077   0.227976    0.0535475   549  SER B CB  
9437  O  OG  . SER B 549 ? 0.823333  0.655054 0.593598 -0.112675   0.233172    0.0414662   549  SER B OG  
9438  N  N   . ARG B 550 ? 0.755367  0.588722 0.563991 -0.122985   0.217582    0.0350454   550  ARG B N   
9439  C  CA  . ARG B 550 ? 0.755111  0.606666 0.595429 -0.140968   0.225367    0.0256804   550  ARG B CA  
9440  C  C   . ARG B 550 ? 0.727341  0.591179 0.590881 -0.137423   0.207841    0.0200908   550  ARG B C   
9441  O  O   . ARG B 550 ? 0.712761  0.581498 0.57527  -0.121065   0.189948    0.0214748   550  ARG B O   
9442  C  CB  . ARG B 550 ? 0.768413  0.659821 0.635898 -0.146729   0.233026    0.0157308   550  ARG B CB  
9443  C  CG  . ARG B 550 ? 0.903135  0.779683 0.750179 -0.157422   0.256259    0.0200607   550  ARG B CG  
9444  C  CD  . ARG B 550 ? 0.877783  0.791678 0.756302 -0.171332   0.270545    0.00843066  550  ARG B CD  
9445  N  NE  . ARG B 550 ? 0.768792  0.72542  0.677121 -0.160128   0.256966    -0.00131422 550  ARG B NE  
9446  C  CZ  . ARG B 550 ? 0.727     0.724072 0.676407 -0.167563   0.256493    -0.0147167  550  ARG B CZ  
9447  N  NH1 . ARG B 550 ? 0.724945  0.729138 0.693433 -0.187328   0.268742    -0.0213314  550  ARG B NH1 
9448  N  NH2 . ARG B 550 ? 0.677864  0.707947 0.648438 -0.154834   0.243842    -0.0218817  550  ARG B NH2 
9449  N  N   . PRO B 551 ? 0.725399  0.592965 0.608803 -0.153031   0.213016    0.013513    551  PRO B N   
9450  C  CA  . PRO B 551 ? 0.660916  0.545756 0.569692 -0.150824   0.197296    0.00611433  551  PRO B CA  
9451  C  C   . PRO B 551 ? 0.61405   0.543616 0.554331 -0.142988   0.185001    -0.00338288 551  PRO B C   
9452  O  O   . PRO B 551 ? 0.583996  0.542611 0.544778 -0.149678   0.193012    -0.0110409  551  PRO B O   
9453  C  CB  . PRO B 551 ? 0.669918  0.553169 0.59415  -0.171676   0.208788    -0.00087798 551  PRO B CB  
9454  C  CG  . PRO B 551 ? 0.715197  0.564818 0.611705 -0.183709   0.230468    0.00688914  551  PRO B CG  
9455  C  CD  . PRO B 551 ? 0.740993  0.592487 0.620122 -0.173939   0.234749    0.0131658   551  PRO B CD  
9456  N  N   . TRP B 552 ? 0.560657  0.495186 0.505006 -0.128998   0.166006    -0.00323558 552  TRP B N   
9457  C  CA  . TRP B 552 ? 0.478686  0.447971 0.44573  -0.118734   0.153418    -0.00985268 552  TRP B CA  
9458  C  C   . TRP B 552 ? 0.455894  0.459748 0.4584   -0.129803   0.155934    -0.0226999  552  TRP B C   
9459  O  O   . TRP B 552 ? 0.454892  0.490608 0.47763  -0.124992   0.152259    -0.029524   552  TRP B O   
9460  C  CB  . TRP B 552 ? 0.474916  0.439398 0.437906 -0.103773   0.134564    -0.00691054 552  TRP B CB  
9461  C  CG  . TRP B 552 ? 0.472535  0.433194 0.444958 -0.107714   0.127725    -0.0101159  552  TRP B CG  
9462  C  CD1 . TRP B 552 ? 0.492443  0.421605 0.445505 -0.107548   0.126652    -0.00398204 552  TRP B CD1 
9463  C  CD2 . TRP B 552 ? 0.449146  0.438176 0.451363 -0.111342   0.120755    -0.0206739  552  TRP B CD2 
9464  N  NE1 . TRP B 552 ? 0.499686  0.43582  0.468835 -0.111174   0.119748    -0.0102844  552  TRP B NE1 
9465  C  CE2 . TRP B 552 ? 0.459868  0.432304 0.458568 -0.113872   0.115985    -0.0204943  552  TRP B CE2 
9466  C  CE3 . TRP B 552 ? 0.411888  0.437957 0.441784 -0.111223   0.117434    -0.0302892  552  TRP B CE3 
9467  C  CZ2 . TRP B 552 ? 0.46174   0.453483 0.482821 -0.116911   0.108162    -0.0296752  552  TRP B CZ2 
9468  C  CZ3 . TRP B 552 ? 0.431021  0.476262 0.482799 -0.113554   0.109223    -0.0390128  552  TRP B CZ3 
9469  C  CH2 . TRP B 552 ? 0.438526  0.466938 0.485684 -0.116759   0.104711    -0.0387994  552  TRP B CH2 
9470  N  N   . GLN B 553 ? 0.457693  0.455086 0.467525 -0.144369   0.16204     -0.0266536  553  GLN B N   
9471  C  CA  . GLN B 553 ? 0.477158  0.508196 0.521238 -0.15618    0.164363    -0.0402469  553  GLN B CA  
9472  C  C   . GLN B 553 ? 0.512122  0.565894 0.56938  -0.165      0.17937     -0.0458101  553  GLN B C   
9473  O  O   . GLN B 553 ? 0.487301  0.580221 0.575616 -0.166933   0.177358    -0.0575788  553  GLN B O   
9474  C  CB  . GLN B 553 ? 0.49623   0.514176 0.544711 -0.172381   0.169725    -0.0444987  553  GLN B CB  
9475  C  CG  . GLN B 553 ? 0.495782  0.501222 0.540334 -0.164954   0.154277    -0.0433858  553  GLN B CG  
9476  C  CD  . GLN B 553 ? 0.527303  0.48696  0.536848 -0.159961   0.154848    -0.0305637  553  GLN B CD  
9477  O  OE1 . GLN B 553 ? 0.582108  0.518329 0.566359 -0.157297   0.163284    -0.0206058  553  GLN B OE1 
9478  N  NE2 . GLN B 553 ? 0.55136   0.497617 0.558184 -0.157956   0.145775    -0.0310565  553  GLN B NE2 
9479  N  N   . GLU B 554 ? 0.561462  0.590658 0.594177 -0.169668   0.194577    -0.0374742  554  GLU B N   
9480  C  CA  . GLU B 554 ? 0.599917  0.647437 0.641997 -0.179019   0.211283    -0.0420786  554  GLU B CA  
9481  C  C   . GLU B 554 ? 0.574328  0.638779 0.614905 -0.162126   0.205108    -0.0407266  554  GLU B C   
9482  O  O   . GLU B 554 ? 0.563624  0.663714 0.628563 -0.16285    0.20867     -0.0502099  554  GLU B O   
9483  C  CB  . GLU B 554 ? 0.706656  0.716423 0.718615 -0.190944   0.231074    -0.032741   554  GLU B CB  
9484  C  CG  . GLU B 554 ? 0.792881  0.787168 0.808761 -0.211653   0.242136    -0.0360148  554  GLU B CG  
9485  C  CD  . GLU B 554 ? 0.917571  0.863246 0.893902 -0.218692   0.258743    -0.023084   554  GLU B CD  
9486  O  OE1 . GLU B 554 ? 1.00339   0.935034 0.953779 -0.208448   0.262353    -0.0135344  554  GLU B OE1 
9487  O  OE2 . GLU B 554 ? 0.96384   0.88383  0.933214 -0.23368    0.267862    -0.022441   554  GLU B OE2 
9488  N  N   . VAL B 555 ? 0.558797  0.59747  0.570827 -0.147      0.195975    -0.029634   555  VAL B N   
9489  C  CA  . VAL B 555 ? 0.557397  0.609237 0.567108 -0.130226   0.187469    -0.0288291  555  VAL B CA  
9490  C  C   . VAL B 555 ? 0.510556  0.601639 0.554567 -0.12398    0.17474     -0.0400726  555  VAL B C   
9491  O  O   . VAL B 555 ? 0.449598  0.566965 0.507542 -0.118983   0.176416    -0.0461391  555  VAL B O   
9492  C  CB  . VAL B 555 ? 0.590047  0.611334 0.567684 -0.115193   0.17684     -0.0171882  555  VAL B CB  
9493  C  CG1 . VAL B 555 ? 0.560058  0.59555  0.537662 -0.0986518  0.166635    -0.0180173  555  VAL B CG1 
9494  C  CG2 . VAL B 555 ? 0.644703  0.628769 0.586337 -0.119268   0.189871    -0.00629906 555  VAL B CG2 
9495  N  N   . LEU B 556 ? 0.521965  0.616763 0.578892 -0.124023   0.16256     -0.0432166  556  LEU B N   
9496  C  CA  . LEU B 556 ? 0.447436  0.575083 0.532083 -0.116173   0.148865    -0.0525395  556  LEU B CA  
9497  C  C   . LEU B 556 ? 0.474696  0.640572 0.590894 -0.124846   0.156902    -0.0655482  556  LEU B C   
9498  O  O   . LEU B 556 ? 0.435137  0.629298 0.568036 -0.114445   0.150844    -0.0719336  556  LEU B O   
9499  C  CB  . LEU B 556 ? 0.457074  0.578582 0.545552 -0.114669   0.135215    -0.0528481  556  LEU B CB  
9500  C  CG  . LEU B 556 ? 0.435842  0.583954 0.544818 -0.103118   0.118861    -0.0597172  556  LEU B CG  
9501  C  CD1 . LEU B 556 ? 0.420281  0.56886  0.520795 -0.0849636  0.108571    -0.055488   556  LEU B CD1 
9502  C  CD2 . LEU B 556 ? 0.418522  0.555634 0.52696  -0.104624   0.108845    -0.0593713  556  LEU B CD2 
9503  N  N   . LYS B 557 ? 0.523841  0.691196 0.649177 -0.143764   0.17026     -0.0702567  557  LYS B N   
9504  C  CA  . LYS B 557 ? 0.541129  0.74751  0.699324 -0.15431    0.178892    -0.0842222  557  LYS B CA  
9505  C  C   . LYS B 557 ? 0.537384  0.760387 0.697618 -0.149795   0.18905     -0.0857969  557  LYS B C   
9506  O  O   . LYS B 557 ? 0.55271   0.814443 0.740014 -0.144326   0.185985    -0.096715   557  LYS B O   
9507  C  CB  . LYS B 557 ? 0.594709  0.792276 0.756802 -0.177856   0.194825    -0.0875081  557  LYS B CB  
9508  C  CG  . LYS B 557 ? 0.591749  0.828971 0.789221 -0.193309   0.206117    -0.103153   557  LYS B CG  
9509  C  CD  . LYS B 557 ? 0.577939  0.831872 0.799934 -0.202382   0.197826    -0.114384   557  LYS B CD  
9510  C  CE  . LYS B 557 ? 0.608109  0.898625 0.864928 -0.221347   0.209887    -0.130801   557  LYS B CE  
9511  N  NZ  . LYS B 557 ? 0.558824  0.900573 0.847883 -0.210036   0.201435    -0.143461   557  LYS B NZ  
9512  N  N   . ASP B 558 ? 0.549443  0.743032 0.679921 -0.150773   0.200644    -0.0751322  558  ASP B N   
9513  C  CA  . ASP B 558 ? 0.58373   0.790707 0.713195 -0.146951   0.2116      -0.0765991  558  ASP B CA  
9514  C  C   . ASP B 558 ? 0.575529  0.801982 0.712927 -0.125736   0.195606    -0.0794041  558  ASP B C   
9515  O  O   . ASP B 558 ? 0.51878   0.777389 0.676018 -0.12133    0.199055    -0.0884703  558  ASP B O   
9516  C  CB  . ASP B 558 ? 0.638311  0.80695  0.729128 -0.148005   0.223483    -0.0635666  558  ASP B CB  
9517  C  CG  . ASP B 558 ? 0.724044  0.875491 0.805621 -0.169403   0.24542     -0.0613588  558  ASP B CG  
9518  O  OD1 . ASP B 558 ? 0.750108  0.927517 0.860625 -0.18502    0.254875    -0.0724999  558  ASP B OD1 
9519  O  OD2 . ASP B 558 ? 0.740136  0.851538 0.785195 -0.170438   0.252655    -0.0487316  558  ASP B OD2 
9520  N  N   . MET B 559 ? 0.539453  0.746023 0.662001 -0.11308    0.178342    -0.0720847  559  MET B N   
9521  C  CA  . MET B 559 ? 0.49813   0.713114 0.620769 -0.0933197  0.164019    -0.0722879  559  MET B CA  
9522  C  C   . MET B 559 ? 0.457469  0.708752 0.612791 -0.0874574  0.152709    -0.0838343  559  MET B C   
9523  O  O   . MET B 559 ? 0.470334  0.747003 0.639766 -0.0775265  0.151561    -0.0907803  559  MET B O   
9524  C  CB  . MET B 559 ? 0.524363  0.705241 0.618719 -0.0829665  0.15176     -0.0606347  559  MET B CB  
9525  C  CG  . MET B 559 ? 0.564222  0.743938 0.648107 -0.0658147  0.144592    -0.0587443  559  MET B CG  
9526  S  SD  . MET B 559 ? 0.615721  0.783993 0.695373 -0.0527185  0.122679    -0.0546745  559  MET B SD  
9527  C  CE  . MET B 559 ? 0.53271   0.693972 0.59803  -0.0344975  0.114168    -0.0523268  559  MET B CE  
9528  N  N   . VAL B 560 ? 0.421859  0.676038 0.588672 -0.0928375  0.144423    -0.0864665  560  VAL B N   
9529  C  CA  . VAL B 560 ? 0.376475  0.659816 0.567457 -0.0830273  0.130065    -0.0954653  560  VAL B CA  
9530  C  C   . VAL B 560 ? 0.402421  0.719441 0.625348 -0.0955406  0.134322    -0.10884    560  VAL B C   
9531  O  O   . VAL B 560 ? 0.354533  0.700359 0.599015 -0.0865767  0.122789    -0.11782    560  VAL B O   
9532  C  CB  . VAL B 560 ? 0.367371  0.632883 0.547487 -0.0735309  0.112494    -0.0895207  560  VAL B CB  
9533  C  CG1 . VAL B 560 ? 0.324006  0.5567   0.473879 -0.0636071  0.108993    -0.0772136  560  VAL B CG1 
9534  C  CG2 . VAL B 560 ? 0.338686  0.593652 0.520071 -0.086755   0.111231    -0.0894506  560  VAL B CG2 
9535  N  N   . GLY B 561 ? 0.479281  0.791301 0.703988 -0.115737   0.150102    -0.110182   561  GLY B N   
9536  C  CA  . GLY B 561 ? 0.524396  0.869237 0.780999 -0.130542   0.155953    -0.124314   561  GLY B CA  
9537  C  C   . GLY B 561 ? 0.539519  0.874816 0.799144 -0.141018   0.149399    -0.126013   561  GLY B C   
9538  O  O   . GLY B 561 ? 0.515421  0.875523 0.800718 -0.154801   0.153107    -0.138381   561  GLY B O   
9539  N  N   . LEU B 562 ? 0.567332  0.866929 0.800914 -0.134731   0.139782    -0.114319   562  LEU B N   
9540  C  CA  . LEU B 562 ? 0.54368   0.830948 0.776733 -0.142412   0.132882    -0.115218   562  LEU B CA  
9541  C  C   . LEU B 562 ? 0.508081  0.746664 0.707142 -0.146993   0.138164    -0.100781   562  LEU B C   
9542  O  O   . LEU B 562 ? 0.525937  0.742303 0.701207 -0.137935   0.139823    -0.0895897  562  LEU B O   
9543  C  CB  . LEU B 562 ? 0.587625  0.886312 0.825423 -0.124435   0.111701    -0.116828   562  LEU B CB  
9544  C  CG  . LEU B 562 ? 0.600317  0.901777 0.846629 -0.129091   0.10121     -0.122835   562  LEU B CG  
9545  C  CD1 . LEU B 562 ? 0.568952  0.91687  0.850873 -0.132467   0.0970091   -0.140488   562  LEU B CD1 
9546  C  CD2 . LEU B 562 ? 0.547629  0.831047 0.775927 -0.11194    0.0845419   -0.11434    562  LEU B CD2 
9547  N  N   . ASP B 563 ? 0.480233  0.702037 0.6765   -0.160249   0.140135    -0.101586   563  ASP B N   
9548  C  CA  . ASP B 563 ? 0.504338  0.679956 0.668922 -0.165496   0.14708     -0.0888389  563  ASP B CA  
9549  C  C   . ASP B 563 ? 0.48968   0.643357 0.638914 -0.154816   0.131319    -0.0824208  563  ASP B C   
9550  O  O   . ASP B 563 ? 0.52984   0.646225 0.654391 -0.157914   0.13475     -0.0730861  563  ASP B O   
9551  C  CB  . ASP B 563 ? 0.607045  0.770697 0.773084 -0.188699   0.164555    -0.0922684  563  ASP B CB  
9552  C  CG  . ASP B 563 ? 0.663096  0.839182 0.850391 -0.202132   0.161679    -0.104575   563  ASP B CG  
9553  O  OD1 . ASP B 563 ? 0.640117  0.830004 0.837501 -0.192493   0.144362    -0.109411   563  ASP B OD1 
9554  O  OD2 . ASP B 563 ? 0.717476  0.889024 0.910703 -0.222962   0.177424    -0.109805   563  ASP B OD2 
9555  N  N   . ALA B 564 ? 0.440532  0.616264 0.602928 -0.141713   0.114713    -0.0871698  564  ALA B N   
9556  C  CA  . ALA B 564 ? 0.420253  0.576718 0.568496 -0.131847   0.100815    -0.0814494  564  ALA B CA  
9557  C  C   . ALA B 564 ? 0.405125  0.572269 0.552097 -0.111801   0.086473    -0.0784466  564  ALA B C   
9558  O  O   . ALA B 564 ? 0.360687  0.557427 0.524725 -0.105346   0.0836438   -0.0846909  564  ALA B O   
9559  C  CB  . ALA B 564 ? 0.384857  0.549316 0.547346 -0.140743   0.0956888   -0.0911964  564  ALA B CB  
9560  N  N   . LEU B 565 ? 0.390144  0.532819 0.517213 -0.102214   0.0776232   -0.0694847  565  LEU B N   
9561  C  CA  . LEU B 565 ? 0.386395  0.535787 0.512131 -0.0855853  0.0632698   -0.0674907  565  LEU B CA  
9562  C  C   . LEU B 565 ? 0.376375  0.556883 0.524997 -0.0834749  0.0543796   -0.0787537  565  LEU B C   
9563  O  O   . LEU B 565 ? 0.423404  0.609977 0.582454 -0.0937694  0.0546242   -0.0862682  565  LEU B O   
9564  C  CB  . LEU B 565 ? 0.37947   0.502606 0.486364 -0.0798255  0.055563    -0.0597898  565  LEU B CB  
9565  C  CG  . LEU B 565 ? 0.435868  0.528229 0.518117 -0.0775175  0.0601814   -0.048341   565  LEU B CG  
9566  C  CD1 . LEU B 565 ? 0.414204  0.493845 0.485282 -0.0668184  0.048591    -0.0433366  565  LEU B CD1 
9567  C  CD2 . LEU B 565 ? 0.415188  0.51356  0.494663 -0.0713931  0.0638972   -0.0453662  565  LEU B CD2 
9568  N  N   . ASP B 566 ? 0.328611  0.526283 0.482764 -0.0693675  0.0458692   -0.0797744  566  ASP B N   
9569  C  CA  . ASP B 566 ? 0.322566  0.552022 0.497557 -0.0645479  0.0370437   -0.0905229  566  ASP B CA  
9570  C  C   . ASP B 566 ? 0.306791  0.537832 0.474916 -0.0458092  0.0252841   -0.0865028  566  ASP B C   
9571  O  O   . ASP B 566 ? 0.302812  0.527026 0.46222  -0.0376452  0.0271927   -0.0804635  566  ASP B O   
9572  C  CB  . ASP B 566 ? 0.353289  0.613519 0.55118  -0.0701109  0.0445523   -0.100482   566  ASP B CB  
9573  C  CG  . ASP B 566 ? 0.406133  0.704138 0.627854 -0.0635394  0.0350932   -0.113028   566  ASP B CG  
9574  O  OD1 . ASP B 566 ? 0.478917  0.779298 0.699373 -0.0563325  0.022448    -0.114917   566  ASP B OD1 
9575  O  OD2 . ASP B 566 ? 0.447255  0.773842 0.689067 -0.0652354  0.0403757   -0.121592   566  ASP B OD2 
9576  N  N   . ALA B 567 ? 0.281373  0.521331 0.452978 -0.0392666  0.0135449   -0.0905088  567  ALA B N   
9577  C  CA  . ALA B 567 ? 0.288415  0.52622  0.450839 -0.0221453  0.00283649  -0.0862502  567  ALA B CA  
9578  C  C   . ALA B 567 ? 0.263066  0.529553 0.440211 -0.0106085  -0.00220708 -0.093311   567  ALA B C   
9579  O  O   . ALA B 567 ? 0.259402  0.521176 0.426897 0.00430851  -0.00986345 -0.0890964  567  ALA B O   
9580  C  CB  . ALA B 567 ? 0.30103   0.530546 0.455247 -0.0193309  -0.00681894 -0.085699   567  ALA B CB  
9581  N  N   . GLN B 568 ? 0.252371  0.547895 0.452313 -0.0169204  0.00216122  -0.10414    568  GLN B N   
9582  C  CA  . GLN B 568 ? 0.271559  0.597671 0.487081 -0.00411521 -0.00467412 -0.11242    568  GLN B CA  
9583  C  C   . GLN B 568 ? 0.224438  0.543424 0.431108 0.0088827   -0.00289042 -0.106144   568  GLN B C   
9584  O  O   . GLN B 568 ? 0.235796  0.559023 0.438585 0.0259732   -0.0122704  -0.105726   568  GLN B O   
9585  C  CB  . GLN B 568 ? 0.311629  0.675685 0.556759 -0.0124114  -0.00073465 -0.12705    568  GLN B CB  
9586  C  CG  . GLN B 568 ? 0.418184  0.80161  0.6771   -0.017901   -0.00874827 -0.137912   568  GLN B CG  
9587  C  CD  . GLN B 568 ? 0.47465   0.862491 0.726239 0.00033693  -0.0253756  -0.13826    568  GLN B CD  
9588  O  OE1 . GLN B 568 ? 0.513976  0.916951 0.768594 0.0175493   -0.0323321  -0.140028   568  GLN B OE1 
9589  N  NE2 . GLN B 568 ? 0.496641  0.868111 0.735636 -0.00243593 -0.0313913  -0.135739   568  GLN B NE2 
9590  N  N   . PRO B 569 ? 0.223294  0.528704 0.423987 0.00203087  0.00899514  -0.100846   569  PRO B N   
9591  C  CA  . PRO B 569 ? 0.216374  0.512361 0.406577 0.0142296   0.0104016   -0.0952732  569  PRO B CA  
9592  C  C   . PRO B 569 ? 0.198461  0.46996  0.367328 0.0271883   0.00099902  -0.0862397  569  PRO B C   
9593  O  O   . PRO B 569 ? 0.212872  0.487395 0.378919 0.0428197   -0.00515582 -0.0863012  569  PRO B O   
9594  C  CB  . PRO B 569 ? 0.235401  0.515845 0.41833  0.00209248  0.0242676   -0.0903138  569  PRO B CB  
9595  C  CG  . PRO B 569 ? 0.234634  0.53058  0.43431  -0.0154627  0.0318644   -0.097711   569  PRO B CG  
9596  C  CD  . PRO B 569 ? 0.231538  0.526417 0.431739 -0.0166787  0.0214106   -0.0993536  569  PRO B CD  
9597  N  N   . LEU B 570 ? 0.191292  0.43821  0.344914 0.0210424   -0.00020371 -0.0787989  570  LEU B N   
9598  C  CA  . LEU B 570 ? 0.184512  0.409243 0.319098 0.0313924   -0.00752754 -0.0707847  570  LEU B CA  
9599  C  C   . LEU B 570 ? 0.199832  0.437676 0.337536 0.0441931   -0.0189738  -0.0748104  570  LEU B C   
9600  O  O   . LEU B 570 ? 0.209831  0.437825 0.335972 0.0581087   -0.0242896  -0.0708136  570  LEU B O   
9601  C  CB  . LEU B 570 ? 0.17411   0.374864 0.295003 0.0220441   -0.00656474 -0.0637791  570  LEU B CB  
9602  C  CG  . LEU B 570 ? 0.181064  0.358102 0.282567 0.0301675   -0.0119868  -0.0553921  570  LEU B CG  
9603  C  CD1 . LEU B 570 ? 0.163501  0.318055 0.253157 0.0204662   -0.00760905 -0.0486809  570  LEU B CD1 
9604  C  CD2 . LEU B 570 ? 0.185483  0.368183 0.286143 0.0367895   -0.0217599  -0.0574658  570  LEU B CD2 
9605  N  N   . LEU B 571 ? 0.192487  0.449619 0.343285 0.0393141   -0.0230914  -0.0824274  571  LEU B N   
9606  C  CA  . LEU B 571 ? 0.217508  0.488556 0.370113 0.0522859   -0.0350451  -0.0869353  571  LEU B CA  
9607  C  C   . LEU B 571 ? 0.222215  0.51192  0.383014 0.0677385   -0.03836    -0.091678   571  LEU B C   
9608  O  O   . LEU B 571 ? 0.212706  0.49792  0.362714 0.0842926   -0.047099   -0.089434   571  LEU B O   
9609  C  CB  . LEU B 571 ? 0.243886  0.5369   0.412582 0.042745    -0.0381793  -0.0968562  571  LEU B CB  
9610  C  CG  . LEU B 571 ? 0.291642  0.564132 0.448777 0.0317638   -0.0377763  -0.0924501  571  LEU B CG  
9611  C  CD1 . LEU B 571 ? 0.326057  0.619789 0.499556 0.0214917   -0.0404321  -0.103745   571  LEU B CD1 
9612  C  CD2 . LEU B 571 ? 0.275469  0.526542 0.410166 0.0435152   -0.0454453  -0.0841553  571  LEU B CD2 
9613  N  N   . LYS B 572 ? 0.223814  0.532635 0.402181 0.0627378   -0.0305416  -0.0978844  572  LYS B N   
9614  C  CA  . LYS B 572 ? 0.251985  0.583081 0.441504 0.0775299   -0.0333953  -0.104358   572  LYS B CA  
9615  C  C   . LYS B 572 ? 0.252436  0.557343 0.421944 0.0901074   -0.0322945  -0.0951764  572  LYS B C   
9616  O  O   . LYS B 572 ? 0.238826  0.546356 0.404005 0.108357    -0.0394886  -0.0959471  572  LYS B O   
9617  C  CB  . LYS B 572 ? 0.300041  0.65822  0.514154 0.0653227   -0.0231528  -0.113719   572  LYS B CB  
9618  C  CG  . LYS B 572 ? 0.407821  0.794171 0.637938 0.0789418   -0.0240772  -0.122302   572  LYS B CG  
9619  C  CD  . LYS B 572 ? 0.462902  0.866714 0.710886 0.0668588   -0.00993965 -0.128213   572  LYS B CD  
9620  C  CE  . LYS B 572 ? 0.459879  0.891762 0.723422 0.0819258   -0.0106081  -0.136947   572  LYS B CE  
9621  N  NZ  . LYS B 572 ? 0.531579  0.981536 0.812538 0.0690717   0.00432119  -0.143083   572  LYS B NZ  
9622  N  N   . TYR B 573 ? 0.241715  0.518515 0.396751 0.0807173   -0.0239123  -0.0862254  573  TYR B N   
9623  C  CA  . TYR B 573 ? 0.225146  0.474922 0.360547 0.0902227   -0.0227996  -0.078105   573  TYR B CA  
9624  C  C   . TYR B 573 ? 0.226998  0.459183 0.344569 0.103763    -0.0328817  -0.0725565  573  TYR B C   
9625  O  O   . TYR B 573 ? 0.225988  0.448978 0.333998 0.11885     -0.0356173  -0.0707658  573  TYR B O   
9626  C  CB  . TYR B 573 ? 0.208165  0.433284 0.331916 0.0763393   -0.0137694  -0.0705488  573  TYR B CB  
9627  C  CG  . TYR B 573 ? 0.212308  0.409629 0.316775 0.0831384   -0.0119285  -0.0633388  573  TYR B CG  
9628  C  CD1 . TYR B 573 ? 0.218532  0.390537 0.304182 0.0885262   -0.0173661  -0.0558791  573  TYR B CD1 
9629  C  CD2 . TYR B 573 ? 0.213385  0.409071 0.317947 0.0827541   -0.00401072 -0.0644054  573  TYR B CD2 
9630  C  CE1 . TYR B 573 ? 0.224865  0.371152 0.29391  0.0925327   -0.015074   -0.0502825  573  TYR B CE1 
9631  C  CE2 . TYR B 573 ? 0.225827  0.395996 0.312945 0.087964    -0.00258153 -0.059106   573  TYR B CE2 
9632  C  CZ  . TYR B 573 ? 0.244922  0.390622 0.315109 0.0922796   -0.00817725 -0.0523162  573  TYR B CZ  
9633  O  OH  . TYR B 573 ? 0.2616    0.381559 0.315307 0.0955254   -0.00654814 -0.0478378  573  TYR B OH  
9634  N  N   . PHE B 574 ? 0.214836  0.440092 0.326133 0.0984335   -0.0376113  -0.0696269  574  PHE B N   
9635  C  CA  . PHE B 574 ? 0.236241  0.439196 0.326456 0.108598    -0.0447164  -0.0625177  574  PHE B CA  
9636  C  C   . PHE B 574 ? 0.268333  0.489026 0.361128 0.122514    -0.0561882  -0.0677186  574  PHE B C   
9637  O  O   . PHE B 574 ? 0.262962  0.465087 0.336097 0.133605    -0.0621356  -0.0618033  574  PHE B O   
9638  C  CB  . PHE B 574 ? 0.244688  0.427456 0.323125 0.09637     -0.0432271  -0.0557523  574  PHE B CB  
9639  C  CG  . PHE B 574 ? 0.218396  0.375572 0.285735 0.0881773   -0.0348965  -0.0482697  574  PHE B CG  
9640  C  CD1 . PHE B 574 ? 0.236985  0.368749 0.286162 0.0960146   -0.0344332  -0.0414956  574  PHE B CD1 
9641  C  CD2 . PHE B 574 ? 0.207593  0.36567  0.281916 0.0728008   -0.02779    -0.048445   574  PHE B CD2 
9642  C  CE1 . PHE B 574 ? 0.245132  0.355824 0.285482 0.0880367   -0.0276526  -0.0361524  574  PHE B CE1 
9643  C  CE2 . PHE B 574 ? 0.221674  0.358617 0.285762 0.0668413   -0.0215314  -0.0424928  574  PHE B CE2 
9644  C  CZ  . PHE B 574 ? 0.228     0.343148 0.276458 0.0740986   -0.0217991  -0.0370238  574  PHE B CZ  
9645  N  N   . GLN B 575 ? 0.292671  0.549271 0.40918  0.122397    -0.0589021  -0.0790731  575  GLN B N   
9646  C  CA  . GLN B 575 ? 0.33211   0.613613 0.456128 0.13443     -0.0707175  -0.0869931  575  GLN B CA  
9647  C  C   . GLN B 575 ? 0.345005  0.609248 0.446451 0.156127    -0.0796662  -0.0812691  575  GLN B C   
9648  O  O   . GLN B 575 ? 0.345883  0.609453 0.437427 0.162377    -0.0886651  -0.08088    575  GLN B O   
9649  C  CB  . GLN B 575 ? 0.39404   0.716061 0.547708 0.134963    -0.0702409  -0.100279   575  GLN B CB  
9650  C  CG  . GLN B 575 ? 0.474354  0.830336 0.64202  0.145392    -0.0827539  -0.111619   575  GLN B CG  
9651  C  CD  . GLN B 575 ? 0.620179  1.01761  0.818601 0.147042    -0.0814023  -0.125296   575  GLN B CD  
9652  O  OE1 . GLN B 575 ? 0.703944  1.10411  0.904313 0.158882    -0.0789976  -0.125719   575  GLN B OE1 
9653  N  NE2 . GLN B 575 ? 0.621963  1.05216  0.84524  0.134565    -0.0821901  -0.137287   575  GLN B NE2 
9654  N  N   . LEU B 576 ? 0.361469  0.609447 0.452502 0.167885    -0.0770087  -0.076692   576  LEU B N   
9655  C  CA  . LEU B 576 ? 0.371722  0.601665 0.440368 0.189801    -0.0848827  -0.0715282  576  LEU B CA  
9656  C  C   . LEU B 576 ? 0.400733  0.592666 0.439793 0.188624    -0.0849337  -0.0594038  576  LEU B C   
9657  O  O   . LEU B 576 ? 0.410493  0.592936 0.431126 0.204581    -0.0936184  -0.0562982  576  LEU B O   
9658  C  CB  . LEU B 576 ? 0.412615  0.630021 0.475197 0.202592    -0.081319   -0.0695983  576  LEU B CB  
9659  C  CG  . LEU B 576 ? 0.421072  0.674701 0.507498 0.21362     -0.0838777  -0.081514   576  LEU B CG  
9660  C  CD1 . LEU B 576 ? 0.419057  0.648638 0.493461 0.222689    -0.0775324  -0.0770426  576  LEU B CD1 
9661  C  CD2 . LEU B 576 ? 0.428875  0.705445 0.517651 0.233601    -0.0982665  -0.0880466  576  LEU B CD2 
9662  N  N   . VAL B 577 ? 0.356896  0.525311 0.389593 0.17219     -0.0747303  -0.052325   577  VAL B N   
9663  C  CA  . VAL B 577 ? 0.350559  0.484644 0.358183 0.168369    -0.0726327  -0.0415591  577  VAL B CA  
9664  C  C   . VAL B 577 ? 0.326237  0.470843 0.336033 0.159998    -0.0769102  -0.0432571  577  VAL B C   
9665  O  O   . VAL B 577 ? 0.326543  0.451146 0.31527  0.163163    -0.0792424  -0.0366554  577  VAL B O   
9666  C  CB  . VAL B 577 ? 0.337005  0.442636 0.336    0.155611    -0.0615195  -0.0340571  577  VAL B CB  
9667  C  CG1 . VAL B 577 ? 0.300891  0.414383 0.313782 0.134372    -0.0552209  -0.0354294  577  VAL B CG1 
9668  C  CG2 . VAL B 577 ? 0.341562  0.40991  0.312019 0.15869     -0.0598062  -0.0234622  577  VAL B CG2 
9669  N  N   . THR B 578 ? 0.302471  0.476779 0.336737 0.148681    -0.0769692  -0.0522099  578  THR B N   
9670  C  CA  . THR B 578 ? 0.334467  0.518611 0.371471 0.140436    -0.0809453  -0.0552034  578  THR B CA  
9671  C  C   . THR B 578 ? 0.394266  0.58603  0.420739 0.158016    -0.0932735  -0.0575454  578  THR B C   
9672  O  O   . THR B 578 ? 0.427844  0.605727 0.43624  0.159299    -0.0966619  -0.0531522  578  THR B O   
9673  C  CB  . THR B 578 ? 0.319147  0.534859 0.385084 0.12701     -0.0790595  -0.0659418  578  THR B CB  
9674  O  OG1 . THR B 578 ? 0.316503  0.51781  0.38466  0.111519    -0.0677851  -0.0613304  578  THR B OG1 
9675  C  CG2 . THR B 578 ? 0.30684   0.535878 0.378135 0.118985    -0.0839882  -0.0716389  578  THR B CG2 
9676  N  N   . GLN B 579 ? 0.387504  0.602197 0.425227 0.17227     -0.0998155  -0.0648509  579  GLN B N   
9677  C  CA  . GLN B 579 ? 0.461682  0.690799 0.493291 0.191414    -0.113276   -0.0694806  579  GLN B CA  
9678  C  C   . GLN B 579 ? 0.453026  0.644108 0.448511 0.206081    -0.114958   -0.0569183  579  GLN B C   
9679  O  O   . GLN B 579 ? 0.513295  0.699033 0.491039 0.214079    -0.122679   -0.0551176  579  GLN B O   
9680  C  CB  . GLN B 579 ? 0.489528  0.752937 0.544578 0.202398    -0.118136   -0.0805896  579  GLN B CB  
9681  C  CG  . GLN B 579 ? 0.668104  0.949859 0.71842  0.225848    -0.133424   -0.0865306  579  GLN B CG  
9682  C  CD  . GLN B 579 ? 0.819172  1.12039  0.871865 0.223793    -0.143494   -0.0937034  579  GLN B CD  
9683  O  OE1 . GLN B 579 ? 0.818567  1.14424  0.895087 0.205918    -0.141627   -0.103015   579  GLN B OE1 
9684  N  NE2 . GLN B 579 ? 0.885611  1.17446  0.911765 0.242424    -0.154135   -0.0895434  579  GLN B NE2 
9685  N  N   . TRP B 580 ? 0.408001  0.571041 0.391602 0.207987    -0.106758   -0.0483137  580  TRP B N   
9686  C  CA  . TRP B 580 ? 0.434204  0.558012 0.383443 0.220862    -0.106303   -0.0363738  580  TRP B CA  
9687  C  C   . TRP B 580 ? 0.446157  0.545553 0.375711 0.21002     -0.102252   -0.0280891  580  TRP B C   
9688  O  O   . TRP B 580 ? 0.491924  0.575942 0.396398 0.221972    -0.107666   -0.0229531  580  TRP B O   
9689  C  CB  . TRP B 580 ? 0.446326  0.544782 0.388534 0.223054    -0.0974979  -0.0303066  580  TRP B CB  
9690  C  CG  . TRP B 580 ? 0.469074  0.526116 0.375947 0.237668    -0.0967356  -0.0189997  580  TRP B CG  
9691  C  CD1 . TRP B 580 ? 0.501408  0.551166 0.392212 0.262253    -0.104494   -0.0179211  580  TRP B CD1 
9692  C  CD2 . TRP B 580 ? 0.47686   0.492651 0.360174 0.228393    -0.0866453  -0.00742263 580  TRP B CD2 
9693  N  NE1 . TRP B 580 ? 0.52376   0.527631 0.380107 0.268542    -0.0996306  -0.00565481 580  TRP B NE1 
9694  C  CE2 . TRP B 580 ? 0.534961  0.518329 0.387292 0.247038    -0.0882341  0.00057186  580  TRP B CE2 
9695  C  CE3 . TRP B 580 ? 0.480343  0.484264 0.365657 0.206543    -0.0766489  -0.00347943 580  TRP B CE3 
9696  C  CZ2 . TRP B 580 ? 0.568871  0.508253 0.393501 0.242286    -0.0787923  0.0120512   580  TRP B CZ2 
9697  C  CZ3 . TRP B 580 ? 0.518256  0.482491 0.3785   0.202539    -0.0682069  0.0069906   580  TRP B CZ3 
9698  C  CH2 . TRP B 580 ? 0.564148  0.496276 0.395116 0.219113    -0.0685489  0.0144998   580  TRP B CH2 
9699  N  N   . LEU B 581 ? 0.396666  0.493828 0.337443 0.188261    -0.0928918  -0.0272636  581  LEU B N   
9700  C  CA  . LEU B 581 ? 0.409229  0.482105 0.33266  0.177647    -0.0871248  -0.0193407  581  LEU B CA  
9701  C  C   . LEU B 581 ? 0.440254  0.524318 0.356597 0.181472    -0.0957316  -0.0223473  581  LEU B C   
9702  O  O   . LEU B 581 ? 0.430689  0.490239 0.32126  0.183795    -0.0941703  -0.0144031  581  LEU B O   
9703  C  CB  . LEU B 581 ? 0.361763  0.436456 0.302007 0.155341    -0.0773974  -0.0200099  581  LEU B CB  
9704  C  CG  . LEU B 581 ? 0.36455   0.420484 0.305115 0.149221    -0.0675489  -0.0151759  581  LEU B CG  
9705  C  CD1 . LEU B 581 ? 0.313115  0.378895 0.273642 0.12982     -0.0605757  -0.0181933  581  LEU B CD1 
9706  C  CD2 . LEU B 581 ? 0.382474  0.401297 0.295157 0.150551    -0.0619631  -0.00436035 581  LEU B CD2 
9707  N  N   . GLN B 582 ? 0.451931  0.572663 0.391921 0.179991    -0.103435   -0.0342862  582  GLN B N   
9708  C  CA  . GLN B 582 ? 0.519796  0.657403 0.457104 0.184127    -0.113466   -0.0403973  582  GLN B CA  
9709  C  C   . GLN B 582 ? 0.578862  0.704184 0.487414 0.206651    -0.122701   -0.0359981  582  GLN B C   
9710  O  O   . GLN B 582 ? 0.571743  0.688812 0.461085 0.208962    -0.126219   -0.0338094  582  GLN B O   
9711  C  CB  . GLN B 582 ? 0.54862   0.729218 0.516492 0.183383    -0.1216     -0.0553297  582  GLN B CB  
9712  C  CG  . GLN B 582 ? 0.598663  0.794145 0.588978 0.161094    -0.116274   -0.0619295  582  GLN B CG  
9713  C  CD  . GLN B 582 ? 0.749934  0.986788 0.767744 0.159454    -0.124506   -0.0774912  582  GLN B CD  
9714  O  OE1 . GLN B 582 ? 0.825547  1.08479  0.865141 0.161256    -0.124796   -0.0842094  582  GLN B OE1 
9715  N  NE2 . GLN B 582 ? 0.766685  1.01451  0.783719 0.155945    -0.130987   -0.0840655  582  GLN B NE2 
9716  N  N   . GLU B 583 ? 0.593685  0.717779 0.498726 0.22376     -0.126545   -0.0350498  583  GLU B N   
9717  C  CA  . GLU B 583 ? 0.610517  0.719778 0.486456 0.247989    -0.135196   -0.0300266  583  GLU B CA  
9718  C  C   . GLU B 583 ? 0.605196  0.666736 0.444704 0.24817     -0.126172   -0.0146071  583  GLU B C   
9719  O  O   . GLU B 583 ? 0.6483    0.696571 0.460573 0.258292    -0.131115   -0.0101784  583  GLU B O   
9720  C  CB  . GLU B 583 ? 0.710685  0.82289  0.589667 0.265693    -0.138809   -0.0310893  583  GLU B CB  
9721  C  CG  . GLU B 583 ? 0.781147  0.941798 0.691595 0.273006    -0.150083   -0.0467012  583  GLU B CG  
9722  C  CD  . GLU B 583 ? 0.814383  0.981502 0.734886 0.286665    -0.150721   -0.0491238  583  GLU B CD  
9723  O  OE1 . GLU B 583 ? 0.807077  0.939903 0.709255 0.292487    -0.143309   -0.0389978  583  GLU B OE1 
9724  O  OE2 . GLU B 583 ? 0.840092  1.05011  0.789604 0.290675    -0.158669   -0.0628956  583  GLU B OE2 
9725  N  N   . GLN B 584 ? 0.574288  0.610755 0.412788 0.236912    -0.112926   -0.00704823 584  GLN B N   
9726  C  CA  . GLN B 584 ? 0.632132  0.624142 0.438023 0.235481    -0.103185   0.00661857  584  GLN B CA  
9727  C  C   . GLN B 584 ? 0.685121  0.670568 0.479045 0.224626    -0.100176   0.00945048  584  GLN B C   
9728  O  O   . GLN B 584 ? 0.661704  0.617178 0.422027 0.231421    -0.0975631  0.0189946   584  GLN B O   
9729  C  CB  . GLN B 584 ? 0.667795  0.639359 0.479952 0.220004    -0.0890537  0.011765    584  GLN B CB  
9730  C  CG  . GLN B 584 ? 0.723904  0.693151 0.542887 0.229356    -0.0889726  0.0106434   584  GLN B CG  
9731  C  CD  . GLN B 584 ? 0.810226  0.754906 0.59851  0.253596    -0.0941179  0.0170664   584  GLN B CD  
9732  O  OE1 . GLN B 584 ? 0.844724  0.747943 0.603309 0.255139    -0.0861046  0.0282321   584  GLN B OE1 
9733  N  NE2 . GLN B 584 ? 0.801177  0.771185 0.596214 0.272645    -0.107312   0.0097506   584  GLN B NE2 
9734  N  N   . ASN B 585 ? 0.575038  0.585591 0.395178 0.20699     -0.0989342  0.00165438  585  ASN B N   
9735  C  CA  . ASN B 585 ? 0.563365  0.565526 0.373051 0.195797    -0.0942764  0.00431606  585  ASN B CA  
9736  C  C   . ASN B 585 ? 0.597628  0.602141 0.384685 0.210445    -0.104649   0.00349585  585  ASN B C   
9737  O  O   . ASN B 585 ? 0.589903  0.568685 0.348836 0.210673    -0.099302   0.011824    585  ASN B O   
9738  C  CB  . ASN B 585 ? 0.477492  0.503851 0.317648 0.176045    -0.0914981  -0.00398705 585  ASN B CB  
9739  C  CG  . ASN B 585 ? 0.428914  0.445836 0.283397 0.161393    -0.0798699  -0.00087193 585  ASN B CG  
9740  O  OD1 . ASN B 585 ? 0.441393  0.428525 0.278885 0.160256    -0.0709204  0.00860148  585  ASN B OD1 
9741  N  ND2 . ASN B 585 ? 0.39227   0.432981 0.276325 0.148747    -0.0792461  -0.00886543 585  ASN B ND2 
9742  N  N   . GLN B 586 ? 0.585432  0.622326 0.386146 0.221352    -0.11883    -0.00731921 586  GLN B N   
9743  C  CA  . GLN B 586 ? 0.68835   0.732265 0.468783 0.239679    -0.132128   -0.0100502  586  GLN B CA  
9744  C  C   . GLN B 586 ? 0.719111  0.725369 0.456738 0.258325    -0.13145    0.00303424  586  GLN B C   
9745  O  O   . GLN B 586 ? 0.745233  0.737519 0.454233 0.264164    -0.133141   0.00727673  586  GLN B O   
9746  C  CB  . GLN B 586 ? 0.678099  0.763714 0.482612 0.250146    -0.147494   -0.0242753  586  GLN B CB  
9747  C  CG  . GLN B 586 ? 0.714352  0.833975 0.558326 0.229892    -0.146666   -0.0370016  586  GLN B CG  
9748  C  CD  . GLN B 586 ? 0.793709  0.957758 0.666241 0.23606     -0.159928   -0.0527713  586  GLN B CD  
9749  O  OE1 . GLN B 586 ? 0.784     0.96765  0.686113 0.23003     -0.157679   -0.0587028  586  GLN B OE1 
9750  N  NE2 . GLN B 586 ? 0.775304  0.957021 0.639736 0.247432    -0.173587   -0.060534   586  GLN B NE2 
9751  N  N   . GLN B 587 ? 0.727756  0.71541  0.458993 0.267519    -0.128268   0.00954992  587  GLN B N   
9752  C  CA  . GLN B 587 ? 0.841664  0.790055 0.530738 0.286011    -0.127189   0.0222283   587  GLN B CA  
9753  C  C   . GLN B 587 ? 0.827866  0.736143 0.489378 0.274186    -0.111735   0.0349784   587  GLN B C   
9754  O  O   . GLN B 587 ? 0.861079  0.739236 0.482936 0.287097    -0.111119   0.0446385   587  GLN B O   
9755  C  CB  . GLN B 587 ? 0.928259  0.85999  0.615749 0.296231    -0.124714   0.0267991   587  GLN B CB  
9756  C  CG  . GLN B 587 ? 1.07982   1.03147  0.766813 0.322683    -0.141498   0.0204608   587  GLN B CG  
9757  C  CD  . GLN B 587 ? 1.18317   1.15127  0.89887  0.324584    -0.142043   0.0143844   587  GLN B CD  
9758  O  OE1 . GLN B 587 ? 1.27782   1.2156   0.980197 0.3306      -0.135105   0.022343    587  GLN B OE1 
9759  N  NE2 . GLN B 587 ? 1.16072   1.17677  0.91572  0.319132    -0.149795   -0.00033038 587  GLN B NE2 
9760  N  N   . ASN B 588 ? 0.757475  0.664664 0.439041 0.250203    -0.0988194  0.0351214   588  ASN B N   
9761  C  CA  . ASN B 588 ? 0.763365  0.638506 0.422758 0.237969    -0.0842763  0.0451983   588  ASN B CA  
9762  C  C   . ASN B 588 ? 0.726051  0.618149 0.386769 0.230013    -0.0863333  0.0401428   588  ASN B C   
9763  O  O   . ASN B 588 ? 0.750562  0.624076 0.399475 0.217382    -0.0741188  0.0459878   588  ASN B O   
9764  C  CB  . ASN B 588 ? 0.74369   0.606115 0.419532 0.21769     -0.0691024  0.0483628   588  ASN B CB  
9765  C  CG  . ASN B 588 ? 0.796255  0.642516 0.47157  0.225014    -0.0672543  0.0519004   588  ASN B CG  
9766  O  OD1 . ASN B 588 ? 0.839266  0.661023 0.48524  0.243708    -0.0701413  0.0588358   588  ASN B OD1 
9767  N  ND2 . ASN B 588 ? 0.803277  0.662835 0.509545 0.211939    -0.0631462  0.0468302   588  ASN B ND2 
9768  N  N   . GLY B 589 ? 0.670883  0.599115 0.347769 0.236825    -0.101314   0.0283476   589  GLY B N   
9769  C  CA  . GLY B 589 ? 0.682629  0.63169  0.365289 0.229654    -0.105421   0.0205294   589  GLY B CA  
9770  C  C   . GLY B 589 ? 0.664503  0.616579 0.368396 0.20491     -0.0929846  0.0189469   589  GLY B C   
9771  O  O   . GLY B 589 ? 0.678362  0.622417 0.369242 0.198048    -0.0873876  0.0206787   589  GLY B O   
9772  N  N   . GLU B 590 ? 0.593327  0.557948 0.32957  0.192391    -0.0889962  0.0151416   590  GLU B N   
9773  C  CA  . GLU B 590 ? 0.565944  0.531626 0.320548 0.170901    -0.0776448  0.014281    590  GLU B CA  
9774  C  C   . GLU B 590 ? 0.547184  0.53938  0.318137 0.162966    -0.0830551  0.00341628  590  GLU B C   
9775  O  O   . GLU B 590 ? 0.557203  0.574478 0.337293 0.170417    -0.0959465  -0.00619944 590  GLU B O   
9776  C  CB  . GLU B 590 ? 0.514741  0.48817  0.298741 0.160087    -0.0729434  0.0122833   590  GLU B CB  
9777  C  CG  . GLU B 590 ? 0.532967  0.481654 0.304194 0.167271    -0.0680614  0.0211317   590  GLU B CG  
9778  C  CD  . GLU B 590 ? 0.575573  0.489474 0.325279 0.160179    -0.0536685  0.0321721   590  GLU B CD  
9779  O  OE1 . GLU B 590 ? 0.550768  0.460178 0.29426  0.150659    -0.0471393  0.0334683   590  GLU B OE1 
9780  O  OE2 . GLU B 590 ? 0.609526  0.500578 0.348702 0.164338    -0.0486386  0.0389779   590  GLU B OE2 
9781  N  N   . VAL B 591 ? 0.521744  0.507373 0.295784 0.147925    -0.072737   0.00468104  591  VAL B N   
9782  C  CA  . VAL B 591 ? 0.509231  0.516781 0.303777 0.136698    -0.0748707  -0.00544185 591  VAL B CA  
9783  C  C   . VAL B 591 ? 0.46411   0.482823 0.290691 0.123314    -0.0705883  -0.00868508 591  VAL B C   
9784  O  O   . VAL B 591 ? 0.482186  0.485611 0.310987 0.115822    -0.0601633  -0.00187043 591  VAL B O   
9785  C  CB  . VAL B 591 ? 0.553677  0.548775 0.331752 0.130646    -0.0671396  -0.00309819 591  VAL B CB  
9786  C  CG1 . VAL B 591 ? 0.515275  0.525981 0.316465 0.116032    -0.0649318  -0.0115767  591  VAL B CG1 
9787  C  CG2 . VAL B 591 ? 0.58554   0.576112 0.333628 0.144484    -0.0741395  -0.00303103 591  VAL B CG2 
9788  N  N   . LEU B 592 ? 0.421258  0.466694 0.271751 0.121367    -0.0790657  -0.0192646  592  LEU B N   
9789  C  CA  . LEU B 592 ? 0.407732  0.46479  0.287149 0.108462    -0.0752638  -0.0232562  592  LEU B CA  
9790  C  C   . LEU B 592 ? 0.3849    0.441009 0.271123 0.0946729   -0.0689283  -0.0257795  592  LEU B C   
9791  O  O   . LEU B 592 ? 0.394485  0.456873 0.275677 0.0946361   -0.0729423  -0.0315608  592  LEU B O   
9792  C  CB  . LEU B 592 ? 0.402305  0.48731  0.304391 0.109965    -0.0847115  -0.0337229  592  LEU B CB  
9793  C  CG  . LEU B 592 ? 0.440853  0.530534 0.337545 0.125852    -0.0923611  -0.0328333  592  LEU B CG  
9794  C  CD1 . LEU B 592 ? 0.450379  0.571439 0.37447  0.125124    -0.0999974  -0.0444015  592  LEU B CD1 
9795  C  CD2 . LEU B 592 ? 0.413908  0.480809 0.303474 0.126624    -0.0834252  -0.021985   592  LEU B CD2 
9796  N  N   . GLY B 593 ? 0.341159  0.38911  0.237582 0.0841291   -0.0595186  -0.0218457  593  GLY B N   
9797  C  CA  . GLY B 593 ? 0.335432  0.381294 0.236953 0.0731243   -0.0535977  -0.0238084  593  GLY B CA  
9798  C  C   . GLY B 593 ? 0.328622  0.354609 0.210163 0.0733124   -0.0451952  -0.0161547  593  GLY B C   
9799  O  O   . GLY B 593 ? 0.335843  0.346889 0.200281 0.0798211   -0.0423038  -0.00838424 593  GLY B O   
9800  N  N   . TRP B 594 ? 0.304484  0.329767 0.188865 0.0656623   -0.0403848  -0.0185871  594  TRP B N   
9801  C  CA  . TRP B 594 ? 0.297118  0.307275 0.168241 0.0632523   -0.0305778  -0.0127396  594  TRP B CA  
9802  C  C   . TRP B 594 ? 0.309423  0.322396 0.173895 0.0622919   -0.0305736  -0.0181639  594  TRP B C   
9803  O  O   . TRP B 594 ? 0.305964  0.319676 0.179576 0.0548434   -0.024993   -0.0204069  594  TRP B O   
9804  C  CB  . TRP B 594 ? 0.28221   0.288635 0.168098 0.0540273   -0.0223614  -0.00960075 594  TRP B CB  
9805  C  CG  . TRP B 594 ? 0.254879  0.273919 0.164027 0.0473162   -0.0251504  -0.0153859  594  TRP B CG  
9806  C  CD1 . TRP B 594 ? 0.244076  0.267746 0.162489 0.0412956   -0.0235583  -0.0203431  594  TRP B CD1 
9807  C  CD2 . TRP B 594 ? 0.245358  0.272574 0.168954 0.0467477   -0.0296911  -0.0168826  594  TRP B CD2 
9808  N  NE1 . TRP B 594 ? 0.231398  0.26322  0.167497 0.0366164   -0.0263742  -0.0239998  594  TRP B NE1 
9809  C  CE2 . TRP B 594 ? 0.227348  0.262571 0.167444 0.039324    -0.0298677  -0.0222058  594  TRP B CE2 
9810  C  CE3 . TRP B 594 ? 0.256504  0.284211 0.179934 0.0522197   -0.0330155  -0.014277   594  TRP B CE3 
9811  C  CZ2 . TRP B 594 ? 0.206929  0.250355 0.162648 0.0360885   -0.0322625  -0.0245542  594  TRP B CZ2 
9812  C  CZ3 . TRP B 594 ? 0.239583  0.277656 0.180353 0.0494053   -0.0356738  -0.0173499  594  TRP B CZ3 
9813  C  CH2 . TRP B 594 ? 0.220359  0.266564 0.176734 0.0410536   -0.0351492  -0.0224652  594  TRP B CH2 
9814  N  N   . PRO B 595 ? 0.321125  0.334869 0.167835 0.0709651   -0.0368365  -0.0203484  595  PRO B N   
9815  C  CA  . PRO B 595 ? 0.332414  0.348628 0.169889 0.0713963   -0.0378424  -0.0265273  595  PRO B CA  
9816  C  C   . PRO B 595 ? 0.354932  0.359333 0.182219 0.0676204   -0.0259352  -0.0226068  595  PRO B C   
9817  O  O   . PRO B 595 ? 0.346384  0.354255 0.174296 0.064896    -0.0246146  -0.0288326  595  PRO B O   
9818  C  CB  . PRO B 595 ? 0.34884   0.367213 0.166692 0.083125    -0.0473452  -0.0284227  595  PRO B CB  
9819  C  CG  . PRO B 595 ? 0.362183  0.370216 0.169899 0.0902643   -0.0467761  -0.0188501  595  PRO B CG  
9820  C  CD  . PRO B 595 ? 0.324157  0.336764 0.157767 0.0822259   -0.0442225  -0.0176151  595  PRO B CD  
9821  N  N   . GLU B 596 ? 0.349802  0.340839 0.169492 0.0667979   -0.0168003  -0.0131109  596  GLU B N   
9822  C  CA  . GLU B 596 ? 0.366982  0.34925  0.180352 0.061806    -0.00414671 -0.00980345 596  GLU B CA  
9823  C  C   . GLU B 596 ? 0.33347   0.322172 0.172222 0.0518275   0.00113838  -0.011588   596  GLU B C   
9824  O  O   . GLU B 596 ? 0.325887  0.308625 0.169307 0.0468614   0.0092794   -0.00614129 596  GLU B O   
9825  C  CB  . GLU B 596 ? 0.404057  0.367766 0.193575 0.0649259   0.00452745  0.00010696  596  GLU B CB  
9826  C  CG  . GLU B 596 ? 0.458116  0.413643 0.217972 0.0763905   -0.00032912 0.0020203   596  GLU B CG  
9827  C  CD  . GLU B 596 ? 0.522316  0.455107 0.252292 0.0799147   0.00995215  0.0123313   596  GLU B CD  
9828  O  OE1 . GLU B 596 ? 0.520328  0.443821 0.253281 0.0714551   0.0229434   0.0175019   596  GLU B OE1 
9829  O  OE2 . GLU B 596 ? 0.56332   0.486859 0.265845 0.0913158   0.0050291   0.0152179   596  GLU B OE2 
9830  N  N   . TYR B 597 ? 0.307045  0.307265 0.161124 0.0490865   -0.00357191 -0.0198152  597  TYR B N   
9831  C  CA  . TYR B 597 ? 0.290776  0.297487 0.168592 0.0423068   -0.00305812 -0.021648   597  TYR B CA  
9832  C  C   . TYR B 597 ? 0.293387  0.298952 0.176219 0.0374119   0.00750738  -0.0207867  597  TYR B C   
9833  O  O   . TYR B 597 ? 0.297854  0.307836 0.198352 0.032591    0.00902989  -0.0212706  597  TYR B O   
9834  C  CB  . TYR B 597 ? 0.267605  0.28364  0.159346 0.0404819   -0.0104346  -0.0300847  597  TYR B CB  
9835  C  CG  . TYR B 597 ? 0.263739  0.280221 0.147055 0.0421928   -0.00998187 -0.0366401  597  TYR B CG  
9836  C  CD1 . TYR B 597 ? 0.257811  0.273905 0.146276 0.0395737   -0.00312406 -0.0388674  597  TYR B CD1 
9837  C  CD2 . TYR B 597 ? 0.277272  0.295176 0.146652 0.0474421   -0.0168038  -0.041139   597  TYR B CD2 
9838  C  CE1 . TYR B 597 ? 0.266144  0.281689 0.145315 0.0420689   -0.00205105 -0.0451186  597  TYR B CE1 
9839  C  CE2 . TYR B 597 ? 0.292533  0.309797 0.151872 0.0493781   -0.016176   -0.0476135  597  TYR B CE2 
9840  C  CZ  . TYR B 597 ? 0.283432  0.298734 0.147359 0.0466359   -0.00826798 -0.0493577  597  TYR B CZ  
9841  O  OH  . TYR B 597 ? 0.294191  0.308367 0.147153 0.0493768   -0.00752585 -0.0562755  597  TYR B OH  
9842  N  N   . GLN B 598 ? 0.331664  0.333021 0.199409 0.0391531   0.0142506   -0.0205726  598  GLN B N   
9843  C  CA  . GLN B 598 ? 0.35548   0.358997 0.228874 0.0348622   0.0248676   -0.0212175  598  GLN B CA  
9844  C  C   . GLN B 598 ? 0.359904  0.356432 0.229787 0.0306375   0.0345589   -0.0137685  598  GLN B C   
9845  O  O   . GLN B 598 ? 0.36085   0.36172  0.239851 0.0253687   0.0437426   -0.0144461  598  GLN B O   
9846  C  CB  . GLN B 598 ? 0.390341  0.393404 0.248768 0.0389014   0.0272903   -0.0257706  598  GLN B CB  
9847  C  CG  . GLN B 598 ? 0.455089  0.46617  0.324964 0.0371066   0.0327877   -0.0320311  598  GLN B CG  
9848  C  CD  . GLN B 598 ? 0.455195  0.464554 0.307824 0.0406691   0.0390027   -0.0353259  598  GLN B CD  
9849  O  OE1 . GLN B 598 ? 0.445185  0.452292 0.285038 0.0457137   0.0330083   -0.0398307  598  GLN B OE1 
9850  N  NE2 . GLN B 598 ? 0.494696  0.50627  0.347455 0.0376635   0.0515564   -0.03403    598  GLN B NE2 
9851  N  N   . TRP B 599 ? 0.356288  0.342577 0.215222 0.0326062   0.0322916   -0.00732395 599  TRP B N   
9852  C  CA  . TRP B 599 ? 0.375711  0.350283 0.226184 0.0287618   0.0421792   -4.836e-05  599  TRP B CA  
9853  C  C   . TRP B 599 ? 0.354301  0.334142 0.226796 0.0206368   0.0456389   -9.905e-05  599  TRP B C   
9854  O  O   . TRP B 599 ? 0.34394   0.329469 0.231303 0.0204795   0.0377333   -0.00158629 599  TRP B O   
9855  C  CB  . TRP B 599 ? 0.395527  0.355074 0.225117 0.0352725   0.0381579   0.00671372  599  TRP B CB  
9856  C  CG  . TRP B 599 ? 0.429274  0.371734 0.246473 0.0314021   0.0491834   0.0146665   599  TRP B CG  
9857  C  CD1 . TRP B 599 ? 0.441873  0.370122 0.236323 0.0308868   0.0604673   0.0195555   599  TRP B CD1 
9858  C  CD2 . TRP B 599 ? 0.406189  0.342972 0.233535 0.026197    0.0511425   0.0180735   599  TRP B CD2 
9859  N  NE1 . TRP B 599 ? 0.454646  0.367584 0.244738 0.024985    0.0696405   0.0259527   599  TRP B NE1 
9860  C  CE2 . TRP B 599 ? 0.441909  0.359802 0.25195  0.0221485   0.0638577   0.0248062   599  TRP B CE2 
9861  C  CE3 . TRP B 599 ? 0.399894  0.344438 0.247414 0.0245565   0.0439023   0.0159499   599  TRP B CE3 
9862  C  CZ2 . TRP B 599 ? 0.464547  0.370928 0.278063 0.0161144   0.0690199   0.0287317   599  TRP B CZ2 
9863  C  CZ3 . TRP B 599 ? 0.411847  0.346544 0.262668 0.0194871   0.0484672   0.0196988   599  TRP B CZ3 
9864  C  CH2 . TRP B 599 ? 0.451186  0.366674 0.285425 0.0152594   0.0605764   0.0257591   599  TRP B CH2 
9865  N  N   . HIS B 600 ? 0.37336   0.352375 0.248132 0.0134517   0.0579666   0.00080026  600  HIS B N   
9866  C  CA  . HIS B 600 ? 0.352005  0.333752 0.243735 0.00507048  0.0625551   0.00102752  600  HIS B CA  
9867  C  C   . HIS B 600 ? 0.362922  0.327519 0.239595 -0.00036634 0.0743652   0.00755021  600  HIS B C   
9868  O  O   . HIS B 600 ? 0.3664    0.322105 0.224317 -2.106e-05  0.0830213   0.010348    600  HIS B O   
9869  C  CB  . HIS B 600 ? 0.348454  0.348993 0.261764 0.00012749  0.0666846   -0.00632226 600  HIS B CB  
9870  C  CG  . HIS B 600 ? 0.357909  0.371035 0.285122 0.00528312  0.0554578   -0.0119342  600  HIS B CG  
9871  N  ND1 . HIS B 600 ? 0.377238  0.393018 0.297765 0.0116709   0.0513949   -0.0153264  600  HIS B ND1 
9872  C  CD2 . HIS B 600 ? 0.335574  0.356722 0.280337 0.00497719  0.0479566   -0.0145389  600  HIS B CD2 
9873  C  CE1 . HIS B 600 ? 0.355764  0.379124 0.289239 0.0144748   0.0421849   -0.0195023  600  HIS B CE1 
9874  N  NE2 . HIS B 600 ? 0.356043  0.382743 0.303775 0.0107561   0.0401969   -0.0187131  600  HIS B NE2 
9875  N  N   . PRO B 601 ? 0.353172  0.310991 0.23617  -0.00592628 0.075985    0.0100109   601  PRO B N   
9876  C  CA  . PRO B 601 ? 0.377523  0.316476 0.246679 -0.0127442  0.0885351   0.015703    601  PRO B CA  
9877  C  C   . PRO B 601 ? 0.38088   0.329212 0.259641 -0.0234261  0.102525    0.0116231   601  PRO B C   
9878  O  O   . PRO B 601 ? 0.359003  0.32992  0.260773 -0.0260427  0.100957    0.00386949  601  PRO B O   
9879  C  CB  . PRO B 601 ? 0.361188  0.295932 0.241658 -0.0164423  0.0847516   0.016151    601  PRO B CB  
9880  C  CG  . PRO B 601 ? 0.337214  0.296031 0.244844 -0.01617    0.0750023   0.00843118  601  PRO B CG  
9881  C  CD  . PRO B 601 ? 0.326994  0.294177 0.23042  -0.00671228 0.0668867   0.00686667  601  PRO B CD  
9882  N  N   . PRO B 602 ? 0.43197   0.363154 0.293488 -0.0299435  0.117156    0.0165271   602  PRO B N   
9883  C  CA  . PRO B 602 ? 0.449065  0.391231 0.323131 -0.0422387  0.131932    0.0116526   602  PRO B CA  
9884  C  C   . PRO B 602 ? 0.439092  0.387708 0.33621  -0.053597   0.134188    0.00725991  602  PRO B C   
9885  O  O   . PRO B 602 ? 0.434997  0.374436 0.332521 -0.0514182  0.125847    0.00958654  602  PRO B O   
9886  C  CB  . PRO B 602 ? 0.492769  0.408274 0.334355 -0.043917   0.145744    0.0202635   602  PRO B CB  
9887  C  CG  . PRO B 602 ? 0.509009  0.396715 0.330005 -0.0385181  0.140247    0.0291092   602  PRO B CG  
9888  C  CD  . PRO B 602 ? 0.471011  0.371154 0.300298 -0.0256502  0.120322    0.0268027   602  PRO B CD  
9889  N  N   . LEU B 603 ? 0.448881  0.415895 0.366798 -0.0651218  0.144494    -0.0003181  603  LEU B N   
9890  C  CA  . LEU B 603 ? 0.469177  0.442901 0.408233 -0.0779411  0.148769    -0.00580252 603  LEU B CA  
9891  C  C   . LEU B 603 ? 0.514036  0.45723  0.43352  -0.0880679  0.162268    0.00104673  603  LEU B C   
9892  O  O   . LEU B 603 ? 0.548436  0.473792 0.444776 -0.0901563  0.175008    0.00723435  603  LEU B O   
9893  C  CB  . LEU B 603 ? 0.477255  0.482167 0.444666 -0.0871198  0.156387    -0.0170558  603  LEU B CB  
9894  C  CG  . LEU B 603 ? 0.479699  0.514799 0.468701 -0.0773823  0.143544    -0.0249447  603  LEU B CG  
9895  C  CD1 . LEU B 603 ? 0.501417  0.564679 0.51153  -0.083392   0.153106    -0.034766   603  LEU B CD1 
9896  C  CD2 . LEU B 603 ? 0.472104  0.516317 0.478704 -0.0743     0.128411    -0.0286857  603  LEU B CD2 
9897  N  N   . PRO B 604 ? 0.518635  0.453229 0.445421 -0.0951423  0.161041    -5.794e-05  604  PRO B N   
9898  C  CA  . PRO B 604 ? 0.563681  0.469099 0.474501 -0.107273   0.17601     0.00475328  604  PRO B CA  
9899  C  C   . PRO B 604 ? 0.610357  0.526189 0.53202  -0.124031   0.195134    -0.00105482 604  PRO B C   
9900  O  O   . PRO B 604 ? 0.545284  0.495801 0.493917 -0.127039   0.194977    -0.0111465  604  PRO B O   
9901  C  CB  . PRO B 604 ? 0.553272  0.454551 0.476214 -0.111297   0.16887     0.00140583  604  PRO B CB  
9902  C  CG  . PRO B 604 ? 0.507934  0.429955 0.444946 -0.0975959  0.148704    -0.00170802 604  PRO B CG  
9903  C  CD  . PRO B 604 ? 0.49315   0.443211 0.441512 -0.091755   0.145849    -0.00591096 604  PRO B CD  
9904  N  N   . ASP B 605 ? 0.732386  0.617211 0.631728 -0.134483   0.212303    0.00547807  605  ASP B N   
9905  C  CA  . ASP B 605 ? 0.883963  0.775701 0.789418 -0.150842   0.233018    0.00117989  605  ASP B CA  
9906  C  C   . ASP B 605 ? 0.839126  0.762841 0.785229 -0.166349   0.235335    -0.0138287  605  ASP B C   
9907  O  O   . ASP B 605 ? 0.82193   0.738783 0.776752 -0.172522   0.231185    -0.0169233  605  ASP B O   
9908  C  CB  . ASP B 605 ? 1.01225   0.860741 0.880507 -0.157608   0.251634    0.0127462   605  ASP B CB  
9909  C  CG  . ASP B 605 ? 1.1171    0.950428 0.952034 -0.144809   0.254472    0.0232366   605  ASP B CG  
9910  O  OD1 . ASP B 605 ? 1.15704   1.01619  1.00196  -0.144258   0.258574    0.0182613   605  ASP B OD1 
9911  O  OD2 . ASP B 605 ? 1.18229   0.978413 0.980962 -0.134708   0.252298    0.0358009   605  ASP B OD2 
9912  N  N   . ASN B 606 ? 0.797439  0.757198 0.767844 -0.170858   0.240756    -0.0236247  606  ASN B N   
9913  C  CA  . ASN B 606 ? 0.841112  0.839912 0.853213 -0.182788   0.241352    -0.039701   606  ASN B CA  
9914  C  C   . ASN B 606 ? 0.845477  0.85689  0.876248 -0.176062   0.220814    -0.0451799  606  ASN B C   
9915  O  O   . ASN B 606 ? 0.858442  0.865923 0.900182 -0.187978   0.222175    -0.0504824  606  ASN B O   
9916  C  CB  . ASN B 606 ? 0.889051  0.880765 0.909291 -0.207      0.261221    -0.045135   606  ASN B CB  
9917  C  CG  . ASN B 606 ? 0.883741  0.864675 0.889384 -0.218702   0.285521    -0.0416829  606  ASN B CG  
9918  O  OD1 . ASN B 606 ? 0.860789  0.865528 0.873256 -0.21456    0.289731    -0.0447668  606  ASN B OD1 
9919  N  ND2 . ASN B 606 ? 0.940116  0.883956 0.924706 -0.23355    0.302502    -0.035454   606  ASN B ND2 
9920  N  N   . TYR B 607 ? 0.818845  0.843519 0.851364 -0.157294   0.202515    -0.0438623  607  TYR B N   
9921  C  CA  . TYR B 607 ? 0.726992  0.768215 0.778315 -0.149837   0.183411    -0.049704   607  TYR B CA  
9922  C  C   . TYR B 607 ? 0.667166  0.754502 0.754969 -0.150691   0.179197    -0.0643022  607  TYR B C   
9923  O  O   . TYR B 607 ? 0.696792  0.802502 0.789574 -0.145512   0.182203    -0.0664632  607  TYR B O   
9924  C  CB  . TYR B 607 ? 0.719286  0.74403  0.748946 -0.130512   0.168004    -0.0392559  607  TYR B CB  
9925  C  CG  . TYR B 607 ? 0.627449  0.667485 0.672434 -0.120528   0.148258    -0.0435984  607  TYR B CG  
9926  C  CD1 . TYR B 607 ? 0.59545   0.619457 0.636824 -0.121833   0.141641    -0.0421152  607  TYR B CD1 
9927  C  CD2 . TYR B 607 ? 0.525561  0.594729 0.587305 -0.109764   0.137193    -0.0492884  607  TYR B CD2 
9928  C  CE1 . TYR B 607 ? 0.57295   0.610452 0.626691 -0.113111   0.12489     -0.0459929  607  TYR B CE1 
9929  C  CE2 . TYR B 607 ? 0.533618  0.614568 0.607003 -0.101118   0.120616    -0.0527221  607  TYR B CE2 
9930  C  CZ  . TYR B 607 ? 0.534424  0.599757 0.603349 -0.102913   0.114674    -0.0508406  607  TYR B CZ  
9931  O  OH  . TYR B 607 ? 0.514282  0.590408 0.592343 -0.0940687  0.099228    -0.0537325  607  TYR B OH  
9932  N  N   . PRO B 608 ? 0.640645  0.748758 0.754437 -0.15577    0.171366    -0.0752551  608  PRO B N   
9933  C  CA  . PRO B 608 ? 0.67191   0.759593 0.780465 -0.160996   0.16672     -0.0740036  608  PRO B CA  
9934  C  C   . PRO B 608 ? 0.704037  0.790239 0.825241 -0.18239    0.17907     -0.0824406  608  PRO B C   
9935  O  O   . PRO B 608 ? 0.733424  0.843198 0.879755 -0.186885   0.171472    -0.0945528  608  PRO B O   
9936  C  CB  . PRO B 608 ? 0.63445   0.751046 0.763556 -0.148527   0.146744    -0.0814911  608  PRO B CB  
9937  C  CG  . PRO B 608 ? 0.609578  0.768472 0.770256 -0.153033   0.150076    -0.0953983  608  PRO B CG  
9938  C  CD  . PRO B 608 ? 0.617605  0.770768 0.76605  -0.154097   0.164748    -0.0897287  608  PRO B CD  
9939  N  N   . GLU B 609 ? 0.823208  0.880131 0.925593 -0.19546    0.197788    -0.0761904  609  GLU B N   
9940  C  CA  . GLU B 609 ? 0.867079  0.919836 0.980598 -0.2181     0.212097    -0.0844578  609  GLU B CA  
9941  C  C   . GLU B 609 ? 0.831586  0.831418 0.909843 -0.224884   0.224264    -0.0717439  609  GLU B C   
9942  O  O   . GLU B 609 ? 0.831249  0.807959 0.896493 -0.218928   0.214105    -0.0672237  609  GLU B O   
9943  C  CB  . GLU B 609 ? 0.904313  0.98426  1.03891  -0.232833   0.229197    -0.0940513  609  GLU B CB  
9944  C  CG  . GLU B 609 ? 0.895314  1.02411  1.05845  -0.222268   0.219289    -0.103934   609  GLU B CG  
9945  C  CD  . GLU B 609 ? 0.96045   1.09943  1.12308  -0.226198   0.236109    -0.103317   609  GLU B CD  
9946  O  OE1 . GLU B 609 ? 1.04724   1.19497  1.2234   -0.246424   0.255173    -0.111182   609  GLU B OE1 
9947  O  OE2 . GLU B 609 ? 0.965431  1.10233  1.11295  -0.209431   0.230842    -0.0950241  609  GLU B OE2 
9948  C  C1  . NAG C .   ? 0.652979  0.890589 0.748411 0.297711    -0.0457975  -0.10807    1    NAG C C1  
9949  C  C2  . NAG C .   ? 0.671048  0.939376 0.790846 0.289893    -0.0349306  -0.118373   1    NAG C C2  
9950  C  C3  . NAG C .   ? 0.65949   0.974017 0.810292 0.274668    -0.0345147  -0.12567    1    NAG C C3  
9951  C  C4  . NAG C .   ? 0.683279  1.0319   0.849783 0.292815    -0.0475077  -0.133547   1    NAG C C4  
9952  C  C5  . NAG C .   ? 0.66205   0.979384 0.802076 0.303205    -0.0596413  -0.123297   1    NAG C C5  
9953  C  C6  . NAG C .   ? 0.71049   1.05499  0.858812 0.327506    -0.0742282  -0.13042    1    NAG C C6  
9954  C  C7  . NAG C .   ? 0.790737  0.99057  0.873648 0.274077    -0.0190739  -0.107083   1    NAG C C7  
9955  C  C8  . NAG C .   ? 0.721389  0.89989  0.794987 0.248996    -0.0115714  -0.0997074  1    NAG C C8  
9956  N  N2  . NAG C .   ? 0.736443  0.981857 0.846865 0.274147    -0.022438   -0.114915   1    NAG C N2  
9957  O  O3  . NAG C .   ? 0.650668  0.990681 0.822199 0.262672    -0.0221251  -0.133678   1    NAG C O3  
9958  O  O4  . NAG C .   ? 0.704985  1.09922  0.902899 0.278007    -0.0469381  -0.142479   1    NAG C O4  
9959  O  O5  . NAG C .   ? 0.656792  0.923817 0.763933 0.313873    -0.0582037  -0.113582   1    NAG C O5  
9960  O  O6  . NAG C .   ? 0.709918  1.05363  0.851977 0.324334    -0.0843323  -0.126011   1    NAG C O6  
9961  O  O7  . NAG C .   ? 0.836698  1.01377  0.903158 0.293759    -0.0220038  -0.106631   1    NAG C O7  
9962  C  C1  . NAG C .   ? 0.736162  1.17984  0.966118 0.284804    -0.0455043  -0.15757    2    NAG C C1  
9963  C  C2  . NAG C .   ? 0.747149  1.23271  1.00685  0.266531    -0.0457216  -0.165814   2    NAG C C2  
9964  C  C3  . NAG C .   ? 0.753712  1.29391  1.05094  0.268264    -0.0401777  -0.182874   2    NAG C C3  
9965  C  C4  . NAG C .   ? 0.77582   1.31065  1.07389  0.262938    -0.0238421  -0.184012   2    NAG C C4  
9966  C  C5  . NAG C .   ? 0.819202  1.31064  1.08573  0.282597    -0.0254884  -0.175529   2    NAG C C5  
9967  C  C6  . NAG C .   ? 0.820422  1.29891  1.08176  0.276085    -0.00964123 -0.175299   2    NAG C C6  
9968  C  C7  . NAG C .   ? 0.796214  1.27009  1.04122  0.262011    -0.0659783  -0.157458   2    NAG C C7  
9969  C  C8  . NAG C .   ? 0.815175  1.31155  1.06637  0.273313    -0.0822294  -0.16272    2    NAG C C8  
9970  N  N2  . NAG C .   ? 0.801352  1.29441  1.05959  0.274457    -0.0612988  -0.165813   2    NAG C N2  
9971  O  O3  . NAG C .   ? 0.711425  1.28782  1.03636  0.247548    -0.0378763  -0.190876   2    NAG C O3  
9972  O  O4  . NAG C .   ? 0.720736  1.30849  1.0538   0.268278    -0.0196588  -0.200682   2    NAG C O4  
9973  O  O5  . NAG C .   ? 0.764687  1.20648  0.998073 0.279035    -0.031062   -0.160079   2    NAG C O5  
9974  O  O6  . NAG C .   ? 0.764545  1.22746  1.02057  0.247539    0.00210855  -0.168402   2    NAG C O6  
9975  O  O7  . NAG C .   ? 0.72365   1.16478  0.952401 0.243347    -0.0579229  -0.1468     2    NAG C O7  
9976  C  C1  . NAG D .   ? 0.319934  0.537767 0.448577 0.0230092   0.054178    -0.0894906  1    NAG D C1  
9977  C  C2  . NAG D .   ? 0.309373  0.55031  0.45122  0.0268054   0.0621575   -0.0987884  1    NAG D C2  
9978  C  C3  . NAG D .   ? 0.336037  0.608286 0.505177 0.0222605   0.0636809   -0.108395   1    NAG D C3  
9979  C  C4  . NAG D .   ? 0.367071  0.637164 0.538599 0.00437948  0.0717069   -0.105832   1    NAG D C4  
9980  C  C5  . NAG D .   ? 0.38897   0.633906 0.545415 0.00295627  0.0622742   -0.0964061  1    NAG D C5  
9981  C  C6  . NAG D .   ? 0.44661   0.683399 0.601451 -0.0132432  0.0692441   -0.092861   1    NAG D C6  
9982  C  C7  . NAG D .   ? 0.291592  0.534232 0.434291 0.0550825   0.0443599   -0.104188   1    NAG D C7  
9983  C  C8  . NAG D .   ? 0.298308  0.535128 0.433883 0.0707074   0.0405262   -0.106891   1    NAG D C8  
9984  N  N2  . NAG D .   ? 0.299247  0.54198  0.439297 0.0424146   0.0570664   -0.102685   1    NAG D N2  
9985  O  O3  . NAG D .   ? 0.294987  0.590814 0.477784 0.0258408   0.0717355   -0.117633   1    NAG D O3  
9986  O  O4  . NAG D .   ? 0.394085  0.695391 0.592948 -0.0003581  0.072677    -0.116642   1    NAG D O4  
9987  O  O5  . NAG D .   ? 0.342521  0.560004 0.474241 0.00830867  0.0604799   -0.0872525  1    NAG D O5  
9988  O  O6  . NAG D .   ? 0.573153  0.80827  0.723685 -0.0233323  0.0852234   -0.0921727  1    NAG D O6  
9989  O  O7  . NAG D .   ? 0.316423  0.561268 0.464996 0.0541308   0.0363856   -0.103162   1    NAG D O7  
9990  C  C1  . FUC D .   ? 0.725408  0.930862 0.851611 -0.0292548  0.0902201   -0.0813134  2    FUC D C1  
9991  C  C2  . FUC D .   ? 0.871505  1.07864  0.997594 -0.043116   0.108178    -0.0821718  2    FUC D C2  
9992  C  C3  . FUC D .   ? 0.930284  1.11392  1.02901  -0.0419023  0.115831    -0.0734406  2    FUC D C3  
9993  C  C4  . FUC D .   ? 0.855714  1.04575  0.951098 -0.0282049  0.112078    -0.0760767  2    FUC D C4  
9994  C  C5  . FUC D .   ? 0.78388   0.981901 0.889603 -0.0156903  0.0953884   -0.0793748  2    FUC D C5  
9995  C  C6  . FUC D .   ? 0.828995  1.01323  0.918537 -0.00255508 0.0872407   -0.0760432  2    FUC D C6  
9996  O  O2  . FUC D .   ? 0.902316  1.14158  1.05266  -0.0449173  0.115044    -0.0939007  2    FUC D O2  
9997  O  O3  . FUC D .   ? 0.81849   0.973065 0.895553 -0.0410477  0.109376    -0.0628118  2    FUC D O3  
9998  O  O4  . FUC D .   ? 0.7999    0.964448 0.867004 -0.0248273  0.1135      -0.0672857  2    FUC D O4  
9999  O  O5  . FUC D .   ? 0.765908  0.954573 0.872209 -0.018842   0.0864607   -0.0753684  2    FUC D O5  
10049 C  C1  . NAG F .   ? 0.591465  0.66243  0.357875 0.135881    -0.149386   -0.0251145  701  NAG A C1  
10050 C  C2  . NAG F .   ? 0.597341  0.670868 0.347862 0.139971    -0.157252   -0.0353564  701  NAG A C2  
10051 C  C3  . NAG F .   ? 0.629522  0.699651 0.36071  0.149347    -0.172259   -0.0348743  701  NAG A C3  
10052 C  C4  . NAG F .   ? 0.638577  0.713607 0.394504 0.151509    -0.184435   -0.03676    701  NAG A C4  
10053 C  C5  . NAG F .   ? 0.656257  0.727881 0.426498 0.147477    -0.174976   -0.0257537  701  NAG A C5  
10054 C  C6  . NAG F .   ? 0.648383  0.725548 0.446157 0.148912    -0.184543   -0.0275332  701  NAG A C6  
10055 C  C7  . NAG F .   ? 0.664497  0.739375 0.399131 0.134629    -0.141477   -0.0433275  701  NAG A C7  
10056 C  C8  . NAG F .   ? 0.670596  0.741741 0.377571 0.135736    -0.133287   -0.0435468  701  NAG A C8  
10057 N  N2  . NAG F .   ? 0.658402  0.728075 0.386434 0.138535    -0.146261   -0.0341911  701  NAG A N2  
10058 O  O3  . NAG F .   ? 0.633756  0.707504 0.353538 0.152418    -0.179569   -0.0463956  701  NAG A O3  
10059 O  O4  . NAG F .   ? 0.726159  0.798881 0.464981 0.160828    -0.200225   -0.0377162  701  NAG A O4  
10060 O  O5  . NAG F .   ? 0.609846  0.684535 0.396071 0.138456    -0.160486   -0.0263939  701  NAG A O5  
10061 O  O6  . NAG F .   ? 0.601965  0.676087 0.413136 0.144795    -0.17457    -0.0184115  701  NAG A O6  
10062 O  O7  . NAG F .   ? 0.663782  0.745981 0.425665 0.130623    -0.143816   -0.0512621  701  NAG A O7  
10063 C  C1  . NAG G .   ? 0.404905  0.336492 0.435795 0.0324776   0.0231366   0.0466711   702  NAG A C1  
10064 C  C2  . NAG G .   ? 0.4293    0.347273 0.468381 0.0362592   0.0207864   0.0471675   702  NAG A C2  
10065 C  C3  . NAG G .   ? 0.48709   0.391339 0.518396 0.03948     0.0202793   0.0597304   702  NAG A C3  
10066 C  C4  . NAG G .   ? 0.498585  0.399525 0.520507 0.034452    0.0258295   0.0691507   702  NAG A C4  
10067 C  C5  . NAG G .   ? 0.466394  0.382952 0.48067  0.0315125   0.0277931   0.0667562   702  NAG A C5  
10068 C  C6  . NAG G .   ? 0.473288  0.386349 0.481238 0.0258331   0.0347023   0.0749019   702  NAG A C6  
10069 C  C7  . NAG G .   ? 0.52627   0.449039 0.576085 0.045842    0.0133834   0.0350033   702  NAG A C7  
10070 C  C8  . NAG G .   ? 0.585991  0.5186   0.637064 0.0518774   0.00924347  0.0291712   702  NAG A C8  
10071 N  N2  . NAG G .   ? 0.488008  0.412749 0.526907 0.0430665   0.0154674   0.0425967   702  NAG A N2  
10072 O  O3  . NAG G .   ? 0.461085  0.350162 0.501424 0.0418819   0.0188894   0.0611886   702  NAG A O3  
10073 O  O4  . NAG G .   ? 0.551378  0.44233  0.561709 0.0395373   0.0237703   0.0803282   702  NAG A O4  
10074 O  O5  . NAG G .   ? 0.43761   0.365447 0.46175  0.0281309   0.0279553   0.0551547   702  NAG A O5  
10075 O  O6  . NAG G .   ? 0.476231  0.398923 0.49026  0.0187252   0.039445    0.069429    702  NAG A O6  
10076 O  O7  . NAG G .   ? 0.651011  0.564577 0.710215 0.0432535   0.0151753   0.0324487   702  NAG A O7  
10077 ZN ZN  . ZN  H .   ? 0.190801  0.289927 0.195659 0.0365756   -0.0171297  -0.0146856  703  ZN  A ZN  
10078 CL CL  . CL  I .   ? 0.179955  0.280899 0.207562 0.0205653   0.00385724  0.00651073  704  CL  A CL  
10110 C  C1  . PGE K .   ? 0.885742  0.798768 0.678027 0.0430424   -0.0202761  -0.173709   701  PGE B C1  
10111 O  O1  . PGE K .   ? 0.864914  0.759203 0.657515 0.0429255   -0.0143924  -0.180402   701  PGE B O1  
10112 C  C2  . PGE K .   ? 0.855894  0.776292 0.638802 0.0521206   -0.0138166  -0.162342   701  PGE B C2  
10113 O  O2  . PGE K .   ? 0.754888  0.667202 0.521942 0.0598213   -0.00677206 -0.167233   701  PGE B O2  
10114 C  C3  . PGE K .   ? 0.726631  0.647349 0.483208 0.0669634   -0.0003161  -0.157955   701  PGE B C3  
10115 C  C4  . PGE K .   ? 0.722522  0.638233 0.479081 0.0734347   0.0115653   -0.156254   701  PGE B C4  
10116 O  O4  . PGE K .   ? 0.755207  0.673246 0.562261 0.077048    0.0284662   -0.135323   701  PGE B O4  
10117 C  C6  . PGE K .   ? 0.75285   0.661299 0.560857 0.0696312   0.0195174   -0.140667   701  PGE B C6  
10118 C  C5  . PGE K .   ? 0.800563  0.706529 0.590184 0.0689025   0.0146209   -0.150858   701  PGE B C5  
10119 O  O3  . PGE K .   ? 0.702866  0.621241 0.479847 0.0721902   0.0163975   -0.146352   701  PGE B O3  
10120 O  O22 . P33 L .   ? 0.80658   0.665251 0.619494 0.0484614   0.00493088  -0.16914    702  P33 B O22 
10121 C  C21 . P33 L .   ? 0.747148  0.594626 0.567838 0.0372085   0.00088705  -0.174659   702  P33 B C21 
10122 C  C20 . P33 L .   ? 0.79442   0.614705 0.612745 0.0382235   0.00644593  -0.179366   702  P33 B C20 
10123 O  O19 . P33 L .   ? 0.817864  0.625858 0.644872 0.0255721   0.00446997  -0.182683   702  P33 B O19 
10124 C  C18 . P33 L .   ? 0.762252  0.546741 0.591406 0.0270113   0.0109881   -0.178005   702  P33 B C18 
10125 C  C17 . P33 L .   ? 0.728321  0.522257 0.571835 0.0244375   0.0114547   -0.164036   702  P33 B C17 
10126 O  O16 . P33 L .   ? 0.767408  0.540774 0.609908 0.0305808   0.0177882   -0.157123   702  P33 B O16 
10127 C  C15 . P33 L .   ? 0.774797  0.561189 0.6274   0.0348884   0.0186727   -0.142861   702  P33 B C15 
10128 C  C14 . P33 L .   ? 0.794846  0.598834 0.646581 0.048578    0.0200318   -0.137554   702  P33 B C14 
10129 O  O13 . P33 L .   ? 0.784877  0.586636 0.641283 0.0574758   0.0234784   -0.127185   702  P33 B O13 
10130 C  C12 . P33 L .   ? 0.787777  0.605307 0.644647 0.0703036   0.0258814   -0.124232   702  P33 B C12 
10131 C  C11 . P33 L .   ? 0.812856  0.660009 0.676754 0.0671007   0.0233532   -0.120118   702  P33 B C11 
10132 O  O10 . P33 L .   ? 0.927885  0.788103 0.788205 0.0769793   0.0270462   -0.121699   702  P33 B O10 
10133 C  C9  . P33 L .   ? 0.938165  0.79528  0.800526 0.0897022   0.0316869   -0.119616   702  P33 B C9  
10134 C  C8  . P33 L .   ? 0.921272  0.803216 0.79701  0.0932607   0.0329741   -0.110211   702  P33 B C8  
10135 O  O7  . P33 L .   ? 0.890918  0.779522 0.769488 0.106892    0.0378386   -0.111011   702  P33 B O7  
10136 C  C6  . P33 L .   ? 0.819946  0.726927 0.697009 0.110285    0.0427009   -0.114567   702  P33 B C6  
10137 C  C5  . P33 L .   ? 0.762128  0.694063 0.648876 0.103587    0.04319     -0.107256   702  P33 B C5  
10138 O  O4  . P33 L .   ? 0.780525  0.723531 0.659405 0.103153    0.0480199   -0.111053   702  P33 B O4  
10139 C  C3  . P33 L .   ? 0.67405   0.616586 0.544109 0.0929445   0.0445664   -0.110168   702  P33 B C3  
10140 C  C2  . P33 L .   ? 0.753935  0.67697  0.608797 0.091297    0.0409347   -0.119157   702  P33 B C2  
10141 O  O1  . P33 L .   ? 0.733706  0.659007 0.578851 0.0833056   0.0368228   -0.11988    702  P33 B O1  
10142 O  O1  . PG4 M .   ? 0.793761  0.704438 0.752661 0.00753835  -0.00346015 -0.0398864  703  PG4 B O1  
10143 C  C1  . PG4 M .   ? 0.794696  0.727732 0.762721 0.00875718  -0.00598818 -0.03738    703  PG4 B C1  
10144 C  C2  . PG4 M .   ? 0.946079  0.894463 0.920087 0.00596611  -0.00808785 -0.0424194  703  PG4 B C2  
10145 O  O2  . PG4 M .   ? 0.85352   0.816382 0.830754 0.0121385   -0.00979617 -0.0408493  703  PG4 B O2  
10146 C  C3  . PG4 M .   ? 0.766376  0.735677 0.742597 0.0134245   -0.0108201  -0.0459251  703  PG4 B C3  
10147 C  C4  . PG4 M .   ? 0.766639  0.735514 0.742534 0.00647631  -0.012149   -0.0518773  703  PG4 B C4  
10148 O  O3  . PG4 M .   ? 0.66022   0.63052  0.631226 0.00946843  -0.0130962  -0.0576334  703  PG4 B O3  
10149 C  C5  . PG4 M .   ? 0.598873  0.576417 0.570261 0.00462027  -0.0160897  -0.0633063  703  PG4 B C5  
10150 C  C6  . PG4 M .   ? 0.632383  0.6003   0.597024 0.00428535  -0.0164218  -0.071794   703  PG4 B C6  
10151 O  O4  . PG4 M .   ? 0.672549  0.651181 0.633662 0.00488094  -0.0199443  -0.0773354  703  PG4 B O4  
10152 C  C7  . PG4 M .   ? 0.645389  0.626617 0.609247 -0.00270422 -0.023503   -0.0851261  703  PG4 B C7  
10153 C  C8  . PG4 M .   ? 0.639066  0.602874 0.599723 -0.00735813 -0.0217809  -0.0926379  703  PG4 B C8  
10154 O  O5  . PG4 M .   ? 0.716312  0.680298 0.684662 -0.0182964  -0.0227001  -0.0980011  703  PG4 B O5  
10155 ZN ZN  . ZN  N .   ? 0.272062  0.269145 0.211271 0.0155862   0.00885643  -0.00804183 704  ZN  B ZN  
10156 CL CL  . CL  O .   ? 0.368049  0.291835 0.292313 -0.0116071  0.0305913   0.0110126   705  CL  B CL  
10188 O  O   . HOH Q .   ? 0.501797  0.615907 0.487565 0.039382    0.0139847   -0.0179199  801  HOH A O   
10189 O  O   . HOH Q .   ? 0.441981  0.596694 0.664942 0.111595    -0.0699582  -0.0373935  802  HOH A O   
10190 O  O   . HOH Q .   ? 0.460886  0.559328 0.42409  0.0183035   -0.0318918  -0.0304135  803  HOH A O   
10191 O  O   . HOH Q .   ? 0.384866  0.493094 0.333417 0.0412632   0.0242998   -0.0104614  804  HOH A O   
10192 O  O   . HOH Q .   ? 0.179545  0.374215 0.418199 0.078411    -0.0607316  -0.0609458  805  HOH A O   
10193 O  O   . HOH Q .   ? 0.3717    0.468467 0.357947 0.0142506   -0.0158637  -0.0231376  806  HOH A O   
10194 O  O   . HOH Q .   ? 0.234994  0.457583 0.708636 -0.00829672 -0.0987727  -0.122494   807  HOH A O   
10195 O  O   . HOH Q .   ? 0.327412  0.457378 0.373787 0.0309847   0.0661524   -0.0242624  808  HOH A O   
10196 O  O   . HOH Q .   ? 0.421251  0.504459 0.521838 0.0726219   0.00794708  -0.0251349  809  HOH A O   
10197 O  O   . HOH Q .   ? 0.513704  0.581215 0.467697 0.0104959   0.0224917   0.0460837   810  HOH A O   
10198 O  O   . HOH Q .   ? 0.231084  0.356239 0.324788 0.0555399   -0.0188917  -0.0354483  811  HOH A O   
10199 O  O   . HOH Q .   ? 0.522558  0.644166 0.533659 0.0832876   -0.153793   -0.151392   812  HOH A O   
10200 O  O   . HOH Q .   ? 0.400776  0.501649 0.371747 0.0364244   0.00634846  -0.00436111 813  HOH A O   
10201 O  O   . HOH Q .   ? 0.365526  0.500991 0.46679  0.0481229   -0.0319531  -0.019223   814  HOH A O   
10202 O  O   . HOH Q .   ? 0.394057  0.485124 0.284292 0.0581913   -0.00329422 -0.00985953 815  HOH A O   
10203 O  O   . HOH Q .   ? 0.251951  0.55251  0.639489 0.0687554   0.00543182  -0.112712   816  HOH A O   
10204 O  O   . HOH Q .   ? 0.340293  0.583894 0.696318 0.0413902   -0.0112353  -0.0641589  817  HOH A O   
10205 O  O   . HOH Q .   ? 0.523315  0.464351 0.522991 -0.00531664 0.0736419   0.0878767   818  HOH A O   
10206 O  O   . HOH Q .   ? 0.517315  0.601273 0.481922 0.0326939   0.0417089   -0.0501587  819  HOH A O   
10207 O  O   . HOH Q .   ? 0.445473  0.546295 0.395323 0.0277608   -0.0506034  -0.0150067  820  HOH A O   
10208 O  O   . HOH Q .   ? 0.220745  0.299963 0.22084  0.029559    0.0218093   -0.0152115  821  HOH A O   
10209 O  O   . HOH Q .   ? 0.220109  0.313357 0.210547 0.0222752   0.00756547  0.00554057  822  HOH A O   
10210 O  O   . HOH Q .   ? 0.408389  0.511625 0.389841 0.0393194   -0.0674218  0.00038492  823  HOH A O   
10211 O  O   . HOH Q .   ? 0.319924  0.294889 0.488493 0.0460191   -0.0618961  -0.00774334 824  HOH A O   
10212 O  O   . HOH Q .   ? 0.312574  0.377125 0.32073  0.0349955   0.0280831   -0.0404317  825  HOH A O   
10213 O  O   . HOH Q .   ? 0.27457   0.34695  0.203808 0.0659989   -0.0352729  0.0151809   826  HOH A O   
10214 O  O   . HOH Q .   ? 0.326653  0.470979 0.529681 0.098814    -0.0384529  -0.0353954  827  HOH A O   
10215 O  O   . HOH Q .   ? 0.357518  0.505245 0.481308 0.0652409   -0.0678154  -0.032136   828  HOH A O   
10216 O  O   . HOH Q .   ? 0.388858  0.393589 0.36609  0.0926261   -0.0447758  0.0492611   829  HOH A O   
10217 O  O   . HOH Q .   ? 0.229356  0.414056 0.505521 0.0136065   -0.0365784  -0.0529913  830  HOH A O   
10218 O  O   . HOH Q .   ? 0.333031  0.429795 0.425697 0.099719    -0.025817   -0.162584   831  HOH A O   
10219 O  O   . HOH Q .   ? 0.325407  0.419448 0.268089 0.0592945   -0.0376669  -0.0124036  832  HOH A O   
10220 O  O   . HOH Q .   ? 0.254994  0.357543 0.248406 0.0864589   -0.0337691  -0.142104   833  HOH A O   
10221 O  O   . HOH Q .   ? 0.304579  0.50573  0.530057 0.0959261   -0.160934   -0.082577   834  HOH A O   
10222 O  O   . HOH Q .   ? 0.323084  0.411375 0.267873 0.0190926   0.0142022   0.00701723  835  HOH A O   
10223 O  O   . HOH Q .   ? 0.297301  0.517351 0.539285 0.0530507   -0.0811841  -0.064549   836  HOH A O   
10224 O  O   . HOH Q .   ? 0.314502  0.3761   0.255315 0.0335021   -0.0362625  0.0399624   837  HOH A O   
10225 O  O   . HOH Q .   ? 0.363715  0.469582 0.367023 0.0353939   -0.00136208 -0.0120642  838  HOH A O   
10226 O  O   . HOH Q .   ? 0.192675  0.409313 0.358829 0.0350015   0.0655917   -0.0601632  839  HOH A O   
10227 O  O   . HOH Q .   ? 0.171063  0.253867 0.233005 0.0561687   0.012459    -0.0160013  840  HOH A O   
10228 O  O   . HOH Q .   ? 0.410588  0.501671 0.291588 0.053119    0.0197386   -0.00114581 841  HOH A O   
10229 O  O   . HOH Q .   ? 0.388428  0.410428 0.407873 0.0446539   0.00940313  0.0105983   842  HOH A O   
10230 O  O   . HOH Q .   ? 0.307093  0.620661 0.731693 0.0621365   -0.0351307  -0.112357   843  HOH A O   
10231 O  O   . HOH Q .   ? 0.23058   0.40704  0.409385 0.0673823   -0.0141208  -0.0615901  844  HOH A O   
10232 O  O   . HOH Q .   ? 0.346886  0.361137 0.389062 0.0358421   0.018194    -0.0257039  845  HOH A O   
10233 O  O   . HOH Q .   ? 0.36264   0.477497 0.377591 0.0708622   -0.076996   -0.0244857  846  HOH A O   
10234 O  O   . HOH Q .   ? 0.258727  0.30174  0.353592 0.0673301   -0.0702056  0.0127781   847  HOH A O   
10235 O  O   . HOH Q .   ? 0.412088  0.538993 0.618053 0.0958964   -0.056215   -0.061485   848  HOH A O   
10236 O  O   . HOH Q .   ? 0.420799  0.484886 0.472654 -0.0106922  0.0409749   0.0542383   849  HOH A O   
10237 O  O   . HOH Q .   ? 0.278073  0.382513 0.32463  0.0002737   -0.0280787  -0.0526971  850  HOH A O   
10238 O  O   . HOH Q .   ? 0.175915  0.321998 0.328379 0.0610996   0.0264055   -0.0368439  851  HOH A O   
10239 O  O   . HOH Q .   ? 0.193186  0.28898  0.202345 0.0643164   -0.0432643  0.00074479  852  HOH A O   
10240 O  O   . HOH Q .   ? 0.294864  0.435368 0.579133 -0.0123231  -0.0291296  -0.0458411  853  HOH A O   
10241 O  O   . HOH Q .   ? 0.476353  0.5556   0.564525 0.0583174   -0.089629   -0.136388   854  HOH A O   
10242 O  O   . HOH Q .   ? 0.26214   0.402032 0.384564 0.108195    -0.117959   -0.0284464  855  HOH A O   
10243 O  O   . HOH Q .   ? 0.185146  0.296758 0.206493 0.0259691   0.0393138   -0.00762261 856  HOH A O   
10244 O  O   . HOH Q .   ? 0.184954  0.288865 0.189372 0.0139496   -0.0148665  -0.0172349  857  HOH A O   
10245 O  O   . HOH Q .   ? 0.265404  0.380526 0.328294 -0.0136736  0.0892408   0.0160097   858  HOH A O   
10246 O  O   . HOH Q .   ? 0.435927  0.531446 0.392309 0.0623667   -0.0471371  -0.0109507  859  HOH A O   
10247 O  O   . HOH Q .   ? 0.295498  0.403589 0.317848 -0.00423748 0.0913239   0.0225375   860  HOH A O   
10248 O  O   . HOH Q .   ? 0.226685  0.387848 0.425148 -0.0226798  -0.0219141  -0.0686394  861  HOH A O   
10249 O  O   . HOH Q .   ? 0.208038  0.294907 0.292145 0.0556637   -0.0308949  -0.033783   862  HOH A O   
10250 O  O   . HOH Q .   ? 0.42753   0.555248 0.54411  -0.00134594 0.0426273   0.0107482   863  HOH A O   
10251 O  O   . HOH Q .   ? 0.338776  0.359128 0.523817 0.0827579   -0.0677918  -0.056903   864  HOH A O   
10252 O  O   . HOH Q .   ? 0.313786  0.404734 0.271166 0.035259    0.0103021   0.00725592  865  HOH A O   
10253 O  O   . HOH Q .   ? 0.455987  0.488346 0.295139 0.0625561   0.00406941  0.0536971   866  HOH A O   
10254 O  O   . HOH Q .   ? 0.368571  0.459531 0.430611 0.0539329   0.0419333   -0.0460368  867  HOH A O   
10255 O  O   . HOH Q .   ? 0.181382  0.409392 0.388386 0.0487181   0.0455197   -0.074892   868  HOH A O   
10256 O  O   . HOH Q .   ? 0.516019  0.569867 0.344382 0.0312511   0.0974228   0.0621233   869  HOH A O   
10257 O  O   . HOH Q .   ? 0.223216  0.488681 0.647603 0.0421059   -0.0728966  -0.0925963  870  HOH A O   
10258 O  O   . HOH Q .   ? 0.457776  0.542705 0.417539 0.0197985   0.00973759  -0.0180564  871  HOH A O   
10259 O  O   . HOH Q .   ? 0.266303  0.462131 0.563837 0.0081583   -0.0146213  -0.0470949  872  HOH A O   
10260 O  O   . HOH Q .   ? 0.139149  0.227801 0.192397 0.0492404   0.0242961   -0.0228085  873  HOH A O   
10261 O  O   . HOH Q .   ? 0.256764  0.374489 0.271847 0.0232777   0.0561607   -0.00971801 874  HOH A O   
10262 O  O   . HOH Q .   ? 0.462901  0.62297  0.626877 0.0385686   -0.0215565  -0.0284067  875  HOH A O   
10263 O  O   . HOH Q .   ? 0.249696  0.28067  0.327046 -0.00765564 -0.00854715 -0.0868933  876  HOH A O   
10264 O  O   . HOH Q .   ? 0.292919  0.358127 0.504391 0.106427    -0.0830946  -0.0457886  877  HOH A O   
10265 O  O   . HOH Q .   ? 0.504186  0.587465 0.256876 0.0984636   -0.0404872  -0.042276   878  HOH A O   
10266 O  O   . HOH Q .   ? 0.258017  0.376389 0.265253 0.0179045   0.0464373   0.00135205  879  HOH A O   
10267 O  O   . HOH Q .   ? 0.259623  0.314035 0.387028 -0.00586648 -0.0006312  0.0211111   880  HOH A O   
10268 O  O   . HOH Q .   ? 0.152746  0.275254 0.208737 0.0459264   -0.0637883  -0.00809062 881  HOH A O   
10269 O  O   . HOH Q .   ? 0.526573  0.569403 0.335005 0.0847303   -0.0346833  0.0358218   882  HOH A O   
10270 O  O   . HOH Q .   ? 0.272329  0.310762 0.456669 0.0902363   -0.0593882  -0.121721   883  HOH A O   
10271 O  O   . HOH Q .   ? 0.484793  0.439633 0.46801  0.0155447   0.0468084   0.073718    884  HOH A O   
10272 O  O   . HOH Q .   ? 0.526467  0.606496 0.421955 0.0508976   0.00700551  0.011405    885  HOH A O   
10273 O  O   . HOH Q .   ? 0.246181  0.376619 0.339549 0.0431082   -0.00820962 -0.01297    886  HOH A O   
10274 O  O   . HOH Q .   ? 0.170845  0.271998 0.310142 0.0261949   -0.0676953  -0.0689453  887  HOH A O   
10275 O  O   . HOH Q .   ? 0.388889  0.401809 0.430636 0.0764267   -0.0145529  0.018236    888  HOH A O   
10276 O  O   . HOH Q .   ? 0.420243  0.468202 0.55551  0.0633508   -0.0725702  -0.132394   889  HOH A O   
10277 O  O   . HOH Q .   ? 0.463006  0.560945 0.274363 0.093612    -0.0484497  -0.0752302  890  HOH A O   
10278 O  O   . HOH Q .   ? 0.429702  0.49999  0.327658 0.0604965   -0.0176031  0.0169574   891  HOH A O   
10279 O  O   . HOH Q .   ? 0.334936  0.398329 0.254809 0.023278    -0.00884774 0.0410492   892  HOH A O   
10280 O  O   . HOH Q .   ? 0.333984  0.348323 0.406499 -0.0305282  0.0806181   0.0430846   893  HOH A O   
10281 O  O   . HOH Q .   ? 0.480855  0.661469 0.724649 0.0165181   -0.0151954  -0.0387148  894  HOH A O   
10282 O  O   . HOH Q .   ? 0.217499  0.310437 0.223711 0.00805784  -0.0164992  -0.0380094  895  HOH A O   
10283 O  O   . HOH Q .   ? 0.340237  0.488451 0.899739 -0.125189   0.128298    0.0228088   896  HOH A O   
10284 O  O   . HOH Q .   ? 0.365218  0.362204 0.460534 0.0511036   -0.0597773  0.0316959   897  HOH A O   
10285 O  O   . HOH Q .   ? 0.482285  0.575636 0.476704 0.0839004   -0.0909959  -0.166683   898  HOH A O   
10286 O  O   . HOH Q .   ? 0.17802   0.322959 0.516851 -0.0234633  -0.0302122  -0.0538811  899  HOH A O   
10287 O  O   . HOH Q .   ? 0.434957  0.529741 0.397431 0.0305377   0.0218044   0.00801262  900  HOH A O   
10288 O  O   . HOH Q .   ? 0.411654  0.491579 0.364638 0.0198091   0.00603531  -0.0361054  901  HOH A O   
10289 O  O   . HOH Q .   ? 0.558042  0.635129 0.458393 0.0323779   -0.0398264  0.0171118   902  HOH A O   
10290 O  O   . HOH Q .   ? 0.19669   0.284237 0.207237 0.00461583  0.0490837   0.0178121   903  HOH A O   
10291 O  O   . HOH Q .   ? 0.308813  0.390352 0.251238 0.0263248   0.0420544   0.0239748   904  HOH A O   
10292 O  O   . HOH Q .   ? 0.384349  0.563378 0.407408 0.0353084   0.107452    -0.0396447  905  HOH A O   
10293 O  O   . HOH Q .   ? 0.544689  0.824339 0.990901 0.00416762  0.0535306   -0.0632288  906  HOH A O   
10294 O  O   . HOH Q .   ? 0.528411  0.623719 0.504528 0.00661558  0.0540152   0.0287569   907  HOH A O   
10295 O  O   . HOH Q .   ? 0.468247  0.554829 0.40148  0.0201479   -0.00603319 -0.0255586  908  HOH A O   
10296 O  O   . HOH Q .   ? 0.206018  0.266195 0.312897 0.0086402   -0.0172126  0.00387449  909  HOH A O   
10297 O  O   . HOH Q .   ? 0.268909  0.320843 0.340897 -0.0116086  0.0176449   -0.0246416  910  HOH A O   
10298 O  O   . HOH Q .   ? 0.11571   0.210128 0.135848 0.0425122   -0.00508529 0.00269011  911  HOH A O   
10299 O  O   . HOH Q .   ? 0.33551   0.450634 0.377465 0.0809331   -0.00777453 -0.113376   912  HOH A O   
10300 O  O   . HOH Q .   ? 0.275537  0.372594 0.315677 0.0433366   0.00786266  -0.00498083 913  HOH A O   
10301 O  O   . HOH Q .   ? 0.334432  0.487352 0.404952 0.091638    -0.164537   -0.0897835  914  HOH A O   
10302 O  O   . HOH Q .   ? 0.324996  0.521676 0.629577 -0.0503948  0.050036    -0.0550552  915  HOH A O   
10303 O  O   . HOH Q .   ? 0.297793  0.414493 0.262601 0.106792    -0.144721   -0.0458468  916  HOH A O   
10304 O  O   . HOH Q .   ? 0.345556  0.446188 0.333845 0.0279358   0.0439101   -0.0197388  917  HOH A O   
10305 O  O   . HOH Q .   ? 0.22433   0.292131 0.218328 0.0114474   0.0346614   0.0212278   918  HOH A O   
10306 O  O   . HOH Q .   ? 0.393295  0.633049 0.667239 0.037828    -0.0714156  -0.0763494  919  HOH A O   
10307 O  O   . HOH Q .   ? 0.398447  0.571437 0.696185 -0.0663859  0.0930782   -0.0308495  920  HOH A O   
10308 O  O   . HOH Q .   ? 0.529928  0.66646  0.352254 0.0708706   0.095578    -0.0518891  921  HOH A O   
10309 O  O   . HOH Q .   ? 0.370013  0.447745 0.463632 0.0848368   -0.0440979  -0.142169   922  HOH A O   
10310 O  O   . HOH Q .   ? 0.429398  0.537606 0.221537 0.0812006   0.0327913   -0.051462   923  HOH A O   
10311 O  O   . HOH Q .   ? 0.286941  0.408462 0.335243 0.0756925   -0.00100677 -0.0971973  924  HOH A O   
10312 O  O   . HOH Q .   ? 0.578515  0.758887 0.733223 0.0945767   -0.174568   -0.0905553  925  HOH A O   
10313 O  O   . HOH Q .   ? 0.167157  0.269027 0.301149 -0.0282862  0.0325671   -0.022492   926  HOH A O   
10314 O  O   . HOH Q .   ? 0.425255  0.38744  0.312982 0.0425229   0.0336427   0.0972702   927  HOH A O   
10315 O  O   . HOH Q .   ? 0.170319  0.367353 0.37685  0.0593021   -0.0797356  -0.0519227  928  HOH A O   
10316 O  O   . HOH Q .   ? 0.195316  0.452224 0.772032 -0.0289463  -0.0662787  -0.118953   929  HOH A O   
10317 O  O   . HOH Q .   ? 0.384718  0.48413  0.47107  0.0585483   -0.11656    -0.144029   930  HOH A O   
10318 O  O   . HOH Q .   ? 0.395507  0.468446 0.502278 -0.00570965 0.0119478   0.0246695   931  HOH A O   
10319 O  O   . HOH Q .   ? 0.336078  0.559533 0.761606 0.0187288   -0.151419   -0.148987   932  HOH A O   
10320 O  O   . HOH Q .   ? 0.158162  0.317301 0.335663 -0.017748   -0.00377911 -0.051239   933  HOH A O   
10321 O  O   . HOH Q .   ? 0.366437  0.504114 0.351661 0.0362412   0.0589687   -0.0213157  934  HOH A O   
10322 O  O   . HOH Q .   ? 0.329058  0.428016 0.447851 0.0757412   -0.0801809  -0.0079034  935  HOH A O   
10323 O  O   . HOH Q .   ? 0.363755  0.474428 0.398628 0.0420487   -0.00730693 -0.0231764  936  HOH A O   
10324 O  O   . HOH Q .   ? 0.523996  0.472045 0.436513 -0.0328481  0.180827    0.154658    937  HOH A O   
10325 O  O   . HOH Q .   ? 0.258333  0.307766 0.416611 0.0859667   -0.0552301  -0.129341   938  HOH A O   
10326 O  O   . HOH Q .   ? 0.321336  0.521332 0.538039 -0.00917657 0.0250388   -0.04756    939  HOH A O   
10327 O  O   . HOH Q .   ? 0.352859  0.476815 0.532319 -0.01511    0.0339677   0.00843318  940  HOH A O   
10328 O  O   . HOH Q .   ? 0.43047   0.51233  0.547533 0.0918626   -0.0364416  -0.141673   941  HOH A O   
10329 O  O   . HOH Q .   ? 0.269247  0.575105 0.629489 0.0795591   0.0638668   -0.133648   942  HOH A O   
10330 O  O   . HOH Q .   ? 0.298737  0.393582 0.308168 0.00349679  0.045863    0.0311773   943  HOH A O   
10331 O  O   . HOH Q .   ? 0.177454  0.276153 0.214868 0.026038    -0.0144736  -0.00598529 944  HOH A O   
10332 O  O   . HOH Q .   ? 0.415542  0.401185 0.293685 0.0734958   -0.0147103  0.0787507   945  HOH A O   
10333 O  O   . HOH Q .   ? 0.419295  0.558932 0.49406  0.0743654   -0.104052   -0.047178   946  HOH A O   
10334 O  O   . HOH Q .   ? 0.4888    0.429944 0.46398  0.0326601   0.0300759   0.0765741   947  HOH A O   
10335 O  O   . HOH Q .   ? 0.145912  0.238387 0.232669 0.0642219   0.00833624  -0.0197427  948  HOH A O   
10336 O  O   . HOH Q .   ? 0.268879  0.372066 0.325468 0.0246438   -0.0181365  -0.0103127  949  HOH A O   
10337 O  O   . HOH Q .   ? 0.235207  0.349684 0.343994 0.0625589   -0.0308905  -0.0360013  950  HOH A O   
10338 O  O   . HOH Q .   ? 0.264723  0.301045 0.299234 0.0433411   -0.0475494  0.0370013   951  HOH A O   
10339 O  O   . HOH Q .   ? 0.434999  0.715415 0.793957 0.0248312   -0.0570479  -0.0970919  952  HOH A O   
10340 O  O   . HOH Q .   ? 0.227907  0.344936 0.25719  0.00754989  0.0605799   0.0145371   953  HOH A O   
10341 O  O   . HOH Q .   ? 0.376051  0.384984 0.554357 0.0525551   -0.0651748  -0.0723613  954  HOH A O   
10342 O  O   . HOH Q .   ? 0.15566   0.304112 0.24297  0.026609    -0.0390958  -0.0272509  955  HOH A O   
10343 O  O   . HOH Q .   ? 0.177014  0.28602  0.283772 0.0269883   -0.0490548  -0.0434141  956  HOH A O   
10344 O  O   . HOH Q .   ? 0.171567  0.264945 0.19968  0.0375742   -0.0225169  -0.0251102  957  HOH A O   
10345 O  O   . HOH Q .   ? 0.207374  0.384305 0.348272 0.0189632   -0.0766988  -0.0613479  958  HOH A O   
10346 O  O   . HOH Q .   ? 0.477957  0.579711 0.27587  0.0737921   0.0376154   -0.0306197  959  HOH A O   
10347 O  O   . HOH Q .   ? 0.188574  0.29192  0.206073 0.021924    0.0148971   0.00562005  960  HOH A O   
10348 O  O   . HOH Q .   ? 0.356064  0.468836 0.368407 0.034033    0.00377511  -0.0124668  961  HOH A O   
10349 O  O   . HOH Q .   ? 0.33958   0.580312 0.685778 0.0685736   -0.172848   -0.125169   962  HOH A O   
10350 O  O   . HOH Q .   ? 0.277802  0.245539 0.339089 0.0139943   0.0253042   0.00183283  963  HOH A O   
10351 O  O   . HOH Q .   ? 0.177099  0.379043 0.404251 -0.0062028  -0.0153326  -0.0623775  964  HOH A O   
10352 O  O   . HOH Q .   ? 0.231116  0.332315 0.245631 0.0332091   -0.0158647  -0.00707794 965  HOH A O   
10353 O  O   . HOH Q .   ? 0.573529  0.613405 0.531064 0.00823047  0.0169486   0.0694485   966  HOH A O   
10354 O  O   . HOH Q .   ? 0.398679  0.358702 0.313968 0.0603521   0.00358486  0.0855059   967  HOH A O   
10355 O  O   . HOH Q .   ? 0.33841   0.326385 0.340855 0.0641326   -0.00647551 0.0404274   968  HOH A O   
10356 O  O   . HOH Q .   ? 0.245855  0.343607 0.256842 0.0316777   -0.00892452 -0.0057806  969  HOH A O   
10357 O  O   . HOH Q .   ? 0.17568   0.310406 0.269282 -3.26e-05   -0.0221047  -0.0411725  970  HOH A O   
10358 O  O   . HOH Q .   ? 0.447208  0.655639 0.640941 0.0586801   0.0220489   -0.0732295  971  HOH A O   
10359 O  O   . HOH Q .   ? 0.212815  0.306642 0.221559 -0.00015625 0.0750238   0.0249985   972  HOH A O   
10360 O  O   . HOH Q .   ? 0.322768  0.493934 0.315373 0.0882455   0.0682554   -0.125512   973  HOH A O   
10361 O  O   . HOH Q .   ? 0.237252  0.244613 0.211878 0.0377168   0.0156347   0.0435957   974  HOH A O   
10362 O  O   . HOH Q .   ? 0.411053  0.523086 0.461669 0.0421062   -0.0535499  -0.0416566  975  HOH A O   
10363 O  O   . HOH Q .   ? 0.320892  0.449145 0.397391 0.0419876   0.0514739   -0.0306773  976  HOH A O   
10364 O  O   . HOH Q .   ? 0.33303   0.461851 0.580226 -0.0542342  0.0268176   -0.0544878  977  HOH A O   
10365 O  O   . HOH Q .   ? 0.410097  0.519779 0.199996 0.0920399   0.00804866  -0.0808224  978  HOH A O   
10366 O  O   . HOH Q .   ? 0.271678  0.485659 0.484053 0.0696479   0.0226447   -0.0865655  979  HOH A O   
10367 O  O   . HOH Q .   ? 0.596687  0.723295 0.762787 0.00449323  -0.00964677 -0.0172043  980  HOH A O   
10368 O  O   . HOH Q .   ? 0.529827  0.60944  0.351226 0.062159    0.0259474   0.00771653  981  HOH A O   
10369 O  O   . HOH Q .   ? 0.283751  0.359397 0.209594 0.0453871   0.00265817  0.0175198   982  HOH A O   
10370 O  O   . HOH Q .   ? 0.335992  0.44893  0.325937 0.0752572   -0.112818   -0.113589   983  HOH A O   
10371 O  O   . HOH Q .   ? 0.267667  0.530695 0.609119 0.093154    0.00570603  -0.118546   984  HOH A O   
10372 O  O   . HOH Q .   ? 0.319521  0.368665 0.366468 -0.00247162 0.0196691   -0.0142912  985  HOH A O   
10373 O  O   . HOH Q .   ? 0.230666  0.329713 0.307361 0.0180137   -0.0155679  -0.0080123  986  HOH A O   
10374 O  O   . HOH Q .   ? 0.343771  0.340232 0.404802 0.0494482   0.0152082   -0.0227833  987  HOH A O   
10375 O  O   . HOH Q .   ? 0.252721  0.5472   0.589579 0.023459    0.0691166   -0.089121   988  HOH A O   
10376 O  O   . HOH Q .   ? 0.387268  0.473695 0.183056 0.0734582   0.0161873   -0.0130265  989  HOH A O   
10377 O  O   . HOH Q .   ? 0.360568  0.465623 0.336946 0.0390241   0.00450027  -0.0123145  990  HOH A O   
10378 O  O   . HOH Q .   ? 0.200441  0.316491 0.231684 0.0694977   -0.00500925 -0.0856081  991  HOH A O   
10379 O  O   . HOH Q .   ? 0.194566  0.347985 0.287474 0.030297    -0.0586482  -0.0327971  992  HOH A O   
10380 O  O   . HOH Q .   ? 0.198743  0.304281 0.222115 0.0116857   0.0118722   -0.00381645 993  HOH A O   
10381 O  O   . HOH Q .   ? 0.344716  0.427094 0.375347 0.0470903   0.045373    -0.0533319  994  HOH A O   
10382 O  O   . HOH Q .   ? 0.180206  0.224802 0.182608 0.0342079   0.01236     0.0112097   995  HOH A O   
10383 O  O   . HOH Q .   ? 0.349978  0.397669 0.401374 -0.00252706 0.0098247   -0.0353647  996  HOH A O   
10384 O  O   . HOH Q .   ? 0.314718  0.439659 0.378238 0.0812216   -0.0853247  -0.021793   997  HOH A O   
10385 O  O   . HOH Q .   ? 0.254537  0.451658 0.483041 0.0477941   0.0502638   -0.046638   998  HOH A O   
10386 O  O   . HOH Q .   ? 0.523001  0.593948 0.452408 0.101451    -0.093101   0.0124342   999  HOH A O   
10387 O  O   . HOH Q .   ? 0.17075   0.248018 0.180574 0.036176    -0.0344977  0.0198001   1000 HOH A O   
10388 O  O   . HOH Q .   ? 0.559861  0.590816 0.369866 0.0731054   -0.00798991 0.0523827   1001 HOH A O   
10389 O  O   . HOH Q .   ? 0.325644  0.416971 0.483905 0.0883439   -0.0370541  -0.0866439  1002 HOH A O   
10390 O  O   . HOH Q .   ? 0.137141  0.279094 0.265904 0.0615419   -0.0632324  -0.0248452  1003 HOH A O   
10391 O  O   . HOH Q .   ? 0.53008   0.519555 0.680435 -0.0289004  0.0108446   -0.067151   1004 HOH A O   
10392 O  O   . HOH Q .   ? 0.455678  0.562867 0.527106 0.0497543   0.031091    -0.0269657  1005 HOH A O   
10393 O  O   . HOH Q .   ? 0.307358  0.364847 0.284388 0.0256316   0.019183    0.0232168   1006 HOH A O   
10394 O  O   . HOH Q .   ? 0.385029  0.434395 0.464164 0.0892955   -0.0263243  0.00299147  1007 HOH A O   
10395 O  O   . HOH Q .   ? 0.390078  0.486465 0.302079 0.0511876   0.00736196  -0.00965712 1008 HOH A O   
10396 O  O   . HOH Q .   ? 0.226319  0.279296 0.215711 0.0195532   0.0232403   0.0206437   1009 HOH A O   
10397 O  O   . HOH Q .   ? 0.493599  0.5769   0.443525 0.0445513   -0.0710969  0.0187683   1010 HOH A O   
10398 O  O   . HOH Q .   ? 0.229514  0.342793 0.38334  0.0290147   -0.0825298  -0.0823536  1011 HOH A O   
10399 O  O   . HOH Q .   ? 0.497715  0.623624 0.586478 0.0976869   0.00040481  -0.143321   1012 HOH A O   
10400 O  O   . HOH Q .   ? 0.454802  0.419614 0.373216 0.0140486   0.0716458   0.100446    1013 HOH A O   
10401 O  O   . HOH Q .   ? 0.18528   0.328605 0.267706 0.0330228   -0.037733   -0.0217388  1014 HOH A O   
10402 O  O   . HOH Q .   ? 0.397423  0.481989 0.618119 -0.0585905  0.0449046   -0.0349025  1015 HOH A O   
10403 O  O   . HOH Q .   ? 0.455802  0.544853 0.389805 0.0221258   -0.0145129  -0.0039259  1016 HOH A O   
10404 O  O   . HOH Q .   ? 0.498915  0.539536 0.427843 0.0288758   -0.0243582  0.0605297   1017 HOH A O   
10405 O  O   . HOH Q .   ? 0.373354  0.426575 0.340173 0.00318936  0.031191    0.0630244   1018 HOH A O   
10406 O  O   . HOH Q .   ? 0.5091    0.457799 0.426702 0.0294014   0.0471295   0.0998983   1019 HOH A O   
10407 O  O   . HOH Q .   ? 0.262578  0.527924 0.586356 0.0384201   -0.0408009  -0.0849848  1020 HOH A O   
10408 O  O   . HOH Q .   ? 0.443995  0.554938 0.617783 0.0887008   -0.0411998  -0.0680763  1021 HOH A O   
10409 O  O   . HOH Q .   ? 0.253607  0.37036  0.370217 0.0428437   -0.0976411  -0.0956856  1022 HOH A O   
10410 O  O   . HOH Q .   ? 0.303614  0.396367 0.25039  0.0240227   0.0547773   0.0198333   1023 HOH A O   
10411 O  O   . HOH Q .   ? 0.379687  0.459307 0.330383 0.0377321   0.00666839  0.0155849   1024 HOH A O   
10412 O  O   . HOH Q .   ? 0.228527  0.357347 0.315154 0.0355428   -0.00544886 -0.0106953  1025 HOH A O   
10413 O  O   . HOH Q .   ? 0.570008  0.70995  0.32954  0.0918038   0.0961335   -0.0857872  1026 HOH A O   
10414 O  O   . HOH Q .   ? 0.55268   0.602013 0.501246 0.110072    -0.0914598  0.030614    1027 HOH A O   
10415 O  O   . HOH Q .   ? 0.288493  0.338303 0.318955 0.00583633  0.0129204   -0.0247363  1028 HOH A O   
10416 O  O   . HOH Q .   ? 0.265604  0.421968 0.417224 0.0677681   -0.0156061  -0.0571158  1029 HOH A O   
10417 O  O   . HOH Q .   ? 0.421445  0.545097 0.426736 0.0370997   0.0207346   -0.0199932  1030 HOH A O   
10418 O  O   . HOH Q .   ? 0.423913  0.428637 0.298349 0.0796365   -0.0280137  0.0667047   1031 HOH A O   
10419 O  O   . HOH Q .   ? 0.372337  0.508949 0.551548 0.0869223   -0.0165505  -0.0337166  1032 HOH A O   
10420 O  O   . HOH Q .   ? 0.313652  0.432338 0.43132  0.0668127   -0.064523   -0.0170912  1033 HOH A O   
10421 O  O   . HOH Q .   ? 0.410533  0.460133 0.28486  0.0599214   -0.00476737 0.0375886   1034 HOH A O   
10422 O  O   . HOH Q .   ? 0.235756  0.352344 0.378957 0.0854847   -0.0226021  -0.0227904  1035 HOH A O   
10423 O  O   . HOH Q .   ? 0.521583  0.578802 0.378344 0.0683715   -0.0177159  0.027354    1036 HOH A O   
10424 O  O   . HOH Q .   ? 0.273927  0.346493 0.35239  -0.00715711 0.0263828   0.0378192   1037 HOH A O   
10425 O  O   . HOH Q .   ? 0.420621  0.568417 0.485873 0.0274742   -0.0809636  -0.0442582  1038 HOH A O   
10426 O  O   . HOH Q .   ? 0.270148  0.30924  0.297287 0.0125092   0.0152423   -0.0250464  1039 HOH A O   
10427 O  O   . HOH Q .   ? 0.550241  0.602048 0.387709 0.0625193   0.00405194  0.0361803   1040 HOH A O   
10428 O  O   . HOH Q .   ? 0.504349  0.613587 0.331466 0.0585708   0.0732166   -0.0132087  1041 HOH A O   
10429 O  O   . HOH Q .   ? 0.461348  0.437732 0.302125 0.0718436   -0.00442153 0.0912045   1042 HOH A O   
10430 O  O   . HOH Q .   ? 0.343673  0.572259 0.451881 0.0689166   0.111394    -0.107603   1043 HOH A O   
10431 O  O   . HOH Q .   ? 0.373884  0.430499 0.309766 0.020792    -0.00500167 0.0490077   1044 HOH A O   
10432 O  O   . HOH Q .   ? 0.41825   0.511578 0.260636 0.11848     -0.141676   -0.0468344  1045 HOH A O   
10433 O  O   . HOH Q .   ? 0.338847  0.430914 0.264068 0.0477302   0.00207377  -0.00208796 1046 HOH A O   
10434 O  O   . HOH Q .   ? 0.433535  0.475614 0.484987 -0.0458937  0.153992    0.076771    1047 HOH A O   
10435 O  O   . HOH Q .   ? 0.397572  0.617693 0.603081 0.0720878   0.0402397   -0.0962284  1048 HOH A O   
10436 O  O   . HOH Q .   ? 0.315468  0.347025 0.360216 0.00102321  0.0229581   -0.00897052 1049 HOH A O   
10437 O  O   . HOH Q .   ? 0.520946  0.479732 0.582563 -0.0167805  0.0621221   0.0489088   1050 HOH A O   
10438 O  O   . HOH Q .   ? 0.436681  0.518382 0.360739 0.0357071   0.0297992   0.0194968   1051 HOH A O   
10439 O  O   . HOH Q .   ? 0.395575  0.596737 0.502339 0.0896033   0.0715534   -0.131399   1052 HOH A O   
10440 O  O   . HOH Q .   ? 0.207957  0.252466 0.283133 0.0646166   0.0177007   -0.032273   1053 HOH A O   
10441 O  O   . HOH Q .   ? 0.316943  0.406331 0.354099 0.0839752   -0.0467451  -0.148761   1054 HOH A O   
10442 O  O   . HOH Q .   ? 0.479968  0.582271 0.641815 -0.0107503  0.0131044   0.00650479  1055 HOH A O   
10443 O  O   . HOH Q .   ? 0.336236  0.428802 0.31456  0.0241305   0.027839    -0.0106987  1056 HOH A O   
10444 O  O   . HOH Q .   ? 0.215862  0.37417  0.366227 0.100066    -0.118944   -0.041096   1057 HOH A O   
10445 O  O   . HOH Q .   ? 0.202262  0.305728 0.227927 0.018357    0.0143149   0.0087516   1058 HOH A O   
10446 O  O   . HOH Q .   ? 0.45632   0.471982 0.656479 0.0848753   -0.067792   -0.090832   1059 HOH A O   
10447 O  O   . HOH Q .   ? 0.150077  0.385854 0.513957 0.107178    -0.0822355  -0.0744666  1060 HOH A O   
10448 O  O   . HOH Q .   ? 0.428134  0.54237  0.432901 0.0116927   0.0622466   0.00991237  1061 HOH A O   
10449 O  O   . HOH Q .   ? 0.3481    0.510601 0.508029 0.0573138   -0.0711138  -0.0436362  1062 HOH A O   
10450 O  O   . HOH Q .   ? 0.237022  0.440977 0.468389 0.0656829   -0.0531655  -0.0597786  1063 HOH A O   
10451 O  O   . HOH Q .   ? 0.412341  0.433838 0.561285 -0.0386755  0.0330398   -0.0279692  1064 HOH A O   
10452 O  O   . HOH Q .   ? 0.419767  0.511348 0.369849 0.0109927   0.0479731   0.0244604   1065 HOH A O   
10453 O  O   . HOH Q .   ? 0.521149  0.631223 0.553631 0.0400168   -0.0262269  -0.0105637  1066 HOH A O   
10454 O  O   . HOH Q .   ? 0.621296  0.616287 0.758759 -0.0782519  0.164339    0.0862445   1067 HOH A O   
10455 O  O   . HOH Q .   ? 0.214011  0.542944 0.656993 0.057782    -0.00633729 -0.11899    1068 HOH A O   
10456 O  O   . HOH Q .   ? 0.304879  0.417511 0.311372 0.029868    0.00973811  -0.00739835 1069 HOH A O   
10457 O  O   . HOH Q .   ? 0.447229  0.454893 0.59685  0.0858198   -0.0893309  0.00696942  1070 HOH A O   
10458 O  O   . HOH Q .   ? 0.42039   0.472021 0.62423  -0.0606684  0.0597196   -0.0163884  1071 HOH A O   
10459 O  O   . HOH Q .   ? 0.279844  0.408144 0.394093 0.0560973   0.0303463   -0.0320695  1072 HOH A O   
10460 O  O   . HOH Q .   ? 0.439047  0.561149 0.39272  0.0975671   -0.145881   -0.0830646  1073 HOH A O   
10461 O  O   . HOH Q .   ? 0.433983  0.543731 0.488356 0.0294506   -0.0220562  -0.0132361  1074 HOH A O   
10462 O  O   . HOH Q .   ? 0.255585  0.338409 0.278947 0.0031116   -0.00956444 -0.0427643  1075 HOH A O   
10463 O  O   . HOH Q .   ? 0.474213  0.409806 0.533309 0.0146006   0.0311741   0.0284127   1076 HOH A O   
10464 O  O   . HOH Q .   ? 0.268891  0.275266 0.380479 0.0216305   -0.0339883  0.0219102   1077 HOH A O   
10465 O  O   . HOH Q .   ? 0.425401  0.481422 0.313695 0.0225538   -0.00193286 0.0493926   1078 HOH A O   
10466 O  O   . HOH Q .   ? 0.407264  0.491583 0.320711 0.0137492   0.0438956   0.0251473   1079 HOH A O   
10467 O  O   . HOH Q .   ? 0.349615  0.596737 0.52431  0.054703    0.106463    -0.0945773  1080 HOH A O   
10468 O  O   . HOH Q .   ? 0.226102  0.387343 0.396983 0.0776704   -0.01099    -0.0734767  1081 HOH A O   
10469 O  O   . HOH Q .   ? 0.47171   0.47762  0.666672 0.0789579   -0.0698802  -0.06614    1082 HOH A O   
10470 O  O   . HOH Q .   ? 0.390976  0.496112 0.382093 0.0288464   0.011635    -0.00152514 1083 HOH A O   
10471 O  O   . HOH Q .   ? 0.246651  0.387545 0.3095   0.0102076   0.0833019   0.00020024  1084 HOH A O   
10472 O  O   . HOH Q .   ? 0.624239  0.608628 0.573165 0.0179572   -0.00956582 0.105273    1085 HOH A O   
10473 O  O   . HOH Q .   ? 0.291074  0.495583 0.530501 0.0771819   -0.0184902  -0.0776781  1086 HOH A O   
10474 O  O   . HOH Q .   ? 0.503571  0.565069 0.418324 0.0290767   -0.0247276  0.0408216   1087 HOH A O   
10475 O  O   . HOH Q .   ? 0.296149  0.393709 0.377875 0.0115233   -0.00420603 0.00192358  1088 HOH A O   
10476 O  O   . HOH Q .   ? 0.285122  0.341705 0.242683 0.0150577   0.00557132  0.0507272   1089 HOH A O   
10477 O  O   . HOH Q .   ? 0.441344  0.684016 0.599429 0.0667761   0.106051    -0.108411   1090 HOH A O   
10478 O  O   . HOH Q .   ? 0.600863  0.722974 0.670183 0.0397643   -0.0177992  -0.0104614  1091 HOH A O   
10479 O  O   . HOH Q .   ? 0.431002  0.578442 0.606005 0.0717255   0.0210561   -0.0430421  1092 HOH A O   
10480 O  O   . HOH Q .   ? 0.41412   0.611731 0.624572 0.0732343   -0.0011544  -0.0783175  1093 HOH A O   
10481 O  O   . HOH Q .   ? 0.281492  0.317587 0.289658 0.0378252   -0.0413524  0.0465628   1094 HOH A O   
10482 O  O   . HOH Q .   ? 0.52816   0.616705 0.715857 0.108053    -0.0354111  -0.13654    1095 HOH A O   
10483 O  O   . HOH Q .   ? 0.264009  0.274324 0.371374 0.0119406   -0.0232836  0.0309427   1096 HOH A O   
10484 O  O   . HOH Q .   ? 0.422511  0.43883  0.469332 0.046794    -0.0542788  0.0445507   1097 HOH A O   
10485 O  O   . HOH Q .   ? 0.346503  0.47812  0.424146 0.0697703   -0.0739173  -0.0261223  1098 HOH A O   
10486 O  O   . HOH Q .   ? 0.66026   0.700359 0.666341 0.0523733   -0.0655914  0.045731    1099 HOH A O   
10487 O  O   . HOH Q .   ? 0.274857  0.508838 0.598519 0.0877618   -0.131756   -0.0857967  1100 HOH A O   
10488 O  O   . HOH Q .   ? 0.638214  0.748598 0.619425 0.0228295   -0.0507173  -0.0271662  1101 HOH A O   
10489 O  O   . HOH Q .   ? 0.449366  0.551163 0.400025 0.0286566   0.0471458   0.00952611  1102 HOH A O   
10490 O  O   . HOH Q .   ? 0.434689  0.723501 0.760649 0.0876593   0.0674523   -0.138262   1103 HOH A O   
10491 O  O   . HOH Q .   ? 0.410396  0.513793 0.555236 -0.0145285  0.0331747   0.0199317   1104 HOH A O   
10492 O  O   . HOH Q .   ? 0.310021  0.521858 0.534357 -0.00617571 0.0429357   -0.0469829  1105 HOH A O   
10493 O  O   . HOH Q .   ? 0.998737  0.86922  0.607605 0.0685573   0.0807203   0.205848    1106 HOH A O   
10494 O  O   . HOH Q .   ? 0.422442  0.628131 0.69426  0.0878985   -0.0542356  -0.0744486  1107 HOH A O   
10495 O  O   . HOH Q .   ? 0.279628  0.618425 0.699483 0.038221    0.0711048   -0.116578   1108 HOH A O   
10496 O  O   . HOH Q .   ? 0.439187  0.544295 0.58274  0.0888543   -0.0159839  -0.024738   1109 HOH A O   
10497 O  O   . HOH Q .   ? 0.346013  0.484886 0.401836 0.0335095   -0.0692708  -0.0266098  1110 HOH A O   
10498 O  O   . HOH Q .   ? 0.597894  0.724774 0.584776 0.0881169   -0.144804   -0.102677   1111 HOH A O   
10499 O  O   . HOH Q .   ? 0.673404  0.729104 0.560743 0.112614    -0.103544   0.0224625   1112 HOH A O   
10500 O  O   . HOH Q .   ? 0.447509  0.538462 0.450118 0.0569872   -0.0905104  0.0155109   1113 HOH A O   
10501 O  O   . HOH Q .   ? 0.518706  0.541409 0.670516 -0.0359047  0.0173949   -0.0503738  1114 HOH A O   
10502 O  O   . HOH Q .   ? 0.327941  0.489214 0.490523 0.0534233   0.0444555   -0.0406073  1115 HOH A O   
10503 O  O   . HOH Q .   ? 0.536102  0.672965 0.555421 0.0378472   0.0326013   -0.0267778  1116 HOH A O   
10504 O  O   . HOH Q .   ? 0.307845  0.615551 0.700476 0.0393086   0.00850016  -0.102969   1117 HOH A O   
10505 O  O   . HOH Q .   ? 0.694489  0.760978 0.575588 0.0565406   -0.00165896 0.0228004   1118 HOH A O   
10506 O  O   . HOH Q .   ? 0.26517   0.586649 0.680723 0.0565778   0.0197948   -0.116374   1119 HOH A O   
10507 O  O   . HOH Q .   ? 0.363705  0.469012 0.355141 0.0242366   0.0447158   -0.0101746  1120 HOH A O   
10508 O  O   . HOH Q .   ? 0.376481  0.428729 0.531446 -0.0356966  0.00384361  -0.0645033  1121 HOH A O   
10509 O  O   . HOH Q .   ? 0.327274  0.505922 0.528079 0.0812062   -0.0100236  -0.0801628  1122 HOH A O   
10510 O  O   . HOH Q .   ? 0.32803   0.437822 0.424982 0.0592711   0.0213374   -0.0276278  1123 HOH A O   
10511 O  O   . HOH Q .   ? 0.337956  0.44473  0.358897 0.0620807   -0.0493964  -0.00837336 1124 HOH A O   
10512 O  O   . HOH Q .   ? 0.664264  0.707442 0.390035 0.0740312   0.0323086   0.0439684   1125 HOH A O   
10513 O  O   . HOH Q .   ? 0.426566  0.454267 0.481342 -0.00044338 0.0178015   -0.0247043  1126 HOH A O   
10514 O  O   . HOH Q .   ? 0.315188  0.521688 0.628188 0.103049    -0.05027    -0.0616385  1127 HOH A O   
10515 O  O   . HOH Q .   ? 0.517167  0.620402 0.4818   0.0396709   -0.0749819  -0.00415695 1128 HOH A O   
10516 O  O   . HOH Q .   ? 0.78042   0.874059 0.591991 0.101846    -0.088489   -0.0667223  1129 HOH A O   
10517 O  O   . HOH Q .   ? 0.339129  0.47299  0.477961 0.0726108   -0.0811641  -0.0215815  1130 HOH A O   
10518 O  O   . HOH Q .   ? 0.527046  0.724988 0.862841 -0.0664654  0.0843991   -0.0457512  1131 HOH A O   
10519 O  O   . HOH Q .   ? 0.421307  0.541158 0.464015 0.0489961   -0.0787571  -0.00635123 1132 HOH A O   
10520 O  O   . HOH Q .   ? 0.372275  0.497264 0.73622  -0.0365195  -0.0237707  -0.048929   1133 HOH A O   
10521 O  O   . HOH Q .   ? 0.501523  0.594389 0.440319 0.0348093   0.028967    0.00993295  1134 HOH A O   
10522 O  O   . HOH Q .   ? 0.560835  0.677197 0.720642 0.0885013   -0.0957984  -0.0191655  1135 HOH A O   
10523 O  O   . HOH Q .   ? 0.448884  0.565194 0.565496 -0.00362496 0.0329504   0.0136049   1136 HOH A O   
10524 O  O   . HOH Q .   ? 0.346977  0.584983 0.631138 0.0596454   -0.0645802  -0.0738541  1137 HOH A O   
10525 O  O   . HOH Q .   ? 0.350764  0.41573  0.484873 0.0910102   -0.0488752  -0.148934   1138 HOH A O   
10526 O  O   . HOH Q .   ? 0.448618  0.403979 0.644688 0.043289    -0.0661379  -0.0124464  1139 HOH A O   
10527 O  O   . HOH Q .   ? 0.308584  0.399928 0.381652 0.0564092   0.0301527   -0.0341218  1140 HOH A O   
10528 O  O   . HOH Q .   ? 0.406171  0.5342   0.382681 0.111878    -0.168237   -0.0658567  1141 HOH A O   
10529 O  O   . HOH Q .   ? 0.584731  0.6262   0.49283  0.0217252   -0.00515608 0.0646809   1142 HOH A O   
10530 O  O   . HOH Q .   ? 0.338656  0.570052 0.704798 0.110993    -0.0678546  -0.0736874  1143 HOH A O   
10531 O  O   . HOH Q .   ? 0.359285  0.5243   0.597776 0.0964734   -0.0799201  -0.0554677  1144 HOH A O   
10532 O  O   . HOH Q .   ? 0.331541  0.516474 0.524491 0.0700511   -0.10551    -0.045282   1145 HOH A O   
10533 O  O   . HOH Q .   ? 0.513812  0.593979 0.627371 0.050131    -0.0952616  -0.131106   1146 HOH A O   
10534 O  O   . HOH Q .   ? 0.444766  0.55671  0.454001 0.0444509   -0.0774369  -0.00341682 1147 HOH A O   
10535 O  O   . HOH Q .   ? 0.59319   0.590597 0.525558 0.0988011   -0.0548249  0.062099    1148 HOH A O   
10536 O  O   . HOH Q .   ? 0.552229  0.627854 0.334376 0.0670872   0.0360408   0.0108772   1149 HOH A O   
10537 O  O   . HOH Q .   ? 0.687677  0.6787   0.586159 0.090893    -0.042494   0.0708876   1150 HOH A O   
10538 O  O   . HOH Q .   ? 0.356202  0.53607  0.636381 0.114923    -0.0622769  -0.052141   1151 HOH A O   
10539 O  O   . HOH Q .   ? 0.150271  0.361498 0.391601 0.0645544   -0.0705671  -0.0608164  1152 HOH A O   
10540 O  O   . HOH Q .   ? 0.38613   0.377906 0.412851 0.0715983   -0.0107079  0.0292791   1153 HOH A O   
10541 O  O   . HOH Q .   ? 0.461365  0.583234 0.535316 0.0313747   -0.0150806  -0.0108734  1154 HOH A O   
10542 O  O   . HOH Q .   ? 0.489695  0.50088  0.497262 0.102896    -0.0553451  0.0411602   1155 HOH A O   
10543 O  O   . HOH Q .   ? 0.34636   0.528138 0.547486 0.054742    0.0531287   -0.0487812  1156 HOH A O   
10544 O  O   . HOH Q .   ? 0.496542  0.722137 0.801745 0.0709776   -0.188482   -0.133478   1157 HOH A O   
10545 O  O   . HOH Q .   ? 0.646349  0.706546 0.384329 0.0732566   0.0358453   0.0252669   1158 HOH A O   
10546 O  O   . HOH Q .   ? 0.612537  0.695726 0.398391 0.0617357   0.0586064   0.0105322   1159 HOH A O   
10547 O  O   . HOH Q .   ? 0.449077  0.641559 0.678096 0.0821451   -0.110601   -0.0510927  1160 HOH A O   
10548 O  O   . HOH R .   ? 1.97261   0.979373 0.76694  0.289672    0.107192    0.27654     801  HOH B O   
10549 O  O   . HOH R .   ? 0.454688  0.478496 0.467071 -0.0292988  -0.0248033  -0.0910098  802  HOH B O   
10550 O  O   . HOH R .   ? 0.69779   0.584927 0.251001 0.221922    -0.123381   0.00350953  803  HOH B O   
10551 O  O   . HOH R .   ? 0.666179  0.522933 0.555913 -0.118414   0.157445    0.0149824   804  HOH B O   
10552 O  O   . HOH R .   ? 1.71844   0.55818  0.569884 -0.00819249 0.384248    0.299228    805  HOH B O   
10553 O  O   . HOH R .   ? 0.917981  0.439088 0.365532 0.11591     0.0608056   0.125529    806  HOH B O   
10554 O  O   . HOH R .   ? 0.886248  0.331398 0.309063 0.109231    0.0781504   0.137196    807  HOH B O   
10555 O  O   . HOH R .   ? 0.434943  0.462204 0.410352 0.00791585  -0.0318419  -0.0596275  808  HOH B O   
10556 O  O   . HOH R .   ? 0.614124  0.367978 0.484622 0.0523714   0.0308563   -0.0245437  809  HOH B O   
10557 O  O   . HOH R .   ? 0.353504  0.620259 0.525555 0.0209533   -0.0466475  -0.116519   810  HOH B O   
10558 O  O   . HOH R .   ? 0.442311  0.770709 0.584524 0.0867743   0.136307    -0.130443   811  HOH B O   
10559 O  O   . HOH R .   ? 0.794497  0.650997 0.662829 0.128237    0.0414802   -0.118592   812  HOH B O   
10560 O  O   . HOH R .   ? 0.368426  0.625275 0.4988   0.12538     -0.0816634  -0.10579    813  HOH B O   
10561 O  O   . HOH R .   ? 0.405083  0.413316 0.406844 0.00295552  -0.00631181 -0.0210127  814  HOH B O   
10562 O  O   . HOH R .   ? 0.430736  0.461274 0.344348 0.0654424   -0.0624648  -0.0338072  815  HOH B O   
10563 O  O   . HOH R .   ? 0.60637   0.548578 0.42339  0.0852555   0.0440718   -0.122536   816  HOH B O   
10564 O  O   . HOH R .   ? 0.633914  0.481473 0.564093 0.00241176  0.00759792  -0.0312913  817  HOH B O   
10565 O  O   . HOH R .   ? 0.344883  0.343848 0.37301  -0.0540652  0.00957658  -0.0500274  818  HOH B O   
10566 O  O   . HOH R .   ? 0.606971  0.357221 0.479254 -0.00743576 0.0315807   -0.00826248 819  HOH B O   
10567 O  O   . HOH R .   ? 0.406261  0.446818 0.28395  0.0932086   0.0966424   -0.10094    820  HOH B O   
10568 O  O   . HOH R .   ? 0.361078  0.561677 0.482785 0.0799735   -0.0246996  -0.0853908  821  HOH B O   
10569 O  O   . HOH R .   ? 0.44569   0.4935   0.453681 0.067954    0.00674531  -0.0632325  822  HOH B O   
10570 O  O   . HOH R .   ? 0.336185  0.426236 0.328035 0.0584635   -0.0693381  -0.0522856  823  HOH B O   
10571 O  O   . HOH R .   ? 0.302168  0.522347 0.479915 -0.0504393  0.023034    -0.103356   824  HOH B O   
10572 O  O   . HOH R .   ? 0.960265  0.531903 0.501838 0.119156    0.0323937   0.1028      825  HOH B O   
10573 O  O   . HOH R .   ? 0.374473  0.568673 0.37819  0.11225     0.143059    -0.124336   826  HOH B O   
10574 O  O   . HOH R .   ? 0.821499  0.849181 0.579652 0.0995526   -0.100612   -0.0918277  827  HOH B O   
10575 O  O   . HOH R .   ? 0.658431  0.460423 0.507131 0.157098    -0.00335344 0.00234349  828  HOH B O   
10576 O  O   . HOH R .   ? 0.541995  0.586961 0.291733 0.196256    -0.159251   -0.0542805  829  HOH B O   
10577 O  O   . HOH R .   ? 0.522402  0.387293 0.253087 0.0373179   0.051347    0.034117    830  HOH B O   
10578 O  O   . HOH R .   ? 0.361425  0.296251 0.319412 0.0469478   -0.00754994 -0.053194   831  HOH B O   
10579 O  O   . HOH R .   ? 0.289138  0.444391 0.353822 0.0575987   0.0485247   -0.0632427  832  HOH B O   
10580 O  O   . HOH R .   ? 0.45002   0.41042  0.338253 -0.0609224  0.142343    0.00842663  833  HOH B O   
10581 O  O   . HOH R .   ? 0.369827  0.652162 0.517391 0.0289519   -0.0642714  -0.107211   834  HOH B O   
10582 O  O   . HOH R .   ? 0.506892  0.59505  0.554064 0.067909    -0.0128826  -0.0538655  835  HOH B O   
10583 O  O   . HOH R .   ? 0.537362  0.487052 0.211679 0.100358    -0.0430549  -0.0478853  836  HOH B O   
10584 O  O   . HOH R .   ? 0.620107  0.536349 0.600468 -0.0375597  0.013467    -0.0668004  837  HOH B O   
10585 O  O   . HOH R .   ? 0.237554  0.311192 0.241267 0.0233621   -0.036117   -0.034966   838  HOH B O   
10586 O  O   . HOH R .   ? 0.561884  0.414001 0.224403 0.0435091   0.0758298   0.0337718   839  HOH B O   
10587 O  O   . HOH R .   ? 0.889441  0.60486  0.511297 0.134763    0.0225806   0.0867656   840  HOH B O   
10588 O  O   . HOH R .   ? 0.619555  0.431848 0.506337 0.0566282   0.0206859   -0.00253655 841  HOH B O   
10589 O  O   . HOH R .   ? 0.379831  0.345292 0.317593 -0.0483151  0.102401    0.00016337  842  HOH B O   
10590 O  O   . HOH R .   ? 0.440284  0.288023 0.327817 -0.00399953 0.0515669   0.0206986   843  HOH B O   
10591 O  O   . HOH R .   ? 0.557842  0.721024 0.611999 -0.0159717  -0.0880385  -0.157965   844  HOH B O   
10592 O  O   . HOH R .   ? 0.417597  0.487422 0.354063 0.010162    -0.0832556  -0.146018   845  HOH B O   
10593 O  O   . HOH R .   ? 0.296121  0.447869 0.394197 -0.0182898  -0.0400312  -0.0974087  846  HOH B O   
10594 O  O   . HOH R .   ? 0.537803  0.892519 0.601789 0.150318    -0.202351   -0.178812   847  HOH B O   
10595 O  O   . HOH R .   ? 1.83064   0.907051 0.715487 0.183106    0.179032    0.26146     848  HOH B O   
10596 O  O   . HOH R .   ? 0.36948   0.41498  0.38766  -0.0233828  -0.0294767  -0.0757624  849  HOH B O   
10597 O  O   . HOH R .   ? 0.6584    0.713394 0.64948  0.197065    -0.0764358  -0.0590875  850  HOH B O   
10598 O  O   . HOH R .   ? 0.451118  0.388438 0.386905 -0.0170483  -0.0194952  -0.126033   851  HOH B O   
10599 O  O   . HOH R .   ? 0.655121  0.339998 0.48177  0.0351517   0.0233171   -0.00510886 852  HOH B O   
10600 O  O   . HOH R .   ? 0.373443  0.392207 0.293003 0.107072    -0.0741851  -0.0216303  853  HOH B O   
10601 O  O   . HOH R .   ? 0.361835  0.314604 0.268548 0.00147347  0.0326516   0.010319    854  HOH B O   
10602 O  O   . HOH R .   ? 0.477249  0.486381 0.469391 -0.00874066 -0.019709   -0.0633239  855  HOH B O   
10603 O  O   . HOH R .   ? 0.355529  0.738205 0.594335 -0.0307499  0.130189    -0.12287    856  HOH B O   
10604 O  O   . HOH R .   ? 0.493562  0.448327 0.453188 -0.0251676  -0.0190008  -0.115095   857  HOH B O   
10605 O  O   . HOH R .   ? 0.565127  0.471229 0.332901 0.175652    -0.0570667  0.0330282   858  HOH B O   
10606 O  O   . HOH R .   ? 0.462622  0.606716 0.603733 -0.110249   0.0569153   -0.0844803  859  HOH B O   
10607 O  O   . HOH R .   ? 0.696515  0.588234 0.434471 0.0750432   -0.00667444 0.0199294   860  HOH B O   
10608 O  O   . HOH R .   ? 0.274621  0.235524 0.212879 0.0619124   -0.0305695  -0.00369995 861  HOH B O   
10609 O  O   . HOH R .   ? 0.373172  0.514844 0.405482 0.102474    -0.0576838  -0.0419813  862  HOH B O   
10610 O  O   . HOH R .   ? 0.41062   0.406896 0.35271  0.0914983   0.0396839   -0.077342   863  HOH B O   
10611 O  O   . HOH R .   ? 0.284586  0.277219 0.279181 -0.00608381 6.539e-05   -0.0117835  864  HOH B O   
10612 O  O   . HOH R .   ? 0.602921  0.411905 0.470957 0.100472    0.0311065   -0.102443   865  HOH B O   
10613 O  O   . HOH R .   ? 0.219235  0.430844 0.359129 -0.010627   0.0182971   -0.0700475  866  HOH B O   
10614 O  O   . HOH R .   ? 0.518472  0.507912 0.366842 0.0954664   -0.068131   -0.0163928  867  HOH B O   
10615 O  O   . HOH R .   ? 0.309089  0.429966 0.362784 0.101538    0.00490217  -0.0548262  868  HOH B O   
10616 O  O   . HOH R .   ? 0.308781  0.582015 0.499608 0.00972232  -0.0111184  -0.111773   869  HOH B O   
10617 O  O   . HOH R .   ? 0.616543  0.540106 0.426398 -0.00246424 0.106529    0.0211049   870  HOH B O   
10618 O  O   . HOH R .   ? 0.405795  0.578764 0.491178 0.10648     0.0132978   -0.0695784  871  HOH B O   
10619 O  O   . HOH R .   ? 0.227814  0.247934 0.234232 -0.00471909 0.0100138   -0.0132823  872  HOH B O   
10620 O  O   . HOH R .   ? 0.575642  0.447134 0.331833 0.184559    -0.0505429  0.040406    873  HOH B O   
10621 O  O   . HOH R .   ? 0.606252  0.438945 0.529552 -0.0973608  0.0937839   -0.00371925 874  HOH B O   
10622 O  O   . HOH R .   ? 0.583025  0.603931 0.462151 0.0271702   -0.0640341  -0.126444   875  HOH B O   
10623 O  O   . HOH R .   ? 0.646708  0.476467 0.499507 0.204228    -0.0180187  -0.0047842  876  HOH B O   
10624 O  O   . HOH R .   ? 0.376633  0.279952 0.30649  -0.00541975 0.0183458   0.00567923  877  HOH B O   
10625 O  O   . HOH R .   ? 0.27214   0.577735 0.478222 -0.0360122  0.0732427   -0.099932   878  HOH B O   
10626 O  O   . HOH R .   ? 0.421117  0.44364  0.424001 0.0238012   -0.00415353 -0.0149041  879  HOH B O   
10627 O  O   . HOH R .   ? 0.669787  0.805145 0.503727 0.137724    -0.167167   -0.118121   880  HOH B O   
10628 O  O   . HOH R .   ? 0.689103  0.570842 0.369993 0.0970759   0.0128182   0.0366785   881  HOH B O   
10629 O  O   . HOH R .   ? 0.690925  0.401474 0.4659   0.176034    -0.0336651  0.0122623   882  HOH B O   
10630 O  O   . HOH R .   ? 0.256555  0.310176 0.271451 0.00912576  -0.0288822  -0.0400846  883  HOH B O   
10631 O  O   . HOH R .   ? 0.455765  0.272131 0.352857 0.00981231  0.0154978   -0.00405401 884  HOH B O   
10632 O  O   . HOH R .   ? 0.400629  0.547935 0.486786 -0.032216   0.0790542   -0.0601452  885  HOH B O   
10633 O  O   . HOH R .   ? 0.349323  0.372567 0.304024 0.017433    0.0160735   -0.018758   886  HOH B O   
10634 O  O   . HOH R .   ? 0.529326  0.74348  0.548388 0.248872    -0.115723   -0.066627   887  HOH B O   
10635 O  O   . HOH R .   ? 0.378707  0.499689 0.284774 0.168106    -0.114153   -0.0382504  888  HOH B O   
10636 O  O   . HOH R .   ? 0.254554  0.227721 0.230158 -0.00511313 0.018822    -0.00317788 889  HOH B O   
10637 O  O   . HOH R .   ? 0.37145   0.543826 0.491937 -0.0366233  0.0638646   -0.0710738  890  HOH B O   
10638 O  O   . HOH R .   ? 0.409076  0.483484 0.437612 0.0964536   0.00563945  -0.0774013  891  HOH B O   
10639 O  O   . HOH R .   ? 0.44535   0.360331 0.369163 0.0737768   -0.0252365  -0.00511381 892  HOH B O   
10640 O  O   . HOH R .   ? 0.450811  0.425627 0.422846 0.0634531   -0.00348856 -0.016255   893  HOH B O   
10641 O  O   . HOH R .   ? 0.368827  0.287517 0.203596 0.0414282   0.0255746   0.0265847   894  HOH B O   
10642 O  O   . HOH R .   ? 0.542943  0.63176  0.559376 0.198765    -0.0295114  -0.0558543  895  HOH B O   
10643 O  O   . HOH R .   ? 0.413369  0.558198 0.551836 -0.0980915  0.0331741   -0.0897317  896  HOH B O   
10644 O  O   . HOH R .   ? 1.17882   0.496025 0.553691 -0.217071   0.439494    0.156749    897  HOH B O   
10645 O  O   . HOH R .   ? 0.308209  0.565922 0.501652 -0.0617305  0.0111457   -0.10852    898  HOH B O   
10646 O  O   . HOH R .   ? 0.829523  0.474346 0.676078 -0.00536486 0.056176    -0.0697305  899  HOH B O   
10647 O  O   . HOH R .   ? 0.396308  0.29315  0.303516 0.148492    -0.0442957  -0.0216981  900  HOH B O   
10648 O  O   . HOH R .   ? 0.531743  0.70853  0.68612  -0.0870016  -0.0248756  -0.155551   901  HOH B O   
10649 O  O   . HOH R .   ? 0.174223  0.230154 0.202085 0.0391119   -0.0123216  -0.0347773  902  HOH B O   
10650 O  O   . HOH R .   ? 0.269528  0.282463 0.127824 0.047505    0.0125066   -0.0550169  903  HOH B O   
10651 O  O   . HOH R .   ? 0.441482  0.457384 0.42561  -0.0224792  -0.0364143  -0.112224   904  HOH B O   
10652 O  O   . HOH R .   ? 0.525042  0.497171 0.497171 0.050368    0.00469573  -0.029248   905  HOH B O   
10653 O  O   . HOH R .   ? 0.303023  0.222607 0.256542 -0.0194946  0.0378672   -0.00136632 906  HOH B O   
10654 O  O   . HOH R .   ? 0.375577  0.516544 0.330963 0.101997    0.134857    -0.113005   907  HOH B O   
10655 O  O   . HOH R .   ? 0.621752  0.440397 0.430231 0.0737878   -0.00768209 0.0337299   908  HOH B O   
10656 O  O   . HOH R .   ? 0.334036  0.220843 0.258185 0.095714    -0.0218256  -0.0252891  909  HOH B O   
10657 O  O   . HOH R .   ? 0.297167  0.248126 0.268964 0.0273131   -0.00995553 -0.0289688  910  HOH B O   
10658 O  O   . HOH R .   ? 0.38633   0.309378 0.322635 0.114997    -0.0331511  -0.0262012  911  HOH B O   
10659 O  O   . HOH R .   ? 0.500977  0.526686 0.426984 0.0467693   -0.0482046  -0.0339465  912  HOH B O   
10660 O  O   . HOH R .   ? 0.620681  0.682273 0.549083 0.256396    -0.130659   -0.0526687  913  HOH B O   
10661 O  O   . HOH R .   ? 0.62191   0.562801 0.424473 0.0519971   -0.00970294 -0.133856   914  HOH B O   
10662 O  O   . HOH R .   ? 0.416477  0.384585 0.249376 0.0754328   0.0461876   -0.100685   915  HOH B O   
10663 O  O   . HOH R .   ? 0.365075  0.419146 0.396086 0.00821777  -0.00745705 -0.0249934  916  HOH B O   
10664 O  O   . HOH R .   ? 0.50016   0.530165 0.486791 0.0294165   0.0143404   -0.0283403  917  HOH B O   
10665 O  O   . HOH R .   ? 0.534299  0.588118 0.511565 0.266998    -0.0481022  -0.05454    918  HOH B O   
10666 O  O   . HOH R .   ? 0.550436  0.886906 0.52705  0.202879    -0.242054   -0.178225   919  HOH B O   
10667 O  O   . HOH R .   ? 0.351988  0.359796 0.268833 0.0230454   0.0211388   -0.0132222  920  HOH B O   
10668 O  O   . HOH R .   ? 0.317682  0.353668 0.31405  0.00660193  0.0159198   -0.0150001  921  HOH B O   
10669 O  O   . HOH R .   ? 0.350899  0.380516 0.254584 0.0825321   -0.04925    -0.0100636  922  HOH B O   
10670 O  O   . HOH R .   ? 0.441432  0.511833 0.370077 0.116331    0.0968533   -0.11132    923  HOH B O   
10671 O  O   . HOH R .   ? 0.579044  0.486841 0.52917  0.0258161   0.0102357   -0.0278527  924  HOH B O   
10672 O  O   . HOH R .   ? 0.362999  0.310854 0.328916 0.0148371   0.0074791   -0.00620703 925  HOH B O   
10673 O  O   . HOH R .   ? 0.578681  0.397492 0.383752 0.0999933   -0.0234936  0.0301762   926  HOH B O   
10674 O  O   . HOH R .   ? 0.249734  0.373006 0.2559   0.10556     -0.0642833  -0.0361183  927  HOH B O   
10675 O  O   . HOH R .   ? 0.328211  0.378817 0.244598 0.052849    -0.0470879  -0.0359886  928  HOH B O   
10676 O  O   . HOH R .   ? 0.46193   0.326092 0.380751 -0.0183867  0.049688    0.00687226  929  HOH B O   
10677 O  O   . HOH R .   ? 0.44101   0.542689 0.475362 0.167232    -0.011012   -0.0613498  930  HOH B O   
10678 O  O   . HOH R .   ? 0.49754   0.391362 0.339512 -0.00809859 0.0651202   0.0274507   931  HOH B O   
10679 O  O   . HOH R .   ? 0.491499  0.422596 0.240323 0.134809    -0.0449479  0.0249103   932  HOH B O   
10680 O  O   . HOH R .   ? 0.472207  0.451006 0.459608 0.00776237  0.00117559  -0.0157927  933  HOH B O   
10681 O  O   . HOH R .   ? 0.377379  0.305202 0.173631 0.114329    -0.0320205  0.0267599   934  HOH B O   
10682 O  O   . HOH R .   ? 0.401607  0.434122 0.407147 0.0276149   0.00101767  -0.0198113  935  HOH B O   
10683 O  O   . HOH R .   ? 0.629197  0.455555 0.588153 -0.122038   0.113485    -0.0322069  936  HOH B O   
10684 O  O   . HOH R .   ? 0.39273   0.672339 0.590959 -0.0178122  -0.0330423  -0.132542   937  HOH B O   
10685 O  O   . HOH R .   ? 0.274065  0.328859 0.236648 0.0272793   -0.038393   -0.0436943  938  HOH B O   
10686 O  O   . HOH R .   ? 0.297487  0.412125 0.327285 0.0288731   0.0515921   -0.0608908  939  HOH B O   
10687 O  O   . HOH R .   ? 0.295901  0.312361 0.239044 0.0123049   0.0357118   -0.0155617  940  HOH B O   
10688 O  O   . HOH R .   ? 0.19594   0.335049 0.286322 0.0197816   -0.00221339 -0.0578091  941  HOH B O   
10689 O  O   . HOH R .   ? 0.629118  0.501822 0.474828 -0.0288049  0.0834361   0.0302275   942  HOH B O   
10690 O  O   . HOH R .   ? 0.319555  0.322917 0.332674 -0.0163785  0.00367225  -0.0290471  943  HOH B O   
10691 O  O   . HOH R .   ? 0.482311  0.478385 0.465261 0.0225901   -0.00016882 -0.0254758  944  HOH B O   
10692 O  O   . HOH R .   ? 0.68283   0.503862 0.35691  0.0856495   0.0371763   0.0597527   945  HOH B O   
10693 O  O   . HOH R .   ? 0.579292  0.581454 0.564862 -0.0071114  -0.0223646  -0.0665273  946  HOH B O   
10694 O  O   . HOH R .   ? 0.362532  0.35171  0.277971 0.0902522   0.047603    -0.088151   947  HOH B O   
10695 O  O   . HOH R .   ? 0.314347  0.336366 0.315554 0.00696239  -0.0134582  -0.0224575  948  HOH B O   
10696 O  O   . HOH R .   ? 0.300003  0.549921 0.410397 0.156617    -0.0557101  -0.0793893  949  HOH B O   
10697 O  O   . HOH R .   ? 0.668512  0.497462 0.583561 -0.00105876 0.0360216   -0.00963017 950  HOH B O   
10698 O  O   . HOH R .   ? 0.364927  0.366633 0.30415  0.0722562   0.0366992   -0.0687137  951  HOH B O   
10699 O  O   . HOH R .   ? 0.301302  0.332364 0.278476 0.0285985   0.00615826  -0.0403927  952  HOH B O   
10700 O  O   . HOH R .   ? 0.644908  0.80726  0.602605 0.0165209   0.186967    -0.075392   953  HOH B O   
10701 O  O   . HOH R .   ? 0.225631  0.247743 0.214071 0.0233811   -0.0133515  -0.00729077 954  HOH B O   
10702 O  O   . HOH R .   ? 0.269237  0.319669 0.295068 0.00590645  0.00061108  -0.0230072  955  HOH B O   
10703 O  O   . HOH R .   ? 0.615345  0.353944 0.497643 -0.0879476  0.114928    -0.0009766  956  HOH B O   
10704 O  O   . HOH R .   ? 0.519982  0.359397 0.433423 0.0738693   -0.00547983 -0.0556966  957  HOH B O   
10705 O  O   . HOH R .   ? 0.617301  0.627352 0.445527 0.0356727   0.0788302   -0.0330377  958  HOH B O   
10706 O  O   . HOH R .   ? 0.973501  0.59457  0.764097 -0.234562   0.273511    0.0284348   959  HOH B O   
10707 O  O   . HOH R .   ? 0.323769  0.362527 0.29651  0.0157186   0.0244112   -0.0261042  960  HOH B O   
10708 O  O   . HOH R .   ? 0.498301  0.518959 0.516008 -0.0123225  -0.0076732  -0.0380575  961  HOH B O   
10709 O  O   . HOH R .   ? 0.362231  0.435397 0.365683 0.0138574   -0.03805    -0.0468422  962  HOH B O   
10710 O  O   . HOH R .   ? 0.326051  0.410271 0.336854 0.0229574   -0.0522803  -0.0599946  963  HOH B O   
10711 O  O   . HOH R .   ? 0.246597  0.215334 0.243227 -0.0190632  0.0119381   -0.0270948  964  HOH B O   
10712 O  O   . HOH R .   ? 0.693779  0.445934 0.514636 0.139551    -0.0244358  0.00157218  965  HOH B O   
10713 O  O   . HOH R .   ? 0.429599  0.431272 0.429095 -0.0114737  -0.0153833  -0.0492142  966  HOH B O   
10714 O  O   . HOH R .   ? 0.429036  0.398918 0.349195 0.0195555   0.00305285  0.00340084  967  HOH B O   
10715 O  O   . HOH R .   ? 0.404262  0.393928 0.230106 0.0799821   0.0681505   -0.0964817  968  HOH B O   
10716 O  O   . HOH R .   ? 0.388194  0.5578   0.401442 0.124072    -0.0871406  -0.052388   969  HOH B O   
10717 O  O   . HOH R .   ? 0.770194  0.519475 0.384675 0.185081    -0.055696   0.060001    970  HOH B O   
10718 O  O   . HOH R .   ? 0.659184  0.373188 0.485547 0.0809228   0.00256065  -0.00268758 971  HOH B O   
10719 O  O   . HOH R .   ? 0.483543  0.399481 0.346249 0.00535363  0.0410568   0.0209602   972  HOH B O   
10720 O  O   . HOH R .   ? 0.7124    0.539354 0.642563 -0.0360775  0.0278779   -0.0282375  973  HOH B O   
10721 O  O   . HOH R .   ? 0.364511  0.387253 0.349021 0.00959076  -0.0222063  -0.0386125  974  HOH B O   
10722 O  O   . HOH R .   ? 0.767733  0.662942 0.355915 0.0887216   0.0429301   -0.0225657  975  HOH B O   
10723 O  O   . HOH R .   ? 0.365222  0.742224 0.633345 -0.0464326  0.0450604   -0.130976   976  HOH B O   
10724 O  O   . HOH R .   ? 0.452599  0.575667 0.515949 0.00342797  -0.0451287  -0.0763617  977  HOH B O   
10725 O  O   . HOH R .   ? 0.413077  0.687954 0.484315 0.0919564   0.160935    -0.128896   978  HOH B O   
10726 O  O   . HOH R .   ? 0.448298  0.470711 0.383992 0.0265702   0.00909064  -0.0293317  979  HOH B O   
10727 O  O   . HOH R .   ? 0.42208   0.314813 0.338765 -0.0171085  0.0338841   0.0112525   980  HOH B O   
10728 O  O   . HOH R .   ? 0.78297   0.685861 0.557994 0.362791    -0.106965   0.00778307  981  HOH B O   
10729 O  O   . HOH R .   ? 0.630202  0.618978 0.552718 0.144429    0.0612565   -0.1137     982  HOH B O   
10730 O  O   . HOH R .   ? 0.714383  0.970994 0.835211 0.0172376   -0.0748228  -0.112623   983  HOH B O   
10731 O  O   . HOH R .   ? 0.476589  0.686324 0.648658 -0.0831229  0.0134404   -0.107134   984  HOH B O   
10732 O  O   . HOH R .   ? 0.379046  0.418482 0.39032  0.00990432  -0.0204828  -0.0263203  985  HOH B O   
10733 O  O   . HOH R .   ? 0.483093  0.403369 0.450791 -0.00831298 0.00137728  -0.0312164  986  HOH B O   
10734 O  O   . HOH R .   ? 0.35044   0.578307 0.533192 -0.0566323  0.0459504   -0.101472   987  HOH B O   
10735 O  O   . HOH R .   ? 0.547965  0.348634 0.428461 -0.108028   0.156871    0.0143541   988  HOH B O   
10736 O  O   . HOH R .   ? 0.42382   0.402805 0.402353 0.139578    -0.0240158  -0.0627178  989  HOH B O   
10737 O  O   . HOH R .   ? 0.415089  0.739119 0.607446 0.00434509  -0.0540439  -0.126857   990  HOH B O   
10738 O  O   . HOH R .   ? 0.256208  0.642447 0.475225 0.132388    -0.025962   -0.122818   991  HOH B O   
10739 O  O   . HOH R .   ? 0.670205  0.539003 0.645665 -0.103775   0.0650914   -0.0387015  992  HOH B O   
10740 O  O   . HOH R .   ? 0.554932  0.522059 0.388926 0.0157603   0.077691    0.00282666  993  HOH B O   
10741 O  O   . HOH R .   ? 0.639681  0.523848 0.484349 0.0354216   0.00948087  0.0264922   994  HOH B O   
10742 O  O   . HOH R .   ? 0.345048  0.426775 0.366929 0.188404    -0.00300238 -0.0696934  995  HOH B O   
10743 O  O   . HOH R .   ? 0.346703  0.373751 0.309727 0.0232185   0.00352787  -0.0316893  996  HOH B O   
10744 O  O   . HOH R .   ? 0.277266  0.312149 0.217369 0.0302028   -0.0264431  -0.0373052  997  HOH B O   
10745 O  O   . HOH R .   ? 0.448374  0.844067 0.712532 0.00069802  0.0175443   -0.130927   998  HOH B O   
10746 O  O   . HOH R .   ? 1.13098   0.573788 0.493162 0.396235    -0.100159   0.111258    999  HOH B O   
10747 O  O   . HOH R .   ? 0.578694  0.502776 0.548684 -0.0391418  -0.0031725  -0.106094   1000 HOH B O   
10748 O  O   . HOH R .   ? 0.386066  0.654888 0.604783 -0.0636627  0.0141448   -0.131515   1001 HOH B O   
10749 O  O   . HOH R .   ? 0.426424  0.506502 0.523767 -0.119744   0.0819614   -0.0629059  1002 HOH B O   
10750 O  O   . HOH R .   ? 0.466769  0.529308 0.492157 0.0491272   0.0437035   -0.0752411  1003 HOH B O   
10751 O  O   . HOH R .   ? 0.731321  0.679901 0.455927 0.293765    -0.164491   -0.0098406  1004 HOH B O   
10752 O  O   . HOH R .   ? 1.11268   0.608095 0.515222 -0.0490414  0.262571    0.140816    1005 HOH B O   
10753 O  O   . HOH R .   ? 0.762109  0.652543 0.527973 0.048173    0.0211141   0.0246616   1006 HOH B O   
10754 O  O   . HOH R .   ? 0.469509  0.333018 0.388401 0.0800779   -0.00263321 -0.0796222  1007 HOH B O   
10755 O  O   . HOH R .   ? 0.575577  0.508419 0.53155  0.00424147  -0.0116581  -0.0759981  1008 HOH B O   
10756 O  O   . HOH R .   ? 0.706824  0.40209  0.375505 0.240209    -0.0287797  0.064985    1009 HOH B O   
10757 O  O   . HOH R .   ? 0.764224  0.632241 0.70362  0.00291897  -0.00176678 -0.0695585  1010 HOH B O   
10758 O  O   . HOH R .   ? 0.474874  0.305894 0.396727 -0.0118594  0.0181331   -0.021162   1011 HOH B O   
10759 O  O   . HOH R .   ? 0.554665  0.560121 0.549878 0.0111203   -0.00527682 -0.0181844  1012 HOH B O   
10760 O  O   . HOH R .   ? 0.391246  0.408283 0.376123 0.02217     0.00415165  -0.0231428  1013 HOH B O   
10761 O  O   . HOH R .   ? 0.824065  0.672979 0.522052 0.0560052   0.0627514   0.0490307   1014 HOH B O   
10762 O  O   . HOH R .   ? 0.490485  0.561632 0.4463   0.0426412   -0.0505832  -0.0424462  1015 HOH B O   
10763 O  O   . HOH R .   ? 0.512445  0.473199 0.297067 0.0499182   0.0367745   -0.00192503 1016 HOH B O   
10764 O  O   . HOH R .   ? 0.851284  0.423883 0.648007 0.0352932   0.0623367   -0.0498227  1017 HOH B O   
10765 O  O   . HOH R .   ? 0.620243  0.441854 0.486753 0.139541    -0.0322148  -0.0113278  1018 HOH B O   
10766 O  O   . HOH R .   ? 0.455828  0.489905 0.40643  0.0242736   0.0241804   -0.0328466  1019 HOH B O   
10767 O  O   . HOH R .   ? 0.403882  0.62918  0.568078 -0.0501043  0.0786501   -0.0919403  1020 HOH B O   
10768 O  O   . HOH R .   ? 0.738914  0.689163 0.575648 -0.0203719  0.130555    0.0107867   1021 HOH B O   
10769 O  O   . HOH R .   ? 0.61996   0.584861 0.421795 0.0333377   0.0640575   -0.00148293 1022 HOH B O   
10770 O  O   . HOH R .   ? 0.714172  0.543716 0.515616 0.00579114  0.0548461   0.0416079   1023 HOH B O   
10771 O  O   . HOH R .   ? 0.479636  0.481533 0.481971 -0.00484711 -0.00565111 -0.0315503  1024 HOH B O   
10772 O  O   . HOH R .   ? 0.528551  0.622495 0.572676 0.117331    -0.0005388  -0.08488    1025 HOH B O   
10773 O  O   . HOH R .   ? 0.630043  0.479194 0.532425 0.119129    -0.0225393  -0.0301464  1026 HOH B O   
10774 O  O   . HOH R .   ? 0.42071   0.508096 0.333182 0.112345    0.118883    -0.116202   1027 HOH B O   
10775 O  O   . HOH R .   ? 0.468737  0.48954  0.424801 0.0293118   0.00068656  -0.0461456  1028 HOH B O   
10776 O  O   . HOH R .   ? 0.596357  0.643479 0.643878 -0.0665178  -0.0286752  -0.138174   1029 HOH B O   
10777 O  O   . HOH R .   ? 0.453046  0.870843 0.63217  0.368928    -0.0997698  -0.15049    1030 HOH B O   
10778 O  O   . HOH R .   ? 0.416472  0.770381 0.664483 -0.012804   0.0682356   -0.136067   1031 HOH B O   
# 
