data_9MGP
# 
_entry.id   9MGP 
# 
_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   9MGP         pdb_00009mgp 10.2210/pdb9mgp/pdb 
WWPDB D_1000290926 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-05 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9MGP 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              dwhittington@tangotx.com 
_pdbx_contact_author.name_first         Douglas 
_pdbx_contact_author.name_last          Whittington 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5946-8543 
# 
_audit_author.name               'Whittington, D.A.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-5946-8543 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                4217 
_citation.page_last                 4236 
_citation.title                     'MTA-Cooperative PRMT5 Inhibitors: Mechanism Switching Through Structure-Based Design.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c01998 
_citation.pdbx_database_id_PubMed   39919252 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cottrell, K.M.'    1  0009-0008-6511-0696 
primary 'Whittington, D.A.' 2  0000-0002-5946-8543 
primary 'Briggs, K.J.'      3  ?                   
primary 'Jahic, H.'         4  ?                   
primary 'Ali, J.A.'         5  ?                   
primary 'Amor, A.J.'        6  ?                   
primary 'Gotur, D.'         7  ?                   
primary 'Tonini, M.R.'      8  ?                   
primary 'Zhang, W.'         9  ?                   
primary 'Huang, A.'         10 ?                   
primary 'Maxwell, J.P.'     11 0000-0002-5969-6490 
# 
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 'Protein arginine N-methyltransferase 5' 73763.625 1   2.1.1.320 ? 'FULL LENGTH' 'N-terminal Flag tag'  
2 polymer     man 'Methylosome protein 50' 37862.406 1   ?         ? ?             'N-terminal His-8 tag' 
3 non-polymer syn "5'-DEOXY-5'-METHYLTHIOADENOSINE" 297.334   1   ?         ? ?             ?                      
4 non-polymer syn 
;[2-(cyclobutylamino)pyridin-4-yl][(3R,4R)-3-hydroxy-4-{6-[(1-methyl-1H-pyrazol-5-yl)methyl]-3,4-dihydroisoquinolin-2(1H)-yl}piperidin-1-yl]methanone
;
500.635   1   ?         ? ?             ?                      
5 non-polymer syn 1,2-ETHANEDIOL 62.068    16  ?         ? ?             ?                      
6 non-polymer syn 'SODIUM ION' 22.990    4   ?         ? ?             ?                      
7 non-polymer syn GLYCEROL 92.094    1   ?         ? ?             ?                      
8 non-polymer syn 'CHLORIDE ION' 35.453    1   ?         ? ?             ?                      
9 water       nat water 18.015    113 ?         ? ?             ?                      
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 
;72 kDa ICln-binding protein,Histone-arginine N-methyltransferase PRMT5,Jak-binding protein 1,Shk1 kinase-binding protein 1 homolog,SKB1Hs
;
2 'MEP-50,Androgen receptor cofactor p44,WD repeat-containing protein 77,Methylosome protein WDR77,p44/Mep50' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MDYKDDDDKAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLL
LSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFW
MRVPLVAPEDLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILP
TSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPL
QPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLMVLGAGRGPLVNASLRAAKQADRRIKLYAVE
KNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFL
APISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFA
GYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRS
YTIGL
;
;MDYKDDDDKAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLL
LSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFW
MRVPLVAPEDLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILP
TSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPL
QPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLMVLGAGRGPLVNASLRAAKQADRRIKLYAVE
KNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFL
APISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFA
GYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRS
YTIGL
;
A ? 
2 'polypeptide(L)' no no 
;MHHHHHHHHRKETPPPLVPPAAREWNLPPNAPACMERQLEAARYRSDGALLLGASSLSGRCWAGSLWLFKDPCAAPNEGF
CSAGVQTEAGVADLTWVGERGILVASDSGAVELWELDENETLIVSKFCKYEHDDIVSTVSVLSSGTQAVSGSKDICIKVW
DLAQQVVLSSYRAHAAQVTCVAASPHKDSVFLSCSEDNRILLWDTRCPKPASQIGCSAPGYLPTSLAWHPQQSEVFVFGD
ENGTVSLVDTKSTSCVLSSAVHSQCVTGLVFSPHSVPFLASLSEDCSLAVLDSSLSELFRSQAHRDFVRDATWSPLNHSL
LTTVGWDHQVVHHVVPTEPLPAPGPASVTE
;
;MHHHHHHHHRKETPPPLVPPAAREWNLPPNAPACMERQLEAARYRSDGALLLGASSLSGRCWAGSLWLFKDPCAAPNEGF
CSAGVQTEAGVADLTWVGERGILVASDSGAVELWELDENETLIVSKFCKYEHDDIVSTVSVLSSGTQAVSGSKDICIKVW
DLAQQVVLSSYRAHAAQVTCVAASPHKDSVFLSCSEDNRILLWDTRCPKPASQIGCSAPGYLPTSLAWHPQQSEVFVFGD
ENGTVSLVDTKSTSCVLSSAVHSQCVTGLVFSPHSVPFLASLSEDCSLAVLDSSLSELFRSQAHRDFVRDATWSPLNHSL
LTTVGWDHQVVHHVVPTEPLPAPGPASVTE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 "5'-DEOXY-5'-METHYLTHIOADENOSINE" MTA   
4 
;[2-(cyclobutylamino)pyridin-4-yl][(3R,4R)-3-hydroxy-4-{6-[(1-methyl-1H-pyrazol-5-yl)methyl]-3,4-dihydroisoquinolin-2(1H)-yl}piperidin-1-yl]methanone
;
A1BLI 
5 1,2-ETHANEDIOL EDO   
6 'SODIUM ION' NA    
7 GLYCEROL GOL   
8 'CHLORIDE ION' CL    
9 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASP n 
1 3   TYR n 
1 4   LYS n 
1 5   ASP n 
1 6   ASP n 
1 7   ASP n 
1 8   ASP n 
1 9   LYS n 
1 10  ALA n 
1 11  ALA n 
1 12  MET n 
1 13  ALA n 
1 14  VAL n 
1 15  GLY n 
1 16  GLY n 
1 17  ALA n 
1 18  GLY n 
1 19  GLY n 
1 20  SER n 
1 21  ARG n 
1 22  VAL n 
1 23  SER n 
1 24  SER n 
1 25  GLY n 
1 26  ARG n 
1 27  ASP n 
1 28  LEU n 
1 29  ASN n 
1 30  CYS n 
1 31  VAL n 
1 32  PRO n 
1 33  GLU n 
1 34  ILE n 
1 35  ALA n 
1 36  ASP n 
1 37  THR n 
1 38  LEU n 
1 39  GLY n 
1 40  ALA n 
1 41  VAL n 
1 42  ALA n 
1 43  LYS n 
1 44  GLN n 
1 45  GLY n 
1 46  PHE n 
1 47  ASP n 
1 48  PHE n 
1 49  LEU n 
1 50  CYS n 
1 51  MET n 
1 52  PRO n 
1 53  VAL n 
1 54  PHE n 
1 55  HIS n 
1 56  PRO n 
1 57  ARG n 
1 58  PHE n 
1 59  LYS n 
1 60  ARG n 
1 61  GLU n 
1 62  PHE n 
1 63  ILE n 
1 64  GLN n 
1 65  GLU n 
1 66  PRO n 
1 67  ALA n 
1 68  LYS n 
1 69  ASN n 
1 70  ARG n 
1 71  PRO n 
1 72  GLY n 
1 73  PRO n 
1 74  GLN n 
1 75  THR n 
1 76  ARG n 
1 77  SER n 
1 78  ASP n 
1 79  LEU n 
1 80  LEU n 
1 81  LEU n 
1 82  SER n 
1 83  GLY n 
1 84  ARG n 
1 85  ASP n 
1 86  TRP n 
1 87  ASN n 
1 88  THR n 
1 89  LEU n 
1 90  ILE n 
1 91  VAL n 
1 92  GLY n 
1 93  LYS n 
1 94  LEU n 
1 95  SER n 
1 96  PRO n 
1 97  TRP n 
1 98  ILE n 
1 99  ARG n 
1 100 PRO n 
1 101 ASP n 
1 102 SER n 
1 103 LYS n 
1 104 VAL n 
1 105 GLU n 
1 106 LYS n 
1 107 ILE n 
1 108 ARG n 
1 109 ARG n 
1 110 ASN n 
1 111 SER n 
1 112 GLU n 
1 113 ALA n 
1 114 ALA n 
1 115 MET n 
1 116 LEU n 
1 117 GLN n 
1 118 GLU n 
1 119 LEU n 
1 120 ASN n 
1 121 PHE n 
1 122 GLY n 
1 123 ALA n 
1 124 TYR n 
1 125 LEU n 
1 126 GLY n 
1 127 LEU n 
1 128 PRO n 
1 129 ALA n 
1 130 PHE n 
1 131 LEU n 
1 132 LEU n 
1 133 PRO n 
1 134 LEU n 
1 135 ASN n 
1 136 GLN n 
1 137 GLU n 
1 138 ASP n 
1 139 ASN n 
1 140 THR n 
1 141 ASN n 
1 142 LEU n 
1 143 ALA n 
1 144 ARG n 
1 145 VAL n 
1 146 LEU n 
1 147 THR n 
1 148 ASN n 
1 149 HIS n 
1 150 ILE n 
1 151 HIS n 
1 152 THR n 
1 153 GLY n 
1 154 HIS n 
1 155 HIS n 
1 156 SER n 
1 157 SER n 
1 158 MET n 
1 159 PHE n 
1 160 TRP n 
1 161 MET n 
1 162 ARG n 
1 163 VAL n 
1 164 PRO n 
1 165 LEU n 
1 166 VAL n 
1 167 ALA n 
1 168 PRO n 
1 169 GLU n 
1 170 ASP n 
1 171 LEU n 
1 172 ARG n 
1 173 ASP n 
1 174 ASP n 
1 175 ILE n 
1 176 ILE n 
1 177 GLU n 
1 178 ASN n 
1 179 ALA n 
1 180 PRO n 
1 181 THR n 
1 182 THR n 
1 183 HIS n 
1 184 THR n 
1 185 GLU n 
1 186 GLU n 
1 187 TYR n 
1 188 SER n 
1 189 GLY n 
1 190 GLU n 
1 191 GLU n 
1 192 LYS n 
1 193 THR n 
1 194 TRP n 
1 195 MET n 
1 196 TRP n 
1 197 TRP n 
1 198 HIS n 
1 199 ASN n 
1 200 PHE n 
1 201 ARG n 
1 202 THR n 
1 203 LEU n 
1 204 CYS n 
1 205 ASP n 
1 206 TYR n 
1 207 SER n 
1 208 LYS n 
1 209 ARG n 
1 210 ILE n 
1 211 ALA n 
1 212 VAL n 
1 213 ALA n 
1 214 LEU n 
1 215 GLU n 
1 216 ILE n 
1 217 GLY n 
1 218 ALA n 
1 219 ASP n 
1 220 LEU n 
1 221 PRO n 
1 222 SER n 
1 223 ASN n 
1 224 HIS n 
1 225 VAL n 
1 226 ILE n 
1 227 ASP n 
1 228 ARG n 
1 229 TRP n 
1 230 LEU n 
1 231 GLY n 
1 232 GLU n 
1 233 PRO n 
1 234 ILE n 
1 235 LYS n 
1 236 ALA n 
1 237 ALA n 
1 238 ILE n 
1 239 LEU n 
1 240 PRO n 
1 241 THR n 
1 242 SER n 
1 243 ILE n 
1 244 PHE n 
1 245 LEU n 
1 246 THR n 
1 247 ASN n 
1 248 LYS n 
1 249 LYS n 
1 250 GLY n 
1 251 PHE n 
1 252 PRO n 
1 253 VAL n 
1 254 LEU n 
1 255 SER n 
1 256 LYS n 
1 257 MET n 
1 258 HIS n 
1 259 GLN n 
1 260 ARG n 
1 261 LEU n 
1 262 ILE n 
1 263 PHE n 
1 264 ARG n 
1 265 LEU n 
1 266 LEU n 
1 267 LYS n 
1 268 LEU n 
1 269 GLU n 
1 270 VAL n 
1 271 GLN n 
1 272 PHE n 
1 273 ILE n 
1 274 ILE n 
1 275 THR n 
1 276 GLY n 
1 277 THR n 
1 278 ASN n 
1 279 HIS n 
1 280 HIS n 
1 281 SER n 
1 282 GLU n 
1 283 LYS n 
1 284 GLU n 
1 285 PHE n 
1 286 CYS n 
1 287 SER n 
1 288 TYR n 
1 289 LEU n 
1 290 GLN n 
1 291 TYR n 
1 292 LEU n 
1 293 GLU n 
1 294 TYR n 
1 295 LEU n 
1 296 SER n 
1 297 GLN n 
1 298 ASN n 
1 299 ARG n 
1 300 PRO n 
1 301 PRO n 
1 302 PRO n 
1 303 ASN n 
1 304 ALA n 
1 305 TYR n 
1 306 GLU n 
1 307 LEU n 
1 308 PHE n 
1 309 ALA n 
1 310 LYS n 
1 311 GLY n 
1 312 TYR n 
1 313 GLU n 
1 314 ASP n 
1 315 TYR n 
1 316 LEU n 
1 317 GLN n 
1 318 SER n 
1 319 PRO n 
1 320 LEU n 
1 321 GLN n 
1 322 PRO n 
1 323 LEU n 
1 324 MET n 
1 325 ASP n 
1 326 ASN n 
1 327 LEU n 
1 328 GLU n 
1 329 SER n 
1 330 GLN n 
1 331 THR n 
1 332 TYR n 
1 333 GLU n 
1 334 VAL n 
1 335 PHE n 
1 336 GLU n 
1 337 LYS n 
1 338 ASP n 
1 339 PRO n 
1 340 ILE n 
1 341 LYS n 
1 342 TYR n 
1 343 SER n 
1 344 GLN n 
1 345 TYR n 
1 346 GLN n 
1 347 GLN n 
1 348 ALA n 
1 349 ILE n 
1 350 TYR n 
1 351 LYS n 
1 352 CYS n 
1 353 LEU n 
1 354 LEU n 
1 355 ASP n 
1 356 ARG n 
1 357 VAL n 
1 358 PRO n 
1 359 GLU n 
1 360 GLU n 
1 361 GLU n 
1 362 LYS n 
1 363 ASP n 
1 364 THR n 
1 365 ASN n 
1 366 VAL n 
1 367 GLN n 
1 368 VAL n 
1 369 LEU n 
1 370 MET n 
1 371 VAL n 
1 372 LEU n 
1 373 GLY n 
1 374 ALA n 
1 375 GLY n 
1 376 ARG n 
1 377 GLY n 
1 378 PRO n 
1 379 LEU n 
1 380 VAL n 
1 381 ASN n 
1 382 ALA n 
1 383 SER n 
1 384 LEU n 
1 385 ARG n 
1 386 ALA n 
1 387 ALA n 
1 388 LYS n 
1 389 GLN n 
1 390 ALA n 
1 391 ASP n 
1 392 ARG n 
1 393 ARG n 
1 394 ILE n 
1 395 LYS n 
1 396 LEU n 
1 397 TYR n 
1 398 ALA n 
1 399 VAL n 
1 400 GLU n 
1 401 LYS n 
1 402 ASN n 
1 403 PRO n 
1 404 ASN n 
1 405 ALA n 
1 406 VAL n 
1 407 VAL n 
1 408 THR n 
1 409 LEU n 
1 410 GLU n 
1 411 ASN n 
1 412 TRP n 
1 413 GLN n 
1 414 PHE n 
1 415 GLU n 
1 416 GLU n 
1 417 TRP n 
1 418 GLY n 
1 419 SER n 
1 420 GLN n 
1 421 VAL n 
1 422 THR n 
1 423 VAL n 
1 424 VAL n 
1 425 SER n 
1 426 SER n 
1 427 ASP n 
1 428 MET n 
1 429 ARG n 
1 430 GLU n 
1 431 TRP n 
1 432 VAL n 
1 433 ALA n 
1 434 PRO n 
1 435 GLU n 
1 436 LYS n 
1 437 ALA n 
1 438 ASP n 
1 439 ILE n 
1 440 ILE n 
1 441 VAL n 
1 442 SER n 
1 443 GLU n 
1 444 LEU n 
1 445 LEU n 
1 446 GLY n 
1 447 SER n 
1 448 PHE n 
1 449 ALA n 
1 450 ASP n 
1 451 ASN n 
1 452 GLU n 
1 453 LEU n 
1 454 SER n 
1 455 PRO n 
1 456 GLU n 
1 457 CYS n 
1 458 LEU n 
1 459 ASP n 
1 460 GLY n 
1 461 ALA n 
1 462 GLN n 
1 463 HIS n 
1 464 PHE n 
1 465 LEU n 
1 466 LYS n 
1 467 ASP n 
1 468 ASP n 
1 469 GLY n 
1 470 VAL n 
1 471 SER n 
1 472 ILE n 
1 473 PRO n 
1 474 GLY n 
1 475 GLU n 
1 476 TYR n 
1 477 THR n 
1 478 SER n 
1 479 PHE n 
1 480 LEU n 
1 481 ALA n 
1 482 PRO n 
1 483 ILE n 
1 484 SER n 
1 485 SER n 
1 486 SER n 
1 487 LYS n 
1 488 LEU n 
1 489 TYR n 
1 490 ASN n 
1 491 GLU n 
1 492 VAL n 
1 493 ARG n 
1 494 ALA n 
1 495 CYS n 
1 496 ARG n 
1 497 GLU n 
1 498 LYS n 
1 499 ASP n 
1 500 ARG n 
1 501 ASP n 
1 502 PRO n 
1 503 GLU n 
1 504 ALA n 
1 505 GLN n 
1 506 PHE n 
1 507 GLU n 
1 508 MET n 
1 509 PRO n 
1 510 TYR n 
1 511 VAL n 
1 512 VAL n 
1 513 ARG n 
1 514 LEU n 
1 515 HIS n 
1 516 ASN n 
1 517 PHE n 
1 518 HIS n 
1 519 GLN n 
1 520 LEU n 
1 521 SER n 
1 522 ALA n 
1 523 PRO n 
1 524 GLN n 
1 525 PRO n 
1 526 CYS n 
1 527 PHE n 
1 528 THR n 
1 529 PHE n 
1 530 SER n 
1 531 HIS n 
1 532 PRO n 
1 533 ASN n 
1 534 ARG n 
1 535 ASP n 
1 536 PRO n 
1 537 MET n 
1 538 ILE n 
1 539 ASP n 
1 540 ASN n 
1 541 ASN n 
1 542 ARG n 
1 543 TYR n 
1 544 CYS n 
1 545 THR n 
1 546 LEU n 
1 547 GLU n 
1 548 PHE n 
1 549 PRO n 
1 550 VAL n 
1 551 GLU n 
1 552 VAL n 
1 553 ASN n 
1 554 THR n 
1 555 VAL n 
1 556 LEU n 
1 557 HIS n 
1 558 GLY n 
1 559 PHE n 
1 560 ALA n 
1 561 GLY n 
1 562 TYR n 
1 563 PHE n 
1 564 GLU n 
1 565 THR n 
1 566 VAL n 
1 567 LEU n 
1 568 TYR n 
1 569 GLN n 
1 570 ASP n 
1 571 ILE n 
1 572 THR n 
1 573 LEU n 
1 574 SER n 
1 575 ILE n 
1 576 ARG n 
1 577 PRO n 
1 578 GLU n 
1 579 THR n 
1 580 HIS n 
1 581 SER n 
1 582 PRO n 
1 583 GLY n 
1 584 MET n 
1 585 PHE n 
1 586 SER n 
1 587 TRP n 
1 588 PHE n 
1 589 PRO n 
1 590 ILE n 
1 591 LEU n 
1 592 PHE n 
1 593 PRO n 
1 594 ILE n 
1 595 LYS n 
1 596 GLN n 
1 597 PRO n 
1 598 ILE n 
1 599 THR n 
1 600 VAL n 
1 601 ARG n 
1 602 GLU n 
1 603 GLY n 
1 604 GLN n 
1 605 THR n 
1 606 ILE n 
1 607 CYS n 
1 608 VAL n 
1 609 ARG n 
1 610 PHE n 
1 611 TRP n 
1 612 ARG n 
1 613 CYS n 
1 614 SER n 
1 615 ASN n 
1 616 SER n 
1 617 LYS n 
1 618 LYS n 
1 619 VAL n 
1 620 TRP n 
1 621 TYR n 
1 622 GLU n 
1 623 TRP n 
1 624 ALA n 
1 625 VAL n 
1 626 THR n 
1 627 ALA n 
1 628 PRO n 
1 629 VAL n 
1 630 CYS n 
1 631 SER n 
1 632 ALA n 
1 633 ILE n 
1 634 HIS n 
1 635 ASN n 
1 636 PRO n 
1 637 THR n 
1 638 GLY n 
1 639 ARG n 
1 640 SER n 
1 641 TYR n 
1 642 THR n 
1 643 ILE n 
1 644 GLY n 
1 645 LEU n 
2 1   MET n 
2 2   HIS n 
2 3   HIS n 
2 4   HIS n 
2 5   HIS n 
2 6   HIS n 
2 7   HIS n 
2 8   HIS n 
2 9   HIS n 
2 10  ARG n 
2 11  LYS n 
2 12  GLU n 
2 13  THR n 
2 14  PRO n 
2 15  PRO n 
2 16  PRO n 
2 17  LEU n 
2 18  VAL n 
2 19  PRO n 
2 20  PRO n 
2 21  ALA n 
2 22  ALA n 
2 23  ARG n 
2 24  GLU n 
2 25  TRP n 
2 26  ASN n 
2 27  LEU n 
2 28  PRO n 
2 29  PRO n 
2 30  ASN n 
2 31  ALA n 
2 32  PRO n 
2 33  ALA n 
2 34  CYS n 
2 35  MET n 
2 36  GLU n 
2 37  ARG n 
2 38  GLN n 
2 39  LEU n 
2 40  GLU n 
2 41  ALA n 
2 42  ALA n 
2 43  ARG n 
2 44  TYR n 
2 45  ARG n 
2 46  SER n 
2 47  ASP n 
2 48  GLY n 
2 49  ALA n 
2 50  LEU n 
2 51  LEU n 
2 52  LEU n 
2 53  GLY n 
2 54  ALA n 
2 55  SER n 
2 56  SER n 
2 57  LEU n 
2 58  SER n 
2 59  GLY n 
2 60  ARG n 
2 61  CYS n 
2 62  TRP n 
2 63  ALA n 
2 64  GLY n 
2 65  SER n 
2 66  LEU n 
2 67  TRP n 
2 68  LEU n 
2 69  PHE n 
2 70  LYS n 
2 71  ASP n 
2 72  PRO n 
2 73  CYS n 
2 74  ALA n 
2 75  ALA n 
2 76  PRO n 
2 77  ASN n 
2 78  GLU n 
2 79  GLY n 
2 80  PHE n 
2 81  CYS n 
2 82  SER n 
2 83  ALA n 
2 84  GLY n 
2 85  VAL n 
2 86  GLN n 
2 87  THR n 
2 88  GLU n 
2 89  ALA n 
2 90  GLY n 
2 91  VAL n 
2 92  ALA n 
2 93  ASP n 
2 94  LEU n 
2 95  THR n 
2 96  TRP n 
2 97  VAL n 
2 98  GLY n 
2 99  GLU n 
2 100 ARG n 
2 101 GLY n 
2 102 ILE n 
2 103 LEU n 
2 104 VAL n 
2 105 ALA n 
2 106 SER n 
2 107 ASP n 
2 108 SER n 
2 109 GLY n 
2 110 ALA n 
2 111 VAL n 
2 112 GLU n 
2 113 LEU n 
2 114 TRP n 
2 115 GLU n 
2 116 LEU n 
2 117 ASP n 
2 118 GLU n 
2 119 ASN n 
2 120 GLU n 
2 121 THR n 
2 122 LEU n 
2 123 ILE n 
2 124 VAL n 
2 125 SER n 
2 126 LYS n 
2 127 PHE n 
2 128 CYS n 
2 129 LYS n 
2 130 TYR n 
2 131 GLU n 
2 132 HIS n 
2 133 ASP n 
2 134 ASP n 
2 135 ILE n 
2 136 VAL n 
2 137 SER n 
2 138 THR n 
2 139 VAL n 
2 140 SER n 
2 141 VAL n 
2 142 LEU n 
2 143 SER n 
2 144 SER n 
2 145 GLY n 
2 146 THR n 
2 147 GLN n 
2 148 ALA n 
2 149 VAL n 
2 150 SER n 
2 151 GLY n 
2 152 SER n 
2 153 LYS n 
2 154 ASP n 
2 155 ILE n 
2 156 CYS n 
2 157 ILE n 
2 158 LYS n 
2 159 VAL n 
2 160 TRP n 
2 161 ASP n 
2 162 LEU n 
2 163 ALA n 
2 164 GLN n 
2 165 GLN n 
2 166 VAL n 
2 167 VAL n 
2 168 LEU n 
2 169 SER n 
2 170 SER n 
2 171 TYR n 
2 172 ARG n 
2 173 ALA n 
2 174 HIS n 
2 175 ALA n 
2 176 ALA n 
2 177 GLN n 
2 178 VAL n 
2 179 THR n 
2 180 CYS n 
2 181 VAL n 
2 182 ALA n 
2 183 ALA n 
2 184 SER n 
2 185 PRO n 
2 186 HIS n 
2 187 LYS n 
2 188 ASP n 
2 189 SER n 
2 190 VAL n 
2 191 PHE n 
2 192 LEU n 
2 193 SER n 
2 194 CYS n 
2 195 SER n 
2 196 GLU n 
2 197 ASP n 
2 198 ASN n 
2 199 ARG n 
2 200 ILE n 
2 201 LEU n 
2 202 LEU n 
2 203 TRP n 
2 204 ASP n 
2 205 THR n 
2 206 ARG n 
2 207 CYS n 
2 208 PRO n 
2 209 LYS n 
2 210 PRO n 
2 211 ALA n 
2 212 SER n 
2 213 GLN n 
2 214 ILE n 
2 215 GLY n 
2 216 CYS n 
2 217 SER n 
2 218 ALA n 
2 219 PRO n 
2 220 GLY n 
2 221 TYR n 
2 222 LEU n 
2 223 PRO n 
2 224 THR n 
2 225 SER n 
2 226 LEU n 
2 227 ALA n 
2 228 TRP n 
2 229 HIS n 
2 230 PRO n 
2 231 GLN n 
2 232 GLN n 
2 233 SER n 
2 234 GLU n 
2 235 VAL n 
2 236 PHE n 
2 237 VAL n 
2 238 PHE n 
2 239 GLY n 
2 240 ASP n 
2 241 GLU n 
2 242 ASN n 
2 243 GLY n 
2 244 THR n 
2 245 VAL n 
2 246 SER n 
2 247 LEU n 
2 248 VAL n 
2 249 ASP n 
2 250 THR n 
2 251 LYS n 
2 252 SER n 
2 253 THR n 
2 254 SER n 
2 255 CYS n 
2 256 VAL n 
2 257 LEU n 
2 258 SER n 
2 259 SER n 
2 260 ALA n 
2 261 VAL n 
2 262 HIS n 
2 263 SER n 
2 264 GLN n 
2 265 CYS n 
2 266 VAL n 
2 267 THR n 
2 268 GLY n 
2 269 LEU n 
2 270 VAL n 
2 271 PHE n 
2 272 SER n 
2 273 PRO n 
2 274 HIS n 
2 275 SER n 
2 276 VAL n 
2 277 PRO n 
2 278 PHE n 
2 279 LEU n 
2 280 ALA n 
2 281 SER n 
2 282 LEU n 
2 283 SER n 
2 284 GLU n 
2 285 ASP n 
2 286 CYS n 
2 287 SER n 
2 288 LEU n 
2 289 ALA n 
2 290 VAL n 
2 291 LEU n 
2 292 ASP n 
2 293 SER n 
2 294 SER n 
2 295 LEU n 
2 296 SER n 
2 297 GLU n 
2 298 LEU n 
2 299 PHE n 
2 300 ARG n 
2 301 SER n 
2 302 GLN n 
2 303 ALA n 
2 304 HIS n 
2 305 ARG n 
2 306 ASP n 
2 307 PHE n 
2 308 VAL n 
2 309 ARG n 
2 310 ASP n 
2 311 ALA n 
2 312 THR n 
2 313 TRP n 
2 314 SER n 
2 315 PRO n 
2 316 LEU n 
2 317 ASN n 
2 318 HIS n 
2 319 SER n 
2 320 LEU n 
2 321 LEU n 
2 322 THR n 
2 323 THR n 
2 324 VAL n 
2 325 GLY n 
2 326 TRP n 
2 327 ASP n 
2 328 HIS n 
2 329 GLN n 
2 330 VAL n 
2 331 VAL n 
2 332 HIS n 
2 333 HIS n 
2 334 VAL n 
2 335 VAL n 
2 336 PRO n 
2 337 THR n 
2 338 GLU n 
2 339 PRO n 
2 340 LEU n 
2 341 PRO n 
2 342 ALA n 
2 343 PRO n 
2 344 GLY n 
2 345 PRO n 
2 346 ALA n 
2 347 SER n 
2 348 VAL n 
2 349 THR n 
2 350 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 645 human ? 'PRMT5, HRMT1L5, IBP72, JBP1, SKB1'       ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? 
? ? ? 'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 350 human ? 'WDR77, MEP50, WD45, HKMT1069, Nbla10071' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? 
? ? ? 'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1BLI non-polymer         . 
;[2-(cyclobutylamino)pyridin-4-yl][(3R,4R)-3-hydroxy-4-{6-[(1-methyl-1H-pyrazol-5-yl)methyl]-3,4-dihydroisoquinolin-2(1H)-yl}piperidin-1-yl]methanone
;
?                               'C29 H36 N6 O2'   500.635 
ALA   'L-peptide linking' y ALANINE ?                               'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE ?                               'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE ?                               'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'      133.103 
CL    non-polymer         . 'CHLORIDE ION' ?                               'Cl -1'           35.453  
CYS   'L-peptide linking' y CYSTEINE ?                               'C3 H7 N O2 S'    121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL'               'C2 H6 O2'        62.068  
GLN   'L-peptide linking' y GLUTAMINE ?                               'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE ?                               'C2 H5 N O2'      75.067  
GOL   non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'        92.094  
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 
MTA   non-polymer         . "5'-DEOXY-5'-METHYLTHIOADENOSINE" ?                               'C11 H15 N5 O3 S' 297.334 
NA    non-polymer         . 'SODIUM ION' ?                               'Na 1'            22.990  
PHE   'L-peptide linking' y PHENYLALANINE ?                               'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE ?                               'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE ?                               'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE ?                               'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                               'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE ?                               'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE ?                               'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -7  ?   ?   ?   A . n 
A 1 2   ASP 2   -6  ?   ?   ?   A . n 
A 1 3   TYR 3   -5  ?   ?   ?   A . n 
A 1 4   LYS 4   -4  ?   ?   ?   A . n 
A 1 5   ASP 5   -3  ?   ?   ?   A . n 
A 1 6   ASP 6   -2  ?   ?   ?   A . n 
A 1 7   ASP 7   -1  ?   ?   ?   A . n 
A 1 8   ASP 8   0   ?   ?   ?   A . n 
A 1 9   LYS 9   1   ?   ?   ?   A . n 
A 1 10  ALA 10  2   ?   ?   ?   A . n 
A 1 11  ALA 11  3   ?   ?   ?   A . n 
A 1 12  MET 12  4   ?   ?   ?   A . n 
A 1 13  ALA 13  5   ?   ?   ?   A . n 
A 1 14  VAL 14  6   ?   ?   ?   A . n 
A 1 15  GLY 15  7   ?   ?   ?   A . n 
A 1 16  GLY 16  8   ?   ?   ?   A . n 
A 1 17  ALA 17  9   ?   ?   ?   A . n 
A 1 18  GLY 18  10  ?   ?   ?   A . n 
A 1 19  GLY 19  11  ?   ?   ?   A . n 
A 1 20  SER 20  12  ?   ?   ?   A . n 
A 1 21  ARG 21  13  13  ARG ARG A . n 
A 1 22  VAL 22  14  14  VAL VAL A . n 
A 1 23  SER 23  15  15  SER SER A . n 
A 1 24  SER 24  16  16  SER SER A . n 
A 1 25  GLY 25  17  17  GLY GLY A . n 
A 1 26  ARG 26  18  18  ARG ARG A . n 
A 1 27  ASP 27  19  19  ASP ASP A . n 
A 1 28  LEU 28  20  20  LEU LEU A . n 
A 1 29  ASN 29  21  21  ASN ASN A . n 
A 1 30  CYS 30  22  22  CYS CYS A . n 
A 1 31  VAL 31  23  23  VAL VAL A . n 
A 1 32  PRO 32  24  24  PRO PRO A . n 
A 1 33  GLU 33  25  25  GLU GLU A . n 
A 1 34  ILE 34  26  26  ILE ILE A . n 
A 1 35  ALA 35  27  27  ALA ALA A . n 
A 1 36  ASP 36  28  28  ASP ASP A . n 
A 1 37  THR 37  29  29  THR THR A . n 
A 1 38  LEU 38  30  30  LEU LEU A . n 
A 1 39  GLY 39  31  31  GLY GLY A . n 
A 1 40  ALA 40  32  32  ALA ALA A . n 
A 1 41  VAL 41  33  33  VAL VAL A . n 
A 1 42  ALA 42  34  34  ALA ALA A . n 
A 1 43  LYS 43  35  35  LYS LYS A . n 
A 1 44  GLN 44  36  36  GLN GLN A . n 
A 1 45  GLY 45  37  37  GLY GLY A . n 
A 1 46  PHE 46  38  38  PHE PHE A . n 
A 1 47  ASP 47  39  39  ASP ASP A . n 
A 1 48  PHE 48  40  40  PHE PHE A . n 
A 1 49  LEU 49  41  41  LEU LEU A . n 
A 1 50  CYS 50  42  42  CYS CYS A . n 
A 1 51  MET 51  43  43  MET MET A . n 
A 1 52  PRO 52  44  44  PRO PRO A . n 
A 1 53  VAL 53  45  45  VAL VAL A . n 
A 1 54  PHE 54  46  46  PHE PHE A . n 
A 1 55  HIS 55  47  47  HIS HIS A . n 
A 1 56  PRO 56  48  48  PRO PRO A . n 
A 1 57  ARG 57  49  49  ARG ARG A . n 
A 1 58  PHE 58  50  50  PHE PHE A . n 
A 1 59  LYS 59  51  51  LYS LYS A . n 
A 1 60  ARG 60  52  52  ARG ARG A . n 
A 1 61  GLU 61  53  53  GLU GLU A . n 
A 1 62  PHE 62  54  54  PHE PHE A . n 
A 1 63  ILE 63  55  55  ILE ILE A . n 
A 1 64  GLN 64  56  56  GLN GLN A . n 
A 1 65  GLU 65  57  57  GLU GLU A . n 
A 1 66  PRO 66  58  58  PRO PRO A . n 
A 1 67  ALA 67  59  59  ALA ALA A . n 
A 1 68  LYS 68  60  60  LYS LYS A . n 
A 1 69  ASN 69  61  61  ASN ASN A . n 
A 1 70  ARG 70  62  62  ARG ARG A . n 
A 1 71  PRO 71  63  63  PRO PRO A . n 
A 1 72  GLY 72  64  64  GLY GLY A . n 
A 1 73  PRO 73  65  65  PRO PRO A . n 
A 1 74  GLN 74  66  66  GLN GLN A . n 
A 1 75  THR 75  67  67  THR THR A . n 
A 1 76  ARG 76  68  68  ARG ARG A . n 
A 1 77  SER 77  69  69  SER SER A . n 
A 1 78  ASP 78  70  70  ASP ASP A . n 
A 1 79  LEU 79  71  71  LEU LEU A . n 
A 1 80  LEU 80  72  72  LEU LEU A . n 
A 1 81  LEU 81  73  73  LEU LEU A . n 
A 1 82  SER 82  74  74  SER SER A . n 
A 1 83  GLY 83  75  75  GLY GLY A . n 
A 1 84  ARG 84  76  76  ARG ARG A . n 
A 1 85  ASP 85  77  77  ASP ASP A . n 
A 1 86  TRP 86  78  78  TRP TRP A . n 
A 1 87  ASN 87  79  79  ASN ASN A . n 
A 1 88  THR 88  80  80  THR THR A . n 
A 1 89  LEU 89  81  81  LEU LEU A . n 
A 1 90  ILE 90  82  82  ILE ILE A . n 
A 1 91  VAL 91  83  83  VAL VAL A . n 
A 1 92  GLY 92  84  84  GLY GLY A . n 
A 1 93  LYS 93  85  85  LYS LYS A . n 
A 1 94  LEU 94  86  86  LEU LEU A . n 
A 1 95  SER 95  87  87  SER SER A . n 
A 1 96  PRO 96  88  88  PRO PRO A . n 
A 1 97  TRP 97  89  89  TRP TRP A . n 
A 1 98  ILE 98  90  90  ILE ILE A . n 
A 1 99  ARG 99  91  91  ARG ARG A . n 
A 1 100 PRO 100 92  92  PRO PRO A . n 
A 1 101 ASP 101 93  93  ASP ASP A . n 
A 1 102 SER 102 94  94  SER SER A . n 
A 1 103 LYS 103 95  95  LYS LYS A . n 
A 1 104 VAL 104 96  96  VAL VAL A . n 
A 1 105 GLU 105 97  97  GLU GLU A . n 
A 1 106 LYS 106 98  98  LYS LYS A . n 
A 1 107 ILE 107 99  99  ILE ILE A . n 
A 1 108 ARG 108 100 100 ARG ARG A . n 
A 1 109 ARG 109 101 101 ARG ARG A . n 
A 1 110 ASN 110 102 102 ASN ASN A . n 
A 1 111 SER 111 103 103 SER SER A . n 
A 1 112 GLU 112 104 104 GLU GLU A . n 
A 1 113 ALA 113 105 105 ALA ALA A . n 
A 1 114 ALA 114 106 106 ALA ALA A . n 
A 1 115 MET 115 107 107 MET MET A . n 
A 1 116 LEU 116 108 108 LEU LEU A . n 
A 1 117 GLN 117 109 109 GLN GLN A . n 
A 1 118 GLU 118 110 110 GLU GLU A . n 
A 1 119 LEU 119 111 111 LEU LEU A . n 
A 1 120 ASN 120 112 112 ASN ASN A . n 
A 1 121 PHE 121 113 113 PHE PHE A . n 
A 1 122 GLY 122 114 114 GLY GLY A . n 
A 1 123 ALA 123 115 115 ALA ALA A . n 
A 1 124 TYR 124 116 116 TYR TYR A . n 
A 1 125 LEU 125 117 117 LEU LEU A . n 
A 1 126 GLY 126 118 118 GLY GLY A . n 
A 1 127 LEU 127 119 119 LEU LEU A . n 
A 1 128 PRO 128 120 120 PRO PRO A . n 
A 1 129 ALA 129 121 121 ALA ALA A . n 
A 1 130 PHE 130 122 122 PHE PHE A . n 
A 1 131 LEU 131 123 123 LEU LEU A . n 
A 1 132 LEU 132 124 124 LEU LEU A . n 
A 1 133 PRO 133 125 125 PRO PRO A . n 
A 1 134 LEU 134 126 126 LEU LEU A . n 
A 1 135 ASN 135 127 127 ASN ASN A . n 
A 1 136 GLN 136 128 128 GLN GLN A . n 
A 1 137 GLU 137 129 129 GLU GLU A . n 
A 1 138 ASP 138 130 130 ASP ASP A . n 
A 1 139 ASN 139 131 131 ASN ASN A . n 
A 1 140 THR 140 132 132 THR THR A . n 
A 1 141 ASN 141 133 133 ASN ASN A . n 
A 1 142 LEU 142 134 134 LEU LEU A . n 
A 1 143 ALA 143 135 135 ALA ALA A . n 
A 1 144 ARG 144 136 136 ARG ARG A . n 
A 1 145 VAL 145 137 137 VAL VAL A . n 
A 1 146 LEU 146 138 138 LEU LEU A . n 
A 1 147 THR 147 139 139 THR THR A . n 
A 1 148 ASN 148 140 140 ASN ASN A . n 
A 1 149 HIS 149 141 141 HIS HIS A . n 
A 1 150 ILE 150 142 142 ILE ILE A . n 
A 1 151 HIS 151 143 143 HIS HIS A . n 
A 1 152 THR 152 144 144 THR THR A . n 
A 1 153 GLY 153 145 145 GLY GLY A . n 
A 1 154 HIS 154 146 146 HIS HIS A . n 
A 1 155 HIS 155 147 147 HIS HIS A . n 
A 1 156 SER 156 148 148 SER SER A . n 
A 1 157 SER 157 149 149 SER SER A . n 
A 1 158 MET 158 150 150 MET MET A . n 
A 1 159 PHE 159 151 151 PHE PHE A . n 
A 1 160 TRP 160 152 152 TRP TRP A . n 
A 1 161 MET 161 153 153 MET MET A . n 
A 1 162 ARG 162 154 154 ARG ARG A . n 
A 1 163 VAL 163 155 155 VAL VAL A . n 
A 1 164 PRO 164 156 156 PRO PRO A . n 
A 1 165 LEU 165 157 157 LEU LEU A . n 
A 1 166 VAL 166 158 158 VAL VAL A . n 
A 1 167 ALA 167 159 159 ALA ALA A . n 
A 1 168 PRO 168 160 160 PRO PRO A . n 
A 1 169 GLU 169 161 161 GLU GLU A . n 
A 1 170 ASP 170 162 162 ASP ASP A . n 
A 1 171 LEU 171 163 163 LEU LEU A . n 
A 1 172 ARG 172 164 164 ARG ARG A . n 
A 1 173 ASP 173 165 165 ASP ASP A . n 
A 1 174 ASP 174 166 166 ASP ASP A . n 
A 1 175 ILE 175 167 167 ILE ILE A . n 
A 1 176 ILE 176 168 168 ILE ILE A . n 
A 1 177 GLU 177 169 169 GLU GLU A . n 
A 1 178 ASN 178 170 170 ASN ASN A . n 
A 1 179 ALA 179 171 171 ALA ALA A . n 
A 1 180 PRO 180 172 172 PRO PRO A . n 
A 1 181 THR 181 173 173 THR THR A . n 
A 1 182 THR 182 174 174 THR THR A . n 
A 1 183 HIS 183 175 175 HIS HIS A . n 
A 1 184 THR 184 176 176 THR THR A . n 
A 1 185 GLU 185 177 177 GLU GLU A . n 
A 1 186 GLU 186 178 178 GLU GLU A . n 
A 1 187 TYR 187 179 179 TYR TYR A . n 
A 1 188 SER 188 180 180 SER SER A . n 
A 1 189 GLY 189 181 181 GLY GLY A . n 
A 1 190 GLU 190 182 182 GLU GLU A . n 
A 1 191 GLU 191 183 183 GLU GLU A . n 
A 1 192 LYS 192 184 184 LYS LYS A . n 
A 1 193 THR 193 185 185 THR THR A . n 
A 1 194 TRP 194 186 186 TRP TRP A . n 
A 1 195 MET 195 187 187 MET MET A . n 
A 1 196 TRP 196 188 188 TRP TRP A . n 
A 1 197 TRP 197 189 189 TRP TRP A . n 
A 1 198 HIS 198 190 190 HIS HIS A . n 
A 1 199 ASN 199 191 191 ASN ASN A . n 
A 1 200 PHE 200 192 192 PHE PHE A . n 
A 1 201 ARG 201 193 193 ARG ARG A . n 
A 1 202 THR 202 194 194 THR THR A . n 
A 1 203 LEU 203 195 195 LEU LEU A . n 
A 1 204 CYS 204 196 196 CYS CYS A . n 
A 1 205 ASP 205 197 197 ASP ASP A . n 
A 1 206 TYR 206 198 198 TYR TYR A . n 
A 1 207 SER 207 199 199 SER SER A . n 
A 1 208 LYS 208 200 200 LYS LYS A . n 
A 1 209 ARG 209 201 201 ARG ARG A . n 
A 1 210 ILE 210 202 202 ILE ILE A . n 
A 1 211 ALA 211 203 203 ALA ALA A . n 
A 1 212 VAL 212 204 204 VAL VAL A . n 
A 1 213 ALA 213 205 205 ALA ALA A . n 
A 1 214 LEU 214 206 206 LEU LEU A . n 
A 1 215 GLU 215 207 207 GLU GLU A . n 
A 1 216 ILE 216 208 208 ILE ILE A . n 
A 1 217 GLY 217 209 209 GLY GLY A . n 
A 1 218 ALA 218 210 210 ALA ALA A . n 
A 1 219 ASP 219 211 211 ASP ASP A . n 
A 1 220 LEU 220 212 212 LEU LEU A . n 
A 1 221 PRO 221 213 213 PRO PRO A . n 
A 1 222 SER 222 214 214 SER SER A . n 
A 1 223 ASN 223 215 215 ASN ASN A . n 
A 1 224 HIS 224 216 216 HIS HIS A . n 
A 1 225 VAL 225 217 217 VAL VAL A . n 
A 1 226 ILE 226 218 218 ILE ILE A . n 
A 1 227 ASP 227 219 219 ASP ASP A . n 
A 1 228 ARG 228 220 220 ARG ARG A . n 
A 1 229 TRP 229 221 221 TRP TRP A . n 
A 1 230 LEU 230 222 222 LEU LEU A . n 
A 1 231 GLY 231 223 223 GLY GLY A . n 
A 1 232 GLU 232 224 224 GLU GLU A . n 
A 1 233 PRO 233 225 225 PRO PRO A . n 
A 1 234 ILE 234 226 226 ILE ILE A . n 
A 1 235 LYS 235 227 227 LYS LYS A . n 
A 1 236 ALA 236 228 228 ALA ALA A . n 
A 1 237 ALA 237 229 229 ALA ALA A . n 
A 1 238 ILE 238 230 230 ILE ILE A . n 
A 1 239 LEU 239 231 231 LEU LEU A . n 
A 1 240 PRO 240 232 232 PRO PRO A . n 
A 1 241 THR 241 233 233 THR THR A . n 
A 1 242 SER 242 234 234 SER SER A . n 
A 1 243 ILE 243 235 235 ILE ILE A . n 
A 1 244 PHE 244 236 236 PHE PHE A . n 
A 1 245 LEU 245 237 237 LEU LEU A . n 
A 1 246 THR 246 238 238 THR THR A . n 
A 1 247 ASN 247 239 239 ASN ASN A . n 
A 1 248 LYS 248 240 240 LYS LYS A . n 
A 1 249 LYS 249 241 241 LYS LYS A . n 
A 1 250 GLY 250 242 242 GLY GLY A . n 
A 1 251 PHE 251 243 243 PHE PHE A . n 
A 1 252 PRO 252 244 244 PRO PRO A . n 
A 1 253 VAL 253 245 245 VAL VAL A . n 
A 1 254 LEU 254 246 246 LEU LEU A . n 
A 1 255 SER 255 247 247 SER SER A . n 
A 1 256 LYS 256 248 248 LYS LYS A . n 
A 1 257 MET 257 249 249 MET MET A . n 
A 1 258 HIS 258 250 250 HIS HIS A . n 
A 1 259 GLN 259 251 251 GLN GLN A . n 
A 1 260 ARG 260 252 252 ARG ARG A . n 
A 1 261 LEU 261 253 253 LEU LEU A . n 
A 1 262 ILE 262 254 254 ILE ILE A . n 
A 1 263 PHE 263 255 255 PHE PHE A . n 
A 1 264 ARG 264 256 256 ARG ARG A . n 
A 1 265 LEU 265 257 257 LEU LEU A . n 
A 1 266 LEU 266 258 258 LEU LEU A . n 
A 1 267 LYS 267 259 259 LYS LYS A . n 
A 1 268 LEU 268 260 260 LEU LEU A . n 
A 1 269 GLU 269 261 261 GLU GLU A . n 
A 1 270 VAL 270 262 262 VAL VAL A . n 
A 1 271 GLN 271 263 263 GLN GLN A . n 
A 1 272 PHE 272 264 264 PHE PHE A . n 
A 1 273 ILE 273 265 265 ILE ILE A . n 
A 1 274 ILE 274 266 266 ILE ILE A . n 
A 1 275 THR 275 267 267 THR THR A . n 
A 1 276 GLY 276 268 268 GLY GLY A . n 
A 1 277 THR 277 269 269 THR THR A . n 
A 1 278 ASN 278 270 270 ASN ASN A . n 
A 1 279 HIS 279 271 271 HIS HIS A . n 
A 1 280 HIS 280 272 272 HIS HIS A . n 
A 1 281 SER 281 273 273 SER SER A . n 
A 1 282 GLU 282 274 274 GLU GLU A . n 
A 1 283 LYS 283 275 275 LYS LYS A . n 
A 1 284 GLU 284 276 276 GLU GLU A . n 
A 1 285 PHE 285 277 277 PHE PHE A . n 
A 1 286 CYS 286 278 278 CYS CYS A . n 
A 1 287 SER 287 279 279 SER SER A . n 
A 1 288 TYR 288 280 280 TYR TYR A . n 
A 1 289 LEU 289 281 281 LEU LEU A . n 
A 1 290 GLN 290 282 282 GLN GLN A . n 
A 1 291 TYR 291 283 283 TYR TYR A . n 
A 1 292 LEU 292 284 284 LEU LEU A . n 
A 1 293 GLU 293 285 285 GLU GLU A . n 
A 1 294 TYR 294 286 286 TYR TYR A . n 
A 1 295 LEU 295 287 287 LEU LEU A . n 
A 1 296 SER 296 288 288 SER SER A . n 
A 1 297 GLN 297 289 289 GLN GLN A . n 
A 1 298 ASN 298 290 290 ASN ASN A . n 
A 1 299 ARG 299 291 291 ARG ARG A . n 
A 1 300 PRO 300 292 292 PRO PRO A . n 
A 1 301 PRO 301 293 293 PRO PRO A . n 
A 1 302 PRO 302 294 294 PRO PRO A . n 
A 1 303 ASN 303 295 295 ASN ASN A . n 
A 1 304 ALA 304 296 296 ALA ALA A . n 
A 1 305 TYR 305 297 297 TYR TYR A . n 
A 1 306 GLU 306 298 298 GLU GLU A . n 
A 1 307 LEU 307 299 299 LEU LEU A . n 
A 1 308 PHE 308 300 300 PHE PHE A . n 
A 1 309 ALA 309 301 301 ALA ALA A . n 
A 1 310 LYS 310 302 302 LYS LYS A . n 
A 1 311 GLY 311 303 303 GLY GLY A . n 
A 1 312 TYR 312 304 304 TYR TYR A . n 
A 1 313 GLU 313 305 305 GLU GLU A . n 
A 1 314 ASP 314 306 306 ASP ASP A . n 
A 1 315 TYR 315 307 307 TYR TYR A . n 
A 1 316 LEU 316 308 308 LEU LEU A . n 
A 1 317 GLN 317 309 309 GLN GLN A . n 
A 1 318 SER 318 310 310 SER SER A . n 
A 1 319 PRO 319 311 311 PRO PRO A . n 
A 1 320 LEU 320 312 312 LEU LEU A . n 
A 1 321 GLN 321 313 313 GLN GLN A . n 
A 1 322 PRO 322 314 314 PRO PRO A . n 
A 1 323 LEU 323 315 315 LEU LEU A . n 
A 1 324 MET 324 316 316 MET MET A . n 
A 1 325 ASP 325 317 317 ASP ASP A . n 
A 1 326 ASN 326 318 318 ASN ASN A . n 
A 1 327 LEU 327 319 319 LEU LEU A . n 
A 1 328 GLU 328 320 320 GLU GLU A . n 
A 1 329 SER 329 321 321 SER SER A . n 
A 1 330 GLN 330 322 322 GLN GLN A . n 
A 1 331 THR 331 323 323 THR THR A . n 
A 1 332 TYR 332 324 324 TYR TYR A . n 
A 1 333 GLU 333 325 325 GLU GLU A . n 
A 1 334 VAL 334 326 326 VAL VAL A . n 
A 1 335 PHE 335 327 327 PHE PHE A . n 
A 1 336 GLU 336 328 328 GLU GLU A . n 
A 1 337 LYS 337 329 329 LYS LYS A . n 
A 1 338 ASP 338 330 330 ASP ASP A . n 
A 1 339 PRO 339 331 331 PRO PRO A . n 
A 1 340 ILE 340 332 332 ILE ILE A . n 
A 1 341 LYS 341 333 333 LYS LYS A . n 
A 1 342 TYR 342 334 334 TYR TYR A . n 
A 1 343 SER 343 335 335 SER SER A . n 
A 1 344 GLN 344 336 336 GLN GLN A . n 
A 1 345 TYR 345 337 337 TYR TYR A . n 
A 1 346 GLN 346 338 338 GLN GLN A . n 
A 1 347 GLN 347 339 339 GLN GLN A . n 
A 1 348 ALA 348 340 340 ALA ALA A . n 
A 1 349 ILE 349 341 341 ILE ILE A . n 
A 1 350 TYR 350 342 342 TYR TYR A . n 
A 1 351 LYS 351 343 343 LYS LYS A . n 
A 1 352 CYS 352 344 344 CYS CYS A . n 
A 1 353 LEU 353 345 345 LEU LEU A . n 
A 1 354 LEU 354 346 346 LEU LEU A . n 
A 1 355 ASP 355 347 347 ASP ASP A . n 
A 1 356 ARG 356 348 348 ARG ARG A . n 
A 1 357 VAL 357 349 349 VAL VAL A . n 
A 1 358 PRO 358 350 350 PRO PRO A . n 
A 1 359 GLU 359 351 351 GLU GLU A . n 
A 1 360 GLU 360 352 352 GLU GLU A . n 
A 1 361 GLU 361 353 353 GLU GLU A . n 
A 1 362 LYS 362 354 354 LYS LYS A . n 
A 1 363 ASP 363 355 355 ASP ASP A . n 
A 1 364 THR 364 356 356 THR THR A . n 
A 1 365 ASN 365 357 357 ASN ASN A . n 
A 1 366 VAL 366 358 358 VAL VAL A . n 
A 1 367 GLN 367 359 359 GLN GLN A . n 
A 1 368 VAL 368 360 360 VAL VAL A . n 
A 1 369 LEU 369 361 361 LEU LEU A . n 
A 1 370 MET 370 362 362 MET MET A . n 
A 1 371 VAL 371 363 363 VAL VAL A . n 
A 1 372 LEU 372 364 364 LEU LEU A . n 
A 1 373 GLY 373 365 365 GLY GLY A . n 
A 1 374 ALA 374 366 366 ALA ALA A . n 
A 1 375 GLY 375 367 367 GLY GLY A . n 
A 1 376 ARG 376 368 368 ARG ARG A . n 
A 1 377 GLY 377 369 369 GLY GLY A . n 
A 1 378 PRO 378 370 370 PRO PRO A . n 
A 1 379 LEU 379 371 371 LEU LEU A . n 
A 1 380 VAL 380 372 372 VAL VAL A . n 
A 1 381 ASN 381 373 373 ASN ASN A . n 
A 1 382 ALA 382 374 374 ALA ALA A . n 
A 1 383 SER 383 375 375 SER SER A . n 
A 1 384 LEU 384 376 376 LEU LEU A . n 
A 1 385 ARG 385 377 377 ARG ARG A . n 
A 1 386 ALA 386 378 378 ALA ALA A . n 
A 1 387 ALA 387 379 379 ALA ALA A . n 
A 1 388 LYS 388 380 380 LYS LYS A . n 
A 1 389 GLN 389 381 381 GLN GLN A . n 
A 1 390 ALA 390 382 382 ALA ALA A . n 
A 1 391 ASP 391 383 383 ASP ASP A . n 
A 1 392 ARG 392 384 384 ARG ARG A . n 
A 1 393 ARG 393 385 385 ARG ARG A . n 
A 1 394 ILE 394 386 386 ILE ILE A . n 
A 1 395 LYS 395 387 387 LYS LYS A . n 
A 1 396 LEU 396 388 388 LEU LEU A . n 
A 1 397 TYR 397 389 389 TYR TYR A . n 
A 1 398 ALA 398 390 390 ALA ALA A . n 
A 1 399 VAL 399 391 391 VAL VAL A . n 
A 1 400 GLU 400 392 392 GLU GLU A . n 
A 1 401 LYS 401 393 393 LYS LYS A . n 
A 1 402 ASN 402 394 394 ASN ASN A . n 
A 1 403 PRO 403 395 395 PRO PRO A . n 
A 1 404 ASN 404 396 396 ASN ASN A . n 
A 1 405 ALA 405 397 397 ALA ALA A . n 
A 1 406 VAL 406 398 398 VAL VAL A . n 
A 1 407 VAL 407 399 399 VAL VAL A . n 
A 1 408 THR 408 400 400 THR THR A . n 
A 1 409 LEU 409 401 401 LEU LEU A . n 
A 1 410 GLU 410 402 402 GLU GLU A . n 
A 1 411 ASN 411 403 403 ASN ASN A . n 
A 1 412 TRP 412 404 404 TRP TRP A . n 
A 1 413 GLN 413 405 405 GLN GLN A . n 
A 1 414 PHE 414 406 406 PHE PHE A . n 
A 1 415 GLU 415 407 407 GLU GLU A . n 
A 1 416 GLU 416 408 408 GLU GLU A . n 
A 1 417 TRP 417 409 409 TRP TRP A . n 
A 1 418 GLY 418 410 410 GLY GLY A . n 
A 1 419 SER 419 411 411 SER SER A . n 
A 1 420 GLN 420 412 412 GLN GLN A . n 
A 1 421 VAL 421 413 413 VAL VAL A . n 
A 1 422 THR 422 414 414 THR THR A . n 
A 1 423 VAL 423 415 415 VAL VAL A . n 
A 1 424 VAL 424 416 416 VAL VAL A . n 
A 1 425 SER 425 417 417 SER SER A . n 
A 1 426 SER 426 418 418 SER SER A . n 
A 1 427 ASP 427 419 419 ASP ASP A . n 
A 1 428 MET 428 420 420 MET MET A . n 
A 1 429 ARG 429 421 421 ARG ARG A . n 
A 1 430 GLU 430 422 422 GLU GLU A . n 
A 1 431 TRP 431 423 423 TRP TRP A . n 
A 1 432 VAL 432 424 424 VAL VAL A . n 
A 1 433 ALA 433 425 425 ALA ALA A . n 
A 1 434 PRO 434 426 426 PRO PRO A . n 
A 1 435 GLU 435 427 427 GLU GLU A . n 
A 1 436 LYS 436 428 428 LYS LYS A . n 
A 1 437 ALA 437 429 429 ALA ALA A . n 
A 1 438 ASP 438 430 430 ASP ASP A . n 
A 1 439 ILE 439 431 431 ILE ILE A . n 
A 1 440 ILE 440 432 432 ILE ILE A . n 
A 1 441 VAL 441 433 433 VAL VAL A . n 
A 1 442 SER 442 434 434 SER SER A . n 
A 1 443 GLU 443 435 435 GLU GLU A . n 
A 1 444 LEU 444 436 436 LEU LEU A . n 
A 1 445 LEU 445 437 437 LEU LEU A . n 
A 1 446 GLY 446 438 438 GLY GLY A . n 
A 1 447 SER 447 439 439 SER SER A . n 
A 1 448 PHE 448 440 440 PHE PHE A . n 
A 1 449 ALA 449 441 441 ALA ALA A . n 
A 1 450 ASP 450 442 442 ASP ASP A . n 
A 1 451 ASN 451 443 443 ASN ASN A . n 
A 1 452 GLU 452 444 444 GLU GLU A . n 
A 1 453 LEU 453 445 445 LEU LEU A . n 
A 1 454 SER 454 446 446 SER SER A . n 
A 1 455 PRO 455 447 447 PRO PRO A . n 
A 1 456 GLU 456 448 448 GLU GLU A . n 
A 1 457 CYS 457 449 449 CYS CYS A . n 
A 1 458 LEU 458 450 450 LEU LEU A . n 
A 1 459 ASP 459 451 451 ASP ASP A . n 
A 1 460 GLY 460 452 452 GLY GLY A . n 
A 1 461 ALA 461 453 453 ALA ALA A . n 
A 1 462 GLN 462 454 454 GLN GLN A . n 
A 1 463 HIS 463 455 455 HIS HIS A . n 
A 1 464 PHE 464 456 456 PHE PHE A . n 
A 1 465 LEU 465 457 457 LEU LEU A . n 
A 1 466 LYS 466 458 458 LYS LYS A . n 
A 1 467 ASP 467 459 459 ASP ASP A . n 
A 1 468 ASP 468 460 460 ASP ASP A . n 
A 1 469 GLY 469 461 461 GLY GLY A . n 
A 1 470 VAL 470 462 462 VAL VAL A . n 
A 1 471 SER 471 463 463 SER SER A . n 
A 1 472 ILE 472 464 464 ILE ILE A . n 
A 1 473 PRO 473 465 465 PRO PRO A . n 
A 1 474 GLY 474 466 466 GLY GLY A . n 
A 1 475 GLU 475 467 467 GLU GLU A . n 
A 1 476 TYR 476 468 468 TYR TYR A . n 
A 1 477 THR 477 469 469 THR THR A . n 
A 1 478 SER 478 470 470 SER SER A . n 
A 1 479 PHE 479 471 471 PHE PHE A . n 
A 1 480 LEU 480 472 472 LEU LEU A . n 
A 1 481 ALA 481 473 473 ALA ALA A . n 
A 1 482 PRO 482 474 474 PRO PRO A . n 
A 1 483 ILE 483 475 475 ILE ILE A . n 
A 1 484 SER 484 476 476 SER SER A . n 
A 1 485 SER 485 477 477 SER SER A . n 
A 1 486 SER 486 478 478 SER SER A . n 
A 1 487 LYS 487 479 479 LYS LYS A . n 
A 1 488 LEU 488 480 480 LEU LEU A . n 
A 1 489 TYR 489 481 481 TYR TYR A . n 
A 1 490 ASN 490 482 482 ASN ASN A . n 
A 1 491 GLU 491 483 483 GLU GLU A . n 
A 1 492 VAL 492 484 484 VAL VAL A . n 
A 1 493 ARG 493 485 485 ARG ARG A . n 
A 1 494 ALA 494 486 486 ALA ALA A . n 
A 1 495 CYS 495 487 487 CYS CYS A . n 
A 1 496 ARG 496 488 488 ARG ARG A . n 
A 1 497 GLU 497 489 489 GLU GLU A . n 
A 1 498 LYS 498 490 490 LYS LYS A . n 
A 1 499 ASP 499 491 491 ASP ASP A . n 
A 1 500 ARG 500 492 492 ARG ARG A . n 
A 1 501 ASP 501 493 493 ASP ASP A . n 
A 1 502 PRO 502 494 494 PRO PRO A . n 
A 1 503 GLU 503 495 495 GLU GLU A . n 
A 1 504 ALA 504 496 496 ALA ALA A . n 
A 1 505 GLN 505 497 497 GLN GLN A . n 
A 1 506 PHE 506 498 498 PHE PHE A . n 
A 1 507 GLU 507 499 499 GLU GLU A . n 
A 1 508 MET 508 500 500 MET MET A . n 
A 1 509 PRO 509 501 501 PRO PRO A . n 
A 1 510 TYR 510 502 502 TYR TYR A . n 
A 1 511 VAL 511 503 503 VAL VAL A . n 
A 1 512 VAL 512 504 504 VAL VAL A . n 
A 1 513 ARG 513 505 505 ARG ARG A . n 
A 1 514 LEU 514 506 506 LEU LEU A . n 
A 1 515 HIS 515 507 507 HIS HIS A . n 
A 1 516 ASN 516 508 508 ASN ASN A . n 
A 1 517 PHE 517 509 509 PHE PHE A . n 
A 1 518 HIS 518 510 510 HIS HIS A . n 
A 1 519 GLN 519 511 511 GLN GLN A . n 
A 1 520 LEU 520 512 512 LEU LEU A . n 
A 1 521 SER 521 513 513 SER SER A . n 
A 1 522 ALA 522 514 514 ALA ALA A . n 
A 1 523 PRO 523 515 515 PRO PRO A . n 
A 1 524 GLN 524 516 516 GLN GLN A . n 
A 1 525 PRO 525 517 517 PRO PRO A . n 
A 1 526 CYS 526 518 518 CYS CYS A . n 
A 1 527 PHE 527 519 519 PHE PHE A . n 
A 1 528 THR 528 520 520 THR THR A . n 
A 1 529 PHE 529 521 521 PHE PHE A . n 
A 1 530 SER 530 522 522 SER SER A . n 
A 1 531 HIS 531 523 523 HIS HIS A . n 
A 1 532 PRO 532 524 524 PRO PRO A . n 
A 1 533 ASN 533 525 525 ASN ASN A . n 
A 1 534 ARG 534 526 526 ARG ARG A . n 
A 1 535 ASP 535 527 527 ASP ASP A . n 
A 1 536 PRO 536 528 ?   ?   ?   A . n 
A 1 537 MET 537 529 ?   ?   ?   A . n 
A 1 538 ILE 538 530 ?   ?   ?   A . n 
A 1 539 ASP 539 531 531 ASP ASP A . n 
A 1 540 ASN 540 532 532 ASN ASN A . n 
A 1 541 ASN 541 533 533 ASN ASN A . n 
A 1 542 ARG 542 534 534 ARG ARG A . n 
A 1 543 TYR 543 535 535 TYR TYR A . n 
A 1 544 CYS 544 536 536 CYS CYS A . n 
A 1 545 THR 545 537 537 THR THR A . n 
A 1 546 LEU 546 538 538 LEU LEU A . n 
A 1 547 GLU 547 539 539 GLU GLU A . n 
A 1 548 PHE 548 540 540 PHE PHE A . n 
A 1 549 PRO 549 541 541 PRO PRO A . n 
A 1 550 VAL 550 542 542 VAL VAL A . n 
A 1 551 GLU 551 543 543 GLU GLU A . n 
A 1 552 VAL 552 544 544 VAL VAL A . n 
A 1 553 ASN 553 545 545 ASN ASN A . n 
A 1 554 THR 554 546 546 THR THR A . n 
A 1 555 VAL 555 547 547 VAL VAL A . n 
A 1 556 LEU 556 548 548 LEU LEU A . n 
A 1 557 HIS 557 549 549 HIS HIS A . n 
A 1 558 GLY 558 550 550 GLY GLY A . n 
A 1 559 PHE 559 551 551 PHE PHE A . n 
A 1 560 ALA 560 552 552 ALA ALA A . n 
A 1 561 GLY 561 553 553 GLY GLY A . n 
A 1 562 TYR 562 554 554 TYR TYR A . n 
A 1 563 PHE 563 555 555 PHE PHE A . n 
A 1 564 GLU 564 556 556 GLU GLU A . n 
A 1 565 THR 565 557 557 THR THR A . n 
A 1 566 VAL 566 558 558 VAL VAL A . n 
A 1 567 LEU 567 559 559 LEU LEU A . n 
A 1 568 TYR 568 560 560 TYR TYR A . n 
A 1 569 GLN 569 561 561 GLN GLN A . n 
A 1 570 ASP 570 562 562 ASP ASP A . n 
A 1 571 ILE 571 563 563 ILE ILE A . n 
A 1 572 THR 572 564 564 THR THR A . n 
A 1 573 LEU 573 565 565 LEU LEU A . n 
A 1 574 SER 574 566 566 SER SER A . n 
A 1 575 ILE 575 567 567 ILE ILE A . n 
A 1 576 ARG 576 568 568 ARG ARG A . n 
A 1 577 PRO 577 569 569 PRO PRO A . n 
A 1 578 GLU 578 570 570 GLU GLU A . n 
A 1 579 THR 579 571 571 THR THR A . n 
A 1 580 HIS 580 572 572 HIS HIS A . n 
A 1 581 SER 581 573 573 SER SER A . n 
A 1 582 PRO 582 574 574 PRO PRO A . n 
A 1 583 GLY 583 575 575 GLY GLY A . n 
A 1 584 MET 584 576 576 MET MET A . n 
A 1 585 PHE 585 577 577 PHE PHE A . n 
A 1 586 SER 586 578 578 SER SER A . n 
A 1 587 TRP 587 579 579 TRP TRP A . n 
A 1 588 PHE 588 580 580 PHE PHE A . n 
A 1 589 PRO 589 581 581 PRO PRO A . n 
A 1 590 ILE 590 582 582 ILE ILE A . n 
A 1 591 LEU 591 583 583 LEU LEU A . n 
A 1 592 PHE 592 584 584 PHE PHE A . n 
A 1 593 PRO 593 585 585 PRO PRO A . n 
A 1 594 ILE 594 586 586 ILE ILE A . n 
A 1 595 LYS 595 587 587 LYS LYS A . n 
A 1 596 GLN 596 588 588 GLN GLN A . n 
A 1 597 PRO 597 589 589 PRO PRO A . n 
A 1 598 ILE 598 590 590 ILE ILE A . n 
A 1 599 THR 599 591 591 THR THR A . n 
A 1 600 VAL 600 592 592 VAL VAL A . n 
A 1 601 ARG 601 593 593 ARG ARG A . n 
A 1 602 GLU 602 594 594 GLU GLU A . n 
A 1 603 GLY 603 595 595 GLY GLY A . n 
A 1 604 GLN 604 596 596 GLN GLN A . n 
A 1 605 THR 605 597 597 THR THR A . n 
A 1 606 ILE 606 598 598 ILE ILE A . n 
A 1 607 CYS 607 599 599 CYS CYS A . n 
A 1 608 VAL 608 600 600 VAL VAL A . n 
A 1 609 ARG 609 601 601 ARG ARG A . n 
A 1 610 PHE 610 602 602 PHE PHE A . n 
A 1 611 TRP 611 603 603 TRP TRP A . n 
A 1 612 ARG 612 604 604 ARG ARG A . n 
A 1 613 CYS 613 605 605 CYS CYS A . n 
A 1 614 SER 614 606 606 SER SER A . n 
A 1 615 ASN 615 607 607 ASN ASN A . n 
A 1 616 SER 616 608 608 SER SER A . n 
A 1 617 LYS 617 609 609 LYS LYS A . n 
A 1 618 LYS 618 610 610 LYS LYS A . n 
A 1 619 VAL 619 611 611 VAL VAL A . n 
A 1 620 TRP 620 612 612 TRP TRP A . n 
A 1 621 TYR 621 613 613 TYR TYR A . n 
A 1 622 GLU 622 614 614 GLU GLU A . n 
A 1 623 TRP 623 615 615 TRP TRP A . n 
A 1 624 ALA 624 616 616 ALA ALA A . n 
A 1 625 VAL 625 617 617 VAL VAL A . n 
A 1 626 THR 626 618 618 THR THR A . n 
A 1 627 ALA 627 619 619 ALA ALA A . n 
A 1 628 PRO 628 620 620 PRO PRO A . n 
A 1 629 VAL 629 621 621 VAL VAL A . n 
A 1 630 CYS 630 622 622 CYS CYS A . n 
A 1 631 SER 631 623 623 SER SER A . n 
A 1 632 ALA 632 624 624 ALA ALA A . n 
A 1 633 ILE 633 625 625 ILE ILE A . n 
A 1 634 HIS 634 626 626 HIS HIS A . n 
A 1 635 ASN 635 627 627 ASN ASN A . n 
A 1 636 PRO 636 628 628 PRO PRO A . n 
A 1 637 THR 637 629 629 THR THR A . n 
A 1 638 GLY 638 630 630 GLY GLY A . n 
A 1 639 ARG 639 631 631 ARG ARG A . n 
A 1 640 SER 640 632 632 SER SER A . n 
A 1 641 TYR 641 633 633 TYR TYR A . n 
A 1 642 THR 642 634 634 THR THR A . n 
A 1 643 ILE 643 635 635 ILE ILE A . n 
A 1 644 GLY 644 636 636 GLY GLY A . n 
A 1 645 LEU 645 637 637 LEU LEU A . n 
B 2 1   MET 1   -7  ?   ?   ?   B . n 
B 2 2   HIS 2   -6  ?   ?   ?   B . n 
B 2 3   HIS 3   -5  ?   ?   ?   B . n 
B 2 4   HIS 4   -4  ?   ?   ?   B . n 
B 2 5   HIS 5   -3  ?   ?   ?   B . n 
B 2 6   HIS 6   -2  ?   ?   ?   B . n 
B 2 7   HIS 7   -1  ?   ?   ?   B . n 
B 2 8   HIS 8   0   ?   ?   ?   B . n 
B 2 9   HIS 9   1   ?   ?   ?   B . n 
B 2 10  ARG 10  2   ?   ?   ?   B . n 
B 2 11  LYS 11  3   ?   ?   ?   B . n 
B 2 12  GLU 12  4   ?   ?   ?   B . n 
B 2 13  THR 13  5   ?   ?   ?   B . n 
B 2 14  PRO 14  6   ?   ?   ?   B . n 
B 2 15  PRO 15  7   ?   ?   ?   B . n 
B 2 16  PRO 16  8   ?   ?   ?   B . n 
B 2 17  LEU 17  9   ?   ?   ?   B . n 
B 2 18  VAL 18  10  ?   ?   ?   B . n 
B 2 19  PRO 19  11  ?   ?   ?   B . n 
B 2 20  PRO 20  12  ?   ?   ?   B . n 
B 2 21  ALA 21  13  ?   ?   ?   B . n 
B 2 22  ALA 22  14  ?   ?   ?   B . n 
B 2 23  ARG 23  15  ?   ?   ?   B . n 
B 2 24  GLU 24  16  ?   ?   ?   B . n 
B 2 25  TRP 25  17  ?   ?   ?   B . n 
B 2 26  ASN 26  18  ?   ?   ?   B . n 
B 2 27  LEU 27  19  ?   ?   ?   B . n 
B 2 28  PRO 28  20  ?   ?   ?   B . n 
B 2 29  PRO 29  21  ?   ?   ?   B . n 
B 2 30  ASN 30  22  ?   ?   ?   B . n 
B 2 31  ALA 31  23  ?   ?   ?   B . n 
B 2 32  PRO 32  24  ?   ?   ?   B . n 
B 2 33  ALA 33  25  ?   ?   ?   B . n 
B 2 34  CYS 34  26  ?   ?   ?   B . n 
B 2 35  MET 35  27  ?   ?   ?   B . n 
B 2 36  GLU 36  28  28  GLU GLU B . n 
B 2 37  ARG 37  29  29  ARG ARG B . n 
B 2 38  GLN 38  30  30  GLN GLN B . n 
B 2 39  LEU 39  31  31  LEU LEU B . n 
B 2 40  GLU 40  32  32  GLU GLU B . n 
B 2 41  ALA 41  33  33  ALA ALA B . n 
B 2 42  ALA 42  34  34  ALA ALA B . n 
B 2 43  ARG 43  35  35  ARG ARG B . n 
B 2 44  TYR 44  36  36  TYR TYR B . n 
B 2 45  ARG 45  37  37  ARG ARG B . n 
B 2 46  SER 46  38  38  SER SER B . n 
B 2 47  ASP 47  39  39  ASP ASP B . n 
B 2 48  GLY 48  40  40  GLY GLY B . n 
B 2 49  ALA 49  41  41  ALA ALA B . n 
B 2 50  LEU 50  42  42  LEU LEU B . n 
B 2 51  LEU 51  43  43  LEU LEU B . n 
B 2 52  LEU 52  44  44  LEU LEU B . n 
B 2 53  GLY 53  45  45  GLY GLY B . n 
B 2 54  ALA 54  46  46  ALA ALA B . n 
B 2 55  SER 55  47  47  SER SER B . n 
B 2 56  SER 56  48  48  SER SER B . n 
B 2 57  LEU 57  49  49  LEU LEU B . n 
B 2 58  SER 58  50  50  SER SER B . n 
B 2 59  GLY 59  51  51  GLY GLY B . n 
B 2 60  ARG 60  52  52  ARG ARG B . n 
B 2 61  CYS 61  53  53  CYS CYS B . n 
B 2 62  TRP 62  54  54  TRP TRP B . n 
B 2 63  ALA 63  55  55  ALA ALA B . n 
B 2 64  GLY 64  56  56  GLY GLY B . n 
B 2 65  SER 65  57  57  SER SER B . n 
B 2 66  LEU 66  58  58  LEU LEU B . n 
B 2 67  TRP 67  59  59  TRP TRP B . n 
B 2 68  LEU 68  60  60  LEU LEU B . n 
B 2 69  PHE 69  61  61  PHE PHE B . n 
B 2 70  LYS 70  62  62  LYS LYS B . n 
B 2 71  ASP 71  63  63  ASP ASP B . n 
B 2 72  PRO 72  64  64  PRO PRO B . n 
B 2 73  CYS 73  65  65  CYS CYS B . n 
B 2 74  ALA 74  66  66  ALA ALA B . n 
B 2 75  ALA 75  67  67  ALA ALA B . n 
B 2 76  PRO 76  68  68  PRO PRO B . n 
B 2 77  ASN 77  69  69  ASN ASN B . n 
B 2 78  GLU 78  70  70  GLU GLU B . n 
B 2 79  GLY 79  71  71  GLY GLY B . n 
B 2 80  PHE 80  72  72  PHE PHE B . n 
B 2 81  CYS 81  73  73  CYS CYS B . n 
B 2 82  SER 82  74  74  SER SER B . n 
B 2 83  ALA 83  75  75  ALA ALA B . n 
B 2 84  GLY 84  76  76  GLY GLY B . n 
B 2 85  VAL 85  77  77  VAL VAL B . n 
B 2 86  GLN 86  78  78  GLN GLN B . n 
B 2 87  THR 87  79  79  THR THR B . n 
B 2 88  GLU 88  80  80  GLU GLU B . n 
B 2 89  ALA 89  81  81  ALA ALA B . n 
B 2 90  GLY 90  82  82  GLY GLY B . n 
B 2 91  VAL 91  83  83  VAL VAL B . n 
B 2 92  ALA 92  84  84  ALA ALA B . n 
B 2 93  ASP 93  85  85  ASP ASP B . n 
B 2 94  LEU 94  86  86  LEU LEU B . n 
B 2 95  THR 95  87  87  THR THR B . n 
B 2 96  TRP 96  88  88  TRP TRP B . n 
B 2 97  VAL 97  89  89  VAL VAL B . n 
B 2 98  GLY 98  90  90  GLY GLY B . n 
B 2 99  GLU 99  91  91  GLU GLU B . n 
B 2 100 ARG 100 92  92  ARG ARG B . n 
B 2 101 GLY 101 93  93  GLY GLY B . n 
B 2 102 ILE 102 94  94  ILE ILE B . n 
B 2 103 LEU 103 95  95  LEU LEU B . n 
B 2 104 VAL 104 96  96  VAL VAL B . n 
B 2 105 ALA 105 97  97  ALA ALA B . n 
B 2 106 SER 106 98  98  SER SER B . n 
B 2 107 ASP 107 99  99  ASP ASP B . n 
B 2 108 SER 108 100 100 SER SER B . n 
B 2 109 GLY 109 101 101 GLY GLY B . n 
B 2 110 ALA 110 102 102 ALA ALA B . n 
B 2 111 VAL 111 103 103 VAL VAL B . n 
B 2 112 GLU 112 104 104 GLU GLU B . n 
B 2 113 LEU 113 105 105 LEU LEU B . n 
B 2 114 TRP 114 106 106 TRP TRP B . n 
B 2 115 GLU 115 107 107 GLU GLU B . n 
B 2 116 LEU 116 108 108 LEU LEU B . n 
B 2 117 ASP 117 109 109 ASP ASP B . n 
B 2 118 GLU 118 110 110 GLU GLU B . n 
B 2 119 ASN 119 111 111 ASN ASN B . n 
B 2 120 GLU 120 112 112 GLU GLU B . n 
B 2 121 THR 121 113 113 THR THR B . n 
B 2 122 LEU 122 114 114 LEU LEU B . n 
B 2 123 ILE 123 115 115 ILE ILE B . n 
B 2 124 VAL 124 116 116 VAL VAL B . n 
B 2 125 SER 125 117 117 SER SER B . n 
B 2 126 LYS 126 118 118 LYS LYS B . n 
B 2 127 PHE 127 119 119 PHE PHE B . n 
B 2 128 CYS 128 120 120 CYS CYS B . n 
B 2 129 LYS 129 121 121 LYS LYS B . n 
B 2 130 TYR 130 122 122 TYR TYR B . n 
B 2 131 GLU 131 123 123 GLU GLU B . n 
B 2 132 HIS 132 124 124 HIS HIS B . n 
B 2 133 ASP 133 125 125 ASP ASP B . n 
B 2 134 ASP 134 126 126 ASP ASP B . n 
B 2 135 ILE 135 127 127 ILE ILE B . n 
B 2 136 VAL 136 128 128 VAL VAL B . n 
B 2 137 SER 137 129 129 SER SER B . n 
B 2 138 THR 138 130 130 THR THR B . n 
B 2 139 VAL 139 131 131 VAL VAL B . n 
B 2 140 SER 140 132 132 SER SER B . n 
B 2 141 VAL 141 133 133 VAL VAL B . n 
B 2 142 LEU 142 134 134 LEU LEU B . n 
B 2 143 SER 143 135 135 SER SER B . n 
B 2 144 SER 144 136 136 SER SER B . n 
B 2 145 GLY 145 137 137 GLY GLY B . n 
B 2 146 THR 146 138 138 THR THR B . n 
B 2 147 GLN 147 139 139 GLN GLN B . n 
B 2 148 ALA 148 140 140 ALA ALA B . n 
B 2 149 VAL 149 141 141 VAL VAL B . n 
B 2 150 SER 150 142 142 SER SER B . n 
B 2 151 GLY 151 143 143 GLY GLY B . n 
B 2 152 SER 152 144 144 SER SER B . n 
B 2 153 LYS 153 145 145 LYS LYS B . n 
B 2 154 ASP 154 146 146 ASP ASP B . n 
B 2 155 ILE 155 147 147 ILE ILE B . n 
B 2 156 CYS 156 148 148 CYS CYS B . n 
B 2 157 ILE 157 149 149 ILE ILE B . n 
B 2 158 LYS 158 150 150 LYS LYS B . n 
B 2 159 VAL 159 151 151 VAL VAL B . n 
B 2 160 TRP 160 152 152 TRP TRP B . n 
B 2 161 ASP 161 153 153 ASP ASP B . n 
B 2 162 LEU 162 154 154 LEU LEU B . n 
B 2 163 ALA 163 155 155 ALA ALA B . n 
B 2 164 GLN 164 156 156 GLN GLN B . n 
B 2 165 GLN 165 157 157 GLN GLN B . n 
B 2 166 VAL 166 158 158 VAL VAL B . n 
B 2 167 VAL 167 159 159 VAL VAL B . n 
B 2 168 LEU 168 160 160 LEU LEU B . n 
B 2 169 SER 169 161 161 SER SER B . n 
B 2 170 SER 170 162 162 SER SER B . n 
B 2 171 TYR 171 163 163 TYR TYR B . n 
B 2 172 ARG 172 164 164 ARG ARG B . n 
B 2 173 ALA 173 165 165 ALA ALA B . n 
B 2 174 HIS 174 166 166 HIS HIS B . n 
B 2 175 ALA 175 167 167 ALA ALA B . n 
B 2 176 ALA 176 168 168 ALA ALA B . n 
B 2 177 GLN 177 169 169 GLN GLN B . n 
B 2 178 VAL 178 170 170 VAL VAL B . n 
B 2 179 THR 179 171 171 THR THR B . n 
B 2 180 CYS 180 172 172 CYS CYS B . n 
B 2 181 VAL 181 173 173 VAL VAL B . n 
B 2 182 ALA 182 174 174 ALA ALA B . n 
B 2 183 ALA 183 175 175 ALA ALA B . n 
B 2 184 SER 184 176 176 SER SER B . n 
B 2 185 PRO 185 177 177 PRO PRO B . n 
B 2 186 HIS 186 178 178 HIS HIS B . n 
B 2 187 LYS 187 179 179 LYS LYS B . n 
B 2 188 ASP 188 180 180 ASP ASP B . n 
B 2 189 SER 189 181 181 SER SER B . n 
B 2 190 VAL 190 182 182 VAL VAL B . n 
B 2 191 PHE 191 183 183 PHE PHE B . n 
B 2 192 LEU 192 184 184 LEU LEU B . n 
B 2 193 SER 193 185 185 SER SER B . n 
B 2 194 CYS 194 186 186 CYS CYS B . n 
B 2 195 SER 195 187 187 SER SER B . n 
B 2 196 GLU 196 188 188 GLU GLU B . n 
B 2 197 ASP 197 189 189 ASP ASP B . n 
B 2 198 ASN 198 190 190 ASN ASN B . n 
B 2 199 ARG 199 191 191 ARG ARG B . n 
B 2 200 ILE 200 192 192 ILE ILE B . n 
B 2 201 LEU 201 193 193 LEU LEU B . n 
B 2 202 LEU 202 194 194 LEU LEU B . n 
B 2 203 TRP 203 195 195 TRP TRP B . n 
B 2 204 ASP 204 196 196 ASP ASP B . n 
B 2 205 THR 205 197 197 THR THR B . n 
B 2 206 ARG 206 198 198 ARG ARG B . n 
B 2 207 CYS 207 199 199 CYS CYS B . n 
B 2 208 PRO 208 200 200 PRO PRO B . n 
B 2 209 LYS 209 201 201 LYS LYS B . n 
B 2 210 PRO 210 202 202 PRO PRO B . n 
B 2 211 ALA 211 203 203 ALA ALA B . n 
B 2 212 SER 212 204 204 SER SER B . n 
B 2 213 GLN 213 205 205 GLN GLN B . n 
B 2 214 ILE 214 206 206 ILE ILE B . n 
B 2 215 GLY 215 207 207 GLY GLY B . n 
B 2 216 CYS 216 208 208 CYS CYS B . n 
B 2 217 SER 217 209 209 SER SER B . n 
B 2 218 ALA 218 210 210 ALA ALA B . n 
B 2 219 PRO 219 211 211 PRO PRO B . n 
B 2 220 GLY 220 212 212 GLY GLY B . n 
B 2 221 TYR 221 213 213 TYR TYR B . n 
B 2 222 LEU 222 214 214 LEU LEU B . n 
B 2 223 PRO 223 215 215 PRO PRO B . n 
B 2 224 THR 224 216 216 THR THR B . n 
B 2 225 SER 225 217 217 SER SER B . n 
B 2 226 LEU 226 218 218 LEU LEU B . n 
B 2 227 ALA 227 219 219 ALA ALA B . n 
B 2 228 TRP 228 220 220 TRP TRP B . n 
B 2 229 HIS 229 221 221 HIS HIS B . n 
B 2 230 PRO 230 222 222 PRO PRO B . n 
B 2 231 GLN 231 223 223 GLN GLN B . n 
B 2 232 GLN 232 224 224 GLN GLN B . n 
B 2 233 SER 233 225 225 SER SER B . n 
B 2 234 GLU 234 226 226 GLU GLU B . n 
B 2 235 VAL 235 227 227 VAL VAL B . n 
B 2 236 PHE 236 228 228 PHE PHE B . n 
B 2 237 VAL 237 229 229 VAL VAL B . n 
B 2 238 PHE 238 230 230 PHE PHE B . n 
B 2 239 GLY 239 231 231 GLY GLY B . n 
B 2 240 ASP 240 232 232 ASP ASP B . n 
B 2 241 GLU 241 233 233 GLU GLU B . n 
B 2 242 ASN 242 234 234 ASN ASN B . n 
B 2 243 GLY 243 235 235 GLY GLY B . n 
B 2 244 THR 244 236 236 THR THR B . n 
B 2 245 VAL 245 237 237 VAL VAL B . n 
B 2 246 SER 246 238 238 SER SER B . n 
B 2 247 LEU 247 239 239 LEU LEU B . n 
B 2 248 VAL 248 240 240 VAL VAL B . n 
B 2 249 ASP 249 241 241 ASP ASP B . n 
B 2 250 THR 250 242 242 THR THR B . n 
B 2 251 LYS 251 243 243 LYS LYS B . n 
B 2 252 SER 252 244 244 SER SER B . n 
B 2 253 THR 253 245 245 THR THR B . n 
B 2 254 SER 254 246 246 SER SER B . n 
B 2 255 CYS 255 247 247 CYS CYS B . n 
B 2 256 VAL 256 248 248 VAL VAL B . n 
B 2 257 LEU 257 249 249 LEU LEU B . n 
B 2 258 SER 258 250 250 SER SER B . n 
B 2 259 SER 259 251 251 SER SER B . n 
B 2 260 ALA 260 252 252 ALA ALA B . n 
B 2 261 VAL 261 253 253 VAL VAL B . n 
B 2 262 HIS 262 254 254 HIS HIS B . n 
B 2 263 SER 263 255 255 SER SER B . n 
B 2 264 GLN 264 256 256 GLN GLN B . n 
B 2 265 CYS 265 257 257 CYS CYS B . n 
B 2 266 VAL 266 258 258 VAL VAL B . n 
B 2 267 THR 267 259 259 THR THR B . n 
B 2 268 GLY 268 260 260 GLY GLY B . n 
B 2 269 LEU 269 261 261 LEU LEU B . n 
B 2 270 VAL 270 262 262 VAL VAL B . n 
B 2 271 PHE 271 263 263 PHE PHE B . n 
B 2 272 SER 272 264 264 SER SER B . n 
B 2 273 PRO 273 265 265 PRO PRO B . n 
B 2 274 HIS 274 266 266 HIS HIS B . n 
B 2 275 SER 275 267 267 SER SER B . n 
B 2 276 VAL 276 268 268 VAL VAL B . n 
B 2 277 PRO 277 269 269 PRO PRO B . n 
B 2 278 PHE 278 270 270 PHE PHE B . n 
B 2 279 LEU 279 271 271 LEU LEU B . n 
B 2 280 ALA 280 272 272 ALA ALA B . n 
B 2 281 SER 281 273 273 SER SER B . n 
B 2 282 LEU 282 274 274 LEU LEU B . n 
B 2 283 SER 283 275 275 SER SER B . n 
B 2 284 GLU 284 276 276 GLU GLU B . n 
B 2 285 ASP 285 277 277 ASP ASP B . n 
B 2 286 CYS 286 278 278 CYS CYS B . n 
B 2 287 SER 287 279 279 SER SER B . n 
B 2 288 LEU 288 280 280 LEU LEU B . n 
B 2 289 ALA 289 281 281 ALA ALA B . n 
B 2 290 VAL 290 282 282 VAL VAL B . n 
B 2 291 LEU 291 283 283 LEU LEU B . n 
B 2 292 ASP 292 284 284 ASP ASP B . n 
B 2 293 SER 293 285 285 SER SER B . n 
B 2 294 SER 294 286 286 SER SER B . n 
B 2 295 LEU 295 287 287 LEU LEU B . n 
B 2 296 SER 296 288 288 SER SER B . n 
B 2 297 GLU 297 289 289 GLU GLU B . n 
B 2 298 LEU 298 290 290 LEU LEU B . n 
B 2 299 PHE 299 291 291 PHE PHE B . n 
B 2 300 ARG 300 292 292 ARG ARG B . n 
B 2 301 SER 301 293 293 SER SER B . n 
B 2 302 GLN 302 294 294 GLN GLN B . n 
B 2 303 ALA 303 295 295 ALA ALA B . n 
B 2 304 HIS 304 296 296 HIS HIS B . n 
B 2 305 ARG 305 297 297 ARG ARG B . n 
B 2 306 ASP 306 298 298 ASP ASP B . n 
B 2 307 PHE 307 299 299 PHE PHE B . n 
B 2 308 VAL 308 300 300 VAL VAL B . n 
B 2 309 ARG 309 301 301 ARG ARG B . n 
B 2 310 ASP 310 302 302 ASP ASP B . n 
B 2 311 ALA 311 303 303 ALA ALA B . n 
B 2 312 THR 312 304 304 THR THR B . n 
B 2 313 TRP 313 305 305 TRP TRP B . n 
B 2 314 SER 314 306 306 SER SER B . n 
B 2 315 PRO 315 307 307 PRO PRO B . n 
B 2 316 LEU 316 308 308 LEU LEU B . n 
B 2 317 ASN 317 309 309 ASN ASN B . n 
B 2 318 HIS 318 310 310 HIS HIS B . n 
B 2 319 SER 319 311 311 SER SER B . n 
B 2 320 LEU 320 312 312 LEU LEU B . n 
B 2 321 LEU 321 313 313 LEU LEU B . n 
B 2 322 THR 322 314 314 THR THR B . n 
B 2 323 THR 323 315 315 THR THR B . n 
B 2 324 VAL 324 316 316 VAL VAL B . n 
B 2 325 GLY 325 317 317 GLY GLY B . n 
B 2 326 TRP 326 318 318 TRP TRP B . n 
B 2 327 ASP 327 319 319 ASP ASP B . n 
B 2 328 HIS 328 320 320 HIS HIS B . n 
B 2 329 GLN 329 321 321 GLN GLN B . n 
B 2 330 VAL 330 322 322 VAL VAL B . n 
B 2 331 VAL 331 323 323 VAL VAL B . n 
B 2 332 HIS 332 324 324 HIS HIS B . n 
B 2 333 HIS 333 325 325 HIS HIS B . n 
B 2 334 VAL 334 326 326 VAL VAL B . n 
B 2 335 VAL 335 327 327 VAL VAL B . n 
B 2 336 PRO 336 328 328 PRO PRO B . n 
B 2 337 THR 337 329 ?   ?   ?   B . n 
B 2 338 GLU 338 330 ?   ?   ?   B . n 
B 2 339 PRO 339 331 ?   ?   ?   B . n 
B 2 340 LEU 340 332 ?   ?   ?   B . n 
B 2 341 PRO 341 333 ?   ?   ?   B . n 
B 2 342 ALA 342 334 ?   ?   ?   B . n 
B 2 343 PRO 343 335 ?   ?   ?   B . n 
B 2 344 GLY 344 336 ?   ?   ?   B . n 
B 2 345 PRO 345 337 ?   ?   ?   B . n 
B 2 346 ALA 346 338 ?   ?   ?   B . n 
B 2 347 SER 347 339 ?   ?   ?   B . n 
B 2 348 VAL 348 340 ?   ?   ?   B . n 
B 2 349 THR 349 341 ?   ?   ?   B . n 
B 2 350 GLU 350 342 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BLI 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BLI 
_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 
C  3 MTA   1  701 1   MTA   MTA A . 
D  4 A1BLI 1  702 1   A1BLI LIG A . 
E  5 EDO   1  703 1   EDO   EDO A . 
F  5 EDO   1  704 2   EDO   EDO A . 
G  5 EDO   1  705 3   EDO   EDO A . 
H  5 EDO   1  706 4   EDO   EDO A . 
I  5 EDO   1  707 5   EDO   EDO A . 
J  5 EDO   1  708 6   EDO   EDO A . 
K  5 EDO   1  709 7   EDO   EDO A . 
L  5 EDO   1  710 8   EDO   EDO A . 
M  5 EDO   1  711 9   EDO   EDO A . 
N  5 EDO   1  712 11  EDO   EDO A . 
O  5 EDO   1  713 12  EDO   EDO A . 
P  5 EDO   1  714 14  EDO   EDO A . 
Q  5 EDO   1  715 15  EDO   EDO A . 
R  5 EDO   1  716 16  EDO   EDO A . 
S  6 NA    1  717 2   NA    NA  A . 
T  6 NA    1  718 3   NA    NA  A . 
U  6 NA    1  719 4   NA    NA  A . 
V  6 NA    1  720 5   NA    NA  A . 
W  7 GOL   1  721 1   GOL   GOL A . 
X  8 CL    1  722 1   CL    CL  A . 
Y  5 EDO   1  401 10  EDO   EDO B . 
Z  5 EDO   1  402 13  EDO   EDO B . 
AA 9 HOH   1  801 34  HOH   HOH A . 
AA 9 HOH   2  802 36  HOH   HOH A . 
AA 9 HOH   3  803 11  HOH   HOH A . 
AA 9 HOH   4  804 43  HOH   HOH A . 
AA 9 HOH   5  805 9   HOH   HOH A . 
AA 9 HOH   6  806 2   HOH   HOH A . 
AA 9 HOH   7  807 79  HOH   HOH A . 
AA 9 HOH   8  808 16  HOH   HOH A . 
AA 9 HOH   9  809 68  HOH   HOH A . 
AA 9 HOH   10 810 38  HOH   HOH A . 
AA 9 HOH   11 811 4   HOH   HOH A . 
AA 9 HOH   12 812 44  HOH   HOH A . 
AA 9 HOH   13 813 78  HOH   HOH A . 
AA 9 HOH   14 814 55  HOH   HOH A . 
AA 9 HOH   15 815 15  HOH   HOH A . 
AA 9 HOH   16 816 13  HOH   HOH A . 
AA 9 HOH   17 817 90  HOH   HOH A . 
AA 9 HOH   18 818 14  HOH   HOH A . 
AA 9 HOH   19 819 39  HOH   HOH A . 
AA 9 HOH   20 820 8   HOH   HOH A . 
AA 9 HOH   21 821 1   HOH   HOH A . 
AA 9 HOH   22 822 98  HOH   HOH A . 
AA 9 HOH   23 823 73  HOH   HOH A . 
AA 9 HOH   24 824 3   HOH   HOH A . 
AA 9 HOH   25 825 66  HOH   HOH A . 
AA 9 HOH   26 826 28  HOH   HOH A . 
AA 9 HOH   27 827 70  HOH   HOH A . 
AA 9 HOH   28 828 92  HOH   HOH A . 
AA 9 HOH   29 829 100 HOH   HOH A . 
AA 9 HOH   30 830 106 HOH   HOH A . 
AA 9 HOH   31 831 76  HOH   HOH A . 
AA 9 HOH   32 832 87  HOH   HOH A . 
AA 9 HOH   33 833 5   HOH   HOH A . 
AA 9 HOH   34 834 27  HOH   HOH A . 
AA 9 HOH   35 835 77  HOH   HOH A . 
AA 9 HOH   36 836 40  HOH   HOH A . 
AA 9 HOH   37 837 74  HOH   HOH A . 
AA 9 HOH   38 838 18  HOH   HOH A . 
AA 9 HOH   39 839 65  HOH   HOH A . 
AA 9 HOH   40 840 12  HOH   HOH A . 
AA 9 HOH   41 841 111 HOH   HOH A . 
AA 9 HOH   42 842 17  HOH   HOH A . 
AA 9 HOH   43 843 56  HOH   HOH A . 
AA 9 HOH   44 844 105 HOH   HOH A . 
AA 9 HOH   45 845 110 HOH   HOH A . 
AA 9 HOH   46 846 6   HOH   HOH A . 
AA 9 HOH   47 847 31  HOH   HOH A . 
AA 9 HOH   48 848 99  HOH   HOH A . 
AA 9 HOH   49 849 35  HOH   HOH A . 
AA 9 HOH   50 850 85  HOH   HOH A . 
AA 9 HOH   51 851 95  HOH   HOH A . 
AA 9 HOH   52 852 7   HOH   HOH A . 
AA 9 HOH   53 853 69  HOH   HOH A . 
AA 9 HOH   54 854 67  HOH   HOH A . 
AA 9 HOH   55 855 21  HOH   HOH A . 
AA 9 HOH   56 856 49  HOH   HOH A . 
AA 9 HOH   57 857 29  HOH   HOH A . 
AA 9 HOH   58 858 33  HOH   HOH A . 
AA 9 HOH   59 859 41  HOH   HOH A . 
AA 9 HOH   60 860 83  HOH   HOH A . 
AA 9 HOH   61 861 109 HOH   HOH A . 
AA 9 HOH   62 862 108 HOH   HOH A . 
AA 9 HOH   63 863 26  HOH   HOH A . 
AA 9 HOH   64 864 54  HOH   HOH A . 
AA 9 HOH   65 865 71  HOH   HOH A . 
AA 9 HOH   66 866 89  HOH   HOH A . 
AA 9 HOH   67 867 88  HOH   HOH A . 
AA 9 HOH   68 868 32  HOH   HOH A . 
AA 9 HOH   69 869 24  HOH   HOH A . 
AA 9 HOH   70 870 107 HOH   HOH A . 
AA 9 HOH   71 871 50  HOH   HOH A . 
AA 9 HOH   72 872 72  HOH   HOH A . 
AA 9 HOH   73 873 93  HOH   HOH A . 
AA 9 HOH   74 874 113 HOH   HOH A . 
AA 9 HOH   75 875 48  HOH   HOH A . 
AA 9 HOH   76 876 81  HOH   HOH A . 
AA 9 HOH   77 877 101 HOH   HOH A . 
AA 9 HOH   78 878 112 HOH   HOH A . 
BA 9 HOH   1  501 46  HOH   HOH B . 
BA 9 HOH   2  502 10  HOH   HOH B . 
BA 9 HOH   3  503 103 HOH   HOH B . 
BA 9 HOH   4  504 61  HOH   HOH B . 
BA 9 HOH   5  505 64  HOH   HOH B . 
BA 9 HOH   6  506 19  HOH   HOH B . 
BA 9 HOH   7  507 97  HOH   HOH B . 
BA 9 HOH   8  508 25  HOH   HOH B . 
BA 9 HOH   9  509 75  HOH   HOH B . 
BA 9 HOH   10 510 42  HOH   HOH B . 
BA 9 HOH   11 511 58  HOH   HOH B . 
BA 9 HOH   12 512 51  HOH   HOH B . 
BA 9 HOH   13 513 63  HOH   HOH B . 
BA 9 HOH   14 514 86  HOH   HOH B . 
BA 9 HOH   15 515 47  HOH   HOH B . 
BA 9 HOH   16 516 60  HOH   HOH B . 
BA 9 HOH   17 517 20  HOH   HOH B . 
BA 9 HOH   18 518 57  HOH   HOH B . 
BA 9 HOH   19 519 22  HOH   HOH B . 
BA 9 HOH   20 520 91  HOH   HOH B . 
BA 9 HOH   21 521 96  HOH   HOH B . 
BA 9 HOH   22 522 104 HOH   HOH B . 
BA 9 HOH   23 523 37  HOH   HOH B . 
BA 9 HOH   24 524 30  HOH   HOH B . 
BA 9 HOH   25 525 59  HOH   HOH B . 
BA 9 HOH   26 526 80  HOH   HOH B . 
BA 9 HOH   27 527 62  HOH   HOH B . 
BA 9 HOH   28 528 45  HOH   HOH B . 
BA 9 HOH   29 529 94  HOH   HOH B . 
BA 9 HOH   30 530 52  HOH   HOH B . 
BA 9 HOH   31 531 102 HOH   HOH B . 
BA 9 HOH   32 532 84  HOH   HOH B . 
BA 9 HOH   33 533 23  HOH   HOH B . 
BA 9 HOH   34 534 53  HOH   HOH B . 
BA 9 HOH   35 535 82  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       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MGP 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     99.140 
_cell.length_a_esd                 ? 
_cell.length_b                     137.690 
_cell.length_b_esd                 ? 
_cell.length_c                     178.430 
_cell.length_c_esd                 ? 
_cell.volume                       2435674.167 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9MGP 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            'I 2 2' 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9MGP 
_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             2.73 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.90 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '10% PEG 4000, 0.1 M sodium citrate (pH 6.0), 0.2 M magnesium chloride' 
_exptl_crystal_grow.pdbx_pH_range   6.0 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-05-31 
_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   0.97853 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97853 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9MGP 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.67 
_reflns.d_resolution_low                               45.1 
_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                                     35013 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.01 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.093 
_reflns.pdbx_Rpim_I_all                                0.036 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.085 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.67 
_reflns_shell.d_res_low                                     2.80 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           29550 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4592 
_reflns_shell.percent_possible_obs                          99.9 
_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                               6.4 
_reflns_shell.pdbx_chi_squared                              0.95 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.2 
_reflns_shell.pdbx_Rrim_I_all                               0.770 
_reflns_shell.pdbx_Rpim_I_all                               0.302 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.934 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.707 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               80.02 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9MGP 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.67 
_refine.ls_d_res_low                             37.44 
_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                     34913 
_refine.ls_number_reflns_R_free                  1722 
_refine.ls_number_reflns_R_work                  33191 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.67 
_refine.ls_percent_reflns_R_free                 4.93 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2226 
_refine.ls_R_factor_R_free                       0.2708 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2200 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 33.2614 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.4477 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.67 
_refine_hist.d_res_low                        37.44 
_refine_hist.number_atoms_solvent             113 
_refine_hist.number_atoms_total               7560 
_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        7315 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         132 
_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' ? 0.0135  ? 7633  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.6749  ? 10367 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0898  ? 1134  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0032  ? 1333  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.6284 ? 2752  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.67 2.75  . . 146 2708 99.27 . . . . 0.4221 . . . . . . . . . . . 0.4189 
'X-RAY DIFFRACTION' 2.75 2.84  . . 117 2756 99.79 . . . . 0.3889 . . . . . . . . . . . 0.4051 
'X-RAY DIFFRACTION' 2.84 2.94  . . 149 2714 99.86 . . . . 0.3518 . . . . . . . . . . . 0.3836 
'X-RAY DIFFRACTION' 2.94 3.06  . . 133 2747 99.76 . . . . 0.2994 . . . . . . . . . . . 0.3634 
'X-RAY DIFFRACTION' 3.06 3.20  . . 137 2755 99.79 . . . . 0.2572 . . . . . . . . . . . 0.3214 
'X-RAY DIFFRACTION' 3.20 3.36  . . 158 2725 99.72 . . . . 0.2576 . . . . . . . . . . . 0.2944 
'X-RAY DIFFRACTION' 3.36 3.57  . . 148 2758 99.79 . . . . 0.2362 . . . . . . . . . . . 0.2910 
'X-RAY DIFFRACTION' 3.57 3.85  . . 130 2791 99.69 . . . . 0.2132 . . . . . . . . . . . 0.2776 
'X-RAY DIFFRACTION' 3.85 4.24  . . 162 2749 99.93 . . . . 0.1929 . . . . . . . . . . . 0.2400 
'X-RAY DIFFRACTION' 4.24 4.85  . . 138 2776 99.93 . . . . 0.1693 . . . . . . . . . . . 0.2131 
'X-RAY DIFFRACTION' 4.85 6.10  . . 154 2809 99.66 . . . . 0.1802 . . . . . . . . . . . 0.2508 
'X-RAY DIFFRACTION' 6.11 37.44 . . 150 2903 98.90 . . . . 0.1799 . . . . . . . . . . . 0.2343 
# 
_struct.entry_id                     9MGP 
_struct.title                        'Crystal structure of PRMT5:MEP50 in complex with MTA and compound 46a' 
_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        9MGP 
_struct_keywords.text            'methyltransferase, inhibitor, MTAP-null, TRANSFERASE, TRANSFERASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   TRANSFERASE/INHIBITOR 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 2 ? 
C  N N 3 ? 
D  N N 4 ? 
E  N N 5 ? 
F  N N 5 ? 
G  N N 5 ? 
H  N N 5 ? 
I  N N 5 ? 
J  N N 5 ? 
K  N N 5 ? 
L  N N 5 ? 
M  N N 5 ? 
N  N N 5 ? 
O  N N 5 ? 
P  N N 5 ? 
Q  N N 5 ? 
R  N N 5 ? 
S  N N 6 ? 
T  N N 6 ? 
U  N N 6 ? 
V  N N 6 ? 
W  N N 7 ? 
X  N N 8 ? 
Y  N N 5 ? 
Z  N N 5 ? 
AA N N 9 ? 
BA N N 9 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP ANM5_HUMAN  O14744 ? 1 
;AAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLLLSGRDWNTL
IVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPE
DLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKK
GFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLES
QTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLMVLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTL
ENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLY
NEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYQ
DITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRSYTIGL
;
2 
2 UNP MEP50_HUMAN Q9BQA1 ? 2 
;RKETPPPLVPPAAREWNLPPNAPACMERQLEAARYRSDGALLLGASSLSGRCWAGSLWLFKDPCAAPNEGFCSAGVQTEA
GVADLTWVGERGILVASDSGAVELWELDENETLIVSKFCKYEHDDIVSTVSVLSSGTQAVSGSKDICIKVWDLAQQVVLS
SYRAHAAQVTCVAASPHKDSVFLSCSEDNRILLWDTRCPKPASQIGCSAPGYLPTSLAWHPQQSEVFVFGDENGTVSLVD
TKSTSCVLSSAVHSQCVTGLVFSPHSVPFLASLSEDCSLAVLDSSLSELFRSQAHRDFVRDATWSPLNHSLLTTVGWDHQ
VVHHVVPTEPLPAPGPASVTE
;
2 
# 
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 9MGP A 10 ? 645 ? O14744 2 ? 637 ? 2 637 
2 2 9MGP B 10 ? 350 ? Q9BQA1 2 ? 342 ? 2 342 
# 
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 9MGP MET A 1 ? UNP O14744 ? ? 'initiating methionine' -7 1  
1 9MGP ASP A 2 ? UNP O14744 ? ? 'expression tag'        -6 2  
1 9MGP TYR A 3 ? UNP O14744 ? ? 'expression tag'        -5 3  
1 9MGP LYS A 4 ? UNP O14744 ? ? 'expression tag'        -4 4  
1 9MGP ASP A 5 ? UNP O14744 ? ? 'expression tag'        -3 5  
1 9MGP ASP A 6 ? UNP O14744 ? ? 'expression tag'        -2 6  
1 9MGP ASP A 7 ? UNP O14744 ? ? 'expression tag'        -1 7  
1 9MGP ASP A 8 ? UNP O14744 ? ? 'expression tag'        0  8  
1 9MGP LYS A 9 ? UNP O14744 ? ? 'expression tag'        1  9  
2 9MGP MET B 1 ? UNP Q9BQA1 ? ? 'initiating methionine' -7 10 
2 9MGP HIS B 2 ? UNP Q9BQA1 ? ? 'expression tag'        -6 11 
2 9MGP HIS B 3 ? UNP Q9BQA1 ? ? 'expression tag'        -5 12 
2 9MGP HIS B 4 ? UNP Q9BQA1 ? ? 'expression tag'        -4 13 
2 9MGP HIS B 5 ? UNP Q9BQA1 ? ? 'expression tag'        -3 14 
2 9MGP HIS B 6 ? UNP Q9BQA1 ? ? 'expression tag'        -2 15 
2 9MGP HIS B 7 ? UNP Q9BQA1 ? ? 'expression tag'        -1 16 
2 9MGP HIS B 8 ? UNP Q9BQA1 ? ? 'expression tag'        0  17 
2 9MGP HIS B 9 ? UNP Q9BQA1 ? ? 'expression tag'        1  18 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   octameric 
_pdbx_struct_assembly.oligomeric_count     8 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA 
1 2 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA 
1 3 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA 
1 4 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000    0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_545 -x,-y-1,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 -137.6900000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
3 'crystal symmetry operation' 3_555 -x,y,-z   -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000    0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_545 x,-y-1,-z 1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 -137.6900000000 0.0000000000 0.0000000000 -1.0000000000 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 GLU A 33  ? GLY A 45  ? GLU A 25  GLY A 37  1 ? 13 
HELX_P HELX_P2  AA2 PRO A 66  ? ARG A 70  ? PRO A 58  ARG A 62  5 ? 5  
HELX_P HELX_P3  AA3 SER A 77  ? LEU A 81  ? SER A 69  LEU A 73  5 ? 5  
HELX_P HELX_P4  AA4 SER A 82  ? LEU A 89  ? SER A 74  LEU A 81  1 ? 8  
HELX_P HELX_P5  AA5 VAL A 104 ? GLY A 126 ? VAL A 96  GLY A 118 1 ? 23 
HELX_P HELX_P6  AA6 ASN A 139 ? HIS A 151 ? ASN A 131 HIS A 143 1 ? 13 
HELX_P HELX_P7  AA7 ALA A 167 ? LEU A 171 ? ALA A 159 LEU A 163 5 ? 5  
HELX_P HELX_P8  AA8 SER A 188 ? GLU A 190 ? SER A 180 GLU A 182 5 ? 3  
HELX_P HELX_P9  AA9 GLU A 191 ? CYS A 204 ? GLU A 183 CYS A 196 1 ? 14 
HELX_P HELX_P10 AB1 SER A 222 ? ARG A 228 ? SER A 214 ARG A 220 1 ? 7  
HELX_P HELX_P11 AB2 SER A 242 ? PHE A 244 ? SER A 234 PHE A 236 5 ? 3  
HELX_P HELX_P12 AB3 SER A 255 ? LEU A 268 ? SER A 247 LEU A 260 1 ? 14 
HELX_P HELX_P13 AB4 PHE A 285 ? GLN A 297 ? PHE A 277 GLN A 289 1 ? 13 
HELX_P HELX_P14 AB5 ASN A 303 ? ALA A 309 ? ASN A 295 ALA A 301 1 ? 7  
HELX_P HELX_P15 AB6 GLU A 328 ? VAL A 334 ? GLU A 320 VAL A 326 1 ? 7  
HELX_P HELX_P16 AB7 ASP A 338 ? VAL A 357 ? ASP A 330 VAL A 349 1 ? 20 
HELX_P HELX_P17 AB8 GLY A 377 ? ASP A 391 ? GLY A 369 ASP A 383 1 ? 15 
HELX_P HELX_P18 AB9 ASN A 402 ? GLU A 416 ? ASN A 394 GLU A 408 1 ? 15 
HELX_P HELX_P19 AC1 LEU A 453 ? ALA A 461 ? LEU A 445 ALA A 453 1 ? 9  
HELX_P HELX_P20 AC2 SER A 485 ? ALA A 494 ? SER A 477 ALA A 486 1 ? 10 
HELX_P HELX_P21 AC3 GLU A 503 ? GLU A 507 ? GLU A 495 GLU A 499 5 ? 5  
HELX_P HELX_P22 AC4 ARG A 576 ? HIS A 580 ? ARG A 568 HIS A 572 5 ? 5  
HELX_P HELX_P23 AC5 ASN A 635 ? ARG A 639 ? ASN A 627 ARG A 631 5 ? 5  
HELX_P HELX_P24 AC6 ASP B 71  ? ALA B 75  ? ASP B 63  ALA B 67  5 ? 5  
HELX_P HELX_P25 AC7 ASN B 77  ? CYS B 81  ? ASN B 69  CYS B 73  5 ? 5  
# 
_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 ? ? B CYS 216 SG ? ? ? 1_555 B  CYS 255 SG ? ? B CYS 208 B CYS 247 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc1 metalc ? ? V NA  .   NA ? ? ? 1_555 AA HOH .   O  ? ? A NA  720 A HOH 858 1_555 ? ? ? ? ? ? ? 3.139 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       216 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      255 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        208 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       247 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 65  A . ? GLU 57  A PRO 66  A ? PRO 58  A 1 0.86  
2 GLY 72  A . ? GLY 64  A PRO 73  A ? PRO 65  A 1 -2.07 
3 PRO 302 A . ? PRO 294 A ASN 303 A ? ASN 295 A 1 2.69  
4 ILE 472 A . ? ILE 464 A PRO 473 A ? PRO 465 A 1 7.29  
5 HIS 531 A . ? HIS 523 A PRO 532 A ? PRO 524 A 1 -1.80 
6 ALA 627 A . ? ALA 619 A PRO 628 A ? PRO 620 A 1 1.92  
7 ALA 75  B . ? ALA 67  B PRO 76  B ? PRO 68  B 1 3.21  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 2 ? 
AA3 ? 5 ? 
AA4 ? 5 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 4 ? 
AB4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA1 8 9 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 24  ? ASP A 27  ? SER A 16  ASP A 19  
AA1 2 PHE A 48  ? CYS A 50  ? PHE A 40  CYS A 42  
AA1 3 ILE A 90  ? LYS A 93  ? ILE A 82  LYS A 85  
AA1 4 ALA A 129 ? PRO A 133 ? ALA A 121 PRO A 125 
AA1 5 MET A 158 ? PRO A 164 ? MET A 150 PRO A 156 
AA1 6 ILE A 210 ? GLU A 215 ? ILE A 202 GLU A 207 
AA1 7 ILE A 234 ? PRO A 240 ? ILE A 226 PRO A 232 
AA1 8 GLN A 271 ? THR A 275 ? GLN A 263 THR A 267 
AA1 9 SER A 24  ? ASP A 27  ? SER A 16  ASP A 19  
AA2 1 LEU A 245 ? THR A 246 ? LEU A 237 THR A 238 
AA2 2 PRO A 252 ? VAL A 253 ? PRO A 244 VAL A 245 
AA3 1 VAL A 421 ? VAL A 424 ? VAL A 413 VAL A 416 
AA3 2 ARG A 393 ? VAL A 399 ? ARG A 385 VAL A 391 
AA3 3 VAL A 366 ? LEU A 372 ? VAL A 358 LEU A 364 
AA3 4 ALA A 437 ? SER A 442 ? ALA A 429 SER A 434 
AA3 5 LEU A 465 ? ILE A 472 ? LEU A 457 ILE A 464 
AA4 1 TYR A 510 ? VAL A 511 ? TYR A 502 VAL A 503 
AA4 2 ILE A 590 ? VAL A 600 ? ILE A 582 VAL A 592 
AA4 3 THR A 554 ? TYR A 568 ? THR A 546 TYR A 560 
AA4 4 GLU A 475 ? SER A 484 ? GLU A 467 SER A 476 
AA4 5 GLN A 524 ? SER A 530 ? GLN A 516 SER A 522 
AA5 1 HIS A 518 ? GLN A 519 ? HIS A 510 GLN A 511 
AA5 2 GLU A 475 ? SER A 484 ? GLU A 467 SER A 476 
AA5 3 THR A 554 ? TYR A 568 ? THR A 546 TYR A 560 
AA5 4 ILE A 571 ? SER A 574 ? ILE A 563 SER A 566 
AA6 1 ARG A 542 ? PRO A 549 ? ARG A 534 PRO A 541 
AA6 2 THR A 605 ? SER A 614 ? THR A 597 SER A 606 
AA6 3 LYS A 618 ? ALA A 627 ? LYS A 610 ALA A 619 
AA6 4 ILE A 643 ? GLY A 644 ? ILE A 635 GLY A 636 
AA7 1 GLN B 38  ? TYR B 44  ? GLN B 30  TYR B 36  
AA7 2 LEU B 50  ? SER B 55  ? LEU B 42  SER B 47  
AA7 3 GLY B 64  ? PHE B 69  ? GLY B 56  PHE B 61  
AA7 4 ALA B 83  ? THR B 87  ? ALA B 75  THR B 79  
AA8 1 VAL B 91  ? VAL B 97  ? VAL B 83  VAL B 89  
AA8 2 GLY B 101 ? SER B 106 ? GLY B 93  SER B 98  
AA8 3 VAL B 111 ? LEU B 116 ? VAL B 103 LEU B 108 
AA8 4 ILE B 123 ? LYS B 129 ? ILE B 115 LYS B 121 
AA9 1 VAL B 136 ? VAL B 141 ? VAL B 128 VAL B 133 
AA9 2 GLN B 147 ? SER B 152 ? GLN B 139 SER B 144 
AA9 3 ILE B 157 ? ASP B 161 ? ILE B 149 ASP B 153 
AA9 4 VAL B 166 ? TYR B 171 ? VAL B 158 TYR B 163 
AB1 1 VAL B 178 ? ALA B 183 ? VAL B 170 ALA B 175 
AB1 2 VAL B 190 ? SER B 195 ? VAL B 182 SER B 187 
AB1 3 ILE B 200 ? ASP B 204 ? ILE B 192 ASP B 196 
AB1 4 ALA B 211 ? GLN B 213 ? ALA B 203 GLN B 205 
AB2 1 PRO B 223 ? TRP B 228 ? PRO B 215 TRP B 220 
AB2 2 VAL B 235 ? ASP B 240 ? VAL B 227 ASP B 232 
AB2 3 THR B 244 ? ASP B 249 ? THR B 236 ASP B 241 
AB2 4 CYS B 255 ? ALA B 260 ? CYS B 247 ALA B 252 
AB3 1 GLY B 268 ? PHE B 271 ? GLY B 260 PHE B 263 
AB3 2 LEU B 279 ? LEU B 282 ? LEU B 271 LEU B 274 
AB3 3 LEU B 288 ? LEU B 291 ? LEU B 280 LEU B 283 
AB3 4 GLU B 297 ? SER B 301 ? GLU B 289 SER B 293 
AB4 1 VAL B 308 ? TRP B 313 ? VAL B 300 TRP B 305 
AB4 2 LEU B 320 ? GLY B 325 ? LEU B 312 GLY B 317 
AB4 3 VAL B 330 ? VAL B 334 ? VAL B 322 VAL B 326 
# 
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 ARG A 26  ? N ARG A 18  O CYS A 50  ? O CYS A 42  
AA1 2 3 N LEU A 49  ? N LEU A 41  O VAL A 91  ? O VAL A 83  
AA1 3 4 N GLY A 92  ? N GLY A 84  O LEU A 131 ? O LEU A 123 
AA1 4 5 N LEU A 132 ? N LEU A 124 O ARG A 162 ? O ARG A 154 
AA1 5 6 N VAL A 163 ? N VAL A 155 O GLU A 215 ? O GLU A 207 
AA1 6 7 N LEU A 214 ? N LEU A 206 O ILE A 238 ? O ILE A 230 
AA1 7 8 N LEU A 239 ? N LEU A 231 O ILE A 273 ? O ILE A 265 
AA1 8 9 O ILE A 274 ? O ILE A 266 N ASP A 27  ? N ASP A 19  
AA2 1 2 N LEU A 245 ? N LEU A 237 O VAL A 253 ? O VAL A 245 
AA3 1 2 O THR A 422 ? O THR A 414 N ALA A 398 ? N ALA A 390 
AA3 2 3 O LYS A 395 ? O LYS A 387 N LEU A 369 ? N LEU A 361 
AA3 3 4 N VAL A 368 ? N VAL A 360 O ASP A 438 ? O ASP A 430 
AA3 4 5 N ALA A 437 ? N ALA A 429 O LYS A 466 ? O LYS A 458 
AA4 1 2 N TYR A 510 ? N TYR A 502 O LEU A 591 ? O LEU A 583 
AA4 2 3 O ILE A 590 ? O ILE A 582 N GLY A 561 ? N GLY A 553 
AA4 3 4 O GLU A 564 ? O GLU A 556 N THR A 477 ? N THR A 469 
AA4 4 5 N SER A 478 ? N SER A 470 O CYS A 526 ? O CYS A 518 
AA5 1 2 O HIS A 518 ? O HIS A 510 N SER A 484 ? N SER A 476 
AA5 2 3 N THR A 477 ? N THR A 469 O GLU A 564 ? O GLU A 556 
AA5 3 4 N TYR A 568 ? N TYR A 560 O ILE A 571 ? O ILE A 563 
AA6 1 2 N PHE A 548 ? N PHE A 540 O ILE A 606 ? O ILE A 598 
AA6 2 3 N CYS A 607 ? N CYS A 599 O THR A 626 ? O THR A 618 
AA6 3 4 N VAL A 619 ? N VAL A 611 O ILE A 643 ? O ILE A 635 
AA7 1 2 N ARG B 43  ? N ARG B 35  O LEU B 51  ? O LEU B 43  
AA7 2 3 N LEU B 50  ? N LEU B 42  O PHE B 69  ? O PHE B 61  
AA7 3 4 N LEU B 66  ? N LEU B 58  O VAL B 85  ? O VAL B 77  
AA8 1 2 N ALA B 92  ? N ALA B 84  O ALA B 105 ? O ALA B 97  
AA8 2 3 N VAL B 104 ? N VAL B 96  O GLU B 112 ? O GLU B 104 
AA8 3 4 N GLU B 115 ? N GLU B 107 O VAL B 124 ? O VAL B 116 
AA9 1 2 N THR B 138 ? N THR B 130 O GLY B 151 ? O GLY B 143 
AA9 2 3 N ALA B 148 ? N ALA B 140 O TRP B 160 ? O TRP B 152 
AA9 3 4 N ILE B 157 ? N ILE B 149 O TYR B 171 ? O TYR B 163 
AB1 1 2 N ALA B 182 ? N ALA B 174 O LEU B 192 ? O LEU B 184 
AB1 2 3 N SER B 193 ? N SER B 185 O LEU B 201 ? O LEU B 193 
AB1 3 4 N LEU B 202 ? N LEU B 194 O SER B 212 ? O SER B 204 
AB2 1 2 N THR B 224 ? N THR B 216 O GLY B 239 ? O GLY B 231 
AB2 2 3 N PHE B 236 ? N PHE B 228 O VAL B 248 ? O VAL B 240 
AB2 3 4 N LEU B 247 ? N LEU B 239 O LEU B 257 ? O LEU B 249 
AB3 1 2 N GLY B 268 ? N GLY B 260 O LEU B 282 ? O LEU B 274 
AB3 2 3 N SER B 281 ? N SER B 273 O ALA B 289 ? O ALA B 281 
AB3 3 4 N VAL B 290 ? N VAL B 282 O LEU B 298 ? O LEU B 290 
AB4 1 2 N THR B 312 ? N THR B 304 O THR B 322 ? O THR B 314 
AB4 2 3 N LEU B 321 ? N LEU B 313 O HIS B 333 ? O HIS B 325 
# 
_pdbx_entry_details.entry_id                   9MGP 
_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_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 61  ? ? -100.30 40.16   
2  1 HIS A 143 ? ? -92.76  32.16   
3  1 THR A 144 ? ? -113.67 70.02   
4  1 HIS A 146 ? ? -68.20  92.74   
5  1 ALA A 171 ? ? -156.55 82.88   
6  1 ASP A 197 ? ? 71.97   43.10   
7  1 PRO A 293 ? ? -99.80  52.91   
8  1 PRO A 350 ? ? -59.09  171.96  
9  1 ASP A 383 ? ? 62.96   61.51   
10 1 GLU A 435 ? ? -148.72 30.06   
11 1 ALA A 441 ? ? 65.91   -74.84  
12 1 GLU A 499 ? ? -99.22  34.71   
13 1 HIS A 507 ? ? -123.61 -73.17  
14 1 CYS A 518 ? ? -105.74 -73.13  
15 1 GLN A 561 ? ? 48.64   -108.66 
16 1 ASN A 607 ? ? -119.74 -162.18 
17 1 LEU B 114 ? ? -170.08 133.60  
18 1 LYS B 118 ? ? -92.49  -61.44  
19 1 ILE B 147 ? ? 86.71   -9.53   
20 1 HIS B 266 ? ? -49.08  151.36  
# 
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 22.9567439603 -93.0320949562 -17.8813576925 0.965090780993 ? 0.243877039156   ? 0.0464655581794  
? 0.672615360283 ? -0.0364029575179  ? 0.293395571917 ? 3.52661960025  ? 0.613777917413   ? 0.507854961409  ? 2.98814335311 ? 
-0.0249650243292 ? 1.8781468576  ? -0.130855076241  ? -0.283507043345  ? -0.245119013125  ? 0.263587148377  ? -0.000123009938495 ? 
-0.0166138860091 ? 0.565999086216   ? 0.416734715006    ? 0.130998930658   ? 
2  'X-RAY DIFFRACTION' ? refined 26.9722278496 -71.117125185  -27.4278452003 0.828129704656 ? 0.0648221672361  ? 0.0928603853883  
? 0.803360645035 ? 0.0554279969624   ? 0.402409380279 ? 0.791741603813 ? -0.418302176676  ? -0.288606690441 ? 3.44674291025 ? 
1.57589364842    ? 2.39291435414 ? 0.0845344808114  ? 0.141451614748   ? 0.0892679114582  ? -0.413238020046 ? 0.0498587987793    ? 
-0.363328649902  ? -0.179971924111  ? 0.734799515458    ? -0.135292892275  ? 
3  'X-RAY DIFFRACTION' ? refined 21.2098062485 -31.2590769211 -9.94241836102 1.40337008538  ? -0.312520725153  ? 0.0636252423587  
? 0.677619048165 ? 0.0438844565095   ? 0.422241826101 ? 1.67582363648  ? 0.939197539588   ? 0.457750502269  ? 2.1756162524  ? 
0.730086296147   ? 1.56010243738 ? -0.0149669852812 ? 0.00651962188562 ? 0.345274053545   ? -0.110621101558 ? -0.00425878201174  ? 
-0.154229837831  ? -1.02752751471   ? 0.545071134403    ? 0.0205107945709  ? 
4  'X-RAY DIFFRACTION' ? refined 9.67856818899 -51.4517932837 -17.0114779805 0.831759486019 ? 0.0101249287009  ? 0.0399912868891  
? 0.482176474626 ? -0.00717436734465 ? 0.191569387688 ? 2.551909855    ? 0.698081955762   ? 0.0847661819359 ? 1.57630505175 ? 
0.455126674453   ? 3.08045642207 ? -0.0203202024996 ? 0.0333253860029  ? -0.117000876782  ? -0.144750705853 ? 0.0176965287205    ? 
-0.091041141509  ? -0.554283885826  ? 0.0107458798724   ? -0.0324674448663 ? 
5  'X-RAY DIFFRACTION' ? refined 9.25127792503 -50.6598765901 -21.7933595123 0.885928893693 ? -0.0319542701049 ? 0.0265536467862  
? 0.486567818345 ? -0.00187367787227 ? 0.282343279868 ? 2.13552671442  ? 0.707616614259   ? 0.985798139729  ? 2.03197280891 ? 
0.0513972665702  ? 1.83263357649 ? 0.06872923777    ? 0.30834332304    ? -0.0275043814387 ? -0.262032668893 ? 0.00512383464088   ? 
-0.03444202817   ? -0.522687342637  ? 0.205720120767    ? -0.062286948294  ? 
6  'X-RAY DIFFRACTION' ? refined 35.4150516769 -115.052921405 -28.0236575628 1.93792021132  ? 0.767681162642   ? 0.148556836731   
? 1.05357328156  ? 0.0245699524743   ? 0.669530683351 ? 4.51606253806  ? 0.00678612376051 ? 0.616944349641  ? 3.90086776554 ? 
3.76826532528    ? 3.74089864383 ? 0.234566001712   ? 0.100794717746   ? -0.446186691373  ? 0.602044974829  ? -0.207079745653    ? 
-0.121495415233  ? 1.14187700898    ? 0.660675183921    ? -0.442506764295  ? 
7  'X-RAY DIFFRACTION' ? refined 38.6627214587 -103.776891148 -39.5520492311 1.40272602732  ? 0.640843365073   ? 0.0972510879016  
? 1.28850361952  ? -0.00208551320418 ? 0.550609383463 ? 2.53227064997  ? -0.988419479384  ? -0.691119546174 ? 2.08119627135 ? 
1.08174159892    ? 1.52821714075 ? 0.163689288951   ? 0.176792359769   ? 0.192848575948   ? -0.468724021577 ? -0.176106864424    ? 
-0.74509362058   ? 0.366884943859   ? 1.07023251935     ? -0.170890771601  ? 
8  'X-RAY DIFFRACTION' ? refined 23.7770523616 -99.1214226482 -47.9684379568 1.75975361715  ? 0.603978235945   ? 0.110486882348   
? 0.794299155311 ? -0.221553798161   ? 0.113761079238 ? 1.74045719245  ? -0.989071265591  ? -2.32441070673  ? 2.99881994042 ? 
1.55569049966    ? 5.14938259535 ? 0.0846598053924  ? -0.0589083686611 ? 0.175012750355   ? -0.48610182144  ? -0.0808429564973   ? 
-0.390761785244  ? 0.291829634868   ? 0.291272119833    ? -0.180696200417  ? 
9  'X-RAY DIFFRACTION' ? refined 13.2617757812 -107.680533566 -46.5101702086 1.68784199016  ? 0.290674810051   ? -0.0831608988324 
? 0.729149342538 ? -0.0569210407568  ? 0.527596995328 ? 5.26240308033  ? 0.82943832327    ? -3.59284205687  ? 3.79353033443 ? 
4.23918321867    ? 8.75746858259 ? 0.0827221942493  ? 1.08698679661    ? 0.0531489394697  ? -0.93063646025  ? 0.25113920258      ? 
0.25692349784    ? 0.00850438081753 ? -0.781405517767   ? 0.196441847463   ? 
10 'X-RAY DIFFRACTION' ? refined 19.1285441146 -119.742593924 -34.5236041098 2.03635793475  ? 0.485349459877   ? 0.020076572684   
? 0.687054420687 ? -0.115329642786   ? 0.629205332791 ? 3.07974983895  ? -0.475094784781  ? 0.760892015538  ? 2.16854900691 ? 
-0.386149088656  ? 1.66102918566 ? -0.0979473712328 ? 0.048071162794   ? -0.847676514524  ? 0.428668658153  ? 0.177595759969     ? 
0.18482292615    ? 1.18919263631    ? -0.00160059664997 ? 0.179459005071   ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  A 1   A 13  ? A 137 A 149 ? ? 
;chain 'A' and (resid   13  through  149 )
;
2  'X-RAY DIFFRACTION' 2  A 138 A 150 ? A 318 A 330 ? ? 
;chain 'A' and (resid  150  through  330 )
;
3  'X-RAY DIFFRACTION' 3  A 319 A 331 ? A 475 A 487 ? ? 
;chain 'A' and (resid  331  through  487 )
;
4  'X-RAY DIFFRACTION' 4  A 476 A 488 ? A 518 A 533 ? ? 
;chain 'A' and (resid  488  through  533 )
;
5  'X-RAY DIFFRACTION' 5  A 519 A 534 ? A 622 A 637 ? ? 
;chain 'A' and (resid  534  through  637 )
;
6  'X-RAY DIFFRACTION' 6  B 1   B 28  ? B 62  B 89  ? ? 
;chain 'B' and (resid   28  through   89 )
;
7  'X-RAY DIFFRACTION' 7  B 63  B 90  ? B 136 B 163 ? ? 
;chain 'B' and (resid   90  through  163 )
;
8  'X-RAY DIFFRACTION' 8  B 137 B 164 ? B 178 B 205 ? ? 
;chain 'B' and (resid  164  through  205 )
;
9  'X-RAY DIFFRACTION' 9  B 179 B 206 ? B 225 B 252 ? ? 
;chain 'B' and (resid  206  through  252 )
;
10 'X-RAY DIFFRACTION' 10 B 226 B 253 ? B 301 B 328 ? ? 
;chain 'B' and (resid  253  through  328 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -7  ? A MET 1   
2  1 Y 1 A ASP -6  ? A ASP 2   
3  1 Y 1 A TYR -5  ? A TYR 3   
4  1 Y 1 A LYS -4  ? A LYS 4   
5  1 Y 1 A ASP -3  ? A ASP 5   
6  1 Y 1 A ASP -2  ? A ASP 6   
7  1 Y 1 A ASP -1  ? A ASP 7   
8  1 Y 1 A ASP 0   ? A ASP 8   
9  1 Y 1 A LYS 1   ? A LYS 9   
10 1 Y 1 A ALA 2   ? A ALA 10  
11 1 Y 1 A ALA 3   ? A ALA 11  
12 1 Y 1 A MET 4   ? A MET 12  
13 1 Y 1 A ALA 5   ? A ALA 13  
14 1 Y 1 A VAL 6   ? A VAL 14  
15 1 Y 1 A GLY 7   ? A GLY 15  
16 1 Y 1 A GLY 8   ? A GLY 16  
17 1 Y 1 A ALA 9   ? A ALA 17  
18 1 Y 1 A GLY 10  ? A GLY 18  
19 1 Y 1 A GLY 11  ? A GLY 19  
20 1 Y 1 A SER 12  ? A SER 20  
21 1 Y 1 A PRO 528 ? A PRO 536 
22 1 Y 1 A MET 529 ? A MET 537 
23 1 Y 1 A ILE 530 ? A ILE 538 
24 1 Y 1 B MET -7  ? B MET 1   
25 1 Y 1 B HIS -6  ? B HIS 2   
26 1 Y 1 B HIS -5  ? B HIS 3   
27 1 Y 1 B HIS -4  ? B HIS 4   
28 1 Y 1 B HIS -3  ? B HIS 5   
29 1 Y 1 B HIS -2  ? B HIS 6   
30 1 Y 1 B HIS -1  ? B HIS 7   
31 1 Y 1 B HIS 0   ? B HIS 8   
32 1 Y 1 B HIS 1   ? B HIS 9   
33 1 Y 1 B ARG 2   ? B ARG 10  
34 1 Y 1 B LYS 3   ? B LYS 11  
35 1 Y 1 B GLU 4   ? B GLU 12  
36 1 Y 1 B THR 5   ? B THR 13  
37 1 Y 1 B PRO 6   ? B PRO 14  
38 1 Y 1 B PRO 7   ? B PRO 15  
39 1 Y 1 B PRO 8   ? B PRO 16  
40 1 Y 1 B LEU 9   ? B LEU 17  
41 1 Y 1 B VAL 10  ? B VAL 18  
42 1 Y 1 B PRO 11  ? B PRO 19  
43 1 Y 1 B PRO 12  ? B PRO 20  
44 1 Y 1 B ALA 13  ? B ALA 21  
45 1 Y 1 B ALA 14  ? B ALA 22  
46 1 Y 1 B ARG 15  ? B ARG 23  
47 1 Y 1 B GLU 16  ? B GLU 24  
48 1 Y 1 B TRP 17  ? B TRP 25  
49 1 Y 1 B ASN 18  ? B ASN 26  
50 1 Y 1 B LEU 19  ? B LEU 27  
51 1 Y 1 B PRO 20  ? B PRO 28  
52 1 Y 1 B PRO 21  ? B PRO 29  
53 1 Y 1 B ASN 22  ? B ASN 30  
54 1 Y 1 B ALA 23  ? B ALA 31  
55 1 Y 1 B PRO 24  ? B PRO 32  
56 1 Y 1 B ALA 25  ? B ALA 33  
57 1 Y 1 B CYS 26  ? B CYS 34  
58 1 Y 1 B MET 27  ? B MET 35  
59 1 Y 1 B THR 329 ? B THR 337 
60 1 Y 1 B GLU 330 ? B GLU 338 
61 1 Y 1 B PRO 331 ? B PRO 339 
62 1 Y 1 B LEU 332 ? B LEU 340 
63 1 Y 1 B PRO 333 ? B PRO 341 
64 1 Y 1 B ALA 334 ? B ALA 342 
65 1 Y 1 B PRO 335 ? B PRO 343 
66 1 Y 1 B GLY 336 ? B GLY 344 
67 1 Y 1 B PRO 337 ? B PRO 345 
68 1 Y 1 B ALA 338 ? B ALA 346 
69 1 Y 1 B SER 339 ? B SER 347 
70 1 Y 1 B VAL 340 ? B VAL 348 
71 1 Y 1 B THR 341 ? B THR 349 
72 1 Y 1 B GLU 342 ? B GLU 350 
# 
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 
A1BLI N3     N  Y N 1   
A1BLI C4     C  Y N 2   
A1BLI C5     C  Y N 3   
A1BLI C6     C  Y N 4   
A1BLI C7     C  N N 5   
A1BLI C8     C  Y N 6   
A1BLI C10    C  Y N 7   
A1BLI C15    C  N N 8   
A1BLI C17    C  Y N 9   
A1BLI C20    C  N N 10  
A1BLI C22    C  N N 11  
A1BLI C28    C  Y N 12  
A1BLI C1     C  N N 13  
A1BLI C11    C  Y N 14  
A1BLI C12    C  N N 15  
A1BLI C14    C  N N 16  
A1BLI C16    C  Y N 17  
A1BLI C18    C  N R 18  
A1BLI C19    C  N N 19  
A1BLI C23    C  N R 20  
A1BLI C25    C  N N 21  
A1BLI C27    C  Y N 22  
A1BLI C29    C  Y N 23  
A1BLI C31    C  Y N 24  
A1BLI C33    C  N N 25  
A1BLI C34    C  N N 26  
A1BLI C35    C  N N 27  
A1BLI C36    C  N N 28  
A1BLI C37    C  Y N 29  
A1BLI C9     C  Y N 30  
A1BLI N13    N  N N 31  
A1BLI N2     N  Y N 32  
A1BLI N21    N  N N 33  
A1BLI N30    N  Y N 34  
A1BLI N32    N  N N 35  
A1BLI O24    O  N N 36  
A1BLI O26    O  N N 37  
A1BLI H4     H  N N 38  
A1BLI H5     H  N N 39  
A1BLI H7     H  N N 40  
A1BLI H6     H  N N 41  
A1BLI H9     H  N N 42  
A1BLI H14    H  N N 43  
A1BLI H15    H  N N 44  
A1BLI H16    H  N N 45  
A1BLI H20    H  N N 46  
A1BLI H21    H  N N 47  
A1BLI H22    H  N N 48  
A1BLI H23    H  N N 49  
A1BLI H26    H  N N 50  
A1BLI H1     H  N N 51  
A1BLI H2     H  N N 52  
A1BLI H3     H  N N 53  
A1BLI H10    H  N N 54  
A1BLI H11    H  N N 55  
A1BLI H12    H  N N 56  
A1BLI H13    H  N N 57  
A1BLI H17    H  N N 58  
A1BLI H18    H  N N 59  
A1BLI H19    H  N N 60  
A1BLI H24    H  N N 61  
A1BLI H27    H  N N 62  
A1BLI H29    H  N N 63  
A1BLI H30    H  N N 64  
A1BLI H31    H  N N 65  
A1BLI H32    H  N N 66  
A1BLI H33    H  N N 67  
A1BLI H35    H  N N 68  
A1BLI H34    H  N N 69  
A1BLI H36    H  N N 70  
A1BLI H8     H  N N 71  
A1BLI H28    H  N N 72  
A1BLI H25    H  N N 73  
ALA   N      N  N N 74  
ALA   CA     C  N S 75  
ALA   C      C  N N 76  
ALA   O      O  N N 77  
ALA   CB     C  N N 78  
ALA   OXT    O  N N 79  
ALA   H      H  N N 80  
ALA   H2     H  N N 81  
ALA   HA     H  N N 82  
ALA   HB1    H  N N 83  
ALA   HB2    H  N N 84  
ALA   HB3    H  N N 85  
ALA   HXT    H  N N 86  
ARG   N      N  N N 87  
ARG   CA     C  N S 88  
ARG   C      C  N N 89  
ARG   O      O  N N 90  
ARG   CB     C  N N 91  
ARG   CG     C  N N 92  
ARG   CD     C  N N 93  
ARG   NE     N  N N 94  
ARG   CZ     C  N N 95  
ARG   NH1    N  N N 96  
ARG   NH2    N  N N 97  
ARG   OXT    O  N N 98  
ARG   H      H  N N 99  
ARG   H2     H  N N 100 
ARG   HA     H  N N 101 
ARG   HB2    H  N N 102 
ARG   HB3    H  N N 103 
ARG   HG2    H  N N 104 
ARG   HG3    H  N N 105 
ARG   HD2    H  N N 106 
ARG   HD3    H  N N 107 
ARG   HE     H  N N 108 
ARG   HH11   H  N N 109 
ARG   HH12   H  N N 110 
ARG   HH21   H  N N 111 
ARG   HH22   H  N N 112 
ARG   HXT    H  N N 113 
ASN   N      N  N N 114 
ASN   CA     C  N S 115 
ASN   C      C  N N 116 
ASN   O      O  N N 117 
ASN   CB     C  N N 118 
ASN   CG     C  N N 119 
ASN   OD1    O  N N 120 
ASN   ND2    N  N N 121 
ASN   OXT    O  N N 122 
ASN   H      H  N N 123 
ASN   H2     H  N N 124 
ASN   HA     H  N N 125 
ASN   HB2    H  N N 126 
ASN   HB3    H  N N 127 
ASN   HD21   H  N N 128 
ASN   HD22   H  N N 129 
ASN   HXT    H  N N 130 
ASP   N      N  N N 131 
ASP   CA     C  N S 132 
ASP   C      C  N N 133 
ASP   O      O  N N 134 
ASP   CB     C  N N 135 
ASP   CG     C  N N 136 
ASP   OD1    O  N N 137 
ASP   OD2    O  N N 138 
ASP   OXT    O  N N 139 
ASP   H      H  N N 140 
ASP   H2     H  N N 141 
ASP   HA     H  N N 142 
ASP   HB2    H  N N 143 
ASP   HB3    H  N N 144 
ASP   HD2    H  N N 145 
ASP   HXT    H  N N 146 
CL    CL     CL N N 147 
CYS   N      N  N N 148 
CYS   CA     C  N R 149 
CYS   C      C  N N 150 
CYS   O      O  N N 151 
CYS   CB     C  N N 152 
CYS   SG     S  N N 153 
CYS   OXT    O  N N 154 
CYS   H      H  N N 155 
CYS   H2     H  N N 156 
CYS   HA     H  N N 157 
CYS   HB2    H  N N 158 
CYS   HB3    H  N N 159 
CYS   HG     H  N N 160 
CYS   HXT    H  N N 161 
EDO   C1     C  N N 162 
EDO   O1     O  N N 163 
EDO   C2     C  N N 164 
EDO   O2     O  N N 165 
EDO   H11    H  N N 166 
EDO   H12    H  N N 167 
EDO   HO1    H  N N 168 
EDO   H21    H  N N 169 
EDO   H22    H  N N 170 
EDO   HO2    H  N N 171 
GLN   N      N  N N 172 
GLN   CA     C  N S 173 
GLN   C      C  N N 174 
GLN   O      O  N N 175 
GLN   CB     C  N N 176 
GLN   CG     C  N N 177 
GLN   CD     C  N N 178 
GLN   OE1    O  N N 179 
GLN   NE2    N  N N 180 
GLN   OXT    O  N N 181 
GLN   H      H  N N 182 
GLN   H2     H  N N 183 
GLN   HA     H  N N 184 
GLN   HB2    H  N N 185 
GLN   HB3    H  N N 186 
GLN   HG2    H  N N 187 
GLN   HG3    H  N N 188 
GLN   HE21   H  N N 189 
GLN   HE22   H  N N 190 
GLN   HXT    H  N N 191 
GLU   N      N  N N 192 
GLU   CA     C  N S 193 
GLU   C      C  N N 194 
GLU   O      O  N N 195 
GLU   CB     C  N N 196 
GLU   CG     C  N N 197 
GLU   CD     C  N N 198 
GLU   OE1    O  N N 199 
GLU   OE2    O  N N 200 
GLU   OXT    O  N N 201 
GLU   H      H  N N 202 
GLU   H2     H  N N 203 
GLU   HA     H  N N 204 
GLU   HB2    H  N N 205 
GLU   HB3    H  N N 206 
GLU   HG2    H  N N 207 
GLU   HG3    H  N N 208 
GLU   HE2    H  N N 209 
GLU   HXT    H  N N 210 
GLY   N      N  N N 211 
GLY   CA     C  N N 212 
GLY   C      C  N N 213 
GLY   O      O  N N 214 
GLY   OXT    O  N N 215 
GLY   H      H  N N 216 
GLY   H2     H  N N 217 
GLY   HA2    H  N N 218 
GLY   HA3    H  N N 219 
GLY   HXT    H  N N 220 
GOL   C1     C  N N 221 
GOL   O1     O  N N 222 
GOL   C2     C  N N 223 
GOL   O2     O  N N 224 
GOL   C3     C  N N 225 
GOL   O3     O  N N 226 
GOL   H11    H  N N 227 
GOL   H12    H  N N 228 
GOL   HO1    H  N N 229 
GOL   H2     H  N N 230 
GOL   HO2    H  N N 231 
GOL   H31    H  N N 232 
GOL   H32    H  N N 233 
GOL   HO3    H  N N 234 
HIS   N      N  N N 235 
HIS   CA     C  N S 236 
HIS   C      C  N N 237 
HIS   O      O  N N 238 
HIS   CB     C  N N 239 
HIS   CG     C  Y N 240 
HIS   ND1    N  Y N 241 
HIS   CD2    C  Y N 242 
HIS   CE1    C  Y N 243 
HIS   NE2    N  Y N 244 
HIS   OXT    O  N N 245 
HIS   H      H  N N 246 
HIS   H2     H  N N 247 
HIS   HA     H  N N 248 
HIS   HB2    H  N N 249 
HIS   HB3    H  N N 250 
HIS   HD1    H  N N 251 
HIS   HD2    H  N N 252 
HIS   HE1    H  N N 253 
HIS   HE2    H  N N 254 
HIS   HXT    H  N N 255 
HOH   O      O  N N 256 
HOH   H1     H  N N 257 
HOH   H2     H  N N 258 
ILE   N      N  N N 259 
ILE   CA     C  N S 260 
ILE   C      C  N N 261 
ILE   O      O  N N 262 
ILE   CB     C  N S 263 
ILE   CG1    C  N N 264 
ILE   CG2    C  N N 265 
ILE   CD1    C  N N 266 
ILE   OXT    O  N N 267 
ILE   H      H  N N 268 
ILE   H2     H  N N 269 
ILE   HA     H  N N 270 
ILE   HB     H  N N 271 
ILE   HG12   H  N N 272 
ILE   HG13   H  N N 273 
ILE   HG21   H  N N 274 
ILE   HG22   H  N N 275 
ILE   HG23   H  N N 276 
ILE   HD11   H  N N 277 
ILE   HD12   H  N N 278 
ILE   HD13   H  N N 279 
ILE   HXT    H  N N 280 
LEU   N      N  N N 281 
LEU   CA     C  N S 282 
LEU   C      C  N N 283 
LEU   O      O  N N 284 
LEU   CB     C  N N 285 
LEU   CG     C  N N 286 
LEU   CD1    C  N N 287 
LEU   CD2    C  N N 288 
LEU   OXT    O  N N 289 
LEU   H      H  N N 290 
LEU   H2     H  N N 291 
LEU   HA     H  N N 292 
LEU   HB2    H  N N 293 
LEU   HB3    H  N N 294 
LEU   HG     H  N N 295 
LEU   HD11   H  N N 296 
LEU   HD12   H  N N 297 
LEU   HD13   H  N N 298 
LEU   HD21   H  N N 299 
LEU   HD22   H  N N 300 
LEU   HD23   H  N N 301 
LEU   HXT    H  N N 302 
LYS   N      N  N N 303 
LYS   CA     C  N S 304 
LYS   C      C  N N 305 
LYS   O      O  N N 306 
LYS   CB     C  N N 307 
LYS   CG     C  N N 308 
LYS   CD     C  N N 309 
LYS   CE     C  N N 310 
LYS   NZ     N  N N 311 
LYS   OXT    O  N N 312 
LYS   H      H  N N 313 
LYS   H2     H  N N 314 
LYS   HA     H  N N 315 
LYS   HB2    H  N N 316 
LYS   HB3    H  N N 317 
LYS   HG2    H  N N 318 
LYS   HG3    H  N N 319 
LYS   HD2    H  N N 320 
LYS   HD3    H  N N 321 
LYS   HE2    H  N N 322 
LYS   HE3    H  N N 323 
LYS   HZ1    H  N N 324 
LYS   HZ2    H  N N 325 
LYS   HZ3    H  N N 326 
LYS   HXT    H  N N 327 
MET   N      N  N N 328 
MET   CA     C  N S 329 
MET   C      C  N N 330 
MET   O      O  N N 331 
MET   CB     C  N N 332 
MET   CG     C  N N 333 
MET   SD     S  N N 334 
MET   CE     C  N N 335 
MET   OXT    O  N N 336 
MET   H      H  N N 337 
MET   H2     H  N N 338 
MET   HA     H  N N 339 
MET   HB2    H  N N 340 
MET   HB3    H  N N 341 
MET   HG2    H  N N 342 
MET   HG3    H  N N 343 
MET   HE1    H  N N 344 
MET   HE2    H  N N 345 
MET   HE3    H  N N 346 
MET   HXT    H  N N 347 
MTA   CS     C  N N 348 
MTA   "S5'"  S  N N 349 
MTA   "C5'"  C  N N 350 
MTA   "C4'"  C  N S 351 
MTA   "O4'"  O  N N 352 
MTA   "C2'"  C  N R 353 
MTA   "O2'"  O  N N 354 
MTA   "C3'"  C  N S 355 
MTA   "O3'"  O  N N 356 
MTA   "C1'"  C  N R 357 
MTA   N9     N  Y N 358 
MTA   C8     C  Y N 359 
MTA   N7     N  Y N 360 
MTA   C5     C  Y N 361 
MTA   C6     C  Y N 362 
MTA   N6     N  N N 363 
MTA   N1     N  Y N 364 
MTA   C2     C  Y N 365 
MTA   N3     N  Y N 366 
MTA   C4     C  Y N 367 
MTA   HCS1   H  N N 368 
MTA   HCS2   H  N N 369 
MTA   HCS3   H  N N 370 
MTA   "H5'1" H  N N 371 
MTA   "H5'2" H  N N 372 
MTA   "H4'"  H  N N 373 
MTA   "H2'"  H  N N 374 
MTA   "HO2'" H  N N 375 
MTA   "H3'"  H  N N 376 
MTA   H3T    H  N N 377 
MTA   "H1'"  H  N N 378 
MTA   H8     H  N N 379 
MTA   H61    H  N N 380 
MTA   H62    H  N N 381 
MTA   H2     H  N N 382 
NA    NA     NA N N 383 
PHE   N      N  N N 384 
PHE   CA     C  N S 385 
PHE   C      C  N N 386 
PHE   O      O  N N 387 
PHE   CB     C  N N 388 
PHE   CG     C  Y N 389 
PHE   CD1    C  Y N 390 
PHE   CD2    C  Y N 391 
PHE   CE1    C  Y N 392 
PHE   CE2    C  Y N 393 
PHE   CZ     C  Y N 394 
PHE   OXT    O  N N 395 
PHE   H      H  N N 396 
PHE   H2     H  N N 397 
PHE   HA     H  N N 398 
PHE   HB2    H  N N 399 
PHE   HB3    H  N N 400 
PHE   HD1    H  N N 401 
PHE   HD2    H  N N 402 
PHE   HE1    H  N N 403 
PHE   HE2    H  N N 404 
PHE   HZ     H  N N 405 
PHE   HXT    H  N N 406 
PRO   N      N  N N 407 
PRO   CA     C  N S 408 
PRO   C      C  N N 409 
PRO   O      O  N N 410 
PRO   CB     C  N N 411 
PRO   CG     C  N N 412 
PRO   CD     C  N N 413 
PRO   OXT    O  N N 414 
PRO   H      H  N N 415 
PRO   HA     H  N N 416 
PRO   HB2    H  N N 417 
PRO   HB3    H  N N 418 
PRO   HG2    H  N N 419 
PRO   HG3    H  N N 420 
PRO   HD2    H  N N 421 
PRO   HD3    H  N N 422 
PRO   HXT    H  N N 423 
SER   N      N  N N 424 
SER   CA     C  N S 425 
SER   C      C  N N 426 
SER   O      O  N N 427 
SER   CB     C  N N 428 
SER   OG     O  N N 429 
SER   OXT    O  N N 430 
SER   H      H  N N 431 
SER   H2     H  N N 432 
SER   HA     H  N N 433 
SER   HB2    H  N N 434 
SER   HB3    H  N N 435 
SER   HG     H  N N 436 
SER   HXT    H  N N 437 
THR   N      N  N N 438 
THR   CA     C  N S 439 
THR   C      C  N N 440 
THR   O      O  N N 441 
THR   CB     C  N R 442 
THR   OG1    O  N N 443 
THR   CG2    C  N N 444 
THR   OXT    O  N N 445 
THR   H      H  N N 446 
THR   H2     H  N N 447 
THR   HA     H  N N 448 
THR   HB     H  N N 449 
THR   HG1    H  N N 450 
THR   HG21   H  N N 451 
THR   HG22   H  N N 452 
THR   HG23   H  N N 453 
THR   HXT    H  N N 454 
TRP   N      N  N N 455 
TRP   CA     C  N S 456 
TRP   C      C  N N 457 
TRP   O      O  N N 458 
TRP   CB     C  N N 459 
TRP   CG     C  Y N 460 
TRP   CD1    C  Y N 461 
TRP   CD2    C  Y N 462 
TRP   NE1    N  Y N 463 
TRP   CE2    C  Y N 464 
TRP   CE3    C  Y N 465 
TRP   CZ2    C  Y N 466 
TRP   CZ3    C  Y N 467 
TRP   CH2    C  Y N 468 
TRP   OXT    O  N N 469 
TRP   H      H  N N 470 
TRP   H2     H  N N 471 
TRP   HA     H  N N 472 
TRP   HB2    H  N N 473 
TRP   HB3    H  N N 474 
TRP   HD1    H  N N 475 
TRP   HE1    H  N N 476 
TRP   HE3    H  N N 477 
TRP   HZ2    H  N N 478 
TRP   HZ3    H  N N 479 
TRP   HH2    H  N N 480 
TRP   HXT    H  N N 481 
TYR   N      N  N N 482 
TYR   CA     C  N S 483 
TYR   C      C  N N 484 
TYR   O      O  N N 485 
TYR   CB     C  N N 486 
TYR   CG     C  Y N 487 
TYR   CD1    C  Y N 488 
TYR   CD2    C  Y N 489 
TYR   CE1    C  Y N 490 
TYR   CE2    C  Y N 491 
TYR   CZ     C  Y N 492 
TYR   OH     O  N N 493 
TYR   OXT    O  N N 494 
TYR   H      H  N N 495 
TYR   H2     H  N N 496 
TYR   HA     H  N N 497 
TYR   HB2    H  N N 498 
TYR   HB3    H  N N 499 
TYR   HD1    H  N N 500 
TYR   HD2    H  N N 501 
TYR   HE1    H  N N 502 
TYR   HE2    H  N N 503 
TYR   HH     H  N N 504 
TYR   HXT    H  N N 505 
VAL   N      N  N N 506 
VAL   CA     C  N S 507 
VAL   C      C  N N 508 
VAL   O      O  N N 509 
VAL   CB     C  N N 510 
VAL   CG1    C  N N 511 
VAL   CG2    C  N N 512 
VAL   OXT    O  N N 513 
VAL   H      H  N N 514 
VAL   H2     H  N N 515 
VAL   HA     H  N N 516 
VAL   HB     H  N N 517 
VAL   HG11   H  N N 518 
VAL   HG12   H  N N 519 
VAL   HG13   H  N N 520 
VAL   HG21   H  N N 521 
VAL   HG22   H  N N 522 
VAL   HG23   H  N N 523 
VAL   HXT    H  N N 524 
# 
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 
A1BLI C1    N2     sing N N 1   
A1BLI N2    N3     sing Y N 2   
A1BLI N2    C6     sing Y N 3   
A1BLI N3    C4     doub Y N 4   
A1BLI C4    C5     sing Y N 5   
A1BLI C5    C6     doub Y N 6   
A1BLI C6    C7     sing N N 7   
A1BLI C7    C8     sing N N 8   
A1BLI C8    C9     doub Y N 9   
A1BLI C8    C17    sing Y N 10  
A1BLI C9    C10    sing Y N 11  
A1BLI C10   C11    doub Y N 12  
A1BLI C11   C12    sing N N 13  
A1BLI C11   C16    sing Y N 14  
A1BLI C12   N13    sing N N 15  
A1BLI N13   C14    sing N N 16  
A1BLI N13   C18    sing N N 17  
A1BLI C14   C15    sing N N 18  
A1BLI C15   C16    sing N N 19  
A1BLI C16   C17    doub Y N 20  
A1BLI C18   C19    sing N N 21  
A1BLI C18   C23    sing N N 22  
A1BLI C19   C20    sing N N 23  
A1BLI C20   N21    sing N N 24  
A1BLI N21   C22    sing N N 25  
A1BLI N21   C25    sing N N 26  
A1BLI C22   C23    sing N N 27  
A1BLI C23   O24    sing N N 28  
A1BLI C25   O26    doub N N 29  
A1BLI C25   C27    sing N N 30  
A1BLI C27   C28    doub Y N 31  
A1BLI C27   C37    sing Y N 32  
A1BLI C28   C29    sing Y N 33  
A1BLI C29   N30    doub Y N 34  
A1BLI N30   C31    sing Y N 35  
A1BLI C31   N32    sing N N 36  
A1BLI C31   C37    doub Y N 37  
A1BLI N32   C33    sing N N 38  
A1BLI C33   C34    sing N N 39  
A1BLI C33   C36    sing N N 40  
A1BLI C34   C35    sing N N 41  
A1BLI C35   C36    sing N N 42  
A1BLI C4    H4     sing N N 43  
A1BLI C5    H5     sing N N 44  
A1BLI C7    H7     sing N N 45  
A1BLI C7    H6     sing N N 46  
A1BLI C10   H9     sing N N 47  
A1BLI C15   H14    sing N N 48  
A1BLI C15   H15    sing N N 49  
A1BLI C17   H16    sing N N 50  
A1BLI C20   H20    sing N N 51  
A1BLI C20   H21    sing N N 52  
A1BLI C22   H22    sing N N 53  
A1BLI C22   H23    sing N N 54  
A1BLI C28   H26    sing N N 55  
A1BLI C1    H1     sing N N 56  
A1BLI C1    H2     sing N N 57  
A1BLI C1    H3     sing N N 58  
A1BLI C12   H10    sing N N 59  
A1BLI C12   H11    sing N N 60  
A1BLI C14   H12    sing N N 61  
A1BLI C14   H13    sing N N 62  
A1BLI C18   H17    sing N N 63  
A1BLI C19   H18    sing N N 64  
A1BLI C19   H19    sing N N 65  
A1BLI C23   H24    sing N N 66  
A1BLI C29   H27    sing N N 67  
A1BLI C33   H29    sing N N 68  
A1BLI C34   H30    sing N N 69  
A1BLI C34   H31    sing N N 70  
A1BLI C35   H32    sing N N 71  
A1BLI C35   H33    sing N N 72  
A1BLI C36   H35    sing N N 73  
A1BLI C36   H34    sing N N 74  
A1BLI C37   H36    sing N N 75  
A1BLI C9    H8     sing N N 76  
A1BLI N32   H28    sing N N 77  
A1BLI O24   H25    sing N N 78  
ALA   N     CA     sing N N 79  
ALA   N     H      sing N N 80  
ALA   N     H2     sing N N 81  
ALA   CA    C      sing N N 82  
ALA   CA    CB     sing N N 83  
ALA   CA    HA     sing N N 84  
ALA   C     O      doub N N 85  
ALA   C     OXT    sing N N 86  
ALA   CB    HB1    sing N N 87  
ALA   CB    HB2    sing N N 88  
ALA   CB    HB3    sing N N 89  
ALA   OXT   HXT    sing N N 90  
ARG   N     CA     sing N N 91  
ARG   N     H      sing N N 92  
ARG   N     H2     sing N N 93  
ARG   CA    C      sing N N 94  
ARG   CA    CB     sing N N 95  
ARG   CA    HA     sing N N 96  
ARG   C     O      doub N N 97  
ARG   C     OXT    sing N N 98  
ARG   CB    CG     sing N N 99  
ARG   CB    HB2    sing N N 100 
ARG   CB    HB3    sing N N 101 
ARG   CG    CD     sing N N 102 
ARG   CG    HG2    sing N N 103 
ARG   CG    HG3    sing N N 104 
ARG   CD    NE     sing N N 105 
ARG   CD    HD2    sing N N 106 
ARG   CD    HD3    sing N N 107 
ARG   NE    CZ     sing N N 108 
ARG   NE    HE     sing N N 109 
ARG   CZ    NH1    sing N N 110 
ARG   CZ    NH2    doub N N 111 
ARG   NH1   HH11   sing N N 112 
ARG   NH1   HH12   sing N N 113 
ARG   NH2   HH21   sing N N 114 
ARG   NH2   HH22   sing N N 115 
ARG   OXT   HXT    sing N N 116 
ASN   N     CA     sing N N 117 
ASN   N     H      sing N N 118 
ASN   N     H2     sing N N 119 
ASN   CA    C      sing N N 120 
ASN   CA    CB     sing N N 121 
ASN   CA    HA     sing N N 122 
ASN   C     O      doub N N 123 
ASN   C     OXT    sing N N 124 
ASN   CB    CG     sing N N 125 
ASN   CB    HB2    sing N N 126 
ASN   CB    HB3    sing N N 127 
ASN   CG    OD1    doub N N 128 
ASN   CG    ND2    sing N N 129 
ASN   ND2   HD21   sing N N 130 
ASN   ND2   HD22   sing N N 131 
ASN   OXT   HXT    sing N N 132 
ASP   N     CA     sing N N 133 
ASP   N     H      sing N N 134 
ASP   N     H2     sing N N 135 
ASP   CA    C      sing N N 136 
ASP   CA    CB     sing N N 137 
ASP   CA    HA     sing N N 138 
ASP   C     O      doub N N 139 
ASP   C     OXT    sing N N 140 
ASP   CB    CG     sing N N 141 
ASP   CB    HB2    sing N N 142 
ASP   CB    HB3    sing N N 143 
ASP   CG    OD1    doub N N 144 
ASP   CG    OD2    sing N N 145 
ASP   OD2   HD2    sing N N 146 
ASP   OXT   HXT    sing N N 147 
CYS   N     CA     sing N N 148 
CYS   N     H      sing N N 149 
CYS   N     H2     sing N N 150 
CYS   CA    C      sing N N 151 
CYS   CA    CB     sing N N 152 
CYS   CA    HA     sing N N 153 
CYS   C     O      doub N N 154 
CYS   C     OXT    sing N N 155 
CYS   CB    SG     sing N N 156 
CYS   CB    HB2    sing N N 157 
CYS   CB    HB3    sing N N 158 
CYS   SG    HG     sing N N 159 
CYS   OXT   HXT    sing N N 160 
EDO   C1    O1     sing N N 161 
EDO   C1    C2     sing N N 162 
EDO   C1    H11    sing N N 163 
EDO   C1    H12    sing N N 164 
EDO   O1    HO1    sing N N 165 
EDO   C2    O2     sing N N 166 
EDO   C2    H21    sing N N 167 
EDO   C2    H22    sing N N 168 
EDO   O2    HO2    sing N N 169 
GLN   N     CA     sing N N 170 
GLN   N     H      sing N N 171 
GLN   N     H2     sing N N 172 
GLN   CA    C      sing N N 173 
GLN   CA    CB     sing N N 174 
GLN   CA    HA     sing N N 175 
GLN   C     O      doub N N 176 
GLN   C     OXT    sing N N 177 
GLN   CB    CG     sing N N 178 
GLN   CB    HB2    sing N N 179 
GLN   CB    HB3    sing N N 180 
GLN   CG    CD     sing N N 181 
GLN   CG    HG2    sing N N 182 
GLN   CG    HG3    sing N N 183 
GLN   CD    OE1    doub N N 184 
GLN   CD    NE2    sing N N 185 
GLN   NE2   HE21   sing N N 186 
GLN   NE2   HE22   sing N N 187 
GLN   OXT   HXT    sing N N 188 
GLU   N     CA     sing N N 189 
GLU   N     H      sing N N 190 
GLU   N     H2     sing N N 191 
GLU   CA    C      sing N N 192 
GLU   CA    CB     sing N N 193 
GLU   CA    HA     sing N N 194 
GLU   C     O      doub N N 195 
GLU   C     OXT    sing N N 196 
GLU   CB    CG     sing N N 197 
GLU   CB    HB2    sing N N 198 
GLU   CB    HB3    sing N N 199 
GLU   CG    CD     sing N N 200 
GLU   CG    HG2    sing N N 201 
GLU   CG    HG3    sing N N 202 
GLU   CD    OE1    doub N N 203 
GLU   CD    OE2    sing N N 204 
GLU   OE2   HE2    sing N N 205 
GLU   OXT   HXT    sing N N 206 
GLY   N     CA     sing N N 207 
GLY   N     H      sing N N 208 
GLY   N     H2     sing N N 209 
GLY   CA    C      sing N N 210 
GLY   CA    HA2    sing N N 211 
GLY   CA    HA3    sing N N 212 
GLY   C     O      doub N N 213 
GLY   C     OXT    sing N N 214 
GLY   OXT   HXT    sing N N 215 
GOL   C1    O1     sing N N 216 
GOL   C1    C2     sing N N 217 
GOL   C1    H11    sing N N 218 
GOL   C1    H12    sing N N 219 
GOL   O1    HO1    sing N N 220 
GOL   C2    O2     sing N N 221 
GOL   C2    C3     sing N N 222 
GOL   C2    H2     sing N N 223 
GOL   O2    HO2    sing N N 224 
GOL   C3    O3     sing N N 225 
GOL   C3    H31    sing N N 226 
GOL   C3    H32    sing N N 227 
GOL   O3    HO3    sing N N 228 
HIS   N     CA     sing N N 229 
HIS   N     H      sing N N 230 
HIS   N     H2     sing N N 231 
HIS   CA    C      sing N N 232 
HIS   CA    CB     sing N N 233 
HIS   CA    HA     sing N N 234 
HIS   C     O      doub N N 235 
HIS   C     OXT    sing N N 236 
HIS   CB    CG     sing N N 237 
HIS   CB    HB2    sing N N 238 
HIS   CB    HB3    sing N N 239 
HIS   CG    ND1    sing Y N 240 
HIS   CG    CD2    doub Y N 241 
HIS   ND1   CE1    doub Y N 242 
HIS   ND1   HD1    sing N N 243 
HIS   CD2   NE2    sing Y N 244 
HIS   CD2   HD2    sing N N 245 
HIS   CE1   NE2    sing Y N 246 
HIS   CE1   HE1    sing N N 247 
HIS   NE2   HE2    sing N N 248 
HIS   OXT   HXT    sing N N 249 
HOH   O     H1     sing N N 250 
HOH   O     H2     sing N N 251 
ILE   N     CA     sing N N 252 
ILE   N     H      sing N N 253 
ILE   N     H2     sing N N 254 
ILE   CA    C      sing N N 255 
ILE   CA    CB     sing N N 256 
ILE   CA    HA     sing N N 257 
ILE   C     O      doub N N 258 
ILE   C     OXT    sing N N 259 
ILE   CB    CG1    sing N N 260 
ILE   CB    CG2    sing N N 261 
ILE   CB    HB     sing N N 262 
ILE   CG1   CD1    sing N N 263 
ILE   CG1   HG12   sing N N 264 
ILE   CG1   HG13   sing N N 265 
ILE   CG2   HG21   sing N N 266 
ILE   CG2   HG22   sing N N 267 
ILE   CG2   HG23   sing N N 268 
ILE   CD1   HD11   sing N N 269 
ILE   CD1   HD12   sing N N 270 
ILE   CD1   HD13   sing N N 271 
ILE   OXT   HXT    sing N N 272 
LEU   N     CA     sing N N 273 
LEU   N     H      sing N N 274 
LEU   N     H2     sing N N 275 
LEU   CA    C      sing N N 276 
LEU   CA    CB     sing N N 277 
LEU   CA    HA     sing N N 278 
LEU   C     O      doub N N 279 
LEU   C     OXT    sing N N 280 
LEU   CB    CG     sing N N 281 
LEU   CB    HB2    sing N N 282 
LEU   CB    HB3    sing N N 283 
LEU   CG    CD1    sing N N 284 
LEU   CG    CD2    sing N N 285 
LEU   CG    HG     sing N N 286 
LEU   CD1   HD11   sing N N 287 
LEU   CD1   HD12   sing N N 288 
LEU   CD1   HD13   sing N N 289 
LEU   CD2   HD21   sing N N 290 
LEU   CD2   HD22   sing N N 291 
LEU   CD2   HD23   sing N N 292 
LEU   OXT   HXT    sing N N 293 
LYS   N     CA     sing N N 294 
LYS   N     H      sing N N 295 
LYS   N     H2     sing N N 296 
LYS   CA    C      sing N N 297 
LYS   CA    CB     sing N N 298 
LYS   CA    HA     sing N N 299 
LYS   C     O      doub N N 300 
LYS   C     OXT    sing N N 301 
LYS   CB    CG     sing N N 302 
LYS   CB    HB2    sing N N 303 
LYS   CB    HB3    sing N N 304 
LYS   CG    CD     sing N N 305 
LYS   CG    HG2    sing N N 306 
LYS   CG    HG3    sing N N 307 
LYS   CD    CE     sing N N 308 
LYS   CD    HD2    sing N N 309 
LYS   CD    HD3    sing N N 310 
LYS   CE    NZ     sing N N 311 
LYS   CE    HE2    sing N N 312 
LYS   CE    HE3    sing N N 313 
LYS   NZ    HZ1    sing N N 314 
LYS   NZ    HZ2    sing N N 315 
LYS   NZ    HZ3    sing N N 316 
LYS   OXT   HXT    sing N N 317 
MET   N     CA     sing N N 318 
MET   N     H      sing N N 319 
MET   N     H2     sing N N 320 
MET   CA    C      sing N N 321 
MET   CA    CB     sing N N 322 
MET   CA    HA     sing N N 323 
MET   C     O      doub N N 324 
MET   C     OXT    sing N N 325 
MET   CB    CG     sing N N 326 
MET   CB    HB2    sing N N 327 
MET   CB    HB3    sing N N 328 
MET   CG    SD     sing N N 329 
MET   CG    HG2    sing N N 330 
MET   CG    HG3    sing N N 331 
MET   SD    CE     sing N N 332 
MET   CE    HE1    sing N N 333 
MET   CE    HE2    sing N N 334 
MET   CE    HE3    sing N N 335 
MET   OXT   HXT    sing N N 336 
MTA   CS    "S5'"  sing N N 337 
MTA   CS    HCS1   sing N N 338 
MTA   CS    HCS2   sing N N 339 
MTA   CS    HCS3   sing N N 340 
MTA   "S5'" "C5'"  sing N N 341 
MTA   "C5'" "C4'"  sing N N 342 
MTA   "C5'" "H5'1" sing N N 343 
MTA   "C5'" "H5'2" sing N N 344 
MTA   "C4'" "O4'"  sing N N 345 
MTA   "C4'" "C3'"  sing N N 346 
MTA   "C4'" "H4'"  sing N N 347 
MTA   "O4'" "C1'"  sing N N 348 
MTA   "C2'" "O2'"  sing N N 349 
MTA   "C2'" "C3'"  sing N N 350 
MTA   "C2'" "C1'"  sing N N 351 
MTA   "C2'" "H2'"  sing N N 352 
MTA   "O2'" "HO2'" sing N N 353 
MTA   "C3'" "O3'"  sing N N 354 
MTA   "C3'" "H3'"  sing N N 355 
MTA   "O3'" H3T    sing N N 356 
MTA   "C1'" N9     sing N N 357 
MTA   "C1'" "H1'"  sing N N 358 
MTA   N9    C8     sing Y N 359 
MTA   N9    C4     sing Y N 360 
MTA   C8    N7     doub Y N 361 
MTA   C8    H8     sing N N 362 
MTA   N7    C5     sing Y N 363 
MTA   C5    C6     sing Y N 364 
MTA   C5    C4     doub Y N 365 
MTA   C6    N6     sing N N 366 
MTA   C6    N1     doub Y N 367 
MTA   N6    H61    sing N N 368 
MTA   N6    H62    sing N N 369 
MTA   N1    C2     sing Y N 370 
MTA   C2    N3     doub Y N 371 
MTA   C2    H2     sing N N 372 
MTA   N3    C4     sing Y N 373 
PHE   N     CA     sing N N 374 
PHE   N     H      sing N N 375 
PHE   N     H2     sing N N 376 
PHE   CA    C      sing N N 377 
PHE   CA    CB     sing N N 378 
PHE   CA    HA     sing N N 379 
PHE   C     O      doub N N 380 
PHE   C     OXT    sing N N 381 
PHE   CB    CG     sing N N 382 
PHE   CB    HB2    sing N N 383 
PHE   CB    HB3    sing N N 384 
PHE   CG    CD1    doub Y N 385 
PHE   CG    CD2    sing Y N 386 
PHE   CD1   CE1    sing Y N 387 
PHE   CD1   HD1    sing N N 388 
PHE   CD2   CE2    doub Y N 389 
PHE   CD2   HD2    sing N N 390 
PHE   CE1   CZ     doub Y N 391 
PHE   CE1   HE1    sing N N 392 
PHE   CE2   CZ     sing Y N 393 
PHE   CE2   HE2    sing N N 394 
PHE   CZ    HZ     sing N N 395 
PHE   OXT   HXT    sing N N 396 
PRO   N     CA     sing N N 397 
PRO   N     CD     sing N N 398 
PRO   N     H      sing N N 399 
PRO   CA    C      sing N N 400 
PRO   CA    CB     sing N N 401 
PRO   CA    HA     sing N N 402 
PRO   C     O      doub N N 403 
PRO   C     OXT    sing N N 404 
PRO   CB    CG     sing N N 405 
PRO   CB    HB2    sing N N 406 
PRO   CB    HB3    sing N N 407 
PRO   CG    CD     sing N N 408 
PRO   CG    HG2    sing N N 409 
PRO   CG    HG3    sing N N 410 
PRO   CD    HD2    sing N N 411 
PRO   CD    HD3    sing N N 412 
PRO   OXT   HXT    sing N N 413 
SER   N     CA     sing N N 414 
SER   N     H      sing N N 415 
SER   N     H2     sing N N 416 
SER   CA    C      sing N N 417 
SER   CA    CB     sing N N 418 
SER   CA    HA     sing N N 419 
SER   C     O      doub N N 420 
SER   C     OXT    sing N N 421 
SER   CB    OG     sing N N 422 
SER   CB    HB2    sing N N 423 
SER   CB    HB3    sing N N 424 
SER   OG    HG     sing N N 425 
SER   OXT   HXT    sing N N 426 
THR   N     CA     sing N N 427 
THR   N     H      sing N N 428 
THR   N     H2     sing N N 429 
THR   CA    C      sing N N 430 
THR   CA    CB     sing N N 431 
THR   CA    HA     sing N N 432 
THR   C     O      doub N N 433 
THR   C     OXT    sing N N 434 
THR   CB    OG1    sing N N 435 
THR   CB    CG2    sing N N 436 
THR   CB    HB     sing N N 437 
THR   OG1   HG1    sing N N 438 
THR   CG2   HG21   sing N N 439 
THR   CG2   HG22   sing N N 440 
THR   CG2   HG23   sing N N 441 
THR   OXT   HXT    sing N N 442 
TRP   N     CA     sing N N 443 
TRP   N     H      sing N N 444 
TRP   N     H2     sing N N 445 
TRP   CA    C      sing N N 446 
TRP   CA    CB     sing N N 447 
TRP   CA    HA     sing N N 448 
TRP   C     O      doub N N 449 
TRP   C     OXT    sing N N 450 
TRP   CB    CG     sing N N 451 
TRP   CB    HB2    sing N N 452 
TRP   CB    HB3    sing N N 453 
TRP   CG    CD1    doub Y N 454 
TRP   CG    CD2    sing Y N 455 
TRP   CD1   NE1    sing Y N 456 
TRP   CD1   HD1    sing N N 457 
TRP   CD2   CE2    doub Y N 458 
TRP   CD2   CE3    sing Y N 459 
TRP   NE1   CE2    sing Y N 460 
TRP   NE1   HE1    sing N N 461 
TRP   CE2   CZ2    sing Y N 462 
TRP   CE3   CZ3    doub Y N 463 
TRP   CE3   HE3    sing N N 464 
TRP   CZ2   CH2    doub Y N 465 
TRP   CZ2   HZ2    sing N N 466 
TRP   CZ3   CH2    sing Y N 467 
TRP   CZ3   HZ3    sing N N 468 
TRP   CH2   HH2    sing N N 469 
TRP   OXT   HXT    sing N N 470 
TYR   N     CA     sing N N 471 
TYR   N     H      sing N N 472 
TYR   N     H2     sing N N 473 
TYR   CA    C      sing N N 474 
TYR   CA    CB     sing N N 475 
TYR   CA    HA     sing N N 476 
TYR   C     O      doub N N 477 
TYR   C     OXT    sing N N 478 
TYR   CB    CG     sing N N 479 
TYR   CB    HB2    sing N N 480 
TYR   CB    HB3    sing N N 481 
TYR   CG    CD1    doub Y N 482 
TYR   CG    CD2    sing Y N 483 
TYR   CD1   CE1    sing Y N 484 
TYR   CD1   HD1    sing N N 485 
TYR   CD2   CE2    doub Y N 486 
TYR   CD2   HD2    sing N N 487 
TYR   CE1   CZ     doub Y N 488 
TYR   CE1   HE1    sing N N 489 
TYR   CE2   CZ     sing Y N 490 
TYR   CE2   HE2    sing N N 491 
TYR   CZ    OH     sing N N 492 
TYR   OH    HH     sing N N 493 
TYR   OXT   HXT    sing N N 494 
VAL   N     CA     sing N N 495 
VAL   N     H      sing N N 496 
VAL   N     H2     sing N N 497 
VAL   CA    C      sing N N 498 
VAL   CA    CB     sing N N 499 
VAL   CA    HA     sing N N 500 
VAL   C     O      doub N N 501 
VAL   C     OXT    sing N N 502 
VAL   CB    CG1    sing N N 503 
VAL   CB    CG2    sing N N 504 
VAL   CB    HB     sing N N 505 
VAL   CG1   HG11   sing N N 506 
VAL   CG1   HG12   sing N N 507 
VAL   CG1   HG13   sing N N 508 
VAL   CG2   HG21   sing N N 509 
VAL   CG2   HG22   sing N N 510 
VAL   CG2   HG23   sing N N 511 
VAL   OXT   HXT    sing N N 512 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8VEO 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9MGP 
_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]   0.010087 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007263 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.005604 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
NA 
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . ARG   A  1 21  ? 40.22000 -68.62900  -18.15400 1.000 112.98295 ? 13  ARG   A N     1 
ATOM   2    C  CA    . ARG   A  1 21  ? 40.37700 -69.52900  -19.34400 1.000 103.21406 ? 13  ARG   A CA    1 
ATOM   3    C  C     . ARG   A  1 21  ? 39.21900 -70.53800  -19.37200 1.000 94.85306  ? 13  ARG   A C     1 
ATOM   4    O  O     . ARG   A  1 21  ? 38.29400 -70.39600  -18.55000 1.000 97.19501  ? 13  ARG   A O     1 
ATOM   5    C  CB    . ARG   A  1 21  ? 41.76100 -70.19100  -19.34400 1.000 107.15704 ? 13  ARG   A CB    1 
ATOM   6    C  CG    . ARG   A  1 21  ? 42.06200 -71.08100  -18.14400 1.000 105.76914 ? 13  ARG   A CG    1 
ATOM   7    C  CD    . ARG   A  1 21  ? 43.53000 -71.47400  -18.11700 1.000 109.48777 ? 13  ARG   A CD    1 
ATOM   8    N  NE    . ARG   A  1 21  ? 44.02900 -71.77100  -16.77900 1.000 115.74686 ? 13  ARG   A NE    1 
ATOM   9    C  CZ    . ARG   A  1 21  ? 45.31600 -71.81900  -16.43200 1.000 117.29226 ? 13  ARG   A CZ    1 
ATOM   10   N  NH1   . ARG   A  1 21  ? 46.26700 -71.58300  -17.32200 1.000 115.36520 ? 13  ARG   A NH1   1 
ATOM   11   N  NH2   . ARG   A  1 21  ? 45.65100 -72.10200  -15.18400 1.000 112.07585 ? 13  ARG   A NH2   1 
ATOM   12   N  N     . VAL   A  1 22  ? 39.26800 -71.51000  -20.28800 1.000 98.54784  ? 14  VAL   A N     1 
ATOM   13   C  CA    . VAL   A  1 22  ? 38.10100 -72.35500  -20.68500 1.000 93.19037  ? 14  VAL   A CA    1 
ATOM   14   C  C     . VAL   A  1 22  ? 38.00500 -73.57300  -19.76000 1.000 90.59162  ? 14  VAL   A C     1 
ATOM   15   O  O     . VAL   A  1 22  ? 38.98700 -74.33400  -19.68200 1.000 90.97456  ? 14  VAL   A O     1 
ATOM   16   C  CB    . VAL   A  1 22  ? 38.19800 -72.80100  -22.15800 1.000 92.60869  ? 14  VAL   A CB    1 
ATOM   17   C  CG1   . VAL   A  1 22  ? 36.91100 -73.45700  -22.63200 1.000 87.52520  ? 14  VAL   A CG1   1 
ATOM   18   C  CG2   . VAL   A  1 22  ? 38.57600 -71.65300  -23.08000 1.000 93.60489  ? 14  VAL   A CG2   1 
ATOM   19   N  N     . SER   A  1 23  ? 36.85600 -73.74300  -19.09900 1.000 89.17037  ? 15  SER   A N     1 
ATOM   20   C  CA    . SER   A  1 23  ? 36.42900 -75.00500  -18.43800 1.000 86.04918  ? 15  SER   A CA    1 
ATOM   21   C  C     . SER   A  1 23  ? 35.90100 -75.95500  -19.51700 1.000 83.09853  ? 15  SER   A C     1 
ATOM   22   O  O     . SER   A  1 23  ? 34.90300 -75.59500  -20.17300 1.000 79.12553  ? 15  SER   A O     1 
ATOM   23   C  CB    . SER   A  1 23  ? 35.39100 -74.75300  -17.37400 1.000 83.33863  ? 15  SER   A CB    1 
ATOM   24   O  OG    . SER   A  1 23  ? 34.90900 -75.97800  -16.84100 1.000 80.52791  ? 15  SER   A OG    1 
ATOM   25   N  N     . SER   A  1 24  ? 36.55100 -77.10900  -19.69800 1.000 78.57218  ? 16  SER   A N     1 
ATOM   26   C  CA    . SER   A  1 24  ? 36.29600 -78.05600  -20.81600 1.000 74.83959  ? 16  SER   A CA    1 
ATOM   27   C  C     . SER   A  1 24  ? 36.26100 -79.50200  -20.31300 1.000 71.67781  ? 16  SER   A C     1 
ATOM   28   O  O     . SER   A  1 24  ? 36.95600 -79.80200  -19.32700 1.000 77.65795  ? 16  SER   A O     1 
ATOM   29   C  CB    . SER   A  1 24  ? 37.33300 -77.89200  -21.89200 1.000 78.25714  ? 16  SER   A CB    1 
ATOM   30   O  OG    . SER   A  1 24  ? 38.62900 -78.15200  -21.37500 1.000 87.52602  ? 16  SER   A OG    1 
ATOM   31   N  N     . GLY   A  1 25  ? 35.49500 -80.35800  -20.99700 1.000 74.33322  ? 17  GLY   A N     1 
ATOM   32   C  CA    . GLY   A  1 25  ? 35.34500 -81.79200  -20.68100 1.000 76.80894  ? 17  GLY   A CA    1 
ATOM   33   C  C     . GLY   A  1 25  ? 35.56300 -82.66900  -21.90300 1.000 73.55177  ? 17  GLY   A C     1 
ATOM   34   O  O     . GLY   A  1 25  ? 35.59200 -82.12800  -23.02100 1.000 70.69213  ? 17  GLY   A O     1 
ATOM   35   N  N     . ARG   A  1 26  ? 35.74000 -83.97500  -21.68300 1.000 71.71977  ? 18  ARG   A N     1 
ATOM   36   C  CA    . ARG   A  1 26  ? 35.88400 -85.01300  -22.73800 1.000 70.76189  ? 18  ARG   A CA    1 
ATOM   37   C  C     . ARG   A  1 26  ? 34.61700 -85.87300  -22.75200 1.000 69.47186  ? 18  ARG   A C     1 
ATOM   38   O  O     . ARG   A  1 26  ? 34.19300 -86.31000  -21.66400 1.000 66.84765  ? 18  ARG   A O     1 
ATOM   39   C  CB    . ARG   A  1 26  ? 37.12200 -85.87700  -22.47400 1.000 69.56352  ? 18  ARG   A CB    1 
ATOM   40   C  CG    . ARG   A  1 26  ? 37.36300 -86.97400  -23.50400 1.000 77.80321  ? 18  ARG   A CG    1 
ATOM   41   C  CD    . ARG   A  1 26  ? 38.12300 -86.49500  -24.72800 1.000 81.11451  ? 18  ARG   A CD    1 
ATOM   42   N  NE    . ARG   A  1 26  ? 38.32300 -87.55700  -25.70900 1.000 86.40673  ? 18  ARG   A NE    1 
ATOM   43   C  CZ    . ARG   A  1 26  ? 37.48300 -87.87200  -26.69700 1.000 81.32796  ? 18  ARG   A CZ    1 
ATOM   44   N  NH1   . ARG   A  1 26  ? 36.35300 -87.20600  -26.86900 1.000 77.14433  ? 18  ARG   A NH1   1 
ATOM   45   N  NH2   . ARG   A  1 26  ? 37.78600 -88.86000  -27.52200 1.000 83.04939  ? 18  ARG   A NH2   1 
ATOM   46   N  N     . ASP   A  1 27  ? 34.04200 -86.09600  -23.93800 1.000 72.83334  ? 19  ASP   A N     1 
ATOM   47   C  CA    . ASP   A  1 27  ? 32.91400 -87.03900  -24.15900 1.000 68.42584  ? 19  ASP   A CA    1 
ATOM   48   C  C     . ASP   A  1 27  ? 33.47400 -88.34200  -24.73400 1.000 66.89729  ? 19  ASP   A C     1 
ATOM   49   O  O     . ASP   A  1 27  ? 34.06100 -88.29500  -25.82900 1.000 75.56258  ? 19  ASP   A O     1 
ATOM   50   C  CB    . ASP   A  1 27  ? 31.84800 -86.44300  -25.08200 1.000 66.93706  ? 19  ASP   A CB    1 
ATOM   51   C  CG    . ASP   A  1 27  ? 30.71000 -87.40100  -25.39900 1.000 63.89158  ? 19  ASP   A CG    1 
ATOM   52   O  OD1   . ASP   A  1 27  ? 30.40800 -88.25600  -24.54500 1.000 65.41143  ? 19  ASP   A OD1   1 
ATOM   53   O  OD2   . ASP   A  1 27  ? 30.14200 -87.29100  -26.49800 1.000 64.54895  ? 19  ASP   A OD2   1 
ATOM   54   N  N     . LEU   A  1 28  ? 33.30400 -89.44900  -24.00500 1.000 64.82647  ? 20  LEU   A N     1 
ATOM   55   C  CA    . LEU   A  1 28  ? 33.65000 -90.82500  -24.45000 1.000 68.11317  ? 20  LEU   A CA    1 
ATOM   56   C  C     . LEU   A  1 28  ? 32.40100 -91.70300  -24.34000 1.000 67.57937  ? 20  LEU   A C     1 
ATOM   57   O  O     . LEU   A  1 28  ? 31.57600 -91.44500  -23.44200 1.000 69.57019  ? 20  LEU   A O     1 
ATOM   58   C  CB    . LEU   A  1 28  ? 34.78800 -91.37100  -23.58200 1.000 68.69662  ? 20  LEU   A CB    1 
ATOM   59   C  CG    . LEU   A  1 28  ? 36.09800 -90.58400  -23.63100 1.000 75.58097  ? 20  LEU   A CG    1 
ATOM   60   C  CD1   . LEU   A  1 28  ? 37.04700 -91.03700  -22.53000 1.000 74.83621  ? 20  LEU   A CD1   1 
ATOM   61   C  CD2   . LEU   A  1 28  ? 36.76500 -90.71000  -24.99200 1.000 77.43352  ? 20  LEU   A CD2   1 
ATOM   62   N  N     . ASN   A  1 29  ? 32.26000 -92.67900  -25.23900 1.000 65.08186  ? 21  ASN   A N     1 
ATOM   63   C  CA    . ASN   A  1 29  ? 31.17700 -93.69700  -25.20800 1.000 65.72710  ? 21  ASN   A CA    1 
ATOM   64   C  C     . ASN   A  1 29  ? 31.80200 -95.06700  -24.90900 1.000 67.92255  ? 21  ASN   A C     1 
ATOM   65   O  O     . ASN   A  1 29  ? 31.06900 -96.07000  -24.95900 1.000 69.23884  ? 21  ASN   A O     1 
ATOM   66   C  CB    . ASN   A  1 29  ? 30.36700 -93.67600  -26.50800 1.000 63.09599  ? 21  ASN   A CB    1 
ATOM   67   C  CG    . ASN   A  1 29  ? 28.87000 -93.78400  -26.29400 1.000 67.72569  ? 21  ASN   A CG    1 
ATOM   68   O  OD1   . ASN   A  1 29  ? 28.34100 -93.33500  -25.27900 1.000 65.03122  ? 21  ASN   A OD1   1 
ATOM   69   N  ND2   . ASN   A  1 29  ? 28.17100 -94.35500  -27.26100 1.000 71.43906  ? 21  ASN   A ND2   1 
ATOM   70   N  N     . CYS   A  1 30  ? 33.10200 -95.09200  -24.58400 1.000 66.91148  ? 22  CYS   A N     1 
ATOM   71   C  CA    . CYS   A  1 30  ? 33.90500 -96.31000  -24.29000 1.000 67.32920  ? 22  CYS   A CA    1 
ATOM   72   C  C     . CYS   A  1 30  ? 34.83200 -96.03200  -23.10100 1.000 74.93184  ? 22  CYS   A C     1 
ATOM   73   O  O     . CYS   A  1 30  ? 35.69700 -95.14100  -23.22700 1.000 78.46619  ? 22  CYS   A O     1 
ATOM   74   C  CB    . CYS   A  1 30  ? 34.72500 -96.72700  -25.50600 1.000 69.92382  ? 22  CYS   A CB    1 
ATOM   75   S  SG    . CYS   A  1 30  ? 35.97700 -97.98800  -25.14700 1.000 74.36713  ? 22  CYS   A SG    1 
ATOM   76   N  N     . VAL   A  1 31  ? 34.64900 -96.76400  -21.99600 1.000 75.13251  ? 23  VAL   A N     1 
ATOM   77   C  CA    . VAL   A  1 31  ? 35.42100 -96.60600  -20.72500 1.000 78.94338  ? 23  VAL   A CA    1 
ATOM   78   C  C     . VAL   A  1 31  ? 35.73100 -97.99700  -20.17300 1.000 82.20916  ? 23  VAL   A C     1 
ATOM   79   O  O     . VAL   A  1 31  ? 34.93200 -98.55600  -19.42500 1.000 84.53995  ? 23  VAL   A O     1 
ATOM   80   C  CB    . VAL   A  1 31  ? 34.64500 -95.74900  -19.70200 1.000 76.55040  ? 23  VAL   A CB    1 
ATOM   81   C  CG1   . VAL   A  1 31  ? 35.40800 -95.58500  -18.39600 1.000 80.52690  ? 23  VAL   A CG1   1 
ATOM   82   C  CG2   . VAL   A  1 31  ? 34.27000 -94.38700  -20.26600 1.000 70.90751  ? 23  VAL   A CG2   1 
ATOM   83   N  N     . PRO   A  1 32  ? 36.88700 -98.61000  -20.52600 1.000 81.38189  ? 24  PRO   A N     1 
ATOM   84   C  CA    . PRO   A  1 32  ? 37.23200 -99.94200  -20.02800 1.000 83.48435  ? 24  PRO   A CA    1 
ATOM   85   C  C     . PRO   A  1 32  ? 37.49900 -99.90100  -18.51500 1.000 89.83246  ? 24  PRO   A C     1 
ATOM   86   O  O     . PRO   A  1 32  ? 36.77100 -100.54400 -17.77800 1.000 92.05512  ? 24  PRO   A O     1 
ATOM   87   C  CB    . PRO   A  1 32  ? 38.48800 -100.35300 -20.81900 1.000 86.13116  ? 24  PRO   A CB    1 
ATOM   88   C  CG    . PRO   A  1 32  ? 38.62700 -99.31400  -21.92100 1.000 86.35542  ? 24  PRO   A CG    1 
ATOM   89   C  CD    . PRO   A  1 32  ? 37.92300 -98.07000  -21.41900 1.000 83.40546  ? 24  PRO   A CD    1 
ATOM   90   N  N     . GLU   A  1 33  ? 38.51000 -99.13000  -18.09900 1.000 90.58726  ? 25  GLU   A N     1 
ATOM   91   C  CA    . GLU   A  1 33  ? 38.89500 -98.92100  -16.67700 1.000 90.30512  ? 25  GLU   A CA    1 
ATOM   92   C  C     . GLU   A  1 33  ? 38.66000 -97.44600  -16.32100 1.000 88.75009  ? 25  GLU   A C     1 
ATOM   93   O  O     . GLU   A  1 33  ? 39.51000 -96.60200  -16.67100 1.000 89.70656  ? 25  GLU   A O     1 
ATOM   94   C  CB    . GLU   A  1 33  ? 40.34800 -99.35300  -16.45100 1.000 92.72505  ? 25  GLU   A CB    1 
ATOM   95   C  CG    . GLU   A  1 33  ? 40.61600 -99.88600  -15.05300 1.000 95.60609  ? 25  GLU   A CG    1 
ATOM   96   C  CD    . GLU   A  1 33  ? 40.24900 -101.34500 -14.83800 1.000 105.66716 ? 25  GLU   A CD    1 
ATOM   97   O  OE1   . GLU   A  1 33  ? 39.44300 -101.87900 -15.62800 1.000 106.05836 ? 25  GLU   A OE1   1 
ATOM   98   O  OE2   . GLU   A  1 33  ? 40.77500 -101.95000 -13.88100 1.000 116.41167 ? 25  GLU   A OE2   1 
ATOM   99   N  N     . ILE   A  1 34  ? 37.52700 -97.15900  -15.67100 1.000 86.11543  ? 26  ILE   A N     1 
ATOM   100  C  CA    . ILE   A  1 34  ? 37.11500 -95.80600  -15.18300 1.000 84.34549  ? 26  ILE   A CA    1 
ATOM   101  C  C     . ILE   A  1 34  ? 38.29900 -95.11100  -14.49200 1.000 83.91548  ? 26  ILE   A C     1 
ATOM   102  O  O     . ILE   A  1 34  ? 38.43300 -93.88200  -14.65500 1.000 81.82430  ? 26  ILE   A O     1 
ATOM   103  C  CB    . ILE   A  1 34  ? 35.88000 -95.91400  -14.26100 1.000 82.16238  ? 26  ILE   A CB    1 
ATOM   104  C  CG1   . ILE   A  1 34  ? 35.38900 -94.53800  -13.80500 1.000 79.42566  ? 26  ILE   A CG1   1 
ATOM   105  C  CG2   . ILE   A  1 34  ? 36.14200 -96.83500  -13.07600 1.000 82.79384  ? 26  ILE   A CG2   1 
ATOM   106  C  CD1   . ILE   A  1 34  ? 33.95400 -94.53300  -13.33600 1.000 82.58872  ? 26  ILE   A CD1   1 
ATOM   107  N  N     . ALA   A  1 35  ? 39.11800 -95.86700  -13.75300 1.000 85.34700  ? 27  ALA   A N     1 
ATOM   108  C  CA    . ALA   A  1 35  ? 40.35200 -95.39100  -13.08300 1.000 84.57671  ? 27  ALA   A CA    1 
ATOM   109  C  C     . ALA   A  1 35  ? 41.33500 -94.84500  -14.12800 1.000 88.79729  ? 27  ALA   A C     1 
ATOM   110  O  O     . ALA   A  1 35  ? 41.65300 -93.64100  -14.06400 1.000 87.11777  ? 27  ALA   A O     1 
ATOM   111  C  CB    . ALA   A  1 35  ? 40.96400 -96.51100  -12.27700 1.000 85.91444  ? 27  ALA   A CB    1 
ATOM   112  N  N     . ASP   A  1 36  ? 41.78000 -95.69800  -15.06000 1.000 89.76130  ? 28  ASP   A N     1 
ATOM   113  C  CA    . ASP   A  1 36  ? 42.77800 -95.36500  -16.11500 1.000 89.30060  ? 28  ASP   A CA    1 
ATOM   114  C  C     . ASP   A  1 36  ? 42.22100 -94.26900  -17.03100 1.000 88.26051  ? 28  ASP   A C     1 
ATOM   115  O  O     . ASP   A  1 36  ? 42.94700 -93.28400  -17.27800 1.000 89.67979  ? 28  ASP   A O     1 
ATOM   116  C  CB    . ASP   A  1 36  ? 43.15200 -96.59200  -16.95300 1.000 90.38250  ? 28  ASP   A CB    1 
ATOM   117  C  CG    . ASP   A  1 36  ? 43.90200 -97.66700  -16.18700 1.000 98.99492  ? 28  ASP   A CG    1 
ATOM   118  O  OD1   . ASP   A  1 36  ? 44.74300 -97.30400  -15.34000 1.000 106.02971 ? 28  ASP   A OD1   1 
ATOM   119  O  OD2   . ASP   A  1 36  ? 43.64100 -98.85800  -16.44900 1.000 102.76337 ? 28  ASP   A OD2   1 
ATOM   120  N  N     . THR   A  1 37  ? 40.99100 -94.45000  -17.52300 1.000 87.75306  ? 29  THR   A N     1 
ATOM   121  C  CA    . THR   A  1 37  ? 40.29400 -93.53200  -18.46600 1.000 85.70237  ? 29  THR   A CA    1 
ATOM   122  C  C     . THR   A  1 37  ? 40.29100 -92.10800  -17.89600 1.000 87.01219  ? 29  THR   A C     1 
ATOM   123  O  O     . THR   A  1 37  ? 40.77500 -91.19700  -18.59500 1.000 83.88908  ? 29  THR   A O     1 
ATOM   124  C  CB    . THR   A  1 37  ? 38.87400 -94.02800  -18.76700 1.000 80.40485  ? 29  THR   A CB    1 
ATOM   125  O  OG1   . THR   A  1 37  ? 38.98700 -95.28600  -19.43300 1.000 80.99252  ? 29  THR   A OG1   1 
ATOM   126  C  CG2   . THR   A  1 37  ? 38.07500 -93.07200  -19.62700 1.000 78.28066  ? 29  THR   A CG2   1 
ATOM   127  N  N     . LEU   A  1 38  ? 39.77000 -91.93100  -16.67700 1.000 84.31631  ? 30  LEU   A N     1 
ATOM   128  C  CA    . LEU   A  1 38  ? 39.62600 -90.60700  -16.01000 1.000 83.10527  ? 30  LEU   A CA    1 
ATOM   129  C  C     . LEU   A  1 38  ? 41.01100 -90.00500  -15.73900 1.000 83.84807  ? 30  LEU   A C     1 
ATOM   130  O  O     . LEU   A  1 38  ? 41.15900 -88.77600  -15.89200 1.000 84.40523  ? 30  LEU   A O     1 
ATOM   131  C  CB    . LEU   A  1 38  ? 38.82900 -90.77600  -14.71200 1.000 79.31366  ? 30  LEU   A CB    1 
ATOM   132  C  CG    . LEU   A  1 38  ? 38.56100 -89.49300  -13.92500 1.000 79.62719  ? 30  LEU   A CG    1 
ATOM   133  C  CD1   . LEU   A  1 38  ? 37.78600 -88.48000  -14.75900 1.000 75.19297  ? 30  LEU   A CD1   1 
ATOM   134  C  CD2   . LEU   A  1 38  ? 37.81400 -89.80100  -12.63700 1.000 76.13688  ? 30  LEU   A CD2   1 
ATOM   135  N  N     . GLY   A  1 39  ? 41.98200 -90.83700  -15.34700 1.000 83.00945  ? 31  GLY   A N     1 
ATOM   136  C  CA    . GLY   A  1 39  ? 43.38500 -90.43000  -15.13100 1.000 85.74526  ? 31  GLY   A CA    1 
ATOM   137  C  C     . GLY   A  1 39  ? 44.03500 -89.92200  -16.40900 1.000 88.02226  ? 31  GLY   A C     1 
ATOM   138  O  O     . GLY   A  1 39  ? 44.92000 -89.04800  -16.31400 1.000 91.04250  ? 31  GLY   A O     1 
ATOM   139  N  N     . ALA   A  1 40  ? 43.61200 -90.44800  -17.56400 1.000 87.04381  ? 32  ALA   A N     1 
ATOM   140  C  CA    . ALA   A  1 40  ? 44.14600 -90.10900  -18.90300 1.000 86.72315  ? 32  ALA   A CA    1 
ATOM   141  C  C     . ALA   A  1 40  ? 43.58100 -88.76200  -19.37700 1.000 90.69178  ? 32  ALA   A C     1 
ATOM   142  O  O     . ALA   A  1 40  ? 44.37400 -87.95300  -19.89100 1.000 97.11164  ? 32  ALA   A O     1 
ATOM   143  C  CB    . ALA   A  1 40  ? 43.83700 -91.21500  -19.88300 1.000 86.79132  ? 32  ALA   A CB    1 
ATOM   144  N  N     . VAL   A  1 41  ? 42.27300 -88.52400  -19.21000 1.000 87.22066  ? 33  VAL   A N     1 
ATOM   145  C  CA    . VAL   A  1 41  ? 41.58900 -87.29600  -19.72400 1.000 87.69663  ? 33  VAL   A CA    1 
ATOM   146  C  C     . VAL   A  1 41  ? 42.04200 -86.09000  -18.88900 1.000 91.03684  ? 33  VAL   A C     1 
ATOM   147  O  O     . VAL   A  1 41  ? 42.18000 -84.99500  -19.46500 1.000 94.19635  ? 33  VAL   A O     1 
ATOM   148  C  CB    . VAL   A  1 41  ? 40.05000 -87.42300  -19.75400 1.000 84.86942  ? 33  VAL   A CB    1 
ATOM   149  C  CG1   . VAL   A  1 41  ? 39.59300 -88.70300  -20.43900 1.000 86.37874  ? 33  VAL   A CG1   1 
ATOM   150  C  CG2   . VAL   A  1 41  ? 39.41900 -87.29900  -18.37600 1.000 82.54198  ? 33  VAL   A CG2   1 
ATOM   151  N  N     . ALA   A  1 42  ? 42.25900 -86.28200  -17.58400 1.000 89.52743  ? 34  ALA   A N     1 
ATOM   152  C  CA    . ALA   A  1 42  ? 42.80200 -85.25600  -16.66200 1.000 90.04420  ? 34  ALA   A CA    1 
ATOM   153  C  C     . ALA   A  1 42  ? 44.24600 -84.93300  -17.06500 1.000 95.59443  ? 34  ALA   A C     1 
ATOM   154  O  O     . ALA   A  1 42  ? 44.61000 -83.74000  -17.06300 1.000 97.67905  ? 34  ALA   A O     1 
ATOM   155  C  CB    . ALA   A  1 42  ? 42.71300 -85.73600  -15.23400 1.000 88.81019  ? 34  ALA   A CB    1 
ATOM   156  N  N     . LYS   A  1 43  ? 45.02200 -85.96800  -17.40900 1.000 94.37930  ? 35  LYS   A N     1 
ATOM   157  C  CA    . LYS   A  1 43  ? 46.41000 -85.86300  -17.94100 1.000 98.88189  ? 35  LYS   A CA    1 
ATOM   158  C  C     . LYS   A  1 43  ? 46.37800 -85.15400  -19.30300 1.000 101.62341 ? 35  LYS   A C     1 
ATOM   159  O  O     . LYS   A  1 43  ? 47.29800 -84.35300  -19.56800 1.000 103.36000 ? 35  LYS   A O     1 
ATOM   160  C  CB    . LYS   A  1 43  ? 47.03800 -87.25800  -18.03800 1.000 100.99252 ? 35  LYS   A CB    1 
ATOM   161  C  CG    . LYS   A  1 43  ? 48.38900 -87.33700  -18.73800 1.000 104.01032 ? 35  LYS   A CG    1 
ATOM   162  C  CD    . LYS   A  1 43  ? 49.54100 -86.79800  -17.91900 1.000 111.64373 ? 35  LYS   A CD    1 
ATOM   163  C  CE    . LYS   A  1 43  ? 50.89100 -87.17700  -18.49100 1.000 115.46901 ? 35  LYS   A CE    1 
ATOM   164  N  NZ    . LYS   A  1 43  ? 51.99500 -86.85000  -17.55900 1.000 116.13407 ? 35  LYS   A NZ    1 
ATOM   165  N  N     . GLN   A  1 44  ? 45.36700 -85.44700  -20.13000 1.000 96.44904  ? 36  GLN   A N     1 
ATOM   166  C  CA    . GLN   A  1 44  ? 45.12400 -84.78000  -21.44100 1.000 98.31607  ? 36  GLN   A CA    1 
ATOM   167  C  C     . GLN   A  1 44  ? 44.86100 -83.28500  -21.20400 1.000 97.88882  ? 36  GLN   A C     1 
ATOM   168  O  O     . GLN   A  1 44  ? 45.27300 -82.47900  -22.06000 1.000 105.15766 ? 36  GLN   A O     1 
ATOM   169  C  CB    . GLN   A  1 44  ? 43.96900 -85.45300  -22.19400 1.000 99.65757  ? 36  GLN   A CB    1 
ATOM   170  C  CG    . GLN   A  1 44  ? 44.37100 -86.73400  -22.91800 1.000 105.57450 ? 36  GLN   A CG    1 
ATOM   171  C  CD    . GLN   A  1 44  ? 43.19400 -87.56100  -23.38300 1.000 101.81659 ? 36  GLN   A CD    1 
ATOM   172  O  OE1   . GLN   A  1 44  ? 42.06600 -87.08100  -23.48600 1.000 97.46357  ? 36  GLN   A OE1   1 
ATOM   173  N  NE2   . GLN   A  1 44  ? 43.45300 -88.82500  -23.67800 1.000 101.38939 ? 36  GLN   A NE2   1 
ATOM   174  N  N     . GLY   A  1 45  ? 44.21000 -82.93500  -20.08700 1.000 97.96855  ? 37  GLY   A N     1 
ATOM   175  C  CA    . GLY   A  1 45  ? 44.03100 -81.54300  -19.62200 1.000 94.48845  ? 37  GLY   A CA    1 
ATOM   176  C  C     . GLY   A  1 45  ? 42.57700 -81.16000  -19.36900 1.000 89.71195  ? 37  GLY   A C     1 
ATOM   177  O  O     . GLY   A  1 45  ? 42.33900 -79.97300  -19.07100 1.000 88.03185  ? 37  GLY   A O     1 
ATOM   178  N  N     . PHE   A  1 46  ? 41.63800 -82.10900  -19.46700 1.000 90.86100  ? 38  PHE   A N     1 
ATOM   179  C  CA    . PHE   A  1 46  ? 40.17800 -81.87700  -19.29500 1.000 84.15090  ? 38  PHE   A CA    1 
ATOM   180  C  C     . PHE   A  1 46  ? 39.85300 -81.69000  -17.80800 1.000 87.63151  ? 38  PHE   A C     1 
ATOM   181  O  O     . PHE   A  1 46  ? 40.58400 -82.23600  -16.95900 1.000 94.01528  ? 38  PHE   A O     1 
ATOM   182  C  CB    . PHE   A  1 46  ? 39.37600 -83.02600  -19.91200 1.000 78.53370  ? 38  PHE   A CB    1 
ATOM   183  C  CG    . PHE   A  1 46  ? 39.46600 -83.09500  -21.41500 1.000 83.22213  ? 38  PHE   A CG    1 
ATOM   184  C  CD1   . PHE   A  1 46  ? 38.69600 -82.25900  -22.20800 1.000 77.65115  ? 38  PHE   A CD1   1 
ATOM   185  C  CD2   . PHE   A  1 46  ? 40.33300 -83.97900  -22.03800 1.000 85.12287  ? 38  PHE   A CD2   1 
ATOM   186  C  CE1   . PHE   A  1 46  ? 38.78100 -82.31500  -23.59000 1.000 76.53116  ? 38  PHE   A CE1   1 
ATOM   187  C  CE2   . PHE   A  1 46  ? 40.41900 -84.03200  -23.42100 1.000 83.96294  ? 38  PHE   A CE2   1 
ATOM   188  C  CZ    . PHE   A  1 46  ? 39.64300 -83.20000  -24.19400 1.000 82.94917  ? 38  PHE   A CZ    1 
ATOM   189  N  N     . ASP   A  1 47  ? 38.78500 -80.93800  -17.51600 1.000 88.15254  ? 39  ASP   A N     1 
ATOM   190  C  CA    . ASP   A  1 47  ? 38.31900 -80.61100  -16.14100 1.000 86.67515  ? 39  ASP   A CA    1 
ATOM   191  C  C     . ASP   A  1 47  ? 37.31000 -81.66300  -15.66100 1.000 79.87488  ? 39  ASP   A C     1 
ATOM   192  O  O     . ASP   A  1 47  ? 37.17000 -81.81600  -14.42900 1.000 87.66339  ? 39  ASP   A O     1 
ATOM   193  C  CB    . ASP   A  1 47  ? 37.70700 -79.20900  -16.07700 1.000 82.63865  ? 39  ASP   A CB    1 
ATOM   194  C  CG    . ASP   A  1 47  ? 38.71900 -78.08700  -16.23400 1.000 88.84889  ? 39  ASP   A CG    1 
ATOM   195  O  OD1   . ASP   A  1 47  ? 39.90900 -78.39100  -16.45700 1.000 90.11396  ? 39  ASP   A OD1   1 
ATOM   196  O  OD2   . ASP   A  1 47  ? 38.30800 -76.91600  -16.12800 1.000 95.84424  ? 39  ASP   A OD2   1 
ATOM   197  N  N     . PHE   A  1 48  ? 36.62500 -82.34600  -16.58500 1.000 76.79115  ? 40  PHE   A N     1 
ATOM   198  C  CA    . PHE   A  1 48  ? 35.59600 -83.37300  -16.27400 1.000 74.79752  ? 40  PHE   A CA    1 
ATOM   199  C  C     . PHE   A  1 48  ? 35.45800 -84.36000  -17.44200 1.000 74.10266  ? 40  PHE   A C     1 
ATOM   200  O  O     . PHE   A  1 48  ? 36.10200 -84.15900  -18.49200 1.000 73.23184  ? 40  PHE   A O     1 
ATOM   201  C  CB    . PHE   A  1 48  ? 34.26900 -82.69400  -15.92200 1.000 74.32043  ? 40  PHE   A CB    1 
ATOM   202  C  CG    . PHE   A  1 48  ? 33.60600 -81.93900  -17.04700 1.000 71.46317  ? 40  PHE   A CG    1 
ATOM   203  C  CD1   . PHE   A  1 48  ? 33.98400 -80.64100  -17.35100 1.000 72.48854  ? 40  PHE   A CD1   1 
ATOM   204  C  CD2   . PHE   A  1 48  ? 32.58200 -82.51800  -17.78200 1.000 69.25475  ? 40  PHE   A CD2   1 
ATOM   205  C  CE1   . PHE   A  1 48  ? 33.36200 -79.94400  -18.37700 1.000 75.22215  ? 40  PHE   A CE1   1 
ATOM   206  C  CE2   . PHE   A  1 48  ? 31.96000 -81.81900  -18.80600 1.000 66.06217  ? 40  PHE   A CE2   1 
ATOM   207  C  CZ    . PHE   A  1 48  ? 32.35000 -80.53300  -19.10000 1.000 68.36225  ? 40  PHE   A CZ    1 
ATOM   208  N  N     . LEU   A  1 49  ? 34.64100 -85.40000  -17.24300 1.000 70.46840  ? 41  LEU   A N     1 
ATOM   209  C  CA    . LEU   A  1 49  ? 34.44800 -86.54000  -18.17800 1.000 68.15166  ? 41  LEU   A CA    1 
ATOM   210  C  C     . LEU   A  1 49  ? 32.94900 -86.81900  -18.33800 1.000 68.71954  ? 41  LEU   A C     1 
ATOM   211  O  O     . LEU   A  1 49  ? 32.27600 -87.01700  -17.30800 1.000 68.55880  ? 41  LEU   A O     1 
ATOM   212  C  CB    . LEU   A  1 49  ? 35.17100 -87.77000  -17.61600 1.000 68.17876  ? 41  LEU   A CB    1 
ATOM   213  C  CG    . LEU   A  1 49  ? 34.83700 -89.10400  -18.28700 1.000 68.54387  ? 41  LEU   A CG    1 
ATOM   214  C  CD1   . LEU   A  1 49  ? 35.42400 -89.16600  -19.68800 1.000 70.85999  ? 41  LEU   A CD1   1 
ATOM   215  C  CD2   . LEU   A  1 49  ? 35.32900 -90.27800  -17.45400 1.000 67.68981  ? 41  LEU   A CD2   1 
ATOM   216  N  N     . CYS   A  1 50  ? 32.46200 -86.84600  -19.58300 1.000 64.94777  ? 42  CYS   A N     1 
ATOM   217  C  CA    . CYS   A  1 50  ? 31.10400 -87.32200  -19.96000 1.000 63.65591  ? 42  CYS   A CA    1 
ATOM   218  C  C     . CYS   A  1 50  ? 31.20900 -88.78300  -20.41500 1.000 66.23302  ? 42  CYS   A C     1 
ATOM   219  O  O     . CYS   A  1 50  ? 31.81200 -89.02500  -21.48200 1.000 70.61779  ? 42  CYS   A O     1 
ATOM   220  C  CB    . CYS   A  1 50  ? 30.49500 -86.45200  -21.05400 1.000 62.54344  ? 42  CYS   A CB    1 
ATOM   221  S  SG    . CYS   A  1 50  ? 30.61700 -84.67700  -20.71400 1.000 65.42177  ? 42  CYS   A SG    1 
ATOM   222  N  N     . MET   A  1 51  ? 30.67300 -89.71800  -19.62200 1.000 68.83113  ? 43  MET   A N     1 
ATOM   223  C  CA    . MET   A  1 51  ? 30.76300 -91.18300  -19.87100 1.000 66.52261  ? 43  MET   A CA    1 
ATOM   224  C  C     . MET   A  1 51  ? 29.39800 -91.83400  -19.66100 1.000 63.78017  ? 43  MET   A C     1 
ATOM   225  O  O     . MET   A  1 51  ? 28.49300 -91.22300  -19.09500 1.000 61.09503  ? 43  MET   A O     1 
ATOM   226  C  CB    . MET   A  1 51  ? 31.78800 -91.84200  -18.94000 1.000 66.36114  ? 43  MET   A CB    1 
ATOM   227  C  CG    . MET   A  1 51  ? 31.47400 -91.69900  -17.45800 1.000 62.58015  ? 43  MET   A CG    1 
ATOM   228  S  SD    . MET   A  1 51  ? 32.68000 -92.55000  -16.39600 1.000 75.70749  ? 43  MET   A SD    1 
ATOM   229  C  CE    . MET   A  1 51  ? 32.24600 -94.26300  -16.69800 1.000 76.69858  ? 43  MET   A CE    1 
ATOM   230  N  N     . PRO   A  1 52  ? 29.20400 -93.08600  -20.13500 1.000 65.45552  ? 44  PRO   A N     1 
ATOM   231  C  CA    . PRO   A  1 52  ? 28.04500 -93.89300  -19.75500 1.000 67.08528  ? 44  PRO   A CA    1 
ATOM   232  C  C     . PRO   A  1 52  ? 28.19800 -94.43900  -18.32700 1.000 62.66361  ? 44  PRO   A C     1 
ATOM   233  O  O     . PRO   A  1 52  ? 29.30600 -94.76200  -17.94400 1.000 61.78439  ? 44  PRO   A O     1 
ATOM   234  C  CB    . PRO   A  1 52  ? 28.03000 -95.05000  -20.77100 1.000 68.16246  ? 44  PRO   A CB    1 
ATOM   235  C  CG    . PRO   A  1 52  ? 29.06600 -94.67800  -21.81800 1.000 65.81167  ? 44  PRO   A CG    1 
ATOM   236  C  CD    . PRO   A  1 52  ? 30.05800 -93.78300  -21.10700 1.000 66.51039  ? 44  PRO   A CD    1 
ATOM   237  N  N     . VAL   A  1 53  ? 27.09000 -94.52900  -17.58600 1.000 58.39372  ? 45  VAL   A N     1 
ATOM   238  C  CA    . VAL   A  1 53  ? 27.05400 -95.06900  -16.19300 1.000 64.45610  ? 45  VAL   A CA    1 
ATOM   239  C  C     . VAL   A  1 53  ? 26.59100 -96.53100  -16.23400 1.000 66.27912  ? 45  VAL   A C     1 
ATOM   240  O  O     . VAL   A  1 53  ? 26.76100 -97.22800  -15.21600 1.000 65.59387  ? 45  VAL   A O     1 
ATOM   241  C  CB    . VAL   A  1 53  ? 26.18500 -94.20100  -15.26000 1.000 63.82026  ? 45  VAL   A CB    1 
ATOM   242  C  CG1   . VAL   A  1 53  ? 26.82800 -92.84500  -15.01700 1.000 60.61442  ? 45  VAL   A CG1   1 
ATOM   243  C  CG2   . VAL   A  1 53  ? 24.75600 -94.03200  -15.76000 1.000 62.70167  ? 45  VAL   A CG2   1 
ATOM   244  N  N     . PHE   A  1 54  ? 26.01000 -96.95700  -17.36100 1.000 64.13534  ? 46  PHE   A N     1 
ATOM   245  C  CA    . PHE   A  1 54  ? 25.83100 -98.37300  -17.77500 1.000 63.17201  ? 46  PHE   A CA    1 
ATOM   246  C  C     . PHE   A  1 54  ? 26.44100 -98.53500  -19.17000 1.000 68.29653  ? 46  PHE   A C     1 
ATOM   247  O  O     . PHE   A  1 54  ? 26.34300 -97.57800  -19.96500 1.000 71.80534  ? 46  PHE   A O     1 
ATOM   248  C  CB    . PHE   A  1 54  ? 24.35000 -98.76100  -17.79700 1.000 60.79677  ? 46  PHE   A CB    1 
ATOM   249  C  CG    . PHE   A  1 54  ? 23.68600 -98.83100  -16.44600 1.000 63.38395  ? 46  PHE   A CG    1 
ATOM   250  C  CD1   . PHE   A  1 54  ? 23.37000 -97.67500  -15.75000 1.000 60.29784  ? 46  PHE   A CD1   1 
ATOM   251  C  CD2   . PHE   A  1 54  ? 23.35800 -100.05300 -15.87800 1.000 65.57677  ? 46  PHE   A CD2   1 
ATOM   252  C  CE1   . PHE   A  1 54  ? 22.75500 -97.73900  -14.50900 1.000 63.70686  ? 46  PHE   A CE1   1 
ATOM   253  C  CE2   . PHE   A  1 54  ? 22.74600 -100.11600 -14.63600 1.000 69.21597  ? 46  PHE   A CE2   1 
ATOM   254  C  CZ    . PHE   A  1 54  ? 22.44400 -98.95900  -13.95400 1.000 67.61518  ? 46  PHE   A CZ    1 
ATOM   255  N  N     . HIS   A  1 55  ? 27.05000 -99.68900  -19.46500 1.000 72.80577  ? 47  HIS   A N     1 
ATOM   256  C  CA    . HIS   A  1 55  ? 27.67100 -99.97500  -20.78700 1.000 76.65281  ? 47  HIS   A CA    1 
ATOM   257  C  C     . HIS   A  1 55  ? 26.64800 -99.67300  -21.88100 1.000 72.38710  ? 47  HIS   A C     1 
ATOM   258  O  O     . HIS   A  1 55  ? 25.54000 -100.20600 -21.85100 1.000 71.24627  ? 47  HIS   A O     1 
ATOM   259  C  CB    . HIS   A  1 55  ? 28.20000 -101.41300 -20.86200 1.000 79.19185  ? 47  HIS   A CB    1 
ATOM   260  C  CG    . HIS   A  1 55  ? 29.15800 -101.63300 -21.98600 1.000 81.18896  ? 47  HIS   A CG    1 
ATOM   261  N  ND1   . HIS   A  1 55  ? 28.80100 -101.45100 -23.30600 1.000 74.21353  ? 47  HIS   A ND1   1 
ATOM   262  C  CD2   . HIS   A  1 55  ? 30.45400 -102.01500 -21.99300 1.000 87.72460  ? 47  HIS   A CD2   1 
ATOM   263  C  CE1   . HIS   A  1 55  ? 29.83600 -101.71200 -24.07900 1.000 81.22537  ? 47  HIS   A CE1   1 
ATOM   264  N  NE2   . HIS   A  1 55  ? 30.86400 -102.06300 -23.29700 1.000 80.93142  ? 47  HIS   A NE2   1 
ATOM   265  N  N     . PRO   A  1 56  ? 26.96800 -98.78200  -22.85100 1.000 69.76622  ? 48  PRO   A N     1 
ATOM   266  C  CA    . PRO   A  1 56  ? 25.99700 -98.34500  -23.85700 1.000 68.70624  ? 48  PRO   A CA    1 
ATOM   267  C  C     . PRO   A  1 56  ? 25.21800 -99.46300  -24.56500 1.000 67.82415  ? 48  PRO   A C     1 
ATOM   268  O  O     . PRO   A  1 56  ? 24.07600 -99.23100  -24.89400 1.000 63.72172  ? 48  PRO   A O     1 
ATOM   269  C  CB    . PRO   A  1 56  ? 26.86900 -97.61000  -24.88400 1.000 66.62442  ? 48  PRO   A CB    1 
ATOM   270  C  CG    . PRO   A  1 56  ? 28.00900 -97.05800  -24.06400 1.000 62.86138  ? 48  PRO   A CG    1 
ATOM   271  C  CD    . PRO   A  1 56  ? 28.26900 -98.11200  -23.00900 1.000 66.91217  ? 48  PRO   A CD    1 
ATOM   272  N  N     . ARG   A  1 57  ? 25.84400 -100.62400 -24.78400 1.000 65.30323  ? 49  ARG   A N     1 
ATOM   273  C  CA    . ARG   A  1 57  ? 25.27200 -101.74200 -25.58300 1.000 73.24448  ? 49  ARG   A CA    1 
ATOM   274  C  C     . ARG   A  1 57  ? 24.55900 -102.75100 -24.67200 1.000 70.82816  ? 49  ARG   A C     1 
ATOM   275  O  O     . ARG   A  1 57  ? 23.84400 -103.61400 -25.21000 1.000 75.46300  ? 49  ARG   A O     1 
ATOM   276  C  CB    . ARG   A  1 57  ? 26.37200 -102.41400 -26.41000 1.000 71.03993  ? 49  ARG   A CB    1 
ATOM   277  C  CG    . ARG   A  1 57  ? 26.95500 -101.51500 -27.49000 1.000 68.95764  ? 49  ARG   A CG    1 
ATOM   278  C  CD    . ARG   A  1 57  ? 27.92600 -102.23800 -28.40200 1.000 76.05130  ? 49  ARG   A CD    1 
ATOM   279  N  NE    . ARG   A  1 57  ? 29.07800 -102.76200 -27.67600 1.000 76.65036  ? 49  ARG   A NE    1 
ATOM   280  C  CZ    . ARG   A  1 57  ? 29.32000 -104.04800 -27.42600 1.000 77.62071  ? 49  ARG   A CZ    1 
ATOM   281  N  NH1   . ARG   A  1 57  ? 28.49000 -104.99000 -27.84300 1.000 76.10625  ? 49  ARG   A NH1   1 
ATOM   282  N  NH2   . ARG   A  1 57  ? 30.40800 -104.39100 -26.75600 1.000 80.54327  ? 49  ARG   A NH2   1 
ATOM   283  N  N     . PHE   A  1 58  ? 24.72800 -102.64100 -23.35200 1.000 69.83135  ? 50  PHE   A N     1 
ATOM   284  C  CA    . PHE   A  1 58  ? 24.12200 -103.55300 -22.34600 1.000 74.82787  ? 50  PHE   A CA    1 
ATOM   285  C  C     . PHE   A  1 58  ? 22.62100 -103.26700 -22.23400 1.000 68.82813  ? 50  PHE   A C     1 
ATOM   286  O  O     . PHE   A  1 58  ? 22.19400 -102.67000 -21.22800 1.000 72.05638  ? 50  PHE   A O     1 
ATOM   287  C  CB    . PHE   A  1 58  ? 24.82300 -103.39600 -20.99300 1.000 76.27754  ? 50  PHE   A CB    1 
ATOM   288  C  CG    . PHE   A  1 58  ? 24.57100 -104.50600 -20.00300 1.000 77.07304  ? 50  PHE   A CG    1 
ATOM   289  C  CD1   . PHE   A  1 58  ? 24.79800 -105.83000 -20.35000 1.000 79.05584  ? 50  PHE   A CD1   1 
ATOM   290  C  CD2   . PHE   A  1 58  ? 24.14900 -104.22700 -18.71200 1.000 74.47109  ? 50  PHE   A CD2   1 
ATOM   291  C  CE1   . PHE   A  1 58  ? 24.59300 -106.85100 -19.43400 1.000 81.36427  ? 50  PHE   A CE1   1 
ATOM   292  C  CE2   . PHE   A  1 58  ? 23.94100 -105.24900 -17.79800 1.000 79.67132  ? 50  PHE   A CE2   1 
ATOM   293  C  CZ    . PHE   A  1 58  ? 24.16600 -106.55900 -18.15900 1.000 81.44790  ? 50  PHE   A CZ    1 
ATOM   294  N  N     . LYS   A  1 59  ? 21.84600 -103.68000 -23.24200 1.000 67.74181  ? 51  LYS   A N     1 
ATOM   295  C  CA    . LYS   A  1 59  ? 20.36700 -103.53400 -23.25200 1.000 68.59760  ? 51  LYS   A CA    1 
ATOM   296  C  C     . LYS   A  1 59  ? 19.80000 -104.44800 -22.16000 1.000 73.59716  ? 51  LYS   A C     1 
ATOM   297  O  O     . LYS   A  1 59  ? 20.35000 -105.55300 -21.97100 1.000 72.03525  ? 51  LYS   A O     1 
ATOM   298  C  CB    . LYS   A  1 59  ? 19.79800 -103.83900 -24.64300 1.000 74.57837  ? 51  LYS   A CB    1 
ATOM   299  C  CG    . LYS   A  1 59  ? 18.30700 -103.56600 -24.80800 1.000 72.98655  ? 51  LYS   A CG    1 
ATOM   300  C  CD    . LYS   A  1 59  ? 17.85300 -103.48900 -26.25600 1.000 79.34216  ? 51  LYS   A CD    1 
ATOM   301  C  CE    . LYS   A  1 59  ? 16.40500 -103.06400 -26.40000 1.000 85.68243  ? 51  LYS   A CE    1 
ATOM   302  N  NZ    . LYS   A  1 59  ? 15.93500 -103.16800 -27.80400 1.000 85.52756  ? 51  LYS   A NZ    1 
ATOM   303  N  N     . ARG   A  1 60  ? 18.76600 -103.98300 -21.45200 1.000 68.08372  ? 52  ARG   A N     1 
ATOM   304  C  CA    . ARG   A  1 60  ? 18.21700 -104.64000 -20.23500 1.000 65.75798  ? 52  ARG   A CA    1 
ATOM   305  C  C     . ARG   A  1 60  ? 16.69700 -104.77700 -20.36700 1.000 66.98294  ? 52  ARG   A C     1 
ATOM   306  O  O     . ARG   A  1 60  ? 16.04400 -103.80200 -20.79500 1.000 70.70350  ? 52  ARG   A O     1 
ATOM   307  C  CB    . ARG   A  1 60  ? 18.61600 -103.83900 -18.99100 1.000 64.11555  ? 52  ARG   A CB    1 
ATOM   308  C  CG    . ARG   A  1 60  ? 20.12000 -103.65500 -18.84300 1.000 65.59124  ? 52  ARG   A CG    1 
ATOM   309  C  CD    . ARG   A  1 60  ? 20.52700 -103.07900 -17.50100 1.000 65.73654  ? 52  ARG   A CD    1 
ATOM   310  N  NE    . ARG   A  1 60  ? 20.10800 -101.69200 -17.35400 1.000 69.21813  ? 52  ARG   A NE    1 
ATOM   311  C  CZ    . ARG   A  1 60  ? 20.70600 -100.64400 -17.91700 1.000 66.48403  ? 52  ARG   A CZ    1 
ATOM   312  N  NH1   . ARG   A  1 60  ? 21.77200 -100.80400 -18.68600 1.000 62.99792  ? 52  ARG   A NH1   1 
ATOM   313  N  NH2   . ARG   A  1 60  ? 20.22800 -99.43000  -17.70500 1.000 63.36713  ? 52  ARG   A NH2   1 
ATOM   314  N  N     . GLU   A  1 61  ? 16.17200 -105.95600 -20.01600 1.000 67.79465  ? 53  GLU   A N     1 
ATOM   315  C  CA    . GLU   A  1 61  ? 14.72800 -106.30700 -20.06400 1.000 69.21123  ? 53  GLU   A CA    1 
ATOM   316  C  C     . GLU   A  1 61  ? 14.16200 -106.22500 -18.64100 1.000 77.29697  ? 53  GLU   A C     1 
ATOM   317  O  O     . GLU   A  1 61  ? 14.84000 -106.70300 -17.70700 1.000 81.38155  ? 53  GLU   A O     1 
ATOM   318  C  CB    . GLU   A  1 61  ? 14.55400 -107.70100 -20.67500 1.000 69.50229  ? 53  GLU   A CB    1 
ATOM   319  C  CG    . GLU   A  1 61  ? 13.11100 -108.16700 -20.77500 1.000 73.81712  ? 53  GLU   A CG    1 
ATOM   320  C  CD    . GLU   A  1 61  ? 12.18600 -107.27300 -21.58400 1.000 74.51771  ? 53  GLU   A CD    1 
ATOM   321  O  OE1   . GLU   A  1 61  ? 12.68100 -106.53700 -22.45800 1.000 74.39226  ? 53  GLU   A OE1   1 
ATOM   322  O  OE2   . GLU   A  1 61  ? 10.96700 -107.32200 -21.33800 1.000 77.06944  ? 53  GLU   A OE2   1 
ATOM   323  N  N     . PHE   A  1 62  ? 12.96800 -105.64000 -18.49300 1.000 72.56928  ? 54  PHE   A N     1 
ATOM   324  C  CA    . PHE   A  1 62  ? 12.30600 -105.35300 -17.19100 1.000 65.90607  ? 54  PHE   A CA    1 
ATOM   325  C  C     . PHE   A  1 62  ? 10.96900 -106.09600 -17.06300 1.000 74.62032  ? 54  PHE   A C     1 
ATOM   326  O  O     . PHE   A  1 62  ? 10.45200 -106.16400 -15.93100 1.000 77.52909  ? 54  PHE   A O     1 
ATOM   327  C  CB    . PHE   A  1 62  ? 12.08900 -103.84600 -17.04600 1.000 63.96611  ? 54  PHE   A CB    1 
ATOM   328  C  CG    . PHE   A  1 62  ? 13.35900 -103.03500 -17.03400 1.000 64.22973  ? 54  PHE   A CG    1 
ATOM   329  C  CD1   . PHE   A  1 62  ? 14.00500 -102.70100 -18.21500 1.000 64.93742  ? 54  PHE   A CD1   1 
ATOM   330  C  CD2   . PHE   A  1 62  ? 13.91100 -102.60500 -15.83800 1.000 63.97386  ? 54  PHE   A CD2   1 
ATOM   331  C  CE1   . PHE   A  1 62  ? 15.17600 -101.95700 -18.19700 1.000 64.39664  ? 54  PHE   A CE1   1 
ATOM   332  C  CE2   . PHE   A  1 62  ? 15.07900 -101.85900 -15.82200 1.000 60.76031  ? 54  PHE   A CE2   1 
ATOM   333  C  CZ    . PHE   A  1 62  ? 15.71100 -101.53800 -17.00100 1.000 64.17517  ? 54  PHE   A CZ    1 
ATOM   334  N  N     . ILE   A  1 63  ? 10.42700 -106.63000 -18.16500 1.000 73.77729  ? 55  ILE   A N     1 
ATOM   335  C  CA    . ILE   A  1 63  ? 9.04900  -107.20400 -18.23200 1.000 75.92081  ? 55  ILE   A CA    1 
ATOM   336  C  C     . ILE   A  1 63  ? 9.12400  -108.71300 -18.49200 1.000 80.56373  ? 55  ILE   A C     1 
ATOM   337  O  O     . ILE   A  1 63  ? 8.69800  -109.48300 -17.60600 1.000 81.94514  ? 55  ILE   A O     1 
ATOM   338  C  CB    . ILE   A  1 63  ? 8.21100  -106.48100 -19.30700 1.000 71.34077  ? 55  ILE   A CB    1 
ATOM   339  C  CG1   . ILE   A  1 63  ? 7.84200  -105.06200 -18.86700 1.000 73.21879  ? 55  ILE   A CG1   1 
ATOM   340  C  CG2   . ILE   A  1 63  ? 6.97800  -107.29600 -19.67200 1.000 76.49642  ? 55  ILE   A CG2   1 
ATOM   341  C  CD1   . ILE   A  1 63  ? 7.24700  -104.20400 -19.96300 1.000 74.76541  ? 55  ILE   A CD1   1 
ATOM   342  N  N     . GLN   A  1 64  ? 9.62000  -109.10400 -19.67200 1.000 84.36500  ? 56  GLN   A N     1 
ATOM   343  C  CA    . GLN   A  1 64  ? 9.46200  -110.46900 -20.24800 1.000 81.98164  ? 56  GLN   A CA    1 
ATOM   344  C  C     . GLN   A  1 64  ? 10.62900 -111.36100 -19.80900 1.000 84.19446  ? 56  GLN   A C     1 
ATOM   345  O  O     . GLN   A  1 64  ? 11.79000 -110.94900 -19.99400 1.000 85.10936  ? 56  GLN   A O     1 
ATOM   346  C  CB    . GLN   A  1 64  ? 9.36700  -110.39000 -21.77500 1.000 79.05370  ? 56  GLN   A CB    1 
ATOM   347  C  CG    . GLN   A  1 64  ? 8.56400  -111.52600 -22.39700 1.000 93.41180  ? 56  GLN   A CG    1 
ATOM   348  C  CD    . GLN   A  1 64  ? 8.47800  -111.44800 -23.90500 1.000 101.70935 ? 56  GLN   A CD    1 
ATOM   349  O  OE1   . GLN   A  1 64  ? 8.98700  -110.52400 -24.53800 1.000 94.60907  ? 56  GLN   A OE1   1 
ATOM   350  N  NE2   . GLN   A  1 64  ? 7.82700  -112.43500 -24.50000 1.000 102.82416 ? 56  GLN   A NE2   1 
ATOM   351  N  N     . GLU   A  1 65  ? 10.31800 -112.53500 -19.24900 1.000 86.37788  ? 57  GLU   A N     1 
ATOM   352  C  CA    . GLU   A  1 65  ? 11.29200 -113.61600 -18.92900 1.000 90.34418  ? 57  GLU   A CA    1 
ATOM   353  C  C     . GLU   A  1 65  ? 11.81900 -114.19600 -20.24100 1.000 97.02127  ? 57  GLU   A C     1 
ATOM   354  O  O     . GLU   A  1 65  ? 11.13300 -114.12100 -21.25800 1.000 99.06237  ? 57  GLU   A O     1 
ATOM   355  C  CB    . GLU   A  1 65  ? 10.61700 -114.69400 -18.07700 1.000 93.10607  ? 57  GLU   A CB    1 
ATOM   356  C  CG    . GLU   A  1 65  ? 10.24000 -114.22400 -16.68000 1.000 102.27031 ? 57  GLU   A CG    1 
ATOM   357  C  CD    . GLU   A  1 65  ? 9.07600  -114.96800 -16.04400 1.000 114.91230 ? 57  GLU   A CD    1 
ATOM   358  O  OE1   . GLU   A  1 65  ? 8.04400  -115.14000 -16.72400 1.000 120.22346 ? 57  GLU   A OE1   1 
ATOM   359  O  OE2   . GLU   A  1 65  ? 9.19800  -115.36400 -14.86500 1.000 112.07823 ? 57  GLU   A OE2   1 
ATOM   360  N  N     . PRO   A  1 66  ? 13.03500 -114.79300 -20.28700 1.000 91.25725  ? 58  PRO   A N     1 
ATOM   361  C  CA    . PRO   A  1 66  ? 13.91200 -114.94700 -19.12400 1.000 88.79720  ? 58  PRO   A CA    1 
ATOM   362  C  C     . PRO   A  1 66  ? 14.93500 -113.82200 -18.88400 1.000 90.22643  ? 58  PRO   A C     1 
ATOM   363  O  O     . PRO   A  1 66  ? 15.59400 -113.86200 -17.86200 1.000 91.95339  ? 58  PRO   A O     1 
ATOM   364  C  CB    . PRO   A  1 66  ? 14.65800 -116.23500 -19.49500 1.000 88.16215  ? 58  PRO   A CB    1 
ATOM   365  C  CG    . PRO   A  1 66  ? 14.85400 -116.11800 -20.99100 1.000 88.38443  ? 58  PRO   A CG    1 
ATOM   366  C  CD    . PRO   A  1 66  ? 13.62400 -115.39100 -21.49500 1.000 90.49226  ? 58  PRO   A CD    1 
ATOM   367  N  N     . ALA   A  1 67  ? 15.05400 -112.86700 -19.81400 1.000 90.47126  ? 59  ALA   A N     1 
ATOM   368  C  CA    . ALA   A  1 67  ? 16.02300 -111.74300 -19.76000 1.000 85.62325  ? 59  ALA   A CA    1 
ATOM   369  C  C     . ALA   A  1 67  ? 15.71800 -110.82900 -18.56400 1.000 86.17396  ? 59  ALA   A C     1 
ATOM   370  O  O     . ALA   A  1 67  ? 16.66500 -110.19100 -18.05200 1.000 82.74627  ? 59  ALA   A O     1 
ATOM   371  C  CB    . ALA   A  1 67  ? 15.99400 -110.97500 -21.05900 1.000 84.90996  ? 59  ALA   A CB    1 
ATOM   372  N  N     . LYS   A  1 68  ? 14.44400 -110.76200 -18.15600 1.000 92.33750  ? 60  LYS   A N     1 
ATOM   373  C  CA    . LYS   A  1 68  ? 13.94600 -110.02100 -16.96200 1.000 89.06939  ? 60  LYS   A CA    1 
ATOM   374  C  C     . LYS   A  1 68  ? 14.82700 -110.33700 -15.74500 1.000 91.06242  ? 60  LYS   A C     1 
ATOM   375  O  O     . LYS   A  1 68  ? 15.20200 -109.38400 -15.02900 1.000 86.29746  ? 60  LYS   A O     1 
ATOM   376  C  CB    . LYS   A  1 68  ? 12.48600 -110.40000 -16.69100 1.000 88.86874  ? 60  LYS   A CB    1 
ATOM   377  C  CG    . LYS   A  1 68  ? 11.82600 -109.72300 -15.49600 1.000 85.66430  ? 60  LYS   A CG    1 
ATOM   378  C  CD    . LYS   A  1 68  ? 10.52400 -110.38500 -15.08700 1.000 89.33328  ? 60  LYS   A CD    1 
ATOM   379  C  CE    . LYS   A  1 68  ? 9.68100  -109.53700 -14.15600 1.000 94.96447  ? 60  LYS   A CE    1 
ATOM   380  N  NZ    . LYS   A  1 68  ? 10.16800 -109.60600 -12.75700 1.000 97.80030  ? 60  LYS   A NZ    1 
ATOM   381  N  N     . ASN   A  1 69  ? 15.14700 -111.62000 -15.53400 1.000 82.89621  ? 61  ASN   A N     1 
ATOM   382  C  CA    . ASN   A  1 69  ? 15.85500 -112.12900 -14.32700 1.000 82.88735  ? 61  ASN   A CA    1 
ATOM   383  C  C     . ASN   A  1 69  ? 17.34400 -112.34500 -14.63600 1.000 81.61042  ? 61  ASN   A C     1 
ATOM   384  O  O     . ASN   A  1 69  ? 17.90800 -113.33600 -14.13700 1.000 84.53124  ? 61  ASN   A O     1 
ATOM   385  C  CB    . ASN   A  1 69  ? 15.19700 -113.40800 -13.80000 1.000 88.51769  ? 61  ASN   A CB    1 
ATOM   386  C  CG    . ASN   A  1 69  ? 13.71500 -113.25200 -13.52300 1.000 91.51022  ? 61  ASN   A CG    1 
ATOM   387  O  OD1   . ASN   A  1 69  ? 12.94300 -114.19100 -13.70800 1.000 98.21980  ? 61  ASN   A OD1   1 
ATOM   388  N  ND2   . ASN   A  1 69  ? 13.30600 -112.07500 -13.07700 1.000 88.83007  ? 61  ASN   A ND2   1 
ATOM   389  N  N     . ARG   A  1 70  ? 17.96500 -111.43400 -15.39500 1.000 78.94669  ? 62  ARG   A N     1 
ATOM   390  C  CA    . ARG   A  1 70  ? 19.41800 -111.45900 -15.71800 1.000 79.08522  ? 62  ARG   A CA    1 
ATOM   391  C  C     . ARG   A  1 70  ? 20.22000 -111.22400 -14.44100 1.000 80.07868  ? 62  ARG   A C     1 
ATOM   392  O  O     . ARG   A  1 70  ? 20.08400 -110.17100 -13.82100 1.000 79.89490  ? 62  ARG   A O     1 
ATOM   393  C  CB    . ARG   A  1 70  ? 19.75700 -110.38800 -16.76000 1.000 76.71638  ? 62  ARG   A CB    1 
ATOM   394  C  CG    . ARG   A  1 70  ? 21.24500 -110.24800 -17.05800 1.000 76.09421  ? 62  ARG   A CG    1 
ATOM   395  C  CD    . ARG   A  1 70  ? 21.54400 -109.11700 -18.02600 1.000 80.52116  ? 62  ARG   A CD    1 
ATOM   396  N  NE    . ARG   A  1 70  ? 20.82000 -109.24600 -19.28400 1.000 80.34299  ? 62  ARG   A NE    1 
ATOM   397  C  CZ    . ARG   A  1 70  ? 20.80500 -108.33700 -20.25600 1.000 79.13779  ? 62  ARG   A CZ    1 
ATOM   398  N  NH1   . ARG   A  1 70  ? 21.47900 -107.20600 -20.13300 1.000 71.98720  ? 62  ARG   A NH1   1 
ATOM   399  N  NH2   . ARG   A  1 70  ? 20.11100 -108.56800 -21.35700 1.000 87.05936  ? 62  ARG   A NH2   1 
ATOM   400  N  N     . PRO   A  1 71  ? 21.08000 -112.17800 -14.01200 1.000 82.76835  ? 63  PRO   A N     1 
ATOM   401  C  CA    . PRO   A  1 71  ? 21.93900 -111.97600 -12.84400 1.000 83.79777  ? 63  PRO   A CA    1 
ATOM   402  C  C     . PRO   A  1 71  ? 22.79300 -110.70400 -12.95300 1.000 81.15027  ? 63  PRO   A C     1 
ATOM   403  O  O     . PRO   A  1 71  ? 23.27300 -110.41500 -14.03600 1.000 83.24872  ? 63  PRO   A O     1 
ATOM   404  C  CB    . PRO   A  1 71  ? 22.85000 -113.21200 -12.83100 1.000 87.27887  ? 63  PRO   A CB    1 
ATOM   405  C  CG    . PRO   A  1 71  ? 22.05900 -114.26700 -13.57100 1.000 88.80550  ? 63  PRO   A CG    1 
ATOM   406  C  CD    . PRO   A  1 71  ? 21.26900 -113.50700 -14.61700 1.000 85.56196  ? 63  PRO   A CD    1 
ATOM   407  N  N     . GLY   A  1 72  ? 22.95000 -109.98400 -11.83700 1.000 82.30603  ? 64  GLY   A N     1 
ATOM   408  C  CA    . GLY   A  1 72  ? 23.78000 -108.76800 -11.74100 1.000 78.73768  ? 64  GLY   A CA    1 
ATOM   409  C  C     . GLY   A  1 72  ? 25.26300 -109.11400 -11.61900 1.000 80.54381  ? 64  GLY   A C     1 
ATOM   410  O  O     . GLY   A  1 72  ? 25.63800 -110.27900 -11.74500 1.000 83.24341  ? 64  GLY   A O     1 
ATOM   411  N  N     . PRO   A  1 73  ? 26.15900 -108.12800 -11.38000 1.000 79.36558  ? 65  PRO   A N     1 
ATOM   412  C  CA    . PRO   A  1 73  ? 25.78100 -106.71500 -11.27300 1.000 76.36349  ? 65  PRO   A CA    1 
ATOM   413  C  C     . PRO   A  1 73  ? 25.32400 -106.09300 -12.60100 1.000 79.20191  ? 65  PRO   A C     1 
ATOM   414  O  O     . PRO   A  1 73  ? 25.74200 -106.56800 -13.64200 1.000 89.13173  ? 65  PRO   A O     1 
ATOM   415  C  CB    . PRO   A  1 73  ? 27.07300 -106.03000 -10.80500 1.000 76.55545  ? 65  PRO   A CB    1 
ATOM   416  C  CG    . PRO   A  1 73  ? 28.17800 -106.94200 -11.29300 1.000 78.69272  ? 65  PRO   A CG    1 
ATOM   417  C  CD    . PRO   A  1 73  ? 27.60200 -108.33700 -11.18300 1.000 81.18609  ? 65  PRO   A CD    1 
ATOM   418  N  N     . GLN   A  1 74  ? 24.49700 -105.04400 -12.52600 1.000 73.41305  ? 66  GLN   A N     1 
ATOM   419  C  CA    . GLN   A  1 74  ? 23.86300 -104.38000 -13.69900 1.000 69.38637  ? 66  GLN   A CA    1 
ATOM   420  C  C     . GLN   A  1 74  ? 24.79000 -103.29300 -14.25700 1.000 71.14196  ? 66  GLN   A C     1 
ATOM   421  O  O     . GLN   A  1 74  ? 24.64700 -102.96600 -15.45100 1.000 74.72078  ? 66  GLN   A O     1 
ATOM   422  C  CB    . GLN   A  1 74  ? 22.50100 -103.80400 -13.31000 1.000 67.04423  ? 66  GLN   A CB    1 
ATOM   423  C  CG    . GLN   A  1 74  ? 21.48800 -104.86200 -12.89500 1.000 68.87340  ? 66  GLN   A CG    1 
ATOM   424  C  CD    . GLN   A  1 74  ? 21.21400 -105.86500 -13.99000 1.000 73.85134  ? 66  GLN   A CD    1 
ATOM   425  O  OE1   . GLN   A  1 74  ? 21.08000 -105.51500 -15.16200 1.000 67.81930  ? 66  GLN   A OE1   1 
ATOM   426  N  NE2   . GLN   A  1 74  ? 21.13100 -107.13100 -13.61300 1.000 77.25635  ? 66  GLN   A NE2   1 
ATOM   427  N  N     . THR   A  1 75  ? 25.68800 -102.74400 -13.43200 1.000 70.79246  ? 67  THR   A N     1 
ATOM   428  C  CA    . THR   A  1 75  ? 26.78100 -101.83000 -13.86600 1.000 67.73648  ? 67  THR   A CA    1 
ATOM   429  C  C     . THR   A  1 75  ? 27.96000 -101.92500 -12.89100 1.000 71.52444  ? 67  THR   A C     1 
ATOM   430  O  O     . THR   A  1 75  ? 27.88900 -102.74400 -11.96000 1.000 73.51672  ? 67  THR   A O     1 
ATOM   431  C  CB    . THR   A  1 75  ? 26.28700 -100.38600 -14.00900 1.000 69.66623  ? 67  THR   A CB    1 
ATOM   432  O  OG1   . THR   A  1 75  ? 27.37200 -99.62300  -14.53600 1.000 72.75869  ? 67  THR   A OG1   1 
ATOM   433  C  CG2   . THR   A  1 75  ? 25.80400 -99.77800  -12.70900 1.000 66.52259  ? 67  THR   A CG2   1 
ATOM   434  N  N     . ARG   A  1 76  ? 28.99900 -101.11500 -13.11100 1.000 72.89859  ? 68  ARG   A N     1 
ATOM   435  C  CA    . ARG   A  1 76  ? 30.24300 -101.10500 -12.29400 1.000 77.25932  ? 68  ARG   A CA    1 
ATOM   436  C  C     . ARG   A  1 76  ? 29.98300 -100.33800 -10.98800 1.000 74.21663  ? 68  ARG   A C     1 
ATOM   437  O  O     . ARG   A  1 76  ? 29.06100 -99.49800  -10.96300 1.000 69.35508  ? 68  ARG   A O     1 
ATOM   438  C  CB    . ARG   A  1 76  ? 31.41100 -100.53300 -13.10800 1.000 81.64984  ? 68  ARG   A CB    1 
ATOM   439  C  CG    . ARG   A  1 76  ? 31.38200 -99.02300  -13.30500 1.000 80.66964  ? 68  ARG   A CG    1 
ATOM   440  C  CD    . ARG   A  1 76  ? 32.71800 -98.46000  -13.76000 1.000 79.85236  ? 68  ARG   A CD    1 
ATOM   441  N  NE    . ARG   A  1 76  ? 32.71300 -98.03800  -15.15600 1.000 86.16500  ? 68  ARG   A NE    1 
ATOM   442  C  CZ    . ARG   A  1 76  ? 33.30100 -98.67500  -16.17000 1.000 87.64195  ? 68  ARG   A CZ    1 
ATOM   443  N  NH1   . ARG   A  1 76  ? 33.96900 -99.80200  -15.98000 1.000 85.55762  ? 68  ARG   A NH1   1 
ATOM   444  N  NH2   . ARG   A  1 76  ? 33.21900 -98.16900  -17.38900 1.000 87.16891  ? 68  ARG   A NH2   1 
ATOM   445  N  N     . SER   A  1 77  ? 30.78700 -100.61500 -9.95600  1.000 77.70351  ? 69  SER   A N     1 
ATOM   446  C  CA    . SER   A  1 77  ? 30.57500 -100.17800 -8.54900  1.000 72.82915  ? 69  SER   A CA    1 
ATOM   447  C  C     . SER   A  1 77  ? 30.81400 -98.67100  -8.39200  1.000 72.42325  ? 69  SER   A C     1 
ATOM   448  O  O     . SER   A  1 77  ? 31.65700 -98.11200  -9.12600  1.000 71.32455  ? 69  SER   A O     1 
ATOM   449  C  CB    . SER   A  1 77  ? 31.45700 -100.95900 -7.60900  1.000 76.25136  ? 69  SER   A CB    1 
ATOM   450  O  OG    . SER   A  1 77  ? 31.09100 -100.72600 -6.25500  1.000 81.37969  ? 69  SER   A OG    1 
ATOM   451  N  N     . ASP   A  1 78  ? 30.10200 -98.05800  -7.43900  1.000 71.16955  ? 70  ASP   A N     1 
ATOM   452  C  CA    . ASP   A  1 78  ? 30.28300 -96.65000  -6.99000  1.000 70.36370  ? 70  ASP   A CA    1 
ATOM   453  C  C     . ASP   A  1 78  ? 31.57000 -96.53200  -6.16000  1.000 72.81237  ? 70  ASP   A C     1 
ATOM   454  O  O     . ASP   A  1 78  ? 32.00800 -95.39500  -5.91100  1.000 72.44450  ? 70  ASP   A O     1 
ATOM   455  C  CB    . ASP   A  1 78  ? 29.06900 -96.17100  -6.18800  1.000 70.09265  ? 70  ASP   A CB    1 
ATOM   456  C  CG    . ASP   A  1 78  ? 28.81400 -96.96100  -4.91400  1.000 72.97945  ? 70  ASP   A CG    1 
ATOM   457  O  OD1   . ASP   A  1 78  ? 29.12600 -98.17000  -4.89900  1.000 74.69930  ? 70  ASP   A OD1   1 
ATOM   458  O  OD2   . ASP   A  1 78  ? 28.31000 -96.36200  -3.94300  1.000 73.73784  ? 70  ASP   A OD2   1 
ATOM   459  N  N     . LEU   A  1 79  ? 32.14700 -97.66500  -5.74400  1.000 75.44397  ? 71  LEU   A N     1 
ATOM   460  C  CA    . LEU   A  1 79  ? 33.38700 -97.74100  -4.92400  1.000 78.33137  ? 71  LEU   A CA    1 
ATOM   461  C  C     . LEU   A  1 79  ? 34.62100 -97.40100  -5.77500  1.000 77.92953  ? 71  LEU   A C     1 
ATOM   462  O  O     . LEU   A  1 79  ? 35.66800 -97.08400  -5.18100  1.000 80.42160  ? 71  LEU   A O     1 
ATOM   463  C  CB    . LEU   A  1 79  ? 33.49900 -99.15100  -4.33300  1.000 81.37524  ? 71  LEU   A CB    1 
ATOM   464  C  CG    . LEU   A  1 79  ? 32.41300 -99.53400  -3.32700  1.000 84.63626  ? 71  LEU   A CG    1 
ATOM   465  C  CD1   . LEU   A  1 79  ? 32.38100 -101.04000 -3.10200  1.000 87.39554  ? 71  LEU   A CD1   1 
ATOM   466  C  CD2   . LEU   A  1 79  ? 32.61300 -98.80500  -2.00700  1.000 84.45689  ? 71  LEU   A CD2   1 
ATOM   467  N  N     . LEU   A  1 80  ? 34.50500 -97.45300  -7.10600  1.000 77.89061  ? 72  LEU   A N     1 
ATOM   468  C  CA    . LEU   A  1 80  ? 35.64300 -97.29700  -8.05700  1.000 79.12043  ? 72  LEU   A CA    1 
ATOM   469  C  C     . LEU   A  1 80  ? 36.13100 -95.84200  -8.08800  1.000 78.62381  ? 72  LEU   A C     1 
ATOM   470  O  O     . LEU   A  1 80  ? 37.25200 -95.61800  -8.58200  1.000 80.22092  ? 72  LEU   A O     1 
ATOM   471  C  CB    . LEU   A  1 80  ? 35.20600 -97.77100  -9.44700  1.000 74.71836  ? 72  LEU   A CB    1 
ATOM   472  C  CG    . LEU   A  1 80  ? 34.84000 -99.25200  -9.55000  1.000 75.85639  ? 72  LEU   A CG    1 
ATOM   473  C  CD1   . LEU   A  1 80  ? 34.21700 -99.56700  -10.89900 1.000 79.65498  ? 72  LEU   A CD1   1 
ATOM   474  C  CD2   . LEU   A  1 80  ? 36.05400 -100.13400 -9.31100  1.000 78.95804  ? 72  LEU   A CD2   1 
ATOM   475  N  N     . LEU   A  1 81  ? 35.33400 -94.89400  -7.58200  1.000 79.34554  ? 73  LEU   A N     1 
ATOM   476  C  CA    . LEU   A  1 81  ? 35.72200 -93.46400  -7.43900  1.000 81.36099  ? 73  LEU   A CA    1 
ATOM   477  C  C     . LEU   A  1 81  ? 35.28600 -92.93200  -6.06900  1.000 77.70314  ? 73  LEU   A C     1 
ATOM   478  O  O     . LEU   A  1 81  ? 34.36000 -93.51400  -5.46600  1.000 79.77022  ? 73  LEU   A O     1 
ATOM   479  C  CB    . LEU   A  1 81  ? 35.06700 -92.64800  -8.55700  1.000 76.32944  ? 73  LEU   A CB    1 
ATOM   480  C  CG    . LEU   A  1 81  ? 35.61900 -92.86100  -9.96300  1.000 74.18552  ? 73  LEU   A CG    1 
ATOM   481  C  CD1   . LEU   A  1 81  ? 34.75000 -92.14200  -10.98300 1.000 74.13045  ? 73  LEU   A CD1   1 
ATOM   482  C  CD2   . LEU   A  1 81  ? 37.06100 -92.38800  -10.06700 1.000 76.49296  ? 73  LEU   A CD2   1 
ATOM   483  N  N     . SER   A  1 82  ? 35.93400 -91.85200  -5.61900  1.000 78.53938  ? 74  SER   A N     1 
ATOM   484  C  CA    . SER   A  1 82  ? 35.55900 -91.05800  -4.42100  1.000 80.15636  ? 74  SER   A CA    1 
ATOM   485  C  C     . SER   A  1 82  ? 34.28300 -90.26800  -4.72400  1.000 76.51958  ? 74  SER   A C     1 
ATOM   486  O  O     . SER   A  1 82  ? 34.07200 -89.92500  -5.90100  1.000 77.85778  ? 74  SER   A O     1 
ATOM   487  C  CB    . SER   A  1 82  ? 36.67800 -90.13600  -4.00900  1.000 83.08857  ? 74  SER   A CB    1 
ATOM   488  O  OG    . SER   A  1 82  ? 36.96500 -89.19800  -5.03700  1.000 80.39012  ? 74  SER   A OG    1 
ATOM   489  N  N     . GLY   A  1 83  ? 33.47500 -89.98900  -3.69800  1.000 75.25723  ? 75  GLY   A N     1 
ATOM   490  C  CA    . GLY   A  1 83  ? 32.26600 -89.14800  -3.80300  1.000 77.54886  ? 75  GLY   A CA    1 
ATOM   491  C  C     . GLY   A  1 83  ? 32.58000 -87.78800  -4.40200  1.000 76.80137  ? 75  GLY   A C     1 
ATOM   492  O  O     . GLY   A  1 83  ? 31.72100 -87.25600  -5.12800  1.000 76.35695  ? 75  GLY   A O     1 
ATOM   493  N  N     . ARG   A  1 84  ? 33.76600 -87.24800  -4.10000  1.000 82.22151  ? 76  ARG   A N     1 
ATOM   494  C  CA    . ARG   A  1 84  ? 34.28700 -85.96600  -4.64800  1.000 82.17349  ? 76  ARG   A CA    1 
ATOM   495  C  C     . ARG   A  1 84  ? 34.43500 -86.08000  -6.16900  1.000 78.06578  ? 76  ARG   A C     1 
ATOM   496  O  O     . ARG   A  1 84  ? 34.01200 -85.13900  -6.86800  1.000 77.07605  ? 76  ARG   A O     1 
ATOM   497  C  CB    . ARG   A  1 84  ? 35.62500 -85.60600  -3.99200  1.000 84.67227  ? 76  ARG   A CB    1 
ATOM   498  C  CG    . ARG   A  1 84  ? 36.45200 -84.59300  -4.77200  1.000 88.92136  ? 76  ARG   A CG    1 
ATOM   499  C  CD    . ARG   A  1 84  ? 37.60300 -84.02800  -3.96100  1.000 101.44521 ? 76  ARG   A CD    1 
ATOM   500  N  NE    . ARG   A  1 84  ? 37.20400 -82.89400  -3.13600  1.000 113.39534 ? 76  ARG   A NE    1 
ATOM   501  C  CZ    . ARG   A  1 84  ? 36.94200 -81.66900  -3.59300  1.000 115.04222 ? 76  ARG   A CZ    1 
ATOM   502  N  NH1   . ARG   A  1 84  ? 37.02200 -81.39600  -4.88600  1.000 106.73241 ? 76  ARG   A NH1   1 
ATOM   503  N  NH2   . ARG   A  1 84  ? 36.59100 -80.71600  -2.74600  1.000 116.62828 ? 76  ARG   A NH2   1 
ATOM   504  N  N     . ASP   A  1 85  ? 35.02500 -87.17900  -6.65200  1.000 78.29113  ? 77  ASP   A N     1 
ATOM   505  C  CA    . ASP   A  1 85  ? 35.26100 -87.43700  -8.09900  1.000 74.15142  ? 77  ASP   A CA    1 
ATOM   506  C  C     . ASP   A  1 85  ? 33.91200 -87.51200  -8.82400  1.000 71.76204  ? 77  ASP   A C     1 
ATOM   507  O  O     . ASP   A  1 85  ? 33.77400 -86.84300  -9.86800  1.000 72.65273  ? 77  ASP   A O     1 
ATOM   508  C  CB    . ASP   A  1 85  ? 36.10900 -88.69300  -8.32600  1.000 74.53128  ? 77  ASP   A CB    1 
ATOM   509  C  CG    . ASP   A  1 85  ? 37.59900 -88.48600  -8.10200  1.000 81.36002  ? 77  ASP   A CG    1 
ATOM   510  O  OD1   . ASP   A  1 85  ? 37.99600 -87.34800  -7.77600  1.000 81.31630  ? 77  ASP   A OD1   1 
ATOM   511  O  OD2   . ASP   A  1 85  ? 38.35400 -89.46600  -8.25800  1.000 87.72568  ? 77  ASP   A OD2   1 
ATOM   512  N  N     . TRP   A  1 86  ? 32.95500 -88.27800  -8.28800  1.000 70.79741  ? 78  TRP   A N     1 
ATOM   513  C  CA    . TRP   A  1 86  ? 31.56800 -88.36800  -8.82200  1.000 68.93026  ? 78  TRP   A CA    1 
ATOM   514  C  C     . TRP   A  1 86  ? 30.93100 -86.97200  -8.84000  1.000 72.00460  ? 78  TRP   A C     1 
ATOM   515  O  O     . TRP   A  1 86  ? 30.27100 -86.63700  -9.84400  1.000 76.75590  ? 78  TRP   A O     1 
ATOM   516  C  CB    . TRP   A  1 86  ? 30.71100 -89.34500  -8.00800  1.000 63.75354  ? 78  TRP   A CB    1 
ATOM   517  C  CG    . TRP   A  1 86  ? 31.12300 -90.78300  -8.10200  1.000 70.01518  ? 78  TRP   A CG    1 
ATOM   518  C  CD1   . TRP   A  1 86  ? 31.58700 -91.56400  -7.08400  1.000 72.02209  ? 78  TRP   A CD1   1 
ATOM   519  C  CD2   . TRP   A  1 86  ? 31.08400 -91.62700  -9.26700  1.000 71.00982  ? 78  TRP   A CD2   1 
ATOM   520  N  NE1   . TRP   A  1 86  ? 31.84300 -92.83100  -7.53200  1.000 68.81833  ? 78  TRP   A NE1   1 
ATOM   521  C  CE2   . TRP   A  1 86  ? 31.54600 -92.90000  -8.86800  1.000 73.21607  ? 78  TRP   A CE2   1 
ATOM   522  C  CE3   . TRP   A  1 86  ? 30.71100 -91.43700  -10.60300 1.000 65.19939  ? 78  TRP   A CE3   1 
ATOM   523  C  CZ2   . TRP   A  1 86  ? 31.64900 -93.96900  -9.75800  1.000 71.16656  ? 78  TRP   A CZ2   1 
ATOM   524  C  CZ3   . TRP   A  1 86  ? 30.81300 -92.49400  -11.48100 1.000 67.52602  ? 78  TRP   A CZ3   1 
ATOM   525  C  CH2   . TRP   A  1 86  ? 31.27400 -93.74200  -11.06200 1.000 67.91171  ? 78  TRP   A CH2   1 
ATOM   526  N  N     . ASN   A  1 87  ? 31.13300 -86.19600  -7.77100  1.000 69.19902  ? 79  ASN   A N     1 
ATOM   527  C  CA    . ASN   A  1 87  ? 30.49500 -84.87000  -7.54100  1.000 71.66338  ? 79  ASN   A CA    1 
ATOM   528  C  C     . ASN   A  1 87  ? 31.03700 -83.81900  -8.51800  1.000 72.20537  ? 79  ASN   A C     1 
ATOM   529  O  O     . ASN   A  1 87  ? 30.26600 -82.90300  -8.86400  1.000 76.63501  ? 79  ASN   A O     1 
ATOM   530  C  CB    . ASN   A  1 87  ? 30.69800 -84.37000  -6.10600  1.000 73.00498  ? 79  ASN   A CB    1 
ATOM   531  C  CG    . ASN   A  1 87  ? 29.63100 -84.83700  -5.13900  1.000 74.49061  ? 79  ASN   A CG    1 
ATOM   532  O  OD1   . ASN   A  1 87  ? 28.77200 -85.64400  -5.48200  1.000 69.65646  ? 79  ASN   A OD1   1 
ATOM   533  N  ND2   . ASN   A  1 87  ? 29.67500 -84.32300  -3.92100  1.000 86.72320  ? 79  ASN   A ND2   1 
ATOM   534  N  N     . THR   A  1 88  ? 32.30500 -83.92100  -8.92700  1.000 67.24927  ? 80  THR   A N     1 
ATOM   535  C  CA    . THR   A  1 88  ? 33.02800 -82.84200  -9.65500  1.000 72.06741  ? 80  THR   A CA    1 
ATOM   536  C  C     . THR   A  1 88  ? 33.36200 -83.25700  -11.09500 1.000 75.53114  ? 80  THR   A C     1 
ATOM   537  O  O     . THR   A  1 88  ? 33.19100 -82.40300  -11.98800 1.000 82.38362  ? 80  THR   A O     1 
ATOM   538  C  CB    . THR   A  1 88  ? 34.28600 -82.41800  -8.88600  1.000 75.06492  ? 80  THR   A CB    1 
ATOM   539  O  OG1   . THR   A  1 88  ? 35.11800 -83.56400  -8.71300  1.000 75.22094  ? 80  THR   A OG1   1 
ATOM   540  C  CG2   . THR   A  1 88  ? 33.96700 -81.81000  -7.53700  1.000 75.08248  ? 80  THR   A CG2   1 
ATOM   541  N  N     . LEU   A  1 89  ? 33.81500 -84.49800  -11.31800 1.000 75.86053  ? 81  LEU   A N     1 
ATOM   542  C  CA    . LEU   A  1 89  ? 34.52600 -84.91200  -12.56300 1.000 75.93381  ? 81  LEU   A CA    1 
ATOM   543  C  C     . LEU   A  1 89  ? 33.60100 -85.63600  -13.55200 1.000 69.59043  ? 81  LEU   A C     1 
ATOM   544  O  O     . LEU   A  1 89  ? 33.92800 -85.61300  -14.74900 1.000 70.67157  ? 81  LEU   A O     1 
ATOM   545  C  CB    . LEU   A  1 89  ? 35.70800 -85.81500  -12.19100 1.000 73.45027  ? 81  LEU   A CB    1 
ATOM   546  C  CG    . LEU   A  1 89  ? 36.62400 -85.30400  -11.07900 1.000 73.33096  ? 81  LEU   A CG    1 
ATOM   547  C  CD1   . LEU   A  1 89  ? 37.81400 -86.23200  -10.89600 1.000 72.44368  ? 81  LEU   A CD1   1 
ATOM   548  C  CD2   . LEU   A  1 89  ? 37.09900 -83.88400  -11.35400 1.000 74.50755  ? 81  LEU   A CD2   1 
ATOM   549  N  N     . ILE   A  1 90  ? 32.52100 -86.27500  -13.09300 1.000 68.98629  ? 82  ILE   A N     1 
ATOM   550  C  CA    . ILE   A  1 90  ? 31.72800 -87.23900  -13.91700 1.000 63.75604  ? 82  ILE   A CA    1 
ATOM   551  C  C     . ILE   A  1 90  ? 30.38400 -86.61700  -14.31400 1.000 64.19702  ? 82  ILE   A C     1 
ATOM   552  O  O     . ILE   A  1 90  ? 29.60400 -86.27400  -13.41300 1.000 68.21667  ? 82  ILE   A O     1 
ATOM   553  C  CB    . ILE   A  1 90  ? 31.53700 -88.57200  -13.16600 1.000 66.26048  ? 82  ILE   A CB    1 
ATOM   554  C  CG1   . ILE   A  1 90  ? 32.87200 -89.15100  -12.68600 1.000 70.71577  ? 82  ILE   A CG1   1 
ATOM   555  C  CG2   . ILE   A  1 90  ? 30.76300 -89.56900  -14.01600 1.000 56.99472  ? 82  ILE   A CG2   1 
ATOM   556  C  CD1   . ILE   A  1 90  ? 33.88700 -89.38500  -13.78700 1.000 70.08254  ? 82  ILE   A CD1   1 
ATOM   557  N  N     . VAL   A  1 91  ? 30.13900 -86.49800  -15.62300 1.000 65.23377  ? 83  VAL   A N     1 
ATOM   558  C  CA    . VAL   A  1 91  ? 28.80600 -86.20000  -16.22600 1.000 63.86667  ? 83  VAL   A CA    1 
ATOM   559  C  C     . VAL   A  1 91  ? 28.25500 -87.51400  -16.78800 1.000 60.90673  ? 83  VAL   A C     1 
ATOM   560  O  O     . VAL   A  1 91  ? 28.95500 -88.14700  -17.59800 1.000 57.34562  ? 83  VAL   A O     1 
ATOM   561  C  CB    . VAL   A  1 91  ? 28.89800 -85.11400  -17.31600 1.000 63.67797  ? 83  VAL   A CB    1 
ATOM   562  C  CG1   . VAL   A  1 91  ? 27.57500 -84.91500  -18.04300 1.000 60.81029  ? 83  VAL   A CG1   1 
ATOM   563  C  CG2   . VAL   A  1 91  ? 29.39600 -83.79200  -16.75300 1.000 62.83693  ? 83  VAL   A CG2   1 
ATOM   564  N  N     . GLY   A  1 92  ? 27.05100 -87.90600  -16.36400 1.000 59.73287  ? 84  GLY   A N     1 
ATOM   565  C  CA    . GLY   A  1 92  ? 26.37400 -89.12800  -16.83700 1.000 60.34683  ? 84  GLY   A CA    1 
ATOM   566  C  C     . GLY   A  1 92  ? 25.87600 -88.97800  -18.26400 1.000 58.82964  ? 84  GLY   A C     1 
ATOM   567  O  O     . GLY   A  1 92  ? 25.75600 -87.82800  -18.73300 1.000 62.77259  ? 84  GLY   A O     1 
ATOM   568  N  N     . LYS   A  1 93  ? 25.59900 -90.09900  -18.93400 1.000 60.93464  ? 85  LYS   A N     1 
ATOM   569  C  CA    . LYS   A  1 93  ? 25.04200 -90.14300  -20.31200 1.000 57.10510  ? 85  LYS   A CA    1 
ATOM   570  C  C     . LYS   A  1 93  ? 23.98400 -91.24600  -20.39700 1.000 55.00444  ? 85  LYS   A C     1 
ATOM   571  O  O     . LYS   A  1 93  ? 24.31700 -92.40200  -20.07800 1.000 57.34528  ? 85  LYS   A O     1 
ATOM   572  C  CB    . LYS   A  1 93  ? 26.15300 -90.40900  -21.33000 1.000 57.95387  ? 85  LYS   A CB    1 
ATOM   573  C  CG    . LYS   A  1 93  ? 27.14900 -89.27300  -21.52300 1.000 59.71577  ? 85  LYS   A CG    1 
ATOM   574  C  CD    . LYS   A  1 93  ? 28.21000 -89.58600  -22.55800 1.000 59.18713  ? 85  LYS   A CD    1 
ATOM   575  C  CE    . LYS   A  1 93  ? 27.67600 -89.60200  -23.97600 1.000 64.62396  ? 85  LYS   A CE    1 
ATOM   576  N  NZ    . LYS   A  1 93  ? 28.39600 -90.58600  -24.81800 1.000 69.14452  ? 85  LYS   A NZ    1 
ATOM   577  N  N     . LEU   A  1 94  ? 22.76200 -90.89800  -20.81200 1.000 51.80234  ? 86  LEU   A N     1 
ATOM   578  C  CA    . LEU   A  1 94  ? 21.66800 -91.87600  -21.05500 1.000 55.32840  ? 86  LEU   A CA    1 
ATOM   579  C  C     . LEU   A  1 94  ? 22.13000 -92.86200  -22.13400 1.000 57.18217  ? 86  LEU   A C     1 
ATOM   580  O  O     . LEU   A  1 94  ? 22.52000 -92.40700  -23.22800 1.000 59.66547  ? 86  LEU   A O     1 
ATOM   581  C  CB    . LEU   A  1 94  ? 20.39500 -91.14400  -21.49200 1.000 48.54339  ? 86  LEU   A CB    1 
ATOM   582  C  CG    . LEU   A  1 94  ? 19.16500 -92.03400  -21.67900 1.000 54.20370  ? 86  LEU   A CG    1 
ATOM   583  C  CD1   . LEU   A  1 94  ? 18.64200 -92.53000  -20.33700 1.000 57.55749  ? 86  LEU   A CD1   1 
ATOM   584  C  CD2   . LEU   A  1 94  ? 18.07000 -91.29800  -22.43600 1.000 54.55263  ? 86  LEU   A CD2   1 
ATOM   585  N  N     . SER   A  1 95  ? 22.09700 -94.16100  -21.83000 1.000 53.92305  ? 87  SER   A N     1 
ATOM   586  C  CA    . SER   A  1 95  ? 22.46100 -95.25100  -22.77000 1.000 57.57103  ? 87  SER   A CA    1 
ATOM   587  C  C     . SER   A  1 95  ? 21.71100 -95.03600  -24.08500 1.000 63.00863  ? 87  SER   A C     1 
ATOM   588  O  O     . SER   A  1 95  ? 20.50700 -94.77900  -24.07900 1.000 60.06497  ? 87  SER   A O     1 
ATOM   589  C  CB    . SER   A  1 95  ? 22.18200 -96.60200  -22.16700 1.000 52.81202  ? 87  SER   A CB    1 
ATOM   590  O  OG    . SER   A  1 95  ? 23.07100 -96.86400  -21.09100 1.000 57.83787  ? 87  SER   A OG    1 
ATOM   591  N  N     . PRO   A  1 96  ? 22.39900 -95.10200  -25.24900 1.000 56.78476  ? 88  PRO   A N     1 
ATOM   592  C  CA    . PRO   A  1 96  ? 21.78600 -94.72500  -26.52200 1.000 54.19452  ? 88  PRO   A CA    1 
ATOM   593  C  C     . PRO   A  1 96  ? 20.61900 -95.62800  -26.95500 1.000 56.41678  ? 88  PRO   A C     1 
ATOM   594  O  O     . PRO   A  1 96  ? 19.80400 -95.16700  -27.72900 1.000 62.78534  ? 88  PRO   A O     1 
ATOM   595  C  CB    . PRO   A  1 96  ? 22.94800 -94.79600  -27.52500 1.000 54.28379  ? 88  PRO   A CB    1 
ATOM   596  C  CG    . PRO   A  1 96  ? 23.95700 -95.72400  -26.88900 1.000 57.86023  ? 88  PRO   A CG    1 
ATOM   597  C  CD    . PRO   A  1 96  ? 23.80000 -95.52400  -25.39800 1.000 57.03152  ? 88  PRO   A CD    1 
ATOM   598  N  N     . TRP   A  1 97  ? 20.54700 -96.86300  -26.44700 1.000 57.03091  ? 89  TRP   A N     1 
ATOM   599  C  CA    . TRP   A  1 97  ? 19.45800 -97.82900  -26.76300 1.000 57.33670  ? 89  TRP   A CA    1 
ATOM   600  C  C     . TRP   A  1 97  ? 18.12900 -97.37300  -26.14400 1.000 59.21378  ? 89  TRP   A C     1 
ATOM   601  O  O     . TRP   A  1 97  ? 17.07700 -97.79600  -26.65400 1.000 57.10353  ? 89  TRP   A O     1 
ATOM   602  C  CB    . TRP   A  1 97  ? 19.82700 -99.25300  -26.32500 1.000 55.36741  ? 89  TRP   A CB    1 
ATOM   603  C  CG    . TRP   A  1 97  ? 19.98000 -99.46600  -24.84900 1.000 59.51731  ? 89  TRP   A CG    1 
ATOM   604  C  CD1   . TRP   A  1 97  ? 21.13700 -99.40100  -24.12900 1.000 60.93529  ? 89  TRP   A CD1   1 
ATOM   605  C  CD2   . TRP   A  1 97  ? 18.95200 -99.83800  -23.91100 1.000 63.97861  ? 89  TRP   A CD2   1 
ATOM   606  N  NE1   . TRP   A  1 97  ? 20.90100 -99.68500  -22.81000 1.000 65.84872  ? 89  TRP   A NE1   1 
ATOM   607  C  CE2   . TRP   A  1 97  ? 19.56900 -99.95600  -22.64600 1.000 64.69709  ? 89  TRP   A CE2   1 
ATOM   608  C  CE3   . TRP   A  1 97  ? 17.57500 -100.07100 -24.01300 1.000 61.30357  ? 89  TRP   A CE3   1 
ATOM   609  C  CZ2   . TRP   A  1 97  ? 18.85700 -100.30100 -21.49800 1.000 62.20474  ? 89  TRP   A CZ2   1 
ATOM   610  C  CZ3   . TRP   A  1 97  ? 16.87200 -100.41000 -22.87700 1.000 63.81282  ? 89  TRP   A CZ3   1 
ATOM   611  C  CH2   . TRP   A  1 97  ? 17.50600 -100.52400 -21.63900 1.000 60.72257  ? 89  TRP   A CH2   1 
ATOM   612  N  N     . ILE   A  1 98  ? 18.17300 -96.54200  -25.09500 1.000 57.48682  ? 90  ILE   A N     1 
ATOM   613  C  CA    . ILE   A  1 98  ? 16.96900 -96.09000  -24.33400 1.000 55.28395  ? 90  ILE   A CA    1 
ATOM   614  C  C     . ILE   A  1 98  ? 16.18500 -95.10800  -25.21300 1.000 58.44528  ? 90  ILE   A C     1 
ATOM   615  O  O     . ILE   A  1 98  ? 16.68400 -93.98500  -25.44700 1.000 60.10714  ? 90  ILE   A O     1 
ATOM   616  C  CB    . ILE   A  1 98  ? 17.36000 -95.48800  -22.96700 1.000 58.61535  ? 90  ILE   A CB    1 
ATOM   617  C  CG1   . ILE   A  1 98  ? 18.15600 -96.49100  -22.12500 1.000 57.28936  ? 90  ILE   A CG1   1 
ATOM   618  C  CG2   . ILE   A  1 98  ? 16.12600 -94.98500  -22.22900 1.000 54.28861  ? 90  ILE   A CG2   1 
ATOM   619  C  CD1   . ILE   A  1 98  ? 18.70800 -95.93100  -20.83400 1.000 54.32672  ? 90  ILE   A CD1   1 
ATOM   620  N  N     . ARG   A  1 99  ? 15.01300 -95.53800  -25.69000 1.000 55.03295  ? 91  ARG   A N     1 
ATOM   621  C  CA    . ARG   A  1 99  ? 14.13400 -94.78500  -26.62700 1.000 56.91302  ? 91  ARG   A CA    1 
ATOM   622  C  C     . ARG   A  1 99  ? 12.71200 -94.78300  -26.07200 1.000 50.81139  ? 91  ARG   A C     1 
ATOM   623  O  O     . ARG   A  1 99  ? 11.90400 -95.64000  -26.42300 1.000 51.90244  ? 91  ARG   A O     1 
ATOM   624  C  CB    . ARG   A  1 99  ? 14.18600 -95.42100  -28.02200 1.000 53.18799  ? 91  ARG   A CB    1 
ATOM   625  C  CG    . ARG   A  1 99  ? 15.53000 -95.29900  -28.72600 1.000 51.94611  ? 91  ARG   A CG    1 
ATOM   626  C  CD    . ARG   A  1 99  ? 15.66100 -96.28700  -29.87800 1.000 79.45826  ? 91  ARG   A CD    1 
ATOM   627  N  NE    . ARG   A  1 99  ? 14.53800 -96.22000  -30.81400 1.000 82.34938  ? 91  ARG   A NE    1 
ATOM   628  C  CZ    . ARG   A  1 99  ? 14.46500 -95.43300  -31.88900 1.000 78.24530  ? 91  ARG   A CZ    1 
ATOM   629  N  NH1   . ARG   A  1 99  ? 15.46600 -94.62700  -32.21100 1.000 76.64316  ? 91  ARG   A NH1   1 
ATOM   630  N  NH2   . ARG   A  1 99  ? 13.38000 -95.45700  -32.64500 1.000 75.98069  ? 91  ARG   A NH2   1 
ATOM   631  N  N     . PRO   A  1 100 ? 12.36200 -93.83600  -25.17400 1.000 51.70074  ? 92  PRO   A N     1 
ATOM   632  C  CA    . PRO   A  1 100 ? 11.02500 -93.79200  -24.58100 1.000 55.32555  ? 92  PRO   A CA    1 
ATOM   633  C  C     . PRO   A  1 100 ? 9.89600  -93.43200  -25.56000 1.000 52.90000  ? 92  PRO   A C     1 
ATOM   634  O  O     . PRO   A  1 100 ? 8.74900  -93.62400  -25.20400 1.000 51.69182  ? 92  PRO   A O     1 
ATOM   635  C  CB    . PRO   A  1 100 ? 11.13200 -92.69800  -23.50700 1.000 55.22626  ? 92  PRO   A CB    1 
ATOM   636  C  CG    . PRO   A  1 100 ? 12.61900 -92.53100  -23.27900 1.000 55.91602  ? 92  PRO   A CG    1 
ATOM   637  C  CD    . PRO   A  1 100 ? 13.24400 -92.79400  -24.63100 1.000 51.87709  ? 92  PRO   A CD    1 
ATOM   638  N  N     . ASP   A  1 101 ? 10.23800 -92.92000  -26.74700 1.000 55.26864  ? 93  ASP   A N     1 
ATOM   639  C  CA    . ASP   A  1 101 ? 9.26000  -92.49300  -27.78400 1.000 53.25342  ? 93  ASP   A CA    1 
ATOM   640  C  C     . ASP   A  1 101 ? 9.31200  -93.43500  -28.99000 1.000 52.53857  ? 93  ASP   A C     1 
ATOM   641  O  O     . ASP   A  1 101 ? 8.79400  -93.04800  -30.04900 1.000 59.24666  ? 93  ASP   A O     1 
ATOM   642  C  CB    . ASP   A  1 101 ? 9.50300  -91.03700  -28.17400 1.000 53.23540  ? 93  ASP   A CB    1 
ATOM   643  C  CG    . ASP   A  1 101 ? 9.09000  -90.08400  -27.07500 1.000 55.25315  ? 93  ASP   A CG    1 
ATOM   644  O  OD1   . ASP   A  1 101 ? 7.87000  -89.90800  -26.89100 1.000 54.89916  ? 93  ASP   A OD1   1 
ATOM   645  O  OD2   . ASP   A  1 101 ? 9.98800  -89.56100  -26.39100 1.000 56.42865  ? 93  ASP   A OD2   1 
ATOM   646  N  N     . SER   A  1 102 ? 9.86900  -94.63800  -28.82600 1.000 53.70842  ? 94  SER   A N     1 
ATOM   647  C  CA    . SER   A  1 102 ? 9.80800  -95.72900  -29.83300 1.000 59.14568  ? 94  SER   A CA    1 
ATOM   648  C  C     . SER   A  1 102 ? 8.34500  -95.98000  -30.21900 1.000 59.99712  ? 94  SER   A C     1 
ATOM   649  O  O     . SER   A  1 102 ? 7.45500  -95.69700  -29.39500 1.000 61.27532  ? 94  SER   A O     1 
ATOM   650  C  CB    . SER   A  1 102 ? 10.46300 -96.99100  -29.33000 1.000 61.38783  ? 94  SER   A CB    1 
ATOM   651  O  OG    . SER   A  1 102 ? 10.34200 -98.04000  -30.28400 1.000 62.39194  ? 94  SER   A OG    1 
ATOM   652  N  N     . LYS   A  1 103 ? 8.11600  -96.48100  -31.43300 1.000 60.33156  ? 95  LYS   A N     1 
ATOM   653  C  CA    . LYS   A  1 103 ? 6.76700  -96.80900  -31.96400 1.000 62.96222  ? 95  LYS   A CA    1 
ATOM   654  C  C     . LYS   A  1 103 ? 6.30600  -98.15200  -31.38600 1.000 62.68907  ? 95  LYS   A C     1 
ATOM   655  O  O     . LYS   A  1 103 ? 5.09600  -98.44200  -31.47200 1.000 64.03546  ? 95  LYS   A O     1 
ATOM   656  C  CB    . LYS   A  1 103 ? 6.79900  -96.84200  -33.49500 1.000 69.07491  ? 95  LYS   A CB    1 
ATOM   657  C  CG    . LYS   A  1 103 ? 7.16200  -95.52300  -34.16500 1.000 66.79155  ? 95  LYS   A CG    1 
ATOM   658  C  CD    . LYS   A  1 103 ? 6.08500  -94.46200  -34.04300 1.000 67.31486  ? 95  LYS   A CD    1 
ATOM   659  C  CE    . LYS   A  1 103 ? 6.26800  -93.31000  -35.01100 1.000 72.80965  ? 95  LYS   A CE    1 
ATOM   660  N  NZ    . LYS   A  1 103 ? 5.97000  -93.70500  -36.41000 1.000 73.33620  ? 95  LYS   A NZ    1 
ATOM   661  N  N     . VAL   A  1 104 ? 7.23400  -98.93000  -30.81600 1.000 64.34143  ? 96  VAL   A N     1 
ATOM   662  C  CA    . VAL   A  1 104 ? 6.97000  -100.27400 -30.21900 1.000 70.39813  ? 96  VAL   A CA    1 
ATOM   663  C  C     . VAL   A  1 104 ? 6.63400  -100.08300 -28.73600 1.000 64.87086  ? 96  VAL   A C     1 
ATOM   664  O  O     . VAL   A  1 104 ? 7.48500  -99.53100  -28.01500 1.000 64.45214  ? 96  VAL   A O     1 
ATOM   665  C  CB    . VAL   A  1 104 ? 8.16800  -101.23100 -30.39700 1.000 70.07490  ? 96  VAL   A CB    1 
ATOM   666  C  CG1   . VAL   A  1 104 ? 7.78800  -102.67100 -30.08700 1.000 68.74280  ? 96  VAL   A CG1   1 
ATOM   667  C  CG2   . VAL   A  1 104 ? 8.78300  -101.13900 -31.78600 1.000 65.62957  ? 96  VAL   A CG2   1 
ATOM   668  N  N     . GLU   A  1 105 ? 5.44500  -100.52700 -28.31200 1.000 67.84396  ? 97  GLU   A N     1 
ATOM   669  C  CA    . GLU   A  1 105 ? 4.96000  -100.46500 -26.90300 1.000 69.86767  ? 97  GLU   A CA    1 
ATOM   670  C  C     . GLU   A  1 105 ? 6.02100  -101.06500 -25.97100 1.000 63.44923  ? 97  GLU   A C     1 
ATOM   671  O  O     . GLU   A  1 105 ? 6.35800  -100.40700 -24.97400 1.000 69.10673  ? 97  GLU   A O     1 
ATOM   672  C  CB    . GLU   A  1 105 ? 3.61000  -101.17900 -26.77000 1.000 72.57264  ? 97  GLU   A CB    1 
ATOM   673  C  CG    . GLU   A  1 105 ? 3.11900  -101.32700 -25.33600 1.000 67.43266  ? 97  GLU   A CG    1 
ATOM   674  C  CD    . GLU   A  1 105 ? 1.61200  -101.46200 -25.17000 1.000 73.43339  ? 97  GLU   A CD    1 
ATOM   675  O  OE1   . GLU   A  1 105 ? 0.93100  -101.80300 -26.15500 1.000 75.31784  ? 97  GLU   A OE1   1 
ATOM   676  O  OE2   . GLU   A  1 105 ? 1.12000  -101.22300 -24.05100 1.000 72.79967  ? 97  GLU   A OE2   1 
ATOM   677  N  N     . LYS   A  1 106 ? 6.54400  -102.24800 -26.30600 1.000 62.23681  ? 98  LYS   A N     1 
ATOM   678  C  CA    . LYS   A  1 106 ? 7.51500  -103.00800 -25.47100 1.000 67.35613  ? 98  LYS   A CA    1 
ATOM   679  C  C     . LYS   A  1 106 ? 8.79200  -102.18100 -25.26900 1.000 66.65351  ? 98  LYS   A C     1 
ATOM   680  O  O     . LYS   A  1 106 ? 9.27100  -102.11700 -24.11800 1.000 67.18753  ? 98  LYS   A O     1 
ATOM   681  C  CB    . LYS   A  1 106 ? 7.83900  -104.36300 -26.11100 1.000 78.54672  ? 98  LYS   A CB    1 
ATOM   682  C  CG    . LYS   A  1 106 ? 6.64900  -105.30000 -26.28200 1.000 82.05092  ? 98  LYS   A CG    1 
ATOM   683  C  CD    . LYS   A  1 106 ? 7.03800  -106.74900 -26.49000 1.000 84.64069  ? 98  LYS   A CD    1 
ATOM   684  C  CE    . LYS   A  1 106 ? 5.84000  -107.66800 -26.60700 1.000 88.19592  ? 98  LYS   A CE    1 
ATOM   685  N  NZ    . LYS   A  1 106 ? 6.24500  -109.09400 -26.62200 1.000 87.22055  ? 98  LYS   A NZ    1 
ATOM   686  N  N     . ILE   A  1 107 ? 9.32200  -101.57900 -26.34000 1.000 65.08104  ? 99  ILE   A N     1 
ATOM   687  C  CA    . ILE   A  1 107 ? 10.59600 -100.79600 -26.32000 1.000 62.42523  ? 99  ILE   A CA    1 
ATOM   688  C  C     . ILE   A  1 107 ? 10.37400 -99.51000  -25.51700 1.000 62.88930  ? 99  ILE   A C     1 
ATOM   689  O  O     . ILE   A  1 107 ? 11.33700 -99.05000  -24.87600 1.000 65.12738  ? 99  ILE   A O     1 
ATOM   690  C  CB    . ILE   A  1 107 ? 11.11400 -100.51200 -27.74600 1.000 63.53251  ? 99  ILE   A CB    1 
ATOM   691  C  CG1   . ILE   A  1 107 ? 11.52900 -101.80800 -28.45200 1.000 63.80736  ? 99  ILE   A CG1   1 
ATOM   692  C  CG2   . ILE   A  1 107 ? 12.24500 -99.48900  -27.71900 1.000 61.49267  ? 99  ILE   A CG2   1 
ATOM   693  C  CD1   . ILE   A  1 107 ? 12.11100 -101.62200 -29.84000 1.000 61.89657  ? 99  ILE   A CD1   1 
ATOM   694  N  N     . ARG   A  1 108 ? 9.16100  -98.95100  -25.56200 1.000 64.49618  ? 100 ARG   A N     1 
ATOM   695  C  CA    . ARG   A  1 108 ? 8.76800  -97.76700  -24.75200 1.000 60.20065  ? 100 ARG   A CA    1 
ATOM   696  C  C     . ARG   A  1 108 ? 8.87100  -98.13100  -23.26800 1.000 65.27387  ? 100 ARG   A C     1 
ATOM   697  O  O     . ARG   A  1 108 ? 9.59600  -97.42400  -22.54300 1.000 67.13058  ? 100 ARG   A O     1 
ATOM   698  C  CB    . ARG   A  1 108 ? 7.35500  -97.29100  -25.10400 1.000 65.17319  ? 100 ARG   A CB    1 
ATOM   699  C  CG    . ARG   A  1 108 ? 7.32500  -96.24100  -26.20400 1.000 65.41075  ? 100 ARG   A CG    1 
ATOM   700  C  CD    . ARG   A  1 108 ? 5.94100  -95.68800  -26.48900 1.000 67.71660  ? 100 ARG   A CD    1 
ATOM   701  N  NE    . ARG   A  1 108 ? 5.34600  -96.30900  -27.66800 1.000 71.88263  ? 100 ARG   A NE    1 
ATOM   702  C  CZ    . ARG   A  1 108 ? 4.10000  -96.77100  -27.76000 1.000 76.85757  ? 100 ARG   A CZ    1 
ATOM   703  N  NH1   . ARG   A  1 108 ? 3.26000  -96.68000  -26.74200 1.000 72.85915  ? 100 ARG   A NH1   1 
ATOM   704  N  NH2   . ARG   A  1 108 ? 3.68900  -97.31700  -28.89300 1.000 84.09828  ? 100 ARG   A NH2   1 
ATOM   705  N  N     . ARG   A  1 109 ? 8.19200  -99.20800  -22.85900 1.000 66.69578  ? 101 ARG   A N     1 
ATOM   706  C  CA    . ARG   A  1 109 ? 8.08700  -99.66000  -21.44400 1.000 61.95771  ? 101 ARG   A CA    1 
ATOM   707  C  C     . ARG   A  1 109 ? 9.48300  -99.97800  -20.90200 1.000 59.39365  ? 101 ARG   A C     1 
ATOM   708  O  O     . ARG   A  1 109 ? 9.79700  -99.50100  -19.79900 1.000 63.17604  ? 101 ARG   A O     1 
ATOM   709  C  CB    . ARG   A  1 109 ? 7.12400  -100.84500 -21.33200 1.000 61.70016  ? 101 ARG   A CB    1 
ATOM   710  C  CG    . ARG   A  1 109 ? 5.67000  -100.44900 -21.54300 1.000 64.95420  ? 101 ARG   A CG    1 
ATOM   711  C  CD    . ARG   A  1 109 ? 4.67200  -101.57200 -21.34800 1.000 63.45123  ? 101 ARG   A CD    1 
ATOM   712  N  NE    . ARG   A  1 109 ? 3.31900  -101.06500 -21.53600 1.000 71.12789  ? 101 ARG   A NE    1 
ATOM   713  C  CZ    . ARG   A  1 109 ? 2.63400  -100.35300 -20.64100 1.000 76.17166  ? 101 ARG   A CZ    1 
ATOM   714  N  NH1   . ARG   A  1 109 ? 3.15800  -100.05900 -19.46000 1.000 72.95065  ? 101 ARG   A NH1   1 
ATOM   715  N  NH2   . ARG   A  1 109 ? 1.41500  -99.93300  -20.93400 1.000 77.93057  ? 101 ARG   A NH2   1 
ATOM   716  N  N     . ASN   A  1 110 ? 10.29400 -100.72500 -21.65500 1.000 58.79798  ? 102 ASN   A N     1 
ATOM   717  C  CA    . ASN   A  1 110 ? 11.69600 -101.04300 -21.27500 1.000 59.86559  ? 102 ASN   A CA    1 
ATOM   718  C  C     . ASN   A  1 110 ? 12.47200 -99.73300  -21.10200 1.000 60.77468  ? 102 ASN   A C     1 
ATOM   719  O  O     . ASN   A  1 110 ? 13.11800 -99.57200  -20.04900 1.000 63.16116  ? 102 ASN   A O     1 
ATOM   720  C  CB    . ASN   A  1 110 ? 12.37100 -101.97600 -22.28300 1.000 58.61723  ? 102 ASN   A CB    1 
ATOM   721  C  CG    . ASN   A  1 110 ? 11.95100 -103.42000 -22.11200 1.000 72.39703  ? 102 ASN   A CG    1 
ATOM   722  O  OD1   . ASN   A  1 110 ? 11.75300 -103.88200 -20.98900 1.000 72.11382  ? 102 ASN   A OD1   1 
ATOM   723  N  ND2   . ASN   A  1 110 ? 11.81900 -104.14100 -23.21500 1.000 77.53315  ? 102 ASN   A ND2   1 
ATOM   724  N  N     . SER   A  1 111 ? 12.37800 -98.83000  -22.08300 1.000 61.60392  ? 103 SER   A N     1 
ATOM   725  C  CA    . SER   A  1 111 ? 13.07500 -97.51600  -22.11700 1.000 60.60050  ? 103 SER   A CA    1 
ATOM   726  C  C     . SER   A  1 111 ? 12.64800 -96.64200  -20.92700 1.000 60.08155  ? 103 SER   A C     1 
ATOM   727  O  O     . SER   A  1 111 ? 13.52300 -95.95700  -20.36400 1.000 57.85864  ? 103 SER   A O     1 
ATOM   728  C  CB    . SER   A  1 111 ? 12.83500 -96.81400  -23.42700 1.000 58.81515  ? 103 SER   A CB    1 
ATOM   729  O  OG    . SER   A  1 111 ? 13.41300 -97.54000  -24.50400 1.000 59.59536  ? 103 SER   A OG    1 
ATOM   730  N  N     . GLU   A  1 112 ? 11.35800 -96.66100  -20.57000 1.000 60.33890  ? 104 GLU   A N     1 
ATOM   731  C  CA    . GLU   A  1 112 ? 10.79800 -95.94700  -19.39000 1.000 59.46783  ? 104 GLU   A CA    1 
ATOM   732  C  C     . GLU   A  1 112 ? 11.52000 -96.42600  -18.12600 1.000 60.84057  ? 104 GLU   A C     1 
ATOM   733  O  O     . GLU   A  1 112 ? 12.15800 -95.58900  -17.45700 1.000 62.63947  ? 104 GLU   A O     1 
ATOM   734  C  CB    . GLU   A  1 112 ? 9.29200  -96.19100  -19.25500 1.000 65.29486  ? 104 GLU   A CB    1 
ATOM   735  C  CG    . GLU   A  1 112 ? 8.44800  -95.38900  -20.23100 1.000 70.61939  ? 104 GLU   A CG    1 
ATOM   736  C  CD    . GLU   A  1 112 ? 6.96600  -95.72900  -20.20600 1.000 75.64321  ? 104 GLU   A CD    1 
ATOM   737  O  OE1   . GLU   A  1 112 ? 6.45500  -96.06900  -19.11600 1.000 81.70972  ? 104 GLU   A OE1   1 
ATOM   738  O  OE2   . GLU   A  1 112 ? 6.32500  -95.65800  -21.27600 1.000 72.84119  ? 104 GLU   A OE2   1 
ATOM   739  N  N     . ALA   A  1 113 ? 11.41900 -97.72600  -17.82900 1.000 60.05844  ? 105 ALA   A N     1 
ATOM   740  C  CA    . ALA   A  1 113 ? 12.04100 -98.39200  -16.65900 1.000 58.01586  ? 105 ALA   A CA    1 
ATOM   741  C  C     . ALA   A  1 113 ? 13.56100 -98.18200  -16.68200 1.000 59.68177  ? 105 ALA   A C     1 
ATOM   742  O  O     . ALA   A  1 113 ? 14.13800 -97.93900  -15.60300 1.000 63.28381  ? 105 ALA   A O     1 
ATOM   743  C  CB    . ALA   A  1 113 ? 11.69000 -99.86100  -16.65200 1.000 58.45007  ? 105 ALA   A CB    1 
ATOM   744  N  N     . ALA   A  1 114 ? 14.17700 -98.27100  -17.86600 1.000 59.63560  ? 106 ALA   A N     1 
ATOM   745  C  CA    . ALA   A  1 114 ? 15.63800 -98.14400  -18.08200 1.000 61.01768  ? 106 ALA   A CA    1 
ATOM   746  C  C     . ALA   A  1 114 ? 16.09500 -96.70900  -17.79800 1.000 59.18516  ? 106 ALA   A C     1 
ATOM   747  O  O     . ALA   A  1 114 ? 17.16800 -96.54000  -17.18500 1.000 53.18192  ? 106 ALA   A O     1 
ATOM   748  C  CB    . ALA   A  1 114 ? 15.98800 -98.55300  -19.48900 1.000 54.53166  ? 106 ALA   A CB    1 
ATOM   749  N  N     . MET   A  1 115 ? 15.31700 -95.71800  -18.24600 1.000 58.74549  ? 107 MET   A N     1 
ATOM   750  C  CA    . MET   A  1 115 ? 15.65300 -94.27500  -18.11400 1.000 56.52491  ? 107 MET   A CA    1 
ATOM   751  C  C     . MET   A  1 115 ? 15.64200 -93.89700  -16.62700 1.000 58.98367  ? 107 MET   A C     1 
ATOM   752  O  O     . MET   A  1 115 ? 16.64700 -93.32100  -16.16400 1.000 57.58365  ? 107 MET   A O     1 
ATOM   753  C  CB    . MET   A  1 115 ? 14.66500 -93.39900  -18.89000 1.000 53.26171  ? 107 MET   A CB    1 
ATOM   754  C  CG    . MET   A  1 115 ? 15.08400 -91.94600  -18.97300 1.000 53.77288  ? 107 MET   A CG    1 
ATOM   755  S  SD    . MET   A  1 115 ? 13.94500 -90.93900  -19.95200 1.000 48.25054  ? 107 MET   A SD    1 
ATOM   756  C  CE    . MET   A  1 115 ? 14.12600 -89.36600  -19.11400 1.000 48.98055  ? 107 MET   A CE    1 
ATOM   757  N  N     . LEU   A  1 116 ? 14.56200 -94.23200  -15.91000 1.000 55.97653  ? 108 LEU   A N     1 
ATOM   758  C  CA    . LEU   A  1 116 ? 14.43100 -94.01000  -14.44000 1.000 56.96142  ? 108 LEU   A CA    1 
ATOM   759  C  C     . LEU   A  1 116 ? 15.63200 -94.64200  -13.72400 1.000 58.16648  ? 108 LEU   A C     1 
ATOM   760  O  O     . LEU   A  1 116 ? 16.20300 -93.97600  -12.85000 1.000 59.82249  ? 108 LEU   A O     1 
ATOM   761  C  CB    . LEU   A  1 116 ? 13.11600 -94.61100  -13.93000 1.000 54.93230  ? 108 LEU   A CB    1 
ATOM   762  C  CG    . LEU   A  1 116 ? 11.83500 -93.93200  -14.41300 1.000 59.40517  ? 108 LEU   A CG    1 
ATOM   763  C  CD1   . LEU   A  1 116 ? 10.61100 -94.71400  -13.96100 1.000 61.94489  ? 108 LEU   A CD1   1 
ATOM   764  C  CD2   . LEU   A  1 116 ? 11.75200 -92.49100  -13.92700 1.000 58.72536  ? 108 LEU   A CD2   1 
ATOM   765  N  N     . GLN   A  1 117 ? 16.00300 -95.86800  -14.10600 1.000 55.06190  ? 109 GLN   A N     1 
ATOM   766  C  CA    . GLN   A  1 117 ? 17.15000 -96.62500  -13.53800 1.000 56.22723  ? 109 GLN   A CA    1 
ATOM   767  C  C     . GLN   A  1 117 ? 18.44700 -95.82500  -13.71600 1.000 55.26603  ? 109 GLN   A C     1 
ATOM   768  O  O     . GLN   A  1 117 ? 19.19800 -95.70600  -12.73600 1.000 62.01583  ? 109 GLN   A O     1 
ATOM   769  C  CB    . GLN   A  1 117 ? 17.26500 -97.99600  -14.20600 1.000 59.16988  ? 109 GLN   A CB    1 
ATOM   770  C  CG    . GLN   A  1 117 ? 18.33400 -98.89000  -13.59600 1.000 58.66788  ? 109 GLN   A CG    1 
ATOM   771  C  CD    . GLN   A  1 117 ? 18.63600 -100.08700 -14.46300 1.000 66.38502  ? 109 GLN   A CD    1 
ATOM   772  O  OE1   . GLN   A  1 117 ? 19.69900 -100.18500 -15.07000 1.000 70.32463  ? 109 GLN   A OE1   1 
ATOM   773  N  NE2   . GLN   A  1 117 ? 17.69300 -101.01000 -14.53700 1.000 65.33702  ? 109 GLN   A NE2   1 
ATOM   774  N  N     . GLU   A  1 118 ? 18.70800 -95.31100  -14.92000 1.000 58.06910  ? 110 GLU   A N     1 
ATOM   775  C  CA    . GLU   A  1 118 ? 19.97000 -94.59100  -15.25500 1.000 58.79540  ? 110 GLU   A CA    1 
ATOM   776  C  C     . GLU   A  1 118 ? 19.97800 -93.21800  -14.56600 1.000 61.47443  ? 110 GLU   A C     1 
ATOM   777  O  O     . GLU   A  1 118 ? 21.04200 -92.83200  -14.03900 1.000 65.62488  ? 110 GLU   A O     1 
ATOM   778  C  CB    . GLU   A  1 118 ? 20.14600 -94.47000  -16.77000 1.000 51.78306  ? 110 GLU   A CB    1 
ATOM   779  C  CG    . GLU   A  1 118 ? 20.32600 -95.81000  -17.46600 1.000 55.53991  ? 110 GLU   A CG    1 
ATOM   780  C  CD    . GLU   A  1 118 ? 21.24600 -95.81800  -18.67800 1.000 59.93861  ? 110 GLU   A CD    1 
ATOM   781  O  OE1   . GLU   A  1 118 ? 21.59200 -94.72800  -19.17800 1.000 58.43662  ? 110 GLU   A OE1   1 
ATOM   782  O  OE2   . GLU   A  1 118 ? 21.61000 -96.92200  -19.12800 1.000 54.96858  ? 110 GLU   A OE2   1 
ATOM   783  N  N     . LEU   A  1 119 ? 18.84100 -92.51500  -14.56000 1.000 54.85985  ? 111 LEU   A N     1 
ATOM   784  C  CA    . LEU   A  1 119 ? 18.68700 -91.19500  -13.89300 1.000 61.29964  ? 111 LEU   A CA    1 
ATOM   785  C  C     . LEU   A  1 119 ? 18.81700 -91.36500  -12.37300 1.000 59.73387  ? 111 LEU   A C     1 
ATOM   786  O  O     . LEU   A  1 119 ? 19.51100 -90.53600  -11.74900 1.000 58.49654  ? 111 LEU   A O     1 
ATOM   787  C  CB    . LEU   A  1 119 ? 17.33400 -90.57700  -14.26700 1.000 59.21201  ? 111 LEU   A CB    1 
ATOM   788  C  CG    . LEU   A  1 119 ? 17.20200 -90.05100  -15.69600 1.000 56.24407  ? 111 LEU   A CG    1 
ATOM   789  C  CD1   . LEU   A  1 119 ? 15.83700 -89.41400  -15.90200 1.000 54.21344  ? 111 LEU   A CD1   1 
ATOM   790  C  CD2   . LEU   A  1 119 ? 18.30300 -89.05600  -16.03600 1.000 54.74370  ? 111 LEU   A CD2   1 
ATOM   791  N  N     . ASN   A  1 120 ? 18.17600 -92.39400  -11.80700 1.000 56.60648  ? 112 ASN   A N     1 
ATOM   792  C  CA    . ASN   A  1 120 ? 18.16600 -92.67200  -10.34400 1.000 59.12009  ? 112 ASN   A CA    1 
ATOM   793  C  C     . ASN   A  1 120 ? 19.57300 -93.08300  -9.89400  1.000 63.12809  ? 112 ASN   A C     1 
ATOM   794  O  O     . ASN   A  1 120 ? 19.94900 -92.73300  -8.75600  1.000 63.75403  ? 112 ASN   A O     1 
ATOM   795  C  CB    . ASN   A  1 120 ? 17.13200 -93.73300  -9.95300  1.000 57.97466  ? 112 ASN   A CB    1 
ATOM   796  C  CG    . ASN   A  1 120 ? 15.70100 -93.24100  -10.01200 1.000 57.78659  ? 112 ASN   A CG    1 
ATOM   797  O  OD1   . ASN   A  1 120 ? 15.43300 -92.05200  -9.86200  1.000 57.30567  ? 112 ASN   A OD1   1 
ATOM   798  N  ND2   . ASN   A  1 120 ? 14.76700 -94.15200  -10.22700 1.000 58.39388  ? 112 ASN   A ND2   1 
ATOM   799  N  N     . PHE   A  1 121 ? 20.31700 -93.80100  -10.74000 1.000 61.25019  ? 113 PHE   A N     1 
ATOM   800  C  CA    . PHE   A  1 121 ? 21.72400 -94.19800  -10.46800 1.000 63.89012  ? 113 PHE   A CA    1 
ATOM   801  C  C     . PHE   A  1 121 ? 22.62500 -92.96100  -10.57200 1.000 65.91224  ? 113 PHE   A C     1 
ATOM   802  O  O     . PHE   A  1 121 ? 23.59200 -92.86100  -9.79200  1.000 69.13817  ? 113 PHE   A O     1 
ATOM   803  C  CB    . PHE   A  1 121 ? 22.19300 -95.31800  -11.40100 1.000 63.14944  ? 113 PHE   A CB    1 
ATOM   804  C  CG    . PHE   A  1 121 ? 23.45900 -95.99300  -10.93500 1.000 61.70217  ? 113 PHE   A CG    1 
ATOM   805  C  CD1   . PHE   A  1 121 ? 23.43600 -96.87500  -9.86600  1.000 61.88672  ? 113 PHE   A CD1   1 
ATOM   806  C  CD2   . PHE   A  1 121 ? 24.67600 -95.72200  -11.54000 1.000 59.17992  ? 113 PHE   A CD2   1 
ATOM   807  C  CE1   . PHE   A  1 121 ? 24.59900 -97.48500  -9.42400  1.000 63.69154  ? 113 PHE   A CE1   1 
ATOM   808  C  CE2   . PHE   A  1 121 ? 25.83900 -96.33300  -11.09600 1.000 61.57117  ? 113 PHE   A CE2   1 
ATOM   809  C  CZ    . PHE   A  1 121 ? 25.79900 -97.21200  -10.03900 1.000 63.21950  ? 113 PHE   A CZ    1 
ATOM   810  N  N     . GLY   A  1 122 ? 22.31900 -92.05100  -11.50200 1.000 58.40807  ? 114 GLY   A N     1 
ATOM   811  C  CA    . GLY   A  1 122 ? 22.99700 -90.74600  -11.61600 1.000 59.94847  ? 114 GLY   A CA    1 
ATOM   812  C  C     . GLY   A  1 122 ? 22.88000 -89.96300  -10.32100 1.000 64.71696  ? 114 GLY   A C     1 
ATOM   813  O  O     . GLY   A  1 122 ? 23.91200 -89.45700  -9.83100  1.000 62.14473  ? 114 GLY   A O     1 
ATOM   814  N  N     . ALA   A  1 123 ? 21.66200 -89.89600  -9.77400  1.000 63.65216  ? 115 ALA   A N     1 
ATOM   815  C  CA    . ALA   A  1 123 ? 21.31300 -89.17600  -8.52700  1.000 61.65630  ? 115 ALA   A CA    1 
ATOM   816  C  C     . ALA   A  1 123 ? 21.98900 -89.85000  -7.32900  1.000 60.63119  ? 115 ALA   A C     1 
ATOM   817  O  O     . ALA   A  1 123 ? 22.35700 -89.13100  -6.38200  1.000 66.76106  ? 115 ALA   A O     1 
ATOM   818  C  CB    . ALA   A  1 123 ? 19.81300 -89.13400  -8.35800  1.000 63.66963  ? 115 ALA   A CB    1 
ATOM   819  N  N     . TYR   A  1 124 ? 22.13300 -91.17800  -7.37300  1.000 60.58586  ? 116 TYR   A N     1 
ATOM   820  C  CA    . TYR   A  1 124 ? 22.79800 -92.00100  -6.32800  1.000 64.12786  ? 116 TYR   A CA    1 
ATOM   821  C  C     . TYR   A  1 124 ? 24.27100 -91.58400  -6.21100  1.000 63.26951  ? 116 TYR   A C     1 
ATOM   822  O  O     . TYR   A  1 124 ? 24.74500 -91.38400  -5.07700  1.000 65.53565  ? 116 TYR   A O     1 
ATOM   823  C  CB    . TYR   A  1 124 ? 22.63500 -93.49200  -6.63900  1.000 63.33041  ? 116 TYR   A CB    1 
ATOM   824  C  CG    . TYR   A  1 124 ? 23.44800 -94.42100  -5.77200  1.000 66.54246  ? 116 TYR   A CG    1 
ATOM   825  C  CD1   . TYR   A  1 124 ? 23.11400 -94.64600  -4.44600  1.000 68.36120  ? 116 TYR   A CD1   1 
ATOM   826  C  CD2   . TYR   A  1 124 ? 24.54300 -95.09700  -6.28600  1.000 66.80822  ? 116 TYR   A CD2   1 
ATOM   827  C  CE1   . TYR   A  1 124 ? 23.85400 -95.50500  -3.65000  1.000 70.95597  ? 116 TYR   A CE1   1 
ATOM   828  C  CE2   . TYR   A  1 124 ? 25.29200 -95.96100  -5.50500  1.000 68.55973  ? 116 TYR   A CE2   1 
ATOM   829  C  CZ    . TYR   A  1 124 ? 24.94800 -96.16500  -4.18200  1.000 71.04175  ? 116 TYR   A CZ    1 
ATOM   830  O  OH    . TYR   A  1 124 ? 25.69000 -97.01500  -3.41600  1.000 73.82128  ? 116 TYR   A OH    1 
ATOM   831  N  N     . LEU   A  1 125 ? 24.96000 -91.43700  -7.34800  1.000 62.02222  ? 117 LEU   A N     1 
ATOM   832  C  CA    . LEU   A  1 125 ? 26.39900 -91.05700  -7.42100  1.000 62.87728  ? 117 LEU   A CA    1 
ATOM   833  C  C     . LEU   A  1 125 ? 26.56900 -89.56200  -7.12100  1.000 61.73866  ? 117 LEU   A C     1 
ATOM   834  O  O     . LEU   A  1 125 ? 27.71300 -89.15100  -6.85600  1.000 65.84131  ? 117 LEU   A O     1 
ATOM   835  C  CB    . LEU   A  1 125 ? 26.94600 -91.38300  -8.81500  1.000 63.23240  ? 117 LEU   A CB    1 
ATOM   836  C  CG    . LEU   A  1 125 ? 26.89300 -92.85100  -9.23900  1.000 60.87198  ? 117 LEU   A CG    1 
ATOM   837  C  CD1   . LEU   A  1 125 ? 27.29800 -92.99700  -10.69600 1.000 63.17331  ? 117 LEU   A CD1   1 
ATOM   838  C  CD2   . LEU   A  1 125 ? 27.77400 -93.71800  -8.35500  1.000 63.36364  ? 117 LEU   A CD2   1 
ATOM   839  N  N     . GLY   A  1 126 ? 25.48600 -88.78200  -7.19700  1.000 60.72163  ? 118 GLY   A N     1 
ATOM   840  C  CA    . GLY   A  1 126 ? 25.49100 -87.32200  -6.97500  1.000 63.54525  ? 118 GLY   A CA    1 
ATOM   841  C  C     . GLY   A  1 126 ? 26.22100 -86.58600  -8.08600  1.000 66.24958  ? 118 GLY   A C     1 
ATOM   842  O  O     . GLY   A  1 126 ? 27.03300 -85.69900  -7.76700  1.000 68.48362  ? 118 GLY   A O     1 
ATOM   843  N  N     . LEU   A  1 127 ? 25.93600 -86.93200  -9.34700  1.000 65.06620  ? 119 LEU   A N     1 
ATOM   844  C  CA    . LEU   A  1 127 ? 26.61000 -86.36300  -10.54800 1.000 66.86423  ? 119 LEU   A CA    1 
ATOM   845  C  C     . LEU   A  1 127 ? 26.18200 -84.91000  -10.73100 1.000 64.70363  ? 119 LEU   A C     1 
ATOM   846  O  O     . LEU   A  1 127 ? 25.00200 -84.58800  -10.59900 1.000 67.01498  ? 119 LEU   A O     1 
ATOM   847  C  CB    . LEU   A  1 127 ? 26.25400 -87.18800  -11.79000 1.000 62.10697  ? 119 LEU   A CB    1 
ATOM   848  C  CG    . LEU   A  1 127 ? 26.65500 -88.66300  -11.75700 1.000 65.77113  ? 119 LEU   A CG    1 
ATOM   849  C  CD1   . LEU   A  1 127 ? 26.22500 -89.36900  -13.03700 1.000 57.16110  ? 119 LEU   A CD1   1 
ATOM   850  C  CD2   . LEU   A  1 127 ? 28.15300 -88.82700  -11.53800 1.000 62.74730  ? 119 LEU   A CD2   1 
ATOM   851  N  N     . PRO   A  1 128 ? 27.12300 -83.99200  -11.05000 1.000 62.45795  ? 120 PRO   A N     1 
ATOM   852  C  CA    . PRO   A  1 128 ? 26.78600 -82.58600  -11.27500 1.000 62.71721  ? 120 PRO   A CA    1 
ATOM   853  C  C     . PRO   A  1 128 ? 25.77600 -82.39400  -12.41700 1.000 63.57399  ? 120 PRO   A C     1 
ATOM   854  O  O     . PRO   A  1 128 ? 24.92600 -81.53200  -12.28700 1.000 67.70093  ? 120 PRO   A O     1 
ATOM   855  C  CB    . PRO   A  1 128 ? 28.13000 -81.91300  -11.60200 1.000 65.78524  ? 120 PRO   A CB    1 
ATOM   856  C  CG    . PRO   A  1 128 ? 29.06100 -83.05100  -11.97600 1.000 66.83082  ? 120 PRO   A CG    1 
ATOM   857  C  CD    . PRO   A  1 128 ? 28.55800 -84.25700  -11.21300 1.000 63.04885  ? 120 PRO   A CD    1 
ATOM   858  N  N     . ALA   A  1 129 ? 25.88100 -83.20100  -13.48200 1.000 62.36284  ? 121 ALA   A N     1 
ATOM   859  C  CA    . ALA   A  1 129 ? 24.96800 -83.18600  -14.65100 1.000 60.91340  ? 121 ALA   A CA    1 
ATOM   860  C  C     . ALA   A  1 129 ? 24.85700 -84.58000  -15.28300 1.000 60.31203  ? 121 ALA   A C     1 
ATOM   861  O  O     . ALA   A  1 129 ? 25.74400 -85.42000  -15.05000 1.000 60.81710  ? 121 ALA   A O     1 
ATOM   862  C  CB    . ALA   A  1 129 ? 25.44900 -82.17300  -15.65700 1.000 63.69638  ? 121 ALA   A CB    1 
ATOM   863  N  N     . PHE   A  1 130 ? 23.80000 -84.79200  -16.07200 1.000 59.66201  ? 122 PHE   A N     1 
ATOM   864  C  CA    . PHE   A  1 130 ? 23.49500 -86.04600  -16.81300 1.000 58.33713  ? 122 PHE   A CA    1 
ATOM   865  C  C     . PHE   A  1 130 ? 22.98200 -85.67000  -18.21200 1.000 57.26329  ? 122 PHE   A C     1 
ATOM   866  O  O     . PHE   A  1 130 ? 22.05500 -84.83800  -18.29200 1.000 57.11516  ? 122 PHE   A O     1 
ATOM   867  C  CB    . PHE   A  1 130 ? 22.48800 -86.87700  -16.01100 1.000 59.95480  ? 122 PHE   A CB    1 
ATOM   868  C  CG    . PHE   A  1 130 ? 22.31700 -88.30500  -16.46700 1.000 61.70325  ? 122 PHE   A CG    1 
ATOM   869  C  CD1   . PHE   A  1 130 ? 21.50600 -88.61300  -17.55000 1.000 59.50038  ? 122 PHE   A CD1   1 
ATOM   870  C  CD2   . PHE   A  1 130 ? 22.95200 -89.34400  -15.80500 1.000 56.78205  ? 122 PHE   A CD2   1 
ATOM   871  C  CE1   . PHE   A  1 130 ? 21.34500 -89.92600  -17.96700 1.000 57.71504  ? 122 PHE   A CE1   1 
ATOM   872  C  CE2   . PHE   A  1 130 ? 22.79300 -90.65700  -16.22500 1.000 58.56080  ? 122 PHE   A CE2   1 
ATOM   873  C  CZ    . PHE   A  1 130 ? 21.98900 -90.94500  -17.30500 1.000 57.40251  ? 122 PHE   A CZ    1 
ATOM   874  N  N     . LEU   A  1 131 ? 23.57000 -86.24600  -19.27100 1.000 58.14521  ? 123 LEU   A N     1 
ATOM   875  C  CA    . LEU   A  1 131 ? 23.28200 -85.90900  -20.69800 1.000 55.21810  ? 123 LEU   A CA    1 
ATOM   876  C  C     . LEU   A  1 131 ? 22.13500 -86.77700  -21.23000 1.000 55.02714  ? 123 LEU   A C     1 
ATOM   877  O  O     . LEU   A  1 131 ? 22.18500 -88.00900  -21.04200 1.000 58.78632  ? 123 LEU   A O     1 
ATOM   878  C  CB    . LEU   A  1 131 ? 24.53900 -86.12100  -21.55100 1.000 48.00911  ? 123 LEU   A CB    1 
ATOM   879  C  CG    . LEU   A  1 131 ? 25.51100 -84.94400  -21.61100 1.000 52.25220  ? 123 LEU   A CG    1 
ATOM   880  C  CD1   . LEU   A  1 131 ? 26.88900 -85.40200  -22.06300 1.000 48.46768  ? 123 LEU   A CD1   1 
ATOM   881  C  CD2   . LEU   A  1 131 ? 24.99100 -83.84900  -22.52800 1.000 51.77038  ? 123 LEU   A CD2   1 
ATOM   882  N  N     . LEU   A  1 132 ? 21.15600 -86.14700  -21.88800 1.000 55.30849  ? 124 LEU   A N     1 
ATOM   883  C  CA    . LEU   A  1 132 ? 20.04200 -86.81700  -22.61400 1.000 55.26128  ? 124 LEU   A CA    1 
ATOM   884  C  C     . LEU   A  1 132 ? 19.93100 -86.21300  -24.01000 1.000 53.15353  ? 124 LEU   A C     1 
ATOM   885  O  O     . LEU   A  1 132 ? 19.93600 -84.99300  -24.15100 1.000 53.86404  ? 124 LEU   A O     1 
ATOM   886  C  CB    . LEU   A  1 132 ? 18.73300 -86.62700  -21.84300 1.000 53.27501  ? 124 LEU   A CB    1 
ATOM   887  C  CG    . LEU   A  1 132 ? 18.66100 -87.32200  -20.48500 1.000 54.81642  ? 124 LEU   A CG    1 
ATOM   888  C  CD1   . LEU   A  1 132 ? 19.09800 -86.38600  -19.36900 1.000 54.36764  ? 124 LEU   A CD1   1 
ATOM   889  C  CD2   . LEU   A  1 132 ? 17.25600 -87.83800  -20.21900 1.000 55.94010  ? 124 LEU   A CD2   1 
ATOM   890  N  N     . PRO   A  1 133 ? 19.82700 -87.03500  -25.07900 1.000 56.28851  ? 125 PRO   A N     1 
ATOM   891  C  CA    . PRO   A  1 133 ? 19.71900 -86.51300  -26.44000 1.000 53.79320  ? 125 PRO   A CA    1 
ATOM   892  C  C     . PRO   A  1 133 ? 18.30500 -86.06500  -26.83700 1.000 52.19678  ? 125 PRO   A C     1 
ATOM   893  O  O     . PRO   A  1 133 ? 17.34700 -86.66000  -26.38200 1.000 55.04891  ? 125 PRO   A O     1 
ATOM   894  C  CB    . PRO   A  1 133 ? 20.13400 -87.72300  -27.28700 1.000 53.00165  ? 125 PRO   A CB    1 
ATOM   895  C  CG    . PRO   A  1 133 ? 19.62700 -88.90400  -26.49300 1.000 56.99555  ? 125 PRO   A CG    1 
ATOM   896  C  CD    . PRO   A  1 133 ? 19.83400 -88.50700  -25.04500 1.000 51.69458  ? 125 PRO   A CD    1 
ATOM   897  N  N     . LEU   A  1 134 ? 18.22600 -85.01800  -27.66200 1.000 48.60930  ? 126 LEU   A N     1 
ATOM   898  C  CA    . LEU   A  1 134 ? 17.04000 -84.68000  -28.49300 1.000 52.48743  ? 126 LEU   A CA    1 
ATOM   899  C  C     . LEU   A  1 134 ? 17.39200 -85.01200  -29.95000 1.000 56.97860  ? 126 LEU   A C     1 
ATOM   900  O  O     . LEU   A  1 134 ? 18.00200 -84.16000  -30.62200 1.000 56.10140  ? 126 LEU   A O     1 
ATOM   901  C  CB    . LEU   A  1 134 ? 16.67600 -83.20500  -28.28600 1.000 55.16067  ? 126 LEU   A CB    1 
ATOM   902  C  CG    . LEU   A  1 134 ? 16.22200 -82.82600  -26.87400 1.000 55.39656  ? 126 LEU   A CG    1 
ATOM   903  C  CD1   . LEU   A  1 134 ? 15.86400 -81.35100  -26.79200 1.000 56.93912  ? 126 LEU   A CD1   1 
ATOM   904  C  CD2   . LEU   A  1 134 ? 15.03800 -83.66600  -26.41900 1.000 52.59364  ? 126 LEU   A CD2   1 
ATOM   905  N  N     . ASN   A  1 135 ? 17.06300 -86.23900  -30.38000 1.000 59.08400  ? 127 ASN   A N     1 
ATOM   906  C  CA    . ASN   A  1 135 ? 17.43500 -86.84600  -31.68900 1.000 51.19243  ? 127 ASN   A CA    1 
ATOM   907  C  C     . ASN   A  1 135 ? 16.34400 -86.60600  -32.73600 1.000 54.67070  ? 127 ASN   A C     1 
ATOM   908  O  O     . ASN   A  1 135 ? 16.69500 -86.49800  -33.92400 1.000 57.60459  ? 127 ASN   A O     1 
ATOM   909  C  CB    . ASN   A  1 135 ? 17.60900 -88.36600  -31.59600 1.000 50.61857  ? 127 ASN   A CB    1 
ATOM   910  C  CG    . ASN   A  1 135 ? 18.80300 -88.80700  -30.77900 1.000 55.28355  ? 127 ASN   A CG    1 
ATOM   911  O  OD1   . ASN   A  1 135 ? 18.74500 -89.83200  -30.10500 1.000 60.43538  ? 127 ASN   A OD1   1 
ATOM   912  N  ND2   . ASN   A  1 135 ? 19.88900 -88.05400  -30.84300 1.000 62.49377  ? 127 ASN   A ND2   1 
ATOM   913  N  N     . GLN   A  1 136 ? 15.07700 -86.59200  -32.31000 1.000 51.02240  ? 128 GLN   A N     1 
ATOM   914  C  CA    . GLN   A  1 136 ? 13.87800 -86.60700  -33.19200 1.000 54.30175  ? 128 GLN   A CA    1 
ATOM   915  C  C     . GLN   A  1 136 ? 12.92500 -85.48800  -32.75500 1.000 55.29612  ? 128 GLN   A C     1 
ATOM   916  O  O     . GLN   A  1 136 ? 13.22600 -84.81600  -31.75300 1.000 54.31446  ? 128 GLN   A O     1 
ATOM   917  C  CB    . GLN   A  1 136 ? 13.20800 -87.98600  -33.16300 1.000 51.75095  ? 128 GLN   A CB    1 
ATOM   918  C  CG    . GLN   A  1 136 ? 13.20300 -88.64800  -31.79000 1.000 55.25652  ? 128 GLN   A CG    1 
ATOM   919  C  CD    . GLN   A  1 136 ? 12.46100 -89.96300  -31.76000 1.000 60.48437  ? 128 GLN   A CD    1 
ATOM   920  O  OE1   . GLN   A  1 136 ? 13.03400 -91.01600  -31.48300 1.000 61.06684  ? 128 GLN   A OE1   1 
ATOM   921  N  NE2   . GLN   A  1 136 ? 11.16800 -89.91200  -32.04000 1.000 61.87132  ? 128 GLN   A NE2   1 
ATOM   922  N  N     . GLU   A  1 137 ? 11.83300 -85.29200  -33.50000 1.000 58.54142  ? 129 GLU   A N     1 
ATOM   923  C  CA    . GLU   A  1 137 ? 10.80500 -84.24700  -33.24500 1.000 53.77089  ? 129 GLU   A CA    1 
ATOM   924  C  C     . GLU   A  1 137 ? 10.02100 -84.60200  -31.97600 1.000 55.17994  ? 129 GLU   A C     1 
ATOM   925  O  O     . GLU   A  1 137 ? 9.87100  -83.71800  -31.11400 1.000 60.48674  ? 129 GLU   A O     1 
ATOM   926  C  CB    . GLU   A  1 137 ? 9.87200  -84.11400  -34.45100 1.000 54.43115  ? 129 GLU   A CB    1 
ATOM   927  C  CG    . GLU   A  1 137 ? 8.89900  -82.95400  -34.34800 1.000 55.15771  ? 129 GLU   A CG    1 
ATOM   928  C  CD    . GLU   A  1 137 ? 8.11000  -82.66100  -35.61200 1.000 57.98061  ? 129 GLU   A CD    1 
ATOM   929  O  OE1   . GLU   A  1 137 ? 8.35900  -83.32300  -36.63500 1.000 75.03160  ? 129 GLU   A OE1   1 
ATOM   930  O  OE2   . GLU   A  1 137 ? 7.24500  -81.76900  -35.56900 1.000 65.84324  ? 129 GLU   A OE2   1 
ATOM   931  N  N     . ASP   A  1 138 ? 9.53700  -85.84300  -31.87500 1.000 54.13340  ? 130 ASP   A N     1 
ATOM   932  C  CA    . ASP   A  1 138 ? 8.66200  -86.31100  -30.76700 1.000 56.55410  ? 130 ASP   A CA    1 
ATOM   933  C  C     . ASP   A  1 138 ? 9.52700  -86.92200  -29.66100 1.000 56.46730  ? 130 ASP   A C     1 
ATOM   934  O  O     . ASP   A  1 138 ? 9.90300  -88.10200  -29.78900 1.000 58.64093  ? 130 ASP   A O     1 
ATOM   935  C  CB    . ASP   A  1 138 ? 7.61400  -87.30700  -31.26700 1.000 58.04585  ? 130 ASP   A CB    1 
ATOM   936  C  CG    . ASP   A  1 138 ? 6.64000  -87.75200  -30.19100 1.000 56.00374  ? 130 ASP   A CG    1 
ATOM   937  O  OD1   . ASP   A  1 138 ? 6.53100  -87.04600  -29.17300 1.000 56.70907  ? 130 ASP   A OD1   1 
ATOM   938  O  OD2   . ASP   A  1 138 ? 6.00100  -88.80200  -30.38000 1.000 63.13823  ? 130 ASP   A OD2   1 
ATOM   939  N  N     . ASN   A  1 139 ? 9.83500  -86.12900  -28.63000 1.000 54.82950  ? 131 ASN   A N     1 
ATOM   940  C  CA    . ASN   A  1 139 ? 10.49100 -86.57300  -27.37100 1.000 55.43630  ? 131 ASN   A CA    1 
ATOM   941  C  C     . ASN   A  1 139 ? 9.53000  -86.32700  -26.19800 1.000 57.57122  ? 131 ASN   A C     1 
ATOM   942  O  O     . ASN   A  1 139 ? 10.00900 -85.94200  -25.11200 1.000 55.70426  ? 131 ASN   A O     1 
ATOM   943  C  CB    . ASN   A  1 139 ? 11.84100 -85.87600  -27.17700 1.000 52.61644  ? 131 ASN   A CB    1 
ATOM   944  C  CG    . ASN   A  1 139 ? 12.85100 -86.25600  -28.23800 1.000 51.95730  ? 131 ASN   A CG    1 
ATOM   945  O  OD1   . ASN   A  1 139 ? 13.07500 -87.43700  -28.49000 1.000 54.11119  ? 131 ASN   A OD1   1 
ATOM   946  N  ND2   . ASN   A  1 139 ? 13.47200 -85.26600  -28.85700 1.000 56.15044  ? 131 ASN   A ND2   1 
ATOM   947  N  N     . THR   A  1 140 ? 8.22900  -86.55600  -26.41200 1.000 55.24601  ? 132 THR   A N     1 
ATOM   948  C  CA    . THR   A  1 140 ? 7.13400  -86.29000  -25.44000 1.000 50.97012  ? 132 THR   A CA    1 
ATOM   949  C  C     . THR   A  1 140 ? 7.29500  -87.19900  -24.21700 1.000 53.96470  ? 132 THR   A C     1 
ATOM   950  O  O     . THR   A  1 140 ? 7.30600  -86.67400  -23.08600 1.000 51.99214  ? 132 THR   A O     1 
ATOM   951  C  CB    . THR   A  1 140 ? 5.75800  -86.48800  -26.08900 1.000 54.98189  ? 132 THR   A CB    1 
ATOM   952  O  OG1   . THR   A  1 140 ? 5.62500  -85.53900  -27.14700 1.000 59.67358  ? 132 THR   A OG1   1 
ATOM   953  C  CG2   . THR   A  1 140 ? 4.61000  -86.31800  -25.12000 1.000 52.81271  ? 132 THR   A CG2   1 
ATOM   954  N  N     . ASN   A  1 141 ? 7.39900  -88.51100  -24.43900 1.000 53.02142  ? 133 ASN   A N     1 
ATOM   955  C  CA    . ASN   A  1 141 ? 7.50800  -89.52600  -23.35800 1.000 56.27981  ? 133 ASN   A CA    1 
ATOM   956  C  C     . ASN   A  1 141 ? 8.83600  -89.33200  -22.61600 1.000 52.86049  ? 133 ASN   A C     1 
ATOM   957  O  O     . ASN   A  1 141 ? 8.82200  -89.41500  -21.37900 1.000 58.24549  ? 133 ASN   A O     1 
ATOM   958  C  CB    . ASN   A  1 141 ? 7.35800  -90.95500  -23.88500 1.000 56.79510  ? 133 ASN   A CB    1 
ATOM   959  C  CG    . ASN   A  1 141 ? 6.96200  -91.94000  -22.80400 1.000 60.76771  ? 133 ASN   A CG    1 
ATOM   960  O  OD1   . ASN   A  1 141 ? 6.47000  -91.54700  -21.74700 1.000 62.81642  ? 133 ASN   A OD1   1 
ATOM   961  N  ND2   . ASN   A  1 141 ? 7.16200  -93.22300  -23.06100 1.000 62.04629  ? 133 ASN   A ND2   1 
ATOM   962  N  N     . LEU   A  1 142 ? 9.92900  -89.07200  -23.34200 1.000 52.32287  ? 134 LEU   A N     1 
ATOM   963  C  CA    . LEU   A  1 142 ? 11.26100 -88.73600  -22.76300 1.000 52.65431  ? 134 LEU   A CA    1 
ATOM   964  C  C     . LEU   A  1 142 ? 11.10700 -87.57300  -21.77000 1.000 55.55273  ? 134 LEU   A C     1 
ATOM   965  O  O     . LEU   A  1 142 ? 11.67100 -87.66200  -20.66800 1.000 53.73824  ? 134 LEU   A O     1 
ATOM   966  C  CB    . LEU   A  1 142 ? 12.22700 -88.37300  -23.89500 1.000 48.57359  ? 134 LEU   A CB    1 
ATOM   967  C  CG    . LEU   A  1 142 ? 13.66300 -88.06100  -23.47300 1.000 49.29541  ? 134 LEU   A CG    1 
ATOM   968  C  CD1   . LEU   A  1 142 ? 14.47500 -89.33500  -23.31000 1.000 54.27936  ? 134 LEU   A CD1   1 
ATOM   969  C  CD2   . LEU   A  1 142 ? 14.33400 -87.13900  -24.47900 1.000 53.21907  ? 134 LEU   A CD2   1 
ATOM   970  N  N     . ALA   A  1 143 ? 10.36700 -86.52700  -22.15200 1.000 53.95950  ? 135 ALA   A N     1 
ATOM   971  C  CA    . ALA   A  1 143 ? 10.10600 -85.32600  -21.32300 1.000 55.76959  ? 135 ALA   A CA    1 
ATOM   972  C  C     . ALA   A  1 143 ? 9.29700  -85.72300  -20.08100 1.000 56.92180  ? 135 ALA   A C     1 
ATOM   973  O  O     . ALA   A  1 143 ? 9.61800  -85.22800  -18.98600 1.000 54.09087  ? 135 ALA   A O     1 
ATOM   974  C  CB    . ALA   A  1 143 ? 9.39100  -84.27400  -22.13700 1.000 52.35508  ? 135 ALA   A CB    1 
ATOM   975  N  N     . ARG   A  1 144 ? 8.29600  -86.59300  -20.25400 1.000 54.57717  ? 136 ARG   A N     1 
ATOM   976  C  CA    . ARG   A  1 144 ? 7.37900  -87.05600  -19.17700 1.000 53.45590  ? 136 ARG   A CA    1 
ATOM   977  C  C     . ARG   A  1 144 ? 8.18200  -87.83000  -18.12600 1.000 55.73813  ? 136 ARG   A C     1 
ATOM   978  O  O     . ARG   A  1 144 ? 8.01200  -87.54400  -16.92400 1.000 60.86940  ? 136 ARG   A O     1 
ATOM   979  C  CB    . ARG   A  1 144 ? 6.25700  -87.91500  -19.76800 1.000 52.19614  ? 136 ARG   A CB    1 
ATOM   980  C  CG    . ARG   A  1 144 ? 4.93800  -87.83700  -19.01200 1.000 53.86762  ? 136 ARG   A CG    1 
ATOM   981  C  CD    . ARG   A  1 144 ? 4.90500  -88.60400  -17.70300 1.000 57.14709  ? 136 ARG   A CD    1 
ATOM   982  N  NE    . ARG   A  1 144 ? 5.19100  -90.02500  -17.83300 1.000 64.06653  ? 136 ARG   A NE    1 
ATOM   983  C  CZ    . ARG   A  1 144 ? 5.25700  -90.88500  -16.81600 1.000 71.57340  ? 136 ARG   A CZ    1 
ATOM   984  N  NH1   . ARG   A  1 144 ? 5.06600  -90.47600  -15.57000 1.000 62.21314  ? 136 ARG   A NH1   1 
ATOM   985  N  NH2   . ARG   A  1 144 ? 5.52300  -92.15900  -17.05600 1.000 81.52224  ? 136 ARG   A NH2   1 
ATOM   986  N  N     . VAL   A  1 145 ? 9.03700  -88.75600  -18.56400 1.000 53.76285  ? 137 VAL   A N     1 
ATOM   987  C  CA    . VAL   A  1 145 ? 9.85600  -89.62600  -17.66900 1.000 58.52577  ? 137 VAL   A CA    1 
ATOM   988  C  C     . VAL   A  1 145 ? 10.85900 -88.74900  -16.90500 1.000 56.72652  ? 137 VAL   A C     1 
ATOM   989  O  O     . VAL   A  1 145 ? 11.01100 -88.96700  -15.69200 1.000 66.11105  ? 137 VAL   A O     1 
ATOM   990  C  CB    . VAL   A  1 145 ? 10.54100 -90.76700  -18.45000 1.000 55.76491  ? 137 VAL   A CB    1 
ATOM   991  C  CG1   . VAL   A  1 145 ? 11.52500 -91.54400  -17.58800 1.000 53.85406  ? 137 VAL   A CG1   1 
ATOM   992  C  CG2   . VAL   A  1 145 ? 9.52100  -91.71900  -19.05900 1.000 55.71594  ? 137 VAL   A CG2   1 
ATOM   993  N  N     . LEU   A  1 146 ? 11.50500 -87.78800  -17.57400 1.000 54.82285  ? 138 LEU   A N     1 
ATOM   994  C  CA    . LEU   A  1 146 ? 12.46800 -86.85000  -16.93200 1.000 53.05679  ? 138 LEU   A CA    1 
ATOM   995  C  C     . LEU   A  1 146 ? 11.72100 -85.96700  -15.92600 1.000 57.43913  ? 138 LEU   A C     1 
ATOM   996  O  O     . LEU   A  1 146 ? 12.26100 -85.74600  -14.83100 1.000 59.89062  ? 138 LEU   A O     1 
ATOM   997  C  CB    . LEU   A  1 146 ? 13.16300 -85.99400  -17.99500 1.000 54.64760  ? 138 LEU   A CB    1 
ATOM   998  C  CG    . LEU   A  1 146 ? 14.13500 -84.94300  -17.45300 1.000 56.80090  ? 138 LEU   A CG    1 
ATOM   999  C  CD1   . LEU   A  1 146 ? 15.26300 -85.59300  -16.66500 1.000 55.07450  ? 138 LEU   A CD1   1 
ATOM   1000 C  CD2   . LEU   A  1 146 ? 14.70000 -84.08900  -18.57700 1.000 49.82928  ? 138 LEU   A CD2   1 
ATOM   1001 N  N     . THR   A  1 147 ? 10.53800 -85.47100  -16.29900 1.000 57.76761  ? 139 THR   A N     1 
ATOM   1002 C  CA    . THR   A  1 147 ? 9.66500  -84.63400  -15.43300 1.000 56.22292  ? 139 THR   A CA    1 
ATOM   1003 C  C     . THR   A  1 147 ? 9.29200  -85.44200  -14.18500 1.000 63.20696  ? 139 THR   A C     1 
ATOM   1004 O  O     . THR   A  1 147 ? 9.36300  -84.87000  -13.08300 1.000 66.51629  ? 139 THR   A O     1 
ATOM   1005 C  CB    . THR   A  1 147 ? 8.43000  -84.13000  -16.19100 1.000 58.49251  ? 139 THR   A CB    1 
ATOM   1006 O  OG1   . THR   A  1 147 ? 8.87500  -83.41500  -17.34400 1.000 59.58649  ? 139 THR   A OG1   1 
ATOM   1007 C  CG2   . THR   A  1 147 ? 7.55000  -83.21900  -15.36200 1.000 57.62414  ? 139 THR   A CG2   1 
ATOM   1008 N  N     . ASN   A  1 148 ? 8.92300  -86.71600  -14.36000 1.000 63.67604  ? 140 ASN   A N     1 
ATOM   1009 C  CA    . ASN   A  1 148 ? 8.60800  -87.66200  -13.25400 1.000 65.00174  ? 140 ASN   A CA    1 
ATOM   1010 C  C     . ASN   A  1 148 ? 9.80300  -87.71700  -12.29300 1.000 64.26075  ? 140 ASN   A C     1 
ATOM   1011 O  O     . ASN   A  1 148 ? 9.59000  -87.53600  -11.08000 1.000 65.36917  ? 140 ASN   A O     1 
ATOM   1012 C  CB    . ASN   A  1 148 ? 8.23400  -89.05200  -13.78300 1.000 73.13508  ? 140 ASN   A CB    1 
ATOM   1013 C  CG    . ASN   A  1 148 ? 8.03000  -90.07800  -12.68500 1.000 83.80231  ? 140 ASN   A CG    1 
ATOM   1014 O  OD1   . ASN   A  1 148 ? 7.34700  -89.81200  -11.69600 1.000 79.65814  ? 140 ASN   A OD1   1 
ATOM   1015 N  ND2   . ASN   A  1 148 ? 8.61300  -91.25700  -12.85200 1.000 76.28324  ? 140 ASN   A ND2   1 
ATOM   1016 N  N     . HIS   A  1 149 ? 11.00900 -87.93000  -12.83000 1.000 63.07092  ? 141 HIS   A N     1 
ATOM   1017 C  CA    . HIS   A  1 149 ? 12.28600 -88.05800  -12.07400 1.000 61.21545  ? 141 HIS   A CA    1 
ATOM   1018 C  C     . HIS   A  1 149 ? 12.60400 -86.76300  -11.31500 1.000 65.40259  ? 141 HIS   A C     1 
ATOM   1019 O  O     . HIS   A  1 149 ? 13.08200 -86.86000  -10.17100 1.000 74.69080  ? 141 HIS   A O     1 
ATOM   1020 C  CB    . HIS   A  1 149 ? 13.42500 -88.44900  -13.02300 1.000 54.59552  ? 141 HIS   A CB    1 
ATOM   1021 C  CG    . HIS   A  1 149 ? 14.77900 -88.41200  -12.39800 1.000 58.29492  ? 141 HIS   A CG    1 
ATOM   1022 N  ND1   . HIS   A  1 149 ? 15.19500 -89.35300  -11.47900 1.000 59.25542  ? 141 HIS   A ND1   1 
ATOM   1023 C  CD2   . HIS   A  1 149 ? 15.81600 -87.56700  -12.57200 1.000 59.72116  ? 141 HIS   A CD2   1 
ATOM   1024 C  CE1   . HIS   A  1 149 ? 16.43100 -89.08500  -11.10900 1.000 59.72169  ? 141 HIS   A CE1   1 
ATOM   1025 N  NE2   . HIS   A  1 149 ? 16.83500 -87.99400  -11.76500 1.000 61.08592  ? 141 HIS   A NE2   1 
ATOM   1026 N  N     . ILE   A  1 150 ? 12.36500 -85.59900  -11.92600 1.000 62.54541  ? 142 ILE   A N     1 
ATOM   1027 C  CA    . ILE   A  1 150 ? 12.69500 -84.26700  -11.33500 1.000 66.01310  ? 142 ILE   A CA    1 
ATOM   1028 C  C     . ILE   A  1 150 ? 11.81400 -84.03000  -10.10000 1.000 73.08745  ? 142 ILE   A C     1 
ATOM   1029 O  O     . ILE   A  1 150 ? 12.33800 -83.47600  -9.11300  1.000 81.96642  ? 142 ILE   A O     1 
ATOM   1030 C  CB    . ILE   A  1 150 ? 12.57700 -83.14800  -12.39300 1.000 64.63829  ? 142 ILE   A CB    1 
ATOM   1031 C  CG1   . ILE   A  1 150 ? 13.79600 -83.15000  -13.32000 1.000 65.83000  ? 142 ILE   A CG1   1 
ATOM   1032 C  CG2   . ILE   A  1 150 ? 12.37400 -81.78500  -11.74700 1.000 68.20781  ? 142 ILE   A CG2   1 
ATOM   1033 C  CD1   . ILE   A  1 150 ? 13.65300 -82.28500  -14.55200 1.000 60.93520  ? 142 ILE   A CD1   1 
ATOM   1034 N  N     . HIS   A  1 151 ? 10.54700 -84.46300  -10.13700 1.000 66.12521  ? 143 HIS   A N     1 
ATOM   1035 C  CA    . HIS   A  1 151 ? 9.55400  -84.29600  -9.04000  1.000 66.08548  ? 143 HIS   A CA    1 
ATOM   1036 C  C     . HIS   A  1 151 ? 9.56100  -85.52400  -8.11800  1.000 73.50909  ? 143 HIS   A C     1 
ATOM   1037 O  O     . HIS   A  1 151 ? 8.49100  -85.84800  -7.56100  1.000 73.92799  ? 143 HIS   A O     1 
ATOM   1038 C  CB    . HIS   A  1 151 ? 8.16200  -84.00700  -9.62200  1.000 62.29276  ? 143 HIS   A CB    1 
ATOM   1039 C  CG    . HIS   A  1 151 ? 8.09100  -82.72800  -10.38600 1.000 67.40952  ? 143 HIS   A CG    1 
ATOM   1040 N  ND1   . HIS   A  1 151 ? 8.55100  -82.61600  -11.68400 1.000 68.58178  ? 143 HIS   A ND1   1 
ATOM   1041 C  CD2   . HIS   A  1 151 ? 7.62100  -81.50900  -10.04300 1.000 73.13280  ? 143 HIS   A CD2   1 
ATOM   1042 C  CE1   . HIS   A  1 151 ? 8.36500  -81.38400  -12.11000 1.000 72.06493  ? 143 HIS   A CE1   1 
ATOM   1043 N  NE2   . HIS   A  1 151 ? 7.79700  -80.68200  -11.12000 1.000 74.94820  ? 143 HIS   A NE2   1 
ATOM   1044 N  N     . THR   A  1 152 ? 10.72600 -86.16400  -7.95500  1.000 76.80063  ? 144 THR   A N     1 
ATOM   1045 C  CA    . THR   A  1 152 ? 10.97700 -87.30100  -7.02600  1.000 80.09313  ? 144 THR   A CA    1 
ATOM   1046 C  C     . THR   A  1 152 ? 11.95500 -86.81100  -5.94800  1.000 96.57750  ? 144 THR   A C     1 
ATOM   1047 O  O     . THR   A  1 152 ? 13.12800 -87.23500  -5.95800  1.000 102.24640 ? 144 THR   A O     1 
ATOM   1048 C  CB    . THR   A  1 152 ? 11.42200 -88.53600  -7.82400  1.000 75.49024  ? 144 THR   A CB    1 
ATOM   1049 O  OG1   . THR   A  1 152 ? 10.27800 -88.98100  -8.55200  1.000 77.90448  ? 144 THR   A OG1   1 
ATOM   1050 C  CG2   . THR   A  1 152 ? 11.94200 -89.68200  -6.98200  1.000 81.40355  ? 144 THR   A CG2   1 
ATOM   1051 N  N     . GLY   A  1 153 ? 11.48200 -85.92200  -5.06600  1.000 105.03575 ? 145 GLY   A N     1 
ATOM   1052 C  CA    . GLY   A  1 153 ? 12.30600 -85.20900  -4.07100  1.000 107.94917 ? 145 GLY   A CA    1 
ATOM   1053 C  C     . GLY   A  1 153 ? 13.06800 -84.05500  -4.70600  1.000 119.27693 ? 145 GLY   A C     1 
ATOM   1054 O  O     . GLY   A  1 153 ? 13.57000 -84.23200  -5.83800  1.000 118.62997 ? 145 GLY   A O     1 
ATOM   1055 N  N     . HIS   A  1 154 ? 13.14500 -82.91100  -4.01400  1.000 124.37351 ? 146 HIS   A N     1 
ATOM   1056 C  CA    . HIS   A  1 154 ? 13.91100 -81.70700  -4.44500  1.000 125.64307 ? 146 HIS   A CA    1 
ATOM   1057 C  C     . HIS   A  1 154 ? 15.41200 -82.02700  -4.39200  1.000 121.47148 ? 146 HIS   A C     1 
ATOM   1058 O  O     . HIS   A  1 154 ? 16.01300 -81.86400  -3.30900  1.000 128.42158 ? 146 HIS   A O     1 
ATOM   1059 C  CB    . HIS   A  1 154 ? 13.55700 -80.48300  -3.58100  1.000 124.48944 ? 146 HIS   A CB    1 
ATOM   1060 C  CG    . HIS   A  1 154 ? 12.11200 -80.10300  -3.59800  1.000 130.67936 ? 146 HIS   A CG    1 
ATOM   1061 N  ND1   . HIS   A  1 154 ? 11.40800 -79.83000  -2.43800  1.000 131.92668 ? 146 HIS   A ND1   1 
ATOM   1062 C  CD2   . HIS   A  1 154 ? 11.23800 -79.94500  -4.61700  1.000 128.19575 ? 146 HIS   A CD2   1 
ATOM   1063 C  CE1   . HIS   A  1 154 ? 10.16400 -79.52000  -2.74200  1.000 126.86691 ? 146 HIS   A CE1   1 
ATOM   1064 N  NE2   . HIS   A  1 154 ? 10.03300 -79.58400  -4.07400  1.000 123.27298 ? 146 HIS   A NE2   1 
ATOM   1065 N  N     . HIS   A  1 155 ? 15.98900 -82.48000  -5.51200  1.000 119.57769 ? 147 HIS   A N     1 
ATOM   1066 C  CA    . HIS   A  1 155 ? 17.40900 -82.91900  -5.61900  1.000 112.98865 ? 147 HIS   A CA    1 
ATOM   1067 C  C     . HIS   A  1 155 ? 18.10800 -82.13200  -6.73300  1.000 105.55500 ? 147 HIS   A C     1 
ATOM   1068 O  O     . HIS   A  1 155 ? 17.71600 -82.29500  -7.90500  1.000 108.24459 ? 147 HIS   A O     1 
ATOM   1069 C  CB    . HIS   A  1 155 ? 17.48100 -84.44300  -5.79800  1.000 109.14145 ? 147 HIS   A CB    1 
ATOM   1070 C  CG    . HIS   A  1 155 ? 16.99200 -85.18600  -4.59900  1.000 117.31011 ? 147 HIS   A CG    1 
ATOM   1071 N  ND1   . HIS   A  1 155 ? 15.96900 -86.11700  -4.66500  1.000 118.75209 ? 147 HIS   A ND1   1 
ATOM   1072 C  CD2   . HIS   A  1 155 ? 17.35200 -85.11100  -3.29700  1.000 116.68357 ? 147 HIS   A CD2   1 
ATOM   1073 C  CE1   . HIS   A  1 155 ? 15.73600 -86.59600  -3.45800  1.000 115.93551 ? 147 HIS   A CE1   1 
ATOM   1074 N  NE2   . HIS   A  1 155 ? 16.57200 -85.99400  -2.60000  1.000 115.63558 ? 147 HIS   A NE2   1 
ATOM   1075 N  N     . SER   A  1 156 ? 19.09600 -81.30900  -6.36200  1.000 99.73936  ? 148 SER   A N     1 
ATOM   1076 C  CA    . SER   A  1 156 ? 19.84300 -80.39500  -7.26700  1.000 93.66391  ? 148 SER   A CA    1 
ATOM   1077 C  C     . SER   A  1 156 ? 20.80400 -81.21100  -8.14100  1.000 92.17721  ? 148 SER   A C     1 
ATOM   1078 O  O     . SER   A  1 156 ? 21.89900 -81.57500  -7.66300  1.000 91.16584  ? 148 SER   A O     1 
ATOM   1079 C  CB    . SER   A  1 156 ? 20.55900 -79.30800  -6.49900  1.000 93.93882  ? 148 SER   A CB    1 
ATOM   1080 O  OG    . SER   A  1 156 ? 21.59100 -79.84400  -5.68500  1.000 97.51973  ? 148 SER   A OG    1 
ATOM   1081 N  N     . SER   A  1 157 ? 20.36600 -81.51200  -9.36500  1.000 85.40359  ? 149 SER   A N     1 
ATOM   1082 C  CA    . SER   A  1 157 ? 21.14900 -82.16700  -10.44100 1.000 77.11088  ? 149 SER   A CA    1 
ATOM   1083 C  C     . SER   A  1 157 ? 20.77000 -81.51800  -11.77300 1.000 70.04900  ? 149 SER   A C     1 
ATOM   1084 O  O     . SER   A  1 157 ? 19.56900 -81.26200  -11.97000 1.000 70.33448  ? 149 SER   A O     1 
ATOM   1085 C  CB    . SER   A  1 157 ? 20.89700 -83.65200  -10.45800 1.000 78.28874  ? 149 SER   A CB    1 
ATOM   1086 O  OG    . SER   A  1 157 ? 19.52300 -83.93600  -10.22600 1.000 80.06770  ? 149 SER   A OG    1 
ATOM   1087 N  N     . MET   A  1 158 ? 21.75400 -81.24700  -12.63400 1.000 63.11790  ? 150 MET   A N     1 
ATOM   1088 C  CA    . MET   A  1 158 ? 21.54000 -80.62000  -13.96700 1.000 61.32397  ? 150 MET   A CA    1 
ATOM   1089 C  C     . MET   A  1 158 ? 21.28200 -81.71300  -15.01100 1.000 61.10987  ? 150 MET   A C     1 
ATOM   1090 O  O     . MET   A  1 158 ? 21.85800 -82.81100  -14.88800 1.000 60.32818  ? 150 MET   A O     1 
ATOM   1091 C  CB    . MET   A  1 158 ? 22.75000 -79.78300  -14.39600 1.000 59.99661  ? 150 MET   A CB    1 
ATOM   1092 C  CG    . MET   A  1 158 ? 22.83400 -78.42500  -13.71600 1.000 65.61538  ? 150 MET   A CG    1 
ATOM   1093 S  SD    . MET   A  1 158 ? 21.33000 -77.41500  -13.87300 1.000 64.03218  ? 150 MET   A SD    1 
ATOM   1094 C  CE    . MET   A  1 158 ? 21.04500 -77.48600  -15.64000 1.000 58.70517  ? 150 MET   A CE    1 
ATOM   1095 N  N     . PHE   A  1 159 ? 20.43700 -81.40800  -15.99800 1.000 60.67925  ? 151 PHE   A N     1 
ATOM   1096 C  CA    . PHE   A  1 159 ? 20.12700 -82.28000  -17.15900 1.000 57.66657  ? 151 PHE   A CA    1 
ATOM   1097 C  C     . PHE   A  1 159 ? 20.45900 -81.51000  -18.43700 1.000 53.10170  ? 151 PHE   A C     1 
ATOM   1098 O  O     . PHE   A  1 159 ? 19.67300 -80.63500  -18.83100 1.000 56.59159  ? 151 PHE   A O     1 
ATOM   1099 C  CB    . PHE   A  1 159 ? 18.67300 -82.75100  -17.09400 1.000 53.86242  ? 151 PHE   A CB    1 
ATOM   1100 C  CG    . PHE   A  1 159 ? 18.35700 -83.50400  -15.82800 1.000 58.20911  ? 151 PHE   A CG    1 
ATOM   1101 C  CD1   . PHE   A  1 159 ? 18.82200 -84.79600  -15.64300 1.000 55.48645  ? 151 PHE   A CD1   1 
ATOM   1102 C  CD2   . PHE   A  1 159 ? 17.63700 -82.90600  -14.80400 1.000 57.71459  ? 151 PHE   A CD2   1 
ATOM   1103 C  CE1   . PHE   A  1 159 ? 18.54900 -85.48300  -14.47200 1.000 61.12319  ? 151 PHE   A CE1   1 
ATOM   1104 C  CE2   . PHE   A  1 159 ? 17.36500 -83.59500  -13.63300 1.000 54.77779  ? 151 PHE   A CE2   1 
ATOM   1105 C  CZ    . PHE   A  1 159 ? 17.82300 -84.88100  -13.47000 1.000 62.09604  ? 151 PHE   A CZ    1 
ATOM   1106 N  N     . TRP   A  1 160 ? 21.62400 -81.80200  -19.01800 1.000 52.78446  ? 152 TRP   A N     1 
ATOM   1107 C  CA    . TRP   A  1 160 ? 22.10000 -81.23300  -20.30500 1.000 55.89524  ? 152 TRP   A CA    1 
ATOM   1108 C  C     . TRP   A  1 160 ? 21.41300 -81.96000  -21.46400 1.000 53.73077  ? 152 TRP   A C     1 
ATOM   1109 O  O     . TRP   A  1 160 ? 21.77700 -83.11900  -21.72300 1.000 55.16496  ? 152 TRP   A O     1 
ATOM   1110 C  CB    . TRP   A  1 160 ? 23.62600 -81.34100  -20.40100 1.000 53.01781  ? 152 TRP   A CB    1 
ATOM   1111 C  CG    . TRP   A  1 160 ? 24.37100 -80.48800  -19.42200 1.000 56.26772  ? 152 TRP   A CG    1 
ATOM   1112 C  CD1   . TRP   A  1 160 ? 23.86100 -79.51200  -18.61400 1.000 54.81829  ? 152 TRP   A CD1   1 
ATOM   1113 C  CD2   . TRP   A  1 160 ? 25.78900 -80.50800  -19.17900 1.000 56.53918  ? 152 TRP   A CD2   1 
ATOM   1114 N  NE1   . TRP   A  1 160 ? 24.85900 -78.93900  -17.87300 1.000 56.43481  ? 152 TRP   A NE1   1 
ATOM   1115 C  CE2   . TRP   A  1 160 ? 26.05300 -79.52500  -18.20100 1.000 55.79839  ? 152 TRP   A CE2   1 
ATOM   1116 C  CE3   . TRP   A  1 160 ? 26.85500 -81.26100  -19.68300 1.000 53.61111  ? 152 TRP   A CE3   1 
ATOM   1117 C  CZ2   . TRP   A  1 160 ? 27.33900 -79.28000  -17.72500 1.000 59.18426  ? 152 TRP   A CZ2   1 
ATOM   1118 C  CZ3   . TRP   A  1 160 ? 28.12500 -81.01800  -19.21000 1.000 54.93949  ? 152 TRP   A CZ3   1 
ATOM   1119 C  CH2   . TRP   A  1 160 ? 28.36200 -80.03900  -18.24600 1.000 58.60930  ? 152 TRP   A CH2   1 
ATOM   1120 N  N     . MET   A  1 161 ? 20.44900 -81.31000  -22.12200 1.000 50.54412  ? 153 MET   A N     1 
ATOM   1121 C  CA    . MET   A  1 161 ? 19.76700 -81.85100  -23.32900 1.000 53.53964  ? 153 MET   A CA    1 
ATOM   1122 C  C     . MET   A  1 161 ? 20.68200 -81.65100  -24.54200 1.000 52.67397  ? 153 MET   A C     1 
ATOM   1123 O  O     . MET   A  1 161 ? 20.95300 -80.48800  -24.89600 1.000 51.21136  ? 153 MET   A O     1 
ATOM   1124 C  CB    . MET   A  1 161 ? 18.42100 -81.16000  -23.57300 1.000 56.51481  ? 153 MET   A CB    1 
ATOM   1125 C  CG    . MET   A  1 161 ? 17.47000 -81.24300  -22.38800 1.000 55.75739  ? 153 MET   A CG    1 
ATOM   1126 S  SD    . MET   A  1 161 ? 17.32200 -82.91300  -21.71000 1.000 50.86291  ? 153 MET   A SD    1 
ATOM   1127 C  CE    . MET   A  1 161 ? 16.72700 -83.81200  -23.14200 1.000 54.00780  ? 153 MET   A CE    1 
ATOM   1128 N  N     . ARG   A  1 162 ? 21.16200 -82.75100  -25.13100 1.000 54.37359  ? 154 ARG   A N     1 
ATOM   1129 C  CA    . ARG   A  1 162 ? 22.05500 -82.74900  -26.32100 1.000 54.36215  ? 154 ARG   A CA    1 
ATOM   1130 C  C     . ARG   A  1 162 ? 21.20600 -82.45000  -27.56200 1.000 52.17697  ? 154 ARG   A C     1 
ATOM   1131 O  O     . ARG   A  1 162 ? 20.41200 -83.32600  -27.96300 1.000 53.09821  ? 154 ARG   A O     1 
ATOM   1132 C  CB    . ARG   A  1 162 ? 22.79500 -84.08700  -26.42800 1.000 53.73376  ? 154 ARG   A CB    1 
ATOM   1133 C  CG    . ARG   A  1 162 ? 24.02600 -84.05500  -27.32000 1.000 54.25825  ? 154 ARG   A CG    1 
ATOM   1134 C  CD    . ARG   A  1 162 ? 24.95800 -85.21600  -27.02900 1.000 58.98621  ? 154 ARG   A CD    1 
ATOM   1135 N  NE    . ARG   A  1 162 ? 26.14600 -85.19600  -27.87300 1.000 60.19077  ? 154 ARG   A NE    1 
ATOM   1136 C  CZ    . ARG   A  1 162 ? 27.23100 -85.94200  -27.68400 1.000 63.63304  ? 154 ARG   A CZ    1 
ATOM   1137 N  NH1   . ARG   A  1 162 ? 27.29700 -86.78600  -26.66600 1.000 66.04453  ? 154 ARG   A NH1   1 
ATOM   1138 N  NH2   . ARG   A  1 162 ? 28.25300 -85.83600  -28.51700 1.000 57.95111  ? 154 ARG   A NH2   1 
ATOM   1139 N  N     . VAL   A  1 163 ? 21.34700 -81.24000  -28.11400 1.000 52.03713  ? 155 VAL   A N     1 
ATOM   1140 C  CA    . VAL   A  1 163 ? 20.61200 -80.75700  -29.32000 1.000 51.75341  ? 155 VAL   A CA    1 
ATOM   1141 C  C     . VAL   A  1 163 ? 21.64200 -80.37100  -30.37600 1.000 55.43456  ? 155 VAL   A C     1 
ATOM   1142 O  O     . VAL   A  1 163 ? 22.61900 -79.69200  -30.06500 1.000 51.58543  ? 155 VAL   A O     1 
ATOM   1143 C  CB    . VAL   A  1 163 ? 19.69100 -79.56300  -29.00400 1.000 52.35241  ? 155 VAL   A CB    1 
ATOM   1144 C  CG1   . VAL   A  1 163 ? 18.63300 -79.38200  -30.08000 1.000 58.03760  ? 155 VAL   A CG1   1 
ATOM   1145 C  CG2   . VAL   A  1 163 ? 19.03900 -79.68700  -27.64000 1.000 56.37270  ? 155 VAL   A CG2   1 
ATOM   1146 N  N     . PRO   A  1 164 ? 21.46200 -80.79200  -31.65000 1.000 57.16017  ? 156 PRO   A N     1 
ATOM   1147 C  CA    . PRO   A  1 164 ? 22.36100 -80.38300  -32.72400 1.000 53.06763  ? 156 PRO   A CA    1 
ATOM   1148 C  C     . PRO   A  1 164 ? 21.94700 -79.02900  -33.31900 1.000 54.95480  ? 156 PRO   A C     1 
ATOM   1149 O  O     . PRO   A  1 164 ? 20.76300 -78.78000  -33.45200 1.000 56.53812  ? 156 PRO   A O     1 
ATOM   1150 C  CB    . PRO   A  1 164 ? 22.20900 -81.53000  -33.73000 1.000 56.09253  ? 156 PRO   A CB    1 
ATOM   1151 C  CG    . PRO   A  1 164 ? 20.76800 -81.97800  -33.56900 1.000 55.61827  ? 156 PRO   A CG    1 
ATOM   1152 C  CD    . PRO   A  1 164 ? 20.40500 -81.69900  -32.12400 1.000 52.69457  ? 156 PRO   A CD    1 
ATOM   1153 N  N     . LEU   A  1 165 ? 22.93100 -78.19100  -33.65500 1.000 56.53731  ? 157 LEU   A N     1 
ATOM   1154 C  CA    . LEU   A  1 165 ? 22.72300 -76.88100  -34.32800 1.000 55.38051  ? 157 LEU   A CA    1 
ATOM   1155 C  C     . LEU   A  1 165 ? 22.02800 -77.13100  -35.67300 1.000 60.26607  ? 157 LEU   A C     1 
ATOM   1156 O  O     . LEU   A  1 165 ? 21.19900 -76.29000  -36.07300 1.000 62.98345  ? 157 LEU   A O     1 
ATOM   1157 C  CB    . LEU   A  1 165 ? 24.08500 -76.19600  -34.49500 1.000 55.76141  ? 157 LEU   A CB    1 
ATOM   1158 C  CG    . LEU   A  1 165 ? 24.08300 -74.68400  -34.72300 1.000 55.48391  ? 157 LEU   A CG    1 
ATOM   1159 C  CD1   . LEU   A  1 165 ? 22.99200 -73.98200  -33.92500 1.000 62.12512  ? 157 LEU   A CD1   1 
ATOM   1160 C  CD2   . LEU   A  1 165 ? 25.44400 -74.10200  -34.37400 1.000 60.70284  ? 157 LEU   A CD2   1 
ATOM   1161 N  N     . VAL   A  1 166 ? 22.35500 -78.26000  -36.31900 1.000 56.88153  ? 158 VAL   A N     1 
ATOM   1162 C  CA    . VAL   A  1 166 ? 21.70000 -78.79300  -37.55200 1.000 57.78229  ? 158 VAL   A CA    1 
ATOM   1163 C  C     . VAL   A  1 166 ? 21.42700 -80.28800  -37.33800 1.000 58.57125  ? 158 VAL   A C     1 
ATOM   1164 O  O     . VAL   A  1 166 ? 22.36300 -81.00000  -36.92400 1.000 58.57576  ? 158 VAL   A O     1 
ATOM   1165 C  CB    . VAL   A  1 166 ? 22.57500 -78.55000  -38.80000 1.000 59.28668  ? 158 VAL   A CB    1 
ATOM   1166 C  CG1   . VAL   A  1 166 ? 21.91800 -79.06700  -40.07200 1.000 59.17572  ? 158 VAL   A CG1   1 
ATOM   1167 C  CG2   . VAL   A  1 166 ? 22.94600 -77.08300  -38.95400 1.000 58.68671  ? 158 VAL   A CG2   1 
ATOM   1168 N  N     . ALA   A  1 167 ? 20.19800 -80.73900  -37.61600 1.000 57.82955  ? 159 ALA   A N     1 
ATOM   1169 C  CA    . ALA   A  1 167 ? 19.74200 -82.14400  -37.46800 1.000 57.37328  ? 159 ALA   A CA    1 
ATOM   1170 C  C     . ALA   A  1 167 ? 20.53300 -83.04700  -38.41200 1.000 61.06773  ? 159 ALA   A C     1 
ATOM   1171 O  O     . ALA   A  1 167 ? 20.86500 -82.63200  -39.52000 1.000 62.29526  ? 159 ALA   A O     1 
ATOM   1172 C  CB    . ALA   A  1 167 ? 18.26100 -82.24100  -37.74700 1.000 55.74487  ? 159 ALA   A CB    1 
ATOM   1173 N  N     . PRO   A  1 168 ? 20.83800 -84.31100  -38.02400 1.000 64.14333  ? 160 PRO   A N     1 
ATOM   1174 C  CA    . PRO   A  1 168 ? 21.66300 -85.19400  -38.85200 1.000 63.29293  ? 160 PRO   A CA    1 
ATOM   1175 C  C     . PRO   A  1 168 ? 21.05700 -85.44400  -40.24300 1.000 59.71806  ? 160 PRO   A C     1 
ATOM   1176 O  O     . PRO   A  1 168 ? 21.81300 -85.65000  -41.17700 1.000 61.89791  ? 160 PRO   A O     1 
ATOM   1177 C  CB    . PRO   A  1 168 ? 21.72600 -86.51000  -38.05800 1.000 57.96770  ? 160 PRO   A CB    1 
ATOM   1178 C  CG    . PRO   A  1 168 ? 21.36900 -86.12200  -36.64400 1.000 56.27552  ? 160 PRO   A CG    1 
ATOM   1179 C  CD    . PRO   A  1 168 ? 20.39800 -84.97000  -36.78400 1.000 61.18516  ? 160 PRO   A CD    1 
ATOM   1180 N  N     . GLU   A  1 169 ? 19.72200 -85.42000  -40.33000 1.000 59.05900  ? 161 GLU   A N     1 
ATOM   1181 C  CA    . GLU   A  1 169 ? 18.93400 -85.60000  -41.58000 1.000 60.36469  ? 161 GLU   A CA    1 
ATOM   1182 C  C     . GLU   A  1 169 ? 19.25000 -84.47400  -42.57300 1.000 61.41636  ? 161 GLU   A C     1 
ATOM   1183 O  O     . GLU   A  1 169 ? 19.22600 -84.74700  -43.78000 1.000 65.60888  ? 161 GLU   A O     1 
ATOM   1184 C  CB    . GLU   A  1 169 ? 17.43800 -85.62600  -41.25500 1.000 59.96487  ? 161 GLU   A CB    1 
ATOM   1185 C  CG    . GLU   A  1 169 ? 16.54200 -85.83800  -42.46500 1.000 64.88339  ? 161 GLU   A CG    1 
ATOM   1186 C  CD    . GLU   A  1 169 ? 16.76300 -87.15300  -43.19400 1.000 68.94873  ? 161 GLU   A CD    1 
ATOM   1187 O  OE1   . GLU   A  1 169 ? 16.80300 -88.20200  -42.51900 1.000 69.00624  ? 161 GLU   A OE1   1 
ATOM   1188 O  OE2   . GLU   A  1 169 ? 16.90200 -87.12800  -44.43400 1.000 66.08918  ? 161 GLU   A OE2   1 
ATOM   1189 N  N     . ASP   A  1 170 ? 19.52600 -83.26200  -42.07900 1.000 62.87176  ? 162 ASP   A N     1 
ATOM   1190 C  CA    . ASP   A  1 170 ? 19.65800 -82.02100  -42.89000 1.000 61.79595  ? 162 ASP   A CA    1 
ATOM   1191 C  C     . ASP   A  1 170 ? 21.13400 -81.69300  -43.15600 1.000 62.53273  ? 162 ASP   A C     1 
ATOM   1192 O  O     . ASP   A  1 170 ? 21.38800 -80.60000  -43.70600 1.000 64.28289  ? 162 ASP   A O     1 
ATOM   1193 C  CB    . ASP   A  1 170 ? 18.97500 -80.83700  -42.19900 1.000 60.84594  ? 162 ASP   A CB    1 
ATOM   1194 C  CG    . ASP   A  1 170 ? 17.52900 -81.08900  -41.80200 1.000 61.30393  ? 162 ASP   A CG    1 
ATOM   1195 O  OD1   . ASP   A  1 170 ? 16.81400 -81.75800  -42.57000 1.000 62.51104  ? 162 ASP   A OD1   1 
ATOM   1196 O  OD2   . ASP   A  1 170 ? 17.12800 -80.60900  -40.72200 1.000 70.23837  ? 162 ASP   A OD2   1 
ATOM   1197 N  N     . LEU   A  1 171 ? 22.07000 -82.57100  -42.77400 1.000 62.33229  ? 163 LEU   A N     1 
ATOM   1198 C  CA    . LEU   A  1 171 ? 23.51600 -82.43700  -43.11900 1.000 63.46206  ? 163 LEU   A CA    1 
ATOM   1199 C  C     . LEU   A  1 171 ? 24.05500 -83.74700  -43.71100 1.000 64.51214  ? 163 LEU   A C     1 
ATOM   1200 O  O     . LEU   A  1 171 ? 25.28500 -83.83200  -43.90900 1.000 65.55024  ? 163 LEU   A O     1 
ATOM   1201 C  CB    . LEU   A  1 171 ? 24.31100 -82.00600  -41.87900 1.000 62.36766  ? 163 LEU   A CB    1 
ATOM   1202 C  CG    . LEU   A  1 171 ? 24.31600 -82.97200  -40.69200 1.000 60.97542  ? 163 LEU   A CG    1 
ATOM   1203 C  CD1   . LEU   A  1 171 ? 25.43500 -83.99900  -40.80800 1.000 63.18599  ? 163 LEU   A CD1   1 
ATOM   1204 C  CD2   . LEU   A  1 171 ? 24.45100 -82.20800  -39.38300 1.000 62.95574  ? 163 LEU   A CD2   1 
ATOM   1205 N  N     . ARG   A  1 172 ? 23.17800 -84.71200  -44.01000 1.000 64.46709  ? 164 ARG   A N     1 
ATOM   1206 C  CA    . ARG   A  1 172 ? 23.55200 -86.01300  -44.62800 1.000 65.56610  ? 164 ARG   A CA    1 
ATOM   1207 C  C     . ARG   A  1 172 ? 24.12100 -85.75000  -46.02600 1.000 67.76153  ? 164 ARG   A C     1 
ATOM   1208 O  O     . ARG   A  1 172 ? 23.67100 -84.78000  -46.67300 1.000 71.97017  ? 164 ARG   A O     1 
ATOM   1209 C  CB    . ARG   A  1 172 ? 22.35000 -86.96400  -44.67600 1.000 65.21166  ? 164 ARG   A CB    1 
ATOM   1210 C  CG    . ARG   A  1 172 ? 21.24200 -86.54800  -45.63300 1.000 66.06592  ? 164 ARG   A CG    1 
ATOM   1211 C  CD    . ARG   A  1 172 ? 20.02300 -87.44800  -45.52600 1.000 66.34208  ? 164 ARG   A CD    1 
ATOM   1212 N  NE    . ARG   A  1 172 ? 18.96000 -87.04300  -46.43900 1.000 70.52076  ? 164 ARG   A NE    1 
ATOM   1213 C  CZ    . ARG   A  1 172 ? 18.94700 -87.26900  -47.75300 1.000 75.18913  ? 164 ARG   A CZ    1 
ATOM   1214 N  NH1   . ARG   A  1 172 ? 19.94800 -87.90600  -48.33900 1.000 73.40279  ? 164 ARG   A NH1   1 
ATOM   1215 N  NH2   . ARG   A  1 172 ? 17.92700 -86.84700  -48.48300 1.000 69.92266  ? 164 ARG   A NH2   1 
ATOM   1216 N  N     . ASP   A  1 173 ? 25.08000 -86.57300  -46.46000 1.000 71.57074  ? 165 ASP   A N     1 
ATOM   1217 C  CA    . ASP   A  1 173 ? 25.67400 -86.52600  -47.82300 1.000 71.39378  ? 165 ASP   A CA    1 
ATOM   1218 C  C     . ASP   A  1 173 ? 24.55800 -86.76300  -48.84600 1.000 72.27536  ? 165 ASP   A C     1 
ATOM   1219 O  O     . ASP   A  1 173 ? 23.68900 -87.62000  -48.58100 1.000 71.44240  ? 165 ASP   A O     1 
ATOM   1220 C  CB    . ASP   A  1 173 ? 26.80600 -87.54700  -47.98100 1.000 72.52165  ? 165 ASP   A CB    1 
ATOM   1221 C  CG    . ASP   A  1 173 ? 28.04600 -87.23700  -47.15700 1.000 74.91129  ? 165 ASP   A CG    1 
ATOM   1222 O  OD1   . ASP   A  1 173 ? 28.15800 -86.09400  -46.66900 1.000 78.72440  ? 165 ASP   A OD1   1 
ATOM   1223 O  OD2   . ASP   A  1 173 ? 28.89300 -88.14200  -47.00900 1.000 74.46071  ? 165 ASP   A OD2   1 
ATOM   1224 N  N     . ASP   A  1 174 ? 24.58000 -86.01900  -49.95800 1.000 74.10351  ? 166 ASP   A N     1 
ATOM   1225 C  CA    . ASP   A  1 174 ? 23.57300 -86.10100  -51.05100 1.000 75.43828  ? 166 ASP   A CA    1 
ATOM   1226 C  C     . ASP   A  1 174 ? 23.91800 -87.30700  -51.93100 1.000 77.11611  ? 166 ASP   A C     1 
ATOM   1227 O  O     . ASP   A  1 174 ? 24.23800 -87.10300  -53.12300 1.000 81.79309  ? 166 ASP   A O     1 
ATOM   1228 C  CB    . ASP   A  1 174 ? 23.51400 -84.78900  -51.84100 1.000 76.95925  ? 166 ASP   A CB    1 
ATOM   1229 C  CG    . ASP   A  1 174 ? 22.37100 -84.70800  -52.84100 1.000 80.39243  ? 166 ASP   A CG    1 
ATOM   1230 O  OD1   . ASP   A  1 174 ? 21.43500 -85.52800  -52.73400 1.000 78.84356  ? 166 ASP   A OD1   1 
ATOM   1231 O  OD2   . ASP   A  1 174 ? 22.42400 -83.82000  -53.71600 1.000 80.27013  ? 166 ASP   A OD2   1 
ATOM   1232 N  N     . ILE   A  1 175 ? 23.84800 -88.51500  -51.35700 1.000 76.10265  ? 167 ILE   A N     1 
ATOM   1233 C  CA    . ILE   A  1 175 ? 24.36900 -89.77700  -51.96600 1.000 77.51224  ? 167 ILE   A CA    1 
ATOM   1234 C  C     . ILE   A  1 175 ? 23.28100 -90.86200  -51.99800 1.000 77.19887  ? 167 ILE   A C     1 
ATOM   1235 O  O     . ILE   A  1 175 ? 23.61200 -91.99800  -52.39000 1.000 78.21852  ? 167 ILE   A O     1 
ATOM   1236 C  CB    . ILE   A  1 175 ? 25.64200 -90.24300  -51.22700 1.000 77.06989  ? 167 ILE   A CB    1 
ATOM   1237 C  CG1   . ILE   A  1 175 ? 25.39200 -90.49100  -49.73600 1.000 74.57043  ? 167 ILE   A CG1   1 
ATOM   1238 C  CG2   . ILE   A  1 175 ? 26.77400 -89.25200  -51.45400 1.000 78.13878  ? 167 ILE   A CG2   1 
ATOM   1239 C  CD1   . ILE   A  1 175 ? 26.55600 -91.12900  -49.01000 1.000 74.40340  ? 167 ILE   A CD1   1 
ATOM   1240 N  N     . ILE   A  1 176 ? 22.03800 -90.53600  -51.62500 1.000 76.06534  ? 168 ILE   A N     1 
ATOM   1241 C  CA    . ILE   A  1 176 ? 20.85100 -91.43100  -51.78800 1.000 76.21877  ? 168 ILE   A CA    1 
ATOM   1242 C  C     . ILE   A  1 176 ? 20.13200 -91.02500  -53.08200 1.000 85.47117  ? 168 ILE   A C     1 
ATOM   1243 O  O     . ILE   A  1 176 ? 19.50400 -89.94700  -53.09600 1.000 84.59490  ? 168 ILE   A O     1 
ATOM   1244 C  CB    . ILE   A  1 176 ? 19.93000 -91.37800  -50.55200 1.000 74.04314  ? 168 ILE   A CB    1 
ATOM   1245 C  CG1   . ILE   A  1 176 ? 20.67300 -91.80700  -49.28200 1.000 79.29161  ? 168 ILE   A CG1   1 
ATOM   1246 C  CG2   . ILE   A  1 176 ? 18.67700 -92.21400  -50.77400 1.000 74.57102  ? 168 ILE   A CG2   1 
ATOM   1247 C  CD1   . ILE   A  1 176 ? 19.95100 -91.47900  -47.99200 1.000 72.74354  ? 168 ILE   A CD1   1 
ATOM   1248 N  N     . GLU   A  1 177 ? 20.22000 -91.87600  -54.11200 1.000 81.32937  ? 169 GLU   A N     1 
ATOM   1249 C  CA    . GLU   A  1 177 ? 19.81900 -91.59400  -55.52000 1.000 82.85903  ? 169 GLU   A CA    1 
ATOM   1250 C  C     . GLU   A  1 177 ? 18.32600 -91.24400  -55.60800 1.000 84.38810  ? 169 GLU   A C     1 
ATOM   1251 O  O     . GLU   A  1 177 ? 18.00000 -90.28400  -56.33100 1.000 88.42724  ? 169 GLU   A O     1 
ATOM   1252 C  CB    . GLU   A  1 177 ? 20.17800 -92.79500  -56.40100 1.000 84.79101  ? 169 GLU   A CB    1 
ATOM   1253 C  CG    . GLU   A  1 177 ? 19.45200 -92.83200  -57.73600 1.000 90.23159  ? 169 GLU   A CG    1 
ATOM   1254 C  CD    . GLU   A  1 177 ? 18.09400 -93.51600  -57.71300 1.000 96.52281  ? 169 GLU   A CD    1 
ATOM   1255 O  OE1   . GLU   A  1 177 ? 17.94800 -94.53200  -56.99100 1.000 86.36944  ? 169 GLU   A OE1   1 
ATOM   1256 O  OE2   . GLU   A  1 177 ? 17.18300 -93.03400  -58.42400 1.000 100.54864 ? 169 GLU   A OE2   1 
ATOM   1257 N  N     . ASN   A  1 178 ? 17.46100 -91.99000  -54.90800 1.000 84.71765  ? 170 ASN   A N     1 
ATOM   1258 C  CA    . ASN   A  1 178 ? 15.97700 -91.90300  -55.02300 1.000 82.36913  ? 170 ASN   A CA    1 
ATOM   1259 C  C     . ASN   A  1 178 ? 15.38600 -91.06500  -53.87800 1.000 85.36485  ? 170 ASN   A C     1 
ATOM   1260 O  O     . ASN   A  1 178 ? 14.15500 -91.13500  -53.67800 1.000 86.91897  ? 170 ASN   A O     1 
ATOM   1261 C  CB    . ASN   A  1 178 ? 15.33700 -93.29500  -55.07000 1.000 85.64988  ? 170 ASN   A CB    1 
ATOM   1262 C  CG    . ASN   A  1 178 ? 15.67000 -94.15700  -53.87000 1.000 89.45785  ? 170 ASN   A CG    1 
ATOM   1263 O  OD1   . ASN   A  1 178 ? 16.41900 -93.74700  -52.98500 1.000 89.06801  ? 170 ASN   A OD1   1 
ATOM   1264 N  ND2   . ASN   A  1 178 ? 15.12700 -95.36300  -53.83300 1.000 87.02404  ? 170 ASN   A ND2   1 
ATOM   1265 N  N     . ALA   A  1 179 ? 16.22000 -90.30400  -53.15800 1.000 80.89825  ? 171 ALA   A N     1 
ATOM   1266 C  CA    . ALA   A  1 179 ? 15.81000 -89.37600  -52.07700 1.000 80.72281  ? 171 ALA   A CA    1 
ATOM   1267 C  C     . ALA   A  1 179 ? 16.88200 -88.30200  -51.90400 1.000 79.85694  ? 171 ALA   A C     1 
ATOM   1268 O  O     . ALA   A  1 179 ? 17.75200 -88.41700  -51.04300 1.000 79.60640  ? 171 ALA   A O     1 
ATOM   1269 C  CB    . ALA   A  1 179 ? 15.57300 -90.14300  -50.80000 1.000 84.07488  ? 171 ALA   A CB    1 
ATOM   1270 N  N     . PRO   A  1 180 ? 16.86500 -87.23000  -52.72900 1.000 85.23086  ? 172 PRO   A N     1 
ATOM   1271 C  CA    . PRO   A  1 180 ? 17.92000 -86.22100  -52.70300 1.000 82.30317  ? 172 PRO   A CA    1 
ATOM   1272 C  C     . PRO   A  1 180 ? 17.66900 -85.15200  -51.62900 1.000 80.60119  ? 172 PRO   A C     1 
ATOM   1273 O  O     . PRO   A  1 180 ? 16.52100 -84.92300  -51.28800 1.000 80.83167  ? 172 PRO   A O     1 
ATOM   1274 C  CB    . PRO   A  1 180 ? 17.87500 -85.63000  -54.12200 1.000 80.05215  ? 172 PRO   A CB    1 
ATOM   1275 C  CG    . PRO   A  1 180 ? 16.45200 -85.86400  -54.61800 1.000 81.21367  ? 172 PRO   A CG    1 
ATOM   1276 C  CD    . PRO   A  1 180 ? 15.83300 -86.92800  -53.73100 1.000 84.17347  ? 172 PRO   A CD    1 
ATOM   1277 N  N     . THR   A  1 181 ? 18.74800 -84.54400  -51.12400 1.000 81.97464  ? 173 THR   A N     1 
ATOM   1278 C  CA    . THR   A  1 181 ? 18.72000 -83.40900  -50.16300 1.000 88.32669  ? 173 THR   A CA    1 
ATOM   1279 C  C     . THR   A  1 181 ? 18.21600 -82.16900  -50.91100 1.000 100.79377 ? 173 THR   A C     1 
ATOM   1280 O  O     . THR   A  1 181 ? 18.87600 -81.77500  -51.89100 1.000 109.97897 ? 173 THR   A O     1 
ATOM   1281 C  CB    . THR   A  1 181 ? 20.09500 -83.17800  -49.51700 1.000 85.72716  ? 173 THR   A CB    1 
ATOM   1282 O  OG1   . THR   A  1 181 ? 21.03500 -82.79600  -50.52000 1.000 82.38293  ? 173 THR   A OG1   1 
ATOM   1283 C  CG2   . THR   A  1 181 ? 20.62000 -84.39600  -48.78800 1.000 77.71006  ? 173 THR   A CG2   1 
ATOM   1284 N  N     . THR   A  1 182 ? 17.08100 -81.60600  -50.48300 1.000 104.26452 ? 174 THR   A N     1 
ATOM   1285 C  CA    . THR   A  1 182 ? 16.38600 -80.46900  -51.15000 1.000 114.54523 ? 174 THR   A CA    1 
ATOM   1286 C  C     . THR   A  1 182 ? 17.36500 -79.29900  -51.32800 1.000 122.57943 ? 174 THR   A C     1 
ATOM   1287 O  O     . THR   A  1 182 ? 17.98500 -78.89500  -50.32200 1.000 119.24840 ? 174 THR   A O     1 
ATOM   1288 C  CB    . THR   A  1 182 ? 15.13000 -80.04900  -50.37000 1.000 117.93346 ? 174 THR   A CB    1 
ATOM   1289 O  OG1   . THR   A  1 182 ? 15.46000 -79.93100  -48.98500 1.000 102.66477 ? 174 THR   A OG1   1 
ATOM   1290 C  CG2   . THR   A  1 182 ? 13.98700 -81.02800  -50.53600 1.000 118.49103 ? 174 THR   A CG2   1 
ATOM   1291 N  N     . HIS   A  1 183 ? 17.48600 -78.78200  -52.55900 1.000 131.34936 ? 175 HIS   A N     1 
ATOM   1292 C  CA    . HIS   A  1 183 ? 18.37700 -77.64700  -52.93200 1.000 129.72031 ? 175 HIS   A CA    1 
ATOM   1293 C  C     . HIS   A  1 183 ? 17.62800 -76.31400  -52.77800 1.000 138.73887 ? 175 HIS   A C     1 
ATOM   1294 O  O     . HIS   A  1 183 ? 18.02300 -75.33500  -53.45400 1.000 142.17981 ? 175 HIS   A O     1 
ATOM   1295 C  CB    . HIS   A  1 183 ? 18.91000 -77.79900  -54.36900 1.000 137.04565 ? 175 HIS   A CB    1 
ATOM   1296 C  CG    . HIS   A  1 183 ? 19.33600 -79.17900  -54.74900 1.000 144.84793 ? 175 HIS   A CG    1 
ATOM   1297 N  ND1   . HIS   A  1 183 ? 20.01400 -80.01700  -53.88100 1.000 139.53974 ? 175 HIS   A ND1   1 
ATOM   1298 C  CD2   . HIS   A  1 183 ? 19.21000 -79.85600  -55.91400 1.000 142.74209 ? 175 HIS   A CD2   1 
ATOM   1299 C  CE1   . HIS   A  1 183 ? 20.27000 -81.16000  -54.48800 1.000 139.54326 ? 175 HIS   A CE1   1 
ATOM   1300 N  NE2   . HIS   A  1 183 ? 19.78800 -81.08600  -55.74000 1.000 145.04109 ? 175 HIS   A NE2   1 
ATOM   1301 N  N     . THR   A  1 184 ? 16.58000 -76.28100  -51.94400 1.000 122.41226 ? 176 THR   A N     1 
ATOM   1302 C  CA    . THR   A  1 184 ? 15.75500 -75.07900  -51.64700 1.000 116.40252 ? 176 THR   A CA    1 
ATOM   1303 C  C     . THR   A  1 184 ? 15.95100 -74.69700  -50.17700 1.000 114.34243 ? 176 THR   A C     1 
ATOM   1304 O  O     . THR   A  1 184 ? 16.34100 -75.57900  -49.38600 1.000 115.27421 ? 176 THR   A O     1 
ATOM   1305 C  CB    . THR   A  1 184 ? 14.27400 -75.32300  -51.96800 1.000 112.85870 ? 176 THR   A CB    1 
ATOM   1306 O  OG1   . THR   A  1 184 ? 13.84500 -76.47800  -51.24400 1.000 113.93924 ? 176 THR   A OG1   1 
ATOM   1307 C  CG2   . THR   A  1 184 ? 14.01600 -75.51600  -53.44700 1.000 104.96447 ? 176 THR   A CG2   1 
ATOM   1308 N  N     . GLU   A  1 185 ? 15.69500 -73.43000  -49.83600 1.000 110.27650 ? 177 GLU   A N     1 
ATOM   1309 C  CA    . GLU   A  1 185 ? 15.80500 -72.89900  -48.45100 1.000 103.72764 ? 177 GLU   A CA    1 
ATOM   1310 C  C     . GLU   A  1 185 ? 14.43000 -72.97800  -47.77600 1.000 103.75382 ? 177 GLU   A C     1 
ATOM   1311 O  O     . GLU   A  1 185 ? 13.46000 -72.43900  -48.34800 1.000 105.03956 ? 177 GLU   A O     1 
ATOM   1312 C  CB    . GLU   A  1 185 ? 16.32600 -71.46100  -48.45400 1.000 100.01465 ? 177 GLU   A CB    1 
ATOM   1313 C  CG    . GLU   A  1 185 ? 16.93900 -71.04200  -47.12700 1.000 99.08176  ? 177 GLU   A CG    1 
ATOM   1314 C  CD    . GLU   A  1 185 ? 16.96800 -69.54500  -46.86500 1.000 103.83839 ? 177 GLU   A CD    1 
ATOM   1315 O  OE1   . GLU   A  1 185 ? 16.85000 -68.76900  -47.83700 1.000 106.55941 ? 177 GLU   A OE1   1 
ATOM   1316 O  OE2   . GLU   A  1 185 ? 17.11400 -69.15600  -45.68800 1.000 102.24424 ? 177 GLU   A OE2   1 
ATOM   1317 N  N     . GLU   A  1 186 ? 14.36200 -73.64800  -46.62100 1.000 97.06777  ? 178 GLU   A N     1 
ATOM   1318 C  CA    . GLU   A  1 186 ? 13.17900 -73.69500  -45.72000 1.000 89.68322  ? 178 GLU   A CA    1 
ATOM   1319 C  C     . GLU   A  1 186 ? 13.55500 -72.98300  -44.41800 1.000 84.43590  ? 178 GLU   A C     1 
ATOM   1320 O  O     . GLU   A  1 186 ? 14.14000 -73.63700  -43.53300 1.000 84.49584  ? 178 GLU   A O     1 
ATOM   1321 C  CB    . GLU   A  1 186 ? 12.74500 -75.14300  -45.48300 1.000 89.29900  ? 178 GLU   A CB    1 
ATOM   1322 C  CG    . GLU   A  1 186 ? 11.98300 -75.74100  -46.65300 1.000 101.76591 ? 178 GLU   A CG    1 
ATOM   1323 C  CD    . GLU   A  1 186 ? 12.20400 -77.22800  -46.87900 1.000 106.46994 ? 178 GLU   A CD    1 
ATOM   1324 O  OE1   . GLU   A  1 186 ? 12.57800 -77.92900  -45.91100 1.000 97.58673  ? 178 GLU   A OE1   1 
ATOM   1325 O  OE2   . GLU   A  1 186 ? 12.00200 -77.68400  -48.02800 1.000 107.72100 ? 178 GLU   A OE2   1 
ATOM   1326 N  N     . TYR   A  1 187 ? 13.24800 -71.68400  -44.33200 1.000 87.33273  ? 179 TYR   A N     1 
ATOM   1327 C  CA    . TYR   A  1 187 ? 13.65400 -70.77100  -43.23200 1.000 83.86470  ? 179 TYR   A CA    1 
ATOM   1328 C  C     . TYR   A  1 187 ? 13.34000 -71.42900  -41.88300 1.000 77.29754  ? 179 TYR   A C     1 
ATOM   1329 O  O     . TYR   A  1 187 ? 14.25800 -71.54700  -41.04800 1.000 74.22195  ? 179 TYR   A O     1 
ATOM   1330 C  CB    . TYR   A  1 187 ? 12.95800 -69.41400  -43.37400 1.000 80.33525  ? 179 TYR   A CB    1 
ATOM   1331 C  CG    . TYR   A  1 187 ? 13.52700 -68.33000  -42.49500 1.000 83.47088  ? 179 TYR   A CG    1 
ATOM   1332 C  CD1   . TYR   A  1 187 ? 14.65000 -67.61400  -42.87900 1.000 80.33350  ? 179 TYR   A CD1   1 
ATOM   1333 C  CD2   . TYR   A  1 187 ? 12.95000 -68.02200  -41.27200 1.000 80.87564  ? 179 TYR   A CD2   1 
ATOM   1334 C  CE1   . TYR   A  1 187 ? 15.18100 -66.61800  -42.07600 1.000 84.84285  ? 179 TYR   A CE1   1 
ATOM   1335 C  CE2   . TYR   A  1 187 ? 13.46900 -67.02800  -40.45700 1.000 73.31076  ? 179 TYR   A CE2   1 
ATOM   1336 C  CZ    . TYR   A  1 187 ? 14.59000 -66.32400  -40.86000 1.000 75.43115  ? 179 TYR   A CZ    1 
ATOM   1337 O  OH    . TYR   A  1 187 ? 15.11100 -65.34400  -40.06600 1.000 76.43399  ? 179 TYR   A OH    1 
ATOM   1338 N  N     . SER   A  1 188 ? 12.08800 -71.86000  -41.69700 1.000 79.34267  ? 180 SER   A N     1 
ATOM   1339 C  CA    . SER   A  1 188 ? 11.57500 -72.50300  -40.45700 1.000 72.34517  ? 180 SER   A CA    1 
ATOM   1340 C  C     . SER   A  1 188 ? 12.10500 -73.93700  -40.34800 1.000 70.65394  ? 180 SER   A C     1 
ATOM   1341 O  O     . SER   A  1 188 ? 12.47300 -74.34200  -39.23000 1.000 68.96568  ? 180 SER   A O     1 
ATOM   1342 C  CB    . SER   A  1 188 ? 10.06900 -72.46400  -40.41300 1.000 68.62148  ? 180 SER   A CB    1 
ATOM   1343 O  OG    . SER   A  1 188 ? 9.60200  -71.12300  -40.42500 1.000 69.96768  ? 180 SER   A OG    1 
ATOM   1344 N  N     . GLY   A  1 189 ? 12.14800 -74.66600  -41.46900 1.000 72.99128  ? 181 GLY   A N     1 
ATOM   1345 C  CA    . GLY   A  1 189 ? 12.66800 -76.04500  -41.55300 1.000 67.04917  ? 181 GLY   A CA    1 
ATOM   1346 C  C     . GLY   A  1 189 ? 14.06900 -76.16400  -40.97500 1.000 67.81887  ? 181 GLY   A C     1 
ATOM   1347 O  O     . GLY   A  1 189 ? 14.32500 -77.14700  -40.25800 1.000 69.15262  ? 181 GLY   A O     1 
ATOM   1348 N  N     . GLU   A  1 190 ? 14.94000 -75.18900  -41.25700 1.000 67.62994  ? 182 GLU   A N     1 
ATOM   1349 C  CA    . GLU   A  1 190 ? 16.36600 -75.17400  -40.82800 1.000 66.85582  ? 182 GLU   A CA    1 
ATOM   1350 C  C     . GLU   A  1 190 ? 16.47800 -74.81100  -39.34000 1.000 69.01010  ? 182 GLU   A C     1 
ATOM   1351 O  O     . GLU   A  1 190 ? 17.61100 -74.85300  -38.81800 1.000 66.84758  ? 182 GLU   A O     1 
ATOM   1352 C  CB    . GLU   A  1 190 ? 17.16400 -74.18800  -41.68500 1.000 71.19563  ? 182 GLU   A CB    1 
ATOM   1353 C  CG    . GLU   A  1 190 ? 17.30200 -74.62000  -43.13600 1.000 75.58935  ? 182 GLU   A CG    1 
ATOM   1354 C  CD    . GLU   A  1 190 ? 17.75200 -73.53300  -44.10000 1.000 85.57946  ? 182 GLU   A CD    1 
ATOM   1355 O  OE1   . GLU   A  1 190 ? 18.11000 -72.43000  -43.63000 1.000 83.76341  ? 182 GLU   A OE1   1 
ATOM   1356 O  OE2   . GLU   A  1 190 ? 17.73900 -73.79100  -45.32200 1.000 84.04183  ? 182 GLU   A OE2   1 
ATOM   1357 N  N     . GLU   A  1 191 ? 15.35800 -74.45800  -38.69300 1.000 68.10947  ? 183 GLU   A N     1 
ATOM   1358 C  CA    . GLU   A  1 191 ? 15.27400 -74.12400  -37.24400 1.000 60.86380  ? 183 GLU   A CA    1 
ATOM   1359 C  C     . GLU   A  1 191 ? 14.55400 -75.24100  -36.47100 1.000 63.85315  ? 183 GLU   A C     1 
ATOM   1360 O  O     . GLU   A  1 191 ? 14.34400 -75.05500  -35.25900 1.000 64.47758  ? 183 GLU   A O     1 
ATOM   1361 C  CB    . GLU   A  1 191 ? 14.51900 -72.80700  -37.03800 1.000 61.80865  ? 183 GLU   A CB    1 
ATOM   1362 C  CG    . GLU   A  1 191 ? 15.14800 -71.61200  -37.73200 1.000 65.50610  ? 183 GLU   A CG    1 
ATOM   1363 C  CD    . GLU   A  1 191 ? 14.35500 -70.32100  -37.59900 1.000 64.94740  ? 183 GLU   A CD    1 
ATOM   1364 O  OE1   . GLU   A  1 191 ? 13.13900 -70.39900  -37.33700 1.000 60.85528  ? 183 GLU   A OE1   1 
ATOM   1365 O  OE2   . GLU   A  1 191 ? 14.95500 -69.23900  -37.74900 1.000 68.86483  ? 183 GLU   A OE2   1 
ATOM   1366 N  N     . LYS   A  1 192 ? 14.19500 -76.35200  -37.12900 1.000 61.97130  ? 184 LYS   A N     1 
ATOM   1367 C  CA    . LYS   A  1 192 ? 13.39400 -77.46000  -36.53100 1.000 58.11366  ? 184 LYS   A CA    1 
ATOM   1368 C  C     . LYS   A  1 192 ? 14.06600 -77.95200  -35.24300 1.000 56.04521  ? 184 LYS   A C     1 
ATOM   1369 O  O     . LYS   A  1 192 ? 13.33700 -78.36000  -34.32000 1.000 55.67771  ? 184 LYS   A O     1 
ATOM   1370 C  CB    . LYS   A  1 192 ? 13.21600 -78.61800  -37.52000 1.000 58.60587  ? 184 LYS   A CB    1 
ATOM   1371 C  CG    . LYS   A  1 192 ? 14.48000 -79.39700  -37.87500 1.000 56.79866  ? 184 LYS   A CG    1 
ATOM   1372 C  CD    . LYS   A  1 192 ? 14.21300 -80.73100  -38.54800 1.000 56.90834  ? 184 LYS   A CD    1 
ATOM   1373 C  CE    . LYS   A  1 192 ? 13.39900 -80.62600  -39.82100 1.000 58.61961  ? 184 LYS   A CE    1 
ATOM   1374 N  NZ    . LYS   A  1 192 ? 14.12200 -79.88900  -40.88300 1.000 59.67436  ? 184 LYS   A NZ    1 
ATOM   1375 N  N     . THR   A  1 193 ? 15.40200 -77.92000  -35.20000 1.000 54.45359  ? 185 THR   A N     1 
ATOM   1376 C  CA    . THR   A  1 193 ? 16.24600 -78.38200  -34.06600 1.000 52.15972  ? 185 THR   A CA    1 
ATOM   1377 C  C     . THR   A  1 193 ? 15.92300 -77.56700  -32.80600 1.000 58.99429  ? 185 THR   A C     1 
ATOM   1378 O  O     . THR   A  1 193 ? 16.04100 -78.12400  -31.69600 1.000 53.22309  ? 185 THR   A O     1 
ATOM   1379 C  CB    . THR   A  1 193 ? 17.73300 -78.30700  -34.43600 1.000 53.98898  ? 185 THR   A CB    1 
ATOM   1380 O  OG1   . THR   A  1 193 ? 18.45500 -79.07000  -33.47200 1.000 53.33628  ? 185 THR   A OG1   1 
ATOM   1381 C  CG2   . THR   A  1 193 ? 18.27300 -76.89300  -34.49100 1.000 59.65279  ? 185 THR   A CG2   1 
ATOM   1382 N  N     . TRP   A  1 194 ? 15.54300 -76.29500  -32.96800 1.000 60.05105  ? 186 TRP   A N     1 
ATOM   1383 C  CA    . TRP   A  1 194 ? 15.15900 -75.38900  -31.85300 1.000 53.75440  ? 186 TRP   A CA    1 
ATOM   1384 C  C     . TRP   A  1 194 ? 13.76600 -75.76000  -31.32600 1.000 53.00494  ? 186 TRP   A C     1 
ATOM   1385 O  O     . TRP   A  1 194 ? 13.57900 -75.70500  -30.09800 1.000 53.65418  ? 186 TRP   A O     1 
ATOM   1386 C  CB    . TRP   A  1 194 ? 15.22600 -73.91800  -32.28500 1.000 55.22139  ? 186 TRP   A CB    1 
ATOM   1387 C  CG    . TRP   A  1 194 ? 14.83800 -72.97600  -31.18900 1.000 59.18802  ? 186 TRP   A CG    1 
ATOM   1388 C  CD1   . TRP   A  1 194 ? 15.66400 -72.38700  -30.27600 1.000 56.09584  ? 186 TRP   A CD1   1 
ATOM   1389 C  CD2   . TRP   A  1 194 ? 13.50600 -72.54600  -30.86000 1.000 54.69895  ? 186 TRP   A CD2   1 
ATOM   1390 N  NE1   . TRP   A  1 194 ? 14.94100 -71.61100  -29.41300 1.000 50.75012  ? 186 TRP   A NE1   1 
ATOM   1391 C  CE2   . TRP   A  1 194 ? 13.61400 -71.68800  -29.74400 1.000 49.87171  ? 186 TRP   A CE2   1 
ATOM   1392 C  CE3   . TRP   A  1 194 ? 12.24000 -72.79800  -31.40000 1.000 52.90036  ? 186 TRP   A CE3   1 
ATOM   1393 C  CZ2   . TRP   A  1 194 ? 12.50100 -71.08100  -29.16600 1.000 51.46306  ? 186 TRP   A CZ2   1 
ATOM   1394 C  CZ3   . TRP   A  1 194 ? 11.14000 -72.20100  -30.82600 1.000 51.45003  ? 186 TRP   A CZ3   1 
ATOM   1395 C  CH2   . TRP   A  1 194 ? 11.27300 -71.35500  -29.72300 1.000 50.70010  ? 186 TRP   A CH2   1 
ATOM   1396 N  N     . MET   A  1 195 ? 12.82500 -76.09700  -32.21700 1.000 52.78462  ? 187 MET   A N     1 
ATOM   1397 C  CA    . MET   A  1 195 ? 11.43600 -76.50300  -31.85900 1.000 52.39465  ? 187 MET   A CA    1 
ATOM   1398 C  C     . MET   A  1 195 ? 11.47800 -77.82000  -31.07200 1.000 54.51425  ? 187 MET   A C     1 
ATOM   1399 O  O     . MET   A  1 195 ? 10.58400 -78.02800  -30.22900 1.000 51.25786  ? 187 MET   A O     1 
ATOM   1400 C  CB    . MET   A  1 195 ? 10.56200 -76.67900  -33.10500 1.000 53.23022  ? 187 MET   A CB    1 
ATOM   1401 C  CG    . MET   A  1 195 ? 9.06800  -76.65000  -32.81700 1.000 56.25957  ? 187 MET   A CG    1 
ATOM   1402 S  SD    . MET   A  1 195 ? 8.48100  -74.99400  -32.34900 1.000 83.90744  ? 187 MET   A SD    1 
ATOM   1403 C  CE    . MET   A  1 195 ? 6.72900  -75.29800  -32.11400 1.000 68.53522  ? 187 MET   A CE    1 
ATOM   1404 N  N     . TRP   A  1 196 ? 12.46600 -78.67800  -31.35300 1.000 51.41664  ? 188 TRP   A N     1 
ATOM   1405 C  CA    . TRP   A  1 196 ? 12.76500 -79.91100  -30.57500 1.000 51.89270  ? 188 TRP   A CA    1 
ATOM   1406 C  C     . TRP   A  1 196 ? 12.97800 -79.52400  -29.10900 1.000 55.08129  ? 188 TRP   A C     1 
ATOM   1407 O  O     . TRP   A  1 196 ? 12.29800 -80.09200  -28.23300 1.000 57.23400  ? 188 TRP   A O     1 
ATOM   1408 C  CB    . TRP   A  1 196 ? 14.00200 -80.62800  -31.13100 1.000 51.80046  ? 188 TRP   A CB    1 
ATOM   1409 C  CG    . TRP   A  1 196 ? 13.82900 -81.26000  -32.47700 1.000 53.10167  ? 188 TRP   A CG    1 
ATOM   1410 C  CD1   . TRP   A  1 196 ? 12.75400 -81.16600  -33.31300 1.000 54.90379  ? 188 TRP   A CD1   1 
ATOM   1411 C  CD2   . TRP   A  1 196 ? 14.80000 -82.06700  -33.16400 1.000 52.29179  ? 188 TRP   A CD2   1 
ATOM   1412 N  NE1   . TRP   A  1 196 ? 12.98200 -81.87500  -34.46200 1.000 53.69209  ? 188 TRP   A NE1   1 
ATOM   1413 C  CE2   . TRP   A  1 196 ? 14.22900 -82.43700  -34.40100 1.000 53.33847  ? 188 TRP   A CE2   1 
ATOM   1414 C  CE3   . TRP   A  1 196 ? 16.08800 -82.51900  -32.85300 1.000 54.37790  ? 188 TRP   A CE3   1 
ATOM   1415 C  CZ2   . TRP   A  1 196 ? 14.90500 -83.23700  -35.32100 1.000 54.06999  ? 188 TRP   A CZ2   1 
ATOM   1416 C  CZ3   . TRP   A  1 196 ? 16.75600 -83.30900  -33.76300 1.000 56.26537  ? 188 TRP   A CZ3   1 
ATOM   1417 C  CH2   . TRP   A  1 196 ? 16.17000 -83.66100  -34.98000 1.000 53.68929  ? 188 TRP   A CH2   1 
ATOM   1418 N  N     . TRP   A  1 197 ? 13.89600 -78.58300  -28.87700 1.000 52.71554  ? 189 TRP   A N     1 
ATOM   1419 C  CA    . TRP   A  1 197 ? 14.27800 -78.06200  -27.53900 1.000 50.54461  ? 189 TRP   A CA    1 
ATOM   1420 C  C     . TRP   A  1 197 ? 13.09300 -77.32800  -26.90200 1.000 51.43334  ? 189 TRP   A C     1 
ATOM   1421 O  O     . TRP   A  1 197 ? 12.80100 -77.59700  -25.72200 1.000 53.44827  ? 189 TRP   A O     1 
ATOM   1422 C  CB    . TRP   A  1 197 ? 15.50500 -77.14800  -27.64300 1.000 48.39632  ? 189 TRP   A CB    1 
ATOM   1423 C  CG    . TRP   A  1 197 ? 15.63500 -76.22300  -26.47500 1.000 48.96255  ? 189 TRP   A CG    1 
ATOM   1424 C  CD1   . TRP   A  1 197 ? 15.41900 -74.87600  -26.46400 1.000 48.86596  ? 189 TRP   A CD1   1 
ATOM   1425 C  CD2   . TRP   A  1 197 ? 15.96300 -76.59000  -25.12500 1.000 47.89665  ? 189 TRP   A CD2   1 
ATOM   1426 N  NE1   . TRP   A  1 197 ? 15.61300 -74.37800  -25.20500 1.000 54.27619  ? 189 TRP   A NE1   1 
ATOM   1427 C  CE2   . TRP   A  1 197 ? 15.94400 -75.40400  -24.36100 1.000 54.37034  ? 189 TRP   A CE2   1 
ATOM   1428 C  CE3   . TRP   A  1 197 ? 16.28200 -77.79600  -24.49100 1.000 51.75967  ? 189 TRP   A CE3   1 
ATOM   1429 C  CZ2   . TRP   A  1 197 ? 16.23100 -75.39200  -22.99700 1.000 50.83993  ? 189 TRP   A CZ2   1 
ATOM   1430 C  CZ3   . TRP   A  1 197 ? 16.56500 -77.78200  -23.14100 1.000 55.39171  ? 189 TRP   A CZ3   1 
ATOM   1431 C  CH2   . TRP   A  1 197 ? 16.53900 -76.59600  -22.40700 1.000 51.24180  ? 189 TRP   A CH2   1 
ATOM   1432 N  N     . HIS   A  1 198 ? 12.45800 -76.42200  -27.64900 1.000 48.77252  ? 190 HIS   A N     1 
ATOM   1433 C  CA    . HIS   A  1 198 ? 11.33000 -75.57900  -27.17200 1.000 50.66927  ? 190 HIS   A CA    1 
ATOM   1434 C  C     . HIS   A  1 198 ? 10.18300 -76.47500  -26.69500 1.000 52.80355  ? 190 HIS   A C     1 
ATOM   1435 O  O     . HIS   A  1 198 ? 9.69100  -76.25300  -25.57300 1.000 54.86119  ? 190 HIS   A O     1 
ATOM   1436 C  CB    . HIS   A  1 198 ? 10.86600 -74.59800  -28.25600 1.000 49.68495  ? 190 HIS   A CB    1 
ATOM   1437 C  CG    . HIS   A  1 198 ? 9.71400  -73.75700  -27.82300 1.000 50.10603  ? 190 HIS   A CG    1 
ATOM   1438 N  ND1   . HIS   A  1 198 ? 9.87100  -72.66300  -26.99800 1.000 49.59541  ? 190 HIS   A ND1   1 
ATOM   1439 C  CD2   . HIS   A  1 198 ? 8.39100  -73.85800  -28.07200 1.000 51.15737  ? 190 HIS   A CD2   1 
ATOM   1440 C  CE1   . HIS   A  1 198 ? 8.69500  -72.11700  -26.76900 1.000 50.27160  ? 190 HIS   A CE1   1 
ATOM   1441 N  NE2   . HIS   A  1 198 ? 7.76900  -72.83000  -27.41900 1.000 51.28853  ? 190 HIS   A NE2   1 
ATOM   1442 N  N     . ASN   A  1 199 ? 9.77900  -77.44700  -27.51500 1.000 51.63432  ? 191 ASN   A N     1 
ATOM   1443 C  CA    . ASN   A  1 199 ? 8.65900  -78.37500  -27.20900 1.000 54.49339  ? 191 ASN   A CA    1 
ATOM   1444 C  C     . ASN   A  1 199 ? 9.01100  -79.19800  -25.96600 1.000 55.39641  ? 191 ASN   A C     1 
ATOM   1445 O  O     . ASN   A  1 199 ? 8.11000  -79.40700  -25.13100 1.000 55.82653  ? 191 ASN   A O     1 
ATOM   1446 C  CB    . ASN   A  1 199 ? 8.30700  -79.26600  -28.40400 1.000 56.50284  ? 191 ASN   A CB    1 
ATOM   1447 C  CG    . ASN   A  1 199 ? 7.48900  -78.54500  -29.45400 1.000 53.16272  ? 191 ASN   A CG    1 
ATOM   1448 O  OD1   . ASN   A  1 199 ? 7.21500  -77.35300  -29.32900 1.000 53.11585  ? 191 ASN   A OD1   1 
ATOM   1449 N  ND2   . ASN   A  1 199 ? 7.08200  -79.26300  -30.48500 1.000 54.97485  ? 191 ASN   A ND2   1 
ATOM   1450 N  N     . PHE   A  1 200 ? 10.27100 -79.62500  -25.83800 1.000 49.93132  ? 192 PHE   A N     1 
ATOM   1451 C  CA    . PHE   A  1 200 ? 10.76400 -80.44800  -24.70200 1.000 52.12022  ? 192 PHE   A CA    1 
ATOM   1452 C  C     . PHE   A  1 200 ? 10.68400 -79.63700  -23.40400 1.000 53.23484  ? 192 PHE   A C     1 
ATOM   1453 O  O     . PHE   A  1 200 ? 9.99100  -80.07300  -22.46600 1.000 54.77298  ? 192 PHE   A O     1 
ATOM   1454 C  CB    . PHE   A  1 200 ? 12.19400 -80.93400  -24.94100 1.000 49.42409  ? 192 PHE   A CB    1 
ATOM   1455 C  CG    . PHE   A  1 200 ? 12.70700 -81.86500  -23.87200 1.000 52.44727  ? 192 PHE   A CG    1 
ATOM   1456 C  CD1   . PHE   A  1 200 ? 12.40900 -83.21800  -23.91100 1.000 53.66754  ? 192 PHE   A CD1   1 
ATOM   1457 C  CD2   . PHE   A  1 200 ? 13.47300 -81.39000  -22.81800 1.000 55.35831  ? 192 PHE   A CD2   1 
ATOM   1458 C  CE1   . PHE   A  1 200 ? 12.87400 -84.07800  -22.92700 1.000 51.98909  ? 192 PHE   A CE1   1 
ATOM   1459 C  CE2   . PHE   A  1 200 ? 13.93600 -82.25100  -21.83500 1.000 56.81167  ? 192 PHE   A CE2   1 
ATOM   1460 C  CZ    . PHE   A  1 200 ? 13.63700 -83.59300  -21.89300 1.000 55.41579  ? 192 PHE   A CZ    1 
ATOM   1461 N  N     . ARG   A  1 201 ? 11.37700 -78.49600  -23.35700 1.000 49.92298  ? 193 ARG   A N     1 
ATOM   1462 C  CA    . ARG   A  1 201 ? 11.49800 -77.64700  -22.14100 1.000 52.11029  ? 193 ARG   A CA    1 
ATOM   1463 C  C     . ARG   A  1 201 ? 10.11400 -77.11100  -21.74300 1.000 55.60162  ? 193 ARG   A C     1 
ATOM   1464 O  O     . ARG   A  1 201 ? 9.88300  -76.94600  -20.52700 1.000 57.28097  ? 193 ARG   A O     1 
ATOM   1465 C  CB    . ARG   A  1 201 ? 12.53900 -76.54300  -22.35700 1.000 48.63435  ? 193 ARG   A CB    1 
ATOM   1466 C  CG    . ARG   A  1 201 ? 12.20000 -75.54100  -23.45100 1.000 53.59995  ? 193 ARG   A CG    1 
ATOM   1467 C  CD    . ARG   A  1 201 ? 11.46300 -74.30700  -22.96200 1.000 53.08880  ? 193 ARG   A CD    1 
ATOM   1468 N  NE    . ARG   A  1 201 ? 11.43200 -73.27500  -23.99100 1.000 48.78499  ? 193 ARG   A NE    1 
ATOM   1469 C  CZ    . ARG   A  1 201 ? 12.42700 -72.43200  -24.26000 1.000 52.54299  ? 193 ARG   A CZ    1 
ATOM   1470 N  NH1   . ARG   A  1 201 ? 13.55600 -72.47500  -23.57100 1.000 50.11605  ? 193 ARG   A NH1   1 
ATOM   1471 N  NH2   . ARG   A  1 201 ? 12.28700 -71.54000  -25.22700 1.000 56.87828  ? 193 ARG   A NH2   1 
ATOM   1472 N  N     . THR   A  1 202 ? 9.22200  -76.87300  -22.71300 1.000 51.16352  ? 194 THR   A N     1 
ATOM   1473 C  CA    . THR   A  1 202 ? 7.82700  -76.40200  -22.48000 1.000 51.79292  ? 194 THR   A CA    1 
ATOM   1474 C  C     . THR   A  1 202 ? 7.02200  -77.50900  -21.79100 1.000 50.95190  ? 194 THR   A C     1 
ATOM   1475 O  O     . THR   A  1 202 ? 6.27100  -77.18600  -20.85800 1.000 51.48769  ? 194 THR   A O     1 
ATOM   1476 C  CB    . THR   A  1 202 ? 7.16100  -75.94300  -23.78300 1.000 50.66529  ? 194 THR   A CB    1 
ATOM   1477 O  OG1   . THR   A  1 202 ? 7.90400  -74.82200  -24.25700 1.000 57.86103  ? 194 THR   A OG1   1 
ATOM   1478 C  CG2   . THR   A  1 202 ? 5.70900  -75.54900  -23.61900 1.000 51.88720  ? 194 THR   A CG2   1 
ATOM   1479 N  N     . LEU   A  1 203 ? 7.17400  -78.75800  -22.24200 1.000 54.35824  ? 195 LEU   A N     1 
ATOM   1480 C  CA    . LEU   A  1 203 ? 6.50800  -79.95600  -21.65600 1.000 55.69218  ? 195 LEU   A CA    1 
ATOM   1481 C  C     . LEU   A  1 203 ? 6.97800  -80.16300  -20.20900 1.000 54.91962  ? 195 LEU   A C     1 
ATOM   1482 O  O     . LEU   A  1 203 ? 6.14500  -80.57400  -19.37800 1.000 53.33963  ? 195 LEU   A O     1 
ATOM   1483 C  CB    . LEU   A  1 203 ? 6.82100  -81.18800  -22.51500 1.000 52.78019  ? 195 LEU   A CB    1 
ATOM   1484 C  CG    . LEU   A  1 203 ? 5.95900  -81.36600  -23.76300 1.000 53.77633  ? 195 LEU   A CG    1 
ATOM   1485 C  CD1   . LEU   A  1 203 ? 6.57300  -82.39500  -24.69600 1.000 53.81549  ? 195 LEU   A CD1   1 
ATOM   1486 C  CD2   . LEU   A  1 203 ? 4.54200  -81.77100  -23.39500 1.000 55.48623  ? 195 LEU   A CD2   1 
ATOM   1487 N  N     . CYS   A  1 204 ? 8.25800  -79.88500  -19.93000 1.000 51.04272  ? 196 CYS   A N     1 
ATOM   1488 C  CA    . CYS   A  1 204 ? 8.91000  -80.04200  -18.60200 1.000 50.89139  ? 196 CYS   A CA    1 
ATOM   1489 C  C     . CYS   A  1 204 ? 8.68500  -78.80100  -17.72700 1.000 51.57067  ? 196 CYS   A C     1 
ATOM   1490 O  O     . CYS   A  1 204 ? 9.16900  -78.80900  -16.57900 1.000 58.96031  ? 196 CYS   A O     1 
ATOM   1491 C  CB    . CYS   A  1 204 ? 10.40400 -80.30300  -18.75300 1.000 50.05497  ? 196 CYS   A CB    1 
ATOM   1492 S  SG    . CYS   A  1 204 ? 10.78400 -81.87500  -19.56900 1.000 50.57101  ? 196 CYS   A SG    1 
ATOM   1493 N  N     . ASP   A  1 205 ? 8.00300  -77.77500  -18.25100 1.000 52.02534  ? 197 ASP   A N     1 
ATOM   1494 C  CA    . ASP   A  1 205 ? 7.48600  -76.60500  -17.48800 1.000 51.52255  ? 197 ASP   A CA    1 
ATOM   1495 C  C     . ASP   A  1 205 ? 8.65600  -75.70100  -17.07200 1.000 51.04119  ? 197 ASP   A C     1 
ATOM   1496 O  O     . ASP   A  1 205 ? 8.65700  -75.21900  -15.92300 1.000 49.71060  ? 197 ASP   A O     1 
ATOM   1497 C  CB    . ASP   A  1 205 ? 6.63800  -77.06500  -16.29600 1.000 54.80344  ? 197 ASP   A CB    1 
ATOM   1498 C  CG    . ASP   A  1 205 ? 5.66700  -76.01600  -15.77600 1.000 54.99888  ? 197 ASP   A CG    1 
ATOM   1499 O  OD1   . ASP   A  1 205 ? 5.74100  -74.85700  -16.24100 1.000 51.68919  ? 197 ASP   A OD1   1 
ATOM   1500 O  OD2   . ASP   A  1 205 ? 4.81800  -76.38000  -14.93300 1.000 60.20012  ? 197 ASP   A OD2   1 
ATOM   1501 N  N     . TYR   A  1 206 ? 9.60000  -75.46600  -17.98700 1.000 55.00000  ? 198 TYR   A N     1 
ATOM   1502 C  CA    . TYR   A  1 206 ? 10.74600 -74.53100  -17.82500 1.000 53.48563  ? 198 TYR   A CA    1 
ATOM   1503 C  C     . TYR   A  1 206 ? 11.48300 -74.82300  -16.51300 1.000 53.22674  ? 198 TYR   A C     1 
ATOM   1504 O  O     . TYR   A  1 206 ? 11.65400 -73.89600  -15.70300 1.000 60.02890  ? 198 TYR   A O     1 
ATOM   1505 C  CB    . TYR   A  1 206 ? 10.26700 -73.07700  -17.86700 1.000 50.22284  ? 198 TYR   A CB    1 
ATOM   1506 C  CG    . TYR   A  1 206 ? 9.83700  -72.58400  -19.22500 1.000 52.87020  ? 198 TYR   A CG    1 
ATOM   1507 C  CD1   . TYR   A  1 206 ? 8.58500  -72.89000  -19.73600 1.000 53.04705  ? 198 TYR   A CD1   1 
ATOM   1508 C  CD2   . TYR   A  1 206 ? 10.67700 -71.79700  -19.99700 1.000 54.87798  ? 198 TYR   A CD2   1 
ATOM   1509 C  CE1   . TYR   A  1 206 ? 8.18200  -72.43700  -20.98300 1.000 56.87389  ? 198 TYR   A CE1   1 
ATOM   1510 C  CE2   . TYR   A  1 206 ? 10.29000 -71.33500  -21.24500 1.000 58.99391  ? 198 TYR   A CE2   1 
ATOM   1511 C  CZ    . TYR   A  1 206 ? 9.03700  -71.65600  -21.74100 1.000 58.73272  ? 198 TYR   A CZ    1 
ATOM   1512 O  OH    . TYR   A  1 206 ? 8.65100  -71.20400  -22.97000 1.000 62.59869  ? 198 TYR   A OH    1 
ATOM   1513 N  N     . SER   A  1 207 ? 11.90300 -76.07500  -16.31300 1.000 53.09384  ? 199 SER   A N     1 
ATOM   1514 C  CA    . SER   A  1 207 ? 12.71700 -76.52100  -15.15200 1.000 49.56654  ? 199 SER   A CA    1 
ATOM   1515 C  C     . SER   A  1 207 ? 14.12600 -75.92500  -15.24900 1.000 51.40941  ? 199 SER   A C     1 
ATOM   1516 O  O     . SER   A  1 207 ? 14.77600 -76.12500  -16.28300 1.000 59.39872  ? 199 SER   A O     1 
ATOM   1517 C  CB    . SER   A  1 207 ? 12.77600 -78.02000  -15.06500 1.000 50.39013  ? 199 SER   A CB    1 
ATOM   1518 O  OG    . SER   A  1 207 ? 13.74700 -78.43100  -14.11300 1.000 55.66407  ? 199 SER   A OG    1 
ATOM   1519 N  N     . LYS   A  1 208 ? 14.58100 -75.24300  -14.19500 1.000 54.09119  ? 200 LYS   A N     1 
ATOM   1520 C  CA    . LYS   A  1 208 ? 15.94100 -74.64500  -14.08600 1.000 55.98046  ? 200 LYS   A CA    1 
ATOM   1521 C  C     . LYS   A  1 208 ? 17.01200 -75.74600  -14.09100 1.000 54.50864  ? 200 LYS   A C     1 
ATOM   1522 O  O     . LYS   A  1 208 ? 18.20400 -75.39800  -14.18300 1.000 50.93004  ? 200 LYS   A O     1 
ATOM   1523 C  CB    . LYS   A  1 208 ? 16.05200 -73.82100  -12.80000 1.000 52.19055  ? 200 LYS   A CB    1 
ATOM   1524 C  CG    . LYS   A  1 208 ? 16.07600 -74.64700  -11.52100 1.000 62.92218  ? 200 LYS   A CG    1 
ATOM   1525 C  CD    . LYS   A  1 208 ? 15.68100 -73.88000  -10.27900 1.000 74.97886  ? 200 LYS   A CD    1 
ATOM   1526 C  CE    . LYS   A  1 208 ? 15.44300 -74.78500  -9.08900  1.000 74.31847  ? 200 LYS   A CE    1 
ATOM   1527 N  NZ    . LYS   A  1 208 ? 15.25200 -74.00300  -7.84500  1.000 74.49187  ? 200 LYS   A NZ    1 
ATOM   1528 N  N     . ARG   A  1 209 ? 16.60300 -77.01300  -13.96000 1.000 53.07841  ? 201 ARG   A N     1 
ATOM   1529 C  CA    . ARG   A  1 209 ? 17.50200 -78.19700  -13.94900 1.000 56.56400  ? 201 ARG   A CA    1 
ATOM   1530 C  C     . ARG   A  1 209 ? 17.70300 -78.72500  -15.37600 1.000 55.40434  ? 201 ARG   A C     1 
ATOM   1531 O  O     . ARG   A  1 209 ? 18.46800 -79.69900  -15.52900 1.000 54.92271  ? 201 ARG   A O     1 
ATOM   1532 C  CB    . ARG   A  1 209 ? 16.92000 -79.29800  -13.05600 1.000 59.91693  ? 201 ARG   A CB    1 
ATOM   1533 C  CG    . ARG   A  1 209 ? 16.67400 -78.87600  -11.61400 1.000 67.66383  ? 201 ARG   A CG    1 
ATOM   1534 C  CD    . ARG   A  1 209 ? 17.02300 -79.97800  -10.62900 1.000 78.99736  ? 201 ARG   A CD    1 
ATOM   1535 N  NE    . ARG   A  1 209 ? 16.44000 -79.80000  -9.30400  1.000 95.25072  ? 201 ARG   A NE    1 
ATOM   1536 C  CZ    . ARG   A  1 209 ? 16.81800 -78.88100  -8.41300  1.000 100.67379 ? 201 ARG   A CZ    1 
ATOM   1537 N  NH1   . ARG   A  1 209 ? 17.77800 -78.01400  -8.69700  1.000 96.99227  ? 201 ARG   A NH1   1 
ATOM   1538 N  NH2   . ARG   A  1 209 ? 16.22200 -78.82400  -7.23300  1.000 103.28332 ? 201 ARG   A NH2   1 
ATOM   1539 N  N     . ILE   A  1 210 ? 17.04600 -78.11500  -16.37100 1.000 52.17957  ? 202 ILE   A N     1 
ATOM   1540 C  CA    . ILE   A  1 210 ? 17.05600 -78.56200  -17.79800 1.000 54.57261  ? 202 ILE   A CA    1 
ATOM   1541 C  C     . ILE   A  1 210 ? 17.68300 -77.46600  -18.66900 1.000 50.65992  ? 202 ILE   A C     1 
ATOM   1542 O  O     . ILE   A  1 210 ? 17.01800 -76.43700  -18.90100 1.000 46.76754  ? 202 ILE   A O     1 
ATOM   1543 C  CB    . ILE   A  1 210 ? 15.63400 -78.93600  -18.26500 1.000 50.87794  ? 202 ILE   A CB    1 
ATOM   1544 C  CG1   . ILE   A  1 210 ? 15.03200 -80.03500  -17.38300 1.000 48.71615  ? 202 ILE   A CG1   1 
ATOM   1545 C  CG2   . ILE   A  1 210 ? 15.64100 -79.32300  -19.73800 1.000 52.50381  ? 202 ILE   A CG2   1 
ATOM   1546 C  CD1   . ILE   A  1 210 ? 13.63800 -80.46700  -17.77500 1.000 49.08978  ? 202 ILE   A CD1   1 
ATOM   1547 N  N     . ALA   A  1 211 ? 18.90800 -77.71000  -19.14900 1.000 47.94482  ? 203 ALA   A N     1 
ATOM   1548 C  CA    . ALA   A  1 211 ? 19.73100 -76.78300  -19.96000 1.000 47.28148  ? 203 ALA   A CA    1 
ATOM   1549 C  C     . ALA   A  1 211 ? 20.09300 -77.43300  -21.30300 1.000 52.26419  ? 203 ALA   A C     1 
ATOM   1550 O  O     . ALA   A  1 211 ? 19.84600 -78.65000  -21.46800 1.000 51.41773  ? 203 ALA   A O     1 
ATOM   1551 C  CB    . ALA   A  1 211 ? 20.97000 -76.40600  -19.18900 1.000 47.98891  ? 203 ALA   A CB    1 
ATOM   1552 N  N     . VAL   A  1 212 ? 20.67300 -76.64400  -22.21400 1.000 53.25245  ? 204 VAL   A N     1 
ATOM   1553 C  CA    . VAL   A  1 212 ? 21.04500 -77.05700  -23.60100 1.000 49.04288  ? 204 VAL   A CA    1 
ATOM   1554 C  C     . VAL   A  1 212 ? 22.54300 -77.36500  -23.64900 1.000 51.75723  ? 204 VAL   A C     1 
ATOM   1555 O  O     . VAL   A  1 212 ? 23.34100 -76.49200  -23.25500 1.000 50.22275  ? 204 VAL   A O     1 
ATOM   1556 C  CB    . VAL   A  1 212 ? 20.68800 -75.96900  -24.63100 1.000 50.46236  ? 204 VAL   A CB    1 
ATOM   1557 C  CG1   . VAL   A  1 212 ? 21.11400 -76.35600  -26.04000 1.000 50.74369  ? 204 VAL   A CG1   1 
ATOM   1558 C  CG2   . VAL   A  1 212 ? 19.20800 -75.62800  -24.59500 1.000 48.43902  ? 204 VAL   A CG2   1 
ATOM   1559 N  N     . ALA   A  1 213 ? 22.89000 -78.56500  -24.12200 1.000 54.71728  ? 205 ALA   A N     1 
ATOM   1560 C  CA    . ALA   A  1 213 ? 24.24200 -78.94100  -24.59400 1.000 50.24889  ? 205 ALA   A CA    1 
ATOM   1561 C  C     . ALA   A  1 213 ? 24.22900 -78.88800  -26.12600 1.000 52.65570  ? 205 ALA   A C     1 
ATOM   1562 O  O     . ALA   A  1 213 ? 23.96100 -79.92700  -26.75600 1.000 53.35357  ? 205 ALA   A O     1 
ATOM   1563 C  CB    . ALA   A  1 213 ? 24.62300 -80.30200  -24.06700 1.000 50.85991  ? 205 ALA   A CB    1 
ATOM   1564 N  N     . LEU   A  1 214 ? 24.46300 -77.70000  -26.69200 1.000 52.40229  ? 206 LEU   A N     1 
ATOM   1565 C  CA    . LEU   A  1 214 ? 24.37900 -77.43500  -28.15200 1.000 54.50307  ? 206 LEU   A CA    1 
ATOM   1566 C  C     . LEU   A  1 214 ? 25.54200 -78.13900  -28.86000 1.000 60.73823  ? 206 LEU   A C     1 
ATOM   1567 O  O     . LEU   A  1 214 ? 26.70500 -77.88400  -28.48800 1.000 55.99139  ? 206 LEU   A O     1 
ATOM   1568 C  CB    . LEU   A  1 214 ? 24.40600 -75.92300  -28.40200 1.000 54.34590  ? 206 LEU   A CB    1 
ATOM   1569 C  CG    . LEU   A  1 214 ? 24.09800 -75.48700  -29.83500 1.000 57.27726  ? 206 LEU   A CG    1 
ATOM   1570 C  CD1   . LEU   A  1 214 ? 22.64700 -75.77400  -30.19700 1.000 56.87693  ? 206 LEU   A CD1   1 
ATOM   1571 C  CD2   . LEU   A  1 214 ? 24.40700 -74.01000  -30.02800 1.000 54.52836  ? 206 LEU   A CD2   1 
ATOM   1572 N  N     . GLU   A  1 215 ? 25.22500 -78.99500  -29.83600 1.000 58.48205  ? 207 GLU   A N     1 
ATOM   1573 C  CA    . GLU   A  1 215 ? 26.21200 -79.77100  -30.63400 1.000 59.11813  ? 207 GLU   A CA    1 
ATOM   1574 C  C     . GLU   A  1 215 ? 26.39800 -79.08900  -31.99400 1.000 61.76890  ? 207 GLU   A C     1 
ATOM   1575 O  O     . GLU   A  1 215 ? 25.38700 -78.85100  -32.68300 1.000 54.78673  ? 207 GLU   A O     1 
ATOM   1576 C  CB    . GLU   A  1 215 ? 25.74900 -81.22000  -30.78100 1.000 59.90440  ? 207 GLU   A CB    1 
ATOM   1577 C  CG    . GLU   A  1 215 ? 26.86300 -82.16800  -31.17700 1.000 60.20403  ? 207 GLU   A CG    1 
ATOM   1578 C  CD    . GLU   A  1 215 ? 26.51800 -83.63700  -31.01700 1.000 65.83512  ? 207 GLU   A CD    1 
ATOM   1579 O  OE1   . GLU   A  1 215 ? 25.32000 -83.94800  -30.85000 1.000 65.99795  ? 207 GLU   A OE1   1 
ATOM   1580 O  OE2   . GLU   A  1 215 ? 27.45100 -84.46300  -31.05200 1.000 67.13679  ? 207 GLU   A OE2   1 
ATOM   1581 N  N     . ILE   A  1 216 ? 27.65200 -78.80100  -32.35500 1.000 59.21028  ? 208 ILE   A N     1 
ATOM   1582 C  CA    . ILE   A  1 216 ? 28.03600 -77.95000  -33.52100 1.000 62.23710  ? 208 ILE   A CA    1 
ATOM   1583 C  C     . ILE   A  1 216 ? 28.67000 -78.84200  -34.59600 1.000 65.60198  ? 208 ILE   A C     1 
ATOM   1584 O  O     . ILE   A  1 216 ? 29.74700 -79.40500  -34.33300 1.000 72.55405  ? 208 ILE   A O     1 
ATOM   1585 C  CB    . ILE   A  1 216 ? 28.97100 -76.81600  -33.05300 1.000 67.38439  ? 208 ILE   A CB    1 
ATOM   1586 C  CG1   . ILE   A  1 216 ? 28.25500 -75.88600  -32.06800 1.000 66.93893  ? 208 ILE   A CG1   1 
ATOM   1587 C  CG2   . ILE   A  1 216 ? 29.54800 -76.04700  -34.23600 1.000 67.07928  ? 208 ILE   A CG2   1 
ATOM   1588 C  CD1   . ILE   A  1 216 ? 29.18000 -75.04300  -31.22200 1.000 67.79645  ? 208 ILE   A CD1   1 
ATOM   1589 N  N     . GLY   A  1 217 ? 28.01800 -78.95600  -35.75800 1.000 66.54761  ? 209 GLY   A N     1 
ATOM   1590 C  CA    . GLY   A  1 217 ? 28.45200 -79.80500  -36.88500 1.000 69.57102  ? 209 GLY   A CA    1 
ATOM   1591 C  C     . GLY   A  1 217 ? 29.55000 -79.15500  -37.71300 1.000 74.18140  ? 209 GLY   A C     1 
ATOM   1592 O  O     . GLY   A  1 217 ? 29.95600 -78.02000  -37.38200 1.000 71.39003  ? 209 GLY   A O     1 
ATOM   1593 N  N     . ALA   A  1 218 ? 30.00600 -79.85200  -38.76100 1.000 73.12419  ? 210 ALA   A N     1 
ATOM   1594 C  CA    . ALA   A  1 218 ? 31.12000 -79.44600  -39.65100 1.000 74.37248  ? 210 ALA   A CA    1 
ATOM   1595 C  C     . ALA   A  1 218 ? 30.76500 -78.14900  -40.38900 1.000 73.57703  ? 210 ALA   A C     1 
ATOM   1596 O  O     . ALA   A  1 218 ? 31.63400 -77.25800  -40.46300 1.000 72.17916  ? 210 ALA   A O     1 
ATOM   1597 C  CB    . ALA   A  1 218 ? 31.43700 -80.56000  -40.62000 1.000 78.52935  ? 210 ALA   A CB    1 
ATOM   1598 N  N     . ASP   A  1 219 ? 29.54100 -78.05700  -40.91900 1.000 67.13882  ? 211 ASP   A N     1 
ATOM   1599 C  CA    . ASP   A  1 219 ? 29.03500 -76.88800  -41.68800 1.000 70.53268  ? 211 ASP   A CA    1 
ATOM   1600 C  C     . ASP   A  1 219 ? 27.93100 -76.19800  -40.88000 1.000 70.27284  ? 211 ASP   A C     1 
ATOM   1601 O  O     . ASP   A  1 219 ? 26.88100 -76.83400  -40.66100 1.000 72.69693  ? 211 ASP   A O     1 
ATOM   1602 C  CB    . ASP   A  1 219 ? 28.51900 -77.31200  -43.06700 1.000 72.41327  ? 211 ASP   A CB    1 
ATOM   1603 C  CG    . ASP   A  1 219 ? 29.53600 -78.07500  -43.89900 1.000 78.82706  ? 211 ASP   A CG    1 
ATOM   1604 O  OD1   . ASP   A  1 219 ? 30.56100 -77.47000  -44.27500 1.000 73.71472  ? 211 ASP   A OD1   1 
ATOM   1605 O  OD2   . ASP   A  1 219 ? 29.29800 -79.27300  -44.15500 1.000 84.20533  ? 211 ASP   A OD2   1 
ATOM   1606 N  N     . LEU   A  1 220 ? 28.15900 -74.94700  -40.46300 1.000 70.74487  ? 212 LEU   A N     1 
ATOM   1607 C  CA    . LEU   A  1 220 ? 27.17200 -74.12700  -39.70900 1.000 64.08633  ? 212 LEU   A CA    1 
ATOM   1608 C  C     . LEU   A  1 220 ? 25.95700 -73.87400  -40.59600 1.000 73.07565  ? 212 LEU   A C     1 
ATOM   1609 O  O     . LEU   A  1 220 ? 26.06700 -73.88000  -41.82100 1.000 80.65626  ? 212 LEU   A O     1 
ATOM   1610 C  CB    . LEU   A  1 220 ? 27.80700 -72.79800  -39.28200 1.000 64.44698  ? 212 LEU   A CB    1 
ATOM   1611 C  CG    . LEU   A  1 220 ? 29.04200 -72.88100  -38.38400 1.000 71.68999  ? 212 LEU   A CG    1 
ATOM   1612 C  CD1   . LEU   A  1 220 ? 29.41200 -71.50300  -37.85600 1.000 70.92932  ? 212 LEU   A CD1   1 
ATOM   1613 C  CD2   . LEU   A  1 220 ? 28.83400 -73.84800  -37.22700 1.000 69.71840  ? 212 LEU   A CD2   1 
ATOM   1614 N  N     . PRO   A  1 221 ? 24.76200 -73.64900  -40.00600 1.000 70.31198  ? 213 PRO   A N     1 
ATOM   1615 C  CA    . PRO   A  1 221 ? 23.60500 -73.17500  -40.76300 1.000 69.26020  ? 213 PRO   A CA    1 
ATOM   1616 C  C     . PRO   A  1 221 ? 23.63800 -71.64700  -40.90200 1.000 67.78739  ? 213 PRO   A C     1 
ATOM   1617 O  O     . PRO   A  1 221 ? 24.61500 -71.04400  -40.48800 1.000 64.04731  ? 213 PRO   A O     1 
ATOM   1618 C  CB    . PRO   A  1 221 ? 22.43200 -73.63300  -39.88700 1.000 72.40243  ? 213 PRO   A CB    1 
ATOM   1619 C  CG    . PRO   A  1 221 ? 22.97400 -73.52200  -38.47300 1.000 66.14944  ? 213 PRO   A CG    1 
ATOM   1620 C  CD    . PRO   A  1 221 ? 24.45300 -73.84200  -38.58100 1.000 68.18377  ? 213 PRO   A CD    1 
ATOM   1621 N  N     . SER   A  1 222 ? 22.57300 -71.06400  -41.46000 1.000 68.71402  ? 214 SER   A N     1 
ATOM   1622 C  CA    . SER   A  1 222 ? 22.36000 -69.59600  -41.55600 1.000 72.05068  ? 214 SER   A CA    1 
ATOM   1623 C  C     . SER   A  1 222 ? 22.36400 -68.99100  -40.14600 1.000 70.12504  ? 214 SER   A C     1 
ATOM   1624 O  O     . SER   A  1 222 ? 22.06000 -69.72700  -39.19000 1.000 70.18338  ? 214 SER   A O     1 
ATOM   1625 C  CB    . SER   A  1 222 ? 21.08600 -69.27800  -42.29700 1.000 72.42513  ? 214 SER   A CB    1 
ATOM   1626 O  OG    . SER   A  1 222 ? 21.15500 -69.73800  -43.64100 1.000 80.87557  ? 214 SER   A OG    1 
ATOM   1627 N  N     . ASN   A  1 223 ? 22.70800 -67.70600  -40.02900 1.000 71.96016  ? 215 ASN   A N     1 
ATOM   1628 C  CA    . ASN   A  1 223 ? 22.85200 -66.99100  -38.73100 1.000 68.59789  ? 215 ASN   A CA    1 
ATOM   1629 C  C     . ASN   A  1 223 ? 21.53000 -67.05100  -37.96000 1.000 70.68519  ? 215 ASN   A C     1 
ATOM   1630 O  O     . ASN   A  1 223 ? 21.58300 -67.22800  -36.72900 1.000 69.39257  ? 215 ASN   A O     1 
ATOM   1631 C  CB    . ASN   A  1 223 ? 23.30800 -65.54300  -38.92200 1.000 75.24739  ? 215 ASN   A CB    1 
ATOM   1632 C  CG    . ASN   A  1 223 ? 24.70600 -65.43600  -39.49100 1.000 86.22858  ? 215 ASN   A CG    1 
ATOM   1633 O  OD1   . ASN   A  1 223 ? 25.44700 -66.41700  -39.52600 1.000 83.89940  ? 215 ASN   A OD1   1 
ATOM   1634 N  ND2   . ASN   A  1 223 ? 25.07700 -64.24600  -39.93600 1.000 91.35111  ? 215 ASN   A ND2   1 
ATOM   1635 N  N     . HIS   A  1 224 ? 20.39500 -66.92700  -38.65800 1.000 69.85098  ? 216 HIS   A N     1 
ATOM   1636 C  CA    . HIS   A  1 224 ? 19.03000 -66.92400  -38.06100 1.000 74.65455  ? 216 HIS   A CA    1 
ATOM   1637 C  C     . HIS   A  1 224 ? 18.79400 -68.22800  -37.28700 1.000 70.23932  ? 216 HIS   A C     1 
ATOM   1638 O  O     . HIS   A  1 224 ? 18.09500 -68.17100  -36.25800 1.000 72.35507  ? 216 HIS   A O     1 
ATOM   1639 C  CB    . HIS   A  1 224 ? 17.95500 -66.63000  -39.12300 1.000 68.21808  ? 216 HIS   A CB    1 
ATOM   1640 C  CG    . HIS   A  1 224 ? 17.76800 -67.69100  -40.15800 1.000 76.72817  ? 216 HIS   A CG    1 
ATOM   1641 N  ND1   . HIS   A  1 224 ? 16.99300 -68.81400  -39.93600 1.000 75.07765  ? 216 HIS   A ND1   1 
ATOM   1642 C  CD2   . HIS   A  1 224 ? 18.21300 -67.78300  -41.43100 1.000 76.74746  ? 216 HIS   A CD2   1 
ATOM   1643 C  CE1   . HIS   A  1 224 ? 16.98800 -69.56200  -41.02100 1.000 74.32295  ? 216 HIS   A CE1   1 
ATOM   1644 N  NE2   . HIS   A  1 224 ? 17.72700 -68.95000  -41.95300 1.000 78.45144  ? 216 HIS   A NE2   1 
ATOM   1645 N  N     . VAL   A  1 225 ? 19.37700 -69.34100  -37.74400 1.000 66.83912  ? 217 VAL   A N     1 
ATOM   1646 C  CA    . VAL   A  1 225 ? 19.32200 -70.67000  -37.06000 1.000 69.80334  ? 217 VAL   A CA    1 
ATOM   1647 C  C     . VAL   A  1 225 ? 20.16600 -70.59100  -35.77900 1.000 69.05516  ? 217 VAL   A C     1 
ATOM   1648 O  O     . VAL   A  1 225 ? 19.72100 -71.12900  -34.74700 1.000 69.78456  ? 217 VAL   A O     1 
ATOM   1649 C  CB    . VAL   A  1 225 ? 19.79200 -71.81100  -37.98900 1.000 70.33770  ? 217 VAL   A CB    1 
ATOM   1650 C  CG1   . VAL   A  1 225 ? 19.81900 -73.16000  -37.28400 1.000 67.22404  ? 217 VAL   A CG1   1 
ATOM   1651 C  CG2   . VAL   A  1 225 ? 18.94500 -71.89700  -39.25100 1.000 69.36123  ? 217 VAL   A CG2   1 
ATOM   1652 N  N     . ILE   A  1 226 ? 21.33600 -69.94800  -35.85100 1.000 70.57052  ? 218 ILE   A N     1 
ATOM   1653 C  CA    . ILE   A  1 226 ? 22.29300 -69.78200  -34.71300 1.000 69.27663  ? 218 ILE   A CA    1 
ATOM   1654 C  C     . ILE   A  1 226 ? 21.72700 -68.74400  -33.73400 1.000 65.74085  ? 218 ILE   A C     1 
ATOM   1655 O  O     . ILE   A  1 226 ? 21.76800 -69.00400  -32.51800 1.000 69.43186  ? 218 ILE   A O     1 
ATOM   1656 C  CB    . ILE   A  1 226 ? 23.70000 -69.41000  -35.23300 1.000 68.76606  ? 218 ILE   A CB    1 
ATOM   1657 C  CG1   . ILE   A  1 226 ? 24.38900 -70.61800  -35.87500 1.000 67.10216  ? 218 ILE   A CG1   1 
ATOM   1658 C  CG2   . ILE   A  1 226 ? 24.55600 -68.80000  -34.13200 1.000 68.20382  ? 218 ILE   A CG2   1 
ATOM   1659 C  CD1   . ILE   A  1 226 ? 25.58800 -70.27700  -36.73300 1.000 63.30598  ? 218 ILE   A CD1   1 
ATOM   1660 N  N     . ASP   A  1 227 ? 21.22000 -67.62100  -34.25400 1.000 67.56294  ? 219 ASP   A N     1 
ATOM   1661 C  CA    . ASP   A  1 227 ? 20.57700 -66.52700  -33.47300 1.000 71.02781  ? 219 ASP   A CA    1 
ATOM   1662 C  C     . ASP   A  1 227 ? 19.40300 -67.09300  -32.66400 1.000 67.79362  ? 219 ASP   A C     1 
ATOM   1663 O  O     . ASP   A  1 227 ? 19.12200 -66.55700  -31.57000 1.000 63.27961  ? 219 ASP   A O     1 
ATOM   1664 C  CB    . ASP   A  1 227 ? 20.10000 -65.39800  -34.39200 1.000 68.54987  ? 219 ASP   A CB    1 
ATOM   1665 C  CG    . ASP   A  1 227 ? 21.22500 -64.62100  -35.05200 1.000 69.37696  ? 219 ASP   A CG    1 
ATOM   1666 O  OD1   . ASP   A  1 227 ? 22.39200 -64.85300  -34.68400 1.000 71.75607  ? 219 ASP   A OD1   1 
ATOM   1667 O  OD2   . ASP   A  1 227 ? 20.92200 -63.79600  -35.93300 1.000 73.18195  ? 219 ASP   A OD2   1 
ATOM   1668 N  N     . ARG   A  1 228 ? 18.76100 -68.14300  -33.18800 1.000 64.87585  ? 220 ARG   A N     1 
ATOM   1669 C  CA    . ARG   A  1 228 ? 17.59300 -68.84100  -32.58200 1.000 62.62867  ? 220 ARG   A CA    1 
ATOM   1670 C  C     . ARG   A  1 228 ? 17.91900 -69.31300  -31.15500 1.000 62.67174  ? 220 ARG   A C     1 
ATOM   1671 O  O     . ARG   A  1 228 ? 16.96600 -69.48900  -30.37600 1.000 55.45675  ? 220 ARG   A O     1 
ATOM   1672 C  CB    . ARG   A  1 228 ? 17.19200 -70.03100  -33.46100 1.000 63.93303  ? 220 ARG   A CB    1 
ATOM   1673 C  CG    . ARG   A  1 228 ? 15.71500 -70.38700  -33.40600 1.000 59.51889  ? 220 ARG   A CG    1 
ATOM   1674 C  CD    . ARG   A  1 228 ? 14.85500 -69.38800  -34.15300 1.000 54.17821  ? 220 ARG   A CD    1 
ATOM   1675 N  NE    . ARG   A  1 228 ? 13.49100 -69.87100  -34.32500 1.000 59.40260  ? 220 ARG   A NE    1 
ATOM   1676 C  CZ    . ARG   A  1 228 ? 12.55400 -69.89100  -33.37700 1.000 63.04221  ? 220 ARG   A CZ    1 
ATOM   1677 N  NH1   . ARG   A  1 228 ? 12.81300 -69.45300  -32.15400 1.000 55.96934  ? 220 ARG   A NH1   1 
ATOM   1678 N  NH2   . ARG   A  1 228 ? 11.34800 -70.35400  -33.66200 1.000 61.41199  ? 220 ARG   A NH2   1 
ATOM   1679 N  N     . TRP   A  1 229 ? 19.20500 -69.51500  -30.83400 1.000 66.04608  ? 221 TRP   A N     1 
ATOM   1680 C  CA    . TRP   A  1 229 ? 19.69400 -70.09300  -29.55000 1.000 60.85432  ? 221 TRP   A CA    1 
ATOM   1681 C  C     . TRP   A  1 229 ? 20.13900 -69.00000  -28.57000 1.000 61.52578  ? 221 TRP   A C     1 
ATOM   1682 O  O     . TRP   A  1 229 ? 20.67200 -69.35700  -27.50000 1.000 58.79227  ? 221 TRP   A O     1 
ATOM   1683 C  CB    . TRP   A  1 229 ? 20.82500 -71.09200  -29.82000 1.000 56.94092  ? 221 TRP   A CB    1 
ATOM   1684 C  CG    . TRP   A  1 229 ? 20.35000 -72.33900  -30.49700 1.000 59.23789  ? 221 TRP   A CG    1 
ATOM   1685 C  CD1   . TRP   A  1 229 ? 20.49000 -72.67000  -31.81200 1.000 57.85108  ? 221 TRP   A CD1   1 
ATOM   1686 C  CD2   . TRP   A  1 229 ? 19.62600 -73.41900  -29.88300 1.000 55.91492  ? 221 TRP   A CD2   1 
ATOM   1687 N  NE1   . TRP   A  1 229 ? 19.91600 -73.88800  -32.05700 1.000 62.25584  ? 221 TRP   A NE1   1 
ATOM   1688 C  CE2   . TRP   A  1 229 ? 19.37600 -74.37100  -30.89300 1.000 58.90481  ? 221 TRP   A CE2   1 
ATOM   1689 C  CE3   . TRP   A  1 229 ? 19.17500 -73.67600  -28.58400 1.000 51.74457  ? 221 TRP   A CE3   1 
ATOM   1690 C  CZ2   . TRP   A  1 229 ? 18.69300 -75.56000  -30.63900 1.000 56.47199  ? 221 TRP   A CZ2   1 
ATOM   1691 C  CZ3   . TRP   A  1 229 ? 18.50000 -74.85100  -28.33300 1.000 51.48124  ? 221 TRP   A CZ3   1 
ATOM   1692 C  CH2   . TRP   A  1 229 ? 18.26500 -75.77900  -29.34900 1.000 57.88745  ? 221 TRP   A CH2   1 
ATOM   1693 N  N     . LEU   A  1 230 ? 19.93300 -67.72500  -28.90700 1.000 64.84384  ? 222 LEU   A N     1 
ATOM   1694 C  CA    . LEU   A  1 230 ? 20.15500 -66.59400  -27.96700 1.000 70.25970  ? 222 LEU   A CA    1 
ATOM   1695 C  C     . LEU   A  1 230 ? 19.02200 -66.59200  -26.93300 1.000 68.25807  ? 222 LEU   A C     1 
ATOM   1696 O  O     . LEU   A  1 230 ? 17.86800 -66.89900  -27.30700 1.000 67.72072  ? 222 LEU   A O     1 
ATOM   1697 C  CB    . LEU   A  1 230 ? 20.22300 -65.27700  -28.75100 1.000 66.37774  ? 222 LEU   A CB    1 
ATOM   1698 C  CG    . LEU   A  1 230 ? 21.42800 -65.12600  -29.68100 1.000 68.17321  ? 222 LEU   A CG    1 
ATOM   1699 C  CD1   . LEU   A  1 230 ? 21.31600 -63.85800  -30.51200 1.000 67.72792  ? 222 LEU   A CD1   1 
ATOM   1700 C  CD2   . LEU   A  1 230 ? 22.73500 -65.13300  -28.90000 1.000 63.48313  ? 222 LEU   A CD2   1 
ATOM   1701 N  N     . GLY   A  1 231 ? 19.35100 -66.30200  -25.67200 1.000 59.94988  ? 223 GLY   A N     1 
ATOM   1702 C  CA    . GLY   A  1 231 ? 18.38600 -66.26600  -24.55700 1.000 58.98171  ? 223 GLY   A CA    1 
ATOM   1703 C  C     . GLY   A  1 231 ? 18.05800 -67.65200  -24.02300 1.000 56.06998  ? 223 GLY   A C     1 
ATOM   1704 O  O     . GLY   A  1 231 ? 17.32900 -67.73300  -23.01700 1.000 60.99969  ? 223 GLY   A O     1 
ATOM   1705 N  N     . GLU   A  1 232 ? 18.57100 -68.70700  -24.66100 1.000 51.74401  ? 224 GLU   A N     1 
ATOM   1706 C  CA    . GLU   A  1 232 ? 18.34600 -70.11800  -24.25100 1.000 56.51958  ? 224 GLU   A CA    1 
ATOM   1707 C  C     . GLU   A  1 232 ? 19.42800 -70.50900  -23.24700 1.000 53.46909  ? 224 GLU   A C     1 
ATOM   1708 O  O     . GLU   A  1 232 ? 20.55200 -70.01300  -23.31500 1.000 57.01228  ? 224 GLU   A O     1 
ATOM   1709 C  CB    . GLU   A  1 232 ? 18.33000 -71.03300  -25.48000 1.000 52.92394  ? 224 GLU   A CB    1 
ATOM   1710 C  CG    . GLU   A  1 232 ? 17.23000 -70.70300  -26.47900 1.000 51.88635  ? 224 GLU   A CG    1 
ATOM   1711 C  CD    . GLU   A  1 232 ? 15.81000 -70.83400  -25.94900 1.000 54.95219  ? 224 GLU   A CD    1 
ATOM   1712 O  OE1   . GLU   A  1 232 ? 15.63500 -71.43400  -24.86900 1.000 52.10845  ? 224 GLU   A OE1   1 
ATOM   1713 O  OE2   . GLU   A  1 232 ? 14.88100 -70.33000  -26.61400 1.000 55.25402  ? 224 GLU   A OE2   1 
ATOM   1714 N  N     . PRO   A  1 233 ? 19.12000 -71.39300  -22.27300 1.000 46.56800  ? 225 PRO   A N     1 
ATOM   1715 C  CA    . PRO   A  1 233 ? 20.08700 -71.76900  -21.24100 1.000 50.78921  ? 225 PRO   A CA    1 
ATOM   1716 C  C     . PRO   A  1 233 ? 21.14100 -72.77100  -21.73500 1.000 49.80155  ? 225 PRO   A C     1 
ATOM   1717 O  O     . PRO   A  1 233 ? 21.04300 -73.93900  -21.41000 1.000 48.42193  ? 225 PRO   A O     1 
ATOM   1718 C  CB    . PRO   A  1 233 ? 19.18300 -72.37500  -20.15700 1.000 46.36771  ? 225 PRO   A CB    1 
ATOM   1719 C  CG    . PRO   A  1 233 ? 18.05000 -73.00100  -20.93400 1.000 46.15803  ? 225 PRO   A CG    1 
ATOM   1720 C  CD    . PRO   A  1 233 ? 17.82000 -72.05800  -22.09700 1.000 46.21619  ? 225 PRO   A CD    1 
ATOM   1721 N  N     . ILE   A  1 234 ? 22.12500 -72.28900  -22.49900 1.000 50.67027  ? 226 ILE   A N     1 
ATOM   1722 C  CA    . ILE   A  1 234 ? 23.27100 -73.10700  -22.99600 1.000 57.68347  ? 226 ILE   A CA    1 
ATOM   1723 C  C     . ILE   A  1 234 ? 24.29000 -73.22700  -21.86000 1.000 56.57295  ? 226 ILE   A C     1 
ATOM   1724 O  O     . ILE   A  1 234 ? 24.87900 -72.19400  -21.49300 1.000 61.95761  ? 226 ILE   A O     1 
ATOM   1725 C  CB    . ILE   A  1 234 ? 23.89900 -72.50200  -24.27000 1.000 57.60077  ? 226 ILE   A CB    1 
ATOM   1726 C  CG1   . ILE   A  1 234 ? 22.88200 -72.38300  -25.40900 1.000 51.76744  ? 226 ILE   A CG1   1 
ATOM   1727 C  CG2   . ILE   A  1 234 ? 25.12500 -73.29800  -24.70100 1.000 58.84720  ? 226 ILE   A CG2   1 
ATOM   1728 C  CD1   . ILE   A  1 234 ? 23.31500 -71.45500  -26.51700 1.000 55.20155  ? 226 ILE   A CD1   1 
ATOM   1729 N  N     . LYS   A  1 235 ? 24.48100 -74.43900  -21.33000 1.000 52.99950  ? 227 LYS   A N     1 
ATOM   1730 C  CA    . LYS   A  1 235 ? 25.48800 -74.74400  -20.27900 1.000 56.09056  ? 227 LYS   A CA    1 
ATOM   1731 C  C     . LYS   A  1 235 ? 26.74400 -75.34400  -20.92000 1.000 60.26402  ? 227 LYS   A C     1 
ATOM   1732 O  O     . LYS   A  1 235 ? 27.84500 -75.08400  -20.39600 1.000 64.72458  ? 227 LYS   A O     1 
ATOM   1733 C  CB    . LYS   A  1 235 ? 24.89800 -75.68400  -19.22200 1.000 54.53220  ? 227 LYS   A CB    1 
ATOM   1734 C  CG    . LYS   A  1 235 ? 23.94300 -75.02000  -18.23900 1.000 58.19913  ? 227 LYS   A CG    1 
ATOM   1735 C  CD    . LYS   A  1 235 ? 24.61600 -73.99400  -17.34300 1.000 68.70096  ? 227 LYS   A CD    1 
ATOM   1736 C  CE    . LYS   A  1 235 ? 23.68500 -72.89400  -16.87600 1.000 75.65433  ? 227 LYS   A CE    1 
ATOM   1737 N  NZ    . LYS   A  1 235 ? 24.37900 -71.58600  -16.81100 1.000 75.00118  ? 227 LYS   A NZ    1 
ATOM   1738 N  N     . ALA   A  1 236 ? 26.58500 -76.10500  -22.00900 1.000 57.54918  ? 228 ALA   A N     1 
ATOM   1739 C  CA    . ALA   A  1 236 ? 27.68500 -76.80600  -22.71200 1.000 58.50400  ? 228 ALA   A CA    1 
ATOM   1740 C  C     . ALA   A  1 236 ? 27.59000 -76.56800  -24.22200 1.000 57.80689  ? 228 ALA   A C     1 
ATOM   1741 O  O     . ALA   A  1 236 ? 26.46600 -76.41600  -24.72700 1.000 60.52862  ? 228 ALA   A O     1 
ATOM   1742 C  CB    . ALA   A  1 236 ? 27.64300 -78.27900  -22.38900 1.000 57.29830  ? 228 ALA   A CB    1 
ATOM   1743 N  N     . ALA   A  1 237 ? 28.74500 -76.53500  -24.89400 1.000 61.33323  ? 229 ALA   A N     1 
ATOM   1744 C  CA    . ALA   A  1 237 ? 28.89700 -76.51600  -26.36800 1.000 62.71274  ? 229 ALA   A CA    1 
ATOM   1745 C  C     . ALA   A  1 237 ? 29.77900 -77.70200  -26.77800 1.000 64.81112  ? 229 ALA   A C     1 
ATOM   1746 O  O     . ALA   A  1 237 ? 30.95200 -77.73600  -26.35800 1.000 62.88727  ? 229 ALA   A O     1 
ATOM   1747 C  CB    . ALA   A  1 237 ? 29.48200 -75.19800  -26.81400 1.000 64.83067  ? 229 ALA   A CB    1 
ATOM   1748 N  N     . ILE   A  1 238 ? 29.22000 -78.64800  -27.54100 1.000 62.69685  ? 230 ILE   A N     1 
ATOM   1749 C  CA    . ILE   A  1 238 ? 29.88800 -79.92800  -27.92700 1.000 60.62920  ? 230 ILE   A CA    1 
ATOM   1750 C  C     . ILE   A  1 238 ? 30.55700 -79.73300  -29.29100 1.000 62.82536  ? 230 ILE   A C     1 
ATOM   1751 O  O     . ILE   A  1 238 ? 29.84400 -79.36400  -30.24300 1.000 67.62972  ? 230 ILE   A O     1 
ATOM   1752 C  CB    . ILE   A  1 238 ? 28.87900 -81.09500  -27.92300 1.000 60.34216  ? 230 ILE   A CB    1 
ATOM   1753 C  CG1   . ILE   A  1 238 ? 28.32300 -81.34100  -26.51600 1.000 61.02441  ? 230 ILE   A CG1   1 
ATOM   1754 C  CG2   . ILE   A  1 238 ? 29.49700 -82.35700  -28.50700 1.000 60.61683  ? 230 ILE   A CG2   1 
ATOM   1755 C  CD1   . ILE   A  1 238 ? 27.04200 -82.14200  -26.48400 1.000 55.83143  ? 230 ILE   A CD1   1 
ATOM   1756 N  N     . LEU   A  1 239 ? 31.87300 -79.97000  -29.36500 1.000 62.18858  ? 231 LEU   A N     1 
ATOM   1757 C  CA    . LEU   A  1 239 ? 32.70500 -79.81800  -30.59100 1.000 64.17644  ? 231 LEU   A CA    1 
ATOM   1758 C  C     . LEU   A  1 239 ? 33.28900 -81.17400  -30.98600 1.000 67.67365  ? 231 LEU   A C     1 
ATOM   1759 O  O     . LEU   A  1 239 ? 34.28700 -81.60500  -30.41400 1.000 66.56658  ? 231 LEU   A O     1 
ATOM   1760 C  CB    . LEU   A  1 239 ? 33.82500 -78.80600  -30.32100 1.000 67.25206  ? 231 LEU   A CB    1 
ATOM   1761 C  CG    . LEU   A  1 239 ? 33.39300 -77.44900  -29.76800 1.000 65.24982  ? 231 LEU   A CG    1 
ATOM   1762 C  CD1   . LEU   A  1 239 ? 34.59800 -76.53800  -29.59200 1.000 67.72609  ? 231 LEU   A CD1   1 
ATOM   1763 C  CD2   . LEU   A  1 239 ? 32.35700 -76.78600  -30.66500 1.000 60.99506  ? 231 LEU   A CD2   1 
ATOM   1764 N  N     . PRO   A  1 240 ? 32.70200 -81.88800  -31.97800 1.000 71.39839  ? 232 PRO   A N     1 
ATOM   1765 C  CA    . PRO   A  1 240 ? 33.29800 -83.12200  -32.48500 1.000 69.43443  ? 232 PRO   A CA    1 
ATOM   1766 C  C     . PRO   A  1 240 ? 34.64600 -82.82000  -33.15400 1.000 71.63026  ? 232 PRO   A C     1 
ATOM   1767 O  O     . PRO   A  1 240 ? 34.75900 -81.78400  -33.77900 1.000 74.69342  ? 232 PRO   A O     1 
ATOM   1768 C  CB    . PRO   A  1 240 ? 32.28300 -83.66300  -33.50700 1.000 65.99758  ? 232 PRO   A CB    1 
ATOM   1769 C  CG    . PRO   A  1 240 ? 31.00400 -82.89100  -33.23300 1.000 65.25913  ? 232 PRO   A CG    1 
ATOM   1770 C  CD    . PRO   A  1 240 ? 31.44500 -81.55800  -32.66600 1.000 65.94144  ? 232 PRO   A CD    1 
ATOM   1771 N  N     . THR   A  1 241 ? 35.61800 -83.72400  -33.00700 1.000 69.55146  ? 233 THR   A N     1 
ATOM   1772 C  CA    . THR   A  1 241 ? 36.99800 -83.60200  -33.55200 1.000 79.30545  ? 233 THR   A CA    1 
ATOM   1773 C  C     . THR   A  1 241 ? 36.95800 -83.45400  -35.08300 1.000 84.03743  ? 233 THR   A C     1 
ATOM   1774 O  O     . THR   A  1 241 ? 37.92700 -82.90200  -35.64300 1.000 85.27524  ? 233 THR   A O     1 
ATOM   1775 C  CB    . THR   A  1 241 ? 37.85300 -84.79800  -33.11400 1.000 80.64235  ? 233 THR   A CB    1 
ATOM   1776 O  OG1   . THR   A  1 241 ? 37.07100 -85.98100  -33.28200 1.000 82.18326  ? 233 THR   A OG1   1 
ATOM   1777 C  CG2   . THR   A  1 241 ? 38.31000 -84.70000  -31.67500 1.000 80.23722  ? 233 THR   A CG2   1 
ATOM   1778 N  N     . SER   A  1 242 ? 35.88000 -83.91900  -35.72600 1.000 79.38116  ? 234 SER   A N     1 
ATOM   1779 C  CA    . SER   A  1 242 ? 35.68200 -83.93100  -37.20000 1.000 78.34827  ? 234 SER   A CA    1 
ATOM   1780 C  C     . SER   A  1 242 ? 35.56000 -82.50700  -37.76800 1.000 81.21669  ? 234 SER   A C     1 
ATOM   1781 O  O     . SER   A  1 242 ? 35.97200 -82.31100  -38.92900 1.000 85.82547  ? 234 SER   A O     1 
ATOM   1782 C  CB    . SER   A  1 242 ? 34.48200 -84.76900  -37.56900 1.000 74.82228  ? 234 SER   A CB    1 
ATOM   1783 O  OG    . SER   A  1 242 ? 33.29700 -84.25400  -36.98200 1.000 73.36225  ? 234 SER   A OG    1 
ATOM   1784 N  N     . ILE   A  1 243 ? 35.03000 -81.55100  -36.99300 1.000 83.66554  ? 235 ILE   A N     1 
ATOM   1785 C  CA    . ILE   A  1 243 ? 34.70300 -80.17000  -37.47300 1.000 85.56116  ? 235 ILE   A CA    1 
ATOM   1786 C  C     . ILE   A  1 243 ? 35.97500 -79.31200  -37.49700 1.000 86.93194  ? 235 ILE   A C     1 
ATOM   1787 O  O     . ILE   A  1 243 ? 35.90200 -78.18300  -38.02000 1.000 89.81243  ? 235 ILE   A O     1 
ATOM   1788 C  CB    . ILE   A  1 243 ? 33.59400 -79.50800  -36.62500 1.000 75.80392  ? 235 ILE   A CB    1 
ATOM   1789 C  CG1   . ILE   A  1 243 ? 34.12800 -78.95900  -35.29600 1.000 79.38910  ? 235 ILE   A CG1   1 
ATOM   1790 C  CG2   . ILE   A  1 243 ? 32.42300 -80.46200  -36.42700 1.000 75.74629  ? 235 ILE   A CG2   1 
ATOM   1791 C  CD1   . ILE   A  1 243 ? 33.11400 -78.18300  -34.48400 1.000 77.97122  ? 235 ILE   A CD1   1 
ATOM   1792 N  N     . PHE   A  1 244 ? 37.08500 -79.81300  -36.94200 1.000 84.54364  ? 236 PHE   A N     1 
ATOM   1793 C  CA    . PHE   A  1 244 ? 38.38900 -79.10200  -36.86600 1.000 88.65062  ? 236 PHE   A CA    1 
ATOM   1794 C  C     . PHE   A  1 244 ? 39.15800 -79.27300  -38.18100 1.000 90.27401  ? 236 PHE   A C     1 
ATOM   1795 O  O     . PHE   A  1 244 ? 39.57800 -80.40500  -38.49800 1.000 91.08490  ? 236 PHE   A O     1 
ATOM   1796 C  CB    . PHE   A  1 244 ? 39.21100 -79.60100  -35.67400 1.000 88.25895  ? 236 PHE   A CB    1 
ATOM   1797 C  CG    . PHE   A  1 244 ? 38.70900 -79.12600  -34.33400 1.000 87.30226  ? 236 PHE   A CG    1 
ATOM   1798 C  CD1   . PHE   A  1 244 ? 37.68300 -79.79200  -33.68200 1.000 84.16943  ? 236 PHE   A CD1   1 
ATOM   1799 C  CD2   . PHE   A  1 244 ? 39.25700 -78.00500  -33.72900 1.000 87.45600  ? 236 PHE   A CD2   1 
ATOM   1800 C  CE1   . PHE   A  1 244 ? 37.21900 -79.35100  -32.45100 1.000 75.97933  ? 236 PHE   A CE1   1 
ATOM   1801 C  CE2   . PHE   A  1 244 ? 38.79300 -77.56600  -32.49800 1.000 84.59203  ? 236 PHE   A CE2   1 
ATOM   1802 C  CZ    . PHE   A  1 244 ? 37.77500 -78.23900  -31.86200 1.000 77.62723  ? 236 PHE   A CZ    1 
ATOM   1803 N  N     . LEU   A  1 245 ? 39.32600 -78.17000  -38.91900 1.000 88.51308  ? 237 LEU   A N     1 
ATOM   1804 C  CA    . LEU   A  1 245 ? 40.21700 -78.06100  -40.10700 1.000 92.90129  ? 237 LEU   A CA    1 
ATOM   1805 C  C     . LEU   A  1 245 ? 41.66600 -78.28300  -39.65900 1.000 95.04980  ? 237 LEU   A C     1 
ATOM   1806 O  O     . LEU   A  1 245 ? 42.02700 -77.79200  -38.57200 1.000 96.51203  ? 237 LEU   A O     1 
ATOM   1807 C  CB    . LEU   A  1 245 ? 40.05200 -76.67400  -40.74300 1.000 92.32916  ? 237 LEU   A CB    1 
ATOM   1808 C  CG    . LEU   A  1 245 ? 38.95100 -76.52500  -41.79500 1.000 86.96122  ? 237 LEU   A CG    1 
ATOM   1809 C  CD1   . LEU   A  1 245 ? 37.67300 -77.24500  -41.38800 1.000 85.52242  ? 237 LEU   A CD1   1 
ATOM   1810 C  CD2   . LEU   A  1 245 ? 38.66400 -75.05500  -42.06300 1.000 83.36165  ? 237 LEU   A CD2   1 
ATOM   1811 N  N     . THR   A  1 246 ? 42.45400 -79.00400  -40.46100 1.000 100.94851 ? 238 THR   A N     1 
ATOM   1812 C  CA    . THR   A  1 246 ? 43.92200 -79.17100  -40.28400 1.000 106.33430 ? 238 THR   A CA    1 
ATOM   1813 C  C     . THR   A  1 246 ? 44.63200 -77.98700  -40.95200 1.000 109.43841 ? 238 THR   A C     1 
ATOM   1814 O  O     . THR   A  1 246 ? 44.13700 -77.52600  -42.00100 1.000 110.13799 ? 238 THR   A O     1 
ATOM   1815 C  CB    . THR   A  1 246 ? 44.40900 -80.50800  -40.85600 1.000 106.80405 ? 238 THR   A CB    1 
ATOM   1816 O  OG1   . THR   A  1 246 ? 43.47400 -81.52500  -40.49400 1.000 106.03548 ? 238 THR   A OG1   1 
ATOM   1817 C  CG2   . THR   A  1 246 ? 45.79100 -80.88400  -40.36800 1.000 109.45547 ? 238 THR   A CG2   1 
ATOM   1818 N  N     . ASN   A  1 247 ? 45.73400 -77.51200  -40.36200 1.000 111.76270 ? 239 ASN   A N     1 
ATOM   1819 C  CA    . ASN   A  1 247 ? 46.56300 -76.40100  -40.90400 1.000 122.60230 ? 239 ASN   A CA    1 
ATOM   1820 C  C     . ASN   A  1 247 ? 47.90100 -76.96900  -41.39700 1.000 131.20357 ? 239 ASN   A C     1 
ATOM   1821 O  O     . ASN   A  1 247 ? 48.10900 -78.19300  -41.27900 1.000 129.76865 ? 239 ASN   A O     1 
ATOM   1822 C  CB    . ASN   A  1 247 ? 46.74700 -75.27300  -39.88300 1.000 126.71269 ? 239 ASN   A CB    1 
ATOM   1823 C  CG    . ASN   A  1 247 ? 47.85500 -75.53100  -38.88300 1.000 130.44335 ? 239 ASN   A CG    1 
ATOM   1824 O  OD1   . ASN   A  1 247 ? 47.94300 -76.61300  -38.30800 1.000 127.20608 ? 239 ASN   A OD1   1 
ATOM   1825 N  ND2   . ASN   A  1 247 ? 48.70400 -74.53900  -38.66600 1.000 137.22834 ? 239 ASN   A ND2   1 
ATOM   1826 N  N     . LYS   A  1 248 ? 48.75600 -76.09800  -41.94200 1.000 152.55598 ? 240 LYS   A N     1 
ATOM   1827 C  CA    . LYS   A  1 248 ? 50.08400 -76.43500  -42.53100 1.000 160.09005 ? 240 LYS   A CA    1 
ATOM   1828 C  C     . LYS   A  1 248 ? 50.89500 -77.32400  -41.57700 1.000 159.74984 ? 240 LYS   A C     1 
ATOM   1829 O  O     . LYS   A  1 248 ? 51.40900 -78.36200  -42.04400 1.000 159.35148 ? 240 LYS   A O     1 
ATOM   1830 C  CB    . LYS   A  1 248 ? 50.85600 -75.15700  -42.88100 1.000 158.71792 ? 240 LYS   A CB    1 
ATOM   1831 C  CG    . LYS   A  1 248 ? 50.93000 -74.09600  -41.78700 1.000 160.39508 ? 240 LYS   A CG    1 
ATOM   1832 C  CD    . LYS   A  1 248 ? 51.32400 -72.72300  -42.29700 1.000 166.08096 ? 240 LYS   A CD    1 
ATOM   1833 C  CE    . LYS   A  1 248 ? 50.22700 -72.03200  -43.08100 1.000 168.89192 ? 240 LYS   A CE    1 
ATOM   1834 N  NZ    . LYS   A  1 248 ? 50.72600 -70.81500  -43.76300 1.000 163.21247 ? 240 LYS   A NZ    1 
ATOM   1835 N  N     . LYS   A  1 249 ? 51.00500 -76.93500  -40.30200 1.000 137.54478 ? 241 LYS   A N     1 
ATOM   1836 C  CA    . LYS   A  1 249 ? 51.86300 -77.60800  -39.28700 1.000 132.96418 ? 241 LYS   A CA    1 
ATOM   1837 C  C     . LYS   A  1 249 ? 51.31300 -79.00700  -38.98000 1.000 126.36939 ? 241 LYS   A C     1 
ATOM   1838 O  O     . LYS   A  1 249 ? 52.12400 -79.95100  -38.91100 1.000 130.58492 ? 241 LYS   A O     1 
ATOM   1839 C  CB    . LYS   A  1 249 ? 51.95300 -76.75800  -38.01500 1.000 132.06004 ? 241 LYS   A CB    1 
ATOM   1840 C  CG    . LYS   A  1 249 ? 52.70700 -75.44400  -38.17200 1.000 133.16401 ? 241 LYS   A CG    1 
ATOM   1841 C  CD    . LYS   A  1 249 ? 52.44500 -74.45300  -37.05600 1.000 132.24769 ? 241 LYS   A CD    1 
ATOM   1842 C  CE    . LYS   A  1 249 ? 53.05400 -73.09100  -37.31600 1.000 130.17803 ? 241 LYS   A CE    1 
ATOM   1843 N  NZ    . LYS   A  1 249 ? 54.53200 -73.11500  -37.20600 1.000 122.62361 ? 241 LYS   A NZ    1 
ATOM   1844 N  N     . GLY   A  1 250 ? 49.99200 -79.12800  -38.81400 1.000 127.92823 ? 242 GLY   A N     1 
ATOM   1845 C  CA    . GLY   A  1 250 ? 49.30500 -80.38400  -38.44800 1.000 122.28431 ? 242 GLY   A CA    1 
ATOM   1846 C  C     . GLY   A  1 250 ? 48.27400 -80.18000  -37.34700 1.000 123.44985 ? 242 GLY   A C     1 
ATOM   1847 O  O     . GLY   A  1 250 ? 47.40100 -81.05900  -37.19800 1.000 120.23247 ? 242 GLY   A O     1 
ATOM   1848 N  N     . PHE   A  1 251 ? 48.37900 -79.07200  -36.59900 1.000 119.56758 ? 243 PHE   A N     1 
ATOM   1849 C  CA    . PHE   A  1 251 ? 47.46700 -78.67500  -35.49000 1.000 116.12934 ? 243 PHE   A CA    1 
ATOM   1850 C  C     . PHE   A  1 251 ? 46.01900 -78.61600  -35.97400 1.000 115.91820 ? 243 PHE   A C     1 
ATOM   1851 O  O     . PHE   A  1 251 ? 45.76100 -78.27900  -37.12800 1.000 118.26423 ? 243 PHE   A O     1 
ATOM   1852 C  CB    . PHE   A  1 251 ? 47.85700 -77.30400  -34.92700 1.000 120.81656 ? 243 PHE   A CB    1 
ATOM   1853 C  CG    . PHE   A  1 251 ? 48.93800 -77.32200  -33.87600 1.000 127.15420 ? 243 PHE   A CG    1 
ATOM   1854 C  CD1   . PHE   A  1 251 ? 50.27700 -77.24700  -34.23000 1.000 127.26745 ? 243 PHE   A CD1   1 
ATOM   1855 C  CD2   . PHE   A  1 251 ? 48.61400 -77.39700  -32.52900 1.000 132.59298 ? 243 PHE   A CD2   1 
ATOM   1856 C  CE1   . PHE   A  1 251 ? 51.26800 -77.25700  -33.26000 1.000 127.76869 ? 243 PHE   A CE1   1 
ATOM   1857 C  CE2   . PHE   A  1 251 ? 49.60600 -77.40800  -31.56100 1.000 134.84428 ? 243 PHE   A CE2   1 
ATOM   1858 C  CZ    . PHE   A  1 251 ? 50.93100 -77.33900  -31.92800 1.000 132.34226 ? 243 PHE   A CZ    1 
ATOM   1859 N  N     . PRO   A  1 252 ? 45.03100 -78.93500  -35.10300 1.000 111.54764 ? 244 PRO   A N     1 
ATOM   1860 C  CA    . PRO   A  1 252 ? 43.62400 -78.66500  -35.39600 1.000 106.87220 ? 244 PRO   A CA    1 
ATOM   1861 C  C     . PRO   A  1 252 ? 43.28100 -77.18400  -35.17700 1.000 101.27910 ? 244 PRO   A C     1 
ATOM   1862 O  O     . PRO   A  1 252 ? 43.75300 -76.61500  -34.20800 1.000 104.97959 ? 244 PRO   A O     1 
ATOM   1863 C  CB    . PRO   A  1 252 ? 42.87800 -79.54900  -34.38900 1.000 101.04758 ? 244 PRO   A CB    1 
ATOM   1864 C  CG    . PRO   A  1 252 ? 43.81400 -79.61600  -33.20300 1.000 102.70296 ? 244 PRO   A CG    1 
ATOM   1865 C  CD    . PRO   A  1 252 ? 45.20900 -79.59000  -33.79700 1.000 110.05251 ? 244 PRO   A CD    1 
ATOM   1866 N  N     . VAL   A  1 253 ? 42.49200 -76.60200  -36.08500 1.000 94.72077  ? 245 VAL   A N     1 
ATOM   1867 C  CA    . VAL   A  1 253 ? 41.95200 -75.21300  -35.98300 1.000 93.26754  ? 245 VAL   A CA    1 
ATOM   1868 C  C     . VAL   A  1 253 ? 40.48400 -75.23900  -36.42200 1.000 90.55514  ? 245 VAL   A C     1 
ATOM   1869 O  O     . VAL   A  1 253 ? 40.00500 -76.32700  -36.79600 1.000 91.65734  ? 245 VAL   A O     1 
ATOM   1870 C  CB    . VAL   A  1 253 ? 42.78700 -74.21400  -36.81000 1.000 93.97266  ? 245 VAL   A CB    1 
ATOM   1871 C  CG1   . VAL   A  1 253 ? 44.23800 -74.17900  -36.35300 1.000 103.18846 ? 245 VAL   A CG1   1 
ATOM   1872 C  CG2   . VAL   A  1 253 ? 42.71200 -74.49200  -38.30500 1.000 94.73546  ? 245 VAL   A CG2   1 
ATOM   1873 N  N     . LEU   A  1 254 ? 39.80500 -74.08900  -36.36900 1.000 87.51190  ? 246 LEU   A N     1 
ATOM   1874 C  CA    . LEU   A  1 254 ? 38.38300 -73.92200  -36.77200 1.000 84.28274  ? 246 LEU   A CA    1 
ATOM   1875 C  C     . LEU   A  1 254 ? 38.27400 -72.76800  -37.77400 1.000 85.57708  ? 246 LEU   A C     1 
ATOM   1876 O  O     . LEU   A  1 254 ? 39.12900 -71.86200  -37.72900 1.000 88.55818  ? 246 LEU   A O     1 
ATOM   1877 C  CB    . LEU   A  1 254 ? 37.53600 -73.64400  -35.52600 1.000 84.05717  ? 246 LEU   A CB    1 
ATOM   1878 C  CG    . LEU   A  1 254 ? 37.36100 -74.81800  -34.56400 1.000 82.60727  ? 246 LEU   A CG    1 
ATOM   1879 C  CD1   . LEU   A  1 254 ? 36.77300 -74.34600  -33.24200 1.000 76.95825  ? 246 LEU   A CD1   1 
ATOM   1880 C  CD2   . LEU   A  1 254 ? 36.48800 -75.90400  -35.17500 1.000 84.36455  ? 246 LEU   A CD2   1 
ATOM   1881 N  N     . SER   A  1 255 ? 37.25000 -72.80200  -38.63200 1.000 83.81824  ? 247 SER   A N     1 
ATOM   1882 C  CA    . SER   A  1 255 ? 36.94100 -71.74700  -39.63100 1.000 78.57383  ? 247 SER   A CA    1 
ATOM   1883 C  C     . SER   A  1 255 ? 36.62600 -70.43200  -38.90800 1.000 83.45338  ? 247 SER   A C     1 
ATOM   1884 O  O     . SER   A  1 255 ? 36.22800 -70.48500  -37.72900 1.000 87.25075  ? 247 SER   A O     1 
ATOM   1885 C  CB    . SER   A  1 255 ? 35.80900 -72.16700  -40.53100 1.000 77.43548  ? 247 SER   A CB    1 
ATOM   1886 O  OG    . SER   A  1 255 ? 34.57500 -72.15500  -39.83300 1.000 74.41336  ? 247 SER   A OG    1 
ATOM   1887 N  N     . LYS   A  1 256 ? 36.79400 -69.30200  -39.60000 1.000 82.89354  ? 248 LYS   A N     1 
ATOM   1888 C  CA    . LYS   A  1 256 ? 36.54800 -67.93400  -39.06700 1.000 89.07464  ? 248 LYS   A CA    1 
ATOM   1889 C  C     . LYS   A  1 256 ? 35.12100 -67.84200  -38.50600 1.000 88.42894  ? 248 LYS   A C     1 
ATOM   1890 O  O     . LYS   A  1 256 ? 34.93500 -67.14200  -37.49000 1.000 87.46829  ? 248 LYS   A O     1 
ATOM   1891 C  CB    . LYS   A  1 256 ? 36.78200 -66.88900  -40.16400 1.000 90.27838  ? 248 LYS   A CB    1 
ATOM   1892 C  CG    . LYS   A  1 256 ? 38.23200 -66.73100  -40.61000 1.000 98.75595  ? 248 LYS   A CG    1 
ATOM   1893 C  CD    . LYS   A  1 256 ? 38.92600 -65.50100  -40.05400 1.000 103.31633 ? 248 LYS   A CD    1 
ATOM   1894 C  CE    . LYS   A  1 256 ? 38.63800 -64.24400  -40.85000 1.000 109.76818 ? 248 LYS   A CE    1 
ATOM   1895 N  NZ    . LYS   A  1 256 ? 39.61700 -63.17000  -40.55700 1.000 109.82893 ? 248 LYS   A NZ    1 
ATOM   1896 N  N     . MET   A  1 257 ? 34.15800 -68.52000  -39.14000 1.000 83.88686  ? 249 MET   A N     1 
ATOM   1897 C  CA    . MET   A  1 257 ? 32.72100 -68.51000  -38.74900 1.000 86.92491  ? 249 MET   A CA    1 
ATOM   1898 C  C     . MET   A  1 257 ? 32.50600 -69.38900  -37.51100 1.000 87.82035  ? 249 MET   A C     1 
ATOM   1899 O  O     . MET   A  1 257 ? 31.61700 -69.05300  -36.70000 1.000 85.92582  ? 249 MET   A O     1 
ATOM   1900 C  CB    . MET   A  1 257 ? 31.82900 -69.01500  -39.88900 1.000 89.32870  ? 249 MET   A CB    1 
ATOM   1901 C  CG    . MET   A  1 257 ? 31.77700 -68.08000  -41.08600 1.000 102.82221 ? 249 MET   A CG    1 
ATOM   1902 S  SD    . MET   A  1 257 ? 31.36300 -66.36700  -40.63500 1.000 121.17215 ? 249 MET   A SD    1 
ATOM   1903 C  CE    . MET   A  1 257 ? 32.97200 -65.59000  -40.78400 1.000 105.34906 ? 249 MET   A CE    1 
ATOM   1904 N  N     . HIS   A  1 258 ? 33.27000 -70.47900  -37.37900 1.000 85.67856  ? 250 HIS   A N     1 
ATOM   1905 C  CA    . HIS   A  1 258 ? 33.27800 -71.35000  -36.17200 1.000 81.45345  ? 250 HIS   A CA    1 
ATOM   1906 C  C     . HIS   A  1 258 ? 33.86600 -70.57000  -34.99000 1.000 82.34086  ? 250 HIS   A C     1 
ATOM   1907 O  O     . HIS   A  1 258 ? 33.28000 -70.64500  -33.89600 1.000 89.15540  ? 250 HIS   A O     1 
ATOM   1908 C  CB    . HIS   A  1 258 ? 34.01700 -72.66900  -36.44000 1.000 76.58146  ? 250 HIS   A CB    1 
ATOM   1909 C  CG    . HIS   A  1 258 ? 33.16800 -73.70800  -37.09100 1.000 77.25172  ? 250 HIS   A CG    1 
ATOM   1910 N  ND1   . HIS   A  1 258 ? 32.81700 -73.64200  -38.42300 1.000 81.01190  ? 250 HIS   A ND1   1 
ATOM   1911 C  CD2   . HIS   A  1 258 ? 32.59800 -74.83000  -36.60400 1.000 78.85573  ? 250 HIS   A CD2   1 
ATOM   1912 C  CE1   . HIS   A  1 258 ? 32.07100 -74.68200  -38.73200 1.000 74.59728  ? 250 HIS   A CE1   1 
ATOM   1913 N  NE2   . HIS   A  1 258 ? 31.92000 -75.42700  -37.63200 1.000 79.42054  ? 250 HIS   A NE2   1 
ATOM   1914 N  N     . GLN   A  1 259 ? 34.96300 -69.83600  -35.21200 1.000 84.40196  ? 251 GLN   A N     1 
ATOM   1915 C  CA    . GLN   A  1 259 ? 35.63300 -68.98900  -34.18600 1.000 84.73831  ? 251 GLN   A CA    1 
ATOM   1916 C  C     . GLN   A  1 259 ? 34.62900 -67.96700  -33.63500 1.000 82.29649  ? 251 GLN   A C     1 
ATOM   1917 O  O     . GLN   A  1 259 ? 34.51400 -67.87100  -32.39500 1.000 80.70323  ? 251 GLN   A O     1 
ATOM   1918 C  CB    . GLN   A  1 259 ? 36.86600 -68.29700  -34.77200 1.000 88.69403  ? 251 GLN   A CB    1 
ATOM   1919 C  CG    . GLN   A  1 259 ? 38.02800 -69.24400  -35.03900 1.000 88.10573  ? 251 GLN   A CG    1 
ATOM   1920 C  CD    . GLN   A  1 259 ? 39.18600 -68.55300  -35.71900 1.000 93.89946  ? 251 GLN   A CD    1 
ATOM   1921 O  OE1   . GLN   A  1 259 ? 39.47500 -67.38500  -35.46500 1.000 97.39935  ? 251 GLN   A OE1   1 
ATOM   1922 N  NE2   . GLN   A  1 259 ? 39.86400 -69.27700  -36.59400 1.000 92.80414  ? 251 GLN   A NE2   1 
ATOM   1923 N  N     . ARG   A  1 260 ? 33.93100 -67.24600  -34.52100 1.000 82.27977  ? 252 ARG   A N     1 
ATOM   1924 C  CA    . ARG   A  1 260 ? 32.84900 -66.28300  -34.16900 1.000 79.34246  ? 252 ARG   A CA    1 
ATOM   1925 C  C     . ARG   A  1 260 ? 31.89400 -66.93300  -33.16100 1.000 77.26190  ? 252 ARG   A C     1 
ATOM   1926 O  O     . ARG   A  1 260 ? 31.64500 -66.32300  -32.10400 1.000 77.81533  ? 252 ARG   A O     1 
ATOM   1927 C  CB    . ARG   A  1 260 ? 32.06100 -65.85400  -35.41000 1.000 85.38992  ? 252 ARG   A CB    1 
ATOM   1928 C  CG    . ARG   A  1 260 ? 32.66600 -64.69000  -36.18400 1.000 91.81698  ? 252 ARG   A CG    1 
ATOM   1929 C  CD    . ARG   A  1 260 ? 31.71200 -64.17900  -37.25300 1.000 99.90523  ? 252 ARG   A CD    1 
ATOM   1930 N  NE    . ARG   A  1 260 ? 30.47900 -63.63800  -36.68300 1.000 110.40823 ? 252 ARG   A NE    1 
ATOM   1931 C  CZ    . ARG   A  1 260 ? 29.37200 -63.35000  -37.37000 1.000 104.04061 ? 252 ARG   A CZ    1 
ATOM   1932 N  NH1   . ARG   A  1 260 ? 29.31800 -63.54800  -38.67800 1.000 102.28239 ? 252 ARG   A NH1   1 
ATOM   1933 N  NH2   . ARG   A  1 260 ? 28.31600 -62.86200  -36.73900 1.000 96.20967  ? 252 ARG   A NH2   1 
ATOM   1934 N  N     . LEU   A  1 261 ? 31.38500 -68.12500  -33.49000 1.000 78.14027  ? 253 LEU   A N     1 
ATOM   1935 C  CA    . LEU   A  1 261 ? 30.41500 -68.89000  -32.66000 1.000 72.71571  ? 253 LEU   A CA    1 
ATOM   1936 C  C     . LEU   A  1 261 ? 31.04500 -69.21300  -31.30100 1.000 72.72360  ? 253 LEU   A C     1 
ATOM   1937 O  O     . LEU   A  1 261 ? 30.34000 -69.06600  -30.28700 1.000 75.12879  ? 253 LEU   A O     1 
ATOM   1938 C  CB    . LEU   A  1 261 ? 30.00800 -70.16600  -33.40500 1.000 71.33756  ? 253 LEU   A CB    1 
ATOM   1939 C  CG    . LEU   A  1 261 ? 28.91700 -71.00900  -32.74500 1.000 68.77346  ? 253 LEU   A CG    1 
ATOM   1940 C  CD1   . LEU   A  1 261 ? 27.59200 -70.26100  -32.69800 1.000 62.37416  ? 253 LEU   A CD1   1 
ATOM   1941 C  CD2   . LEU   A  1 261 ? 28.74800 -72.33400  -33.47000 1.000 62.70081  ? 253 LEU   A CD2   1 
ATOM   1942 N  N     . ILE   A  1 262 ? 32.31800 -69.62400  -31.28500 1.000 69.93651  ? 254 ILE   A N     1 
ATOM   1943 C  CA    . ILE   A  1 262 ? 33.07200 -69.97400  -30.04200 1.000 73.55227  ? 254 ILE   A CA    1 
ATOM   1944 C  C     . ILE   A  1 262 ? 33.19500 -68.71300  -29.17600 1.000 77.86266  ? 254 ILE   A C     1 
ATOM   1945 O  O     . ILE   A  1 262 ? 32.97500 -68.81900  -27.95500 1.000 77.62505  ? 254 ILE   A O     1 
ATOM   1946 C  CB    . ILE   A  1 262 ? 34.45100 -70.59400  -30.35800 1.000 73.56263  ? 254 ILE   A CB    1 
ATOM   1947 C  CG1   . ILE   A  1 262 ? 34.34300 -71.87400  -31.19300 1.000 71.89041  ? 254 ILE   A CG1   1 
ATOM   1948 C  CG2   . ILE   A  1 262 ? 35.24400 -70.83400  -29.08000 1.000 74.32701  ? 254 ILE   A CG2   1 
ATOM   1949 C  CD1   . ILE   A  1 262 ? 33.59700 -73.00800  -30.52400 1.000 67.93030  ? 254 ILE   A CD1   1 
ATOM   1950 N  N     . PHE   A  1 263 ? 33.52700 -67.57000  -29.78500 1.000 78.12015  ? 255 PHE   A N     1 
ATOM   1951 C  CA    . PHE   A  1 263 ? 33.69000 -66.26000  -29.09700 1.000 74.26829  ? 255 PHE   A CA    1 
ATOM   1952 C  C     . PHE   A  1 263 ? 32.37100 -65.85600  -28.42600 1.000 75.11815  ? 255 PHE   A C     1 
ATOM   1953 O  O     . PHE   A  1 263 ? 32.41800 -65.38700  -27.27200 1.000 77.97094  ? 255 PHE   A O     1 
ATOM   1954 C  CB    . PHE   A  1 263 ? 34.18500 -65.18400  -30.06800 1.000 77.48528  ? 255 PHE   A CB    1 
ATOM   1955 C  CG    . PHE   A  1 263 ? 35.65500 -65.26800  -30.39700 1.000 83.19195  ? 255 PHE   A CG    1 
ATOM   1956 C  CD1   . PHE   A  1 263 ? 36.61000 -65.20200  -29.39300 1.000 87.19785  ? 255 PHE   A CD1   1 
ATOM   1957 C  CD2   . PHE   A  1 263 ? 36.08800 -65.40000  -31.70700 1.000 83.80389  ? 255 PHE   A CD2   1 
ATOM   1958 C  CE1   . PHE   A  1 263 ? 37.96100 -65.27900  -29.69200 1.000 88.54925  ? 255 PHE   A CE1   1 
ATOM   1959 C  CE2   . PHE   A  1 263 ? 37.44000 -65.47400  -32.00400 1.000 87.37646  ? 255 PHE   A CE2   1 
ATOM   1960 C  CZ    . PHE   A  1 263 ? 38.37500 -65.41200  -30.99600 1.000 89.94373  ? 255 PHE   A CZ    1 
ATOM   1961 N  N     . ARG   A  1 264 ? 31.24000 -66.03900  -29.11700 1.000 73.65227  ? 256 ARG   A N     1 
ATOM   1962 C  CA    . ARG   A  1 264 ? 29.88200 -65.72500  -28.58900 1.000 72.43893  ? 256 ARG   A CA    1 
ATOM   1963 C  C     . ARG   A  1 264 ? 29.55900 -66.65700  -27.41200 1.000 70.01697  ? 256 ARG   A C     1 
ATOM   1964 O  O     . ARG   A  1 264 ? 28.94000 -66.18000  -26.44500 1.000 73.16836  ? 256 ARG   A O     1 
ATOM   1965 C  CB    . ARG   A  1 264 ? 28.82200 -65.81000  -29.69600 1.000 77.19182  ? 256 ARG   A CB    1 
ATOM   1966 C  CG    . ARG   A  1 264 ? 28.47900 -64.46200  -30.31700 1.000 86.54369  ? 256 ARG   A CG    1 
ATOM   1967 C  CD    . ARG   A  1 264 ? 27.68200 -64.53000  -31.61200 1.000 85.49559  ? 256 ARG   A CD    1 
ATOM   1968 N  NE    . ARG   A  1 264 ? 26.39500 -65.21000  -31.47300 1.000 92.43457  ? 256 ARG   A NE    1 
ATOM   1969 C  CZ    . ARG   A  1 264 ? 25.34400 -65.04500  -32.27900 1.000 84.81999  ? 256 ARG   A CZ    1 
ATOM   1970 N  NH1   . ARG   A  1 264 ? 25.39700 -64.19900  -33.29600 1.000 89.97235  ? 256 ARG   A NH1   1 
ATOM   1971 N  NH2   . ARG   A  1 264 ? 24.23100 -65.72600  -32.05700 1.000 69.67422  ? 256 ARG   A NH2   1 
ATOM   1972 N  N     . LEU   A  1 265 ? 29.97900 -67.92400  -27.48500 1.000 72.83323  ? 257 LEU   A N     1 
ATOM   1973 C  CA    . LEU   A  1 265 ? 29.72200 -68.95400  -26.44200 1.000 72.28742  ? 257 LEU   A CA    1 
ATOM   1974 C  C     . LEU   A  1 265 ? 30.58600 -68.68100  -25.20100 1.000 76.99769  ? 257 LEU   A C     1 
ATOM   1975 O  O     . LEU   A  1 265 ? 30.11100 -68.97400  -24.08400 1.000 72.37848  ? 257 LEU   A O     1 
ATOM   1976 C  CB    . LEU   A  1 265 ? 30.00100 -70.34400  -27.02300 1.000 68.49071  ? 257 LEU   A CB    1 
ATOM   1977 C  CG    . LEU   A  1 265 ? 28.95100 -70.86700  -28.00300 1.000 66.88137  ? 257 LEU   A CG    1 
ATOM   1978 C  CD1   . LEU   A  1 265 ? 29.52600 -71.96900  -28.88100 1.000 64.66992  ? 257 LEU   A CD1   1 
ATOM   1979 C  CD2   . LEU   A  1 265 ? 27.71600 -71.36100  -27.26500 1.000 60.91502  ? 257 LEU   A CD2   1 
ATOM   1980 N  N     . LEU   A  1 266 ? 31.79700 -68.14300  -25.38600 1.000 75.25036  ? 258 LEU   A N     1 
ATOM   1981 C  CA    . LEU   A  1 266 ? 32.74700 -67.81700  -24.28500 1.000 74.86899  ? 258 LEU   A CA    1 
ATOM   1982 C  C     . LEU   A  1 266 ? 32.19900 -66.65800  -23.44000 1.000 78.84576  ? 258 LEU   A C     1 
ATOM   1983 O  O     . LEU   A  1 266 ? 32.51100 -66.61800  -22.23200 1.000 80.20394  ? 258 LEU   A O     1 
ATOM   1984 C  CB    . LEU   A  1 266 ? 34.12000 -67.47900  -24.87500 1.000 76.87135  ? 258 LEU   A CB    1 
ATOM   1985 C  CG    . LEU   A  1 266 ? 34.95600 -68.68100  -25.31300 1.000 79.43416  ? 258 LEU   A CG    1 
ATOM   1986 C  CD1   . LEU   A  1 266 ? 36.02400 -68.26800  -26.31400 1.000 81.25030  ? 258 LEU   A CD1   1 
ATOM   1987 C  CD2   . LEU   A  1 266 ? 35.58700 -69.37500  -24.11600 1.000 79.27133  ? 258 LEU   A CD2   1 
ATOM   1988 N  N     . LYS   A  1 267 ? 31.41300 -65.75800  -24.04500 1.000 79.21227  ? 259 LYS   A N     1 
ATOM   1989 C  CA    . LYS   A  1 267 ? 30.70200 -64.65600  -23.33700 1.000 74.64950  ? 259 LYS   A CA    1 
ATOM   1990 C  C     . LYS   A  1 267 ? 29.59900 -65.25100  -22.45200 1.000 78.17839  ? 259 LYS   A C     1 
ATOM   1991 O  O     . LYS   A  1 267 ? 29.41300 -64.74600  -21.32800 1.000 82.35677  ? 259 LYS   A O     1 
ATOM   1992 C  CB    . LYS   A  1 267 ? 30.12000 -63.64200  -24.32800 1.000 75.08157  ? 259 LYS   A CB    1 
ATOM   1993 C  CG    . LYS   A  1 267 ? 31.12900 -62.67300  -24.93200 1.000 77.47683  ? 259 LYS   A CG    1 
ATOM   1994 C  CD    . LYS   A  1 267 ? 30.49000 -61.50800  -25.66200 1.000 82.80860  ? 259 LYS   A CD    1 
ATOM   1995 C  CE    . LYS   A  1 267 ? 29.53900 -61.94100  -26.76000 1.000 85.29535  ? 259 LYS   A CE    1 
ATOM   1996 N  NZ    . LYS   A  1 267 ? 29.11100 -60.80000  -27.60500 1.000 92.26944  ? 259 LYS   A NZ    1 
ATOM   1997 N  N     . LEU   A  1 268 ? 28.90800 -66.28800  -22.93900 1.000 74.07411  ? 260 LEU   A N     1 
ATOM   1998 C  CA    . LEU   A  1 268 ? 27.86800 -67.03900  -22.18000 1.000 76.48709  ? 260 LEU   A CA    1 
ATOM   1999 C  C     . LEU   A  1 268 ? 28.52200 -67.93300  -21.11500 1.000 75.37067  ? 260 LEU   A C     1 
ATOM   2000 O  O     . LEU   A  1 268 ? 27.77700 -68.48700  -20.28300 1.000 72.30852  ? 260 LEU   A O     1 
ATOM   2001 C  CB    . LEU   A  1 268 ? 27.02500 -67.87000  -23.15500 1.000 71.61014  ? 260 LEU   A CB    1 
ATOM   2002 C  CG    . LEU   A  1 268 ? 25.74900 -67.19800  -23.66100 1.000 73.72638  ? 260 LEU   A CG    1 
ATOM   2003 C  CD1   . LEU   A  1 268 ? 26.05700 -65.88300  -24.36300 1.000 78.67808  ? 260 LEU   A CD1   1 
ATOM   2004 C  CD2   . LEU   A  1 268 ? 24.98400 -68.12800  -24.58900 1.000 74.17448  ? 260 LEU   A CD2   1 
ATOM   2005 N  N     . GLU   A  1 269 ? 29.85000 -68.08700  -21.15900 1.000 67.81675  ? 261 GLU   A N     1 
ATOM   2006 C  CA    . GLU   A  1 269 ? 30.66600 -68.82000  -20.15200 1.000 73.24794  ? 261 GLU   A CA    1 
ATOM   2007 C  C     . GLU   A  1 269 ? 30.22700 -70.29000  -20.11600 1.000 72.21862  ? 261 GLU   A C     1 
ATOM   2008 O  O     . GLU   A  1 269 ? 30.01300 -70.82600  -19.00700 1.000 78.51202  ? 261 GLU   A O     1 
ATOM   2009 C  CB    . GLU   A  1 269 ? 30.53800 -68.16800  -18.77100 1.000 79.95911  ? 261 GLU   A CB    1 
ATOM   2010 C  CG    . GLU   A  1 269 ? 30.81700 -66.67500  -18.76200 1.000 82.18885  ? 261 GLU   A CG    1 
ATOM   2011 C  CD    . GLU   A  1 269 ? 30.78700 -66.04000  -17.38000 1.000 87.81245  ? 261 GLU   A CD    1 
ATOM   2012 O  OE1   . GLU   A  1 269 ? 31.45400 -66.57600  -16.47000 1.000 87.67245  ? 261 GLU   A OE1   1 
ATOM   2013 O  OE2   . GLU   A  1 269 ? 30.09900 -65.01000  -17.21600 1.000 89.36932  ? 261 GLU   A OE2   1 
ATOM   2014 N  N     . VAL   A  1 270 ? 30.10800 -70.91800  -21.28900 1.000 70.84885  ? 262 VAL   A N     1 
ATOM   2015 C  CA    . VAL   A  1 270 ? 29.68600 -72.34400  -21.43800 1.000 70.57939  ? 262 VAL   A CA    1 
ATOM   2016 C  C     . VAL   A  1 270 ? 30.89900 -73.23600  -21.15500 1.000 69.12086  ? 262 VAL   A C     1 
ATOM   2017 O  O     . VAL   A  1 270 ? 32.03900 -72.73000  -21.22500 1.000 69.57963  ? 262 VAL   A O     1 
ATOM   2018 C  CB    . VAL   A  1 270 ? 29.08500 -72.63100  -22.82900 1.000 67.88221  ? 262 VAL   A CB    1 
ATOM   2019 C  CG1   . VAL   A  1 270 ? 27.96300 -71.66200  -23.17400 1.000 67.14937  ? 262 VAL   A CG1   1 
ATOM   2020 C  CG2   . VAL   A  1 270 ? 30.13800 -72.63800  -23.92900 1.000 69.31138  ? 262 VAL   A CG2   1 
ATOM   2021 N  N     . GLN   A  1 271 ? 30.64900 -74.50800  -20.83500 1.000 66.51478  ? 263 GLN   A N     1 
ATOM   2022 C  CA    . GLN   A  1 271 ? 31.68400 -75.57000  -20.73900 1.000 71.50313  ? 263 GLN   A CA    1 
ATOM   2023 C  C     . GLN   A  1 271 ? 31.78800 -76.24200  -22.11300 1.000 73.34050  ? 263 GLN   A C     1 
ATOM   2024 O  O     . GLN   A  1 271 ? 30.74700 -76.68700  -22.62800 1.000 69.32374  ? 263 GLN   A O     1 
ATOM   2025 C  CB    . GLN   A  1 271 ? 31.33300 -76.56300  -19.62700 1.000 70.81601  ? 263 GLN   A CB    1 
ATOM   2026 C  CG    . GLN   A  1 271 ? 31.48300 -75.99100  -18.22300 1.000 68.18296  ? 263 GLN   A CG    1 
ATOM   2027 C  CD    . GLN   A  1 271 ? 30.94100 -76.92700  -17.17100 1.000 68.57696  ? 263 GLN   A CD    1 
ATOM   2028 O  OE1   . GLN   A  1 271 ? 29.73700 -77.15800  -17.08000 1.000 69.46717  ? 263 GLN   A OE1   1 
ATOM   2029 N  NE2   . GLN   A  1 271 ? 31.83200 -77.47800  -16.36300 1.000 69.21699  ? 263 GLN   A NE2   1 
ATOM   2030 N  N     . PHE   A  1 272 ? 32.98700 -76.27900  -22.69900 1.000 69.12468  ? 264 PHE   A N     1 
ATOM   2031 C  CA    . PHE   A  1 272 ? 33.24400 -76.85700  -24.04400 1.000 65.29081  ? 264 PHE   A CA    1 
ATOM   2032 C  C     . PHE   A  1 272 ? 33.56800 -78.34500  -23.89700 1.000 69.06588  ? 264 PHE   A C     1 
ATOM   2033 O  O     . PHE   A  1 272 ? 34.53400 -78.68100  -23.19400 1.000 73.12100  ? 264 PHE   A O     1 
ATOM   2034 C  CB    . PHE   A  1 272 ? 34.35700 -76.08700  -24.75700 1.000 72.30632  ? 264 PHE   A CB    1 
ATOM   2035 C  CG    . PHE   A  1 272 ? 33.95500 -74.69600  -25.17400 1.000 74.00585  ? 264 PHE   A CG    1 
ATOM   2036 C  CD1   . PHE   A  1 272 ? 33.97900 -73.65000  -24.26500 1.000 73.91581  ? 264 PHE   A CD1   1 
ATOM   2037 C  CD2   . PHE   A  1 272 ? 33.52600 -74.43800  -26.46800 1.000 71.55278  ? 264 PHE   A CD2   1 
ATOM   2038 C  CE1   . PHE   A  1 272 ? 33.59800 -72.37200  -24.64500 1.000 73.23603  ? 264 PHE   A CE1   1 
ATOM   2039 C  CE2   . PHE   A  1 272 ? 33.14400 -73.15900  -26.84600 1.000 70.38738  ? 264 PHE   A CE2   1 
ATOM   2040 C  CZ    . PHE   A  1 272 ? 33.18100 -72.12900  -25.93400 1.000 73.25842  ? 264 PHE   A CZ    1 
ATOM   2041 N  N     . ILE   A  1 273 ? 32.76900 -79.20200  -24.53800 1.000 68.48776  ? 265 ILE   A N     1 
ATOM   2042 C  CA    . ILE   A  1 273 ? 32.94200 -80.68500  -24.54600 1.000 66.26701  ? 265 ILE   A CA    1 
ATOM   2043 C  C     . ILE   A  1 273 ? 33.54600 -81.09200  -25.89500 1.000 66.43120  ? 265 ILE   A C     1 
ATOM   2044 O  O     . ILE   A  1 273 ? 33.05100 -80.60800  -26.92800 1.000 67.24511  ? 265 ILE   A O     1 
ATOM   2045 C  CB    . ILE   A  1 273 ? 31.59900 -81.39000  -24.26200 1.000 66.49957  ? 265 ILE   A CB    1 
ATOM   2046 C  CG1   . ILE   A  1 273 ? 31.06000 -81.02700  -22.87500 1.000 62.31050  ? 265 ILE   A CG1   1 
ATOM   2047 C  CG2   . ILE   A  1 273 ? 31.72600 -82.89700  -24.43900 1.000 65.90495  ? 265 ILE   A CG2   1 
ATOM   2048 C  CD1   . ILE   A  1 273 ? 29.62400 -81.43300  -22.64200 1.000 56.16227  ? 265 ILE   A CD1   1 
ATOM   2049 N  N     . ILE   A  1 274 ? 34.58900 -81.92700  -25.87400 1.000 67.14292  ? 266 ILE   A N     1 
ATOM   2050 C  CA    . ILE   A  1 274 ? 35.20500 -82.55100  -27.08200 1.000 64.82834  ? 266 ILE   A CA    1 
ATOM   2051 C  C     . ILE   A  1 274 ? 34.71200 -84.00000  -27.16400 1.000 71.06142  ? 266 ILE   A C     1 
ATOM   2052 O  O     . ILE   A  1 274 ? 35.05400 -84.78900  -26.26200 1.000 72.08576  ? 266 ILE   A O     1 
ATOM   2053 C  CB    . ILE   A  1 274 ? 36.74600 -82.47300  -27.04200 1.000 67.53862  ? 266 ILE   A CB    1 
ATOM   2054 C  CG1   . ILE   A  1 274 ? 37.25000 -81.07600  -26.67300 1.000 68.08737  ? 266 ILE   A CG1   1 
ATOM   2055 C  CG2   . ILE   A  1 274 ? 37.33700 -82.94700  -28.36200 1.000 72.24994  ? 266 ILE   A CG2   1 
ATOM   2056 C  CD1   . ILE   A  1 274 ? 36.95100 -80.01400  -27.70700 1.000 74.80786  ? 266 ILE   A CD1   1 
ATOM   2057 N  N     . THR   A  1 275 ? 33.92600 -84.31600  -28.19900 1.000 72.33602  ? 267 THR   A N     1 
ATOM   2058 C  CA    . THR   A  1 275 ? 33.41900 -85.67900  -28.52200 1.000 70.23972  ? 267 THR   A CA    1 
ATOM   2059 C  C     . THR   A  1 275 ? 34.18900 -86.20700  -29.73900 1.000 69.11989  ? 267 THR   A C     1 
ATOM   2060 O  O     . THR   A  1 275 ? 34.95800 -85.42400  -30.33000 1.000 68.73905  ? 267 THR   A O     1 
ATOM   2061 C  CB    . THR   A  1 275 ? 31.89500 -85.67600  -28.72400 1.000 62.82656  ? 267 THR   A CB    1 
ATOM   2062 O  OG1   . THR   A  1 275 ? 31.45800 -87.02400  -28.89200 1.000 67.04289  ? 267 THR   A OG1   1 
ATOM   2063 C  CG2   . THR   A  1 275 ? 31.43900 -84.85200  -29.90800 1.000 65.96390  ? 267 THR   A CG2   1 
ATOM   2064 N  N     . GLY   A  1 276 ? 34.00600 -87.48700  -30.07400 1.000 72.24104  ? 268 GLY   A N     1 
ATOM   2065 C  CA    . GLY   A  1 276 ? 34.67600 -88.15500  -31.20800 1.000 78.78694  ? 268 GLY   A CA    1 
ATOM   2066 C  C     . GLY   A  1 276 ? 36.12200 -88.50600  -30.89300 1.000 80.22413  ? 268 GLY   A C     1 
ATOM   2067 O  O     . GLY   A  1 276 ? 36.63500 -88.03600  -29.85700 1.000 84.49910  ? 268 GLY   A O     1 
ATOM   2068 N  N     . THR   A  1 277 ? 36.75800 -89.29800  -31.76300 1.000 80.23337  ? 269 THR   A N     1 
ATOM   2069 C  CA    . THR   A  1 277 ? 38.14800 -89.80900  -31.61000 1.000 91.75371  ? 269 THR   A CA    1 
ATOM   2070 C  C     . THR   A  1 277 ? 39.13300 -88.84100  -32.27600 1.000 90.20811  ? 269 THR   A C     1 
ATOM   2071 O  O     . THR   A  1 277 ? 38.67800 -87.95600  -33.02900 1.000 89.83046  ? 269 THR   A O     1 
ATOM   2072 C  CB    . THR   A  1 277 ? 38.28800 -91.22100  -32.19500 1.000 92.62947  ? 269 THR   A CB    1 
ATOM   2073 O  OG1   . THR   A  1 277 ? 37.99700 -91.15000  -33.59200 1.000 88.62193  ? 269 THR   A OG1   1 
ATOM   2074 C  CG2   . THR   A  1 277 ? 37.37800 -92.22700  -31.52400 1.000 92.19199  ? 269 THR   A CG2   1 
ATOM   2075 N  N     . ASN   A  1 278 ? 40.43200 -89.02400  -32.01400 1.000 93.08879  ? 270 ASN   A N     1 
ATOM   2076 C  CA    . ASN   A  1 278 ? 41.52800 -88.14200  -32.49700 1.000 99.71894  ? 270 ASN   A CA    1 
ATOM   2077 C  C     . ASN   A  1 278 ? 41.77300 -88.41200  -33.98800 1.000 106.70097 ? 270 ASN   A C     1 
ATOM   2078 O  O     . ASN   A  1 278 ? 42.10900 -89.56500  -34.32900 1.000 108.33500 ? 270 ASN   A O     1 
ATOM   2079 C  CB    . ASN   A  1 278 ? 42.80800 -88.33600  -31.67600 1.000 101.32836 ? 270 ASN   A CB    1 
ATOM   2080 C  CG    . ASN   A  1 278 ? 43.78500 -87.18400  -31.80200 1.000 114.00192 ? 270 ASN   A CG    1 
ATOM   2081 O  OD1   . ASN   A  1 278 ? 43.71800 -86.40100  -32.74800 1.000 115.48837 ? 270 ASN   A OD1   1 
ATOM   2082 N  ND2   . ASN   A  1 278 ? 44.69700 -87.07100  -30.85000 1.000 122.72576 ? 270 ASN   A ND2   1 
ATOM   2083 N  N     . HIS   A  1 279 ? 41.60600 -87.38700  -34.83300 1.000 105.17670 ? 271 HIS   A N     1 
ATOM   2084 C  CA    . HIS   A  1 279 ? 41.86800 -87.42500  -36.30000 1.000 107.62039 ? 271 HIS   A CA    1 
ATOM   2085 C  C     . HIS   A  1 279 ? 43.21600 -86.76900  -36.62100 1.000 118.78254 ? 271 HIS   A C     1 
ATOM   2086 O  O     . HIS   A  1 279 ? 43.75800 -87.04900  -37.71100 1.000 125.99307 ? 271 HIS   A O     1 
ATOM   2087 C  CB    . HIS   A  1 279 ? 40.71200 -86.77700  -37.06900 1.000 97.00226  ? 271 HIS   A CB    1 
ATOM   2088 C  CG    . HIS   A  1 279 ? 39.42600 -87.51100  -36.90500 1.000 95.13094  ? 271 HIS   A CG    1 
ATOM   2089 N  ND1   . HIS   A  1 279 ? 38.22900 -86.86100  -36.68100 1.000 93.63141  ? 271 HIS   A ND1   1 
ATOM   2090 C  CD2   . HIS   A  1 279 ? 39.14900 -88.83300  -36.90100 1.000 96.34093  ? 271 HIS   A CD2   1 
ATOM   2091 C  CE1   . HIS   A  1 279 ? 37.26500 -87.75100  -36.56400 1.000 90.01824  ? 271 HIS   A CE1   1 
ATOM   2092 N  NE2   . HIS   A  1 279 ? 37.80400 -88.96900  -36.69200 1.000 91.94906  ? 271 HIS   A NE2   1 
ATOM   2093 N  N     . HIS   A  1 280 ? 43.72400 -85.92500  -35.71500 1.000 118.52679 ? 272 HIS   A N     1 
ATOM   2094 C  CA    . HIS   A  1 280 ? 45.09500 -85.34700  -35.75100 1.000 127.25947 ? 272 HIS   A CA    1 
ATOM   2095 C  C     . HIS   A  1 280 ? 46.01100 -86.23500  -34.90000 1.000 135.03669 ? 272 HIS   A C     1 
ATOM   2096 O  O     . HIS   A  1 280 ? 46.42300 -85.80200  -33.80200 1.000 134.46412 ? 272 HIS   A O     1 
ATOM   2097 C  CB    . HIS   A  1 280 ? 45.04900 -83.87300  -35.32500 1.000 121.49537 ? 272 HIS   A CB    1 
ATOM   2098 C  CG    . HIS   A  1 280 ? 44.12400 -83.05500  -36.16400 1.000 121.20385 ? 272 HIS   A CG    1 
ATOM   2099 N  ND1   . HIS   A  1 280 ? 42.80200 -82.84500  -35.81800 1.000 121.43620 ? 272 HIS   A ND1   1 
ATOM   2100 C  CD2   . HIS   A  1 280 ? 44.31200 -82.42300  -37.34200 1.000 124.37075 ? 272 HIS   A CD2   1 
ATOM   2101 C  CE1   . HIS   A  1 280 ? 42.22000 -82.10700  -36.74100 1.000 120.91964 ? 272 HIS   A CE1   1 
ATOM   2102 N  NE2   . HIS   A  1 280 ? 43.12600 -81.83100  -37.68500 1.000 124.01546 ? 272 HIS   A NE2   1 
ATOM   2103 N  N     . SER   A  1 281 ? 46.30400 -87.43700  -35.41400 1.000 148.63429 ? 273 SER   A N     1 
ATOM   2104 C  CA    . SER   A  1 281 ? 46.93300 -88.58100  -34.69800 1.000 155.78736 ? 273 SER   A CA    1 
ATOM   2105 C  C     . SER   A  1 281 ? 48.36700 -88.25000  -34.26300 1.000 158.82348 ? 273 SER   A C     1 
ATOM   2106 O  O     . SER   A  1 281 ? 48.81900 -88.83100  -33.25400 1.000 161.37919 ? 273 SER   A O     1 
ATOM   2107 C  CB    . SER   A  1 281 ? 46.90100 -89.82500  -35.55400 1.000 148.91409 ? 273 SER   A CB    1 
ATOM   2108 O  OG    . SER   A  1 281 ? 45.57500 -90.12600  -35.96300 1.000 142.31286 ? 273 SER   A OG    1 
ATOM   2109 N  N     . GLU   A  1 282 ? 49.05200 -87.35500  -34.98600 1.000 146.92032 ? 274 GLU   A N     1 
ATOM   2110 C  CA    . GLU   A  1 282 ? 50.45800 -86.94500  -34.71000 1.000 144.63774 ? 274 GLU   A CA    1 
ATOM   2111 C  C     . GLU   A  1 282 ? 50.49600 -85.85600  -33.62500 1.000 141.97215 ? 274 GLU   A C     1 
ATOM   2112 O  O     . GLU   A  1 282 ? 51.54400 -85.18700  -33.50900 1.000 140.20292 ? 274 GLU   A O     1 
ATOM   2113 C  CB    . GLU   A  1 282 ? 51.12400 -86.45400  -35.99800 1.000 140.91130 ? 274 GLU   A CB    1 
ATOM   2114 C  CG    . GLU   A  1 282 ? 51.22400 -87.51700  -37.07700 1.000 136.58585 ? 274 GLU   A CG    1 
ATOM   2115 C  CD    . GLU   A  1 282 ? 51.91800 -87.05300  -38.34700 1.000 143.68513 ? 274 GLU   A CD    1 
ATOM   2116 O  OE1   . GLU   A  1 282 ? 51.55500 -85.97400  -38.85600 1.000 142.65198 ? 274 GLU   A OE1   1 
ATOM   2117 O  OE2   . GLU   A  1 282 ? 52.81700 -87.77300  -38.82600 1.000 144.07159 ? 274 GLU   A OE2   1 
ATOM   2118 N  N     . LYS   A  1 283 ? 49.41100 -85.69100  -32.85700 1.000 140.83678 ? 275 LYS   A N     1 
ATOM   2119 C  CA    . LYS   A  1 283 ? 49.28100 -84.67700  -31.77500 1.000 141.45768 ? 275 LYS   A CA    1 
ATOM   2120 C  C     . LYS   A  1 283 ? 48.62200 -85.30600  -30.54100 1.000 145.62345 ? 275 LYS   A C     1 
ATOM   2121 O  O     . LYS   A  1 283 ? 47.80300 -86.23200  -30.71300 1.000 145.61738 ? 275 LYS   A O     1 
ATOM   2122 C  CB    . LYS   A  1 283 ? 48.43500 -83.49100  -32.25000 1.000 138.11213 ? 275 LYS   A CB    1 
ATOM   2123 C  CG    . LYS   A  1 283 ? 49.01500 -82.68300  -33.40400 1.000 131.61193 ? 275 LYS   A CG    1 
ATOM   2124 C  CD    . LYS   A  1 283 ? 50.21100 -81.83800  -33.01500 1.000 132.17556 ? 275 LYS   A CD    1 
ATOM   2125 C  CE    . LYS   A  1 283 ? 50.45200 -80.67500  -33.95500 1.000 124.38467 ? 275 LYS   A CE    1 
ATOM   2126 N  NZ    . LYS   A  1 283 ? 50.86400 -81.13000  -35.30400 1.000 123.59214 ? 275 LYS   A NZ    1 
ATOM   2127 N  N     . GLU   A  1 284 ? 48.96200 -84.80100  -29.34900 1.000 146.84285 ? 276 GLU   A N     1 
ATOM   2128 C  CA    . GLU   A  1 284 ? 48.25800 -85.07600  -28.06400 1.000 150.78043 ? 276 GLU   A CA    1 
ATOM   2129 C  C     . GLU   A  1 284 ? 46.84700 -84.47500  -28.15500 1.000 151.65968 ? 276 GLU   A C     1 
ATOM   2130 O  O     . GLU   A  1 284 ? 46.64400 -83.58000  -29.00000 1.000 154.21353 ? 276 GLU   A O     1 
ATOM   2131 C  CB    . GLU   A  1 284 ? 49.07600 -84.50300  -26.89900 1.000 153.94848 ? 276 GLU   A CB    1 
ATOM   2132 C  CG    . GLU   A  1 284 ? 48.48200 -84.74100  -25.51600 1.000 155.94865 ? 276 GLU   A CG    1 
ATOM   2133 C  CD    . GLU   A  1 284 ? 48.37400 -86.19200  -25.07900 1.000 159.17413 ? 276 GLU   A CD    1 
ATOM   2134 O  OE1   . GLU   A  1 284 ? 49.40800 -86.89400  -25.09400 1.000 163.22709 ? 276 GLU   A OE1   1 
ATOM   2135 O  OE2   . GLU   A  1 284 ? 47.25700 -86.61200  -24.70400 1.000 143.46551 ? 276 GLU   A OE2   1 
ATOM   2136 N  N     . PHE   A  1 285 ? 45.90800 -84.95200  -27.33100 1.000 135.39574 ? 277 PHE   A N     1 
ATOM   2137 C  CA    . PHE   A  1 285 ? 44.47400 -84.55100  -27.36100 1.000 126.59203 ? 277 PHE   A CA    1 
ATOM   2138 C  C     . PHE   A  1 285 ? 44.30800 -83.11000  -26.85800 1.000 123.10032 ? 277 PHE   A C     1 
ATOM   2139 O  O     . PHE   A  1 285 ? 43.27500 -82.48400  -27.17800 1.000 111.60767 ? 277 PHE   A O     1 
ATOM   2140 C  CB    . PHE   A  1 285 ? 43.61500 -85.51300  -26.53600 1.000 119.58199 ? 277 PHE   A CB    1 
ATOM   2141 C  CG    . PHE   A  1 285 ? 42.28100 -85.82600  -27.16200 1.000 107.31744 ? 277 PHE   A CG    1 
ATOM   2142 C  CD1   . PHE   A  1 285 ? 41.22500 -84.93300  -27.07000 1.000 104.03327 ? 277 PHE   A CD1   1 
ATOM   2143 C  CD2   . PHE   A  1 285 ? 42.09000 -87.00900  -27.86000 1.000 106.27372 ? 277 PHE   A CD2   1 
ATOM   2144 C  CE1   . PHE   A  1 285 ? 40.00200 -85.22300  -27.65500 1.000 104.41718 ? 277 PHE   A CE1   1 
ATOM   2145 C  CE2   . PHE   A  1 285 ? 40.86600 -87.29700  -28.44300 1.000 103.88090 ? 277 PHE   A CE2   1 
ATOM   2146 C  CZ    . PHE   A  1 285 ? 39.82500 -86.40200  -28.34200 1.000 102.22112 ? 277 PHE   A CZ    1 
ATOM   2147 N  N     . CYS   A  1 286 ? 45.27800 -82.60900  -26.08400 1.000 127.11695 ? 278 CYS   A N     1 
ATOM   2148 C  CA    . CYS   A  1 286 ? 45.33800 -81.20500  -25.59200 1.000 127.53615 ? 278 CYS   A CA    1 
ATOM   2149 C  C     . CYS   A  1 286 ? 45.42100 -80.23300  -26.77800 1.000 132.68468 ? 278 CYS   A C     1 
ATOM   2150 O  O     . CYS   A  1 286 ? 44.99200 -79.07900  -26.60600 1.000 130.23406 ? 278 CYS   A O     1 
ATOM   2151 C  CB    . CYS   A  1 286 ? 46.51000 -80.98900  -24.64000 1.000 125.57454 ? 278 CYS   A CB    1 
ATOM   2152 S  SG    . CYS   A  1 286 ? 48.11900 -81.44900  -25.33300 1.000 133.75094 ? 278 CYS   A SG    1 
ATOM   2153 N  N     . SER   A  1 287 ? 45.94100 -80.68300  -27.93000 1.000 126.23673 ? 279 SER   A N     1 
ATOM   2154 C  CA    . SER   A  1 287 ? 45.99300 -79.92200  -29.21000 1.000 117.14086 ? 279 SER   A CA    1 
ATOM   2155 C  C     . SER   A  1 287 ? 44.64500 -79.23700  -29.47100 1.000 108.14055 ? 279 SER   A C     1 
ATOM   2156 O  O     . SER   A  1 287 ? 44.65100 -78.06700  -29.89800 1.000 107.71150 ? 279 SER   A O     1 
ATOM   2157 C  CB    . SER   A  1 287 ? 46.38500 -80.81300  -30.36300 1.000 116.83726 ? 279 SER   A CB    1 
ATOM   2158 O  OG    . SER   A  1 287 ? 45.41800 -81.83200  -30.57200 1.000 117.44648 ? 279 SER   A OG    1 
ATOM   2159 N  N     . TYR   A  1 288 ? 43.53800 -79.94100  -29.21400 1.000 100.59957 ? 280 TYR   A N     1 
ATOM   2160 C  CA    . TYR   A  1 288 ? 42.14900 -79.42400  -29.34100 1.000 99.03904  ? 280 TYR   A CA    1 
ATOM   2161 C  C     . TYR   A  1 288 ? 41.88400 -78.38500  -28.24300 1.000 101.91224 ? 280 TYR   A C     1 
ATOM   2162 O  O     . TYR   A  1 288 ? 41.37800 -77.29300  -28.57000 1.000 102.05871 ? 280 TYR   A O     1 
ATOM   2163 C  CB    . TYR   A  1 288 ? 41.13600 -80.57200  -29.29500 1.000 95.81017  ? 280 TYR   A CB    1 
ATOM   2164 C  CG    . TYR   A  1 288 ? 41.20200 -81.51400  -30.47100 1.000 94.92134  ? 280 TYR   A CG    1 
ATOM   2165 C  CD1   . TYR   A  1 288 ? 40.62400 -81.18500  -31.68700 1.000 89.86896  ? 280 TYR   A CD1   1 
ATOM   2166 C  CD2   . TYR   A  1 288 ? 41.84200 -82.73900  -30.37100 1.000 97.16097  ? 280 TYR   A CD2   1 
ATOM   2167 C  CE1   . TYR   A  1 288 ? 40.68000 -82.04500  -32.77200 1.000 92.77929  ? 280 TYR   A CE1   1 
ATOM   2168 C  CE2   . TYR   A  1 288 ? 41.90700 -83.61200  -31.44500 1.000 98.29781  ? 280 TYR   A CE2   1 
ATOM   2169 C  CZ    . TYR   A  1 288 ? 41.32500 -83.26400  -32.65100 1.000 98.69205  ? 280 TYR   A CZ    1 
ATOM   2170 O  OH    . TYR   A  1 288 ? 41.38600 -84.12200  -33.71100 1.000 101.13808 ? 280 TYR   A OH    1 
ATOM   2171 N  N     . LEU   A  1 289 ? 42.21500 -78.71100  -26.98800 1.000 100.78249 ? 281 LEU   A N     1 
ATOM   2172 C  CA    . LEU   A  1 289 ? 42.06800 -77.79300  -25.82300 1.000 97.29762  ? 281 LEU   A CA    1 
ATOM   2173 C  C     . LEU   A  1 289 ? 42.99700 -76.58700  -26.00200 1.000 102.12565 ? 281 LEU   A C     1 
ATOM   2174 O  O     . LEU   A  1 289 ? 42.53800 -75.45400  -25.77000 1.000 102.19946 ? 281 LEU   A O     1 
ATOM   2175 C  CB    . LEU   A  1 289 ? 42.38900 -78.53800  -24.52200 1.000 96.20833  ? 281 LEU   A CB    1 
ATOM   2176 C  CG    . LEU   A  1 289 ? 41.38100 -79.60100  -24.08400 1.000 91.40525  ? 281 LEU   A CG    1 
ATOM   2177 C  CD1   . LEU   A  1 289 ? 41.75000 -80.15300  -22.71500 1.000 84.54112  ? 281 LEU   A CD1   1 
ATOM   2178 C  CD2   . LEU   A  1 289 ? 39.96500 -79.04700  -24.06600 1.000 84.98118  ? 281 LEU   A CD2   1 
ATOM   2179 N  N     . GLN   A  1 290 ? 44.25100 -76.83200  -26.39700 1.000 105.68206 ? 282 GLN   A N     1 
ATOM   2180 C  CA    . GLN   A  1 290 ? 45.28100 -75.78800  -26.65800 1.000 106.99449 ? 282 GLN   A CA    1 
ATOM   2181 C  C     . GLN   A  1 290 ? 44.69300 -74.71600  -27.58300 1.000 104.07341 ? 282 GLN   A C     1 
ATOM   2182 O  O     . GLN   A  1 290 ? 44.94900 -73.52300  -27.33000 1.000 105.41160 ? 282 GLN   A O     1 
ATOM   2183 C  CB    . GLN   A  1 290 ? 46.54800 -76.39900  -27.26700 1.000 110.88714 ? 282 GLN   A CB    1 
ATOM   2184 C  CG    . GLN   A  1 290 ? 47.52700 -76.94300  -26.23400 1.000 116.71967 ? 282 GLN   A CG    1 
ATOM   2185 C  CD    . GLN   A  1 290 ? 48.75900 -77.55600  -26.85900 1.000 129.61777 ? 282 GLN   A CD    1 
ATOM   2186 O  OE1   . GLN   A  1 290 ? 48.95600 -77.51600  -28.07200 1.000 127.07710 ? 282 GLN   A OE1   1 
ATOM   2187 N  NE2   . GLN   A  1 290 ? 49.60800 -78.13400  -26.02500 1.000 131.48007 ? 282 GLN   A NE2   1 
ATOM   2188 N  N     . TYR   A  1 291 ? 43.92600 -75.12400  -28.60000 1.000 95.73485  ? 283 TYR   A N     1 
ATOM   2189 C  CA    . TYR   A  1 291 ? 43.29300 -74.20800  -29.58400 1.000 97.04149  ? 283 TYR   A CA    1 
ATOM   2190 C  C     . TYR   A  1 291 ? 42.18100 -73.40300  -28.90100 1.000 94.63087  ? 283 TYR   A C     1 
ATOM   2191 O  O     . TYR   A  1 291 ? 42.14700 -72.17300  -29.09300 1.000 97.08926  ? 283 TYR   A O     1 
ATOM   2192 C  CB    . TYR   A  1 291 ? 42.75900 -74.96300  -30.80400 1.000 96.83172  ? 283 TYR   A CB    1 
ATOM   2193 C  CG    . TYR   A  1 291 ? 42.33300 -74.05100  -31.92700 1.000 96.37433  ? 283 TYR   A CG    1 
ATOM   2194 C  CD1   . TYR   A  1 291 ? 43.26600 -73.29300  -32.61600 1.000 94.47211  ? 283 TYR   A CD1   1 
ATOM   2195 C  CD2   . TYR   A  1 291 ? 41.00000 -73.91800  -32.28100 1.000 94.58962  ? 283 TYR   A CD2   1 
ATOM   2196 C  CE1   . TYR   A  1 291 ? 42.88800 -72.43600  -33.63700 1.000 97.53470  ? 283 TYR   A CE1   1 
ATOM   2197 C  CE2   . TYR   A  1 291 ? 40.60600 -73.06800  -33.30100 1.000 93.20772  ? 283 TYR   A CE2   1 
ATOM   2198 C  CZ    . TYR   A  1 291 ? 41.55300 -72.32500  -33.98300 1.000 96.93463  ? 283 TYR   A CZ    1 
ATOM   2199 O  OH    . TYR   A  1 291 ? 41.17200 -71.48700  -34.99000 1.000 100.55789 ? 283 TYR   A OH    1 
ATOM   2200 N  N     . LEU   A  1 292 ? 41.30500 -74.06700  -28.13900 1.000 94.78950  ? 284 LEU   A N     1 
ATOM   2201 C  CA    . LEU   A  1 292 ? 40.22500 -73.40600  -27.35300 1.000 95.22274  ? 284 LEU   A CA    1 
ATOM   2202 C  C     . LEU   A  1 292 ? 40.85300 -72.39900  -26.38300 1.000 98.58179  ? 284 LEU   A C     1 
ATOM   2203 O  O     . LEU   A  1 292 ? 40.34500 -71.26300  -26.29800 1.000 96.54827  ? 284 LEU   A O     1 
ATOM   2204 C  CB    . LEU   A  1 292 ? 39.40900 -74.45600  -26.59200 1.000 89.66773  ? 284 LEU   A CB    1 
ATOM   2205 C  CG    . LEU   A  1 292 ? 38.42900 -75.28200  -27.42400 1.000 88.59684  ? 284 LEU   A CG    1 
ATOM   2206 C  CD1   . LEU   A  1 292 ? 37.78500 -76.36200  -26.57000 1.000 81.96741  ? 284 LEU   A CD1   1 
ATOM   2207 C  CD2   . LEU   A  1 292 ? 37.35900 -74.40100  -28.05500 1.000 87.83417  ? 284 LEU   A CD2   1 
ATOM   2208 N  N     . GLU   A  1 293 ? 41.91300 -72.81600  -25.68100 1.000 97.70435  ? 285 GLU   A N     1 
ATOM   2209 C  CA    . GLU   A  1 293 ? 42.69100 -71.97400  -24.73200 1.000 97.28618  ? 285 GLU   A CA    1 
ATOM   2210 C  C     . GLU   A  1 293 ? 43.24200 -70.75900  -25.48500 1.000 98.88993  ? 285 GLU   A C     1 
ATOM   2211 O  O     . GLU   A  1 293 ? 43.01500 -69.62700  -25.01700 1.000 101.80950 ? 285 GLU   A O     1 
ATOM   2212 C  CB    . GLU   A  1 293 ? 43.81400 -72.79200  -24.08900 1.000 99.30209  ? 285 GLU   A CB    1 
ATOM   2213 C  CG    . GLU   A  1 293 ? 43.32400 -73.76500  -23.02900 1.000 101.66743 ? 285 GLU   A CG    1 
ATOM   2214 C  CD    . GLU   A  1 293 ? 42.91000 -73.11600  -21.71800 1.000 105.99010 ? 285 GLU   A CD    1 
ATOM   2215 O  OE1   . GLU   A  1 293 ? 43.66700 -72.25800  -21.22200 1.000 107.95835 ? 285 GLU   A OE1   1 
ATOM   2216 O  OE2   . GLU   A  1 293 ? 41.83400 -73.47100  -21.19600 1.000 104.78802 ? 285 GLU   A OE2   1 
ATOM   2217 N  N     . TYR   A  1 294 ? 43.92200 -71.00000  -26.61100 1.000 99.51281  ? 286 TYR   A N     1 
ATOM   2218 C  CA    . TYR   A  1 294 ? 44.48900 -69.96800  -27.52300 1.000 102.13783 ? 286 TYR   A CA    1 
ATOM   2219 C  C     . TYR   A  1 294 ? 43.37800 -69.00300  -27.95900 1.000 100.12508 ? 286 TYR   A C     1 
ATOM   2220 O  O     . TYR   A  1 294 ? 43.60300 -67.77700  -27.90800 1.000 100.84548 ? 286 TYR   A O     1 
ATOM   2221 C  CB    . TYR   A  1 294 ? 45.19100 -70.63700  -28.71000 1.000 99.77741  ? 286 TYR   A CB    1 
ATOM   2222 C  CG    . TYR   A  1 294 ? 45.34400 -69.78400  -29.94600 1.000 101.37644 ? 286 TYR   A CG    1 
ATOM   2223 C  CD1   . TYR   A  1 294 ? 46.16600 -68.66800  -29.95400 1.000 104.64734 ? 286 TYR   A CD1   1 
ATOM   2224 C  CD2   . TYR   A  1 294 ? 44.68200 -70.10700  -31.12000 1.000 102.65891 ? 286 TYR   A CD2   1 
ATOM   2225 C  CE1   . TYR   A  1 294 ? 46.31100 -67.88600  -31.09000 1.000 108.77488 ? 286 TYR   A CE1   1 
ATOM   2226 C  CE2   . TYR   A  1 294 ? 44.81800 -69.33800  -32.26500 1.000 103.71810 ? 286 TYR   A CE2   1 
ATOM   2227 C  CZ    . TYR   A  1 294 ? 45.63600 -68.22300  -32.25000 1.000 107.38972 ? 286 TYR   A CZ    1 
ATOM   2228 O  OH    . TYR   A  1 294 ? 45.77700 -67.46300  -33.37500 1.000 113.15106 ? 286 TYR   A OH    1 
ATOM   2229 N  N     . LEU   A  1 295 ? 42.21800 -69.54100  -28.35600 1.000 101.49609 ? 287 LEU   A N     1 
ATOM   2230 C  CA    . LEU   A  1 295 ? 41.03800 -68.75900  -28.82400 1.000 100.66282 ? 287 LEU   A CA    1 
ATOM   2231 C  C     . LEU   A  1 295 ? 40.56400 -67.81600  -27.71100 1.000 104.84905 ? 287 LEU   A C     1 
ATOM   2232 O  O     . LEU   A  1 295 ? 40.52800 -66.59400  -27.95700 1.000 107.25717 ? 287 LEU   A O     1 
ATOM   2233 C  CB    . LEU   A  1 295 ? 39.91600 -69.71100  -29.26100 1.000 95.66206  ? 287 LEU   A CB    1 
ATOM   2234 C  CG    . LEU   A  1 295 ? 39.63700 -69.77200  -30.76400 1.000 93.08532  ? 287 LEU   A CG    1 
ATOM   2235 C  CD1   . LEU   A  1 295 ? 40.89900 -70.05900  -31.56500 1.000 96.01557  ? 287 LEU   A CD1   1 
ATOM   2236 C  CD2   . LEU   A  1 295 ? 38.57200 -70.81300  -31.07200 1.000 87.94136  ? 287 LEU   A CD2   1 
ATOM   2237 N  N     . SER   A  1 296 ? 40.24200 -68.36200  -26.53300 1.000 114.07582 ? 288 SER   A N     1 
ATOM   2238 C  CA    . SER   A  1 296 ? 39.66900 -67.62500  -25.37300 1.000 108.66257 ? 288 SER   A CA    1 
ATOM   2239 C  C     . SER   A  1 296 ? 40.67600 -66.60400  -24.82200 1.000 108.60149 ? 288 SER   A C     1 
ATOM   2240 O  O     . SER   A  1 296 ? 40.23500 -65.65600  -24.14800 1.000 106.22227 ? 288 SER   A O     1 
ATOM   2241 C  CB    . SER   A  1 296 ? 39.21300 -68.57500  -24.29200 1.000 105.13005 ? 288 SER   A CB    1 
ATOM   2242 O  OG    . SER   A  1 296 ? 40.32400 -69.13200  -23.60300 1.000 109.79073 ? 288 SER   A OG    1 
ATOM   2243 N  N     . GLN   A  1 297 ? 41.97200 -66.79700  -25.08600 1.000 108.70146 ? 289 GLN   A N     1 
ATOM   2244 C  CA    . GLN   A  1 297 ? 43.06100 -65.88100  -24.64800 1.000 112.06000 ? 289 GLN   A CA    1 
ATOM   2245 C  C     . GLN   A  1 297 ? 43.27800 -64.79000  -25.70700 1.000 111.49173 ? 289 GLN   A C     1 
ATOM   2246 O  O     . GLN   A  1 297 ? 44.01900 -63.83200  -25.41000 1.000 114.98962 ? 289 GLN   A O     1 
ATOM   2247 C  CB    . GLN   A  1 297 ? 44.35400 -66.66500  -24.39600 1.000 117.02874 ? 289 GLN   A CB    1 
ATOM   2248 C  CG    . GLN   A  1 297 ? 45.07600 -66.26200  -23.11700 1.000 127.92142 ? 289 GLN   A CG    1 
ATOM   2249 C  CD    . GLN   A  1 297 ? 44.30800 -66.64200  -21.87200 1.000 132.14965 ? 289 GLN   A CD    1 
ATOM   2250 O  OE1   . GLN   A  1 297 ? 43.53900 -67.60300  -21.85600 1.000 125.22097 ? 289 GLN   A OE1   1 
ATOM   2251 N  NE2   . GLN   A  1 297 ? 44.51300 -65.88100  -20.80900 1.000 131.29419 ? 289 GLN   A NE2   1 
ATOM   2252 N  N     . ASN   A  1 298 ? 42.66000 -64.93100  -26.88700 1.000 110.17728 ? 290 ASN   A N     1 
ATOM   2253 C  CA    . ASN   A  1 298 ? 42.81000 -64.00100  -28.04100 1.000 111.11080 ? 290 ASN   A CA    1 
ATOM   2254 C  C     . ASN   A  1 298 ? 41.45100 -63.40100  -28.42900 1.000 108.67702 ? 290 ASN   A C     1 
ATOM   2255 O  O     . ASN   A  1 298 ? 41.35300 -62.85100  -29.54700 1.000 111.01407 ? 290 ASN   A O     1 
ATOM   2256 C  CB    . ASN   A  1 298 ? 43.48000 -64.69800  -29.22700 1.000 112.47921 ? 290 ASN   A CB    1 
ATOM   2257 C  CG    . ASN   A  1 298 ? 44.97800 -64.82500  -29.05200 1.000 115.83700 ? 290 ASN   A CG    1 
ATOM   2258 O  OD1   . ASN   A  1 298 ? 45.71600 -63.86900  -29.28000 1.000 122.46063 ? 290 ASN   A OD1   1 
ATOM   2259 N  ND2   . ASN   A  1 298 ? 45.43600 -65.99700  -28.64600 1.000 114.32190 ? 290 ASN   A ND2   1 
ATOM   2260 N  N     . ARG   A  1 299 ? 40.44900 -63.48300  -27.54700 1.000 107.16115 ? 291 ARG   A N     1 
ATOM   2261 C  CA    . ARG   A  1 299 ? 39.17900 -62.71700  -27.66900 1.000 103.84170 ? 291 ARG   A CA    1 
ATOM   2262 C  C     . ARG   A  1 299 ? 39.50600 -61.24100  -27.45700 1.000 109.39036 ? 291 ARG   A C     1 
ATOM   2263 O  O     . ARG   A  1 299 ? 40.51100 -60.92200  -26.82100 1.000 108.53917 ? 291 ARG   A O     1 
ATOM   2264 C  CB    . ARG   A  1 299 ? 38.13900 -63.22100  -26.66200 1.000 102.70260 ? 291 ARG   A CB    1 
ATOM   2265 C  CG    . ARG   A  1 299 ? 38.46400 -62.90100  -25.20800 1.000 105.28420 ? 291 ARG   A CG    1 
ATOM   2266 C  CD    . ARG   A  1 299 ? 37.86700 -63.88900  -24.22000 1.000 95.38214  ? 291 ARG   A CD    1 
ATOM   2267 N  NE    . ARG   A  1 299 ? 36.46300 -63.64500  -23.92400 1.000 94.05910  ? 291 ARG   A NE    1 
ATOM   2268 C  CZ    . ARG   A  1 299 ? 35.72100 -64.38700  -23.10400 1.000 92.08965  ? 291 ARG   A CZ    1 
ATOM   2269 N  NH1   . ARG   A  1 299 ? 36.24800 -65.43400  -22.48800 1.000 88.09444  ? 291 ARG   A NH1   1 
ATOM   2270 N  NH2   . ARG   A  1 299 ? 34.45100 -64.08000  -22.90400 1.000 85.54062  ? 291 ARG   A NH2   1 
ATOM   2271 N  N     . PRO   A  1 300 ? 38.69800 -60.29300  -27.98700 1.000 113.57938 ? 292 PRO   A N     1 
ATOM   2272 C  CA    . PRO   A  1 300 ? 38.89400 -58.87800  -27.67000 1.000 114.68225 ? 292 PRO   A CA    1 
ATOM   2273 C  C     . PRO   A  1 300 ? 38.77100 -58.70700  -26.15700 1.000 115.00439 ? 292 PRO   A C     1 
ATOM   2274 O  O     . PRO   A  1 300 ? 37.91000 -59.33500  -25.54400 1.000 116.35520 ? 292 PRO   A O     1 
ATOM   2275 C  CB    . PRO   A  1 300 ? 37.79200 -58.15300  -28.46300 1.000 114.23970 ? 292 PRO   A CB    1 
ATOM   2276 C  CG    . PRO   A  1 300 ? 36.77000 -59.22900  -28.78400 1.000 108.10651 ? 292 PRO   A CG    1 
ATOM   2277 C  CD    . PRO   A  1 300 ? 37.56300 -60.51600  -28.89600 1.000 107.91590 ? 292 PRO   A CD    1 
ATOM   2278 N  N     . PRO   A  1 301 ? 39.63800 -57.90100  -25.49500 1.000 117.72515 ? 293 PRO   A N     1 
ATOM   2279 C  CA    . PRO   A  1 301 ? 39.55500 -57.70600  -24.04700 1.000 124.62755 ? 293 PRO   A CA    1 
ATOM   2280 C  C     . PRO   A  1 301 ? 38.87000 -56.42400  -23.56600 1.000 130.33639 ? 293 PRO   A C     1 
ATOM   2281 O  O     . PRO   A  1 301 ? 39.44800 -55.67200  -22.78200 1.000 129.95306 ? 293 PRO   A O     1 
ATOM   2282 C  CB    . PRO   A  1 301 ? 41.05700 -57.69700  -23.72100 1.000 121.48707 ? 293 PRO   A CB    1 
ATOM   2283 C  CG    . PRO   A  1 301 ? 41.66300 -56.89500  -24.85900 1.000 113.92160 ? 293 PRO   A CG    1 
ATOM   2284 C  CD    . PRO   A  1 301 ? 40.80100 -57.20500  -26.06900 1.000 114.96808 ? 293 PRO   A CD    1 
ATOM   2285 N  N     . PRO   A  1 302 ? 37.62800 -56.11600  -24.01700 1.000 141.11173 ? 294 PRO   A N     1 
ATOM   2286 C  CA    . PRO   A  1 302 ? 36.76900 -55.15100  -23.32500 1.000 130.79943 ? 294 PRO   A CA    1 
ATOM   2287 C  C     . PRO   A  1 302 ? 36.61700 -55.45700  -21.83400 1.000 125.26170 ? 294 PRO   A C     1 
ATOM   2288 O  O     . PRO   A  1 302 ? 36.83900 -56.59200  -21.41300 1.000 121.39557 ? 294 PRO   A O     1 
ATOM   2289 C  CB    . PRO   A  1 302 ? 35.42400 -55.31700  -24.05500 1.000 128.99730 ? 294 PRO   A CB    1 
ATOM   2290 C  CG    . PRO   A  1 302 ? 35.80700 -55.70800  -25.45500 1.000 132.42568 ? 294 PRO   A CG    1 
ATOM   2291 C  CD    . PRO   A  1 302 ? 37.01200 -56.60100  -25.26300 1.000 134.46294 ? 294 PRO   A CD    1 
ATOM   2292 N  N     . ASN   A  1 303 ? 36.22200 -54.45800  -21.03100 1.000 121.94436 ? 295 ASN   A N     1 
ATOM   2293 C  CA    . ASN   A  1 303 ? 35.87400 -53.11900  -21.48300 1.000 115.64762 ? 295 ASN   A CA    1 
ATOM   2294 C  C     . ASN   A  1 303 ? 35.91600 -52.16100  -20.29000 1.000 115.28670 ? 295 ASN   A C     1 
ATOM   2295 O  O     . ASN   A  1 303 ? 36.20200 -52.62200  -19.16700 1.000 113.63174 ? 295 ASN   A O     1 
ATOM   2296 C  CB    . ASN   A  1 303 ? 34.46000 -53.05200  -22.06800 1.000 110.24941 ? 295 ASN   A CB    1 
ATOM   2297 C  CG    . ASN   A  1 303 ? 34.29900 -52.03300  -23.17700 1.000 111.87299 ? 295 ASN   A CG    1 
ATOM   2298 O  OD1   . ASN   A  1 303 ? 33.24600 -51.41000  -23.30100 1.000 106.54661 ? 295 ASN   A OD1   1 
ATOM   2299 N  ND2   . ASN   A  1 303 ? 35.33100 -51.85400  -23.98500 1.000 121.50557 ? 295 ASN   A ND2   1 
ATOM   2300 N  N     . ALA   A  1 304 ? 35.61500 -50.88200  -20.53000 1.000 113.95218 ? 296 ALA   A N     1 
ATOM   2301 C  CA    . ALA   A  1 304 ? 35.23800 -49.90100  -19.48800 1.000 116.03915 ? 296 ALA   A CA    1 
ATOM   2302 C  C     . ALA   A  1 304 ? 33.94700 -50.38300  -18.81500 1.000 114.95374 ? 296 ALA   A C     1 
ATOM   2303 O  O     . ALA   A  1 304 ? 33.97200 -50.64000  -17.59800 1.000 117.46068 ? 296 ALA   A O     1 
ATOM   2304 C  CB    . ALA   A  1 304 ? 35.07600 -48.53200  -20.10200 1.000 114.55675 ? 296 ALA   A CB    1 
ATOM   2305 N  N     . TYR   A  1 305 ? 32.88100 -50.54900  -19.60600 1.000 98.67381  ? 297 TYR   A N     1 
ATOM   2306 C  CA    . TYR   A  1 305 ? 31.51000 -50.91400  -19.15800 1.000 93.77701  ? 297 TYR   A CA    1 
ATOM   2307 C  C     . TYR   A  1 305 ? 31.47200 -52.37300  -18.68400 1.000 96.28891  ? 297 TYR   A C     1 
ATOM   2308 O  O     . TYR   A  1 305 ? 30.95900 -52.62900  -17.57700 1.000 99.84253  ? 297 TYR   A O     1 
ATOM   2309 C  CB    . TYR   A  1 305 ? 30.51400 -50.67900  -20.29800 1.000 86.95432  ? 297 TYR   A CB    1 
ATOM   2310 C  CG    . TYR   A  1 305 ? 29.06100 -50.85400  -19.93500 1.000 79.69709  ? 297 TYR   A CG    1 
ATOM   2311 C  CD1   . TYR   A  1 305 ? 28.47500 -52.10900  -19.90900 1.000 77.24390  ? 297 TYR   A CD1   1 
ATOM   2312 C  CD2   . TYR   A  1 305 ? 28.26100 -49.76100  -19.63900 1.000 78.17974  ? 297 TYR   A CD2   1 
ATOM   2313 C  CE1   . TYR   A  1 305 ? 27.13900 -52.27700  -19.58600 1.000 71.82372  ? 297 TYR   A CE1   1 
ATOM   2314 C  CE2   . TYR   A  1 305 ? 26.92100 -49.91100  -19.31400 1.000 73.69741  ? 297 TYR   A CE2   1 
ATOM   2315 C  CZ    . TYR   A  1 305 ? 26.35700 -51.17400  -19.28700 1.000 71.07988  ? 297 TYR   A CZ    1 
ATOM   2316 O  OH    . TYR   A  1 305 ? 25.03800 -51.32500  -18.97100 1.000 65.87041  ? 297 TYR   A OH    1 
ATOM   2317 N  N     . GLU   A  1 306 ? 31.99400 -53.29100  -19.50500 1.000 96.99500  ? 298 GLU   A N     1 
ATOM   2318 C  CA    . GLU   A  1 306 ? 31.87200 -54.76800  -19.34600 1.000 97.57971  ? 298 GLU   A CA    1 
ATOM   2319 C  C     . GLU   A  1 306 ? 32.59500 -55.24400  -18.07800 1.000 96.82282  ? 298 GLU   A C     1 
ATOM   2320 O  O     . GLU   A  1 306 ? 31.99300 -56.04500  -17.33200 1.000 97.72252  ? 298 GLU   A O     1 
ATOM   2321 C  CB    . GLU   A  1 306 ? 32.43400 -55.49200  -20.57300 1.000 105.83424 ? 298 GLU   A CB    1 
ATOM   2322 C  CG    . GLU   A  1 306 ? 31.69200 -55.18300  -21.86300 1.000 107.65915 ? 298 GLU   A CG    1 
ATOM   2323 C  CD    . GLU   A  1 306 ? 32.20200 -55.93400  -23.08200 1.000 114.11304 ? 298 GLU   A CD    1 
ATOM   2324 O  OE1   . GLU   A  1 306 ? 32.57300 -57.11600  -22.93400 1.000 112.58342 ? 298 GLU   A OE1   1 
ATOM   2325 O  OE2   . GLU   A  1 306 ? 32.23300 -55.33300  -24.17500 1.000 116.18666 ? 298 GLU   A OE2   1 
ATOM   2326 N  N     . LEU   A  1 307 ? 33.83200 -54.79000  -17.84700 1.000 97.65665  ? 299 LEU   A N     1 
ATOM   2327 C  CA    . LEU   A  1 307 ? 34.67200 -55.22800  -16.69700 1.000 97.38017  ? 299 LEU   A CA    1 
ATOM   2328 C  C     . LEU   A  1 307 ? 34.05700 -54.71800  -15.38500 1.000 99.99350  ? 299 LEU   A C     1 
ATOM   2329 O  O     . LEU   A  1 307 ? 34.12900 -55.45800  -14.38200 1.000 98.58764  ? 299 LEU   A O     1 
ATOM   2330 C  CB    . LEU   A  1 307 ? 36.10900 -54.72500  -16.87200 1.000 100.33157 ? 299 LEU   A CB    1 
ATOM   2331 C  CG    . LEU   A  1 307 ? 37.16900 -55.49600  -16.08300 1.000 103.92178 ? 299 LEU   A CG    1 
ATOM   2332 C  CD1   . LEU   A  1 307 ? 37.70800 -56.66600  -16.89600 1.000 99.89171  ? 299 LEU   A CD1   1 
ATOM   2333 C  CD2   . LEU   A  1 307 ? 38.30600 -54.58200  -15.65000 1.000 103.24994 ? 299 LEU   A CD2   1 
ATOM   2334 N  N     . PHE   A  1 308 ? 33.47800 -53.51000  -15.39300 1.000 97.32639  ? 300 PHE   A N     1 
ATOM   2335 C  CA    . PHE   A  1 308 ? 32.74000 -52.91400  -14.24400 1.000 94.08797  ? 300 PHE   A CA    1 
ATOM   2336 C  C     . PHE   A  1 308 ? 31.40900 -53.65000  -14.03400 1.000 91.80493  ? 300 PHE   A C     1 
ATOM   2337 O  O     . PHE   A  1 308 ? 30.95100 -53.73300  -12.87500 1.000 87.76288  ? 300 PHE   A O     1 
ATOM   2338 C  CB    . PHE   A  1 308 ? 32.48900 -51.41400  -14.44800 1.000 93.67936  ? 300 PHE   A CB    1 
ATOM   2339 C  CG    . PHE   A  1 308 ? 33.61700 -50.49500  -14.04400 1.000 101.93366 ? 300 PHE   A CG    1 
ATOM   2340 C  CD1   . PHE   A  1 308 ? 34.34500 -50.71300  -12.88100 1.000 103.66336 ? 300 PHE   A CD1   1 
ATOM   2341 C  CD2   . PHE   A  1 308 ? 33.92500 -49.37700  -14.80700 1.000 101.56757 ? 300 PHE   A CD2   1 
ATOM   2342 C  CE1   . PHE   A  1 308 ? 35.37200 -49.85700  -12.51300 1.000 103.00149 ? 300 PHE   A CE1   1 
ATOM   2343 C  CE2   . PHE   A  1 308 ? 34.95000 -48.52100  -14.43600 1.000 105.08964 ? 300 PHE   A CE2   1 
ATOM   2344 C  CZ    . PHE   A  1 308 ? 35.67200 -48.76100  -13.29000 1.000 105.55457 ? 300 PHE   A CZ    1 
ATOM   2345 N  N     . ALA   A  1 309 ? 30.81000 -54.16000  -15.11700 1.000 91.08164  ? 301 ALA   A N     1 
ATOM   2346 C  CA    . ALA   A  1 309 ? 29.48700 -54.83000  -15.13100 1.000 85.18264  ? 301 ALA   A CA    1 
ATOM   2347 C  C     . ALA   A  1 309 ? 29.63500 -56.34400  -14.93100 1.000 86.15660  ? 301 ALA   A C     1 
ATOM   2348 O  O     . ALA   A  1 309 ? 28.59200 -57.02500  -14.85800 1.000 81.98252  ? 301 ALA   A O     1 
ATOM   2349 C  CB    . ALA   A  1 309 ? 28.77200 -54.52300  -16.42400 1.000 83.63362  ? 301 ALA   A CB    1 
ATOM   2350 N  N     . LYS   A  1 310 ? 30.86900 -56.85500  -14.84200 1.000 83.40607  ? 302 LYS   A N     1 
ATOM   2351 C  CA    . LYS   A  1 310 ? 31.14900 -58.30900  -14.69800 1.000 80.96668  ? 302 LYS   A CA    1 
ATOM   2352 C  C     . LYS   A  1 310 ? 30.69500 -58.76800  -13.30800 1.000 77.62448  ? 302 LYS   A C     1 
ATOM   2353 O  O     . LYS   A  1 310 ? 31.31000 -58.33700  -12.31500 1.000 79.90888  ? 302 LYS   A O     1 
ATOM   2354 C  CB    . LYS   A  1 310 ? 32.63300 -58.60900  -14.93800 1.000 84.89786  ? 302 LYS   A CB    1 
ATOM   2355 C  CG    . LYS   A  1 310 ? 32.98800 -60.08700  -15.06000 1.000 86.34731  ? 302 LYS   A CG    1 
ATOM   2356 C  CD    . LYS   A  1 310 ? 32.14200 -60.83800  -16.07500 1.000 84.19173  ? 302 LYS   A CD    1 
ATOM   2357 C  CE    . LYS   A  1 310 ? 32.49300 -62.30500  -16.20500 1.000 82.11985  ? 302 LYS   A CE    1 
ATOM   2358 N  NZ    . LYS   A  1 310 ? 33.74800 -62.50800  -16.96600 1.000 83.12184  ? 302 LYS   A NZ    1 
ATOM   2359 N  N     . GLY   A  1 311 ? 29.65100 -59.60300  -13.25700 1.000 75.62683  ? 303 GLY   A N     1 
ATOM   2360 C  CA    . GLY   A  1 311 ? 29.05600 -60.14900  -12.02100 1.000 73.00029  ? 303 GLY   A CA    1 
ATOM   2361 C  C     . GLY   A  1 311 ? 27.55500 -59.92000  -11.96700 1.000 72.63383  ? 303 GLY   A C     1 
ATOM   2362 O  O     . GLY   A  1 311 ? 26.86500 -60.70100  -11.27900 1.000 74.82745  ? 303 GLY   A O     1 
ATOM   2363 N  N     . TYR   A  1 312 ? 27.06400 -58.89600  -12.67300 1.000 66.02036  ? 304 TYR   A N     1 
ATOM   2364 C  CA    . TYR   A  1 312 ? 25.65600 -58.41900  -12.62200 1.000 71.14637  ? 304 TYR   A CA    1 
ATOM   2365 C  C     . TYR   A  1 312 ? 24.84400 -59.00800  -13.78400 1.000 66.54449  ? 304 TYR   A C     1 
ATOM   2366 O  O     . TYR   A  1 312 ? 23.65400 -58.64600  -13.91100 1.000 64.59771  ? 304 TYR   A O     1 
ATOM   2367 C  CB    . TYR   A  1 312 ? 25.61400 -56.88700  -12.65000 1.000 70.79950  ? 304 TYR   A CB    1 
ATOM   2368 C  CG    . TYR   A  1 312 ? 26.15300 -56.20800  -11.41400 1.000 70.62670  ? 304 TYR   A CG    1 
ATOM   2369 C  CD1   . TYR   A  1 312 ? 25.33200 -55.93700  -10.33000 1.000 69.40774  ? 304 TYR   A CD1   1 
ATOM   2370 C  CD2   . TYR   A  1 312 ? 27.48000 -55.81500  -11.33200 1.000 70.06176  ? 304 TYR   A CD2   1 
ATOM   2371 C  CE1   . TYR   A  1 312 ? 25.81500 -55.30600  -9.19500  1.000 70.49567  ? 304 TYR   A CE1   1 
ATOM   2372 C  CE2   . TYR   A  1 312 ? 27.97900 -55.18300  -10.20400 1.000 71.95258  ? 304 TYR   A CE2   1 
ATOM   2373 C  CZ    . TYR   A  1 312 ? 27.14400 -54.92700  -9.13100  1.000 72.56701  ? 304 TYR   A CZ    1 
ATOM   2374 O  OH    . TYR   A  1 312 ? 27.63300 -54.30300  -8.02100  1.000 80.72379  ? 304 TYR   A OH    1 
ATOM   2375 N  N     . GLU   A  1 313 ? 25.45000 -59.89100  -14.58800 1.000 68.10998  ? 305 GLU   A N     1 
ATOM   2376 C  CA    . GLU   A  1 313 ? 24.86100 -60.41800  -15.84900 1.000 61.52840  ? 305 GLU   A CA    1 
ATOM   2377 C  C     . GLU   A  1 313 ? 23.61100 -61.24300  -15.52600 1.000 58.91278  ? 305 GLU   A C     1 
ATOM   2378 O  O     . GLU   A  1 313 ? 23.73800 -62.21700  -14.76400 1.000 65.54466  ? 305 GLU   A O     1 
ATOM   2379 C  CB    . GLU   A  1 313 ? 25.87000 -61.27400  -16.61800 1.000 65.35923  ? 305 GLU   A CB    1 
ATOM   2380 C  CG    . GLU   A  1 313 ? 27.12300 -60.52700  -17.04000 1.000 64.43783  ? 305 GLU   A CG    1 
ATOM   2381 C  CD    . GLU   A  1 313 ? 28.39000 -60.97500  -16.33100 1.000 77.62750  ? 305 GLU   A CD    1 
ATOM   2382 O  OE1   . GLU   A  1 313 ? 28.42100 -60.92700  -15.08300 1.000 75.14581  ? 305 GLU   A OE1   1 
ATOM   2383 O  OE2   . GLU   A  1 313 ? 29.33700 -61.38800  -17.03100 1.000 84.05409  ? 305 GLU   A OE2   1 
ATOM   2384 N  N     . ASP   A  1 314 ? 22.45800 -60.84500  -16.07600 1.000 56.52587  ? 306 ASP   A N     1 
ATOM   2385 C  CA    . ASP   A  1 314 ? 21.14300 -61.53600  -15.95100 1.000 59.63869  ? 306 ASP   A CA    1 
ATOM   2386 C  C     . ASP   A  1 314 ? 20.76200 -61.69200  -14.47300 1.000 59.18648  ? 306 ASP   A C     1 
ATOM   2387 O  O     . ASP   A  1 314 ? 19.93400 -62.57400  -14.15900 1.000 58.22945  ? 306 ASP   A O     1 
ATOM   2388 C  CB    . ASP   A  1 314 ? 21.16000 -62.87600  -16.68700 1.000 57.59801  ? 306 ASP   A CB    1 
ATOM   2389 C  CG    . ASP   A  1 314 ? 21.36000 -62.72100  -18.18200 1.000 64.03791  ? 306 ASP   A CG    1 
ATOM   2390 O  OD1   . ASP   A  1 314 ? 20.83400 -61.73300  -18.74500 1.000 57.04078  ? 306 ASP   A OD1   1 
ATOM   2391 O  OD2   . ASP   A  1 314 ? 22.05100 -63.57900  -18.77100 1.000 71.51418  ? 306 ASP   A OD2   1 
ATOM   2392 N  N     . TYR   A  1 315 ? 21.32300 -60.84100  -13.61200 1.000 55.00525  ? 307 TYR   A N     1 
ATOM   2393 C  CA    . TYR   A  1 315 ? 21.03100 -60.78000  -12.16000 1.000 58.45150  ? 307 TYR   A CA    1 
ATOM   2394 C  C     . TYR   A  1 315 ? 19.92000 -59.74900  -11.95600 1.000 53.94517  ? 307 TYR   A C     1 
ATOM   2395 O  O     . TYR   A  1 315 ? 20.15900 -58.55200  -12.21100 1.000 56.81413  ? 307 TYR   A O     1 
ATOM   2396 C  CB    . TYR   A  1 315 ? 22.30800 -60.45300  -11.38200 1.000 63.50487  ? 307 TYR   A CB    1 
ATOM   2397 C  CG    . TYR   A  1 315 ? 22.10600 -60.20600  -9.91000  1.000 67.88914  ? 307 TYR   A CG    1 
ATOM   2398 C  CD1   . TYR   A  1 315 ? 21.97700 -61.25700  -9.01600  1.000 71.24525  ? 307 TYR   A CD1   1 
ATOM   2399 C  CD2   . TYR   A  1 315 ? 22.05400 -58.91600  -9.40700  1.000 69.59122  ? 307 TYR   A CD2   1 
ATOM   2400 C  CE1   . TYR   A  1 315 ? 21.79700 -61.03300  -7.65900  1.000 71.76480  ? 307 TYR   A CE1   1 
ATOM   2401 C  CE2   . TYR   A  1 315 ? 21.87600 -58.67500  -8.05500  1.000 75.29991  ? 307 TYR   A CE2   1 
ATOM   2402 C  CZ    . TYR   A  1 315 ? 21.74500 -59.73600  -7.17800  1.000 73.72039  ? 307 TYR   A CZ    1 
ATOM   2403 O  OH    . TYR   A  1 315 ? 21.56900 -59.49800  -5.84700  1.000 88.31970  ? 307 TYR   A OH    1 
ATOM   2404 N  N     . LEU   A  1 316 ? 18.73600 -60.21500  -11.55000 1.000 50.93745  ? 308 LEU   A N     1 
ATOM   2405 C  CA    . LEU   A  1 316 ? 17.54000 -59.36500  -11.31600 1.000 55.25168  ? 308 LEU   A CA    1 
ATOM   2406 C  C     . LEU   A  1 316 ? 17.74300 -58.55800  -10.02700 1.000 61.36779  ? 308 LEU   A C     1 
ATOM   2407 O  O     . LEU   A  1 316 ? 18.30300 -59.11400  -9.05900  1.000 66.30598  ? 308 LEU   A O     1 
ATOM   2408 C  CB    . LEU   A  1 316 ? 16.29100 -60.25000  -11.23400 1.000 54.06176  ? 308 LEU   A CB    1 
ATOM   2409 C  CG    . LEU   A  1 316 ? 15.96900 -61.06200  -12.48800 1.000 49.92017  ? 308 LEU   A CG    1 
ATOM   2410 C  CD1   . LEU   A  1 316 ? 14.77700 -61.97300  -12.25000 1.000 48.42687  ? 308 LEU   A CD1   1 
ATOM   2411 C  CD2   . LEU   A  1 316 ? 15.70400 -60.15700  -13.68200 1.000 50.43115  ? 308 LEU   A CD2   1 
ATOM   2412 N  N     . GLN   A  1 317 ? 17.32500 -57.28800  -10.04100 1.000 58.46049  ? 309 GLN   A N     1 
ATOM   2413 C  CA    . GLN   A  1 317 ? 17.37700 -56.34600  -8.88900  1.000 57.32956  ? 309 GLN   A CA    1 
ATOM   2414 C  C     . GLN   A  1 317 ? 16.08800 -55.51900  -8.86500  1.000 55.83355  ? 309 GLN   A C     1 
ATOM   2415 O  O     . GLN   A  1 317 ? 15.61000 -55.14400  -9.95500  1.000 57.60092  ? 309 GLN   A O     1 
ATOM   2416 C  CB    . GLN   A  1 317 ? 18.58700 -55.41500  -8.99800  1.000 56.14564  ? 309 GLN   A CB    1 
ATOM   2417 C  CG    . GLN   A  1 317 ? 19.86300 -56.12000  -9.43800  1.000 63.00138  ? 309 GLN   A CG    1 
ATOM   2418 C  CD    . GLN   A  1 317 ? 21.09400 -55.25400  -9.33300  1.000 65.97777  ? 309 GLN   A CD    1 
ATOM   2419 O  OE1   . GLN   A  1 317 ? 21.90900 -55.19800  -10.25200 1.000 64.66563  ? 309 GLN   A OE1   1 
ATOM   2420 N  NE2   . GLN   A  1 317 ? 21.24400 -54.57300  -8.20700  1.000 65.90781  ? 309 GLN   A NE2   1 
ATOM   2421 N  N     . SER   A  1 318 ? 15.54600 -55.25000  -7.67500  1.000 57.78829  ? 310 SER   A N     1 
ATOM   2422 C  CA    . SER   A  1 318 ? 14.43500 -54.28500  -7.46900  1.000 59.11751  ? 310 SER   A CA    1 
ATOM   2423 C  C     . SER   A  1 318 ? 14.92500 -52.89900  -7.88200  1.000 62.94396  ? 310 SER   A C     1 
ATOM   2424 O  O     . SER   A  1 318 ? 16.05200 -52.52800  -7.55700  1.000 63.93645  ? 310 SER   A O     1 
ATOM   2425 C  CB    . SER   A  1 318 ? 13.94700 -54.30400  -6.04400  1.000 61.62053  ? 310 SER   A CB    1 
ATOM   2426 O  OG    . SER   A  1 318 ? 13.51900 -55.60500  -5.67100  1.000 73.82121  ? 310 SER   A OG    1 
ATOM   2427 N  N     . PRO   A  1 319 ? 14.14400 -52.11100  -8.65700  1.000 60.98006  ? 311 PRO   A N     1 
ATOM   2428 C  CA    . PRO   A  1 319 ? 14.52800 -50.73700  -8.97000  1.000 64.28027  ? 311 PRO   A CA    1 
ATOM   2429 C  C     . PRO   A  1 319 ? 14.55100 -49.89000  -7.68800  1.000 70.79653  ? 311 PRO   A C     1 
ATOM   2430 O  O     . PRO   A  1 319 ? 13.56000 -49.88800  -6.97300  1.000 68.68415  ? 311 PRO   A O     1 
ATOM   2431 C  CB    . PRO   A  1 319 ? 13.45100 -50.24400  -9.95200  1.000 60.63480  ? 311 PRO   A CB    1 
ATOM   2432 C  CG    . PRO   A  1 319 ? 12.78000 -51.50800  -10.45400 1.000 57.24145  ? 311 PRO   A CG    1 
ATOM   2433 C  CD    . PRO   A  1 319 ? 12.88500 -52.49600  -9.31100  1.000 62.16304  ? 311 PRO   A CD    1 
ATOM   2434 N  N     . LEU   A  1 320 ? 15.67800 -49.22400  -7.41600  1.000 70.15797  ? 312 LEU   A N     1 
ATOM   2435 C  CA    . LEU   A  1 320 ? 15.84200 -48.30400  -6.25900  1.000 69.31636  ? 312 LEU   A CA    1 
ATOM   2436 C  C     . LEU   A  1 320 ? 14.79500 -47.19100  -6.36900  1.000 68.46716  ? 312 LEU   A C     1 
ATOM   2437 O  O     . LEU   A  1 320 ? 14.47200 -46.79200  -7.51200  1.000 67.81972  ? 312 LEU   A O     1 
ATOM   2438 C  CB    . LEU   A  1 320 ? 17.26100 -47.72000  -6.23800  1.000 62.69254  ? 312 LEU   A CB    1 
ATOM   2439 C  CG    . LEU   A  1 320 ? 18.39100 -48.69800  -5.90900  1.000 68.35509  ? 312 LEU   A CG    1 
ATOM   2440 C  CD1   . LEU   A  1 320 ? 19.72900 -47.97400  -5.84900  1.000 61.45927  ? 312 LEU   A CD1   1 
ATOM   2441 C  CD2   . LEU   A  1 320 ? 18.13400 -49.43200  -4.60000  1.000 71.74511  ? 312 LEU   A CD2   1 
ATOM   2442 N  N     . GLN   A  1 321 ? 14.28000 -46.74000  -5.22100  1.000 66.42575  ? 313 GLN   A N     1 
ATOM   2443 C  CA    . GLN   A  1 321 ? 13.35700 -45.58200  -5.09300  1.000 64.36938  ? 313 GLN   A CA    1 
ATOM   2444 C  C     . GLN   A  1 321 ? 14.00300 -44.57100  -4.15100  1.000 66.53702  ? 313 GLN   A C     1 
ATOM   2445 O  O     . GLN   A  1 321 ? 13.70600 -44.55800  -2.95800  1.000 64.24014  ? 313 GLN   A O     1 
ATOM   2446 C  CB    . GLN   A  1 321 ? 11.98700 -46.04900  -4.59900  1.000 59.08923  ? 313 GLN   A CB    1 
ATOM   2447 C  CG    . GLN   A  1 321 ? 11.44000 -47.23200  -5.38600  1.000 57.53034  ? 313 GLN   A CG    1 
ATOM   2448 C  CD    . GLN   A  1 321 ? 9.94300  -47.37300  -5.26500  1.000 62.71621  ? 313 GLN   A CD    1 
ATOM   2449 O  OE1   . GLN   A  1 321 ? 9.26300  -46.53300  -4.67800  1.000 64.76011  ? 313 GLN   A OE1   1 
ATOM   2450 N  NE2   . GLN   A  1 321 ? 9.41400  -48.44100  -5.84000  1.000 61.71862  ? 313 GLN   A NE2   1 
ATOM   2451 N  N     . PRO   A  1 322 ? 14.92900 -43.71900  -4.65400  1.000 65.61478  ? 314 PRO   A N     1 
ATOM   2452 C  CA    . PRO   A  1 322 ? 15.61100 -42.72800  -3.81700  1.000 63.23622  ? 314 PRO   A CA    1 
ATOM   2453 C  C     . PRO   A  1 322 ? 14.67500 -41.72400  -3.12400  1.000 63.36107  ? 314 PRO   A C     1 
ATOM   2454 O  O     . PRO   A  1 322 ? 15.11600 -41.09600  -2.18200  1.000 65.23188  ? 314 PRO   A O     1 
ATOM   2455 C  CB    . PRO   A  1 322 ? 16.53200 -41.98900  -4.80400  1.000 63.04727  ? 314 PRO   A CB    1 
ATOM   2456 C  CG    . PRO   A  1 322 ? 16.72800 -42.97000  -5.94000  1.000 61.80292  ? 314 PRO   A CG    1 
ATOM   2457 C  CD    . PRO   A  1 322 ? 15.40000 -43.68800  -6.04800  1.000 60.66432  ? 314 PRO   A CD    1 
ATOM   2458 N  N     . LEU   A  1 323 ? 13.43200 -41.59500  -3.60300  1.000 63.20888  ? 315 LEU   A N     1 
ATOM   2459 C  CA    . LEU   A  1 323 ? 12.39200 -40.69700  -3.03400  1.000 64.34289  ? 315 LEU   A CA    1 
ATOM   2460 C  C     . LEU   A  1 323 ? 11.73900 -41.36700  -1.81500  1.000 67.10883  ? 315 LEU   A C     1 
ATOM   2461 O  O     . LEU   A  1 323 ? 11.85000 -40.81800  -0.70200  1.000 69.64566  ? 315 LEU   A O     1 
ATOM   2462 C  CB    . LEU   A  1 323 ? 11.36000 -40.38200  -4.12500  1.000 64.48991  ? 315 LEU   A CB    1 
ATOM   2463 C  CG    . LEU   A  1 323 ? 10.29100 -39.35600  -3.75100  1.000 65.94146  ? 315 LEU   A CG    1 
ATOM   2464 C  CD1   . LEU   A  1 323 ? 10.91500 -37.99500  -3.50000  1.000 67.49570  ? 315 LEU   A CD1   1 
ATOM   2465 C  CD2   . LEU   A  1 323 ? 9.23100  -39.25300  -4.83400  1.000 66.16729  ? 315 LEU   A CD2   1 
ATOM   2466 N  N     . MET   A  1 324 ? 11.08100 -42.50900  -2.02300  1.000 62.99646  ? 316 MET   A N     1 
ATOM   2467 C  CA    . MET   A  1 324 ? 10.31700 -43.25600  -0.98700  1.000 66.39304  ? 316 MET   A CA    1 
ATOM   2468 C  C     . MET   A  1 324 ? 11.27000 -43.74700  0.11200   1.000 62.93694  ? 316 MET   A C     1 
ATOM   2469 O  O     . MET   A  1 324 ? 10.87900 -43.69800  1.29300   1.000 63.79397  ? 316 MET   A O     1 
ATOM   2470 C  CB    . MET   A  1 324 ? 9.60300  -44.45200  -1.62700  1.000 66.28327  ? 316 MET   A CB    1 
ATOM   2471 C  CG    . MET   A  1 324 ? 8.80300  -45.30200  -0.65700  1.000 66.97739  ? 316 MET   A CG    1 
ATOM   2472 S  SD    . MET   A  1 324 ? 8.10400  -46.77000  -1.46900  1.000 83.48578  ? 316 MET   A SD    1 
ATOM   2473 C  CE    . MET   A  1 324 ? 9.58700  -47.71900  -1.81500  1.000 59.21472  ? 316 MET   A CE    1 
ATOM   2474 N  N     . ASP   A  1 325 ? 12.46200 -44.21700  -0.27600  1.000 64.66277  ? 317 ASP   A N     1 
ATOM   2475 C  CA    . ASP   A  1 325 ? 13.50300 -44.78000  0.62600   1.000 62.30965  ? 317 ASP   A CA    1 
ATOM   2476 C  C     . ASP   A  1 325 ? 14.70400 -43.83200  0.67800   1.000 63.25848  ? 317 ASP   A C     1 
ATOM   2477 O  O     . ASP   A  1 325 ? 14.98200 -43.18200  -0.34200  1.000 65.26716  ? 317 ASP   A O     1 
ATOM   2478 C  CB    . ASP   A  1 325 ? 13.98000 -46.15200  0.14500   1.000 60.97004  ? 317 ASP   A CB    1 
ATOM   2479 C  CG    . ASP   A  1 325 ? 12.88900 -47.20200  0.03100   1.000 64.21819  ? 317 ASP   A CG    1 
ATOM   2480 O  OD1   . ASP   A  1 325 ? 12.17600 -47.42200  1.03400   1.000 61.87063  ? 317 ASP   A OD1   1 
ATOM   2481 O  OD2   . ASP   A  1 325 ? 12.76900 -47.79800  -1.06000  1.000 69.42119  ? 317 ASP   A OD2   1 
ATOM   2482 N  N     . ASN   A  1 326 ? 15.38900 -43.76600  1.82300   1.000 64.25091  ? 318 ASN   A N     1 
ATOM   2483 C  CA    . ASN   A  1 326 ? 16.69300 -43.06800  1.97400   1.000 65.35320  ? 318 ASN   A CA    1 
ATOM   2484 C  C     . ASN   A  1 326 ? 17.79600 -44.01600  1.50000   1.000 64.65893  ? 318 ASN   A C     1 
ATOM   2485 O  O     . ASN   A  1 326 ? 17.90000 -45.11800  2.06400   1.000 64.57406  ? 318 ASN   A O     1 
ATOM   2486 C  CB    . ASN   A  1 326 ? 16.94600 -42.61400  3.41500   1.000 66.96087  ? 318 ASN   A CB    1 
ATOM   2487 C  CG    . ASN   A  1 326 ? 16.09000 -41.44000  3.83900   1.000 68.02256  ? 318 ASN   A CG    1 
ATOM   2488 O  OD1   . ASN   A  1 326 ? 15.67100 -40.63200  3.01400   1.000 68.00148  ? 318 ASN   A OD1   1 
ATOM   2489 N  ND2   . ASN   A  1 326 ? 15.83600 -41.32900  5.13300   1.000 69.76469  ? 318 ASN   A ND2   1 
ATOM   2490 N  N     . LEU   A  1 327 ? 18.57400 -43.60900  0.49300   1.000 64.70394  ? 319 LEU   A N     1 
ATOM   2491 C  CA    . LEU   A  1 327 ? 19.69100 -44.41800  -0.06500  1.000 64.28313  ? 319 LEU   A CA    1 
ATOM   2492 C  C     . LEU   A  1 327 ? 20.78000 -44.56600  1.00100   1.000 65.63041  ? 319 LEU   A C     1 
ATOM   2493 O  O     . LEU   A  1 327 ? 20.97900 -43.61700  1.78400   1.000 67.17260  ? 319 LEU   A O     1 
ATOM   2494 C  CB    . LEU   A  1 327 ? 20.24300 -43.75100  -1.32900  1.000 64.50239  ? 319 LEU   A CB    1 
ATOM   2495 C  CG    . LEU   A  1 327 ? 19.30000 -43.71600  -2.53100  1.000 63.33713  ? 319 LEU   A CG    1 
ATOM   2496 C  CD1   . LEU   A  1 327 ? 19.94800 -42.98400  -3.69500  1.000 63.99773  ? 319 LEU   A CD1   1 
ATOM   2497 C  CD2   . LEU   A  1 327 ? 18.88600 -45.11800  -2.95400  1.000 61.60050  ? 319 LEU   A CD2   1 
ATOM   2498 N  N     . GLU   A  1 328 ? 21.44800 -45.72100  1.01900   1.000 65.21325  ? 320 GLU   A N     1 
ATOM   2499 C  CA    . GLU   A  1 328 ? 22.50900 -46.06700  2.00000   1.000 66.62390  ? 320 GLU   A CA    1 
ATOM   2500 C  C     . GLU   A  1 328 ? 23.79900 -45.34400  1.60000   1.000 68.09621  ? 320 GLU   A C     1 
ATOM   2501 O  O     . GLU   A  1 328 ? 23.88300 -44.86900  0.45200   1.000 67.71514  ? 320 GLU   A O     1 
ATOM   2502 C  CB    . GLU   A  1 328 ? 22.69700 -47.58300  2.06300   1.000 65.76441  ? 320 GLU   A CB    1 
ATOM   2503 C  CG    . GLU   A  1 328 ? 21.41600 -48.33300  2.39300   1.000 66.71685  ? 320 GLU   A CG    1 
ATOM   2504 C  CD    . GLU   A  1 328 ? 21.56400 -49.83900  2.51600   1.000 74.44606  ? 320 GLU   A CD    1 
ATOM   2505 O  OE1   . GLU   A  1 328 ? 22.60300 -50.37200  2.07600   1.000 77.16079  ? 320 GLU   A OE1   1 
ATOM   2506 O  OE2   . GLU   A  1 328 ? 20.63400 -50.47600  3.05000   1.000 86.14171  ? 320 GLU   A OE2   1 
ATOM   2507 N  N     . SER   A  1 329 ? 24.75900 -45.25800  2.52200   1.000 69.95385  ? 321 SER   A N     1 
ATOM   2508 C  CA    . SER   A  1 329 ? 26.03400 -44.51500  2.34800   1.000 71.91515  ? 321 SER   A CA    1 
ATOM   2509 C  C     . SER   A  1 329 ? 26.85300 -45.13300  1.20800   1.000 71.65508  ? 321 SER   A C     1 
ATOM   2510 O  O     . SER   A  1 329 ? 27.31900 -44.37000  0.34200   1.000 72.15907  ? 321 SER   A O     1 
ATOM   2511 C  CB    . SER   A  1 329 ? 26.81400 -44.47700  3.63200   1.000 74.07584  ? 321 SER   A CB    1 
ATOM   2512 O  OG    . SER   A  1 329 ? 28.01800 -43.74800  3.46300   1.000 76.19368  ? 321 SER   A OG    1 
ATOM   2513 N  N     . GLN   A  1 330 ? 27.00900 -46.46200  1.20500   1.000 73.74379  ? 322 GLN   A N     1 
ATOM   2514 C  CA    . GLN   A  1 330 ? 27.81000 -47.21200  0.19700   1.000 71.80501  ? 322 GLN   A CA    1 
ATOM   2515 C  C     . GLN   A  1 330 ? 27.15400 -47.11000  -1.18600  1.000 73.71004  ? 322 GLN   A C     1 
ATOM   2516 O  O     . GLN   A  1 330 ? 27.90000 -47.12800  -2.17900  1.000 79.79058  ? 322 GLN   A O     1 
ATOM   2517 C  CB    . GLN   A  1 330 ? 27.98100 -48.68100  0.59000   1.000 71.01052  ? 322 GLN   A CB    1 
ATOM   2518 C  CG    . GLN   A  1 330 ? 29.30800 -48.97800  1.27600   1.000 74.46940  ? 322 GLN   A CG    1 
ATOM   2519 C  CD    . GLN   A  1 330 ? 29.57900 -50.45700  1.40700   1.000 83.74081  ? 322 GLN   A CD    1 
ATOM   2520 O  OE1   . GLN   A  1 330 ? 29.09700 -51.27500  0.62500   1.000 89.36576  ? 322 GLN   A OE1   1 
ATOM   2521 N  NE2   . GLN   A  1 330 ? 30.36800 -50.81500  2.40700   1.000 83.39969  ? 322 GLN   A NE2   1 
ATOM   2522 N  N     . THR   A  1 331 ? 25.82100 -47.02500  -1.25100  1.000 69.79866  ? 323 THR   A N     1 
ATOM   2523 C  CA    . THR   A  1 331 ? 25.04900 -46.82900  -2.50900  1.000 68.67721  ? 323 THR   A CA    1 
ATOM   2524 C  C     . THR   A  1 331 ? 25.51000 -45.53000  -3.17700  1.000 67.46631  ? 323 THR   A C     1 
ATOM   2525 O  O     . THR   A  1 331 ? 25.90600 -45.58100  -4.35200  1.000 72.12599  ? 323 THR   A O     1 
ATOM   2526 C  CB    . THR   A  1 331 ? 23.53700 -46.80700  -2.25500  1.000 66.27598  ? 323 THR   A CB    1 
ATOM   2527 O  OG1   . THR   A  1 331 ? 23.15200 -48.09300  -1.76900  1.000 64.89713  ? 323 THR   A OG1   1 
ATOM   2528 C  CG2   . THR   A  1 331 ? 22.73300 -46.46800  -3.49100  1.000 62.89704  ? 323 THR   A CG2   1 
ATOM   2529 N  N     . TYR   A  1 332 ? 25.45800 -44.41400  -2.44800  1.000 68.27997  ? 324 TYR   A N     1 
ATOM   2530 C  CA    . TYR   A  1 332 ? 25.98200 -43.09900  -2.89600  1.000 69.83270  ? 324 TYR   A CA    1 
ATOM   2531 C  C     . TYR   A  1 332 ? 27.43100 -43.28200  -3.37200  1.000 74.54461  ? 324 TYR   A C     1 
ATOM   2532 O  O     . TYR   A  1 332 ? 27.72600 -42.95900  -4.53500  1.000 82.46730  ? 324 TYR   A O     1 
ATOM   2533 C  CB    . TYR   A  1 332 ? 25.88900 -42.05400  -1.77900  1.000 71.35553  ? 324 TYR   A CB    1 
ATOM   2534 C  CG    . TYR   A  1 332 ? 24.51600 -41.48500  -1.51500  1.000 70.50994  ? 324 TYR   A CG    1 
ATOM   2535 C  CD1   . TYR   A  1 332 ? 23.80800 -40.82300  -2.50600  1.000 70.05174  ? 324 TYR   A CD1   1 
ATOM   2536 C  CD2   . TYR   A  1 332 ? 23.93700 -41.56900  -0.25800  1.000 70.46980  ? 324 TYR   A CD2   1 
ATOM   2537 C  CE1   . TYR   A  1 332 ? 22.55300 -40.28700  -2.26500  1.000 69.54178  ? 324 TYR   A CE1   1 
ATOM   2538 C  CE2   . TYR   A  1 332 ? 22.68400 -41.03900  0.00100   1.000 69.93485  ? 324 TYR   A CE2   1 
ATOM   2539 C  CZ    . TYR   A  1 332 ? 21.98800 -40.39400  -1.00600  1.000 69.47375  ? 324 TYR   A CZ    1 
ATOM   2540 O  OH    . TYR   A  1 332 ? 20.75300 -39.87400  -0.75200  1.000 69.17358  ? 324 TYR   A OH    1 
ATOM   2541 N  N     . GLU   A  1 333 ? 28.29300 -43.83100  -2.51100  1.000 72.39490  ? 325 GLU   A N     1 
ATOM   2542 C  CA    . GLU   A  1 333 ? 29.76600 -43.92800  -2.72200  1.000 74.32034  ? 325 GLU   A CA    1 
ATOM   2543 C  C     . GLU   A  1 333 ? 30.08700 -44.43000  -4.13800  1.000 77.99193  ? 325 GLU   A C     1 
ATOM   2544 O  O     . GLU   A  1 333 ? 30.97800 -43.83400  -4.77700  1.000 84.47897  ? 325 GLU   A O     1 
ATOM   2545 C  CB    . GLU   A  1 333 ? 30.40600 -44.85300  -1.68400  1.000 74.98556  ? 325 GLU   A CB    1 
ATOM   2546 C  CG    . GLU   A  1 333 ? 31.92600 -44.81900  -1.69900  1.000 77.58883  ? 325 GLU   A CG    1 
ATOM   2547 C  CD    . GLU   A  1 333 ? 32.60900 -45.75800  -0.71700  1.000 78.56837  ? 325 GLU   A CD    1 
ATOM   2548 O  OE1   . GLU   A  1 333 ? 32.11200 -46.88700  -0.53300  1.000 76.81776  ? 325 GLU   A OE1   1 
ATOM   2549 O  OE2   . GLU   A  1 333 ? 33.64200 -45.35800  -0.14200  1.000 81.28351  ? 325 GLU   A OE2   1 
ATOM   2550 N  N     . VAL   A  1 334 ? 29.39900 -45.47600  -4.61100  1.000 72.15410  ? 326 VAL   A N     1 
ATOM   2551 C  CA    . VAL   A  1 334 ? 29.76200 -46.20100  -5.86700  1.000 78.81526  ? 326 VAL   A CA    1 
ATOM   2552 C  C     . VAL   A  1 334 ? 29.26600 -45.42500  -7.09300  1.000 80.76941  ? 326 VAL   A C     1 
ATOM   2553 O  O     . VAL   A  1 334 ? 29.65200 -45.81600  -8.20400  1.000 87.29222  ? 326 VAL   A O     1 
ATOM   2554 C  CB    . VAL   A  1 334 ? 29.22700 -47.64800  -5.89600  1.000 77.38327  ? 326 VAL   A CB    1 
ATOM   2555 C  CG1   . VAL   A  1 334 ? 29.61600 -48.42900  -4.65100  1.000 73.83248  ? 326 VAL   A CG1   1 
ATOM   2556 C  CG2   . VAL   A  1 334 ? 27.72400 -47.70700  -6.12500  1.000 73.89939  ? 326 VAL   A CG2   1 
ATOM   2557 N  N     . PHE   A  1 335 ? 28.42900 -44.39800  -6.91800  1.000 76.94797  ? 327 PHE   A N     1 
ATOM   2558 C  CA    . PHE   A  1 335 ? 27.76900 -43.67500  -8.03700  1.000 73.79530  ? 327 PHE   A CA    1 
ATOM   2559 C  C     . PHE   A  1 335 ? 28.20500 -42.20200  -8.08300  1.000 80.59445  ? 327 PHE   A C     1 
ATOM   2560 O  O     . PHE   A  1 335 ? 27.62100 -41.44700  -8.88300  1.000 82.40443  ? 327 PHE   A O     1 
ATOM   2561 C  CB    . PHE   A  1 335 ? 26.25300 -43.85800  -7.94200  1.000 68.14197  ? 327 PHE   A CB    1 
ATOM   2562 C  CG    . PHE   A  1 335 ? 25.77700 -45.25200  -8.26900  1.000 72.70140  ? 327 PHE   A CG    1 
ATOM   2563 C  CD1   . PHE   A  1 335 ? 26.03400 -45.81300  -9.51200  1.000 65.31687  ? 327 PHE   A CD1   1 
ATOM   2564 C  CD2   . PHE   A  1 335 ? 25.06600 -46.00200  -7.34500  1.000 68.37602  ? 327 PHE   A CD2   1 
ATOM   2565 C  CE1   . PHE   A  1 335 ? 25.59900 -47.09300  -9.81800  1.000 63.45198  ? 327 PHE   A CE1   1 
ATOM   2566 C  CE2   . PHE   A  1 335 ? 24.63400 -47.28300  -7.65300  1.000 62.54010  ? 327 PHE   A CE2   1 
ATOM   2567 C  CZ    . PHE   A  1 335 ? 24.90200 -47.82600  -8.88800  1.000 62.07384  ? 327 PHE   A CZ    1 
ATOM   2568 N  N     . GLU   A  1 336 ? 29.22200 -41.81600  -7.30200  1.000 79.20800  ? 328 GLU   A N     1 
ATOM   2569 C  CA    . GLU   A  1 336 ? 29.89100 -40.48700  -7.39800  1.000 77.19767  ? 328 GLU   A CA    1 
ATOM   2570 C  C     . GLU   A  1 336 ? 31.25000 -40.65700  -8.08600  1.000 84.24532  ? 328 GLU   A C     1 
ATOM   2571 O  O     . GLU   A  1 336 ? 31.98400 -39.65800  -8.19600  1.000 87.16097  ? 328 GLU   A O     1 
ATOM   2572 C  CB    . GLU   A  1 336 ? 30.05700 -39.82400  -6.02700  1.000 79.60696  ? 328 GLU   A CB    1 
ATOM   2573 C  CG    . GLU   A  1 336 ? 30.56300 -40.74900  -4.93200  1.000 78.38973  ? 328 GLU   A CG    1 
ATOM   2574 C  CD    . GLU   A  1 336 ? 30.77300 -40.09200  -3.57700  1.000 81.18753  ? 328 GLU   A CD    1 
ATOM   2575 O  OE1   . GLU   A  1 336 ? 29.99400 -39.18300  -3.23300  1.000 79.96696  ? 328 GLU   A OE1   1 
ATOM   2576 O  OE2   . GLU   A  1 336 ? 31.70600 -40.50500  -2.86100  1.000 81.34945  ? 328 GLU   A OE2   1 
ATOM   2577 N  N     . LYS   A  1 337 ? 31.55200 -41.87300  -8.55300  1.000 109.85520 ? 329 LYS   A N     1 
ATOM   2578 C  CA    . LYS   A  1 337 ? 32.85800 -42.25300  -9.15700  1.000 114.85163 ? 329 LYS   A CA    1 
ATOM   2579 C  C     . LYS   A  1 337 ? 32.68200 -42.53400  -10.65600 1.000 111.35526 ? 329 LYS   A C     1 
ATOM   2580 O  O     . LYS   A  1 337 ? 33.56700 -43.19700  -11.22800 1.000 114.35164 ? 329 LYS   A O     1 
ATOM   2581 C  CB    . LYS   A  1 337 ? 33.43800 -43.46900  -8.42300  1.000 115.37909 ? 329 LYS   A CB    1 
ATOM   2582 C  CG    . LYS   A  1 337 ? 32.51600 -44.68100  -8.32200  1.000 110.72589 ? 329 LYS   A CG    1 
ATOM   2583 C  CD    . LYS   A  1 337 ? 33.24400 -46.01400  -8.28300  1.000 114.59026 ? 329 LYS   A CD    1 
ATOM   2584 C  CE    . LYS   A  1 337 ? 32.31000 -47.20700  -8.34900  1.000 111.83294 ? 329 LYS   A CE    1 
ATOM   2585 N  NZ    . LYS   A  1 337 ? 33.04400 -48.49200  -8.42100  1.000 110.18358 ? 329 LYS   A NZ    1 
ATOM   2586 N  N     . ASP   A  1 338 ? 31.59000 -42.05200  -11.26500 1.000 87.16131  ? 330 ASP   A N     1 
ATOM   2587 C  CA    . ASP   A  1 338 ? 31.30000 -42.19800  -12.71800 1.000 81.35032  ? 330 ASP   A CA    1 
ATOM   2588 C  C     . ASP   A  1 338 ? 31.74800 -40.92000  -13.42300 1.000 80.28581  ? 330 ASP   A C     1 
ATOM   2589 O  O     . ASP   A  1 338 ? 30.95800 -39.99300  -13.58300 1.000 80.38395  ? 330 ASP   A O     1 
ATOM   2590 C  CB    . ASP   A  1 338 ? 29.82100 -42.51200  -12.96200 1.000 76.69422  ? 330 ASP   A CB    1 
ATOM   2591 C  CG    . ASP   A  1 338 ? 29.56100 -43.22200  -14.27900 1.000 73.77109  ? 330 ASP   A CG    1 
ATOM   2592 O  OD1   . ASP   A  1 338 ? 30.32400 -42.98400  -15.23300 1.000 76.59845  ? 330 ASP   A OD1   1 
ATOM   2593 O  OD2   . ASP   A  1 338 ? 28.60800 -44.02000  -14.33300 1.000 71.33934  ? 330 ASP   A OD2   1 
ATOM   2594 N  N     . PRO   A  1 339 ? 33.01900 -40.83500  -13.88100 1.000 76.55195  ? 331 PRO   A N     1 
ATOM   2595 C  CA    . PRO   A  1 339 ? 33.58700 -39.56800  -14.34300 1.000 77.79842  ? 331 PRO   A CA    1 
ATOM   2596 C  C     . PRO   A  1 339 ? 32.91700 -39.04100  -15.62100 1.000 80.74861  ? 331 PRO   A C     1 
ATOM   2597 O  O     . PRO   A  1 339 ? 32.87800 -37.83900  -15.79700 1.000 84.91371  ? 331 PRO   A O     1 
ATOM   2598 C  CB    . PRO   A  1 339 ? 35.06600 -39.90500  -14.59200 1.000 74.54400  ? 331 PRO   A CB    1 
ATOM   2599 C  CG    . PRO   A  1 339 ? 35.05400 -41.38200  -14.91200 1.000 73.73238  ? 331 PRO   A CG    1 
ATOM   2600 C  CD    . PRO   A  1 339 ? 33.96000 -41.95500  -14.03600 1.000 74.65348  ? 331 PRO   A CD    1 
ATOM   2601 N  N     . ILE   A  1 340 ? 32.39300 -39.94400  -16.45700 1.000 74.71181  ? 332 ILE   A N     1 
ATOM   2602 C  CA    . ILE   A  1 340 ? 31.70100 -39.60500  -17.73800 1.000 75.61442  ? 332 ILE   A CA    1 
ATOM   2603 C  C     . ILE   A  1 340 ? 30.45200 -38.78600  -17.39400 1.000 71.55832  ? 332 ILE   A C     1 
ATOM   2604 O  O     . ILE   A  1 340 ? 30.27700 -37.69800  -17.96800 1.000 77.71541  ? 332 ILE   A O     1 
ATOM   2605 C  CB    . ILE   A  1 340 ? 31.33600 -40.86200  -18.56000 1.000 75.75476  ? 332 ILE   A CB    1 
ATOM   2606 C  CG1   . ILE   A  1 340 ? 32.43200 -41.93600  -18.55500 1.000 77.12439  ? 332 ILE   A CG1   1 
ATOM   2607 C  CG2   . ILE   A  1 340 ? 30.94500 -40.46700  -19.97900 1.000 71.86911  ? 332 ILE   A CG2   1 
ATOM   2608 C  CD1   . ILE   A  1 340 ? 33.70700 -41.54300  -19.27100 1.000 80.31295  ? 332 ILE   A CD1   1 
ATOM   2609 N  N     . LYS   A  1 341 ? 29.62900 -39.29500  -16.47500 1.000 67.78347  ? 333 LYS   A N     1 
ATOM   2610 C  CA    . LYS   A  1 341 ? 28.32600 -38.69800  -16.07800 1.000 69.82748  ? 333 LYS   A CA    1 
ATOM   2611 C  C     . LYS   A  1 341 ? 28.53300 -37.26400  -15.57900 1.000 73.87635  ? 333 LYS   A C     1 
ATOM   2612 O  O     . LYS   A  1 341 ? 27.72700 -36.39500  -15.95400 1.000 75.61705  ? 333 LYS   A O     1 
ATOM   2613 C  CB    . LYS   A  1 341 ? 27.65900 -39.54200  -14.98700 1.000 72.09243  ? 333 LYS   A CB    1 
ATOM   2614 C  CG    . LYS   A  1 341 ? 26.15300 -39.36000  -14.86600 1.000 64.43957  ? 333 LYS   A CG    1 
ATOM   2615 C  CD    . LYS   A  1 341 ? 25.57600 -39.99600  -13.62900 1.000 68.50195  ? 333 LYS   A CD    1 
ATOM   2616 C  CE    . LYS   A  1 341 ? 25.35700 -39.01900  -12.49400 1.000 74.94721  ? 333 LYS   A CE    1 
ATOM   2617 N  NZ    . LYS   A  1 341 ? 24.85000 -39.71500  -11.28900 1.000 67.24665  ? 333 LYS   A NZ    1 
ATOM   2618 N  N     . TYR   A  1 342 ? 29.56400 -37.03500  -14.75800 1.000 72.28832  ? 334 TYR   A N     1 
ATOM   2619 C  CA    . TYR   A  1 342 ? 29.84100 -35.74200  -14.07900 1.000 71.27229  ? 334 TYR   A CA    1 
ATOM   2620 C  C     . TYR   A  1 342 ? 30.68200 -34.83700  -14.98200 1.000 75.76038  ? 334 TYR   A C     1 
ATOM   2621 O  O     . TYR   A  1 342 ? 30.56600 -33.60500  -14.84100 1.000 82.30889  ? 334 TYR   A O     1 
ATOM   2622 C  CB    . TYR   A  1 342 ? 30.49800 -35.98000  -12.72000 1.000 72.59631  ? 334 TYR   A CB    1 
ATOM   2623 C  CG    . TYR   A  1 342 ? 29.58900 -36.67300  -11.74000 1.000 72.52023  ? 334 TYR   A CG    1 
ATOM   2624 C  CD1   . TYR   A  1 342 ? 28.46300 -36.03700  -11.24200 1.000 72.24393  ? 334 TYR   A CD1   1 
ATOM   2625 C  CD2   . TYR   A  1 342 ? 29.83300 -37.97400  -11.33500 1.000 74.32551  ? 334 TYR   A CD2   1 
ATOM   2626 C  CE1   . TYR   A  1 342 ? 27.61200 -36.67000  -10.35200 1.000 71.41647  ? 334 TYR   A CE1   1 
ATOM   2627 C  CE2   . TYR   A  1 342 ? 28.99300 -38.62100  -10.44600 1.000 75.62359  ? 334 TYR   A CE2   1 
ATOM   2628 C  CZ    . TYR   A  1 342 ? 27.87900 -37.96700  -9.95400  1.000 73.69763  ? 334 TYR   A CZ    1 
ATOM   2629 O  OH    . TYR   A  1 342 ? 27.05300 -38.60200  -9.07500  1.000 74.79981  ? 334 TYR   A OH    1 
ATOM   2630 N  N     . SER   A  1 343 ? 31.49800 -35.41700  -15.87000 1.000 73.63610  ? 335 SER   A N     1 
ATOM   2631 C  CA    . SER   A  1 343 ? 32.14000 -34.69300  -16.99700 1.000 75.60125  ? 335 SER   A CA    1 
ATOM   2632 C  C     . SER   A  1 343 ? 31.03800 -33.99200  -17.79500 1.000 75.30541  ? 335 SER   A C     1 
ATOM   2633 O  O     . SER   A  1 343 ? 31.16700 -32.77900  -18.04800 1.000 76.96897  ? 335 SER   A O     1 
ATOM   2634 C  CB    . SER   A  1 343 ? 32.95400 -35.61500  -17.87100 1.000 76.40084  ? 335 SER   A CB    1 
ATOM   2635 O  OG    . SER   A  1 343 ? 34.13200 -36.04000  -17.20500 1.000 77.37176  ? 335 SER   A OG    1 
ATOM   2636 N  N     . GLN   A  1 344 ? 29.97600 -34.73800  -18.11900 1.000 73.33893  ? 336 GLN   A N     1 
ATOM   2637 C  CA    . GLN   A  1 344 ? 28.81600 -34.27500  -18.92800 1.000 76.38405  ? 336 GLN   A CA    1 
ATOM   2638 C  C     . GLN   A  1 344 ? 28.01000 -33.24000  -18.13500 1.000 75.97241  ? 336 GLN   A C     1 
ATOM   2639 O  O     . GLN   A  1 344 ? 27.61500 -32.22500  -18.73500 1.000 82.33445  ? 336 GLN   A O     1 
ATOM   2640 C  CB    . GLN   A  1 344 ? 27.95200 -35.46500  -19.35200 1.000 70.90583  ? 336 GLN   A CB    1 
ATOM   2641 C  CG    . GLN   A  1 344 ? 28.62600 -36.36400  -20.38100 1.000 73.20141  ? 336 GLN   A CG    1 
ATOM   2642 C  CD    . GLN   A  1 344 ? 28.75700 -35.68900  -21.72300 1.000 74.36890  ? 336 GLN   A CD    1 
ATOM   2643 O  OE1   . GLN   A  1 344 ? 29.81000 -35.16400  -22.07500 1.000 75.66145  ? 336 GLN   A OE1   1 
ATOM   2644 N  NE2   . GLN   A  1 344 ? 27.66900 -35.67400  -22.47500 1.000 72.79377  ? 336 GLN   A NE2   1 
ATOM   2645 N  N     . TYR   A  1 345 ? 27.78300 -33.47500  -16.84100 1.000 73.50154  ? 337 TYR   A N     1 
ATOM   2646 C  CA    . TYR   A  1 345 ? 27.04900 -32.54100  -15.94400 1.000 75.22206  ? 337 TYR   A CA    1 
ATOM   2647 C  C     . TYR   A  1 345 ? 27.86700 -31.25500  -15.75400 1.000 80.19926  ? 337 TYR   A C     1 
ATOM   2648 O  O     . TYR   A  1 345 ? 27.25800 -30.16600  -15.73900 1.000 79.35297  ? 337 TYR   A O     1 
ATOM   2649 C  CB    . TYR   A  1 345 ? 26.69300 -33.21400  -14.61500 1.000 71.08983  ? 337 TYR   A CB    1 
ATOM   2650 C  CG    . TYR   A  1 345 ? 25.27700 -33.72800  -14.54700 1.000 73.44401  ? 337 TYR   A CG    1 
ATOM   2651 C  CD1   . TYR   A  1 345 ? 24.22200 -32.86700  -14.28900 1.000 70.34796  ? 337 TYR   A CD1   1 
ATOM   2652 C  CD2   . TYR   A  1 345 ? 24.98300 -35.06800  -14.75000 1.000 73.06568  ? 337 TYR   A CD2   1 
ATOM   2653 C  CE1   . TYR   A  1 345 ? 22.91500 -33.32100  -14.22700 1.000 69.39095  ? 337 TYR   A CE1   1 
ATOM   2654 C  CE2   . TYR   A  1 345 ? 23.68100 -35.54000  -14.69300 1.000 72.25670  ? 337 TYR   A CE2   1 
ATOM   2655 C  CZ    . TYR   A  1 345 ? 22.64300 -34.66300  -14.43000 1.000 70.74745  ? 337 TYR   A CZ    1 
ATOM   2656 O  OH    . TYR   A  1 345 ? 21.35700 -35.11200  -14.37300 1.000 62.39994  ? 337 TYR   A OH    1 
ATOM   2657 N  N     . GLN   A  1 346 ? 29.19500 -31.37100  -15.62700 1.000 78.76802  ? 338 GLN   A N     1 
ATOM   2658 C  CA    . GLN   A  1 346 ? 30.12400 -30.21400  -15.50800 1.000 82.13911  ? 338 GLN   A CA    1 
ATOM   2659 C  C     . GLN   A  1 346 ? 30.01300 -29.36300  -16.77800 1.000 82.41257  ? 338 GLN   A C     1 
ATOM   2660 O  O     . GLN   A  1 346 ? 29.69700 -28.16500  -16.65600 1.000 86.01574  ? 338 GLN   A O     1 
ATOM   2661 C  CB    . GLN   A  1 346 ? 31.56300 -30.68100  -15.27200 1.000 82.48734  ? 338 GLN   A CB    1 
ATOM   2662 C  CG    . GLN   A  1 346 ? 32.53800 -29.54400  -14.98700 1.000 82.21667  ? 338 GLN   A CG    1 
ATOM   2663 C  CD    . GLN   A  1 346 ? 33.92700 -30.03200  -14.65100 1.000 90.04835  ? 338 GLN   A CD    1 
ATOM   2664 O  OE1   . GLN   A  1 346 ? 34.11900 -31.15700  -14.19400 1.000 93.56782  ? 338 GLN   A OE1   1 
ATOM   2665 N  NE2   . GLN   A  1 346 ? 34.91400 -29.17800  -14.86900 1.000 87.81300  ? 338 GLN   A NE2   1 
ATOM   2666 N  N     . GLN   A  1 347 ? 30.23700 -29.97500  -17.94500 1.000 81.15077  ? 339 GLN   A N     1 
ATOM   2667 C  CA    . GLN   A  1 347 ? 30.19600 -29.30400  -19.27500 1.000 80.89737  ? 339 GLN   A CA    1 
ATOM   2668 C  C     . GLN   A  1 347 ? 28.81400 -28.67000  -19.49600 1.000 80.44933  ? 339 GLN   A C     1 
ATOM   2669 O  O     . GLN   A  1 347 ? 28.76800 -27.54800  -20.01900 1.000 87.00920  ? 339 GLN   A O     1 
ATOM   2670 C  CB    . GLN   A  1 347 ? 30.52800 -30.29800  -20.39100 1.000 80.89833  ? 339 GLN   A CB    1 
ATOM   2671 C  CG    . GLN   A  1 347 ? 30.83700 -29.64100  -21.73100 1.000 83.74873  ? 339 GLN   A CG    1 
ATOM   2672 C  CD    . GLN   A  1 347 ? 32.24400 -29.10000  -21.82700 1.000 91.87875  ? 339 GLN   A CD    1 
ATOM   2673 O  OE1   . GLN   A  1 347 ? 33.17800 -29.62400  -21.22500 1.000 93.21491  ? 339 GLN   A OE1   1 
ATOM   2674 N  NE2   . GLN   A  1 347 ? 32.40900 -28.04700  -22.61000 1.000 90.54179  ? 339 GLN   A NE2   1 
ATOM   2675 N  N     . ALA   A  1 348 ? 27.73500 -29.36100  -19.11300 1.000 78.08394  ? 340 ALA   A N     1 
ATOM   2676 C  CA    . ALA   A  1 348 ? 26.33400 -28.88600  -19.22700 1.000 78.06311  ? 340 ALA   A CA    1 
ATOM   2677 C  C     . ALA   A  1 348 ? 26.17300 -27.55000  -18.49200 1.000 83.38389  ? 340 ALA   A C     1 
ATOM   2678 O  O     . ALA   A  1 348 ? 25.57500 -26.62500  -19.07600 1.000 85.95882  ? 340 ALA   A O     1 
ATOM   2679 C  CB    . ALA   A  1 348 ? 25.38100 -29.92500  -18.68500 1.000 77.34449  ? 340 ALA   A CB    1 
ATOM   2680 N  N     . ILE   A  1 349 ? 26.68300 -27.46300  -17.25900 1.000 78.51549  ? 341 ILE   A N     1 
ATOM   2681 C  CA    . ILE   A  1 349 ? 26.67400 -26.22500  -16.42100 1.000 81.57695  ? 341 ILE   A CA    1 
ATOM   2682 C  C     . ILE   A  1 349 ? 27.62600 -25.20500  -17.05900 1.000 84.14905  ? 341 ILE   A C     1 
ATOM   2683 O  O     . ILE   A  1 349 ? 27.20900 -24.04400  -17.23600 1.000 84.58052  ? 341 ILE   A O     1 
ATOM   2684 C  CB    . ILE   A  1 349 ? 27.04400 -26.55100  -14.95700 1.000 86.93277  ? 341 ILE   A CB    1 
ATOM   2685 C  CG1   . ILE   A  1 349 ? 25.98300 -27.43500  -14.29300 1.000 83.43710  ? 341 ILE   A CG1   1 
ATOM   2686 C  CG2   . ILE   A  1 349 ? 27.29300 -25.28300  -14.15000 1.000 80.29670  ? 341 ILE   A CG2   1 
ATOM   2687 C  CD1   . ILE   A  1 349 ? 26.48900 -28.22800  -13.11200 1.000 74.81556  ? 341 ILE   A CD1   1 
ATOM   2688 N  N     . TYR   A  1 350 ? 28.84700 -25.64200  -17.39400 1.000 83.39863  ? 342 TYR   A N     1 
ATOM   2689 C  CA    . TYR   A  1 350 ? 29.91500 -24.85200  -18.06700 1.000 86.09145  ? 342 TYR   A CA    1 
ATOM   2690 C  C     . TYR   A  1 350 ? 29.30200 -23.97200  -19.16300 1.000 87.86328  ? 342 TYR   A C     1 
ATOM   2691 O  O     . TYR   A  1 350 ? 29.54100 -22.74800  -19.15600 1.000 89.95343  ? 342 TYR   A O     1 
ATOM   2692 C  CB    . TYR   A  1 350 ? 30.97200 -25.79500  -18.65400 1.000 88.14555  ? 342 TYR   A CB    1 
ATOM   2693 C  CG    . TYR   A  1 350 ? 32.17700 -25.13600  -19.28100 1.000 95.30035  ? 342 TYR   A CG    1 
ATOM   2694 C  CD1   . TYR   A  1 350 ? 32.11100 -24.56200  -20.54100 1.000 94.99071  ? 342 TYR   A CD1   1 
ATOM   2695 C  CD2   . TYR   A  1 350 ? 33.40200 -25.12400  -18.63200 1.000 98.04039  ? 342 TYR   A CD2   1 
ATOM   2696 C  CE1   . TYR   A  1 350 ? 33.21800 -23.96900  -21.12700 1.000 96.14208  ? 342 TYR   A CE1   1 
ATOM   2697 C  CE2   . TYR   A  1 350 ? 34.51900 -24.53600  -19.20400 1.000 95.18798  ? 342 TYR   A CE2   1 
ATOM   2698 C  CZ    . TYR   A  1 350 ? 34.42900 -23.95700  -20.45700 1.000 98.33322  ? 342 TYR   A CZ    1 
ATOM   2699 O  OH    . TYR   A  1 350 ? 35.52500 -23.37600  -21.02800 1.000 98.24703  ? 342 TYR   A OH    1 
ATOM   2700 N  N     . LYS   A  1 351 ? 28.53400 -24.58600  -20.06900 1.000 86.62154  ? 343 LYS   A N     1 
ATOM   2701 C  CA    . LYS   A  1 351 ? 27.98400 -23.93800  -21.29000 1.000 88.21994  ? 343 LYS   A CA    1 
ATOM   2702 C  C     . LYS   A  1 351 ? 26.78200 -23.05800  -20.92800 1.000 88.20479  ? 343 LYS   A C     1 
ATOM   2703 O  O     . LYS   A  1 351 ? 26.63400 -21.99100  -21.55300 1.000 90.54266  ? 343 LYS   A O     1 
ATOM   2704 C  CB    . LYS   A  1 351 ? 27.59800 -24.99200  -22.33300 1.000 88.39178  ? 343 LYS   A CB    1 
ATOM   2705 C  CG    . LYS   A  1 351 ? 28.74800 -25.86800  -22.81200 1.000 90.06173  ? 343 LYS   A CG    1 
ATOM   2706 C  CD    . LYS   A  1 351 ? 28.58100 -26.39900  -24.21700 1.000 87.86065  ? 343 LYS   A CD    1 
ATOM   2707 C  CE    . LYS   A  1 351 ? 29.52400 -27.54500  -24.51900 1.000 87.52410  ? 343 LYS   A CE    1 
ATOM   2708 N  NZ    . LYS   A  1 351 ? 29.51700 -27.90000  -25.95900 1.000 93.47427  ? 343 LYS   A NZ    1 
ATOM   2709 N  N     . CYS   A  1 352 ? 25.95400 -23.48800  -19.97100 1.000 85.86309  ? 344 CYS   A N     1 
ATOM   2710 C  CA    . CYS   A  1 352 ? 24.74400 -22.74700  -19.52100 1.000 85.75600  ? 344 CYS   A CA    1 
ATOM   2711 C  C     . CYS   A  1 352 ? 25.15200 -21.41800  -18.87100 1.000 89.59526  ? 344 CYS   A C     1 
ATOM   2712 O  O     . CYS   A  1 352 ? 24.47900 -20.40500  -19.14700 1.000 91.90362  ? 344 CYS   A O     1 
ATOM   2713 C  CB    . CYS   A  1 352 ? 23.90300 -23.56400  -18.54900 1.000 83.42656  ? 344 CYS   A CB    1 
ATOM   2714 S  SG    . CYS   A  1 352 ? 22.27900 -22.82300  -18.24300 1.000 83.19988  ? 344 CYS   A SG    1 
ATOM   2715 N  N     . LEU   A  1 353 ? 26.21000 -21.42500  -18.05100 1.000 88.14870  ? 345 LEU   A N     1 
ATOM   2716 C  CA    . LEU   A  1 353 ? 26.74900 -20.21500  -17.37000 1.000 90.63503  ? 345 LEU   A CA    1 
ATOM   2717 C  C     . LEU   A  1 353 ? 27.16300 -19.17700  -18.42200 1.000 93.41299  ? 345 LEU   A C     1 
ATOM   2718 O  O     . LEU   A  1 353 ? 26.82400 -17.99200  -18.24000 1.000 95.25996  ? 345 LEU   A O     1 
ATOM   2719 C  CB    . LEU   A  1 353 ? 27.93200 -20.60200  -16.47300 1.000 90.84014  ? 345 LEU   A CB    1 
ATOM   2720 C  CG    . LEU   A  1 353 ? 27.59200 -21.41200  -15.21900 1.000 87.54942  ? 345 LEU   A CG    1 
ATOM   2721 C  CD1   . LEU   A  1 353 ? 28.85400 -21.77700  -14.45200 1.000 87.61020  ? 345 LEU   A CD1   1 
ATOM   2722 C  CD2   . LEU   A  1 353 ? 26.62600 -20.66300  -14.31100 1.000 87.42799  ? 345 LEU   A CD2   1 
ATOM   2723 N  N     . LEU   A  1 354 ? 27.85100 -19.61200  -19.48300 1.000 94.11699  ? 346 LEU   A N     1 
ATOM   2724 C  CA    . LEU   A  1 354 ? 28.33600 -18.73400  -20.58400 1.000 97.26285  ? 346 LEU   A CA    1 
ATOM   2725 C  C     . LEU   A  1 354 ? 27.14000 -18.14300  -21.34200 1.000 98.06516  ? 346 LEU   A C     1 
ATOM   2726 O  O     . LEU   A  1 354 ? 27.13800 -16.91600  -21.56900 1.000 106.75519 ? 346 LEU   A O     1 
ATOM   2727 C  CB    . LEU   A  1 354 ? 29.23800 -19.53600  -21.53000 1.000 97.56980  ? 346 LEU   A CB    1 
ATOM   2728 C  CG    . LEU   A  1 354 ? 30.56600 -20.02200  -20.94600 1.000 97.50588  ? 346 LEU   A CG    1 
ATOM   2729 C  CD1   . LEU   A  1 354 ? 31.34300 -20.82700  -21.97600 1.000 97.98713  ? 346 LEU   A CD1   1 
ATOM   2730 C  CD2   . LEU   A  1 354 ? 31.41100 -18.86200  -20.44000 1.000 100.11270 ? 346 LEU   A CD2   1 
ATOM   2731 N  N     . ASP   A  1 355 ? 26.17100 -18.98300  -21.71900 1.000 95.95304  ? 347 ASP   A N     1 
ATOM   2732 C  CA    . ASP   A  1 355 ? 24.98700 -18.59800  -22.53700 1.000 96.61238  ? 347 ASP   A CA    1 
ATOM   2733 C  C     . ASP   A  1 355 ? 24.11400 -17.59600  -21.76700 1.000 98.03760  ? 347 ASP   A C     1 
ATOM   2734 O  O     . ASP   A  1 355 ? 23.53300 -16.70800  -22.42100 1.000 101.09467 ? 347 ASP   A O     1 
ATOM   2735 C  CB    . ASP   A  1 355 ? 24.18000 -19.83000  -22.96100 1.000 94.00674  ? 347 ASP   A CB    1 
ATOM   2736 C  CG    . ASP   A  1 355 ? 24.87000 -20.71300  -23.99200 1.000 93.95894  ? 347 ASP   A CG    1 
ATOM   2737 O  OD1   . ASP   A  1 355 ? 26.06900 -20.48800  -24.25700 1.000 98.33122  ? 347 ASP   A OD1   1 
ATOM   2738 O  OD2   . ASP   A  1 355 ? 24.20000 -21.61800  -24.52700 1.000 92.31165  ? 347 ASP   A OD2   1 
ATOM   2739 N  N     . ARG   A  1 356 ? 24.03000 -17.72200  -20.43600 1.000 99.50769  ? 348 ARG   A N     1 
ATOM   2740 C  CA    . ARG   A  1 356 ? 23.09800 -16.93300  -19.58200 1.000 96.62982  ? 348 ARG   A CA    1 
ATOM   2741 C  C     . ARG   A  1 356 ? 23.68200 -15.54300  -19.29800 1.000 101.20374 ? 348 ARG   A C     1 
ATOM   2742 O  O     . ARG   A  1 356 ? 23.00100 -14.55300  -19.62900 1.000 111.30648 ? 348 ARG   A O     1 
ATOM   2743 C  CB    . ARG   A  1 356 ? 22.77200 -17.67600  -18.28200 1.000 93.02381  ? 348 ARG   A CB    1 
ATOM   2744 C  CG    . ARG   A  1 356 ? 21.63700 -18.68200  -18.42000 1.000 90.45370  ? 348 ARG   A CG    1 
ATOM   2745 C  CD    . ARG   A  1 356 ? 21.11400 -19.18200  -17.08700 1.000 88.20430  ? 348 ARG   A CD    1 
ATOM   2746 N  NE    . ARG   A  1 356 ? 20.25800 -18.21300  -16.41300 1.000 89.28650  ? 348 ARG   A NE    1 
ATOM   2747 C  CZ    . ARG   A  1 356 ? 18.97500 -17.99300  -16.69200 1.000 89.41020  ? 348 ARG   A CZ    1 
ATOM   2748 N  NH1   . ARG   A  1 356 ? 18.37000 -18.66700  -17.65700 1.000 88.47706  ? 348 ARG   A NH1   1 
ATOM   2749 N  NH2   . ARG   A  1 356 ? 18.29900 -17.09200  -16.00200 1.000 90.62305  ? 348 ARG   A NH2   1 
ATOM   2750 N  N     . VAL   A  1 357 ? 24.88000 -15.46600  -18.70400 1.000 99.32903  ? 349 VAL   A N     1 
ATOM   2751 C  CA    . VAL   A  1 357 ? 25.50900 -14.17700  -18.27800 1.000 104.65189 ? 349 VAL   A CA    1 
ATOM   2752 C  C     . VAL   A  1 357 ? 26.70000 -13.87200  -19.18800 1.000 106.56876 ? 349 VAL   A C     1 
ATOM   2753 O  O     . VAL   A  1 357 ? 27.64500 -14.65500  -19.26800 1.000 103.68345 ? 349 VAL   A O     1 
ATOM   2754 C  CB    . VAL   A  1 357 ? 25.88400 -14.18300  -16.77900 1.000 105.24581 ? 349 VAL   A CB    1 
ATOM   2755 C  CG1   . VAL   A  1 357 ? 24.79100 -14.82100  -15.93600 1.000 105.05087 ? 349 VAL   A CG1   1 
ATOM   2756 C  CG2   . VAL   A  1 357 ? 27.21900 -14.84800  -16.49000 1.000 104.65823 ? 349 VAL   A CG2   1 
ATOM   2757 N  N     . PRO   A  1 358 ? 26.67500 -12.73400  -19.92500 1.000 115.13461 ? 350 PRO   A N     1 
ATOM   2758 C  CA    . PRO   A  1 358 ? 27.79600 -12.32400  -20.77700 1.000 115.73014 ? 350 PRO   A CA    1 
ATOM   2759 C  C     . PRO   A  1 358 ? 29.14600 -12.11500  -20.07000 1.000 117.67369 ? 350 PRO   A C     1 
ATOM   2760 O  O     . PRO   A  1 358 ? 29.19000 -12.12600  -18.85300 1.000 123.30357 ? 350 PRO   A O     1 
ATOM   2761 C  CB    . PRO   A  1 358 ? 27.34000 -10.97000  -21.34400 1.000 118.33000 ? 350 PRO   A CB    1 
ATOM   2762 C  CG    . PRO   A  1 358 ? 25.83300 -11.02200  -21.28300 1.000 117.02132 ? 350 PRO   A CG    1 
ATOM   2763 C  CD    . PRO   A  1 358 ? 25.53400 -11.80800  -20.02700 1.000 114.72419 ? 350 PRO   A CD    1 
ATOM   2764 N  N     . GLU   A  1 359 ? 30.20200 -11.90500  -20.86500 1.000 113.64238 ? 351 GLU   A N     1 
ATOM   2765 C  CA    . GLU   A  1 359 ? 31.61900 -11.76000  -20.42600 1.000 114.93039 ? 351 GLU   A CA    1 
ATOM   2766 C  C     . GLU   A  1 359 ? 31.78100 -10.49200  -19.57700 1.000 117.08765 ? 351 GLU   A C     1 
ATOM   2767 O  O     . GLU   A  1 359 ? 32.36100 -10.59100  -18.47900 1.000 117.77633 ? 351 GLU   A O     1 
ATOM   2768 C  CB    . GLU   A  1 359 ? 32.54200 -11.72100  -21.64900 1.000 122.43741 ? 351 GLU   A CB    1 
ATOM   2769 C  CG    . GLU   A  1 359 ? 34.00500 -11.45500  -21.32700 1.000 120.56789 ? 351 GLU   A CG    1 
ATOM   2770 C  CD    . GLU   A  1 359 ? 34.67800 -12.49400  -20.44500 1.000 117.80737 ? 351 GLU   A CD    1 
ATOM   2771 O  OE1   . GLU   A  1 359 ? 34.22600 -13.65700  -20.44600 1.000 117.66276 ? 351 GLU   A OE1   1 
ATOM   2772 O  OE2   . GLU   A  1 359 ? 35.65700 -12.13600  -19.76100 1.000 118.74561 ? 351 GLU   A OE2   1 
ATOM   2773 N  N     . GLU   A  1 360 ? 31.29900 -9.34800   -20.07600 1.000 119.78430 ? 352 GLU   A N     1 
ATOM   2774 C  CA    . GLU   A  1 360 ? 31.41800 -8.01900   -19.41100 1.000 122.38408 ? 352 GLU   A CA    1 
ATOM   2775 C  C     . GLU   A  1 360 ? 30.61400 -8.00000   -18.10100 1.000 120.36599 ? 352 GLU   A C     1 
ATOM   2776 O  O     . GLU   A  1 360 ? 30.86200 -7.09500   -17.27900 1.000 122.03203 ? 352 GLU   A O     1 
ATOM   2777 C  CB    . GLU   A  1 360 ? 30.97100 -6.88900   -20.34600 1.000 125.74304 ? 352 GLU   A CB    1 
ATOM   2778 C  CG    . GLU   A  1 360 ? 29.54300 -7.01800   -20.85900 1.000 124.71176 ? 352 GLU   A CG    1 
ATOM   2779 C  CD    . GLU   A  1 360 ? 29.38500 -7.71700   -22.20100 1.000 124.96671 ? 352 GLU   A CD    1 
ATOM   2780 O  OE1   . GLU   A  1 360 ? 30.31100 -7.62000   -23.03200 1.000 132.78324 ? 352 GLU   A OE1   1 
ATOM   2781 O  OE2   . GLU   A  1 360 ? 28.32900 -8.34400   -22.41800 1.000 122.18757 ? 352 GLU   A OE2   1 
ATOM   2782 N  N     . GLU   A  1 361 ? 29.69700 -8.95900   -17.91300 1.000 117.21830 ? 353 GLU   A N     1 
ATOM   2783 C  CA    . GLU   A  1 361 ? 28.82000 -9.07500   -16.71500 1.000 114.99206 ? 353 GLU   A CA    1 
ATOM   2784 C  C     . GLU   A  1 361 ? 29.36500 -10.12000  -15.72700 1.000 112.20452 ? 353 GLU   A C     1 
ATOM   2785 O  O     . GLU   A  1 361 ? 28.64900 -10.40900  -14.75000 1.000 113.19728 ? 353 GLU   A O     1 
ATOM   2786 C  CB    . GLU   A  1 361 ? 27.40200 -9.47500   -17.13400 1.000 113.29462 ? 353 GLU   A CB    1 
ATOM   2787 C  CG    . GLU   A  1 361 ? 26.59800 -8.35500   -17.76800 1.000 115.99226 ? 353 GLU   A CG    1 
ATOM   2788 C  CD    . GLU   A  1 361 ? 25.10800 -8.64600   -17.84400 1.000 114.39611 ? 353 GLU   A CD    1 
ATOM   2789 O  OE1   . GLU   A  1 361 ? 24.52200 -8.99200   -16.80000 1.000 117.13673 ? 353 GLU   A OE1   1 
ATOM   2790 O  OE2   . GLU   A  1 361 ? 24.53900 -8.54200   -18.94600 1.000 116.38206 ? 353 GLU   A OE2   1 
ATOM   2791 N  N     . LYS   A  1 362 ? 30.57600 -10.65200  -15.94200 1.000 112.24383 ? 354 LYS   A N     1 
ATOM   2792 C  CA    . LYS   A  1 362 ? 31.07800 -11.87000  -15.24000 1.000 111.44685 ? 354 LYS   A CA    1 
ATOM   2793 C  C     . LYS   A  1 362 ? 31.20800 -11.61100  -13.73200 1.000 112.70717 ? 354 LYS   A C     1 
ATOM   2794 O  O     . LYS   A  1 362 ? 30.83000 -12.51300  -12.95200 1.000 116.42814 ? 354 LYS   A O     1 
ATOM   2795 C  CB    . LYS   A  1 362 ? 32.40300 -12.35900  -15.83900 1.000 110.24129 ? 354 LYS   A CB    1 
ATOM   2796 C  CG    . LYS   A  1 362 ? 33.65100 -11.56800  -15.46400 1.000 113.02795 ? 354 LYS   A CG    1 
ATOM   2797 C  CD    . LYS   A  1 362 ? 34.93200 -12.19000  -15.98600 1.000 113.61686 ? 354 LYS   A CD    1 
ATOM   2798 C  CE    . LYS   A  1 362 ? 36.13400 -11.89500  -15.11300 1.000 121.19687 ? 354 LYS   A CE    1 
ATOM   2799 N  NZ    . LYS   A  1 362 ? 37.35100 -12.58200  -15.60700 1.000 115.63089 ? 354 LYS   A NZ    1 
ATOM   2800 N  N     . ASP   A  1 363 ? 31.72200 -10.44000  -13.33700 1.000 111.96186 ? 355 ASP   A N     1 
ATOM   2801 C  CA    . ASP   A  1 363 ? 32.01000 -10.08600  -11.91900 1.000 112.50022 ? 355 ASP   A CA    1 
ATOM   2802 C  C     . ASP   A  1 363 ? 30.75600 -9.49900   -11.25900 1.000 111.96724 ? 355 ASP   A C     1 
ATOM   2803 O  O     . ASP   A  1 363 ? 30.59900 -9.69500   -10.03700 1.000 117.15321 ? 355 ASP   A O     1 
ATOM   2804 C  CB    . ASP   A  1 363 ? 33.20300 -9.13200   -11.81200 1.000 115.46559 ? 355 ASP   A CB    1 
ATOM   2805 C  CG    . ASP   A  1 363 ? 34.53400 -9.75600   -12.20000 1.000 115.74975 ? 355 ASP   A CG    1 
ATOM   2806 O  OD1   . ASP   A  1 363 ? 34.67000 -10.99000  -12.06600 1.000 115.70438 ? 355 ASP   A OD1   1 
ATOM   2807 O  OD2   . ASP   A  1 363 ? 35.42600 -9.00300   -12.63700 1.000 125.55150 ? 355 ASP   A OD2   1 
ATOM   2808 N  N     . THR   A  1 364 ? 29.89700 -8.82000   -12.02700 1.000 113.19006 ? 356 THR   A N     1 
ATOM   2809 C  CA    . THR   A  1 364 ? 28.64200 -8.18800   -11.53300 1.000 113.40115 ? 356 THR   A CA    1 
ATOM   2810 C  C     . THR   A  1 364 ? 27.56300 -9.26300   -11.32400 1.000 114.34005 ? 356 THR   A C     1 
ATOM   2811 O  O     . THR   A  1 364 ? 26.88700 -9.21500   -10.27700 1.000 112.36712 ? 356 THR   A O     1 
ATOM   2812 C  CB    . THR   A  1 364 ? 28.18400 -7.05700   -12.46700 1.000 116.31046 ? 356 THR   A CB    1 
ATOM   2813 O  OG1   . THR   A  1 364 ? 27.38800 -6.15800   -11.69500 1.000 124.73525 ? 356 THR   A OG1   1 
ATOM   2814 C  CG2   . THR   A  1 364 ? 27.39000 -7.52600   -13.66700 1.000 115.36579 ? 356 THR   A CG2   1 
ATOM   2815 N  N     . ASN   A  1 365 ? 27.41800 -10.19500  -12.27500 1.000 109.59800 ? 357 ASN   A N     1 
ATOM   2816 C  CA    . ASN   A  1 365 ? 26.32000 -11.20000  -12.31900 1.000 105.34792 ? 357 ASN   A CA    1 
ATOM   2817 C  C     . ASN   A  1 365 ? 26.76400 -12.48700  -11.61200 1.000 108.60899 ? 357 ASN   A C     1 
ATOM   2818 O  O     . ASN   A  1 365 ? 27.69300 -13.15600  -12.11600 1.000 105.39277 ? 357 ASN   A O     1 
ATOM   2819 C  CB    . ASN   A  1 365 ? 25.87800 -11.49500  -13.75700 1.000 109.34336 ? 357 ASN   A CB    1 
ATOM   2820 C  CG    . ASN   A  1 365 ? 24.54200 -12.20600  -13.84600 1.000 103.98775 ? 357 ASN   A CG    1 
ATOM   2821 O  OD1   . ASN   A  1 365 ? 24.28200 -13.15600  -13.11100 1.000 100.02898 ? 357 ASN   A OD1   1 
ATOM   2822 N  ND2   . ASN   A  1 365 ? 23.69300 -11.76300  -14.75900 1.000 104.69529 ? 357 ASN   A ND2   1 
ATOM   2823 N  N     . VAL   A  1 366 ? 26.10000 -12.81800  -10.49900 1.000 106.72045 ? 358 VAL   A N     1 
ATOM   2824 C  CA    . VAL   A  1 366 ? 26.23300 -14.11700  -9.77400  1.000 104.06845 ? 358 VAL   A CA    1 
ATOM   2825 C  C     . VAL   A  1 366 ? 24.94300 -14.91600  -10.01400 1.000 95.34416  ? 358 VAL   A C     1 
ATOM   2826 O  O     . VAL   A  1 366 ? 23.84800 -14.34700  -9.83700  1.000 95.82971  ? 358 VAL   A O     1 
ATOM   2827 C  CB    . VAL   A  1 366 ? 26.55200 -13.92100  -8.27400  1.000 101.80815 ? 358 VAL   A CB    1 
ATOM   2828 C  CG1   . VAL   A  1 366 ? 25.64100 -12.90600  -7.59600  1.000 99.31514  ? 358 VAL   A CG1   1 
ATOM   2829 C  CG2   . VAL   A  1 366 ? 26.54300 -15.23600  -7.50800  1.000 95.11174  ? 358 VAL   A CG2   1 
ATOM   2830 N  N     . GLN   A  1 367 ? 25.08000 -16.17900  -10.43100 1.000 93.01732  ? 359 GLN   A N     1 
ATOM   2831 C  CA    . GLN   A  1 367 ? 23.95800 -17.06200  -10.85100 1.000 90.71364  ? 359 GLN   A CA    1 
ATOM   2832 C  C     . GLN   A  1 367 ? 23.53400 -17.95100  -9.67600  1.000 89.16071  ? 359 GLN   A C     1 
ATOM   2833 O  O     . GLN   A  1 367 ? 24.34900 -18.79400  -9.24700  1.000 87.17964  ? 359 GLN   A O     1 
ATOM   2834 C  CB    . GLN   A  1 367 ? 24.38400 -17.91000  -12.04900 1.000 89.78625  ? 359 GLN   A CB    1 
ATOM   2835 C  CG    . GLN   A  1 367 ? 24.53400 -17.10700  -13.33300 1.000 98.14518  ? 359 GLN   A CG    1 
ATOM   2836 C  CD    . GLN   A  1 367 ? 23.21800 -16.93300  -14.04800 1.000 98.75534  ? 359 GLN   A CD    1 
ATOM   2837 O  OE1   . GLN   A  1 367 ? 22.62500 -17.88600  -14.55000 1.000 96.65635  ? 359 GLN   A OE1   1 
ATOM   2838 N  NE2   . GLN   A  1 367 ? 22.75100 -15.69800  -14.10200 1.000 95.87937  ? 359 GLN   A NE2   1 
ATOM   2839 N  N     . VAL   A  1 368 ? 22.30600 -17.76500  -9.17900  1.000 88.08156  ? 360 VAL   A N     1 
ATOM   2840 C  CA    . VAL   A  1 368 ? 21.70800 -18.60700  -8.09800  1.000 85.85131  ? 360 VAL   A CA    1 
ATOM   2841 C  C     . VAL   A  1 368 ? 21.43600 -19.99800  -8.69000  1.000 84.26368  ? 360 VAL   A C     1 
ATOM   2842 O  O     . VAL   A  1 368 ? 20.50900 -20.13800  -9.51700  1.000 82.70542  ? 360 VAL   A O     1 
ATOM   2843 C  CB    . VAL   A  1 368 ? 20.46200 -17.96800  -7.44300  1.000 88.54719  ? 360 VAL   A CB    1 
ATOM   2844 C  CG1   . VAL   A  1 368 ? 19.51600 -17.31900  -8.44100  1.000 95.62067  ? 360 VAL   A CG1   1 
ATOM   2845 C  CG2   . VAL   A  1 368 ? 19.70400 -18.95600  -6.56700  1.000 85.34471  ? 360 VAL   A CG2   1 
ATOM   2846 N  N     . LEU   A  1 369 ? 22.25100 -20.97400  -8.27700  1.000 84.40408  ? 361 LEU   A N     1 
ATOM   2847 C  CA    . LEU   A  1 369 ? 22.32500 -22.35400  -8.82500  1.000 79.56767  ? 361 LEU   A CA    1 
ATOM   2848 C  C     . LEU   A  1 369 ? 21.89100 -23.33800  -7.73200  1.000 79.52524  ? 361 LEU   A C     1 
ATOM   2849 O  O     . LEU   A  1 369 ? 22.46500 -23.27600  -6.62900  1.000 83.22441  ? 361 LEU   A O     1 
ATOM   2850 C  CB    . LEU   A  1 369 ? 23.77200 -22.59700  -9.26700  1.000 80.12231  ? 361 LEU   A CB    1 
ATOM   2851 C  CG    . LEU   A  1 369 ? 23.96100 -23.51100  -10.47500 1.000 79.39068  ? 361 LEU   A CG    1 
ATOM   2852 C  CD1   . LEU   A  1 369 ? 25.31200 -23.26900  -11.12900 1.000 80.57954  ? 361 LEU   A CD1   1 
ATOM   2853 C  CD2   . LEU   A  1 369 ? 23.81300 -24.97100  -10.08000 1.000 79.37542  ? 361 LEU   A CD2   1 
ATOM   2854 N  N     . MET   A  1 370 ? 20.91400 -24.20300  -8.01800  1.000 75.66974  ? 362 MET   A N     1 
ATOM   2855 C  CA    . MET   A  1 370 ? 20.27200 -25.08800  -7.00800  1.000 74.27087  ? 362 MET   A CA    1 
ATOM   2856 C  C     . MET   A  1 370 ? 20.38900 -26.55800  -7.43300  1.000 73.07225  ? 362 MET   A C     1 
ATOM   2857 O  O     . MET   A  1 370 ? 19.81600 -26.91800  -8.47800  1.000 74.29103  ? 362 MET   A O     1 
ATOM   2858 C  CB    . MET   A  1 370 ? 18.79800 -24.71800  -6.82900  1.000 75.71913  ? 362 MET   A CB    1 
ATOM   2859 C  CG    . MET   A  1 370 ? 18.59600 -23.30100  -6.32900  1.000 78.53268  ? 362 MET   A CG    1 
ATOM   2860 S  SD    . MET   A  1 370 ? 16.88400 -22.96800  -5.86200  1.000 77.88940  ? 362 MET   A SD    1 
ATOM   2861 C  CE    . MET   A  1 370 ? 17.06900 -21.38100  -5.05100  1.000 81.36376  ? 362 MET   A CE    1 
ATOM   2862 N  N     . VAL   A  1 371 ? 21.10800 -27.36200  -6.64000  1.000 70.96551  ? 363 VAL   A N     1 
ATOM   2863 C  CA    . VAL   A  1 371 ? 21.22800 -28.84300  -6.79200  1.000 68.97001  ? 363 VAL   A CA    1 
ATOM   2864 C  C     . VAL   A  1 371 ? 20.09500 -29.49300  -5.98900  1.000 71.29531  ? 363 VAL   A C     1 
ATOM   2865 O  O     . VAL   A  1 371 ? 20.17700 -29.47900  -4.74400  1.000 73.51720  ? 363 VAL   A O     1 
ATOM   2866 C  CB    . VAL   A  1 371 ? 22.60800 -29.35500  -6.33100  1.000 69.19119  ? 363 VAL   A CB    1 
ATOM   2867 C  CG1   . VAL   A  1 371 ? 22.72900 -30.86600  -6.47500  1.000 71.43188  ? 363 VAL   A CG1   1 
ATOM   2868 C  CG2   . VAL   A  1 371 ? 23.74600 -28.66100  -7.06200  1.000 70.86206  ? 363 VAL   A CG2   1 
ATOM   2869 N  N     . LEU   A  1 372 ? 19.08100 -30.03700  -6.67200  1.000 66.45147  ? 364 LEU   A N     1 
ATOM   2870 C  CA    . LEU   A  1 372 ? 17.87300 -30.63000  -6.03500  1.000 66.37580  ? 364 LEU   A CA    1 
ATOM   2871 C  C     . LEU   A  1 372 ? 18.05100 -32.14900  -5.93200  1.000 64.51680  ? 364 LEU   A C     1 
ATOM   2872 O  O     . LEU   A  1 372 ? 17.80500 -32.85200  -6.93100  1.000 68.43299  ? 364 LEU   A O     1 
ATOM   2873 C  CB    . LEU   A  1 372 ? 16.62800 -30.25100  -6.84500  1.000 64.96545  ? 364 LEU   A CB    1 
ATOM   2874 C  CG    . LEU   A  1 372 ? 16.51100 -28.78100  -7.25000  1.000 67.31190  ? 364 LEU   A CG    1 
ATOM   2875 C  CD1   . LEU   A  1 372 ? 15.10400 -28.47400  -7.74000  1.000 66.98587  ? 364 LEU   A CD1   1 
ATOM   2876 C  CD2   . LEU   A  1 372 ? 16.87600 -27.84900  -6.10600  1.000 68.49624  ? 364 LEU   A CD2   1 
ATOM   2877 N  N     . GLY   A  1 373 ? 18.45300 -32.62600  -4.75200  1.000 66.26720  ? 365 GLY   A N     1 
ATOM   2878 C  CA    . GLY   A  1 373 ? 18.90200 -34.01000  -4.51900  1.000 61.78168  ? 365 GLY   A CA    1 
ATOM   2879 C  C     . GLY   A  1 373 ? 20.41100 -34.10800  -4.63600  1.000 65.59288  ? 365 GLY   A C     1 
ATOM   2880 O  O     . GLY   A  1 373 ? 20.89200 -34.70400  -5.62600  1.000 69.35088  ? 365 GLY   A O     1 
ATOM   2881 N  N     . ALA   A  1 374 ? 21.12700 -33.52800  -3.66700  1.000 63.80979  ? 366 ALA   A N     1 
ATOM   2882 C  CA    . ALA   A  1 374 ? 22.59100 -33.30700  -3.69200  1.000 65.01568  ? 366 ALA   A CA    1 
ATOM   2883 C  C     . ALA   A  1 374 ? 23.33500 -34.49200  -3.06600  1.000 64.55336  ? 366 ALA   A C     1 
ATOM   2884 O  O     . ALA   A  1 374 ? 24.56100 -34.56000  -3.25200  1.000 67.00400  ? 366 ALA   A O     1 
ATOM   2885 C  CB    . ALA   A  1 374 ? 22.92500 -32.02200  -2.97600  1.000 66.86846  ? 366 ALA   A CB    1 
ATOM   2886 N  N     . GLY   A  1 375 ? 22.62900 -35.37200  -2.34600  1.000 63.44504  ? 367 GLY   A N     1 
ATOM   2887 C  CA    . GLY   A  1 375 ? 23.19900 -36.53000  -1.62400  1.000 63.14317  ? 367 GLY   A CA    1 
ATOM   2888 C  C     . GLY   A  1 375 ? 24.47400 -36.16500  -0.88000  1.000 69.02150  ? 367 GLY   A C     1 
ATOM   2889 O  O     . GLY   A  1 375 ? 24.37200 -35.42000  0.11100   1.000 69.33874  ? 367 GLY   A O     1 
ATOM   2890 N  N     . ARG   A  1 376 ? 25.62900 -36.66100  -1.34200  1.000 65.23343  ? 368 ARG   A N     1 
ATOM   2891 C  CA    . ARG   A  1 376 ? 26.97100 -36.39300  -0.74800  1.000 67.01679  ? 368 ARG   A CA    1 
ATOM   2892 C  C     . ARG   A  1 376 ? 27.70600 -35.32100  -1.56900  1.000 70.06199  ? 368 ARG   A C     1 
ATOM   2893 O  O     . ARG   A  1 376 ? 28.90200 -35.09800  -1.30100  1.000 70.64080  ? 368 ARG   A O     1 
ATOM   2894 C  CB    . ARG   A  1 376 ? 27.76900 -37.69800  -0.65400  1.000 74.28899  ? 368 ARG   A CB    1 
ATOM   2895 C  CG    . ARG   A  1 376 ? 27.14500 -38.73000  0.27600   1.000 68.59466  ? 368 ARG   A CG    1 
ATOM   2896 C  CD    . ARG   A  1 376 ? 27.67900 -40.13900  0.10100   1.000 67.23329  ? 368 ARG   A CD    1 
ATOM   2897 N  NE    . ARG   A  1 376 ? 28.70700 -40.51900  1.06200   1.000 68.80999  ? 368 ARG   A NE    1 
ATOM   2898 C  CZ    . ARG   A  1 376 ? 29.87900 -41.08400  0.77100   1.000 71.33901  ? 368 ARG   A CZ    1 
ATOM   2899 N  NH1   . ARG   A  1 376 ? 30.22100 -41.34900  -0.47900  1.000 72.13728  ? 368 ARG   A NH1   1 
ATOM   2900 N  NH2   . ARG   A  1 376 ? 30.71500 -41.39000  1.74700   1.000 76.80812  ? 368 ARG   A NH2   1 
ATOM   2901 N  N     . GLY   A  1 377 ? 27.01500 -34.70000  -2.53400  1.000 71.50293  ? 369 GLY   A N     1 
ATOM   2902 C  CA    . GLY   A  1 377 ? 27.42600 -33.45900  -3.22400  1.000 72.25819  ? 369 GLY   A CA    1 
ATOM   2903 C  C     . GLY   A  1 377 ? 28.46500 -33.65500  -4.33000  1.000 77.77984  ? 369 GLY   A C     1 
ATOM   2904 O  O     . GLY   A  1 377 ? 29.41300 -32.87600  -4.41400  1.000 78.55185  ? 369 GLY   A O     1 
ATOM   2905 N  N     . PRO   A  1 378 ? 28.33100 -34.65900  -5.23100  1.000 73.02431  ? 370 PRO   A N     1 
ATOM   2906 C  CA    . PRO   A  1 378 ? 29.18500 -34.73800  -6.41600  1.000 73.45193  ? 370 PRO   A CA    1 
ATOM   2907 C  C     . PRO   A  1 378 ? 28.72900 -33.78600  -7.53300  1.000 76.78272  ? 370 PRO   A C     1 
ATOM   2908 O  O     . PRO   A  1 378 ? 29.52400 -33.49700  -8.40800  1.000 75.76755  ? 370 PRO   A O     1 
ATOM   2909 C  CB    . PRO   A  1 378 ? 29.03500 -36.19900  -6.85500  1.000 74.13752  ? 370 PRO   A CB    1 
ATOM   2910 C  CG    . PRO   A  1 378 ? 27.62500 -36.55500  -6.44000  1.000 70.24095  ? 370 PRO   A CG    1 
ATOM   2911 C  CD    . PRO   A  1 378 ? 27.38500 -35.78300  -5.15600  1.000 69.97294  ? 370 PRO   A CD    1 
ATOM   2912 N  N     . LEU   A  1 379 ? 27.46900 -33.33900  -7.47900  1.000 73.68522  ? 371 LEU   A N     1 
ATOM   2913 C  CA    . LEU   A  1 379 ? 26.87200 -32.37100  -8.44000  1.000 70.82023  ? 371 LEU   A CA    1 
ATOM   2914 C  C     . LEU   A  1 379 ? 27.16000 -30.94500  -7.95600  1.000 78.01428  ? 371 LEU   A C     1 
ATOM   2915 O  O     . LEU   A  1 379 ? 27.35800 -30.06500  -8.81200  1.000 78.87825  ? 371 LEU   A O     1 
ATOM   2916 C  CB    . LEU   A  1 379 ? 25.36600 -32.63400  -8.55100  1.000 69.77569  ? 371 LEU   A CB    1 
ATOM   2917 C  CG    . LEU   A  1 379 ? 24.80400 -32.67900  -9.97100  1.000 71.25712  ? 371 LEU   A CG    1 
ATOM   2918 C  CD1   . LEU   A  1 379 ? 25.38500 -33.84700  -10.75900 1.000 74.08066  ? 371 LEU   A CD1   1 
ATOM   2919 C  CD2   . LEU   A  1 379 ? 23.28700 -32.77800  -9.94200  1.000 67.84855  ? 371 LEU   A CD2   1 
ATOM   2920 N  N     . VAL   A  1 380 ? 27.17800 -30.73500  -6.63300  1.000 78.74062  ? 372 VAL   A N     1 
ATOM   2921 C  CA    . VAL   A  1 380 ? 27.61200 -29.46000  -5.98500  1.000 76.99467  ? 372 VAL   A CA    1 
ATOM   2922 C  C     . VAL   A  1 380 ? 29.05900 -29.18700  -6.41200  1.000 81.45407  ? 372 VAL   A C     1 
ATOM   2923 O  O     . VAL   A  1 380 ? 29.35200 -28.03900  -6.80000  1.000 83.69590  ? 372 VAL   A O     1 
ATOM   2924 C  CB    . VAL   A  1 380 ? 27.47700 -29.51200  -4.44900  1.000 73.51726  ? 372 VAL   A CB    1 
ATOM   2925 C  CG1   . VAL   A  1 380 ? 28.09500 -28.28900  -3.78400  1.000 75.37541  ? 372 VAL   A CG1   1 
ATOM   2926 C  CG2   . VAL   A  1 380 ? 26.03000 -29.67100  -4.00600  1.000 71.75703  ? 372 VAL   A CG2   1 
ATOM   2927 N  N     . ASN   A  1 381 ? 29.91900 -30.21000  -6.33600  1.000 78.14856  ? 373 ASN   A N     1 
ATOM   2928 C  CA    . ASN   A  1 381 ? 31.35300 -30.14100  -6.72900  1.000 79.98458  ? 373 ASN   A CA    1 
ATOM   2929 C  C     . ASN   A  1 381 ? 31.44700 -29.86600  -8.23300  1.000 84.14786  ? 373 ASN   A C     1 
ATOM   2930 O  O     . ASN   A  1 381 ? 32.26400 -29.01300  -8.62600  1.000 85.45760  ? 373 ASN   A O     1 
ATOM   2931 C  CB    . ASN   A  1 381 ? 32.11500 -31.41500  -6.35200  1.000 80.48378  ? 373 ASN   A CB    1 
ATOM   2932 C  CG    . ASN   A  1 381 ? 32.28700 -31.59000  -4.85700  1.000 81.34770  ? 373 ASN   A CG    1 
ATOM   2933 O  OD1   . ASN   A  1 381 ? 32.63800 -30.65000  -4.14900  1.000 77.69472  ? 373 ASN   A OD1   1 
ATOM   2934 N  ND2   . ASN   A  1 381 ? 32.05400 -32.79700  -4.36700  1.000 85.21998  ? 373 ASN   A ND2   1 
ATOM   2935 N  N     . ALA   A  1 382 ? 30.63700 -30.56400  -9.03600  1.000 82.46478  ? 374 ALA   A N     1 
ATOM   2936 C  CA    . ALA   A  1 382 ? 30.55600 -30.40100  -10.50700 1.000 79.76629  ? 374 ALA   A CA    1 
ATOM   2937 C  C     . ALA   A  1 382 ? 30.18400 -28.95100  -10.84300 1.000 82.09791  ? 374 ALA   A C     1 
ATOM   2938 O  O     . ALA   A  1 382 ? 30.78700 -28.39000  -11.77900 1.000 87.22480  ? 374 ALA   A O     1 
ATOM   2939 C  CB    . ALA   A  1 382 ? 29.56400 -31.38000  -11.08400 1.000 76.75214  ? 374 ALA   A CB    1 
ATOM   2940 N  N     . SER   A  1 383 ? 29.24300 -28.37100  -10.09200 1.000 78.89589  ? 375 SER   A N     1 
ATOM   2941 C  CA    . SER   A  1 383 ? 28.75200 -26.97700  -10.26000 1.000 77.89234  ? 375 SER   A CA    1 
ATOM   2942 C  C     . SER   A  1 383 ? 29.87400 -25.97700  -9.95300  1.000 88.38170  ? 375 SER   A C     1 
ATOM   2943 O  O     . SER   A  1 383 ? 29.93400 -24.94100  -10.64100 1.000 93.57785  ? 375 SER   A O     1 
ATOM   2944 C  CB    . SER   A  1 383 ? 27.53600 -26.72600  -9.40700  1.000 76.86167  ? 375 SER   A CB    1 
ATOM   2945 O  OG    . SER   A  1 383 ? 26.49500 -27.63800  -9.72800  1.000 74.69435  ? 375 SER   A OG    1 
ATOM   2946 N  N     . LEU   A  1 384 ? 30.72900 -26.27800  -8.96800  1.000 87.13441  ? 376 LEU   A N     1 
ATOM   2947 C  CA    . LEU   A  1 384 ? 31.88000 -25.41800  -8.56700  1.000 91.91960  ? 376 LEU   A CA    1 
ATOM   2948 C  C     . LEU   A  1 384 ? 32.96200 -25.45000  -9.65300  1.000 96.41462  ? 376 LEU   A C     1 
ATOM   2949 O  O     . LEU   A  1 384 ? 33.44800 -24.36600  -10.02200 1.000 103.95520 ? 376 LEU   A O     1 
ATOM   2950 C  CB    . LEU   A  1 384 ? 32.45300 -25.89200  -7.22500  1.000 85.51356  ? 376 LEU   A CB    1 
ATOM   2951 C  CG    . LEU   A  1 384 ? 31.64300 -25.53500  -5.98000  1.000 84.97850  ? 376 LEU   A CG    1 
ATOM   2952 C  CD1   . LEU   A  1 384 ? 32.30200 -26.10500  -4.73300  1.000 85.83472  ? 376 LEU   A CD1   1 
ATOM   2953 C  CD2   . LEU   A  1 384 ? 31.47200 -24.02900  -5.84000  1.000 89.70753  ? 376 LEU   A CD2   1 
ATOM   2954 N  N     . ARG   A  1 385 ? 33.34200 -26.64600  -10.11600 1.000 90.21363  ? 377 ARG   A N     1 
ATOM   2955 C  CA    . ARG   A  1 385 ? 34.38300 -26.85100  -11.16200 1.000 91.56811  ? 377 ARG   A CA    1 
ATOM   2956 C  C     . ARG   A  1 385 ? 33.96800 -26.11400  -12.44100 1.000 96.28289  ? 377 ARG   A C     1 
ATOM   2957 O  O     . ARG   A  1 385 ? 34.81800 -25.40500  -13.01100 1.000 96.02755  ? 377 ARG   A O     1 
ATOM   2958 C  CB    . ARG   A  1 385 ? 34.59400 -28.34400  -11.43700 1.000 89.04224  ? 377 ARG   A CB    1 
ATOM   2959 C  CG    . ARG   A  1 385 ? 35.30300 -29.09000  -10.31600 1.000 86.62003  ? 377 ARG   A CG    1 
ATOM   2960 C  CD    . ARG   A  1 385 ? 35.78400 -30.46300  -10.74900 1.000 86.60642  ? 377 ARG   A CD    1 
ATOM   2961 N  NE    . ARG   A  1 385 ? 34.71200 -31.29400  -11.28700 1.000 88.34927  ? 377 ARG   A NE    1 
ATOM   2962 C  CZ    . ARG   A  1 385 ? 33.85900 -32.01800  -10.56400 1.000 83.88592  ? 377 ARG   A CZ    1 
ATOM   2963 N  NH1   . ARG   A  1 385 ? 33.92700 -32.02500  -9.24300  1.000 80.65874  ? 377 ARG   A NH1   1 
ATOM   2964 N  NH2   . ARG   A  1 385 ? 32.92800 -32.73500  -11.17100 1.000 85.29316  ? 377 ARG   A NH2   1 
ATOM   2965 N  N     . ALA   A  1 386 ? 32.70500 -26.27100  -12.85200 1.000 94.71904  ? 378 ALA   A N     1 
ATOM   2966 C  CA    . ALA   A  1 386 ? 32.10100 -25.64500  -14.05300 1.000 94.44149  ? 378 ALA   A CA    1 
ATOM   2967 C  C     . ALA   A  1 386 ? 32.16700 -24.11700  -13.94200 1.000 95.66957  ? 378 ALA   A C     1 
ATOM   2968 O  O     . ALA   A  1 386 ? 32.43200 -23.46100  -14.96800 1.000 97.27473  ? 378 ALA   A O     1 
ATOM   2969 C  CB    . ALA   A  1 386 ? 30.67700 -26.12000  -14.21800 1.000 86.73311  ? 378 ALA   A CB    1 
ATOM   2970 N  N     . ALA   A  1 387 ? 31.94000 -23.58000  -12.73900 1.000 97.11492  ? 379 ALA   A N     1 
ATOM   2971 C  CA    . ALA   A  1 387 ? 31.87600 -22.12900  -12.44900 1.000 92.54659  ? 379 ALA   A CA    1 
ATOM   2972 C  C     . ALA   A  1 387 ? 33.24400 -21.47900  -12.67900 1.000 100.96505 ? 379 ALA   A C     1 
ATOM   2973 O  O     . ALA   A  1 387 ? 33.28800 -20.46000  -13.40000 1.000 105.32761 ? 379 ALA   A O     1 
ATOM   2974 C  CB    . ALA   A  1 387 ? 31.38600 -21.89800  -11.04200 1.000 94.25401  ? 379 ALA   A CB    1 
ATOM   2975 N  N     . LYS   A  1 388 ? 34.31500 -22.04000  -12.10300 1.000 103.15209 ? 380 LYS   A N     1 
ATOM   2976 C  CA    . LYS   A  1 388 ? 35.68600 -21.46300  -12.20400 1.000 112.87195 ? 380 LYS   A CA    1 
ATOM   2977 C  C     . LYS   A  1 388 ? 36.47000 -22.14800  -13.33600 1.000 109.91705 ? 380 LYS   A C     1 
ATOM   2978 O  O     . LYS   A  1 388 ? 37.70300 -21.96400  -13.38800 1.000 112.52351 ? 380 LYS   A O     1 
ATOM   2979 C  CB    . LYS   A  1 388 ? 36.39900 -21.50100  -10.84500 1.000 117.14729 ? 380 LYS   A CB    1 
ATOM   2980 C  CG    . LYS   A  1 388 ? 36.96400 -22.84200  -10.39400 1.000 114.50128 ? 380 LYS   A CG    1 
ATOM   2981 C  CD    . LYS   A  1 388 ? 37.96300 -22.70700  -9.25300  1.000 124.83103 ? 380 LYS   A CD    1 
ATOM   2982 C  CE    . LYS   A  1 388 ? 37.38600 -22.09000  -7.99400  1.000 123.84862 ? 380 LYS   A CE    1 
ATOM   2983 N  NZ    . LYS   A  1 388 ? 36.38200 -22.97600  -7.35600  1.000 123.16599 ? 380 LYS   A NZ    1 
ATOM   2984 N  N     . GLN   A  1 389 ? 35.78200 -22.88100  -14.22100 1.000 102.24789 ? 381 GLN   A N     1 
ATOM   2985 C  CA    . GLN   A  1 389 ? 36.29800 -23.28800  -15.55800 1.000 100.80292 ? 381 GLN   A CA    1 
ATOM   2986 C  C     . GLN   A  1 389 ? 35.75300 -22.30200  -16.60200 1.000 101.44389 ? 381 GLN   A C     1 
ATOM   2987 O  O     . GLN   A  1 389 ? 36.52600 -21.90400  -17.50000 1.000 98.91379  ? 381 GLN   A O     1 
ATOM   2988 C  CB    . GLN   A  1 389 ? 35.90400 -24.73200  -15.88400 1.000 100.12373 ? 381 GLN   A CB    1 
ATOM   2989 C  CG    . GLN   A  1 389 ? 36.91700 -25.46500  -16.75500 1.000 99.12819  ? 381 GLN   A CG    1 
ATOM   2990 C  CD    . GLN   A  1 389 ? 36.37600 -26.75100  -17.33500 1.000 105.75669 ? 381 GLN   A CD    1 
ATOM   2991 O  OE1   . GLN   A  1 389 ? 35.40800 -27.32700  -16.83900 1.000 102.97803 ? 381 GLN   A OE1   1 
ATOM   2992 N  NE2   . GLN   A  1 389 ? 37.00400 -27.21700  -18.40300 1.000 100.54212 ? 381 GLN   A NE2   1 
ATOM   2993 N  N     . ALA   A  1 390 ? 34.47400 -21.92700  -16.47500 1.000 104.09202 ? 382 ALA   A N     1 
ATOM   2994 C  CA    . ALA   A  1 390 ? 33.78600 -20.89600  -17.29000 1.000 99.61563  ? 382 ALA   A CA    1 
ATOM   2995 C  C     . ALA   A  1 390 ? 34.14000 -19.49200  -16.77900 1.000 99.10784  ? 382 ALA   A C     1 
ATOM   2996 O  O     . ALA   A  1 390 ? 33.91400 -18.52400  -17.52900 1.000 105.02886 ? 382 ALA   A O     1 
ATOM   2997 C  CB    . ALA   A  1 390 ? 32.29300 -21.12500  -17.25800 1.000 94.33863  ? 382 ALA   A CB    1 
ATOM   2998 N  N     . ASP   A  1 391 ? 34.65200 -19.39100  -15.54600 1.000 102.00492 ? 383 ASP   A N     1 
ATOM   2999 C  CA    . ASP   A  1 391 ? 35.04900 -18.11800  -14.88200 1.000 105.27812 ? 383 ASP   A CA    1 
ATOM   3000 C  C     . ASP   A  1 391 ? 33.80200 -17.23800  -14.71200 1.000 101.90440 ? 383 ASP   A C     1 
ATOM   3001 O  O     . ASP   A  1 391 ? 33.76400 -16.13500  -15.29600 1.000 104.66456 ? 383 ASP   A O     1 
ATOM   3002 C  CB    . ASP   A  1 391 ? 36.17400 -17.41700  -15.65300 1.000 104.68598 ? 383 ASP   A CB    1 
ATOM   3003 C  CG    . ASP   A  1 391 ? 36.79500 -16.23100  -14.92700 1.000 110.63587 ? 383 ASP   A CG    1 
ATOM   3004 O  OD1   . ASP   A  1 391 ? 36.57200 -16.09900  -13.70600 1.000 115.62717 ? 383 ASP   A OD1   1 
ATOM   3005 O  OD2   . ASP   A  1 391 ? 37.49600 -15.44400  -15.59100 1.000 112.42681 ? 383 ASP   A OD2   1 
ATOM   3006 N  N     . ARG   A  1 392 ? 32.81800 -17.73200  -13.95300 1.000 98.72375  ? 384 ARG   A N     1 
ATOM   3007 C  CA    . ARG   A  1 392 ? 31.56900 -17.01000  -13.58800 1.000 100.89229 ? 384 ARG   A CA    1 
ATOM   3008 C  C     . ARG   A  1 392 ? 31.25600 -17.28200  -12.11100 1.000 104.94457 ? 384 ARG   A C     1 
ATOM   3009 O  O     . ARG   A  1 392 ? 31.54100 -18.40500  -11.64600 1.000 99.61912  ? 384 ARG   A O     1 
ATOM   3010 C  CB    . ARG   A  1 392 ? 30.40600 -17.45600  -14.48100 1.000 99.01773  ? 384 ARG   A CB    1 
ATOM   3011 C  CG    . ARG   A  1 392 ? 30.58900 -17.15400  -15.96200 1.000 104.65927 ? 384 ARG   A CG    1 
ATOM   3012 C  CD    . ARG   A  1 392 ? 30.51200 -15.67300  -16.28600 1.000 107.55662 ? 384 ARG   A CD    1 
ATOM   3013 N  NE    . ARG   A  1 392 ? 30.18500 -15.43700  -17.69000 1.000 103.00460 ? 384 ARG   A NE    1 
ATOM   3014 C  CZ    . ARG   A  1 392 ? 31.06100 -15.21300  -18.66600 1.000 105.21253 ? 384 ARG   A CZ    1 
ATOM   3015 N  NH1   . ARG   A  1 392 ? 32.36100 -15.17900  -18.42100 1.000 106.48085 ? 384 ARG   A NH1   1 
ATOM   3016 N  NH2   . ARG   A  1 392 ? 30.62400 -15.01900  -19.89800 1.000 106.31924 ? 384 ARG   A NH2   1 
ATOM   3017 N  N     . ARG   A  1 393 ? 30.69900 -16.29200  -11.40400 1.000 102.88505 ? 385 ARG   A N     1 
ATOM   3018 C  CA    . ARG   A  1 393 ? 30.31800 -16.39600  -9.96800  1.000 96.66533  ? 385 ARG   A CA    1 
ATOM   3019 C  C     . ARG   A  1 393 ? 28.95400 -17.09000  -9.86900  1.000 95.38029  ? 385 ARG   A C     1 
ATOM   3020 O  O     . ARG   A  1 393 ? 28.08800 -16.81500  -10.72800 1.000 94.12764  ? 385 ARG   A O     1 
ATOM   3021 C  CB    . ARG   A  1 393 ? 30.30200 -15.01200  -9.30900  1.000 104.82246 ? 385 ARG   A CB    1 
ATOM   3022 C  CG    . ARG   A  1 393 ? 31.60600 -14.24000  -9.46400  1.000 110.93259 ? 385 ARG   A CG    1 
ATOM   3023 C  CD    . ARG   A  1 393 ? 31.94500 -13.35000  -8.28100  1.000 118.17958 ? 385 ARG   A CD    1 
ATOM   3024 N  NE    . ARG   A  1 393 ? 30.96400 -12.29200  -8.06100  1.000 118.88571 ? 385 ARG   A NE    1 
ATOM   3025 C  CZ    . ARG   A  1 393 ? 30.33400 -12.03800  -6.91200  1.000 122.84165 ? 385 ARG   A CZ    1 
ATOM   3026 N  NH1   . ARG   A  1 393 ? 30.57300 -12.75800  -5.82700  1.000 127.98009 ? 385 ARG   A NH1   1 
ATOM   3027 N  NH2   . ARG   A  1 393 ? 29.46400 -11.04300  -6.84900  1.000 124.35740 ? 385 ARG   A NH2   1 
ATOM   3028 N  N     . ILE   A  1 394 ? 28.78500 -17.96600  -8.87100  1.000 94.91203  ? 386 ILE   A N     1 
ATOM   3029 C  CA    . ILE   A  1 394 ? 27.53600 -18.75000  -8.62800  1.000 89.44795  ? 386 ILE   A CA    1 
ATOM   3030 C  C     . ILE   A  1 394 ? 27.22600 -18.76000  -7.12800  1.000 94.43083  ? 386 ILE   A C     1 
ATOM   3031 O  O     . ILE   A  1 394 ? 28.18000 -18.77500  -6.32200  1.000 98.41721  ? 386 ILE   A O     1 
ATOM   3032 C  CB    . ILE   A  1 394 ? 27.65600 -20.18700  -9.17400  1.000 87.13759  ? 386 ILE   A CB    1 
ATOM   3033 C  CG1   . ILE   A  1 394 ? 28.91800 -20.88900  -8.66400  1.000 87.42802  ? 386 ILE   A CG1   1 
ATOM   3034 C  CG2   . ILE   A  1 394 ? 27.58200 -20.19600  -10.69200 1.000 87.48890  ? 386 ILE   A CG2   1 
ATOM   3035 C  CD1   . ILE   A  1 394 ? 28.83700 -22.39700  -8.70400  1.000 85.92368  ? 386 ILE   A CD1   1 
ATOM   3036 N  N     . LYS   A  1 395 ? 25.93600 -18.76000  -6.78200  1.000 88.53871  ? 387 LYS   A N     1 
ATOM   3037 C  CA    . LYS   A  1 395 ? 25.42600 -18.97800  -5.40300  1.000 87.10020  ? 387 LYS   A CA    1 
ATOM   3038 C  C     . LYS   A  1 395 ? 24.74000 -20.34600  -5.38200  1.000 86.67516  ? 387 LYS   A C     1 
ATOM   3039 O  O     . LYS   A  1 395 ? 23.76800 -20.52400  -6.14500  1.000 89.03005  ? 387 LYS   A O     1 
ATOM   3040 C  CB    . LYS   A  1 395 ? 24.48000 -17.84400  -4.99900  1.000 88.55855  ? 387 LYS   A CB    1 
ATOM   3041 C  CG    . LYS   A  1 395 ? 24.02600 -17.86200  -3.54600  1.000 88.35338  ? 387 LYS   A CG    1 
ATOM   3042 C  CD    . LYS   A  1 395 ? 23.35700 -16.57400  -3.11600  1.000 90.46379  ? 387 LYS   A CD    1 
ATOM   3043 C  CE    . LYS   A  1 395 ? 22.52600 -16.72300  -1.86100  1.000 90.00007  ? 387 LYS   A CE    1 
ATOM   3044 N  NZ    . LYS   A  1 395 ? 21.73500 -15.50000  -1.58900  1.000 94.90922  ? 387 LYS   A NZ    1 
ATOM   3045 N  N     . LEU   A  1 396 ? 25.24900 -21.27700  -4.56900  1.000 89.44432  ? 388 LEU   A N     1 
ATOM   3046 C  CA    . LEU   A  1 396 ? 24.81300 -22.70000  -4.55100  1.000 83.27236  ? 388 LEU   A CA    1 
ATOM   3047 C  C     . LEU   A  1 396 ? 23.79300 -22.93000  -3.43000  1.000 81.99048  ? 388 LEU   A C     1 
ATOM   3048 O  O     . LEU   A  1 396 ? 23.98900 -22.39400  -2.32200  1.000 84.96896  ? 388 LEU   A O     1 
ATOM   3049 C  CB    . LEU   A  1 396 ? 26.03500 -23.60900  -4.37600  1.000 81.59526  ? 388 LEU   A CB    1 
ATOM   3050 C  CG    . LEU   A  1 396 ? 26.75000 -23.99000  -5.67200  1.000 79.85964  ? 388 LEU   A CG    1 
ATOM   3051 C  CD1   . LEU   A  1 396 ? 28.16800 -24.46600  -5.39600  1.000 81.78587  ? 388 LEU   A CD1   1 
ATOM   3052 C  CD2   . LEU   A  1 396 ? 25.97000 -25.05100  -6.43100  1.000 79.10229  ? 388 LEU   A CD2   1 
ATOM   3053 N  N     . TYR   A  1 397 ? 22.73700 -23.68500  -3.73800  1.000 81.04029  ? 389 TYR   A N     1 
ATOM   3054 C  CA    . TYR   A  1 397 ? 21.83700 -24.35000  -2.76200  1.000 76.62949  ? 389 TYR   A CA    1 
ATOM   3055 C  C     . TYR   A  1 397 ? 21.92000 -25.85700  -3.01400  1.000 76.83098  ? 389 TYR   A C     1 
ATOM   3056 O  O     . TYR   A  1 397 ? 21.83400 -26.26100  -4.18900  1.000 77.99726  ? 389 TYR   A O     1 
ATOM   3057 C  CB    . TYR   A  1 397 ? 20.40300 -23.83200  -2.88800  1.000 76.47783  ? 389 TYR   A CB    1 
ATOM   3058 C  CG    . TYR   A  1 397 ? 20.19800 -22.41800  -2.40600  1.000 84.09409  ? 389 TYR   A CG    1 
ATOM   3059 C  CD1   . TYR   A  1 397 ? 20.52300 -21.33600  -3.20800  1.000 81.94204  ? 389 TYR   A CD1   1 
ATOM   3060 C  CD2   . TYR   A  1 397 ? 19.67500 -22.15900  -1.14900  1.000 83.29595  ? 389 TYR   A CD2   1 
ATOM   3061 C  CE1   . TYR   A  1 397 ? 20.33600 -20.03400  -2.77500  1.000 84.07227  ? 389 TYR   A CE1   1 
ATOM   3062 C  CE2   . TYR   A  1 397 ? 19.48300 -20.86200  -0.69900  1.000 83.11404  ? 389 TYR   A CE2   1 
ATOM   3063 C  CZ    . TYR   A  1 397 ? 19.81400 -19.79500  -1.51600  1.000 86.47573  ? 389 TYR   A CZ    1 
ATOM   3064 O  OH    . TYR   A  1 397 ? 19.62800 -18.51300  -1.08500  1.000 90.85960  ? 389 TYR   A OH    1 
ATOM   3065 N  N     . ALA   A  1 398 ? 22.12400 -26.64300  -1.95300  1.000 75.89471  ? 390 ALA   A N     1 
ATOM   3066 C  CA    . ALA   A  1 398 ? 22.18400 -28.12200  -1.98200  1.000 71.45327  ? 390 ALA   A CA    1 
ATOM   3067 C  C     . ALA   A  1 398 ? 20.96900 -28.68000  -1.23200  1.000 73.60772  ? 390 ALA   A C     1 
ATOM   3068 O  O     . ALA   A  1 398 ? 21.10700 -29.03500  -0.04300  1.000 76.09224  ? 390 ALA   A O     1 
ATOM   3069 C  CB    . ALA   A  1 398 ? 23.49000 -28.59800  -1.39200  1.000 71.87942  ? 390 ALA   A CB    1 
ATOM   3070 N  N     . VAL   A  1 399 ? 19.81600 -28.72900  -1.90700  1.000 69.42849  ? 391 VAL   A N     1 
ATOM   3071 C  CA    . VAL   A  1 399 ? 18.54200 -29.29100  -1.36600  1.000 71.12669  ? 391 VAL   A CA    1 
ATOM   3072 C  C     . VAL   A  1 399 ? 18.68400 -30.81800  -1.32900  1.000 69.30172  ? 391 VAL   A C     1 
ATOM   3073 O  O     . VAL   A  1 399 ? 19.01200 -31.39700  -2.37900  1.000 71.31399  ? 391 VAL   A O     1 
ATOM   3074 C  CB    . VAL   A  1 399 ? 17.32400 -28.84500  -2.20100  1.000 68.19475  ? 391 VAL   A CB    1 
ATOM   3075 C  CG1   . VAL   A  1 399 ? 16.03100 -29.48500  -1.71500  1.000 67.16267  ? 391 VAL   A CG1   1 
ATOM   3076 C  CG2   . VAL   A  1 399 ? 17.17900 -27.33100  -2.23300  1.000 70.25145  ? 391 VAL   A CG2   1 
ATOM   3077 N  N     . GLU   A  1 400 ? 18.46600 -31.43400  -0.16100  1.000 66.24356  ? 392 GLU   A N     1 
ATOM   3078 C  CA    . GLU   A  1 400 ? 18.55200 -32.90600  0.04300   1.000 64.70536  ? 392 GLU   A CA    1 
ATOM   3079 C  C     . GLU   A  1 400 ? 17.52300 -33.33800  1.09700   1.000 65.20254  ? 392 GLU   A C     1 
ATOM   3080 O  O     . GLU   A  1 400 ? 17.54800 -32.78200  2.20500   1.000 67.07155  ? 392 GLU   A O     1 
ATOM   3081 C  CB    . GLU   A  1 400 ? 19.97100 -33.30500  0.45600   1.000 65.18595  ? 392 GLU   A CB    1 
ATOM   3082 C  CG    . GLU   A  1 400 ? 20.14100 -34.79600  0.69100   1.000 63.90758  ? 392 GLU   A CG    1 
ATOM   3083 C  CD    . GLU   A  1 400 ? 19.58400 -35.67700  -0.41600  1.000 65.38717  ? 392 GLU   A CD    1 
ATOM   3084 O  OE1   . GLU   A  1 400 ? 20.14800 -35.65800  -1.52800  1.000 62.91449  ? 392 GLU   A OE1   1 
ATOM   3085 O  OE2   . GLU   A  1 400 ? 18.57400 -36.36700  -0.16900  1.000 66.33604  ? 392 GLU   A OE2   1 
ATOM   3086 N  N     . LYS   A  1 401 ? 16.66300 -34.30100  0.75200   1.000 63.74705  ? 393 LYS   A N     1 
ATOM   3087 C  CA    . LYS   A  1 401 ? 15.56600 -34.81200  1.61700   1.000 63.65736  ? 393 LYS   A CA    1 
ATOM   3088 C  C     . LYS   A  1 401 ? 16.09300 -35.91000  2.54900   1.000 63.99960  ? 393 LYS   A C     1 
ATOM   3089 O  O     . LYS   A  1 401 ? 15.50900 -36.08100  3.63500   1.000 64.55228  ? 393 LYS   A O     1 
ATOM   3090 C  CB    . LYS   A  1 401 ? 14.41300 -35.36200  0.77100   1.000 61.90527  ? 393 LYS   A CB    1 
ATOM   3091 C  CG    . LYS   A  1 401 ? 14.73800 -36.61400  -0.03800  1.000 62.99841  ? 393 LYS   A CG    1 
ATOM   3092 C  CD    . LYS   A  1 401 ? 13.87000 -37.81000  0.30200   1.000 66.28745  ? 393 LYS   A CD    1 
ATOM   3093 C  CE    . LYS   A  1 401 ? 14.61800 -39.12400  0.23100   1.000 66.01465  ? 393 LYS   A CE    1 
ATOM   3094 N  NZ    . LYS   A  1 401 ? 13.86600 -40.21400  0.89500   1.000 61.51215  ? 393 LYS   A NZ    1 
ATOM   3095 N  N     . ASN   A  1 402 ? 17.12800 -36.64300  2.12700   1.000 61.71138  ? 394 ASN   A N     1 
ATOM   3096 C  CA    . ASN   A  1 402 ? 17.75000 -37.74400  2.91000   1.000 63.59385  ? 394 ASN   A CA    1 
ATOM   3097 C  C     . ASN   A  1 402 ? 18.55100 -37.12600  4.05300   1.000 68.39080  ? 394 ASN   A C     1 
ATOM   3098 O  O     . ASN   A  1 402 ? 19.62100 -36.56800  3.82400   1.000 70.71687  ? 394 ASN   A O     1 
ATOM   3099 C  CB    . ASN   A  1 402 ? 18.62400 -38.64200  2.03000   1.000 62.70034  ? 394 ASN   A CB    1 
ATOM   3100 C  CG    . ASN   A  1 402 ? 19.13900 -39.87500  2.74600   1.000 64.25755  ? 394 ASN   A CG    1 
ATOM   3101 O  OD1   . ASN   A  1 402 ? 18.94700 -40.03300  3.94800   1.000 65.70246  ? 394 ASN   A OD1   1 
ATOM   3102 N  ND2   . ASN   A  1 402 ? 19.80100 -40.75600  2.01600   1.000 66.23443  ? 394 ASN   A ND2   1 
ATOM   3103 N  N     . PRO   A  1 403 ? 18.08100 -37.21900  5.31900   1.000 64.25425  ? 395 PRO   A N     1 
ATOM   3104 C  CA    . PRO   A  1 403 ? 18.73400 -36.52400  6.42800   1.000 68.94304  ? 395 PRO   A CA    1 
ATOM   3105 C  C     . PRO   A  1 403 ? 20.11800 -37.10900  6.75600   1.000 66.72065  ? 395 PRO   A C     1 
ATOM   3106 O  O     . PRO   A  1 403 ? 20.94900 -36.38000  7.26600   1.000 68.27513  ? 395 PRO   A O     1 
ATOM   3107 C  CB    . PRO   A  1 403 ? 17.74400 -36.70300  7.59000   1.000 66.80239  ? 395 PRO   A CB    1 
ATOM   3108 C  CG    . PRO   A  1 403 ? 17.04100 -38.00400  7.27400   1.000 65.16057  ? 395 PRO   A CG    1 
ATOM   3109 C  CD    . PRO   A  1 403 ? 16.93700 -38.03100  5.76300   1.000 64.70033  ? 395 PRO   A CD    1 
ATOM   3110 N  N     . ASN   A  1 404 ? 20.33100 -38.39000  6.44000   1.000 65.56964  ? 396 ASN   A N     1 
ATOM   3111 C  CA    . ASN   A  1 404 ? 21.62400 -39.10200  6.63100   1.000 66.07609  ? 396 ASN   A CA    1 
ATOM   3112 C  C     . ASN   A  1 404 ? 22.67900 -38.48700  5.70300   1.000 68.37343  ? 396 ASN   A C     1 
ATOM   3113 O  O     . ASN   A  1 404 ? 23.83700 -38.32900  6.14300   1.000 67.71630  ? 396 ASN   A O     1 
ATOM   3114 C  CB    . ASN   A  1 404 ? 21.48000 -40.60500  6.38400   1.000 64.80263  ? 396 ASN   A CB    1 
ATOM   3115 C  CG    . ASN   A  1 404 ? 20.33800 -41.22600  7.16000   1.000 67.84528  ? 396 ASN   A CG    1 
ATOM   3116 O  OD1   . ASN   A  1 404 ? 20.38900 -41.31900  8.38600   1.000 69.84985  ? 396 ASN   A OD1   1 
ATOM   3117 N  ND2   . ASN   A  1 404 ? 19.30500 -41.65600  6.45400   1.000 65.43865  ? 396 ASN   A ND2   1 
ATOM   3118 N  N     . ALA   A  1 405 ? 22.28100 -38.16200  4.46700   1.000 69.43502  ? 397 ALA   A N     1 
ATOM   3119 C  CA    . ALA   A  1 405 ? 23.12400 -37.53200  3.42200   1.000 65.38267  ? 397 ALA   A CA    1 
ATOM   3120 C  C     . ALA   A  1 405 ? 23.41100 -36.07100  3.79300   1.000 67.03888  ? 397 ALA   A C     1 
ATOM   3121 O  O     . ALA   A  1 405 ? 24.54200 -35.61300  3.54200   1.000 69.34930  ? 397 ALA   A O     1 
ATOM   3122 C  CB    . ALA   A  1 405 ? 22.44200 -37.63800  2.08100   1.000 63.80744  ? 397 ALA   A CB    1 
ATOM   3123 N  N     . VAL   A  1 406 ? 22.42100 -35.37900  4.37100   1.000 67.38552  ? 398 VAL   A N     1 
ATOM   3124 C  CA    . VAL   A  1 406 ? 22.51500 -33.95800  4.82700   1.000 69.08142  ? 398 VAL   A CA    1 
ATOM   3125 C  C     . VAL   A  1 406 ? 23.67300 -33.82000  5.82400   1.000 70.84846  ? 398 VAL   A C     1 
ATOM   3126 O  O     . VAL   A  1 406 ? 24.31400 -32.75500  5.83200   1.000 72.30932  ? 398 VAL   A O     1 
ATOM   3127 C  CB    . VAL   A  1 406 ? 21.18300 -33.46800  5.43200   1.000 69.24978  ? 398 VAL   A CB    1 
ATOM   3128 C  CG1   . VAL   A  1 406 ? 21.34200 -32.17100  6.21400   1.000 71.31931  ? 398 VAL   A CG1   1 
ATOM   3129 C  CG2   . VAL   A  1 406 ? 20.10700 -33.31500  4.36700   1.000 67.93578  ? 398 VAL   A CG2   1 
ATOM   3130 N  N     . VAL   A  1 407 ? 23.92200 -34.85000  6.63700   1.000 70.86784  ? 399 VAL   A N     1 
ATOM   3131 C  CA    . VAL   A  1 407 ? 25.04100 -34.88200  7.62700   1.000 72.96933  ? 399 VAL   A CA    1 
ATOM   3132 C  C     . VAL   A  1 407 ? 26.36400 -34.75100  6.86500   1.000 76.13640  ? 399 VAL   A C     1 
ATOM   3133 O  O     . VAL   A  1 407 ? 27.23100 -33.97800  7.31900   1.000 78.44221  ? 399 VAL   A O     1 
ATOM   3134 C  CB    . VAL   A  1 407 ? 25.00700 -36.15900  8.48900   1.000 72.52684  ? 399 VAL   A CB    1 
ATOM   3135 C  CG1   . VAL   A  1 407 ? 26.29100 -36.35800  9.28100   1.000 74.32639  ? 399 VAL   A CG1   1 
ATOM   3136 C  CG2   . VAL   A  1 407 ? 23.80400 -36.16800  9.41700   1.000 72.60957  ? 399 VAL   A CG2   1 
ATOM   3137 N  N     . THR   A  1 408 ? 26.50100 -35.48100  5.75400   1.000 71.67904  ? 400 THR   A N     1 
ATOM   3138 C  CA    . THR   A  1 408 ? 27.71100 -35.49600  4.88900   1.000 75.53317  ? 400 THR   A CA    1 
ATOM   3139 C  C     . THR   A  1 408 ? 27.93700 -34.09800  4.30400   1.000 72.97985  ? 400 THR   A C     1 
ATOM   3140 O  O     . THR   A  1 408 ? 29.09800 -33.64700  4.30600   1.000 76.64059  ? 400 THR   A O     1 
ATOM   3141 C  CB    . THR   A  1 408 ? 27.59400 -36.55100  3.78100   1.000 71.48302  ? 400 THR   A CB    1 
ATOM   3142 O  OG1   . THR   A  1 408 ? 27.04900 -37.74200  4.34900   1.000 69.37994  ? 400 THR   A OG1   1 
ATOM   3143 C  CG2   . THR   A  1 408 ? 28.92300 -36.85300  3.12500   1.000 71.32796  ? 400 THR   A CG2   1 
ATOM   3144 N  N     . LEU   A  1 409 ? 26.86100 -33.44900  3.84200   1.000 72.18371  ? 401 LEU   A N     1 
ATOM   3145 C  CA    . LEU   A  1 409 ? 26.87800 -32.11200  3.18300   1.000 75.93696  ? 401 LEU   A CA    1 
ATOM   3146 C  C     . LEU   A  1 409 ? 27.28500 -31.03200  4.19000   1.000 79.25993  ? 401 LEU   A C     1 
ATOM   3147 O  O     . LEU   A  1 409 ? 28.20300 -30.25400  3.87000   1.000 78.37783  ? 401 LEU   A O     1 
ATOM   3148 C  CB    . LEU   A  1 409 ? 25.49000 -31.80500  2.61200   1.000 71.73689  ? 401 LEU   A CB    1 
ATOM   3149 C  CG    . LEU   A  1 409 ? 25.03800 -32.69200  1.45500   1.000 71.18964  ? 401 LEU   A CG    1 
ATOM   3150 C  CD1   . LEU   A  1 409 ? 23.57300 -32.44300  1.13000   1.000 69.47671  ? 401 LEU   A CD1   1 
ATOM   3151 C  CD2   . LEU   A  1 409 ? 25.90400 -32.46600  0.22500   1.000 73.36081  ? 401 LEU   A CD2   1 
ATOM   3152 N  N     . GLU   A  1 410 ? 26.60700 -30.97900  5.34300   1.000 78.12152  ? 402 GLU   A N     1 
ATOM   3153 C  CA    . GLU   A  1 410 ? 26.81300 -29.94800  6.39700   1.000 77.57253  ? 402 GLU   A CA    1 
ATOM   3154 C  C     . GLU   A  1 410 ? 28.23600 -30.06600  6.95400   1.000 79.17998  ? 402 GLU   A C     1 
ATOM   3155 O  O     . GLU   A  1 410 ? 28.83800 -29.01000  7.23700   1.000 82.47064  ? 402 GLU   A O     1 
ATOM   3156 C  CB    . GLU   A  1 410 ? 25.74700 -30.06800  7.48800   1.000 77.55351  ? 402 GLU   A CB    1 
ATOM   3157 C  CG    . GLU   A  1 410 ? 24.38700 -29.55900  7.04300   1.000 76.71008  ? 402 GLU   A CG    1 
ATOM   3158 C  CD    . GLU   A  1 410 ? 23.26000 -29.70500  8.05100   1.000 78.62857  ? 402 GLU   A CD    1 
ATOM   3159 O  OE1   . GLU   A  1 410 ? 23.23200 -30.72600  8.77100   1.000 79.31912  ? 402 GLU   A OE1   1 
ATOM   3160 O  OE2   . GLU   A  1 410 ? 22.40500 -28.80000  8.10600   1.000 81.12588  ? 402 GLU   A OE2   1 
ATOM   3161 N  N     . ASN   A  1 411 ? 28.75400 -31.29400  7.09100   1.000 78.58329  ? 403 ASN   A N     1 
ATOM   3162 C  CA    . ASN   A  1 411 ? 30.17400 -31.56200  7.45400   1.000 82.44561  ? 403 ASN   A CA    1 
ATOM   3163 C  C     . ASN   A  1 411 ? 31.07900 -30.97400  6.36500   1.000 86.02129  ? 403 ASN   A C     1 
ATOM   3164 O  O     . ASN   A  1 411 ? 32.05800 -30.28900  6.71700   1.000 90.17228  ? 403 ASN   A O     1 
ATOM   3165 C  CB    . ASN   A  1 411 ? 30.46400 -33.05300  7.67200   1.000 80.31423  ? 403 ASN   A CB    1 
ATOM   3166 C  CG    . ASN   A  1 411 ? 30.44300 -33.45500  9.13300   1.000 82.92876  ? 403 ASN   A CG    1 
ATOM   3167 O  OD1   . ASN   A  1 411 ? 31.47000 -33.82600  9.69800   1.000 85.47550  ? 403 ASN   A OD1   1 
ATOM   3168 N  ND2   . ASN   A  1 411 ? 29.28200 -33.37600  9.76000   1.000 79.91067  ? 403 ASN   A ND2   1 
ATOM   3169 N  N     . TRP   A  1 412 ? 30.74300 -31.22100  5.09500   1.000 86.93952  ? 404 TRP   A N     1 
ATOM   3170 C  CA    . TRP   A  1 412 ? 31.50600 -30.75600  3.90500   1.000 84.53444  ? 404 TRP   A CA    1 
ATOM   3171 C  C     . TRP   A  1 412 ? 31.32900 -29.24000  3.71700   1.000 86.28962  ? 404 TRP   A C     1 
ATOM   3172 O  O     . TRP   A  1 412 ? 32.30500 -28.58700  3.29800   1.000 86.79348  ? 404 TRP   A O     1 
ATOM   3173 C  CB    . TRP   A  1 412 ? 31.07600 -31.54800  2.66400   1.000 85.85902  ? 404 TRP   A CB    1 
ATOM   3174 C  CG    . TRP   A  1 412 ? 32.04800 -31.48400  1.52800   1.000 94.36320  ? 404 TRP   A CG    1 
ATOM   3175 C  CD1   . TRP   A  1 412 ? 32.00500 -30.63000  0.46700   1.000 95.02222  ? 404 TRP   A CD1   1 
ATOM   3176 C  CD2   . TRP   A  1 412 ? 33.21100 -32.30800  1.32700   1.000 99.53394  ? 404 TRP   A CD2   1 
ATOM   3177 N  NE1   . TRP   A  1 412 ? 33.05300 -30.86000  -0.38300  1.000 90.92023  ? 404 TRP   A NE1   1 
ATOM   3178 C  CE2   . TRP   A  1 412 ? 33.81300 -31.88400  0.12000   1.000 99.51835  ? 404 TRP   A CE2   1 
ATOM   3179 C  CE3   . TRP   A  1 412 ? 33.80400 -33.35300  2.04600   1.000 96.12834  ? 404 TRP   A CE3   1 
ATOM   3180 C  CZ2   . TRP   A  1 412 ? 34.97400 -32.47300  -0.37900  1.000 97.10342  ? 404 TRP   A CZ2   1 
ATOM   3181 C  CZ3   . TRP   A  1 412 ? 34.95200 -33.93300  1.55200   1.000 101.24215 ? 404 TRP   A CZ3   1 
ATOM   3182 C  CH2   . TRP   A  1 412 ? 35.52600 -33.49800  0.35600   1.000 102.09128 ? 404 TRP   A CH2   1 
ATOM   3183 N  N     . GLN   A  1 413 ? 30.14100 -28.70300  4.02600   1.000 84.16183  ? 405 GLN   A N     1 
ATOM   3184 C  CA    . GLN   A  1 413 ? 29.81300 -27.25200  3.93400   1.000 83.93002  ? 405 GLN   A CA    1 
ATOM   3185 C  C     . GLN   A  1 413 ? 30.67700 -26.47800  4.93600   1.000 83.95787  ? 405 GLN   A C     1 
ATOM   3186 O  O     . GLN   A  1 413 ? 31.29900 -25.47800  4.53100   1.000 85.55211  ? 405 GLN   A O     1 
ATOM   3187 C  CB    . GLN   A  1 413 ? 28.32200 -27.01000  4.19200   1.000 86.46939  ? 405 GLN   A CB    1 
ATOM   3188 C  CG    . GLN   A  1 413 ? 27.85600 -25.59400  3.86300   1.000 86.73795  ? 405 GLN   A CG    1 
ATOM   3189 C  CD    . GLN   A  1 413 ? 28.04900 -24.60500  4.98900   1.000 86.65272  ? 405 GLN   A CD    1 
ATOM   3190 O  OE1   . GLN   A  1 413 ? 28.33700 -24.97000  6.12600   1.000 91.95430  ? 405 GLN   A OE1   1 
ATOM   3191 N  NE2   . GLN   A  1 413 ? 27.88100 -23.33100  4.67700   1.000 90.90101  ? 405 GLN   A NE2   1 
ATOM   3192 N  N     . PHE   A  1 414 ? 30.70100 -26.92500  6.19500   1.000 84.37352  ? 406 PHE   A N     1 
ATOM   3193 C  CA    . PHE   A  1 414 ? 31.48300 -26.30900  7.29900   1.000 88.45360  ? 406 PHE   A CA    1 
ATOM   3194 C  C     . PHE   A  1 414 ? 32.97900 -26.39900  6.98200   1.000 88.07128  ? 406 PHE   A C     1 
ATOM   3195 O  O     . PHE   A  1 414 ? 33.68000 -25.38000  7.11600   1.000 94.18384  ? 406 PHE   A O     1 
ATOM   3196 C  CB    . PHE   A  1 414 ? 31.16700 -26.98200  8.63800   1.000 86.84857  ? 406 PHE   A CB    1 
ATOM   3197 C  CG    . PHE   A  1 414 ? 32.06400 -26.55800  9.77300   1.000 89.34292  ? 406 PHE   A CG    1 
ATOM   3198 C  CD1   . PHE   A  1 414 ? 31.78600 -25.41700  10.51000  1.000 91.07901  ? 406 PHE   A CD1   1 
ATOM   3199 C  CD2   . PHE   A  1 414 ? 33.19700 -27.29200  10.09500  1.000 91.49628  ? 406 PHE   A CD2   1 
ATOM   3200 C  CE1   . PHE   A  1 414 ? 32.61600 -25.02300  11.54800  1.000 93.48937  ? 406 PHE   A CE1   1 
ATOM   3201 C  CE2   . PHE   A  1 414 ? 34.02800 -26.89500  11.13300  1.000 92.58162  ? 406 PHE   A CE2   1 
ATOM   3202 C  CZ    . PHE   A  1 414 ? 33.73500 -25.76300  11.85800  1.000 94.22852  ? 406 PHE   A CZ    1 
ATOM   3203 N  N     . GLU   A  1 415 ? 33.44600 -27.58300  6.57600   1.000 86.99054  ? 407 GLU   A N     1 
ATOM   3204 C  CA    . GLU   A  1 415 ? 34.88900 -27.89800  6.39200   1.000 88.31265  ? 407 GLU   A CA    1 
ATOM   3205 C  C     . GLU   A  1 415 ? 35.43900 -27.20400  5.13900   1.000 90.77749  ? 407 GLU   A C     1 
ATOM   3206 O  O     . GLU   A  1 415 ? 36.49500 -26.55000  5.26000   1.000 93.38071  ? 407 GLU   A O     1 
ATOM   3207 C  CB    . GLU   A  1 415 ? 35.11000 -29.40900  6.29300   1.000 87.03479  ? 407 GLU   A CB    1 
ATOM   3208 C  CG    . GLU   A  1 415 ? 35.08000 -30.12200  7.63400   1.000 87.40961  ? 407 GLU   A CG    1 
ATOM   3209 C  CD    . GLU   A  1 415 ? 35.17200 -31.63600  7.54500   1.000 96.79781  ? 407 GLU   A CD    1 
ATOM   3210 O  OE1   . GLU   A  1 415 ? 34.57500 -32.21500  6.61400   1.000 99.77763  ? 407 GLU   A OE1   1 
ATOM   3211 O  OE2   . GLU   A  1 415 ? 35.84500 -32.23600  8.40500   1.000 102.31417 ? 407 GLU   A OE2   1 
ATOM   3212 N  N     . GLU   A  1 416 ? 34.76200 -27.34200  3.99100   1.000 87.09888  ? 408 GLU   A N     1 
ATOM   3213 C  CA    . GLU   A  1 416 ? 35.34000 -27.06300  2.64500   1.000 88.77049  ? 408 GLU   A CA    1 
ATOM   3214 C  C     . GLU   A  1 416 ? 34.61900 -25.90200  1.94500   1.000 87.47013  ? 408 GLU   A C     1 
ATOM   3215 O  O     . GLU   A  1 416 ? 35.26000 -24.85200  1.76000   1.000 89.49600  ? 408 GLU   A O     1 
ATOM   3216 C  CB    . GLU   A  1 416 ? 35.28700 -28.32300  1.77900   1.000 88.16045  ? 408 GLU   A CB    1 
ATOM   3217 C  CG    . GLU   A  1 416 ? 36.00800 -29.51400  2.38800   1.000 91.00818  ? 408 GLU   A CG    1 
ATOM   3218 C  CD    . GLU   A  1 416 ? 37.50200 -29.32400  2.58100   1.000 95.93583  ? 408 GLU   A CD    1 
ATOM   3219 O  OE1   . GLU   A  1 416 ? 38.17100 -28.89600  1.62100   1.000 102.03848 ? 408 GLU   A OE1   1 
ATOM   3220 O  OE2   . GLU   A  1 416 ? 37.99300 -29.60800  3.69000   1.000 103.78010 ? 408 GLU   A OE2   1 
ATOM   3221 N  N     . TRP   A  1 417 ? 33.35600 -26.09300  1.54300   1.000 85.48589  ? 409 TRP   A N     1 
ATOM   3222 C  CA    . TRP   A  1 417 ? 32.60500 -25.17800  0.63900   1.000 85.35787  ? 409 TRP   A CA    1 
ATOM   3223 C  C     . TRP   A  1 417 ? 32.54000 -23.76600  1.22900   1.000 87.37707  ? 409 TRP   A C     1 
ATOM   3224 O  O     . TRP   A  1 417 ? 33.06500 -22.83600  0.59000   1.000 95.08887  ? 409 TRP   A O     1 
ATOM   3225 C  CB    . TRP   A  1 417 ? 31.19400 -25.70900  0.35300   1.000 86.69162  ? 409 TRP   A CB    1 
ATOM   3226 C  CG    . TRP   A  1 417 ? 31.14900 -26.93100  -0.51200  1.000 85.57097  ? 409 TRP   A CG    1 
ATOM   3227 C  CD1   . TRP   A  1 417 ? 32.01200 -27.26300  -1.51600  1.000 86.78834  ? 409 TRP   A CD1   1 
ATOM   3228 C  CD2   . TRP   A  1 417 ? 30.16000 -27.97600  -0.47400  1.000 80.68926  ? 409 TRP   A CD2   1 
ATOM   3229 N  NE1   . TRP   A  1 417 ? 31.64300 -28.45000  -2.08800  1.000 85.93773  ? 409 TRP   A NE1   1 
ATOM   3230 C  CE2   . TRP   A  1 417 ? 30.50700 -28.90800  -1.47600  1.000 84.95038  ? 409 TRP   A CE2   1 
ATOM   3231 C  CE3   . TRP   A  1 417 ? 29.02700 -28.22100  0.31100   1.000 78.14885  ? 409 TRP   A CE3   1 
ATOM   3232 C  CZ2   . TRP   A  1 417 ? 29.76500 -30.06700  -1.70300  1.000 82.99950  ? 409 TRP   A CZ2   1 
ATOM   3233 C  CZ3   . TRP   A  1 417 ? 28.29200 -29.36300  0.08200   1.000 82.07915  ? 409 TRP   A CZ3   1 
ATOM   3234 C  CH2   . TRP   A  1 417 ? 28.65900 -30.27300  -0.91100  1.000 80.15962  ? 409 TRP   A CH2   1 
ATOM   3235 N  N     . GLY   A  1 418 ? 31.90500 -23.62300  2.39400   1.000 87.39337  ? 410 GLY   A N     1 
ATOM   3236 C  CA    . GLY   A  1 418 ? 31.61800 -22.32400  3.03300   1.000 89.34644  ? 410 GLY   A CA    1 
ATOM   3237 C  C     . GLY   A  1 418 ? 30.19600 -21.87400  2.74800   1.000 91.13630  ? 410 GLY   A C     1 
ATOM   3238 O  O     . GLY   A  1 418 ? 29.35200 -22.73900  2.44100   1.000 86.29766  ? 410 GLY   A O     1 
ATOM   3239 N  N     . SER   A  1 419 ? 29.94300 -20.56500  2.82600   1.000 90.25837  ? 411 SER   A N     1 
ATOM   3240 C  CA    . SER   A  1 419 ? 28.59600 -19.94600  2.70100   1.000 89.80716  ? 411 SER   A CA    1 
ATOM   3241 C  C     . SER   A  1 419 ? 28.17500 -19.83900  1.22800   1.000 88.98514  ? 411 SER   A C     1 
ATOM   3242 O  O     . SER   A  1 419 ? 27.01900 -19.44000  0.98400   1.000 89.39456  ? 411 SER   A O     1 
ATOM   3243 C  CB    . SER   A  1 419 ? 28.55600 -18.60100  3.38000   1.000 95.11945  ? 411 SER   A CB    1 
ATOM   3244 O  OG    . SER   A  1 419 ? 29.48500 -17.70600  2.78600   1.000 94.25956  ? 411 SER   A OG    1 
ATOM   3245 N  N     . GLN   A  1 420 ? 29.06400 -20.16600  0.28300   1.000 88.85769  ? 412 GLN   A N     1 
ATOM   3246 C  CA    . GLN   A  1 420 ? 28.71800 -20.26700  -1.16200  1.000 88.37978  ? 412 GLN   A CA    1 
ATOM   3247 C  C     . GLN   A  1 420 ? 27.58100 -21.28600  -1.30900  1.000 86.76541  ? 412 GLN   A C     1 
ATOM   3248 O  O     . GLN   A  1 420 ? 26.58900 -20.96400  -1.99200  1.000 91.58693  ? 412 GLN   A O     1 
ATOM   3249 C  CB    . GLN   A  1 420 ? 29.94200 -20.64600  -2.00100  1.000 88.28499  ? 412 GLN   A CB    1 
ATOM   3250 C  CG    . GLN   A  1 420 ? 29.68600 -20.60100  -3.50300  1.000 88.38922  ? 412 GLN   A CG    1 
ATOM   3251 C  CD    . GLN   A  1 420 ? 30.95400 -20.55400  -4.32400  1.000 99.38002  ? 412 GLN   A CD    1 
ATOM   3252 O  OE1   . GLN   A  1 420 ? 32.04000 -20.88000  -3.85000  1.000 106.93843 ? 412 GLN   A OE1   1 
ATOM   3253 N  NE2   . GLN   A  1 420 ? 30.82300 -20.14300  -5.57600  1.000 89.96701  ? 412 GLN   A NE2   1 
ATOM   3254 N  N     . VAL   A  1 421 ? 27.71300 -22.44800  -0.66000  1.000 83.85186  ? 413 VAL   A N     1 
ATOM   3255 C  CA    . VAL   A  1 421 ? 26.67400 -23.52100  -0.62000  1.000 84.82796  ? 413 VAL   A CA    1 
ATOM   3256 C  C     . VAL   A  1 421 ? 25.84200 -23.35100  0.65700   1.000 82.94241  ? 413 VAL   A C     1 
ATOM   3257 O  O     . VAL   A  1 421 ? 26.41800 -23.45300  1.75900   1.000 85.11945  ? 413 VAL   A O     1 
ATOM   3258 C  CB    . VAL   A  1 421 ? 27.29900 -24.93000  -0.69100  1.000 84.41697  ? 413 VAL   A CB    1 
ATOM   3259 C  CG1   . VAL   A  1 421 ? 26.23700 -26.01200  -0.83000  1.000 77.49110  ? 413 VAL   A CG1   1 
ATOM   3260 C  CG2   . VAL   A  1 421 ? 28.31900 -25.04600  -1.81300  1.000 80.70298  ? 413 VAL   A CG2   1 
ATOM   3261 N  N     . THR   A  1 422 ? 24.54100 -23.09100  0.50400   1.000 80.96873  ? 414 THR   A N     1 
ATOM   3262 C  CA    . THR   A  1 422 ? 23.50800 -23.23200  1.56300   1.000 80.60871  ? 414 THR   A CA    1 
ATOM   3263 C  C     . THR   A  1 422 ? 22.93800 -24.65300  1.48100   1.000 81.19852  ? 414 THR   A C     1 
ATOM   3264 O  O     . THR   A  1 422 ? 22.21700 -24.93800  0.50200   1.000 81.48572  ? 414 THR   A O     1 
ATOM   3265 C  CB    . THR   A  1 422 ? 22.40400 -22.17800  1.40700   1.000 83.32169  ? 414 THR   A CB    1 
ATOM   3266 O  OG1   . THR   A  1 422 ? 23.02000 -20.89100  1.43900   1.000 91.39078  ? 414 THR   A OG1   1 
ATOM   3267 C  CG2   . THR   A  1 422 ? 21.33500 -22.27300  2.47400   1.000 81.48112  ? 414 THR   A CG2   1 
ATOM   3268 N  N     . VAL   A  1 423 ? 23.26900 -25.51700  2.44400   1.000 80.73434  ? 415 VAL   A N     1 
ATOM   3269 C  CA    . VAL   A  1 423 ? 22.72900 -26.90700  2.52200   1.000 76.11924  ? 415 VAL   A CA    1 
ATOM   3270 C  C     . VAL   A  1 423 ? 21.30300 -26.81900  3.07300   1.000 75.19228  ? 415 VAL   A C     1 
ATOM   3271 O  O     . VAL   A  1 423 ? 21.15000 -26.38400  4.22900   1.000 81.13374  ? 415 VAL   A O     1 
ATOM   3272 C  CB    . VAL   A  1 423 ? 23.61500 -27.83000  3.38200   1.000 76.11029  ? 415 VAL   A CB    1 
ATOM   3273 C  CG1   . VAL   A  1 423 ? 23.03300 -29.23200  3.48300   1.000 73.38325  ? 415 VAL   A CG1   1 
ATOM   3274 C  CG2   . VAL   A  1 423 ? 25.04200 -27.88800  2.86000   1.000 77.38378  ? 415 VAL   A CG2   1 
ATOM   3275 N  N     . VAL   A  1 424 ? 20.31000 -27.19100  2.26000   1.000 73.72771  ? 416 VAL   A N     1 
ATOM   3276 C  CA    . VAL   A  1 424 ? 18.86800 -27.22200  2.64000   1.000 73.35500  ? 416 VAL   A CA    1 
ATOM   3277 C  C     . VAL   A  1 424 ? 18.47700 -28.67800  2.90400   1.000 73.57610  ? 416 VAL   A C     1 
ATOM   3278 O  O     . VAL   A  1 424 ? 18.63800 -29.50600  1.98700   1.000 77.24771  ? 416 VAL   A O     1 
ATOM   3279 C  CB    . VAL   A  1 424 ? 17.98300 -26.58600  1.55200   1.000 73.29461  ? 416 VAL   A CB    1 
ATOM   3280 C  CG1   . VAL   A  1 424 ? 16.50000 -26.77800  1.83300   1.000 72.81495  ? 416 VAL   A CG1   1 
ATOM   3281 C  CG2   . VAL   A  1 424 ? 18.30200 -25.11200  1.36300   1.000 75.42741  ? 416 VAL   A CG2   1 
ATOM   3282 N  N     . SER   A  1 425 ? 17.98800 -28.96200  4.11400   1.000 72.00804  ? 417 SER   A N     1 
ATOM   3283 C  CA    . SER   A  1 425 ? 17.53500 -30.30000  4.57600   1.000 70.38728  ? 417 SER   A CA    1 
ATOM   3284 C  C     . SER   A  1 425 ? 16.01700 -30.40500  4.39800   1.000 72.02831  ? 417 SER   A C     1 
ATOM   3285 O  O     . SER   A  1 425 ? 15.29900 -30.39900  5.41900   1.000 78.69997  ? 417 SER   A O     1 
ATOM   3286 C  CB    . SER   A  1 425 ? 17.94600 -30.53300  6.00800   1.000 71.45555  ? 417 SER   A CB    1 
ATOM   3287 O  OG    . SER   A  1 425 ? 17.51000 -31.80400  6.46500   1.000 78.55829  ? 417 SER   A OG    1 
ATOM   3288 N  N     . SER   A  1 426 ? 15.55200 -30.49500  3.14700   1.000 69.19466  ? 418 SER   A N     1 
ATOM   3289 C  CA    . SER   A  1 426 ? 14.11400 -30.42900  2.77700   1.000 68.15077  ? 418 SER   A CA    1 
ATOM   3290 C  C     . SER   A  1 426 ? 13.81900 -31.25900  1.52200   1.000 69.23337  ? 418 SER   A C     1 
ATOM   3291 O  O     . SER   A  1 426 ? 14.76800 -31.62800  0.79500   1.000 68.64702  ? 418 SER   A O     1 
ATOM   3292 C  CB    . SER   A  1 426 ? 13.68900 -28.99500  2.58400   1.000 70.19147  ? 418 SER   A CB    1 
ATOM   3293 O  OG    . SER   A  1 426 ? 12.29900 -28.91000  2.30900   1.000 73.64712  ? 418 SER   A OG    1 
ATOM   3294 N  N     . ASP   A  1 427 ? 12.53300 -31.54100  1.29900   1.000 68.32680  ? 419 ASP   A N     1 
ATOM   3295 C  CA    . ASP   A  1 427 ? 11.97800 -32.05100  0.01800   1.000 64.52782  ? 419 ASP   A CA    1 
ATOM   3296 C  C     . ASP   A  1 427 ? 11.77800 -30.84900  -0.91400  1.000 69.67600  ? 419 ASP   A C     1 
ATOM   3297 O  O     . ASP   A  1 427 ? 11.26300 -29.81500  -0.43800  1.000 71.74098  ? 419 ASP   A O     1 
ATOM   3298 C  CB    . ASP   A  1 427 ? 10.67600 -32.82000  0.25700   1.000 63.37474  ? 419 ASP   A CB    1 
ATOM   3299 C  CG    . ASP   A  1 427 ? 10.24300 -33.69200  -0.90800  1.000 66.94381  ? 419 ASP   A CG    1 
ATOM   3300 O  OD1   . ASP   A  1 427 ? 10.45500 -33.27800  -2.06700  1.000 64.91300  ? 419 ASP   A OD1   1 
ATOM   3301 O  OD2   . ASP   A  1 427 ? 9.70000  -34.78600  -0.64800  1.000 75.16565  ? 419 ASP   A OD2   1 
ATOM   3302 N  N     . MET   A  1 428 ? 12.16500 -30.97900  -2.18600  1.000 65.67401  ? 420 MET   A N     1 
ATOM   3303 C  CA    . MET   A  1 428 ? 12.15600 -29.86500  -3.17400  1.000 65.54508  ? 420 MET   A CA    1 
ATOM   3304 C  C     . MET   A  1 428 ? 10.71300 -29.45800  -3.50700  1.000 67.90043  ? 420 MET   A C     1 
ATOM   3305 O  O     . MET   A  1 428 ? 10.51900 -28.29000  -3.89300  1.000 69.49069  ? 420 MET   A O     1 
ATOM   3306 C  CB    . MET   A  1 428 ? 12.91200 -30.24000  -4.45400  1.000 64.66152  ? 420 MET   A CB    1 
ATOM   3307 C  CG    . MET   A  1 428 ? 12.24100 -31.31800  -5.28800  1.000 63.64054  ? 420 MET   A CG    1 
ATOM   3308 S  SD    . MET   A  1 428 ? 13.22200 -31.75800  -6.74300  1.000 62.15689  ? 420 MET   A SD    1 
ATOM   3309 C  CE    . MET   A  1 428 ? 14.48700 -32.78800  -5.99900  1.000 61.21556  ? 420 MET   A CE    1 
ATOM   3310 N  N     . ARG   A  1 429 ? 9.74200  -30.36800  -3.34900  1.000 67.50405  ? 421 ARG   A N     1 
ATOM   3311 C  CA    . ARG   A  1 429 ? 8.29500  -30.08700  -3.56800  1.000 67.32607  ? 421 ARG   A CA    1 
ATOM   3312 C  C     . ARG   A  1 429 ? 7.74500  -29.22400  -2.42600  1.000 72.59230  ? 421 ARG   A C     1 
ATOM   3313 O  O     . ARG   A  1 429 ? 6.71700  -28.55800  -2.64800  1.000 78.89129  ? 421 ARG   A O     1 
ATOM   3314 C  CB    . ARG   A  1 429 ? 7.47000  -31.37500  -3.66800  1.000 68.31923  ? 421 ARG   A CB    1 
ATOM   3315 C  CG    . ARG   A  1 429 ? 7.83900  -32.27400  -4.84100  1.000 65.90830  ? 421 ARG   A CG    1 
ATOM   3316 C  CD    . ARG   A  1 429 ? 8.32600  -33.63900  -4.39600  1.000 61.56125  ? 421 ARG   A CD    1 
ATOM   3317 N  NE    . ARG   A  1 429 ? 7.24800  -34.61700  -4.32500  1.000 59.26871  ? 421 ARG   A NE    1 
ATOM   3318 C  CZ    . ARG   A  1 429 ? 7.23800  -35.69200  -3.53800  1.000 69.17921  ? 421 ARG   A CZ    1 
ATOM   3319 N  NH1   . ARG   A  1 429 ? 8.24500  -35.94300  -2.71500  1.000 69.85734  ? 421 ARG   A NH1   1 
ATOM   3320 N  NH2   . ARG   A  1 429 ? 6.20300  -36.51500  -3.56800  1.000 71.34922  ? 421 ARG   A NH2   1 
ATOM   3321 N  N     . GLU   A  1 430 ? 8.39100  -29.25000  -1.25400  1.000 71.15887  ? 422 GLU   A N     1 
ATOM   3322 C  CA    . GLU   A  1 430 ? 7.93500  -28.56000  -0.01500  1.000 74.52560  ? 422 GLU   A CA    1 
ATOM   3323 C  C     . GLU   A  1 430 ? 8.70500  -27.24900  0.18300   1.000 71.60910  ? 422 GLU   A C     1 
ATOM   3324 O  O     . GLU   A  1 430 ? 8.05300  -26.23000  0.49500   1.000 73.56746  ? 422 GLU   A O     1 
ATOM   3325 C  CB    . GLU   A  1 430 ? 8.13300  -29.46900  1.20000   1.000 80.68138  ? 422 GLU   A CB    1 
ATOM   3326 C  CG    . GLU   A  1 430 ? 7.18800  -30.65900  1.23200   1.000 83.55113  ? 422 GLU   A CG    1 
ATOM   3327 C  CD    . GLU   A  1 430 ? 5.75100  -30.34400  1.61400   1.000 98.01391  ? 422 GLU   A CD    1 
ATOM   3328 O  OE1   . GLU   A  1 430 ? 5.46400  -29.17400  1.95300   1.000 103.59063 ? 422 GLU   A OE1   1 
ATOM   3329 O  OE2   . GLU   A  1 430 ? 4.91900  -31.27600  1.57600   1.000 104.87036 ? 422 GLU   A OE2   1 
ATOM   3330 N  N     . TRP   A  1 431 ? 10.03300 -27.28500  0.02000   1.000 72.15249  ? 423 TRP   A N     1 
ATOM   3331 C  CA    . TRP   A  1 431 ? 10.97200 -26.17000  0.32900   1.000 75.28956  ? 423 TRP   A CA    1 
ATOM   3332 C  C     . TRP   A  1 431 ? 10.42600 -24.84200  -0.20800  1.000 74.55853  ? 423 TRP   A C     1 
ATOM   3333 O  O     . TRP   A  1 431 ? 10.27600 -24.71900  -1.43700  1.000 81.86583  ? 423 TRP   A O     1 
ATOM   3334 C  CB    . TRP   A  1 431 ? 12.37000 -26.46000  -0.23400  1.000 73.74679  ? 423 TRP   A CB    1 
ATOM   3335 C  CG    . TRP   A  1 431 ? 13.39200 -25.42400  0.12000   1.000 73.55349  ? 423 TRP   A CG    1 
ATOM   3336 C  CD1   . TRP   A  1 431 ? 13.62900 -24.89600  1.35500   1.000 75.22371  ? 423 TRP   A CD1   1 
ATOM   3337 C  CD2   . TRP   A  1 431 ? 14.33400 -24.79600  -0.76900  1.000 75.07187  ? 423 TRP   A CD2   1 
ATOM   3338 N  NE1   . TRP   A  1 431 ? 14.64300 -23.97900  1.29500   1.000 78.93808  ? 423 TRP   A NE1   1 
ATOM   3339 C  CE2   . TRP   A  1 431 ? 15.09600 -23.89600  0.00600   1.000 76.01917  ? 423 TRP   A CE2   1 
ATOM   3340 C  CE3   . TRP   A  1 431 ? 14.60600 -24.90100  -2.13700  1.000 82.55889  ? 423 TRP   A CE3   1 
ATOM   3341 C  CZ2   . TRP   A  1 431 ? 16.10600 -23.10800  -0.54500  1.000 80.89883  ? 423 TRP   A CZ2   1 
ATOM   3342 C  CZ3   . TRP   A  1 431 ? 15.60600 -24.12400  -2.68100  1.000 84.28407  ? 423 TRP   A CZ3   1 
ATOM   3343 C  CH2   . TRP   A  1 431 ? 16.34600 -23.24000  -1.89300  1.000 84.18122  ? 423 TRP   A CH2   1 
ATOM   3344 N  N     . VAL   A  1 432 ? 10.14700 -23.89400  0.69200   1.000 79.98944  ? 424 VAL   A N     1 
ATOM   3345 C  CA    . VAL   A  1 432 ? 9.81500  -22.47500  0.36000   1.000 83.53819  ? 424 VAL   A CA    1 
ATOM   3346 C  C     . VAL   A  1 432 ? 11.14100 -21.70800  0.28100   1.000 80.05031  ? 424 VAL   A C     1 
ATOM   3347 O  O     . VAL   A  1 432 ? 11.76700 -21.50600  1.33500   1.000 80.84916  ? 424 VAL   A O     1 
ATOM   3348 C  CB    . VAL   A  1 432 ? 8.84600  -21.85400  1.38700   1.000 80.95008  ? 424 VAL   A CB    1 
ATOM   3349 C  CG1   . VAL   A  1 432 ? 8.35100  -20.48900  0.93600   1.000 83.39012  ? 424 VAL   A CG1   1 
ATOM   3350 C  CG2   . VAL   A  1 432 ? 7.66600  -22.76900  1.68500   1.000 79.90796  ? 424 VAL   A CG2   1 
ATOM   3351 N  N     . ALA   A  1 433 ? 11.55900 -21.32800  -0.93000  1.000 87.55830  ? 425 ALA   A N     1 
ATOM   3352 C  CA    . ALA   A  1 433 ? 12.91400 -20.81200  -1.23700  1.000 89.13459  ? 425 ALA   A CA    1 
ATOM   3353 C  C     . ALA   A  1 433 ? 13.01000 -19.32900  -0.88600  1.000 96.03036  ? 425 ALA   A C     1 
ATOM   3354 O  O     . ALA   A  1 433 ? 12.01300 -18.61100  -0.92800  1.000 99.80329  ? 425 ALA   A O     1 
ATOM   3355 C  CB    . ALA   A  1 433 ? 13.23800 -21.05300  -2.69200  1.000 87.29537  ? 425 ALA   A CB    1 
ATOM   3356 N  N     . PRO   A  1 434 ? 14.21400 -18.82700  -0.52800  1.000 88.88668  ? 426 PRO   A N     1 
ATOM   3357 C  CA    . PRO   A  1 434 ? 14.41300 -17.39800  -0.28600  1.000 87.53911  ? 426 PRO   A CA    1 
ATOM   3358 C  C     . PRO   A  1 434 ? 14.34500 -16.57800  -1.58300  1.000 89.40506  ? 426 PRO   A C     1 
ATOM   3359 O  O     . PRO   A  1 434 ? 13.76300 -15.50900  -1.56400  1.000 97.80220  ? 426 PRO   A O     1 
ATOM   3360 C  CB    . PRO   A  1 434 ? 15.81600 -17.32700  0.33500   1.000 90.38002  ? 426 PRO   A CB    1 
ATOM   3361 C  CG    . PRO   A  1 434 ? 16.52600 -18.55600  -0.19700  1.000 91.32928  ? 426 PRO   A CG    1 
ATOM   3362 C  CD    . PRO   A  1 434 ? 15.44600 -19.60900  -0.32800  1.000 85.25719  ? 426 PRO   A CD    1 
ATOM   3363 N  N     . GLU   A  1 435 ? 14.92900 -17.11000  -2.66300  1.000 90.22770  ? 427 GLU   A N     1 
ATOM   3364 C  CA    . GLU   A  1 435 ? 15.03700 -16.46300  -4.00000  1.000 88.46455  ? 427 GLU   A CA    1 
ATOM   3365 C  C     . GLU   A  1 435 ? 14.79300 -17.51900  -5.08400  1.000 92.18922  ? 427 GLU   A C     1 
ATOM   3366 O  O     . GLU   A  1 435 ? 15.00100 -18.71700  -4.79900  1.000 83.86243  ? 427 GLU   A O     1 
ATOM   3367 C  CB    . GLU   A  1 435 ? 16.41400 -15.81300  -4.16500  1.000 89.84352  ? 427 GLU   A CB    1 
ATOM   3368 C  CG    . GLU   A  1 435 ? 17.56800 -16.71900  -3.76900  1.000 88.18674  ? 427 GLU   A CG    1 
ATOM   3369 C  CD    . GLU   A  1 435 ? 18.95400 -16.11500  -3.91000  1.000 89.65454  ? 427 GLU   A CD    1 
ATOM   3370 O  OE1   . GLU   A  1 435 ? 19.05000 -14.92400  -4.26100  1.000 103.39747 ? 427 GLU   A OE1   1 
ATOM   3371 O  OE2   . GLU   A  1 435 ? 19.93700 -16.84000  -3.66300  1.000 88.50930  ? 427 GLU   A OE2   1 
ATOM   3372 N  N     . LYS   A  1 436 ? 14.37000 -17.08800  -6.27600  1.000 89.52270  ? 428 LYS   A N     1 
ATOM   3373 C  CA    . LYS   A  1 436 ? 14.15100 -17.97500  -7.45000  1.000 85.24906  ? 428 LYS   A CA    1 
ATOM   3374 C  C     . LYS   A  1 436 ? 15.51700 -18.34400  -8.04100  1.000 84.61772  ? 428 LYS   A C     1 
ATOM   3375 O  O     . LYS   A  1 436 ? 16.48500 -17.60900  -7.77600  1.000 86.17689  ? 428 LYS   A O     1 
ATOM   3376 C  CB    . LYS   A  1 436 ? 13.21500 -17.30000  -8.45900  1.000 87.72728  ? 428 LYS   A CB    1 
ATOM   3377 C  CG    . LYS   A  1 436 ? 11.84100 -16.94800  -7.90100  1.000 87.58127  ? 428 LYS   A CG    1 
ATOM   3378 C  CD    . LYS   A  1 436 ? 10.77400 -16.72000  -8.95000  1.000 88.37601  ? 428 LYS   A CD    1 
ATOM   3379 C  CE    . LYS   A  1 436 ? 9.37600  -16.76900  -8.37100  1.000 88.55531  ? 428 LYS   A CE    1 
ATOM   3380 N  NZ    . LYS   A  1 436 ? 8.38700  -16.11100  -9.25600  1.000 94.93105  ? 428 LYS   A NZ    1 
ATOM   3381 N  N     . ALA   A  1 437 ? 15.58800 -19.45200  -8.78700  1.000 82.52949  ? 429 ALA   A N     1 
ATOM   3382 C  CA    . ALA   A  1 437 ? 16.83900 -20.06800  -9.29200  1.000 82.67311  ? 429 ALA   A CA    1 
ATOM   3383 C  C     . ALA   A  1 437 ? 17.07500 -19.69000  -10.75900 1.000 88.03413  ? 429 ALA   A C     1 
ATOM   3384 O  O     . ALA   A  1 437 ? 16.08900 -19.61600  -11.51800 1.000 89.90946  ? 429 ALA   A O     1 
ATOM   3385 C  CB    . ALA   A  1 437 ? 16.76600 -21.56500  -9.13600  1.000 78.79997  ? 429 ALA   A CB    1 
ATOM   3386 N  N     . ASP   A  1 438 ? 18.34400 -19.49300  -11.13600 1.000 85.62609  ? 430 ASP   A N     1 
ATOM   3387 C  CA    . ASP   A  1 438 ? 18.79000 -19.27200  -12.53800 1.000 85.81536  ? 430 ASP   A CA    1 
ATOM   3388 C  C     . ASP   A  1 438 ? 18.87500 -20.62800  -13.24300 1.000 82.59364  ? 430 ASP   A C     1 
ATOM   3389 O  O     . ASP   A  1 438 ? 18.37800 -20.73200  -14.38200 1.000 83.50443  ? 430 ASP   A O     1 
ATOM   3390 C  CB    . ASP   A  1 438 ? 20.13900 -18.55300  -12.60000 1.000 87.87978  ? 430 ASP   A CB    1 
ATOM   3391 C  CG    . ASP   A  1 438 ? 20.04600 -17.05100  -12.40400 1.000 91.77768  ? 430 ASP   A CG    1 
ATOM   3392 O  OD1   . ASP   A  1 438 ? 19.42300 -16.38700  -13.25900 1.000 90.95554  ? 430 ASP   A OD1   1 
ATOM   3393 O  OD2   . ASP   A  1 438 ? 20.59800 -16.56000  -11.40000 1.000 90.94688  ? 430 ASP   A OD2   1 
ATOM   3394 N  N     . ILE   A  1 439 ? 19.50100 -21.61000  -12.58000 1.000 85.47910  ? 431 ILE   A N     1 
ATOM   3395 C  CA    . ILE   A  1 439 ? 19.61300 -23.03100  -13.03000 1.000 78.15231  ? 431 ILE   A CA    1 
ATOM   3396 C  C     . ILE   A  1 439 ? 19.20500 -23.94500  -11.86800 1.000 76.00629  ? 431 ILE   A C     1 
ATOM   3397 O  O     . ILE   A  1 439 ? 19.79300 -23.80200  -10.78000 1.000 77.83109  ? 431 ILE   A O     1 
ATOM   3398 C  CB    . ILE   A  1 439 ? 21.04300 -23.35900  -13.51300 1.000 80.19049  ? 431 ILE   A CB    1 
ATOM   3399 C  CG1   . ILE   A  1 439 ? 21.59600 -22.30200  -14.47400 1.000 84.50995  ? 431 ILE   A CG1   1 
ATOM   3400 C  CG2   . ILE   A  1 439 ? 21.09400 -24.75400  -14.12300 1.000 76.42620  ? 431 ILE   A CG2   1 
ATOM   3401 C  CD1   . ILE   A  1 439 ? 23.08500 -22.41400  -14.72800 1.000 82.15821  ? 431 ILE   A CD1   1 
ATOM   3402 N  N     . ILE   A  1 440 ? 18.24400 -24.84700  -12.09700 1.000 80.40200  ? 432 ILE   A N     1 
ATOM   3403 C  CA    . ILE   A  1 440 ? 17.97100 -26.02100  -11.21200 1.000 75.55703  ? 432 ILE   A CA    1 
ATOM   3404 C  C     . ILE   A  1 440 ? 18.68700 -27.23000  -11.82400 1.000 70.47372  ? 432 ILE   A C     1 
ATOM   3405 O  O     . ILE   A  1 440 ? 18.36800 -27.58500  -12.96900 1.000 71.78786  ? 432 ILE   A O     1 
ATOM   3406 C  CB    . ILE   A  1 440 ? 16.46000 -26.26900  -10.99200 1.000 74.64663  ? 432 ILE   A CB    1 
ATOM   3407 C  CG1   . ILE   A  1 440 ? 15.66100 -26.34400  -12.29900 1.000 70.94082  ? 432 ILE   A CG1   1 
ATOM   3408 C  CG2   . ILE   A  1 440 ? 15.89400 -25.22300  -10.04000 1.000 72.36866  ? 432 ILE   A CG2   1 
ATOM   3409 C  CD1   . ILE   A  1 440 ? 14.24000 -26.84400  -12.13600 1.000 69.78285  ? 432 ILE   A CD1   1 
ATOM   3410 N  N     . VAL   A  1 441 ? 19.65400 -27.79800  -11.10100 1.000 69.91226  ? 433 VAL   A N     1 
ATOM   3411 C  CA    . VAL   A  1 441 ? 20.47100 -28.96800  -11.54400 1.000 70.78068  ? 433 VAL   A CA    1 
ATOM   3412 C  C     . VAL   A  1 441 ? 20.04000 -30.19100  -10.72500 1.000 69.05181  ? 433 VAL   A C     1 
ATOM   3413 O  O     . VAL   A  1 441 ? 20.06800 -30.10500  -9.48300  1.000 68.80030  ? 433 VAL   A O     1 
ATOM   3414 C  CB    . VAL   A  1 441 ? 21.97700 -28.67400  -11.40300 1.000 70.07227  ? 433 VAL   A CB    1 
ATOM   3415 C  CG1   . VAL   A  1 441 ? 22.83400 -29.84100  -11.86900 1.000 69.18781  ? 433 VAL   A CG1   1 
ATOM   3416 C  CG2   . VAL   A  1 441 ? 22.36900 -27.40600  -12.14400 1.000 72.34947  ? 433 VAL   A CG2   1 
ATOM   3417 N  N     . SER   A  1 442 ? 19.64800 -31.28000  -11.39500 1.000 68.51038  ? 434 SER   A N     1 
ATOM   3418 C  CA    . SER   A  1 442 ? 19.08000 -32.50300  -10.76600 1.000 63.16616  ? 434 SER   A CA    1 
ATOM   3419 C  C     . SER   A  1 442 ? 19.69200 -33.76800  -11.37900 1.000 62.69597  ? 434 SER   A C     1 
ATOM   3420 O  O     . SER   A  1 442 ? 20.33700 -33.66800  -12.43900 1.000 68.50187  ? 434 SER   A O     1 
ATOM   3421 C  CB    . SER   A  1 442 ? 17.58100 -32.50900  -10.87500 1.000 62.43009  ? 434 SER   A CB    1 
ATOM   3422 O  OG    . SER   A  1 442 ? 17.17300 -32.41400  -12.22900 1.000 72.69997  ? 434 SER   A OG    1 
ATOM   3423 N  N     . GLU   A  1 443 ? 19.45100 -34.91100  -10.73000 1.000 65.04829  ? 435 GLU   A N     1 
ATOM   3424 C  CA    . GLU   A  1 443 ? 20.15800 -36.20600  -10.92400 1.000 59.62831  ? 435 GLU   A CA    1 
ATOM   3425 C  C     . GLU   A  1 443 ? 19.18000 -37.35900  -10.64800 1.000 61.07017  ? 435 GLU   A C     1 
ATOM   3426 O  O     . GLU   A  1 443 ? 19.63700 -38.43600  -10.21100 1.000 59.72599  ? 435 GLU   A O     1 
ATOM   3427 C  CB    . GLU   A  1 443 ? 21.33700 -36.23600  -9.94700  1.000 67.84171  ? 435 GLU   A CB    1 
ATOM   3428 C  CG    . GLU   A  1 443 ? 22.48600 -37.14300  -10.34200 1.000 66.11961  ? 435 GLU   A CG    1 
ATOM   3429 C  CD    . GLU   A  1 443 ? 23.67900 -37.04700  -9.40300  1.000 68.77757  ? 435 GLU   A CD    1 
ATOM   3430 O  OE1   . GLU   A  1 443 ? 23.61700 -36.25900  -8.43600  1.000 66.09023  ? 435 GLU   A OE1   1 
ATOM   3431 O  OE2   . GLU   A  1 443 ? 24.67300 -37.75000  -9.64800  1.000 71.30969  ? 435 GLU   A OE2   1 
ATOM   3432 N  N     . LEU   A  1 444 ? 17.88500 -37.14200  -10.90500 1.000 59.42686  ? 436 LEU   A N     1 
ATOM   3433 C  CA    . LEU   A  1 444 ? 16.76500 -37.96900  -10.37600 1.000 55.87922  ? 436 LEU   A CA    1 
ATOM   3434 C  C     . LEU   A  1 444 ? 16.33500 -39.02200  -11.40300 1.000 54.70337  ? 436 LEU   A C     1 
ATOM   3435 O  O     . LEU   A  1 444 ? 15.24400 -39.59600  -11.22500 1.000 59.22065  ? 436 LEU   A O     1 
ATOM   3436 C  CB    . LEU   A  1 444 ? 15.58500 -37.05400  -10.03300 1.000 56.28828  ? 436 LEU   A CB    1 
ATOM   3437 C  CG    . LEU   A  1 444 ? 15.92200 -35.78900  -9.24500  1.000 60.13424  ? 436 LEU   A CG    1 
ATOM   3438 C  CD1   . LEU   A  1 444 ? 14.68600 -34.91900  -9.07300  1.000 60.84865  ? 436 LEU   A CD1   1 
ATOM   3439 C  CD2   . LEU   A  1 444 ? 16.53100 -36.12800  -7.89300  1.000 62.13159  ? 436 LEU   A CD2   1 
ATOM   3440 N  N     . LEU   A  1 445 ? 17.14200 -39.26200  -12.43900 1.000 58.23837  ? 437 LEU   A N     1 
ATOM   3441 C  CA    . LEU   A  1 445 ? 16.80300 -40.21200  -13.53100 1.000 56.42892  ? 437 LEU   A CA    1 
ATOM   3442 C  C     . LEU   A  1 445 ? 17.09500 -41.64000  -13.06700 1.000 52.96970  ? 437 LEU   A C     1 
ATOM   3443 O  O     . LEU   A  1 445 ? 18.03800 -41.82200  -12.27500 1.000 56.88749  ? 437 LEU   A O     1 
ATOM   3444 C  CB    . LEU   A  1 445 ? 17.61500 -39.88000  -14.78600 1.000 59.55057  ? 437 LEU   A CB    1 
ATOM   3445 C  CG    . LEU   A  1 445 ? 17.40200 -38.48700  -15.37600 1.000 59.79535  ? 437 LEU   A CG    1 
ATOM   3446 C  CD1   . LEU   A  1 445 ? 17.85900 -38.45600  -16.82700 1.000 57.42493  ? 437 LEU   A CD1   1 
ATOM   3447 C  CD2   . LEU   A  1 445 ? 15.94900 -38.04800  -15.26800 1.000 57.51099  ? 437 LEU   A CD2   1 
ATOM   3448 N  N     . GLY   A  1 446 ? 16.29700 -42.59600  -13.54600 1.000 53.36243  ? 438 GLY   A N     1 
ATOM   3449 C  CA    . GLY   A  1 446 ? 16.52100 -44.04300  -13.37100 1.000 55.70374  ? 438 GLY   A CA    1 
ATOM   3450 C  C     . GLY   A  1 446 ? 16.84900 -44.71000  -14.69600 1.000 57.34125  ? 438 GLY   A C     1 
ATOM   3451 O  O     . GLY   A  1 446 ? 17.10600 -43.98400  -15.67800 1.000 52.11021  ? 438 GLY   A O     1 
ATOM   3452 N  N     . SER   A  1 447 ? 16.83700 -46.04500  -14.72100 1.000 54.18917  ? 439 SER   A N     1 
ATOM   3453 C  CA    . SER   A  1 447 ? 17.15700 -46.88300  -15.90600 1.000 54.16813  ? 439 SER   A CA    1 
ATOM   3454 C  C     . SER   A  1 447 ? 16.13300 -46.63900  -17.02100 1.000 51.63671  ? 439 SER   A C     1 
ATOM   3455 O  O     . SER   A  1 447 ? 16.50400 -46.78400  -18.19600 1.000 50.30170  ? 439 SER   A O     1 
ATOM   3456 C  CB    . SER   A  1 447 ? 17.22800 -48.33500  -15.52400 1.000 53.52825  ? 439 SER   A CB    1 
ATOM   3457 O  OG    . SER   A  1 447 ? 18.29100 -48.55500  -14.60800 1.000 58.62549  ? 439 SER   A OG    1 
ATOM   3458 N  N     . PHE   A  1 448 ? 14.90000 -46.26500  -16.66300 1.000 51.06554  ? 440 PHE   A N     1 
ATOM   3459 C  CA    . PHE   A  1 448 ? 13.77500 -46.02200  -17.60400 1.000 51.40293  ? 440 PHE   A CA    1 
ATOM   3460 C  C     . PHE   A  1 448 ? 13.41000 -44.53200  -17.61200 1.000 51.84768  ? 440 PHE   A C     1 
ATOM   3461 O  O     . PHE   A  1 448 ? 12.21800 -44.20600  -17.78700 1.000 51.17714  ? 440 PHE   A O     1 
ATOM   3462 C  CB    . PHE   A  1 448 ? 12.58900 -46.90600  -17.21200 1.000 49.77518  ? 440 PHE   A CB    1 
ATOM   3463 C  CG    . PHE   A  1 448 ? 11.61200 -47.18600  -18.32500 1.000 51.87883  ? 440 PHE   A CG    1 
ATOM   3464 C  CD1   . PHE   A  1 448 ? 12.03600 -47.76000  -19.51200 1.000 51.00523  ? 440 PHE   A CD1   1 
ATOM   3465 C  CD2   . PHE   A  1 448 ? 10.26500 -46.89400  -18.17700 1.000 51.55133  ? 440 PHE   A CD2   1 
ATOM   3466 C  CE1   . PHE   A  1 448 ? 11.13500 -48.02300  -20.53200 1.000 53.47204  ? 440 PHE   A CE1   1 
ATOM   3467 C  CE2   . PHE   A  1 448 ? 9.36500  -47.16100  -19.19600 1.000 52.69076  ? 440 PHE   A CE2   1 
ATOM   3468 C  CZ    . PHE   A  1 448 ? 9.80100  -47.72400  -20.37200 1.000 51.71044  ? 440 PHE   A CZ    1 
ATOM   3469 N  N     . ALA   A  1 449 ? 14.41500 -43.66200  -17.44900 1.000 55.49140  ? 441 ALA   A N     1 
ATOM   3470 C  CA    . ALA   A  1 449 ? 14.30000 -42.18400  -17.39000 1.000 57.28229  ? 441 ALA   A CA    1 
ATOM   3471 C  C     . ALA   A  1 449 ? 13.52300 -41.76100  -16.14000 1.000 53.57669  ? 441 ALA   A C     1 
ATOM   3472 O  O     . ALA   A  1 449 ? 14.16700 -41.30700  -15.18000 1.000 58.77353  ? 441 ALA   A O     1 
ATOM   3473 C  CB    . ALA   A  1 449 ? 13.65200 -41.64300  -18.64400 1.000 55.91481  ? 441 ALA   A CB    1 
ATOM   3474 N  N     . ASP   A  1 450 ? 12.19800 -41.94200  -16.14900 1.000 53.95005  ? 442 ASP   A N     1 
ATOM   3475 C  CA    . ASP   A  1 450 ? 11.24600 -41.29600  -15.20300 1.000 55.54785  ? 442 ASP   A CA    1 
ATOM   3476 C  C     . ASP   A  1 450 ? 10.83800 -42.24400  -14.06100 1.000 55.15873  ? 442 ASP   A C     1 
ATOM   3477 O  O     . ASP   A  1 450 ? 9.96300  -41.83900  -13.26600 1.000 55.04553  ? 442 ASP   A O     1 
ATOM   3478 C  CB    . ASP   A  1 450 ? 10.01100 -40.79700  -15.95900 1.000 54.16926  ? 442 ASP   A CB    1 
ATOM   3479 C  CG    . ASP   A  1 450 ? 9.26900  -41.89500  -16.69900 1.000 55.26442  ? 442 ASP   A CG    1 
ATOM   3480 O  OD1   . ASP   A  1 450 ? 9.72700  -42.27700  -17.79800 1.000 60.70187  ? 442 ASP   A OD1   1 
ATOM   3481 O  OD2   . ASP   A  1 450 ? 8.25500  -42.37700  -16.15800 1.000 50.06376  ? 442 ASP   A OD2   1 
ATOM   3482 N  N     . ASN   A  1 451 ? 11.44700 -43.43300  -13.95100 1.000 53.06418  ? 443 ASN   A N     1 
ATOM   3483 C  CA    . ASN   A  1 451 ? 11.00800 -44.50100  -13.00700 1.000 53.29618  ? 443 ASN   A CA    1 
ATOM   3484 C  C     . ASN   A  1 451 ? 11.39900 -44.14500  -11.56500 1.000 51.08199  ? 443 ASN   A C     1 
ATOM   3485 O  O     . ASN   A  1 451 ? 10.80400 -44.73100  -10.64600 1.000 56.68878  ? 443 ASN   A O     1 
ATOM   3486 C  CB    . ASN   A  1 451 ? 11.51700 -45.89100  -13.41000 1.000 49.38571  ? 443 ASN   A CB    1 
ATOM   3487 C  CG    . ASN   A  1 451 ? 13.02500 -45.99600  -13.49100 1.000 54.04424  ? 443 ASN   A CG    1 
ATOM   3488 O  OD1   . ASN   A  1 451 ? 13.66500 -45.22800  -14.20700 1.000 54.25218  ? 443 ASN   A OD1   1 
ATOM   3489 N  ND2   . ASN   A  1 451 ? 13.59600 -46.96600  -12.79300 1.000 54.94165  ? 443 ASN   A ND2   1 
ATOM   3490 N  N     . GLU   A  1 452 ? 12.34500 -43.22200  -11.36500 1.000 54.92920  ? 444 GLU   A N     1 
ATOM   3491 C  CA    . GLU   A  1 452 ? 12.71300 -42.67700  -10.02600 1.000 53.60749  ? 444 GLU   A CA    1 
ATOM   3492 C  C     . GLU   A  1 452 ? 11.97000 -41.35700  -9.77600  1.000 54.86608  ? 444 GLU   A C     1 
ATOM   3493 O  O     . GLU   A  1 452 ? 12.33300 -40.66600  -8.81300  1.000 58.18248  ? 444 GLU   A O     1 
ATOM   3494 C  CB    . GLU   A  1 452 ? 14.23000 -42.50900  -9.91000  1.000 50.77235  ? 444 GLU   A CB    1 
ATOM   3495 C  CG    . GLU   A  1 452 ? 14.96600 -43.83100  -9.80100  1.000 53.40050  ? 444 GLU   A CG    1 
ATOM   3496 C  CD    . GLU   A  1 452 ? 16.47100 -43.73200  -9.62100  1.000 56.69534  ? 444 GLU   A CD    1 
ATOM   3497 O  OE1   . GLU   A  1 452 ? 16.97600 -42.61700  -9.37700  1.000 54.92114  ? 444 GLU   A OE1   1 
ATOM   3498 O  OE2   . GLU   A  1 452 ? 17.13500 -44.77700  -9.73400  1.000 61.85232  ? 444 GLU   A OE2   1 
ATOM   3499 N  N     . LEU   A  1 453 ? 10.97300 -41.03100  -10.60900 1.000 54.65592  ? 445 LEU   A N     1 
ATOM   3500 C  CA    . LEU   A  1 453 ? 9.97400  -39.94200  -10.40700 1.000 56.16358  ? 445 LEU   A CA    1 
ATOM   3501 C  C     . LEU   A  1 453 ? 10.64000 -38.55700  -10.45300 1.000 58.04560  ? 445 LEU   A C     1 
ATOM   3502 O  O     . LEU   A  1 453 ? 10.25600 -37.68500  -9.64900  1.000 58.52102  ? 445 LEU   A O     1 
ATOM   3503 C  CB    . LEU   A  1 453 ? 9.23500  -40.18700  -9.08500  1.000 55.83594  ? 445 LEU   A CB    1 
ATOM   3504 C  CG    . LEU   A  1 453 ? 7.99800  -41.08000  -9.17300  1.000 59.10460  ? 445 LEU   A CG    1 
ATOM   3505 C  CD1   . LEU   A  1 453 ? 8.21900  -42.26600  -10.10200 1.000 53.99375  ? 445 LEU   A CD1   1 
ATOM   3506 C  CD2   . LEU   A  1 453 ? 7.58800  -41.56000  -7.79000  1.000 54.91890  ? 445 LEU   A CD2   1 
ATOM   3507 N  N     . SER   A  1 454 ? 11.54900 -38.34100  -11.40900 1.000 59.18611  ? 446 SER   A N     1 
ATOM   3508 C  CA    . SER   A  1 454 ? 12.15100 -37.01600  -11.72100 1.000 58.86924  ? 446 SER   A CA    1 
ATOM   3509 C  C     . SER   A  1 454 ? 11.06200 -36.01500  -12.10700 1.000 60.45331  ? 446 SER   A C     1 
ATOM   3510 O  O     . SER   A  1 454 ? 11.08800 -34.88200  -11.63500 1.000 64.17936  ? 446 SER   A O     1 
ATOM   3511 C  CB    . SER   A  1 454 ? 13.20400 -37.11600  -12.79800 1.000 61.01196  ? 446 SER   A CB    1 
ATOM   3512 O  OG    . SER   A  1 454 ? 13.86500 -35.86900  -12.97000 1.000 59.15751  ? 446 SER   A OG    1 
ATOM   3513 N  N     . PRO   A  1 455 ? 10.07900 -36.37800  -12.96800 1.000 59.78900  ? 447 PRO   A N     1 
ATOM   3514 C  CA    . PRO   A  1 455 ? 9.01200  -35.45200  -13.35600 1.000 62.92465  ? 447 PRO   A CA    1 
ATOM   3515 C  C     . PRO   A  1 455 ? 8.25700  -34.81600  -12.17700 1.000 65.50034  ? 447 PRO   A C     1 
ATOM   3516 O  O     . PRO   A  1 455 ? 8.15600  -33.60100  -12.14900 1.000 64.12215  ? 447 PRO   A O     1 
ATOM   3517 C  CB    . PRO   A  1 455 ? 8.05400  -36.33000  -14.17900 1.000 60.73762  ? 447 PRO   A CB    1 
ATOM   3518 C  CG    . PRO   A  1 455 ? 8.95000  -37.40400  -14.75000 1.000 59.33317  ? 447 PRO   A CG    1 
ATOM   3519 C  CD    . PRO   A  1 455 ? 9.95200  -37.67800  -13.64900 1.000 58.14364  ? 447 PRO   A CD    1 
ATOM   3520 N  N     . GLU   A  1 456 ? 7.75400  -35.64100  -11.24900 1.000 63.29600  ? 448 GLU   A N     1 
ATOM   3521 C  CA    . GLU   A  1 456 ? 6.92400  -35.20600  -10.08900 1.000 63.43994  ? 448 GLU   A CA    1 
ATOM   3522 C  C     . GLU   A  1 456 ? 7.74800  -34.28700  -9.17800  1.000 62.20092  ? 448 GLU   A C     1 
ATOM   3523 O  O     . GLU   A  1 456 ? 7.20100  -33.25800  -8.72500  1.000 59.98943  ? 448 GLU   A O     1 
ATOM   3524 C  CB    . GLU   A  1 456 ? 6.40100  -36.41100  -9.30100  1.000 57.96991  ? 448 GLU   A CB    1 
ATOM   3525 C  CG    . GLU   A  1 456 ? 5.20200  -37.09100  -9.94200  1.000 60.23519  ? 448 GLU   A CG    1 
ATOM   3526 C  CD    . GLU   A  1 456 ? 5.51500  -38.05100  -11.07900 1.000 60.61209  ? 448 GLU   A CD    1 
ATOM   3527 O  OE1   . GLU   A  1 456 ? 6.70800  -38.35200  -11.29000 1.000 62.13591  ? 448 GLU   A OE1   1 
ATOM   3528 O  OE2   . GLU   A  1 456 ? 4.56300  -38.49900  -11.75100 1.000 56.72915  ? 448 GLU   A OE2   1 
ATOM   3529 N  N     . CYS   A  1 457 ? 9.01000  -34.64900  -8.92700  1.000 58.28709  ? 449 CYS   A N     1 
ATOM   3530 C  CA    . CYS   A  1 457 ? 9.94600  -33.92000  -8.03000  1.000 59.24963  ? 449 CYS   A CA    1 
ATOM   3531 C  C     . CYS   A  1 457 ? 10.19900 -32.51200  -8.57700  1.000 62.67163  ? 449 CYS   A C     1 
ATOM   3532 O  O     . CYS   A  1 457 ? 10.00400 -31.54700  -7.81700  1.000 68.30855  ? 449 CYS   A O     1 
ATOM   3533 C  CB    . CYS   A  1 457 ? 11.25900 -34.67600  -7.87000  1.000 60.62156  ? 449 CYS   A CB    1 
ATOM   3534 S  SG    . CYS   A  1 457 ? 11.10200 -36.18000  -6.87100  1.000 64.80529  ? 449 CYS   A SG    1 
ATOM   3535 N  N     . LEU   A  1 458 ? 10.60100 -32.40600  -9.84800  1.000 66.17241  ? 450 LEU   A N     1 
ATOM   3536 C  CA    . LEU   A  1 458 ? 10.97300 -31.12300  -10.50500 1.000 64.28868  ? 450 LEU   A CA    1 
ATOM   3537 C  C     . LEU   A  1 458 ? 9.72600  -30.25400  -10.71700 1.000 70.12695  ? 450 LEU   A C     1 
ATOM   3538 O  O     . LEU   A  1 458 ? 9.85700  -29.02200  -10.59800 1.000 70.61846  ? 450 LEU   A O     1 
ATOM   3539 C  CB    . LEU   A  1 458 ? 11.68700 -31.41600  -11.82900 1.000 63.11399  ? 450 LEU   A CB    1 
ATOM   3540 C  CG    . LEU   A  1 458 ? 13.03000 -32.13700  -11.70500 1.000 61.59758  ? 450 LEU   A CG    1 
ATOM   3541 C  CD1   . LEU   A  1 458 ? 13.59000 -32.48600  -13.07500 1.000 61.49687  ? 450 LEU   A CD1   1 
ATOM   3542 C  CD2   . LEU   A  1 458 ? 14.03200 -31.30300  -10.92200 1.000 62.98387  ? 450 LEU   A CD2   1 
ATOM   3543 N  N     . ASP   A  1 459 ? 8.57000  -30.86500  -11.00800 1.000 68.64951  ? 451 ASP   A N     1 
ATOM   3544 C  CA    . ASP   A  1 459 ? 7.25400  -30.17200  -11.11400 1.000 69.19397  ? 451 ASP   A CA    1 
ATOM   3545 C  C     . ASP   A  1 459 ? 6.97700  -29.40000  -9.81700  1.000 69.59241  ? 451 ASP   A C     1 
ATOM   3546 O  O     . ASP   A  1 459 ? 6.57900  -28.22200  -9.90500  1.000 73.88375  ? 451 ASP   A O     1 
ATOM   3547 C  CB    . ASP   A  1 459 ? 6.10900  -31.15100  -11.39400 1.000 68.81970  ? 451 ASP   A CB    1 
ATOM   3548 C  CG    . ASP   A  1 459 ? 5.91300  -31.49500  -12.86100 1.000 71.42690  ? 451 ASP   A CG    1 
ATOM   3549 O  OD1   . ASP   A  1 459 ? 6.82000  -31.19600  -13.66600 1.000 79.07247  ? 451 ASP   A OD1   1 
ATOM   3550 O  OD2   . ASP   A  1 459 ? 4.84900  -32.06000  -13.18500 1.000 71.61832  ? 451 ASP   A OD2   1 
ATOM   3551 N  N     . GLY   A  1 460 ? 7.18500  -30.04800  -8.66500  1.000 68.55162  ? 452 GLY   A N     1 
ATOM   3552 C  CA    . GLY   A  1 460 ? 6.97600  -29.46200  -7.32500  1.000 71.85588  ? 452 GLY   A CA    1 
ATOM   3553 C  C     . GLY   A  1 460 ? 8.03000  -28.42400  -6.96800  1.000 69.47029  ? 452 GLY   A C     1 
ATOM   3554 O  O     . GLY   A  1 460 ? 7.77600  -27.63400  -6.03900  1.000 73.71978  ? 452 GLY   A O     1 
ATOM   3555 N  N     . ALA   A  1 461 ? 9.17200  -28.43300  -7.66600  1.000 71.66212  ? 453 ALA   A N     1 
ATOM   3556 C  CA    . ALA   A  1 461 ? 10.31900 -27.51500  -7.46400  1.000 72.14369  ? 453 ALA   A CA    1 
ATOM   3557 C  C     . ALA   A  1 461 ? 10.33200 -26.42000  -8.53800  1.000 75.24169  ? 453 ALA   A C     1 
ATOM   3558 O  O     . ALA   A  1 461 ? 11.22000 -25.54600  -8.47300  1.000 77.22196  ? 453 ALA   A O     1 
ATOM   3559 C  CB    . ALA   A  1 461 ? 11.60400 -28.30500  -7.48900  1.000 67.76168  ? 453 ALA   A CB    1 
ATOM   3560 N  N     . GLN   A  1 462 ? 9.38900  -26.46600  -9.48500  1.000 74.36199  ? 454 GLN   A N     1 
ATOM   3561 C  CA    . GLN   A  1 462 ? 9.38500  -25.61500  -10.70600 1.000 78.30827  ? 454 GLN   A CA    1 
ATOM   3562 C  C     . GLN   A  1 462 ? 9.05000  -24.16500  -10.33300 1.000 80.08073  ? 454 GLN   A C     1 
ATOM   3563 O  O     . GLN   A  1 462 ? 9.61900  -23.25500  -10.96300 1.000 84.71389  ? 454 GLN   A O     1 
ATOM   3564 C  CB    . GLN   A  1 462 ? 8.39500  -26.17100  -11.73300 1.000 76.16235  ? 454 GLN   A CB    1 
ATOM   3565 C  CG    . GLN   A  1 462 ? 8.50600  -25.51900  -13.10400 1.000 78.70009  ? 454 GLN   A CG    1 
ATOM   3566 C  CD    . GLN   A  1 462 ? 7.83900  -26.33400  -14.18500 1.000 81.00146  ? 454 GLN   A CD    1 
ATOM   3567 O  OE1   . GLN   A  1 462 ? 8.11800  -27.51900  -14.35800 1.000 85.40135  ? 454 GLN   A OE1   1 
ATOM   3568 N  NE2   . GLN   A  1 462 ? 6.95500  -25.69800  -14.93600 1.000 79.19722  ? 454 GLN   A NE2   1 
ATOM   3569 N  N     . HIS   A  1 463 ? 8.17300  -23.96200  -9.34200  1.000 76.77792  ? 455 HIS   A N     1 
ATOM   3570 C  CA    . HIS   A  1 463 ? 7.61800  -22.63700  -8.94700  1.000 77.17318  ? 455 HIS   A CA    1 
ATOM   3571 C  C     . HIS   A  1 463 ? 8.73400  -21.67200  -8.52400  1.000 78.68606  ? 455 HIS   A C     1 
ATOM   3572 O  O     . HIS   A  1 463 ? 8.53000  -20.45200  -8.69600  1.000 88.69800  ? 455 HIS   A O     1 
ATOM   3573 C  CB    . HIS   A  1 463 ? 6.55800  -22.78700  -7.84600  1.000 77.79680  ? 455 HIS   A CB    1 
ATOM   3574 C  CG    . HIS   A  1 463 ? 7.09400  -23.27300  -6.54100  1.000 81.42537  ? 455 HIS   A CG    1 
ATOM   3575 N  ND1   . HIS   A  1 463 ? 7.50600  -22.41100  -5.54300  1.000 80.18440  ? 455 HIS   A ND1   1 
ATOM   3576 C  CD2   . HIS   A  1 463 ? 7.28300  -24.52200  -6.06700  1.000 75.34563  ? 455 HIS   A CD2   1 
ATOM   3577 C  CE1   . HIS   A  1 463 ? 7.92700  -23.11100  -4.50900  1.000 79.64532  ? 455 HIS   A CE1   1 
ATOM   3578 N  NE2   . HIS   A  1 463 ? 7.80200  -24.41000  -4.80700  1.000 77.23519  ? 455 HIS   A NE2   1 
ATOM   3579 N  N     . PHE   A  1 464 ? 9.85400  -22.17600  -7.98800  1.000 79.15387  ? 456 PHE   A N     1 
ATOM   3580 C  CA    . PHE   A  1 464 ? 11.00300 -21.34400  -7.53200  1.000 81.34223  ? 456 PHE   A CA    1 
ATOM   3581 C  C     . PHE   A  1 464 ? 12.11000 -21.32000  -8.59700  1.000 80.68716  ? 456 PHE   A C     1 
ATOM   3582 O  O     . PHE   A  1 464 ? 13.24600 -20.92700  -8.26400  1.000 79.50649  ? 456 PHE   A O     1 
ATOM   3583 C  CB    . PHE   A  1 464 ? 11.50700 -21.78700  -6.15300  1.000 78.01164  ? 456 PHE   A CB    1 
ATOM   3584 C  CG    . PHE   A  1 464 ? 12.10700 -23.16800  -6.05200  1.000 75.46816  ? 456 PHE   A CG    1 
ATOM   3585 C  CD1   . PHE   A  1 464 ? 13.38500 -23.43400  -6.52400  1.000 74.94493  ? 456 PHE   A CD1   1 
ATOM   3586 C  CD2   . PHE   A  1 464 ? 11.41700 -24.18800  -5.41700  1.000 77.47639  ? 456 PHE   A CD2   1 
ATOM   3587 C  CE1   . PHE   A  1 464 ? 13.93800 -24.69900  -6.40100  1.000 74.85230  ? 456 PHE   A CE1   1 
ATOM   3588 C  CE2   . PHE   A  1 464 ? 11.97400 -25.45200  -5.29100  1.000 77.33279  ? 456 PHE   A CE2   1 
ATOM   3589 C  CZ    . PHE   A  1 464 ? 13.23300 -25.70500  -5.78400  1.000 77.89438  ? 456 PHE   A CZ    1 
ATOM   3590 N  N     . LEU   A  1 465 ? 11.79000 -21.69300  -9.84000  1.000 79.67404  ? 457 LEU   A N     1 
ATOM   3591 C  CA    . LEU   A  1 465 ? 12.65700 -21.45200  -11.02500 1.000 83.13621  ? 457 LEU   A CA    1 
ATOM   3592 C  C     . LEU   A  1 465 ? 12.27200 -20.10400  -11.64800 1.000 82.81870  ? 457 LEU   A C     1 
ATOM   3593 O  O     . LEU   A  1 465 ? 11.06100 -19.85100  -11.81300 1.000 82.37476  ? 457 LEU   A O     1 
ATOM   3594 C  CB    . LEU   A  1 465 ? 12.49100 -22.60200  -12.02400 1.000 83.90334  ? 457 LEU   A CB    1 
ATOM   3595 C  CG    . LEU   A  1 465 ? 13.42100 -22.57100  -13.23500 1.000 84.92942  ? 457 LEU   A CG    1 
ATOM   3596 C  CD1   . LEU   A  1 465 ? 14.88300 -22.59000  -12.81200 1.000 82.69886  ? 457 LEU   A CD1   1 
ATOM   3597 C  CD2   . LEU   A  1 465 ? 13.12400 -23.73400  -14.16800 1.000 76.84397  ? 457 LEU   A CD2   1 
ATOM   3598 N  N     . LYS   A  1 466 ? 13.26700 -19.27100  -11.96500 1.000 83.46071  ? 458 LYS   A N     1 
ATOM   3599 C  CA    . LYS   A  1 466 ? 13.07400 -17.93000  -12.58300 1.000 87.28366  ? 458 LYS   A CA    1 
ATOM   3600 C  C     . LYS   A  1 466 ? 12.33900 -18.11300  -13.91800 1.000 92.62696  ? 458 LYS   A C     1 
ATOM   3601 O  O     . LYS   A  1 466 ? 12.51200 -19.18100  -14.54300 1.000 93.50142  ? 458 LYS   A O     1 
ATOM   3602 C  CB    . LYS   A  1 466 ? 14.42200 -17.22000  -12.76400 1.000 88.02863  ? 458 LYS   A CB    1 
ATOM   3603 C  CG    . LYS   A  1 466 ? 14.43300 -15.74100  -12.40000 1.000 91.90905  ? 458 LYS   A CG    1 
ATOM   3604 C  CD    . LYS   A  1 466 ? 15.82400 -15.13100  -12.32500 1.000 97.39480  ? 458 LYS   A CD    1 
ATOM   3605 C  CE    . LYS   A  1 466 ? 16.76000 -15.87400  -11.39200 1.000 91.06986  ? 458 LYS   A CE    1 
ATOM   3606 N  NZ    . LYS   A  1 466 ? 17.89800 -15.02500  -10.96500 1.000 94.21149  ? 458 LYS   A NZ    1 
ATOM   3607 N  N     . ASP   A  1 467 ? 11.54900 -17.11400  -14.32800 1.000 94.65304  ? 459 ASP   A N     1 
ATOM   3608 C  CA    . ASP   A  1 467 ? 10.68200 -17.15600  -15.54000 1.000 89.68262  ? 459 ASP   A CA    1 
ATOM   3609 C  C     . ASP   A  1 467 ? 11.52200 -17.53300  -16.76700 1.000 89.45504  ? 459 ASP   A C     1 
ATOM   3610 O  O     . ASP   A  1 467 ? 10.97800 -18.21700  -17.65600 1.000 92.19091  ? 459 ASP   A O     1 
ATOM   3611 C  CB    . ASP   A  1 467 ? 9.95000  -15.82600  -15.74800 1.000 93.05596  ? 459 ASP   A CB    1 
ATOM   3612 C  CG    . ASP   A  1 467 ? 8.79500  -15.59400  -14.78700 1.000 93.26756  ? 459 ASP   A CG    1 
ATOM   3613 O  OD1   . ASP   A  1 467 ? 8.14300  -16.58600  -14.40100 1.000 91.01185  ? 459 ASP   A OD1   1 
ATOM   3614 O  OD2   . ASP   A  1 467 ? 8.55400  -14.42300  -14.43300 1.000 95.91876  ? 459 ASP   A OD2   1 
ATOM   3615 N  N     . ASP   A  1 468 ? 12.79300 -17.11300  -16.80300 1.000 90.32637  ? 460 ASP   A N     1 
ATOM   3616 C  CA    . ASP   A  1 468 ? 13.75500 -17.39700  -17.90500 1.000 90.45291  ? 460 ASP   A CA    1 
ATOM   3617 C  C     . ASP   A  1 468 ? 14.75900 -18.46400  -17.44500 1.000 87.92587  ? 460 ASP   A C     1 
ATOM   3618 O  O     . ASP   A  1 468 ? 15.87400 -18.50300  -17.99700 1.000 88.39893  ? 460 ASP   A O     1 
ATOM   3619 C  CB    . ASP   A  1 468 ? 14.44700 -16.10900  -18.36700 1.000 93.68639  ? 460 ASP   A CB    1 
ATOM   3620 C  CG    . ASP   A  1 468 ? 15.27500 -15.42000  -17.29100 1.000 98.49820  ? 460 ASP   A CG    1 
ATOM   3621 O  OD1   . ASP   A  1 468 ? 16.42200 -15.85300  -17.06500 1.000 93.71820  ? 460 ASP   A OD1   1 
ATOM   3622 O  OD2   . ASP   A  1 468 ? 14.76300 -14.46000  -16.67900 1.000 100.23775 ? 460 ASP   A OD2   1 
ATOM   3623 N  N     . GLY   A  1 469 ? 14.36500 -19.31800  -16.49600 1.000 87.20547  ? 461 GLY   A N     1 
ATOM   3624 C  CA    . GLY   A  1 469 ? 15.25600 -20.29200  -15.83400 1.000 83.81124  ? 461 GLY   A CA    1 
ATOM   3625 C  C     . GLY   A  1 469 ? 15.49800 -21.52500  -16.69000 1.000 84.97372  ? 461 GLY   A C     1 
ATOM   3626 O  O     . GLY   A  1 469 ? 14.58500 -21.91200  -17.45100 1.000 82.65287  ? 461 GLY   A O     1 
ATOM   3627 N  N     . VAL   A  1 470 ? 16.69300 -22.11300  -16.57000 1.000 80.47842  ? 462 VAL   A N     1 
ATOM   3628 C  CA    . VAL   A  1 470 ? 17.09300 -23.39400  -17.22500 1.000 78.62893  ? 462 VAL   A CA    1 
ATOM   3629 C  C     . VAL   A  1 470 ? 16.94000 -24.52400  -16.20100 1.000 81.94541  ? 462 VAL   A C     1 
ATOM   3630 O  O     . VAL   A  1 470 ? 17.17700 -24.27300  -15.00400 1.000 84.54209  ? 462 VAL   A O     1 
ATOM   3631 C  CB    . VAL   A  1 470 ? 18.53300 -23.31700  -17.77200 1.000 79.66006  ? 462 VAL   A CB    1 
ATOM   3632 C  CG1   . VAL   A  1 470 ? 19.09500 -24.68600  -18.12800 1.000 77.73059  ? 462 VAL   A CG1   1 
ATOM   3633 C  CG2   . VAL   A  1 470 ? 18.62800 -22.38100  -18.96400 1.000 82.26114  ? 462 VAL   A CG2   1 
ATOM   3634 N  N     . SER   A  1 471 ? 16.54200 -25.71400  -16.66000 1.000 74.03937  ? 463 SER   A N     1 
ATOM   3635 C  CA    . SER   A  1 471 ? 16.61900 -26.99100  -15.90400 1.000 71.55085  ? 463 SER   A CA    1 
ATOM   3636 C  C     . SER   A  1 471 ? 17.67200 -27.88500  -16.56200 1.000 70.86995  ? 463 SER   A C     1 
ATOM   3637 O  O     . SER   A  1 471 ? 17.64500 -28.01400  -17.80000 1.000 75.44738  ? 463 SER   A O     1 
ATOM   3638 C  CB    . SER   A  1 471 ? 15.28100 -27.67900  -15.83500 1.000 69.99046  ? 463 SER   A CB    1 
ATOM   3639 O  OG    . SER   A  1 471 ? 15.37000 -28.89500  -15.10600 1.000 67.78711  ? 463 SER   A OG    1 
ATOM   3640 N  N     . ILE   A  1 472 ? 18.59000 -28.43000  -15.76100 1.000 70.04462  ? 464 ILE   A N     1 
ATOM   3641 C  CA    . ILE   A  1 472 ? 19.57600 -29.47100  -16.17000 1.000 69.21825  ? 464 ILE   A CA    1 
ATOM   3642 C  C     . ILE   A  1 472 ? 19.26100 -30.72400  -15.35500 1.000 72.65212  ? 464 ILE   A C     1 
ATOM   3643 O  O     . ILE   A  1 472 ? 19.50800 -30.75800  -14.15000 1.000 72.74882  ? 464 ILE   A O     1 
ATOM   3644 C  CB    . ILE   A  1 472 ? 21.02300 -28.96900  -15.98000 1.000 70.72315  ? 464 ILE   A CB    1 
ATOM   3645 C  CG1   . ILE   A  1 472 ? 21.32400 -27.78100  -16.90100 1.000 73.18382  ? 464 ILE   A CG1   1 
ATOM   3646 C  CG2   . ILE   A  1 472 ? 22.02500 -30.10000  -16.17300 1.000 69.89958  ? 464 ILE   A CG2   1 
ATOM   3647 C  CD1   . ILE   A  1 472 ? 22.65300 -27.10000  -16.64400 1.000 74.98108  ? 464 ILE   A CD1   1 
ATOM   3648 N  N     . PRO   A  1 473 ? 18.67700 -31.78500  -15.96000 1.000 69.38281  ? 465 PRO   A N     1 
ATOM   3649 C  CA    . PRO   A  1 473 ? 18.46400 -31.86200  -17.40400 1.000 65.88742  ? 465 PRO   A CA    1 
ATOM   3650 C  C     . PRO   A  1 473 ? 17.20700 -31.12000  -17.87800 1.000 66.55330  ? 465 PRO   A C     1 
ATOM   3651 O  O     . PRO   A  1 473 ? 16.28600 -30.95700  -17.09500 1.000 65.96726  ? 465 PRO   A O     1 
ATOM   3652 C  CB    . PRO   A  1 473 ? 18.30100 -33.37000  -17.62500 1.000 66.74697  ? 465 PRO   A CB    1 
ATOM   3653 C  CG    . PRO   A  1 473 ? 17.60100 -33.84200  -16.37000 1.000 62.33197  ? 465 PRO   A CG    1 
ATOM   3654 C  CD    . PRO   A  1 473 ? 18.14700 -32.96500  -15.26000 1.000 63.26069  ? 465 PRO   A CD    1 
ATOM   3655 N  N     . GLY   A  1 474 ? 17.21500 -30.69100  -19.14400 1.000 67.94901  ? 466 GLY   A N     1 
ATOM   3656 C  CA    . GLY   A  1 474 ? 16.07700 -30.03200  -19.81200 1.000 68.89531  ? 466 GLY   A CA    1 
ATOM   3657 C  C     . GLY   A  1 474 ? 15.08000 -31.05000  -20.33300 1.000 67.36371  ? 466 GLY   A C     1 
ATOM   3658 O  O     . GLY   A  1 474 ? 13.87100 -30.76200  -20.30900 1.000 69.03201  ? 466 GLY   A O     1 
ATOM   3659 N  N     . GLU   A  1 475 ? 15.56900 -32.21300  -20.76800 1.000 66.16559  ? 467 GLU   A N     1 
ATOM   3660 C  CA    . GLU   A  1 475 ? 14.75100 -33.25200  -21.44300 1.000 64.88629  ? 467 GLU   A CA    1 
ATOM   3661 C  C     . GLU   A  1 475 ? 15.29800 -34.64200  -21.10900 1.000 62.98555  ? 467 GLU   A C     1 
ATOM   3662 O  O     . GLU   A  1 475 ? 16.52800 -34.77000  -20.94100 1.000 63.26430  ? 467 GLU   A O     1 
ATOM   3663 C  CB    . GLU   A  1 475 ? 14.78200 -33.01800  -22.95200 1.000 66.42646  ? 467 GLU   A CB    1 
ATOM   3664 C  CG    . GLU   A  1 475 ? 13.46200 -33.28700  -23.63800 1.000 67.60985  ? 467 GLU   A CG    1 
ATOM   3665 C  CD    . GLU   A  1 475 ? 13.59600 -33.39100  -25.14300 1.000 73.41997  ? 467 GLU   A CD    1 
ATOM   3666 O  OE1   . GLU   A  1 475 ? 14.21500 -34.36800  -25.60400 1.000 75.10935  ? 467 GLU   A OE1   1 
ATOM   3667 O  OE2   . GLU   A  1 475 ? 13.10800 -32.48200  -25.84400 1.000 79.04491  ? 467 GLU   A OE2   1 
ATOM   3668 N  N     . TYR   A  1 476 ? 14.40700 -35.63200  -21.01100 1.000 61.28586  ? 468 TYR   A N     1 
ATOM   3669 C  CA    . TYR   A  1 476 ? 14.75300 -37.07700  -20.98400 1.000 59.63527  ? 468 TYR   A CA    1 
ATOM   3670 C  C     . TYR   A  1 476 ? 13.63900 -37.88000  -21.66400 1.000 58.71140  ? 468 TYR   A C     1 
ATOM   3671 O  O     . TYR   A  1 476 ? 12.46400 -37.46400  -21.61900 1.000 58.77940  ? 468 TYR   A O     1 
ATOM   3672 C  CB    . TYR   A  1 476 ? 15.05800 -37.56300  -19.56300 1.000 59.27338  ? 468 TYR   A CB    1 
ATOM   3673 C  CG    . TYR   A  1 476 ? 14.20100 -37.01000  -18.45100 1.000 61.41006  ? 468 TYR   A CG    1 
ATOM   3674 C  CD1   . TYR   A  1 476 ? 12.99800 -37.60500  -18.10600 1.000 58.34327  ? 468 TYR   A CD1   1 
ATOM   3675 C  CD2   . TYR   A  1 476 ? 14.62600 -35.92900  -17.69700 1.000 60.80462  ? 468 TYR   A CD2   1 
ATOM   3676 C  CE1   . TYR   A  1 476 ? 12.22600 -37.12200  -17.06000 1.000 60.22342  ? 468 TYR   A CE1   1 
ATOM   3677 C  CE2   . TYR   A  1 476 ? 13.86700 -35.43200  -16.64900 1.000 60.60068  ? 468 TYR   A CE2   1 
ATOM   3678 C  CZ    . TYR   A  1 476 ? 12.66100 -36.02900  -16.33100 1.000 65.68194  ? 468 TYR   A CZ    1 
ATOM   3679 O  OH    . TYR   A  1 476 ? 11.91000 -35.53900  -15.30300 1.000 68.09263  ? 468 TYR   A OH    1 
ATOM   3680 N  N     . THR   A  1 477 ? 14.02700 -38.98800  -22.30200 1.000 58.05618  ? 469 THR   A N     1 
ATOM   3681 C  CA    . THR   A  1 477 ? 13.14700 -39.88200  -23.10100 1.000 57.31184  ? 469 THR   A CA    1 
ATOM   3682 C  C     . THR   A  1 477 ? 13.48100 -41.33800  -22.76400 1.000 55.67272  ? 469 THR   A C     1 
ATOM   3683 O  O     . THR   A  1 477 ? 14.67600 -41.68900  -22.79500 1.000 55.90331  ? 469 THR   A O     1 
ATOM   3684 C  CB    . THR   A  1 477 ? 13.30100 -39.60100  -24.60200 1.000 58.89658  ? 469 THR   A CB    1 
ATOM   3685 O  OG1   . THR   A  1 477 ? 12.95500 -38.23500  -24.83200 1.000 60.54718  ? 469 THR   A OG1   1 
ATOM   3686 C  CG2   . THR   A  1 477 ? 12.44100 -40.49300  -25.47000 1.000 58.33673  ? 469 THR   A CG2   1 
ATOM   3687 N  N     . SER   A  1 478 ? 12.45900 -42.13700  -22.44700 1.000 54.24945  ? 470 SER   A N     1 
ATOM   3688 C  CA    . SER   A  1 478 ? 12.56000 -43.60100  -22.20800 1.000 52.75921  ? 470 SER   A CA    1 
ATOM   3689 C  C     . SER   A  1 478 ? 12.41400 -44.34800  -23.54000 1.000 58.53822  ? 470 SER   A C     1 
ATOM   3690 O  O     . SER   A  1 478 ? 11.62600 -43.89400  -24.39800 1.000 53.71215  ? 470 SER   A O     1 
ATOM   3691 C  CB    . SER   A  1 478 ? 11.53300 -44.05700  -21.20600 1.000 52.97233  ? 470 SER   A CB    1 
ATOM   3692 O  OG    . SER   A  1 478 ? 10.22100 -43.72400  -21.63400 1.000 56.58769  ? 470 SER   A OG    1 
ATOM   3693 N  N     . PHE   A  1 479 ? 13.16100 -45.44300  -23.70200 1.000 54.44646  ? 471 PHE   A N     1 
ATOM   3694 C  CA    . PHE   A  1 479 ? 13.13800 -46.33300  -24.89200 1.000 54.70050  ? 471 PHE   A CA    1 
ATOM   3695 C  C     . PHE   A  1 479 ? 12.75000 -47.74700  -24.45100 1.000 53.85118  ? 471 PHE   A C     1 
ATOM   3696 O  O     . PHE   A  1 479 ? 13.15100 -48.14600  -23.34400 1.000 54.67661  ? 471 PHE   A O     1 
ATOM   3697 C  CB    . PHE   A  1 479 ? 14.49900 -46.33200  -25.59100 1.000 53.99412  ? 471 PHE   A CB    1 
ATOM   3698 C  CG    . PHE   A  1 479 ? 14.77800 -45.10400  -26.41800 1.000 57.43689  ? 471 PHE   A CG    1 
ATOM   3699 C  CD1   . PHE   A  1 479 ? 15.23700 -43.94000  -25.82400 1.000 57.41509  ? 471 PHE   A CD1   1 
ATOM   3700 C  CD2   . PHE   A  1 479 ? 14.58000 -45.11200  -27.79000 1.000 57.53910  ? 471 PHE   A CD2   1 
ATOM   3701 C  CE1   . PHE   A  1 479 ? 15.49400 -42.81000  -26.58500 1.000 59.72011  ? 471 PHE   A CE1   1 
ATOM   3702 C  CE2   . PHE   A  1 479 ? 14.83600 -43.98100  -28.54900 1.000 58.98809  ? 471 PHE   A CE2   1 
ATOM   3703 C  CZ    . PHE   A  1 479 ? 15.29300 -42.83200  -27.94500 1.000 59.70129  ? 471 PHE   A CZ    1 
ATOM   3704 N  N     . LEU   A  1 480 ? 11.98900 -48.45800  -25.29100 1.000 52.25975  ? 472 LEU   A N     1 
ATOM   3705 C  CA    . LEU   A  1 480 ? 11.61400 -49.88600  -25.10600 1.000 52.38139  ? 472 LEU   A CA    1 
ATOM   3706 C  C     . LEU   A  1 480 ? 12.07900 -50.69200  -26.32200 1.000 53.63557  ? 472 LEU   A C     1 
ATOM   3707 O  O     . LEU   A  1 480 ? 12.13900 -50.11900  -27.42500 1.000 57.82132  ? 472 LEU   A O     1 
ATOM   3708 C  CB    . LEU   A  1 480 ? 10.09700 -50.00200  -24.93000 1.000 51.79275  ? 472 LEU   A CB    1 
ATOM   3709 C  CG    . LEU   A  1 480 ? 9.56200  -49.62800  -23.55100 1.000 51.41307  ? 472 LEU   A CG    1 
ATOM   3710 C  CD1   . LEU   A  1 480 ? 8.04600  -49.52400  -23.57300 1.000 47.58588  ? 472 LEU   A CD1   1 
ATOM   3711 C  CD2   . LEU   A  1 480 ? 10.01500 -50.63000  -22.50000 1.000 50.04627  ? 472 LEU   A CD2   1 
ATOM   3712 N  N     . ALA   A  1 481 ? 12.39300 -51.97200  -26.11100 1.000 50.83291  ? 473 ALA   A N     1 
ATOM   3713 C  CA    . ALA   A  1 481 ? 12.76400 -52.94800  -27.16000 1.000 51.37155  ? 473 ALA   A CA    1 
ATOM   3714 C  C     . ALA   A  1 481 ? 12.28400 -54.33100  -26.73400 1.000 51.94302  ? 473 ALA   A C     1 
ATOM   3715 O  O     . ALA   A  1 481 ? 12.57500 -54.76000  -25.62000 1.000 50.46369  ? 473 ALA   A O     1 
ATOM   3716 C  CB    . ALA   A  1 481 ? 14.25600 -52.92400  -27.38800 1.000 51.40767  ? 473 ALA   A CB    1 
ATOM   3717 N  N     . PRO   A  1 482 ? 11.53000 -55.06400  -27.58500 1.000 51.01225  ? 474 PRO   A N     1 
ATOM   3718 C  CA    . PRO   A  1 482 ? 11.11200 -56.42400  -27.25200 1.000 50.42740  ? 474 PRO   A CA    1 
ATOM   3719 C  C     . PRO   A  1 482 ? 12.34800 -57.32900  -27.21400 1.000 49.24699  ? 474 PRO   A C     1 
ATOM   3720 O  O     . PRO   A  1 482 ? 13.23400 -57.11200  -28.01400 1.000 55.75405  ? 474 PRO   A O     1 
ATOM   3721 C  CB    . PRO   A  1 482 ? 10.14000 -56.81100  -28.37600 1.000 54.15253  ? 474 PRO   A CB    1 
ATOM   3722 C  CG    . PRO   A  1 482 ? 10.53200 -55.91600  -29.53600 1.000 52.36352  ? 474 PRO   A CG    1 
ATOM   3723 C  CD    . PRO   A  1 482 ? 11.05000 -54.63800  -28.90800 1.000 50.10682  ? 474 PRO   A CD    1 
ATOM   3724 N  N     . ILE   A  1 483 ? 12.39300 -58.27300  -26.26900 1.000 47.58973  ? 475 ILE   A N     1 
ATOM   3725 C  CA    . ILE   A  1 483 ? 13.53800 -59.21400  -26.08800 1.000 50.70632  ? 475 ILE   A CA    1 
ATOM   3726 C  C     . ILE   A  1 483 ? 13.01900 -60.65000  -25.98600 1.000 52.40684  ? 475 ILE   A C     1 
ATOM   3727 O  O     . ILE   A  1 483 ? 11.83700 -60.84300  -25.63200 1.000 46.84116  ? 475 ILE   A O     1 
ATOM   3728 C  CB    . ILE   A  1 483 ? 14.39000 -58.84400  -24.85700 1.000 49.28460  ? 475 ILE   A CB    1 
ATOM   3729 C  CG1   . ILE   A  1 483 ? 13.62100 -59.01300  -23.54300 1.000 47.38018  ? 475 ILE   A CG1   1 
ATOM   3730 C  CG2   . ILE   A  1 483 ? 14.96400 -57.44500  -24.99900 1.000 48.65339  ? 475 ILE   A CG2   1 
ATOM   3731 C  CD1   . ILE   A  1 483 ? 14.48800 -59.45700  -22.38800 1.000 46.52744  ? 475 ILE   A CD1   1 
ATOM   3732 N  N     . SER   A  1 484 ? 13.90100 -61.60900  -26.27700 1.000 49.80448  ? 476 SER   A N     1 
ATOM   3733 C  CA    . SER   A  1 484 ? 13.70600 -63.06300  -26.05700 1.000 54.72623  ? 476 SER   A CA    1 
ATOM   3734 C  C     . SER   A  1 484 ? 14.81600 -63.56900  -25.13400 1.000 53.13612  ? 476 SER   A C     1 
ATOM   3735 O  O     . SER   A  1 484 ? 15.99600 -63.49600  -25.53000 1.000 60.86039  ? 476 SER   A O     1 
ATOM   3736 C  CB    . SER   A  1 484 ? 13.69100 -63.81900  -27.35900 1.000 52.54366  ? 476 SER   A CB    1 
ATOM   3737 O  OG    . SER   A  1 484 ? 13.54700 -65.21300  -27.13100 1.000 51.67003  ? 476 SER   A OG    1 
ATOM   3738 N  N     . SER   A  1 485 ? 14.44700 -64.01600  -23.93300 1.000 48.03907  ? 477 SER   A N     1 
ATOM   3739 C  CA    . SER   A  1 485 ? 15.33700 -64.72000  -22.97800 1.000 53.89734  ? 477 SER   A CA    1 
ATOM   3740 C  C     . SER   A  1 485 ? 14.50100 -65.65200  -22.09900 1.000 51.46678  ? 477 SER   A C     1 
ATOM   3741 O  O     . SER   A  1 485 ? 13.93000 -65.17300  -21.10200 1.000 55.10120  ? 477 SER   A O     1 
ATOM   3742 C  CB    . SER   A  1 485 ? 16.13700 -63.74400  -22.15500 1.000 53.66487  ? 477 SER   A CB    1 
ATOM   3743 O  OG    . SER   A  1 485 ? 16.95900 -64.42400  -21.21700 1.000 53.11759  ? 477 SER   A OG    1 
ATOM   3744 N  N     . SER   A  1 486 ? 14.42000 -66.92900  -22.48100 1.000 49.34924  ? 478 SER   A N     1 
ATOM   3745 C  CA    . SER   A  1 486 ? 13.85500 -68.02900  -21.65800 1.000 51.47692  ? 478 SER   A CA    1 
ATOM   3746 C  C     . SER   A  1 486 ? 14.62400 -68.10800  -20.33300 1.000 51.66268  ? 478 SER   A C     1 
ATOM   3747 O  O     . SER   A  1 486 ? 14.00100 -68.43900  -19.31000 1.000 57.46104  ? 478 SER   A O     1 
ATOM   3748 C  CB    . SER   A  1 486 ? 13.88500 -69.34100  -22.40600 1.000 52.75320  ? 478 SER   A CB    1 
ATOM   3749 O  OG    . SER   A  1 486 ? 12.97500 -69.32700  -23.49800 1.000 51.37962  ? 478 SER   A OG    1 
ATOM   3750 N  N     . LYS   A  1 487 ? 15.92500 -67.79400  -20.36500 1.000 49.95505  ? 479 LYS   A N     1 
ATOM   3751 C  CA    . LYS   A  1 487 ? 16.82200 -67.68800  -19.18000 1.000 55.78764  ? 479 LYS   A CA    1 
ATOM   3752 C  C     . LYS   A  1 487 ? 16.27000 -66.64100  -18.20100 1.000 54.10435  ? 479 LYS   A C     1 
ATOM   3753 O  O     . LYS   A  1 487 ? 16.06200 -66.99400  -17.02500 1.000 54.45743  ? 479 LYS   A O     1 
ATOM   3754 C  CB    . LYS   A  1 487 ? 18.24600 -67.34800  -19.63700 1.000 60.21893  ? 479 LYS   A CB    1 
ATOM   3755 C  CG    . LYS   A  1 487 ? 19.18300 -66.79600  -18.56800 1.000 61.90522  ? 479 LYS   A CG    1 
ATOM   3756 C  CD    . LYS   A  1 487 ? 19.46600 -67.75800  -17.43300 1.000 66.68395  ? 479 LYS   A CD    1 
ATOM   3757 C  CE    . LYS   A  1 487 ? 20.44400 -67.20000  -16.41800 1.000 75.86583  ? 479 LYS   A CE    1 
ATOM   3758 N  NZ    . LYS   A  1 487 ? 21.80900 -67.05500  -16.98000 1.000 72.04753  ? 479 LYS   A NZ    1 
ATOM   3759 N  N     . LEU   A  1 488 ? 16.05200 -65.40500  -18.66500 1.000 51.87625  ? 480 LEU   A N     1 
ATOM   3760 C  CA    . LEU   A  1 488 ? 15.56200 -64.27100  -17.83100 1.000 52.34336  ? 480 LEU   A CA    1 
ATOM   3761 C  C     . LEU   A  1 488 ? 14.09800 -64.50100  -17.43800 1.000 51.27012  ? 480 LEU   A C     1 
ATOM   3762 O  O     . LEU   A  1 488 ? 13.69900 -64.00600  -16.36600 1.000 52.17983  ? 480 LEU   A O     1 
ATOM   3763 C  CB    . LEU   A  1 488 ? 15.71100 -62.95000  -18.59400 1.000 55.64053  ? 480 LEU   A CB    1 
ATOM   3764 C  CG    . LEU   A  1 488 ? 17.11700 -62.35200  -18.61900 1.000 51.35351  ? 480 LEU   A CG    1 
ATOM   3765 C  CD1   . LEU   A  1 488 ? 17.21100 -61.24200  -19.65300 1.000 50.65031  ? 480 LEU   A CD1   1 
ATOM   3766 C  CD2   . LEU   A  1 488 ? 17.51200 -61.82900  -17.24800 1.000 47.80596  ? 480 LEU   A CD2   1 
ATOM   3767 N  N     . TYR   A  1 489 ? 13.32500 -65.19500  -18.27900 1.000 44.97540  ? 481 TYR   A N     1 
ATOM   3768 C  CA    . TYR   A  1 489 ? 11.91300 -65.56300  -17.99400 1.000 48.57362  ? 481 TYR   A CA    1 
ATOM   3769 C  C     . TYR   A  1 489 ? 11.87000 -66.51700  -16.79200 1.000 55.23592  ? 481 TYR   A C     1 
ATOM   3770 O  O     . TYR   A  1 489 ? 10.99300 -66.34200  -15.92100 1.000 51.97329  ? 481 TYR   A O     1 
ATOM   3771 C  CB    . TYR   A  1 489 ? 11.24100 -66.18500  -19.21800 1.000 47.86395  ? 481 TYR   A CB    1 
ATOM   3772 C  CG    . TYR   A  1 489 ? 9.84900  -66.69800  -18.95300 1.000 47.68213  ? 481 TYR   A CG    1 
ATOM   3773 C  CD1   . TYR   A  1 489 ? 8.77700  -65.82900  -18.82700 1.000 49.98130  ? 481 TYR   A CD1   1 
ATOM   3774 C  CD2   . TYR   A  1 489 ? 9.60400  -68.05300  -18.81400 1.000 52.17424  ? 481 TYR   A CD2   1 
ATOM   3775 C  CE1   . TYR   A  1 489 ? 7.49600  -66.29400  -18.57800 1.000 47.96502  ? 481 TYR   A CE1   1 
ATOM   3776 C  CE2   . TYR   A  1 489 ? 8.33000  -68.53600  -18.56100 1.000 53.15248  ? 481 TYR   A CE2   1 
ATOM   3777 C  CZ    . TYR   A  1 489 ? 7.27200  -67.65300  -18.44300 1.000 52.91267  ? 481 TYR   A CZ    1 
ATOM   3778 O  OH    . TYR   A  1 489 ? 6.01900  -68.13300  -18.19300 1.000 55.69242  ? 481 TYR   A OH    1 
ATOM   3779 N  N     . ASN   A  1 490 ? 12.78900 -67.48900  -16.75400 1.000 49.25948  ? 482 ASN   A N     1 
ATOM   3780 C  CA    . ASN   A  1 490 ? 12.97600 -68.43500  -15.62000 1.000 51.46476  ? 482 ASN   A CA    1 
ATOM   3781 C  C     . ASN   A  1 490 ? 13.29500 -67.65300  -14.33700 1.000 51.18621  ? 482 ASN   A C     1 
ATOM   3782 O  O     . ASN   A  1 490 ? 12.67800 -67.95700  -13.29600 1.000 50.79026  ? 482 ASN   A O     1 
ATOM   3783 C  CB    . ASN   A  1 490 ? 14.06900 -69.47100  -15.90800 1.000 53.00732  ? 482 ASN   A CB    1 
ATOM   3784 C  CG    . ASN   A  1 490 ? 13.53400 -70.87200  -16.12500 1.000 61.70042  ? 482 ASN   A CG    1 
ATOM   3785 O  OD1   . ASN   A  1 490 ? 12.37700 -71.15700  -15.82200 1.000 64.26256  ? 482 ASN   A OD1   1 
ATOM   3786 N  ND2   . ASN   A  1 490 ? 14.37600 -71.76100  -16.63000 1.000 59.23301  ? 482 ASN   A ND2   1 
ATOM   3787 N  N     . GLU   A  1 491 ? 14.21900 -66.68800  -14.41400 1.000 49.29600  ? 483 GLU   A N     1 
ATOM   3788 C  CA    . GLU   A  1 491 ? 14.71800 -65.89400  -13.25500 1.000 53.84031  ? 483 GLU   A CA    1 
ATOM   3789 C  C     . GLU   A  1 491 ? 13.54900 -65.13500  -12.61200 1.000 52.41133  ? 483 GLU   A C     1 
ATOM   3790 O  O     . GLU   A  1 491 ? 13.46000 -65.13700  -11.37000 1.000 51.21697  ? 483 GLU   A O     1 
ATOM   3791 C  CB    . GLU   A  1 491 ? 15.82400 -64.92700  -13.68800 1.000 50.31999  ? 483 GLU   A CB    1 
ATOM   3792 C  CG    . GLU   A  1 491 ? 17.07500 -65.61500  -14.21000 1.000 50.14614  ? 483 GLU   A CG    1 
ATOM   3793 C  CD    . GLU   A  1 491 ? 18.13500 -65.94500  -13.17200 1.000 71.32233  ? 483 GLU   A CD    1 
ATOM   3794 O  OE1   . GLU   A  1 491 ? 17.81700 -65.93000  -11.96100 1.000 78.44248  ? 483 GLU   A OE1   1 
ATOM   3795 O  OE2   . GLU   A  1 491 ? 19.28400 -66.21900  -13.58100 1.000 76.65256  ? 483 GLU   A OE2   1 
ATOM   3796 N  N     . VAL   A  1 492 ? 12.68900 -64.51800  -13.43000 1.000 50.83183  ? 484 VAL   A N     1 
ATOM   3797 C  CA    . VAL   A  1 492 ? 11.47000 -63.77900  -12.98000 1.000 47.89669  ? 484 VAL   A CA    1 
ATOM   3798 C  C     . VAL   A  1 492 ? 10.50800 -64.77900  -12.32500 1.000 50.63169  ? 484 VAL   A C     1 
ATOM   3799 O  O     . VAL   A  1 492 ? 10.03700 -64.49300  -11.21400 1.000 53.55573  ? 484 VAL   A O     1 
ATOM   3800 C  CB    . VAL   A  1 492 ? 10.79500 -63.02600  -14.14600 1.000 48.81241  ? 484 VAL   A CB    1 
ATOM   3801 C  CG1   . VAL   A  1 492 ? 9.44600  -62.44100  -13.74700 1.000 46.77394  ? 484 VAL   A CG1   1 
ATOM   3802 C  CG2   . VAL   A  1 492 ? 11.69500 -61.93800  -14.71300 1.000 44.11397  ? 484 VAL   A CG2   1 
ATOM   3803 N  N     . ARG   A  1 493 ? 10.24400 -65.90700  -12.99000 1.000 50.04706  ? 485 ARG   A N     1 
ATOM   3804 C  CA    . ARG   A  1 493 ? 9.29100  -66.96200  -12.54100 1.000 51.25384  ? 485 ARG   A CA    1 
ATOM   3805 C  C     . ARG   A  1 493 ? 9.71800  -67.49800  -11.16800 1.000 53.81255  ? 485 ARG   A C     1 
ATOM   3806 O  O     . ARG   A  1 493 ? 8.83000  -67.90000  -10.38800 1.000 53.97089  ? 485 ARG   A O     1 
ATOM   3807 C  CB    . ARG   A  1 493 ? 9.23600  -68.09200  -13.57400 1.000 51.52003  ? 485 ARG   A CB    1 
ATOM   3808 C  CG    . ARG   A  1 493 ? 7.92800  -68.87000  -13.59200 1.000 57.66159  ? 485 ARG   A CG    1 
ATOM   3809 C  CD    . ARG   A  1 493 ? 7.83900  -69.73800  -14.83200 1.000 52.39724  ? 485 ARG   A CD    1 
ATOM   3810 N  NE    . ARG   A  1 493 ? 8.73400  -70.87600  -14.68400 1.000 57.84859  ? 485 ARG   A NE    1 
ATOM   3811 C  CZ    . ARG   A  1 493 ? 8.36800  -72.09400  -14.29700 1.000 56.62888  ? 485 ARG   A CZ    1 
ATOM   3812 N  NH1   . ARG   A  1 493 ? 7.09800  -72.37200  -14.04400 1.000 52.87449  ? 485 ARG   A NH1   1 
ATOM   3813 N  NH2   . ARG   A  1 493 ? 9.28400  -73.04000  -14.17700 1.000 52.39091  ? 485 ARG   A NH2   1 
ATOM   3814 N  N     . ALA   A  1 494 ? 11.02600 -67.49000  -10.88800 1.000 51.71038  ? 486 ALA   A N     1 
ATOM   3815 C  CA    . ALA   A  1 494 ? 11.64500 -67.99600  -9.64100  1.000 49.26857  ? 486 ALA   A CA    1 
ATOM   3816 C  C     . ALA   A  1 494 ? 11.49000 -66.98200  -8.49800  1.000 52.91776  ? 486 ALA   A C     1 
ATOM   3817 O  O     . ALA   A  1 494 ? 11.87500 -67.32500  -7.36800  1.000 58.30937  ? 486 ALA   A O     1 
ATOM   3818 C  CB    . ALA   A  1 494 ? 13.10000 -68.31300  -9.89200  1.000 47.02358  ? 486 ALA   A CB    1 
ATOM   3819 N  N     . CYS   A  1 495 ? 10.96000 -65.78400  -8.77300  1.000 54.62359  ? 487 CYS   A N     1 
ATOM   3820 C  CA    . CYS   A  1 495 ? 10.80900 -64.67600  -7.78800  1.000 53.55992  ? 487 CYS   A CA    1 
ATOM   3821 C  C     . CYS   A  1 495 ? 9.42200  -64.71200  -7.13000  1.000 54.57769  ? 487 CYS   A C     1 
ATOM   3822 O  O     . CYS   A  1 495 ? 9.04700  -63.69700  -6.50900  1.000 56.06506  ? 487 CYS   A O     1 
ATOM   3823 C  CB    . CYS   A  1 495 ? 11.02900 -63.31300  -8.43900  1.000 48.10364  ? 487 CYS   A CB    1 
ATOM   3824 S  SG    . CYS   A  1 495 ? 12.73000 -63.03400  -8.99100  1.000 50.68174  ? 487 CYS   A SG    1 
ATOM   3825 N  N     . ARG   A  1 496 ? 8.68900  -65.82600  -7.23800  1.000 48.91417  ? 488 ARG   A N     1 
ATOM   3826 C  CA    . ARG   A  1 496 ? 7.40100  -66.00900  -6.51800  1.000 54.22158  ? 488 ARG   A CA    1 
ATOM   3827 C  C     . ARG   A  1 496 ? 7.68800  -66.04000  -5.01400  1.000 57.23434  ? 488 ARG   A C     1 
ATOM   3828 O  O     . ARG   A  1 496 ? 8.56800  -66.81700  -4.59800  1.000 57.96017  ? 488 ARG   A O     1 
ATOM   3829 C  CB    . ARG   A  1 496 ? 6.67400  -67.28700  -6.94300  1.000 54.88831  ? 488 ARG   A CB    1 
ATOM   3830 C  CG    . ARG   A  1 496 ? 5.26900  -67.40200  -6.36800  1.000 54.65760  ? 488 ARG   A CG    1 
ATOM   3831 C  CD    . ARG   A  1 496 ? 4.36300  -68.29800  -7.19100  1.000 65.81703  ? 488 ARG   A CD    1 
ATOM   3832 N  NE    . ARG   A  1 496 ? 4.71700  -69.70600  -7.07700  1.000 72.56984  ? 488 ARG   A NE    1 
ATOM   3833 C  CZ    . ARG   A  1 496 ? 4.42000  -70.48800  -6.04400  1.000 64.45331  ? 488 ARG   A CZ    1 
ATOM   3834 N  NH1   . ARG   A  1 496 ? 3.75800  -70.00800  -5.00300  1.000 60.72530  ? 488 ARG   A NH1   1 
ATOM   3835 N  NH2   . ARG   A  1 496 ? 4.79600  -71.75500  -6.05800  1.000 59.11176  ? 488 ARG   A NH2   1 
ATOM   3836 N  N     . GLU   A  1 497 ? 6.98100  -65.20400  -4.25000  1.000 58.11381  ? 489 GLU   A N     1 
ATOM   3837 C  CA    . GLU   A  1 497 ? 7.11000  -65.07400  -2.77600  1.000 54.55064  ? 489 GLU   A CA    1 
ATOM   3838 C  C     . GLU   A  1 497 ? 5.77000  -65.42700  -2.12700  1.000 55.58770  ? 489 GLU   A C     1 
ATOM   3839 O  O     . GLU   A  1 497 ? 4.72100  -65.18400  -2.75700  1.000 54.31878  ? 489 GLU   A O     1 
ATOM   3840 C  CB    . GLU   A  1 497 ? 7.54700  -63.65700  -2.40400  1.000 54.27521  ? 489 GLU   A CB    1 
ATOM   3841 C  CG    . GLU   A  1 497 ? 9.02400  -63.40800  -2.64500  1.000 63.33687  ? 489 GLU   A CG    1 
ATOM   3842 C  CD    . GLU   A  1 497 ? 9.48700  -61.97800  -2.42100  1.000 67.60675  ? 489 GLU   A CD    1 
ATOM   3843 O  OE1   . GLU   A  1 497 ? 8.62700  -61.10700  -2.16800  1.000 61.16139  ? 489 GLU   A OE1   1 
ATOM   3844 O  OE2   . GLU   A  1 497 ? 10.71100 -61.73800  -2.50100  1.000 75.54733  ? 489 GLU   A OE2   1 
ATOM   3845 N  N     . LYS   A  1 498 ? 5.82200  -66.00000  -0.92200  1.000 60.34641  ? 490 LYS   A N     1 
ATOM   3846 C  CA    . LYS   A  1 498 ? 4.64000  -66.27800  -0.06400  1.000 59.99448  ? 490 LYS   A CA    1 
ATOM   3847 C  C     . LYS   A  1 498 ? 3.95800  -64.95000  0.29100   1.000 60.19359  ? 490 LYS   A C     1 
ATOM   3848 O  O     . LYS   A  1 498 ? 4.64400  -63.90400  0.28300   1.000 56.46293  ? 490 LYS   A O     1 
ATOM   3849 C  CB    . LYS   A  1 498 ? 5.06400  -67.05600  1.18800   1.000 62.09209  ? 490 LYS   A CB    1 
ATOM   3850 C  CG    . LYS   A  1 498 ? 6.08200  -66.36100  2.08600   1.000 64.89138  ? 490 LYS   A CG    1 
ATOM   3851 C  CD    . LYS   A  1 498 ? 7.04800  -67.31500  2.76300   1.000 68.61301  ? 490 LYS   A CD    1 
ATOM   3852 C  CE    . LYS   A  1 498 ? 8.23500  -66.61200  3.38700   1.000 73.86429  ? 490 LYS   A CE    1 
ATOM   3853 N  NZ    . LYS   A  1 498 ? 9.29000  -67.57400  3.78700   1.000 76.89038  ? 490 LYS   A NZ    1 
ATOM   3854 N  N     . ASP   A  1 499 ? 2.64800  -64.99800  0.55600   1.000 61.41737  ? 491 ASP   A N     1 
ATOM   3855 C  CA    . ASP   A  1 499 ? 1.84400  -63.87400  1.11100   1.000 60.10559  ? 491 ASP   A CA    1 
ATOM   3856 C  C     . ASP   A  1 499 ? 1.72900  -62.73900  0.08500   1.000 56.54586  ? 491 ASP   A C     1 
ATOM   3857 O  O     . ASP   A  1 499 ? 1.69700  -61.56900  0.50800   1.000 59.58678  ? 491 ASP   A O     1 
ATOM   3858 C  CB    . ASP   A  1 499 ? 2.44600  -63.36500  2.42300   1.000 57.66922  ? 491 ASP   A CB    1 
ATOM   3859 C  CG    . ASP   A  1 499 ? 2.82800  -64.47500  3.38600   1.000 57.37856  ? 491 ASP   A CG    1 
ATOM   3860 O  OD1   . ASP   A  1 499 ? 2.19400  -65.54900  3.32500   1.000 56.15552  ? 491 ASP   A OD1   1 
ATOM   3861 O  OD2   . ASP   A  1 499 ? 3.77000  -64.26000  4.16900   1.000 60.40435  ? 491 ASP   A OD2   1 
ATOM   3862 N  N     . ARG   A  1 500 ? 1.66200  -63.07100  -1.20800  1.000 57.30171  ? 492 ARG   A N     1 
ATOM   3863 C  CA    . ARG   A  1 500 ? 1.34600  -62.10500  -2.29700  1.000 60.07691  ? 492 ARG   A CA    1 
ATOM   3864 C  C     . ARG   A  1 500 ? 0.85600  -62.87200  -3.53200  1.000 56.56686  ? 492 ARG   A C     1 
ATOM   3865 O  O     . ARG   A  1 500 ? 0.91600  -64.12000  -3.51800  1.000 55.92979  ? 492 ARG   A O     1 
ATOM   3866 C  CB    . ARG   A  1 500 ? 2.55800  -61.21800  -2.60800  1.000 56.58044  ? 492 ARG   A CB    1 
ATOM   3867 C  CG    . ARG   A  1 500 ? 3.49100  -61.74700  -3.68800  1.000 48.26448  ? 492 ARG   A CG    1 
ATOM   3868 C  CD    . ARG   A  1 500 ? 4.72100  -60.87300  -3.81400  1.000 50.27422  ? 492 ARG   A CD    1 
ATOM   3869 N  NE    . ARG   A  1 500 ? 5.63500  -61.33300  -4.84900  1.000 52.64336  ? 492 ARG   A NE    1 
ATOM   3870 C  CZ    . ARG   A  1 500 ? 6.77000  -60.72500  -5.18000  1.000 53.02722  ? 492 ARG   A CZ    1 
ATOM   3871 N  NH1   . ARG   A  1 500 ? 7.14500  -59.61900  -4.55700  1.000 56.33273  ? 492 ARG   A NH1   1 
ATOM   3872 N  NH2   . ARG   A  1 500 ? 7.52900  -61.22700  -6.13800  1.000 52.97385  ? 492 ARG   A NH2   1 
ATOM   3873 N  N     . ASP   A  1 501 ? 0.37400  -62.14400  -4.54500  1.000 50.74615  ? 493 ASP   A N     1 
ATOM   3874 C  CA    . ASP   A  1 501 ? -0.08300 -62.71000  -5.84200  1.000 53.00010  ? 493 ASP   A CA    1 
ATOM   3875 C  C     . ASP   A  1 501 ? 0.97900  -63.69700  -6.32400  1.000 55.88580  ? 493 ASP   A C     1 
ATOM   3876 O  O     . ASP   A  1 501 ? 2.16600  -63.37300  -6.32000  1.000 50.85503  ? 493 ASP   A O     1 
ATOM   3877 C  CB    . ASP   A  1 501 ? -0.35100 -61.60200  -6.86700  1.000 55.58440  ? 493 ASP   A CB    1 
ATOM   3878 C  CG    . ASP   A  1 501 ? -1.32800 -61.98400  -7.96700  1.000 64.45806  ? 493 ASP   A CG    1 
ATOM   3879 O  OD1   . ASP   A  1 501 ? -1.07000 -62.99100  -8.66400  1.000 59.25518  ? 493 ASP   A OD1   1 
ATOM   3880 O  OD2   . ASP   A  1 501 ? -2.34300 -61.26800  -8.11800  1.000 69.50255  ? 493 ASP   A OD2   1 
ATOM   3881 N  N     . PRO   A  1 502 ? 0.60200  -64.94100  -6.70600  1.000 57.97377  ? 494 PRO   A N     1 
ATOM   3882 C  CA    . PRO   A  1 502 ? 1.55500  -65.89700  -7.27500  1.000 54.05307  ? 494 PRO   A CA    1 
ATOM   3883 C  C     . PRO   A  1 502 ? 2.28700  -65.39700  -8.53200  1.000 55.32918  ? 494 PRO   A C     1 
ATOM   3884 O  O     . PRO   A  1 502 ? 3.36500  -65.89100  -8.79800  1.000 55.27454  ? 494 PRO   A O     1 
ATOM   3885 C  CB    . PRO   A  1 502 ? 0.68300  -67.10400  -7.64900  1.000 53.80762  ? 494 PRO   A CB    1 
ATOM   3886 C  CG    . PRO   A  1 502 ? -0.51700 -66.99700  -6.73900  1.000 54.33135  ? 494 PRO   A CG    1 
ATOM   3887 C  CD    . PRO   A  1 502 ? -0.74700 -65.51100  -6.57100  1.000 51.84768  ? 494 PRO   A CD    1 
ATOM   3888 N  N     . GLU   A  1 503 ? 1.69100  -64.44800  -9.26500  1.000 48.99985  ? 495 GLU   A N     1 
ATOM   3889 C  CA    . GLU   A  1 503 ? 2.21300  -63.91900  -10.55400 1.000 55.15753  ? 495 GLU   A CA    1 
ATOM   3890 C  C     . GLU   A  1 503 ? 2.68300  -62.46500  -10.39400 1.000 51.39250  ? 495 GLU   A C     1 
ATOM   3891 O  O     . GLU   A  1 503 ? 3.00400  -61.84000  -11.42700 1.000 51.80742  ? 495 GLU   A O     1 
ATOM   3892 C  CB    . GLU   A  1 503 ? 1.13100  -64.03300  -11.63200 1.000 58.66180  ? 495 GLU   A CB    1 
ATOM   3893 C  CG    . GLU   A  1 503 ? 0.46900  -65.39900  -11.69300 1.000 57.88826  ? 495 GLU   A CG    1 
ATOM   3894 C  CD    . GLU   A  1 503 ? -0.33500 -65.66300  -12.95500 1.000 62.44438  ? 495 GLU   A CD    1 
ATOM   3895 O  OE1   . GLU   A  1 503 ? -1.29600 -64.91000  -13.22100 1.000 61.17192  ? 495 GLU   A OE1   1 
ATOM   3896 O  OE2   . GLU   A  1 503 ? 0.00600  -66.61900  -13.67300 1.000 73.65291  ? 495 GLU   A OE2   1 
ATOM   3897 N  N     . ALA   A  1 504 ? 2.75500  -61.95500  -9.15900  1.000 47.28783  ? 496 ALA   A N     1 
ATOM   3898 C  CA    . ALA   A  1 504 ? 3.18600  -60.57300  -8.83200  1.000 46.97641  ? 496 ALA   A CA    1 
ATOM   3899 C  C     . ALA   A  1 504 ? 4.55000  -60.28400  -9.46700  1.000 50.66277  ? 496 ALA   A C     1 
ATOM   3900 O  O     . ALA   A  1 504 ? 4.76000  -59.14100  -9.92000  1.000 52.92418  ? 496 ALA   A O     1 
ATOM   3901 C  CB    . ALA   A  1 504 ? 3.24700  -60.38000  -7.33800  1.000 53.48059  ? 496 ALA   A CB    1 
ATOM   3902 N  N     . GLN   A  1 505 ? 5.43800  -61.28300  -9.48400  1.000 49.00036  ? 497 GLN   A N     1 
ATOM   3903 C  CA    . GLN   A  1 505 ? 6.84200  -61.16500  -9.96800  1.000 48.69927  ? 497 GLN   A CA    1 
ATOM   3904 C  C     . GLN   A  1 505 ? 6.86600  -60.75200  -11.44500 1.000 46.68746  ? 497 GLN   A C     1 
ATOM   3905 O  O     . GLN   A  1 505 ? 7.85900  -60.13000  -11.85000 1.000 49.70821  ? 497 GLN   A O     1 
ATOM   3906 C  CB    . GLN   A  1 505 ? 7.62000  -62.46800  -9.75000  1.000 47.23954  ? 497 GLN   A CB    1 
ATOM   3907 C  CG    . GLN   A  1 505 ? 7.05000  -63.68400  -10.47100 1.000 46.43828  ? 497 GLN   A CG    1 
ATOM   3908 C  CD    . GLN   A  1 505 ? 5.99500  -64.40400  -9.67100  1.000 52.56362  ? 497 GLN   A CD    1 
ATOM   3909 O  OE1   . GLN   A  1 505 ? 5.20300  -63.79300  -8.95900  1.000 52.27175  ? 497 GLN   A OE1   1 
ATOM   3910 N  NE2   . GLN   A  1 505 ? 5.96900  -65.72000  -9.79300  1.000 59.36886  ? 497 GLN   A NE2   1 
ATOM   3911 N  N     . PHE   A  1 506 ? 5.83100  -61.09600  -12.21700 1.000 41.46464  ? 498 PHE   A N     1 
ATOM   3912 C  CA    . PHE   A  1 506 ? 5.73900  -60.80100  -13.67300 1.000 50.10905  ? 498 PHE   A CA    1 
ATOM   3913 C  C     . PHE   A  1 506 ? 5.23100  -59.37000  -13.89100 1.000 47.43186  ? 498 PHE   A C     1 
ATOM   3914 O  O     . PHE   A  1 506 ? 5.51900  -58.79800  -14.96200 1.000 40.55128  ? 498 PHE   A O     1 
ATOM   3915 C  CB    . PHE   A  1 506 ? 4.83900  -61.81400  -14.38500 1.000 46.90120  ? 498 PHE   A CB    1 
ATOM   3916 C  CG    . PHE   A  1 506 ? 5.43300  -63.19400  -14.51300 1.000 48.52071  ? 498 PHE   A CG    1 
ATOM   3917 C  CD1   . PHE   A  1 506 ? 6.57100  -63.40100  -15.27400 1.000 47.67766  ? 498 PHE   A CD1   1 
ATOM   3918 C  CD2   . PHE   A  1 506 ? 4.85100  -64.28400  -13.88400 1.000 48.13347  ? 498 PHE   A CD2   1 
ATOM   3919 C  CE1   . PHE   A  1 506 ? 7.11700  -64.66800  -15.40000 1.000 50.28988  ? 498 PHE   A CE1   1 
ATOM   3920 C  CE2   . PHE   A  1 506 ? 5.39800  -65.55100  -14.01000 1.000 47.76858  ? 498 PHE   A CE2   1 
ATOM   3921 C  CZ    . PHE   A  1 506 ? 6.53000  -65.74000  -14.76800 1.000 51.17818  ? 498 PHE   A CZ    1 
ATOM   3922 N  N     . GLU   A  1 507 ? 4.51600  -58.81300  -12.90800 1.000 49.25723  ? 499 GLU   A N     1 
ATOM   3923 C  CA    . GLU   A  1 507 ? 3.82500  -57.50100  -13.00700 1.000 47.83733  ? 499 GLU   A CA    1 
ATOM   3924 C  C     . GLU   A  1 507 ? 4.66800  -56.40200  -12.34600 1.000 46.53280  ? 499 GLU   A C     1 
ATOM   3925 O  O     . GLU   A  1 507 ? 4.07000  -55.46700  -11.77300 1.000 46.17181  ? 499 GLU   A O     1 
ATOM   3926 C  CB    . GLU   A  1 507 ? 2.44300  -57.59900  -12.36100 1.000 47.86053  ? 499 GLU   A CB    1 
ATOM   3927 C  CG    . GLU   A  1 507 ? 1.50700  -58.55700  -13.06800 1.000 46.19988  ? 499 GLU   A CG    1 
ATOM   3928 C  CD    . GLU   A  1 507 ? 0.04400  -58.36200  -12.71300 1.000 48.13990  ? 499 GLU   A CD    1 
ATOM   3929 O  OE1   . GLU   A  1 507 ? -0.24800 -58.10600  -11.52700 1.000 50.73793  ? 499 GLU   A OE1   1 
ATOM   3930 O  OE2   . GLU   A  1 507 ? -0.79800 -58.43600  -13.62800 1.000 49.12300  ? 499 GLU   A OE2   1 
ATOM   3931 N  N     . MET   A  1 508 ? 5.99900  -56.48800  -12.43600 1.000 38.83483  ? 500 MET   A N     1 
ATOM   3932 C  CA    . MET   A  1 508 ? 6.91800  -55.44700  -11.90100 1.000 45.66452  ? 500 MET   A CA    1 
ATOM   3933 C  C     . MET   A  1 508 ? 8.21500  -55.43400  -12.70400 1.000 48.34981  ? 500 MET   A C     1 
ATOM   3934 O  O     . MET   A  1 508 ? 8.69600  -56.47900  -13.13500 1.000 47.96051  ? 500 MET   A O     1 
ATOM   3935 C  CB    . MET   A  1 508 ? 7.23900  -55.68100  -10.42200 1.000 45.05244  ? 500 MET   A CB    1 
ATOM   3936 C  CG    . MET   A  1 508 ? 7.99800  -56.96600  -10.14500 1.000 47.19994  ? 500 MET   A CG    1 
ATOM   3937 S  SD    . MET   A  1 508 ? 8.42400  -57.13300  -8.40300  1.000 47.26717  ? 500 MET   A SD    1 
ATOM   3938 C  CE    . MET   A  1 508 ? 6.79400  -57.30500  -7.67700  1.000 45.87840  ? 500 MET   A CE    1 
ATOM   3939 N  N     . PRO   A  1 509 ? 8.82400  -54.24500  -12.91100 1.000 46.03413  ? 501 PRO   A N     1 
ATOM   3940 C  CA    . PRO   A  1 509 ? 10.08100 -54.14500  -13.64600 1.000 46.96212  ? 501 PRO   A CA    1 
ATOM   3941 C  C     . PRO   A  1 509 ? 11.29200 -54.48500  -12.76900 1.000 45.35752  ? 501 PRO   A C     1 
ATOM   3942 O  O     . PRO   A  1 509 ? 11.25200 -54.19200  -11.59400 1.000 48.84943  ? 501 PRO   A O     1 
ATOM   3943 C  CB    . PRO   A  1 509 ? 10.09900 -52.66700  -14.05400 1.000 50.80541  ? 501 PRO   A CB    1 
ATOM   3944 C  CG    . PRO   A  1 509 ? 9.41500  -51.97000  -12.89900 1.000 50.08877  ? 501 PRO   A CG    1 
ATOM   3945 C  CD    . PRO   A  1 509 ? 8.33900  -52.93600  -12.44700 1.000 44.78097  ? 501 PRO   A CD    1 
ATOM   3946 N  N     . TYR   A  1 510 ? 12.33300 -55.07000  -13.36600 1.000 48.42019  ? 502 TYR   A N     1 
ATOM   3947 C  CA    . TYR   A  1 510 ? 13.62900 -55.38200  -12.70900 1.000 52.27595  ? 502 TYR   A CA    1 
ATOM   3948 C  C     . TYR   A  1 510 ? 14.75400 -54.63100  -13.42400 1.000 48.90847  ? 502 TYR   A C     1 
ATOM   3949 O  O     . TYR   A  1 510 ? 14.75700 -54.61100  -14.66400 1.000 50.16244  ? 502 TYR   A O     1 
ATOM   3950 C  CB    . TYR   A  1 510 ? 13.89100 -56.88900  -12.72800 1.000 48.50543  ? 502 TYR   A CB    1 
ATOM   3951 C  CG    . TYR   A  1 510 ? 12.80900 -57.70800  -12.07600 1.000 48.11087  ? 502 TYR   A CG    1 
ATOM   3952 C  CD1   . TYR   A  1 510 ? 11.63900 -58.00200  -12.75500 1.000 47.30592  ? 502 TYR   A CD1   1 
ATOM   3953 C  CD2   . TYR   A  1 510 ? 12.94500 -58.17500  -10.78000 1.000 49.30632  ? 502 TYR   A CD2   1 
ATOM   3954 C  CE1   . TYR   A  1 510 ? 10.63200 -58.74700  -12.16500 1.000 47.87288  ? 502 TYR   A CE1   1 
ATOM   3955 C  CE2   . TYR   A  1 510 ? 11.94600 -58.91900  -10.17400 1.000 48.94022  ? 502 TYR   A CE2   1 
ATOM   3956 C  CZ    . TYR   A  1 510 ? 10.78600 -59.20600  -10.87000 1.000 42.34982  ? 502 TYR   A CZ    1 
ATOM   3957 O  OH    . TYR   A  1 510 ? 9.79400  -59.93700  -10.28800 1.000 49.01299  ? 502 TYR   A OH    1 
ATOM   3958 N  N     . VAL   A  1 511 ? 15.66400 -54.02300  -12.66000 1.000 47.82656  ? 503 VAL   A N     1 
ATOM   3959 C  CA    . VAL   A  1 511 ? 16.98600 -53.55000  -13.16600 1.000 52.45988  ? 503 VAL   A CA    1 
ATOM   3960 C  C     . VAL   A  1 511 ? 17.87000 -54.79100  -13.31800 1.000 52.68033  ? 503 VAL   A C     1 
ATOM   3961 O  O     . VAL   A  1 511 ? 17.93100 -55.59100  -12.36600 1.000 55.82921  ? 503 VAL   A O     1 
ATOM   3962 C  CB    . VAL   A  1 511 ? 17.62200 -52.49600  -12.23900 1.000 50.65771  ? 503 VAL   A CB    1 
ATOM   3963 C  CG1   . VAL   A  1 511 ? 19.08900 -52.25600  -12.56500 1.000 48.76164  ? 503 VAL   A CG1   1 
ATOM   3964 C  CG2   . VAL   A  1 511 ? 16.84800 -51.18700  -12.27200 1.000 50.99450  ? 503 VAL   A CG2   1 
ATOM   3965 N  N     . VAL   A  1 512 ? 18.50700 -54.95100  -14.47900 1.000 52.07542  ? 504 VAL   A N     1 
ATOM   3966 C  CA    . VAL   A  1 512 ? 19.30100 -56.16300  -14.83500 1.000 52.77965  ? 504 VAL   A CA    1 
ATOM   3967 C  C     . VAL   A  1 512 ? 20.22400 -55.81900  -16.00700 1.000 52.99321  ? 504 VAL   A C     1 
ATOM   3968 O  O     . VAL   A  1 512 ? 19.73700 -55.20300  -16.97100 1.000 51.15824  ? 504 VAL   A O     1 
ATOM   3969 C  CB    . VAL   A  1 512 ? 18.37300 -57.35100  -15.16800 1.000 56.29848  ? 504 VAL   A CB    1 
ATOM   3970 C  CG1   . VAL   A  1 512 ? 17.26400 -56.96700  -16.14000 1.000 49.58320  ? 504 VAL   A CG1   1 
ATOM   3971 C  CG2   . VAL   A  1 512 ? 19.14700 -58.55600  -15.68500 1.000 53.32697  ? 504 VAL   A CG2   1 
ATOM   3972 N  N     . ARG   A  1 513 ? 21.50200 -56.20000  -15.91900 1.000 51.76972  ? 505 ARG   A N     1 
ATOM   3973 C  CA    . ARG   A  1 513 ? 22.44300 -56.16000  -17.06800 1.000 56.29137  ? 505 ARG   A CA    1 
ATOM   3974 C  C     . ARG   A  1 513 ? 22.09500 -57.33600  -17.98800 1.000 58.41594  ? 505 ARG   A C     1 
ATOM   3975 O  O     . ARG   A  1 513 ? 22.75500 -58.38900  -17.88700 1.000 59.45045  ? 505 ARG   A O     1 
ATOM   3976 C  CB    . ARG   A  1 513 ? 23.90400 -56.18700  -16.60500 1.000 56.23991  ? 505 ARG   A CB    1 
ATOM   3977 C  CG    . ARG   A  1 513 ? 24.85400 -55.41900  -17.51500 1.000 61.90444  ? 505 ARG   A CG    1 
ATOM   3978 C  CD    . ARG   A  1 513 ? 25.08700 -56.03300  -18.89000 1.000 67.78533  ? 505 ARG   A CD    1 
ATOM   3979 N  NE    . ARG   A  1 513 ? 23.95100 -55.95200  -19.80700 1.000 62.93150  ? 505 ARG   A NE    1 
ATOM   3980 C  CZ    . ARG   A  1 513 ? 23.50500 -54.84300  -20.39800 1.000 64.05762  ? 505 ARG   A CZ    1 
ATOM   3981 N  NH1   . ARG   A  1 513 ? 24.07900 -53.67300  -20.17000 1.000 67.16169  ? 505 ARG   A NH1   1 
ATOM   3982 N  NH2   . ARG   A  1 513 ? 22.47000 -54.90700  -21.21700 1.000 59.72085  ? 505 ARG   A NH2   1 
ATOM   3983 N  N     . LEU   A  1 514 ? 21.08400 -57.14400  -18.84300 1.000 56.82342  ? 506 LEU   A N     1 
ATOM   3984 C  CA    . LEU   A  1 514 ? 20.57800 -58.15500  -19.81000 1.000 53.73976  ? 506 LEU   A CA    1 
ATOM   3985 C  C     . LEU   A  1 514 ? 21.78000 -58.70200  -20.58700 1.000 57.90743  ? 506 LEU   A C     1 
ATOM   3986 O  O     . LEU   A  1 514 ? 22.48100 -57.88800  -21.21500 1.000 61.49656  ? 506 LEU   A O     1 
ATOM   3987 C  CB    . LEU   A  1 514 ? 19.55500 -57.49700  -20.74400 1.000 53.73262  ? 506 LEU   A CB    1 
ATOM   3988 C  CG    . LEU   A  1 514 ? 18.34700 -56.84500  -20.06900 1.000 50.77074  ? 506 LEU   A CG    1 
ATOM   3989 C  CD1   . LEU   A  1 514 ? 17.67200 -55.85800  -21.00500 1.000 51.72648  ? 506 LEU   A CD1   1 
ATOM   3990 C  CD2   . LEU   A  1 514 ? 17.35000 -57.88800  -19.59600 1.000 52.58357  ? 506 LEU   A CD2   1 
ATOM   3991 N  N     . HIS   A  1 515 ? 22.04000 -60.01000  -20.50000 1.000 58.34617  ? 507 HIS   A N     1 
ATOM   3992 C  CA    . HIS   A  1 515 ? 23.26400 -60.65900  -21.04200 1.000 59.48363  ? 507 HIS   A CA    1 
ATOM   3993 C  C     . HIS   A  1 515 ? 22.88700 -61.77700  -22.01900 1.000 64.21816  ? 507 HIS   A C     1 
ATOM   3994 O  O     . HIS   A  1 515 ? 23.09900 -61.58100  -23.23300 1.000 69.56499  ? 507 HIS   A O     1 
ATOM   3995 C  CB    . HIS   A  1 515 ? 24.16300 -61.15300  -19.90500 1.000 59.32486  ? 507 HIS   A CB    1 
ATOM   3996 C  CG    . HIS   A  1 515 ? 25.50800 -61.58700  -20.37500 1.000 60.85381  ? 507 HIS   A CG    1 
ATOM   3997 N  ND1   . HIS   A  1 515 ? 26.47600 -60.68200  -20.76000 1.000 67.96004  ? 507 HIS   A ND1   1 
ATOM   3998 C  CD2   . HIS   A  1 515 ? 26.04400 -62.81400  -20.53600 1.000 63.78534  ? 507 HIS   A CD2   1 
ATOM   3999 C  CE1   . HIS   A  1 515 ? 27.55800 -61.33400  -21.13200 1.000 70.53200  ? 507 HIS   A CE1   1 
ATOM   4000 N  NE2   . HIS   A  1 515 ? 27.31900 -62.64400  -21.00300 1.000 70.57440  ? 507 HIS   A NE2   1 
ATOM   4001 N  N     . ASN   A  1 516 ? 22.38600 -62.91100  -21.51700 1.000 67.26257  ? 508 ASN   A N     1 
ATOM   4002 C  CA    . ASN   A  1 516 ? 21.87000 -64.02000  -22.36200 1.000 66.91053  ? 508 ASN   A CA    1 
ATOM   4003 C  C     . ASN   A  1 516 ? 20.43500 -63.66100  -22.76300 1.000 67.72051  ? 508 ASN   A C     1 
ATOM   4004 O  O     . ASN   A  1 516 ? 19.49700 -64.07100  -22.05100 1.000 67.55616  ? 508 ASN   A O     1 
ATOM   4005 C  CB    . ASN   A  1 516 ? 21.97700 -65.38400  -21.67000 1.000 68.36623  ? 508 ASN   A CB    1 
ATOM   4006 C  CG    . ASN   A  1 516 ? 21.63500 -66.54100  -22.58900 1.000 68.28318  ? 508 ASN   A CG    1 
ATOM   4007 O  OD1   . ASN   A  1 516 ? 21.71400 -66.42000  -23.81000 1.000 67.65191  ? 508 ASN   A OD1   1 
ATOM   4008 N  ND2   . ASN   A  1 516 ? 21.25500 -67.67000  -22.01400 1.000 69.05869  ? 508 ASN   A ND2   1 
ATOM   4009 N  N     . PHE   A  1 517 ? 20.28900 -62.88800  -23.84400 1.000 65.43884  ? 509 PHE   A N     1 
ATOM   4010 C  CA    . PHE   A  1 517 ? 18.98800 -62.41400  -24.38700 1.000 62.24770  ? 509 PHE   A CA    1 
ATOM   4011 C  C     . PHE   A  1 517 ? 19.13700 -62.10300  -25.88100 1.000 58.65332  ? 509 PHE   A C     1 
ATOM   4012 O  O     . PHE   A  1 517 ? 20.27100 -62.09600  -26.39300 1.000 62.84159  ? 509 PHE   A O     1 
ATOM   4013 C  CB    . PHE   A  1 517 ? 18.49100 -61.19900  -23.59800 1.000 56.79327  ? 509 PHE   A CB    1 
ATOM   4014 C  CG    . PHE   A  1 517 ? 19.09100 -59.87800  -24.00900 1.000 54.73556  ? 509 PHE   A CG    1 
ATOM   4015 C  CD1   . PHE   A  1 517 ? 20.45400 -59.64900  -23.89700 1.000 54.50405  ? 509 PHE   A CD1   1 
ATOM   4016 C  CD2   . PHE   A  1 517 ? 18.29100 -58.85600  -24.49900 1.000 54.10614  ? 509 PHE   A CD2   1 
ATOM   4017 C  CE1   . PHE   A  1 517 ? 21.00400 -58.43300  -24.27400 1.000 54.34300  ? 509 PHE   A CE1   1 
ATOM   4018 C  CE2   . PHE   A  1 517 ? 18.84300 -57.64100  -24.87500 1.000 51.91869  ? 509 PHE   A CE2   1 
ATOM   4019 C  CZ    . PHE   A  1 517 ? 20.19800 -57.43100  -24.76100 1.000 50.62550  ? 509 PHE   A CZ    1 
ATOM   4020 N  N     . HIS   A  1 518 ? 18.00900 -61.85100  -26.55000 1.000 56.95989  ? 510 HIS   A N     1 
ATOM   4021 C  CA    . HIS   A  1 518 ? 17.92500 -61.51700  -27.99500 1.000 56.45759  ? 510 HIS   A CA    1 
ATOM   4022 C  C     . HIS   A  1 518 ? 17.00800 -60.30400  -28.18100 1.000 54.97354  ? 510 HIS   A C     1 
ATOM   4023 O  O     . HIS   A  1 518 ? 15.80200 -60.43300  -27.90600 1.000 54.51566  ? 510 HIS   A O     1 
ATOM   4024 C  CB    . HIS   A  1 518 ? 17.44400 -62.74400  -28.78300 1.000 59.30054  ? 510 HIS   A CB    1 
ATOM   4025 C  CG    . HIS   A  1 518 ? 17.59500 -62.62300  -30.26200 1.000 60.63908  ? 510 HIS   A CG    1 
ATOM   4026 N  ND1   . HIS   A  1 518 ? 16.71300 -63.21600  -31.14300 1.000 58.06107  ? 510 HIS   A ND1   1 
ATOM   4027 C  CD2   . HIS   A  1 518 ? 18.51400 -61.98400  -31.01800 1.000 59.22803  ? 510 HIS   A CD2   1 
ATOM   4028 C  CE1   . HIS   A  1 518 ? 17.08600 -62.95700  -32.37800 1.000 56.28165  ? 510 HIS   A CE1   1 
ATOM   4029 N  NE2   . HIS   A  1 518 ? 18.18900 -62.20200  -32.32900 1.000 60.34380  ? 510 HIS   A NE2   1 
ATOM   4030 N  N     . GLN   A  1 519 ? 17.56700 -59.17100  -28.61700 1.000 53.17670  ? 511 GLN   A N     1 
ATOM   4031 C  CA    . GLN   A  1 519 ? 16.80000 -57.94400  -28.96500 1.000 53.98955  ? 511 GLN   A CA    1 
ATOM   4032 C  C     . GLN   A  1 519 ? 16.08700 -58.19200  -30.29900 1.000 54.38734  ? 511 GLN   A C     1 
ATOM   4033 O  O     . GLN   A  1 519 ? 16.78500 -58.44400  -31.29800 1.000 53.20351  ? 511 GLN   A O     1 
ATOM   4034 C  CB    . GLN   A  1 519 ? 17.73000 -56.72900  -29.01000 1.000 55.51001  ? 511 GLN   A CB    1 
ATOM   4035 C  CG    . GLN   A  1 519 ? 16.99300 -55.39600  -29.03400 1.000 60.81877  ? 511 GLN   A CG    1 
ATOM   4036 C  CD    . GLN   A  1 519 ? 17.71900 -54.30600  -28.28100 1.000 57.96395  ? 511 GLN   A CD    1 
ATOM   4037 O  OE1   . GLN   A  1 519 ? 18.20400 -53.33900  -28.86500 1.000 64.35305  ? 511 GLN   A OE1   1 
ATOM   4038 N  NE2   . GLN   A  1 519 ? 17.79900 -54.45700  -26.96800 1.000 51.40217  ? 511 GLN   A NE2   1 
ATOM   4039 N  N     . LEU   A  1 520 ? 14.75200 -58.14500  -30.29900 1.000 50.59020  ? 512 LEU   A N     1 
ATOM   4040 C  CA    . LEU   A  1 520 ? 13.89100 -58.61300  -31.41900 1.000 54.37338  ? 512 LEU   A CA    1 
ATOM   4041 C  C     . LEU   A  1 520 ? 13.50800 -57.44600  -32.33600 1.000 57.47723  ? 512 LEU   A C     1 
ATOM   4042 O  O     . LEU   A  1 520 ? 12.88200 -57.71200  -33.38400 1.000 60.65183  ? 512 LEU   A O     1 
ATOM   4043 C  CB    . LEU   A  1 520 ? 12.63800 -59.27800  -30.84000 1.000 55.65253  ? 512 LEU   A CB    1 
ATOM   4044 C  CG    . LEU   A  1 520 ? 12.87800 -60.33900  -29.76700 1.000 54.83240  ? 512 LEU   A CG    1 
ATOM   4045 C  CD1   . LEU   A  1 520 ? 11.56400 -60.97400  -29.34400 1.000 47.47078  ? 512 LEU   A CD1   1 
ATOM   4046 C  CD2   . LEU   A  1 520 ? 13.85500 -61.40300  -30.24600 1.000 56.05677  ? 512 LEU   A CD2   1 
ATOM   4047 N  N     . SER   A  1 521 ? 13.85300 -56.21000  -31.96300 1.000 55.58708  ? 513 SER   A N     1 
ATOM   4048 C  CA    . SER   A  1 521 ? 13.57800 -54.98200  -32.75700 1.000 58.38386  ? 513 SER   A CA    1 
ATOM   4049 C  C     . SER   A  1 521 ? 14.45600 -53.83000  -32.25600 1.000 60.27449  ? 513 SER   A C     1 
ATOM   4050 O  O     . SER   A  1 521 ? 14.95500 -53.91500  -31.11900 1.000 59.33564  ? 513 SER   A O     1 
ATOM   4051 C  CB    . SER   A  1 521 ? 12.11200 -54.63100  -32.70000 1.000 53.92032  ? 513 SER   A CB    1 
ATOM   4052 O  OG    . SER   A  1 521 ? 11.78400 -53.64100  -33.66100 1.000 57.74568  ? 513 SER   A OG    1 
ATOM   4053 N  N     . ALA   A  1 522 ? 14.64400 -52.79700  -33.08000 1.000 56.22329  ? 514 ALA   A N     1 
ATOM   4054 C  CA    . ALA   A  1 522 ? 15.41700 -51.58200  -32.73200 1.000 53.51009  ? 514 ALA   A CA    1 
ATOM   4055 C  C     . ALA   A  1 522 ? 14.66500 -50.82300  -31.64300 1.000 58.80582  ? 514 ALA   A C     1 
ATOM   4056 O  O     . ALA   A  1 522 ? 13.45400 -50.63500  -31.75700 1.000 59.66615  ? 514 ALA   A O     1 
ATOM   4057 C  CB    . ALA   A  1 522 ? 15.63300 -50.72500  -33.95500 1.000 54.27174  ? 514 ALA   A CB    1 
ATOM   4058 N  N     . PRO   A  1 523 ? 15.33800 -50.37900  -30.55500 1.000 55.99283  ? 515 PRO   A N     1 
ATOM   4059 C  CA    . PRO   A  1 523 ? 14.67500 -49.59700  -29.51300 1.000 56.89481  ? 515 PRO   A CA    1 
ATOM   4060 C  C     . PRO   A  1 523 ? 13.93600 -48.38200  -30.09500 1.000 58.39999  ? 515 PRO   A C     1 
ATOM   4061 O  O     . PRO   A  1 523 ? 14.48300 -47.73000  -30.96900 1.000 58.55306  ? 515 PRO   A O     1 
ATOM   4062 C  CB    . PRO   A  1 523 ? 15.82300 -49.16700  -28.58500 1.000 58.27497  ? 515 PRO   A CB    1 
ATOM   4063 C  CG    . PRO   A  1 523 ? 16.88500 -50.22600  -28.79700 1.000 60.33171  ? 515 PRO   A CG    1 
ATOM   4064 C  CD    . PRO   A  1 523 ? 16.76000 -50.61700  -30.25500 1.000 58.59298  ? 515 PRO   A CD    1 
ATOM   4065 N  N     . GLN   A  1 524 ? 12.71200 -48.13900  -29.61400 1.000 54.55631  ? 516 GLN   A N     1 
ATOM   4066 C  CA    . GLN   A  1 524 ? 11.84500 -46.99600  -30.00900 1.000 56.93326  ? 516 GLN   A CA    1 
ATOM   4067 C  C     . GLN   A  1 524 ? 11.49500 -46.19300  -28.76000 1.000 58.28559  ? 516 GLN   A C     1 
ATOM   4068 O  O     . GLN   A  1 524 ? 11.42800 -46.74800  -27.66500 1.000 56.78198  ? 516 GLN   A O     1 
ATOM   4069 C  CB    . GLN   A  1 524 ? 10.58100 -47.49500  -30.71400 1.000 52.23210  ? 516 GLN   A CB    1 
ATOM   4070 C  CG    . GLN   A  1 524 ? 10.85000 -48.16200  -32.05600 1.000 51.88882  ? 516 GLN   A CG    1 
ATOM   4071 C  CD    . GLN   A  1 524 ? 9.57800  -48.55200  -32.76900 1.000 53.59582  ? 516 GLN   A CD    1 
ATOM   4072 O  OE1   . GLN   A  1 524 ? 8.61300  -47.79400  -32.82300 1.000 55.27049  ? 516 GLN   A OE1   1 
ATOM   4073 N  NE2   . GLN   A  1 524 ? 9.57200  -49.74900  -33.33100 1.000 53.33182  ? 516 GLN   A NE2   1 
ATOM   4074 N  N     . PRO   A  1 525 ? 11.25100 -44.86800  -28.88700 1.000 54.28257  ? 517 PRO   A N     1 
ATOM   4075 C  CA    . PRO   A  1 525 ? 10.95400 -44.02200  -27.73400 1.000 51.33419  ? 517 PRO   A CA    1 
ATOM   4076 C  C     . PRO   A  1 525 ? 9.54600  -44.27900  -27.17800 1.000 59.92886  ? 517 PRO   A C     1 
ATOM   4077 O  O     . PRO   A  1 525 ? 8.63100  -44.45700  -27.96800 1.000 53.52749  ? 517 PRO   A O     1 
ATOM   4078 C  CB    . PRO   A  1 525 ? 11.07100 -42.60400  -28.30400 1.000 53.59600  ? 517 PRO   A CB    1 
ATOM   4079 C  CG    . PRO   A  1 525 ? 10.67000 -42.76500  -29.75100 1.000 59.92708  ? 517 PRO   A CG    1 
ATOM   4080 C  CD    . PRO   A  1 525 ? 11.22000 -44.11800  -30.15200 1.000 53.70014  ? 517 PRO   A CD    1 
ATOM   4081 N  N     . CYS   A  1 526 ? 9.41900  -44.28200  -25.84600 1.000 58.58464  ? 518 CYS   A N     1 
ATOM   4082 C  CA    . CYS   A  1 526 ? 8.16900  -44.57300  -25.09400 1.000 54.51265  ? 518 CYS   A CA    1 
ATOM   4083 C  C     . CYS   A  1 526 ? 7.59000  -43.27200  -24.52100 1.000 58.01239  ? 518 CYS   A C     1 
ATOM   4084 O  O     . CYS   A  1 526 ? 6.56900  -42.79900  -25.06300 1.000 56.73976  ? 518 CYS   A O     1 
ATOM   4085 C  CB    . CYS   A  1 526 ? 8.42500  -45.59800  -23.99600 1.000 53.32396  ? 518 CYS   A CB    1 
ATOM   4086 S  SG    . CYS   A  1 526 ? 6.91900  -46.11200  -23.13100 1.000 52.97645  ? 518 CYS   A SG    1 
ATOM   4087 N  N     . PHE   A  1 527 ? 8.21900  -42.71300  -23.47800 1.000 59.62193  ? 519 PHE   A N     1 
ATOM   4088 C  CA    . PHE   A  1 527 ? 7.76400  -41.49300  -22.75900 1.000 54.59337  ? 519 PHE   A CA    1 
ATOM   4089 C  C     . PHE   A  1 527 ? 8.87800  -40.44400  -22.75000 1.000 53.57351  ? 519 PHE   A C     1 
ATOM   4090 O  O     . PHE   A  1 527 ? 10.04800 -40.81000  -22.53000 1.000 54.13452  ? 519 PHE   A O     1 
ATOM   4091 C  CB    . PHE   A  1 527 ? 7.36100  -41.81400  -21.31800 1.000 52.53313  ? 519 PHE   A CB    1 
ATOM   4092 C  CG    . PHE   A  1 527 ? 6.28500  -42.85900  -21.16900 1.000 54.51395  ? 519 PHE   A CG    1 
ATOM   4093 C  CD1   . PHE   A  1 527 ? 5.11300  -42.78500  -21.90500 1.000 52.76816  ? 519 PHE   A CD1   1 
ATOM   4094 C  CD2   . PHE   A  1 527 ? 6.43400  -43.90200  -20.27000 1.000 54.88636  ? 519 PHE   A CD2   1 
ATOM   4095 C  CE1   . PHE   A  1 527 ? 4.12300  -43.74400  -21.76000 1.000 55.01964  ? 519 PHE   A CE1   1 
ATOM   4096 C  CE2   . PHE   A  1 527 ? 5.44100  -44.85900  -20.12500 1.000 52.18487  ? 519 PHE   A CE2   1 
ATOM   4097 C  CZ    . PHE   A  1 527 ? 4.28800  -44.77800  -20.86900 1.000 52.76494  ? 519 PHE   A CZ    1 
ATOM   4098 N  N     . THR   A  1 528 ? 8.50600  -39.18100  -22.97500 1.000 54.13213  ? 520 THR   A N     1 
ATOM   4099 C  CA    . THR   A  1 528 ? 9.40100  -37.99300  -22.93100 1.000 55.93581  ? 520 THR   A CA    1 
ATOM   4100 C  C     . THR   A  1 528 ? 8.87000  -37.01600  -21.87800 1.000 56.99964  ? 520 THR   A C     1 
ATOM   4101 O  O     . THR   A  1 528 ? 7.63900  -36.95300  -21.70000 1.000 57.21373  ? 520 THR   A O     1 
ATOM   4102 C  CB    . THR   A  1 528 ? 9.50700  -37.32800  -24.31100 1.000 58.02570  ? 520 THR   A CB    1 
ATOM   4103 O  OG1   . THR   A  1 528 ? 9.90900  -38.32900  -25.24600 1.000 57.04366  ? 520 THR   A OG1   1 
ATOM   4104 C  CG2   . THR   A  1 528 ? 10.48800 -36.17500  -24.34900 1.000 60.06925  ? 520 THR   A CG2   1 
ATOM   4105 N  N     . PHE   A  1 529 ? 9.77000  -36.29200  -21.21000 1.000 57.81993  ? 521 PHE   A N     1 
ATOM   4106 C  CA    . PHE   A  1 529 ? 9.45100  -35.19400  -20.26200 1.000 59.37830  ? 521 PHE   A CA    1 
ATOM   4107 C  C     . PHE   A  1 529 ? 10.42600 -34.03800  -20.49400 1.000 61.67606  ? 521 PHE   A C     1 
ATOM   4108 O  O     . PHE   A  1 529 ? 11.61900 -34.30400  -20.74300 1.000 64.19790  ? 521 PHE   A O     1 
ATOM   4109 C  CB    . PHE   A  1 529 ? 9.51200  -35.68700  -18.81500 1.000 58.00083  ? 521 PHE   A CB    1 
ATOM   4110 C  CG    . PHE   A  1 529 ? 8.43600  -36.67800  -18.45100 1.000 61.74650  ? 521 PHE   A CG    1 
ATOM   4111 C  CD1   . PHE   A  1 529 ? 7.19200  -36.24600  -18.01900 1.000 60.92235  ? 521 PHE   A CD1   1 
ATOM   4112 C  CD2   . PHE   A  1 529 ? 8.66300  -38.04300  -18.55600 1.000 57.71292  ? 521 PHE   A CD2   1 
ATOM   4113 C  CE1   . PHE   A  1 529 ? 6.19900  -37.15800  -17.69600 1.000 60.75813  ? 521 PHE   A CE1   1 
ATOM   4114 C  CE2   . PHE   A  1 529 ? 7.67000  -38.95300  -18.23200 1.000 53.72080  ? 521 PHE   A CE2   1 
ATOM   4115 C  CZ    . PHE   A  1 529 ? 6.44000  -38.50900  -17.80300 1.000 56.50856  ? 521 PHE   A CZ    1 
ATOM   4116 N  N     . SER   A  1 530 ? 9.91500  -32.80500  -20.42900 1.000 64.20192  ? 522 SER   A N     1 
ATOM   4117 C  CA    . SER   A  1 530 ? 10.68100 -31.54000  -20.56900 1.000 66.95651  ? 522 SER   A CA    1 
ATOM   4118 C  C     . SER   A  1 530 ? 10.59100 -30.75400  -19.25800 1.000 68.78756  ? 522 SER   A C     1 
ATOM   4119 O  O     . SER   A  1 530 ? 9.54800  -30.86100  -18.58200 1.000 69.87507  ? 522 SER   A O     1 
ATOM   4120 C  CB    . SER   A  1 530 ? 10.17500 -30.72600  -21.73400 1.000 69.51539  ? 522 SER   A CB    1 
ATOM   4121 O  OG    . SER   A  1 530 ? 10.19800 -31.48500  -22.93400 1.000 74.09142  ? 522 SER   A OG    1 
ATOM   4122 N  N     . HIS   A  1 531 ? 11.64500 -30.00500  -18.91800 1.000 70.97989  ? 523 HIS   A N     1 
ATOM   4123 C  CA    . HIS   A  1 531 ? 11.73000 -29.13700  -17.71100 1.000 71.15641  ? 523 HIS   A CA    1 
ATOM   4124 C  C     . HIS   A  1 531 ? 12.45400 -27.83900  -18.06000 1.000 74.49285  ? 523 HIS   A C     1 
ATOM   4125 O  O     . HIS   A  1 531 ? 13.53500 -27.87800  -18.64100 1.000 74.72958  ? 523 HIS   A O     1 
ATOM   4126 C  CB    . HIS   A  1 531 ? 12.40000 -29.89800  -16.55900 1.000 68.99448  ? 523 HIS   A CB    1 
ATOM   4127 C  CG    . HIS   A  1 531 ? 11.62300 -31.09900  -16.14300 1.000 67.33573  ? 523 HIS   A CG    1 
ATOM   4128 N  ND1   . HIS   A  1 531 ? 10.39400 -30.99800  -15.52300 1.000 70.44932  ? 523 HIS   A ND1   1 
ATOM   4129 C  CD2   . HIS   A  1 531 ? 11.86800 -32.41900  -16.29400 1.000 63.93009  ? 523 HIS   A CD2   1 
ATOM   4130 C  CE1   . HIS   A  1 531 ? 9.92000  -32.20600  -15.29700 1.000 68.52544  ? 523 HIS   A CE1   1 
ATOM   4131 N  NE2   . HIS   A  1 531 ? 10.80600 -33.09600  -15.76100 1.000 61.81112  ? 523 HIS   A NE2   1 
ATOM   4132 N  N     . PRO   A  1 532 ? 11.89300 -26.65000  -17.73400 1.000 77.40761  ? 524 PRO   A N     1 
ATOM   4133 C  CA    . PRO   A  1 532 ? 10.58500 -26.53800  -17.08500 1.000 81.35125  ? 524 PRO   A CA    1 
ATOM   4134 C  C     . PRO   A  1 532 ? 9.42100  -26.95300  -17.99900 1.000 87.70835  ? 524 PRO   A C     1 
ATOM   4135 O  O     . PRO   A  1 532 ? 9.52700  -26.77700  -19.19800 1.000 89.80307  ? 524 PRO   A O     1 
ATOM   4136 C  CB    . PRO   A  1 532 ? 10.48200 -25.04400  -16.74000 1.000 82.32918  ? 524 PRO   A CB    1 
ATOM   4137 C  CG    . PRO   A  1 532 ? 11.36700 -24.36600  -17.76200 1.000 83.67675  ? 524 PRO   A CG    1 
ATOM   4138 C  CD    . PRO   A  1 532 ? 12.50900 -25.33600  -17.97800 1.000 81.02619  ? 524 PRO   A CD    1 
ATOM   4139 N  N     . ASN   A  1 533 ? 8.35600  -27.50300  -17.40900 1.000 84.29672  ? 525 ASN   A N     1 
ATOM   4140 C  CA    . ASN   A  1 533 ? 7.11600  -27.92000  -18.11600 1.000 95.91895  ? 525 ASN   A CA    1 
ATOM   4141 C  C     . ASN   A  1 533 ? 6.22300  -26.69000  -18.32800 1.000 102.80046 ? 525 ASN   A C     1 
ATOM   4142 O  O     . ASN   A  1 533 ? 5.29200  -26.49200  -17.52200 1.000 107.72311 ? 525 ASN   A O     1 
ATOM   4143 C  CB    . ASN   A  1 533 ? 6.38800  -29.03200  -17.35400 1.000 91.53202  ? 525 ASN   A CB    1 
ATOM   4144 C  CG    . ASN   A  1 533 ? 5.10300  -29.47500  -18.02300 1.000 102.50731 ? 525 ASN   A CG    1 
ATOM   4145 O  OD1   . ASN   A  1 533 ? 4.11700  -29.76700  -17.35100 1.000 104.16481 ? 525 ASN   A OD1   1 
ATOM   4146 N  ND2   . ASN   A  1 533 ? 5.09900  -29.51800  -19.34500 1.000 107.56093 ? 525 ASN   A ND2   1 
ATOM   4147 N  N     . ARG   A  1 534 ? 6.50100  -25.90000  -19.37300 1.000 111.80313 ? 526 ARG   A N     1 
ATOM   4148 C  CA    . ARG   A  1 534 ? 5.72100  -24.68500  -19.74900 1.000 120.48450 ? 526 ARG   A CA    1 
ATOM   4149 C  C     . ARG   A  1 534 ? 4.40700  -25.12600  -20.41100 1.000 129.41801 ? 526 ARG   A C     1 
ATOM   4150 O  O     . ARG   A  1 534 ? 4.26200  -24.94300  -21.64000 1.000 128.74589 ? 526 ARG   A O     1 
ATOM   4151 C  CB    . ARG   A  1 534 ? 6.54500  -23.76300  -20.65600 1.000 124.04061 ? 526 ARG   A CB    1 
ATOM   4152 C  CG    . ARG   A  1 534 ? 7.74400  -23.12500  -19.96800 1.000 118.07657 ? 526 ARG   A CG    1 
ATOM   4153 C  CD    . ARG   A  1 534 ? 8.27300  -21.90300  -20.69800 1.000 123.46167 ? 526 ARG   A CD    1 
ATOM   4154 N  NE    . ARG   A  1 534 ? 7.42600  -20.72900  -20.51800 1.000 125.90414 ? 526 ARG   A NE    1 
ATOM   4155 C  CZ    . ARG   A  1 534 ? 7.73300  -19.49200  -20.91100 1.000 128.92949 ? 526 ARG   A CZ    1 
ATOM   4156 N  NH1   . ARG   A  1 534 ? 8.88200  -19.24000  -21.51700 1.000 123.41537 ? 526 ARG   A NH1   1 
ATOM   4157 N  NH2   . ARG   A  1 534 ? 6.88300  -18.50200  -20.69200 1.000 134.05052 ? 526 ARG   A NH2   1 
ATOM   4158 N  N     . ASP   A  1 535 ? 3.53600  -25.76700  -19.62300 1.000 121.45705 ? 527 ASP   A N     1 
ATOM   4159 C  CA    . ASP   A  1 535 ? 2.22100  -26.23600  -20.13700 1.000 119.23020 ? 527 ASP   A CA    1 
ATOM   4160 C  C     . ASP   A  1 535 ? 1.20300  -26.19300  -18.99300 1.000 114.15288 ? 527 ASP   A C     1 
ATOM   4161 O  O     . ASP   A  1 535 ? 1.53600  -25.57500  -17.96500 1.000 110.51325 ? 527 ASP   A O     1 
ATOM   4162 C  CB    . ASP   A  1 535 ? 2.31400  -27.63800  -20.73900 1.000 118.44161 ? 527 ASP   A CB    1 
ATOM   4163 C  CG    . ASP   A  1 535 ? 1.02200  -28.09400  -21.39200 1.000 125.99668 ? 527 ASP   A CG    1 
ATOM   4164 O  OD1   . ASP   A  1 535 ? 0.09300  -28.47300  -20.65200 1.000 131.79556 ? 527 ASP   A OD1   1 
ATOM   4165 O  OD2   . ASP   A  1 535 ? 0.95500  -28.06600  -22.63400 1.000 115.65883 ? 527 ASP   A OD2   1 
ATOM   4166 N  N     . ASP   A  1 539 ? -0.55600 -33.32100  -17.99100 1.000 74.31984  ? 531 ASP   A N     1 
ATOM   4167 C  CA    . ASP   A  1 539 ? -0.10800 -33.91500  -16.69900 1.000 70.44194  ? 531 ASP   A CA    1 
ATOM   4168 C  C     . ASP   A  1 539 ? 1.05900  -34.87600  -16.97700 1.000 68.10782  ? 531 ASP   A C     1 
ATOM   4169 O  O     . ASP   A  1 539 ? 1.59100  -34.84100  -18.10200 1.000 69.80069  ? 531 ASP   A O     1 
ATOM   4170 C  CB    . ASP   A  1 539 ? -1.29100 -34.56300  -15.96900 1.000 73.72827  ? 531 ASP   A CB    1 
ATOM   4171 C  CG    . ASP   A  1 539 ? -1.94800 -35.70600  -16.72300 1.000 69.37259  ? 531 ASP   A CG    1 
ATOM   4172 O  OD1   . ASP   A  1 539 ? -1.21200 -36.57900  -17.20900 1.000 71.54244  ? 531 ASP   A OD1   1 
ATOM   4173 O  OD2   . ASP   A  1 539 ? -3.19100 -35.70700  -16.82300 1.000 74.50436  ? 531 ASP   A OD2   1 
ATOM   4174 N  N     . ASN   A  1 540 ? 1.45700  -35.68400  -15.98900 1.000 61.89680  ? 532 ASN   A N     1 
ATOM   4175 C  CA    . ASN   A  1 540 ? 2.62500  -36.60400  -16.07900 1.000 61.62700  ? 532 ASN   A CA    1 
ATOM   4176 C  C     . ASN   A  1 540 ? 2.16300  -38.04200  -16.36500 1.000 60.37729  ? 532 ASN   A C     1 
ATOM   4177 O  O     . ASN   A  1 540 ? 3.04100  -38.90700  -16.54100 1.000 58.74770  ? 532 ASN   A O     1 
ATOM   4178 C  CB    . ASN   A  1 540 ? 3.49100  -36.54000  -14.81800 1.000 62.46561  ? 532 ASN   A CB    1 
ATOM   4179 C  CG    . ASN   A  1 540 ? 4.30800  -35.26900  -14.72400 1.000 64.14681  ? 532 ASN   A CG    1 
ATOM   4180 O  OD1   . ASN   A  1 540 ? 4.93100  -34.84900  -15.69700 1.000 67.73763  ? 532 ASN   A OD1   1 
ATOM   4181 N  ND2   . ASN   A  1 540 ? 4.32200  -34.65700  -13.55300 1.000 69.48255  ? 532 ASN   A ND2   1 
ATOM   4182 N  N     . ASN   A  1 541 ? 0.84900  -38.29200  -16.41200 1.000 59.31387  ? 533 ASN   A N     1 
ATOM   4183 C  CA    . ASN   A  1 541 ? 0.26900  -39.58300  -16.87100 1.000 57.04815  ? 533 ASN   A CA    1 
ATOM   4184 C  C     . ASN   A  1 541 ? 0.42300  -39.67800  -18.39300 1.000 63.48921  ? 533 ASN   A C     1 
ATOM   4185 O  O     . ASN   A  1 541 ? 0.27300  -38.64600  -19.07200 1.000 64.45436  ? 533 ASN   A O     1 
ATOM   4186 C  CB    . ASN   A  1 541 ? -1.19600 -39.74700  -16.45800 1.000 59.25903  ? 533 ASN   A CB    1 
ATOM   4187 C  CG    . ASN   A  1 541 ? -1.37700 -39.99700  -14.97700 1.000 62.14777  ? 533 ASN   A CG    1 
ATOM   4188 O  OD1   . ASN   A  1 541 ? -0.42700 -40.33600  -14.27400 1.000 64.31813  ? 533 ASN   A OD1   1 
ATOM   4189 N  ND2   . ASN   A  1 541 ? -2.59900 -39.84200  -14.49600 1.000 68.22540  ? 533 ASN   A ND2   1 
ATOM   4190 N  N     . ARG   A  1 542 ? 0.71200  -40.87600  -18.90400 1.000 64.96054  ? 534 ARG   A N     1 
ATOM   4191 C  CA    . ARG   A  1 542 ? 1.03600  -41.11600  -20.33600 1.000 61.30999  ? 534 ARG   A CA    1 
ATOM   4192 C  C     . ARG   A  1 542 ? 0.38600  -42.42000  -20.81400 1.000 60.52402  ? 534 ARG   A C     1 
ATOM   4193 O  O     . ARG   A  1 542 ? 0.10100  -43.28900  -19.97000 1.000 64.78815  ? 534 ARG   A O     1 
ATOM   4194 C  CB    . ARG   A  1 542 ? 2.55300  -41.19700  -20.53000 1.000 57.97109  ? 534 ARG   A CB    1 
ATOM   4195 C  CG    . ARG   A  1 542 ? 3.31800  -39.94300  -20.13100 1.000 56.61959  ? 534 ARG   A CG    1 
ATOM   4196 C  CD    . ARG   A  1 542 ? 2.98200  -38.75700  -21.01100 1.000 58.22600  ? 534 ARG   A CD    1 
ATOM   4197 N  NE    . ARG   A  1 542 ? 4.11800  -37.85900  -21.16500 1.000 58.81082  ? 534 ARG   A NE    1 
ATOM   4198 C  CZ    . ARG   A  1 542 ? 4.34400  -36.76800  -20.44100 1.000 55.89178  ? 534 ARG   A CZ    1 
ATOM   4199 N  NH1   . ARG   A  1 542 ? 3.50900  -36.40300  -19.48200 1.000 60.69756  ? 534 ARG   A NH1   1 
ATOM   4200 N  NH2   . ARG   A  1 542 ? 5.41800  -36.03800  -20.68000 1.000 56.76483  ? 534 ARG   A NH2   1 
ATOM   4201 N  N     . TYR   A  1 543 ? 0.17300  -42.53100  -22.12800 1.000 64.20067  ? 535 TYR   A N     1 
ATOM   4202 C  CA    . TYR   A  1 543 ? -0.26700 -43.75400  -22.84700 1.000 56.73364  ? 535 TYR   A CA    1 
ATOM   4203 C  C     . TYR   A  1 543 ? 0.40900  -43.75400  -24.22000 1.000 60.51417  ? 535 TYR   A C     1 
ATOM   4204 O  O     . TYR   A  1 543 ? 0.20700  -42.79600  -24.98400 1.000 66.41018  ? 535 TYR   A O     1 
ATOM   4205 C  CB    . TYR   A  1 543 ? -1.79500 -43.80600  -22.93900 1.000 55.92060  ? 535 TYR   A CB    1 
ATOM   4206 C  CG    . TYR   A  1 543 ? -2.36100 -44.85200  -23.86700 1.000 60.39815  ? 535 TYR   A CG    1 
ATOM   4207 C  CD1   . TYR   A  1 543 ? -1.78300 -46.10800  -23.98900 1.000 58.67023  ? 535 TYR   A CD1   1 
ATOM   4208 C  CD2   . TYR   A  1 543 ? -3.50700 -44.59700  -24.60400 1.000 65.95479  ? 535 TYR   A CD2   1 
ATOM   4209 C  CE1   . TYR   A  1 543 ? -2.31500 -47.07000  -24.83400 1.000 57.60995  ? 535 TYR   A CE1   1 
ATOM   4210 C  CE2   . TYR   A  1 543 ? -4.05300 -45.54800  -25.45200 1.000 63.36857  ? 535 TYR   A CE2   1 
ATOM   4211 C  CZ    . TYR   A  1 543 ? -3.45600 -46.79100  -25.56600 1.000 62.15075  ? 535 TYR   A CZ    1 
ATOM   4212 O  OH    . TYR   A  1 543 ? -3.99400 -47.72600  -26.40100 1.000 62.48734  ? 535 TYR   A OH    1 
ATOM   4213 N  N     . CYS   A  1 544 ? 1.21100  -44.78400  -24.49600 1.000 59.59076  ? 536 CYS   A N     1 
ATOM   4214 C  CA    . CYS   A  1 544 ? 2.05000  -44.91300  -25.71600 1.000 58.02947  ? 536 CYS   A CA    1 
ATOM   4215 C  C     . CYS   A  1 544 ? 1.88400  -46.31200  -26.31500 1.000 57.38611  ? 536 CYS   A C     1 
ATOM   4216 O  O     . CYS   A  1 544 ? 2.11300  -47.29500  -25.58100 1.000 60.50951  ? 536 CYS   A O     1 
ATOM   4217 C  CB    . CYS   A  1 544 ? 3.51800  -44.66900  -25.39400 1.000 53.85255  ? 536 CYS   A CB    1 
ATOM   4218 S  SG    . CYS   A  1 544 ? 4.60500  -44.85500  -26.83100 1.000 62.12509  ? 536 CYS   A SG    1 
ATOM   4219 N  N     . THR   A  1 545 ? 1.50300  -46.38100  -27.59400 1.000 59.32693  ? 537 THR   A N     1 
ATOM   4220 C  CA    . THR   A  1 545 ? 1.42900  -47.62200  -28.40900 1.000 56.36817  ? 537 THR   A CA    1 
ATOM   4221 C  C     . THR   A  1 545 ? 2.67600  -47.67900  -29.29600 1.000 55.66543  ? 537 THR   A C     1 
ATOM   4222 O  O     . THR   A  1 545 ? 2.96300  -46.66500  -29.95600 1.000 63.13445  ? 537 THR   A O     1 
ATOM   4223 C  CB    . THR   A  1 545 ? 0.13500  -47.66500  -29.23000 1.000 53.12912  ? 537 THR   A CB    1 
ATOM   4224 O  OG1   . THR   A  1 545 ? -0.96400 -47.55600  -28.32600 1.000 55.55651  ? 537 THR   A OG1   1 
ATOM   4225 C  CG2   . THR   A  1 545 ? -0.00900 -48.92600  -30.05300 1.000 51.11710  ? 537 THR   A CG2   1 
ATOM   4226 N  N     . LEU   A  1 546 ? 3.39200  -48.80600  -29.29000 1.000 53.63908  ? 538 LEU   A N     1 
ATOM   4227 C  CA    . LEU   A  1 546 ? 4.58500  -49.04800  -30.14500 1.000 54.41628  ? 538 LEU   A CA    1 
ATOM   4228 C  C     . LEU   A  1 546 ? 4.32800  -50.26300  -31.04300 1.000 54.26370  ? 538 LEU   A C     1 
ATOM   4229 O  O     . LEU   A  1 546 ? 3.66100  -51.21100  -30.58700 1.000 53.78065  ? 538 LEU   A O     1 
ATOM   4230 C  CB    . LEU   A  1 546 ? 5.81400  -49.26100  -29.25500 1.000 52.32943  ? 538 LEU   A CB    1 
ATOM   4231 C  CG    . LEU   A  1 546 ? 6.14300  -48.12100  -28.29100 1.000 55.67134  ? 538 LEU   A CG    1 
ATOM   4232 C  CD1   . LEU   A  1 546 ? 7.38400  -48.44200  -27.47300 1.000 52.06980  ? 538 LEU   A CD1   1 
ATOM   4233 C  CD2   . LEU   A  1 546 ? 6.33200  -46.80700  -29.03300 1.000 58.94476  ? 538 LEU   A CD2   1 
ATOM   4234 N  N     . GLU   A  1 547 ? 4.82300  -50.20800  -32.28300 1.000 59.48526  ? 539 GLU   A N     1 
ATOM   4235 C  CA    . GLU   A  1 547 ? 4.79300  -51.32400  -33.26600 1.000 56.93286  ? 539 GLU   A CA    1 
ATOM   4236 C  C     . GLU   A  1 547 ? 6.24100  -51.68900  -33.61300 1.000 53.45584  ? 539 GLU   A C     1 
ATOM   4237 O  O     . GLU   A  1 547 ? 6.94500  -50.83000  -34.17500 1.000 54.28589  ? 539 GLU   A O     1 
ATOM   4238 C  CB    . GLU   A  1 547 ? 3.98100  -50.93000  -34.50000 1.000 54.10639  ? 539 GLU   A CB    1 
ATOM   4239 C  CG    . GLU   A  1 547 ? 2.50100  -50.74100  -34.21600 1.000 53.77263  ? 539 GLU   A CG    1 
ATOM   4240 C  CD    . GLU   A  1 547 ? 1.59300  -50.98700  -35.40900 1.000 72.24817  ? 539 GLU   A CD    1 
ATOM   4241 O  OE1   . GLU   A  1 547 ? 1.66300  -50.20900  -36.38500 1.000 76.85210  ? 539 GLU   A OE1   1 
ATOM   4242 O  OE2   . GLU   A  1 547 ? 0.82900  -51.97000  -35.36800 1.000 77.92166  ? 539 GLU   A OE2   1 
ATOM   4243 N  N     . PHE   A  1 548 ? 6.66300  -52.90400  -33.24700 1.000 52.45749  ? 540 PHE   A N     1 
ATOM   4244 C  CA    . PHE   A  1 548 ? 8.05100  -53.41900  -33.39200 1.000 55.04868  ? 540 PHE   A CA    1 
ATOM   4245 C  C     . PHE   A  1 548 ? 8.09500  -54.45700  -34.51100 1.000 61.17419  ? 540 PHE   A C     1 
ATOM   4246 O  O     . PHE   A  1 548 ? 7.58900  -55.56500  -34.33500 1.000 60.54454  ? 540 PHE   A O     1 
ATOM   4247 C  CB    . PHE   A  1 548 ? 8.53400  -54.03300  -32.07600 1.000 50.98712  ? 540 PHE   A CB    1 
ATOM   4248 C  CG    . PHE   A  1 548 ? 8.84400  -53.03400  -30.99000 1.000 55.67751  ? 540 PHE   A CG    1 
ATOM   4249 C  CD1   . PHE   A  1 548 ? 9.96500  -52.22300  -31.07400 1.000 57.22561  ? 540 PHE   A CD1   1 
ATOM   4250 C  CD2   . PHE   A  1 548 ? 8.02100  -52.90700  -29.88200 1.000 49.56404  ? 540 PHE   A CD2   1 
ATOM   4251 C  CE1   . PHE   A  1 548 ? 10.25500 -51.30400  -30.07800 1.000 51.90024  ? 540 PHE   A CE1   1 
ATOM   4252 C  CE2   . PHE   A  1 548 ? 8.31100  -51.98600  -28.88700 1.000 49.63096  ? 540 PHE   A CE2   1 
ATOM   4253 C  CZ    . PHE   A  1 548 ? 9.42600  -51.18600  -28.98700 1.000 53.02939  ? 540 PHE   A CZ    1 
ATOM   4254 N  N     . PRO   A  1 549 ? 8.69200  -54.13900  -35.68600 1.000 56.80598  ? 541 PRO   A N     1 
ATOM   4255 C  CA    . PRO   A  1 549 ? 8.84200  -55.11900  -36.76100 1.000 58.85184  ? 541 PRO   A CA    1 
ATOM   4256 C  C     . PRO   A  1 549 ? 9.89300  -56.18100  -36.40100 1.000 59.34417  ? 541 PRO   A C     1 
ATOM   4257 O  O     . PRO   A  1 549 ? 11.02600 -55.81400  -36.13100 1.000 60.33644  ? 541 PRO   A O     1 
ATOM   4258 C  CB    . PRO   A  1 549 ? 9.27000  -54.27400  -37.97100 1.000 59.50820  ? 541 PRO   A CB    1 
ATOM   4259 C  CG    . PRO   A  1 549 ? 9.95800  -53.06900  -37.36600 1.000 59.23891  ? 541 PRO   A CG    1 
ATOM   4260 C  CD    . PRO   A  1 549 ? 9.25000  -52.82500  -36.04800 1.000 57.55326  ? 541 PRO   A CD    1 
ATOM   4261 N  N     . VAL   A  1 550 ? 9.48300  -57.45500  -36.39600 1.000 56.75026  ? 542 VAL   A N     1 
ATOM   4262 C  CA    . VAL   A  1 550 ? 10.32000 -58.63600  -36.02500 1.000 60.25202  ? 542 VAL   A CA    1 
ATOM   4263 C  C     . VAL   A  1 550 ? 10.64600 -59.42600  -37.29900 1.000 67.28012  ? 542 VAL   A C     1 
ATOM   4264 O  O     . VAL   A  1 550 ? 9.69800  -59.82100  -38.01100 1.000 65.47603  ? 542 VAL   A O     1 
ATOM   4265 C  CB    . VAL   A  1 550 ? 9.59900  -59.50800  -34.97800 1.000 59.62775  ? 542 VAL   A CB    1 
ATOM   4266 C  CG1   . VAL   A  1 550 ? 10.38000 -60.76900  -34.64300 1.000 63.03270  ? 542 VAL   A CG1   1 
ATOM   4267 C  CG2   . VAL   A  1 550 ? 9.29600  -58.72200  -33.71200 1.000 58.99427  ? 542 VAL   A CG2   1 
ATOM   4268 N  N     . GLU   A  1 551 ? 11.93600 -59.65800  -37.56100 1.000 61.40030  ? 543 GLU   A N     1 
ATOM   4269 C  CA    . GLU   A  1 551 ? 12.44600 -60.27800  -38.81400 1.000 62.81391  ? 543 GLU   A CA    1 
ATOM   4270 C  C     . GLU   A  1 551 ? 13.05000 -61.65800  -38.51300 1.000 64.57868  ? 543 GLU   A C     1 
ATOM   4271 O  O     . GLU   A  1 551 ? 13.94200 -62.08600  -39.27300 1.000 75.18889  ? 543 GLU   A O     1 
ATOM   4272 C  CB    . GLU   A  1 551 ? 13.46500 -59.34500  -39.47500 1.000 64.65972  ? 543 GLU   A CB    1 
ATOM   4273 C  CG    . GLU   A  1 551 ? 12.91300 -57.96600  -39.80800 1.000 71.67921  ? 543 GLU   A CG    1 
ATOM   4274 C  CD    . GLU   A  1 551 ? 11.72400 -57.94200  -40.76100 1.000 87.34313  ? 543 GLU   A CD    1 
ATOM   4275 O  OE1   . GLU   A  1 551 ? 11.75500 -58.67200  -41.78300 1.000 86.94261  ? 543 GLU   A OE1   1 
ATOM   4276 O  OE2   . GLU   A  1 551 ? 10.76800 -57.18300  -40.48400 1.000 77.81681  ? 543 GLU   A OE2   1 
ATOM   4277 N  N     . VAL   A  1 552 ? 12.56700 -62.33800  -37.46800 1.000 65.39877  ? 544 VAL   A N     1 
ATOM   4278 C  CA    . VAL   A  1 552 ? 13.01300 -63.70600  -37.05900 1.000 61.38777  ? 544 VAL   A CA    1 
ATOM   4279 C  C     . VAL   A  1 552 ? 11.84100 -64.43500  -36.39500 1.000 62.03293  ? 544 VAL   A C     1 
ATOM   4280 O  O     . VAL   A  1 552 ? 10.97500 -63.75300  -35.81800 1.000 57.93112  ? 544 VAL   A O     1 
ATOM   4281 C  CB    . VAL   A  1 552 ? 14.21600 -63.65300  -36.09800 1.000 62.32041  ? 544 VAL   A CB    1 
ATOM   4282 C  CG1   . VAL   A  1 552 ? 15.51500 -63.31700  -36.81200 1.000 63.33390  ? 544 VAL   A CG1   1 
ATOM   4283 C  CG2   . VAL   A  1 552 ? 13.97500 -62.69500  -34.94000 1.000 62.98587  ? 544 VAL   A CG2   1 
ATOM   4284 N  N     . ASN   A  1 553 ? 11.83000 -65.76900  -36.46700 1.000 63.58530  ? 545 ASN   A N     1 
ATOM   4285 C  CA    . ASN   A  1 553 ? 11.01600 -66.63300  -35.57100 1.000 59.73733  ? 545 ASN   A CA    1 
ATOM   4286 C  C     . ASN   A  1 553 ? 11.64900 -66.54900  -34.17800 1.000 57.56984  ? 545 ASN   A C     1 
ATOM   4287 O  O     . ASN   A  1 553 ? 12.89000 -66.62700  -34.10200 1.000 58.64280  ? 545 ASN   A O     1 
ATOM   4288 C  CB    . ASN   A  1 553 ? 10.93800 -68.08200  -36.06200 1.000 61.89222  ? 545 ASN   A CB    1 
ATOM   4289 C  CG    . ASN   A  1 553 ? 10.33600 -68.23700  -37.44400 1.000 65.94700  ? 545 ASN   A CG    1 
ATOM   4290 O  OD1   . ASN   A  1 553 ? 9.39800  -67.53200  -37.81200 1.000 67.80226  ? 545 ASN   A OD1   1 
ATOM   4291 N  ND2   . ASN   A  1 553 ? 10.85700 -69.18000  -38.21200 1.000 64.58837  ? 545 ASN   A ND2   1 
ATOM   4292 N  N     . THR   A  1 554 ? 10.84600 -66.36500  -33.12500 1.000 55.33781  ? 546 THR   A N     1 
ATOM   4293 C  CA    . THR   A  1 554 ? 11.34200 -66.16000  -31.73700 1.000 57.54452  ? 546 THR   A CA    1 
ATOM   4294 C  C     . THR   A  1 554 ? 10.20900 -66.31500  -30.71400 1.000 57.47097  ? 546 THR   A C     1 
ATOM   4295 O  O     . THR   A  1 554 ? 9.06900  -66.61500  -31.12200 1.000 54.34313  ? 546 THR   A O     1 
ATOM   4296 C  CB    . THR   A  1 554 ? 12.01500 -64.78700  -31.60900 1.000 54.89477  ? 546 THR   A CB    1 
ATOM   4297 O  OG1   . THR   A  1 554 ? 12.60400 -64.71000  -30.31100 1.000 52.30472  ? 546 THR   A OG1   1 
ATOM   4298 C  CG2   . THR   A  1 554 ? 11.05600 -63.63700  -31.82700 1.000 56.94643  ? 546 THR   A CG2   1 
ATOM   4299 N  N     . VAL   A  1 555 ? 10.53700 -66.11900  -29.43200 1.000 53.86636  ? 547 VAL   A N     1 
ATOM   4300 C  CA    . VAL   A  1 555 ? 9.59100  -66.15300  -28.27700 1.000 55.92203  ? 547 VAL   A CA    1 
ATOM   4301 C  C     . VAL   A  1 555 ? 9.80500  -64.88700  -27.43700 1.000 54.76448  ? 547 VAL   A C     1 
ATOM   4302 O  O     . VAL   A  1 555 ? 10.89500 -64.74800  -26.85200 1.000 48.51401  ? 547 VAL   A O     1 
ATOM   4303 C  CB    . VAL   A  1 555 ? 9.79000  -67.43000  -27.43900 1.000 49.91488  ? 547 VAL   A CB    1 
ATOM   4304 C  CG1   . VAL   A  1 555 ? 8.95400  -67.42300  -26.16800 1.000 53.04931  ? 547 VAL   A CG1   1 
ATOM   4305 C  CG2   . VAL   A  1 555 ? 9.50700  -68.68000  -28.25800 1.000 50.51125  ? 547 VAL   A CG2   1 
ATOM   4306 N  N     . LEU   A  1 556 ? 8.80000  -64.00500  -27.38700 1.000 51.95239  ? 548 LEU   A N     1 
ATOM   4307 C  CA    . LEU   A  1 556 ? 8.80700  -62.74700  -26.58800 1.000 55.07285  ? 548 LEU   A CA    1 
ATOM   4308 C  C     . LEU   A  1 556 ? 8.62800  -63.08400  -25.10100 1.000 51.10400  ? 548 LEU   A C     1 
ATOM   4309 O  O     . LEU   A  1 556 ? 7.62300  -63.73800  -24.77200 1.000 49.17468  ? 548 LEU   A O     1 
ATOM   4310 C  CB    . LEU   A  1 556 ? 7.68000  -61.83400  -27.08900 1.000 50.65371  ? 548 LEU   A CB    1 
ATOM   4311 C  CG    . LEU   A  1 556 ? 7.39300  -60.59300  -26.24500 1.000 47.58296  ? 548 LEU   A CG    1 
ATOM   4312 C  CD1   . LEU   A  1 556 ? 8.60700  -59.68100  -26.18800 1.000 49.53909  ? 548 LEU   A CD1   1 
ATOM   4313 C  CD2   . LEU   A  1 556 ? 6.18800  -59.83900  -26.78400 1.000 45.76352  ? 548 LEU   A CD2   1 
ATOM   4314 N  N     . HIS   A  1 557 ? 9.55900  -62.64400  -24.24600 1.000 46.41700  ? 549 HIS   A N     1 
ATOM   4315 C  CA    . HIS   A  1 557 ? 9.54700  -62.87000  -22.77300 1.000 46.41310  ? 549 HIS   A CA    1 
ATOM   4316 C  C     . HIS   A  1 557 ? 9.36800  -61.55700  -22.00000 1.000 49.41594  ? 549 HIS   A C     1 
ATOM   4317 O  O     . HIS   A  1 557 ? 8.96100  -61.63000  -20.82600 1.000 55.86076  ? 549 HIS   A O     1 
ATOM   4318 C  CB    . HIS   A  1 557 ? 10.82100 -63.59900  -22.33200 1.000 48.94168  ? 549 HIS   A CB    1 
ATOM   4319 C  CG    . HIS   A  1 557 ? 10.91000 -64.99100  -22.85900 1.000 54.45679  ? 549 HIS   A CG    1 
ATOM   4320 N  ND1   . HIS   A  1 557 ? 11.77000 -65.33800  -23.87800 1.000 49.70674  ? 549 HIS   A ND1   1 
ATOM   4321 C  CD2   . HIS   A  1 557 ? 10.23200 -66.11100  -22.53100 1.000 51.55238  ? 549 HIS   A CD2   1 
ATOM   4322 C  CE1   . HIS   A  1 557 ? 11.63000 -66.61800  -24.14600 1.000 56.42719  ? 549 HIS   A CE1   1 
ATOM   4323 N  NE2   . HIS   A  1 557 ? 10.69300 -67.11700  -23.33200 1.000 54.99213  ? 549 HIS   A NE2   1 
ATOM   4324 N  N     . GLY   A  1 558 ? 9.66800  -60.40900  -22.61300 1.000 50.76862  ? 550 GLY   A N     1 
ATOM   4325 C  CA    . GLY   A  1 558 ? 9.51700  -59.08400  -21.98100 1.000 48.42980  ? 550 GLY   A CA    1 
ATOM   4326 C  C     . GLY   A  1 558 ? 10.06300 -57.97200  -22.85600 1.000 48.74308  ? 550 GLY   A C     1 
ATOM   4327 O  O     . GLY   A  1 558 ? 10.35800 -58.23800  -24.04100 1.000 49.13195  ? 550 GLY   A O     1 
ATOM   4328 N  N     . PHE   A  1 559 ? 10.19600 -56.76900  -22.28900 1.000 49.67977  ? 551 PHE   A N     1 
ATOM   4329 C  CA    . PHE   A  1 559 ? 10.66900 -55.54400  -22.98400 1.000 45.99636  ? 551 PHE   A CA    1 
ATOM   4330 C  C     . PHE   A  1 559 ? 11.80200 -54.90700  -22.18000 1.000 43.64946  ? 551 PHE   A C     1 
ATOM   4331 O  O     . PHE   A  1 559 ? 11.56400 -54.50700  -21.03300 1.000 49.60915  ? 551 PHE   A O     1 
ATOM   4332 C  CB    . PHE   A  1 559 ? 9.50700  -54.57100  -23.18800 1.000 43.12782  ? 551 PHE   A CB    1 
ATOM   4333 C  CG    . PHE   A  1 559 ? 8.46200  -55.07900  -24.14700 1.000 51.15469  ? 551 PHE   A CG    1 
ATOM   4334 C  CD1   . PHE   A  1 559 ? 7.48500  -55.96800  -23.72500 1.000 47.03885  ? 551 PHE   A CD1   1 
ATOM   4335 C  CD2   . PHE   A  1 559 ? 8.47600  -54.69400  -25.48000 1.000 52.46495  ? 551 PHE   A CD2   1 
ATOM   4336 C  CE1   . PHE   A  1 559 ? 6.53500  -56.45000  -24.61200 1.000 44.83614  ? 551 PHE   A CE1   1 
ATOM   4337 C  CE2   . PHE   A  1 559 ? 7.52300  -55.17400  -26.36400 1.000 48.52734  ? 551 PHE   A CE2   1 
ATOM   4338 C  CZ    . PHE   A  1 559 ? 6.55700  -56.05300  -25.92900 1.000 51.22878  ? 551 PHE   A CZ    1 
ATOM   4339 N  N     . ALA   A  1 560 ? 12.99800 -54.84100  -22.76800 1.000 45.05556  ? 552 ALA   A N     1 
ATOM   4340 C  CA    . ALA   A  1 560 ? 14.15500 -54.08700  -22.23800 1.000 45.02419  ? 552 ALA   A CA    1 
ATOM   4341 C  C     . ALA   A  1 560 ? 13.83200 -52.59200  -22.31100 1.000 47.73171  ? 552 ALA   A C     1 
ATOM   4342 O  O     . ALA   A  1 560 ? 13.31000 -52.14700  -23.35000 1.000 48.21522  ? 552 ALA   A O     1 
ATOM   4343 C  CB    . ALA   A  1 560 ? 15.40600 -54.42400  -23.01200 1.000 45.88954  ? 552 ALA   A CB    1 
ATOM   4344 N  N     . GLY   A  1 561 ? 14.10300 -51.86000  -21.23000 1.000 49.16737  ? 553 GLY   A N     1 
ATOM   4345 C  CA    . GLY   A  1 561 ? 13.93100 -50.39900  -21.15800 1.000 47.01313  ? 553 GLY   A CA    1 
ATOM   4346 C  C     . GLY   A  1 561 ? 15.26800 -49.70800  -20.98000 1.000 49.91678  ? 553 GLY   A C     1 
ATOM   4347 O  O     . GLY   A  1 561 ? 16.06900 -50.17200  -20.14200 1.000 56.65092  ? 553 GLY   A O     1 
ATOM   4348 N  N     . TYR   A  1 562 ? 15.51200 -48.66100  -21.76900 1.000 48.78514  ? 554 TYR   A N     1 
ATOM   4349 C  CA    . TYR   A  1 562 ? 16.70500 -47.78100  -21.70000 1.000 52.03575  ? 554 TYR   A CA    1 
ATOM   4350 C  C     . TYR   A  1 562 ? 16.21800 -46.33200  -21.60600 1.000 53.70643  ? 554 TYR   A C     1 
ATOM   4351 O  O     . TYR   A  1 562 ? 14.99300 -46.12600  -21.49400 1.000 54.71132  ? 554 TYR   A O     1 
ATOM   4352 C  CB    . TYR   A  1 562 ? 17.59100 -47.99300  -22.93000 1.000 55.43571  ? 554 TYR   A CB    1 
ATOM   4353 C  CG    . TYR   A  1 562 ? 17.88300 -49.43000  -23.28400 1.000 51.65289  ? 554 TYR   A CG    1 
ATOM   4354 C  CD1   . TYR   A  1 562 ? 18.96500 -50.09900  -22.73300 1.000 50.96248  ? 554 TYR   A CD1   1 
ATOM   4355 C  CD2   . TYR   A  1 562 ? 17.09900 -50.11300  -24.20000 1.000 49.15723  ? 554 TYR   A CD2   1 
ATOM   4356 C  CE1   . TYR   A  1 562 ? 19.25500 -51.41000  -23.07700 1.000 54.89814  ? 554 TYR   A CE1   1 
ATOM   4357 C  CE2   . TYR   A  1 562 ? 17.37400 -51.42500  -24.55400 1.000 50.82086  ? 554 TYR   A CE2   1 
ATOM   4358 C  CZ    . TYR   A  1 562 ? 18.45600 -52.07700  -23.99000 1.000 52.18204  ? 554 TYR   A CZ    1 
ATOM   4359 O  OH    . TYR   A  1 562 ? 18.73300 -53.36900  -24.33200 1.000 49.64414  ? 554 TYR   A OH    1 
ATOM   4360 N  N     . PHE   A  1 563 ? 17.13000 -45.35800  -21.66500 1.000 51.93070  ? 555 PHE   A N     1 
ATOM   4361 C  CA    . PHE   A  1 563 ? 16.78300 -43.91400  -21.69100 1.000 52.01320  ? 555 PHE   A CA    1 
ATOM   4362 C  C     . PHE   A  1 563 ? 17.92700 -43.08500  -22.28300 1.000 54.82363  ? 555 PHE   A C     1 
ATOM   4363 O  O     . PHE   A  1 563 ? 19.09500 -43.52200  -22.25000 1.000 56.59550  ? 555 PHE   A O     1 
ATOM   4364 C  CB    . PHE   A  1 563 ? 16.44400 -43.41800  -20.28400 1.000 56.74031  ? 555 PHE   A CB    1 
ATOM   4365 C  CG    . PHE   A  1 563 ? 17.63800 -43.07900  -19.42700 1.000 55.16975  ? 555 PHE   A CG    1 
ATOM   4366 C  CD1   . PHE   A  1 563 ? 18.30700 -44.06400  -18.71900 1.000 55.56557  ? 555 PHE   A CD1   1 
ATOM   4367 C  CD2   . PHE   A  1 563 ? 18.09900 -41.77400  -19.33700 1.000 58.24402  ? 555 PHE   A CD2   1 
ATOM   4368 C  CE1   . PHE   A  1 563 ? 19.40700 -43.75200  -17.93600 1.000 56.77669  ? 555 PHE   A CE1   1 
ATOM   4369 C  CE2   . PHE   A  1 563 ? 19.20100 -41.46200  -18.55600 1.000 57.61003  ? 555 PHE   A CE2   1 
ATOM   4370 C  CZ    . PHE   A  1 563 ? 19.85200 -42.45200  -17.85600 1.000 59.98473  ? 555 PHE   A CZ    1 
ATOM   4371 N  N     . GLU   A  1 564 ? 17.56800 -41.91200  -22.81100 1.000 53.82944  ? 556 GLU   A N     1 
ATOM   4372 C  CA    . GLU   A  1 564 ? 18.48400 -40.79300  -23.15200 1.000 57.24761  ? 556 GLU   A CA    1 
ATOM   4373 C  C     . GLU   A  1 564 ? 17.99500 -39.54100  -22.42200 1.000 58.72676  ? 556 GLU   A C     1 
ATOM   4374 O  O     . GLU   A  1 564 ? 16.78600 -39.47700  -22.11500 1.000 58.58703  ? 556 GLU   A O     1 
ATOM   4375 C  CB    . GLU   A  1 564 ? 18.48900 -40.50700  -24.65300 1.000 63.47866  ? 556 GLU   A CB    1 
ATOM   4376 C  CG    . GLU   A  1 564 ? 18.84600 -41.69400  -25.52300 1.000 57.19544  ? 556 GLU   A CG    1 
ATOM   4377 C  CD    . GLU   A  1 564 ? 18.96400 -41.31700  -26.98800 1.000 69.19736  ? 556 GLU   A CD    1 
ATOM   4378 O  OE1   . GLU   A  1 564 ? 18.07800 -40.58600  -27.48100 1.000 70.43520  ? 556 GLU   A OE1   1 
ATOM   4379 O  OE2   . GLU   A  1 564 ? 19.95000 -41.73400  -27.62800 1.000 73.89187  ? 556 GLU   A OE2   1 
ATOM   4380 N  N     . THR   A  1 565 ? 18.88900 -38.58100  -22.17300 1.000 57.63918  ? 557 THR   A N     1 
ATOM   4381 C  CA    . THR   A  1 565 ? 18.55900 -37.28600  -21.52200 1.000 58.47086  ? 557 THR   A CA    1 
ATOM   4382 C  C     . THR   A  1 565 ? 19.42400 -36.17400  -22.11300 1.000 60.82443  ? 557 THR   A C     1 
ATOM   4383 O  O     . THR   A  1 565 ? 20.63300 -36.40500  -22.31000 1.000 61.56594  ? 557 THR   A O     1 
ATOM   4384 C  CB    . THR   A  1 565 ? 18.70600 -37.36200  -19.99600 1.000 57.53598  ? 557 THR   A CB    1 
ATOM   4385 O  OG1   . THR   A  1 565 ? 18.31600 -36.09000  -19.47800 1.000 58.58906  ? 557 THR   A OG1   1 
ATOM   4386 C  CG2   . THR   A  1 565 ? 20.10600 -37.70700  -19.53500 1.000 58.27456  ? 557 THR   A CG2   1 
ATOM   4387 N  N     . VAL   A  1 566 ? 18.79900 -35.02700  -22.39300 1.000 62.10229  ? 558 VAL   A N     1 
ATOM   4388 C  CA    . VAL   A  1 566 ? 19.46800 -33.74200  -22.74700 1.000 64.58017  ? 558 VAL   A CA    1 
ATOM   4389 C  C     . VAL   A  1 566 ? 19.74300 -32.99400  -21.43900 1.000 66.95169  ? 558 VAL   A C     1 
ATOM   4390 O  O     . VAL   A  1 566 ? 18.79200 -32.40900  -20.87500 1.000 66.86051  ? 558 VAL   A O     1 
ATOM   4391 C  CB    . VAL   A  1 566 ? 18.60300 -32.90300  -23.70900 1.000 65.98932  ? 558 VAL   A CB    1 
ATOM   4392 C  CG1   . VAL   A  1 566 ? 19.27000 -31.58400  -24.07300 1.000 69.21156  ? 558 VAL   A CG1   1 
ATOM   4393 C  CG2   . VAL   A  1 566 ? 18.23600 -33.68100  -24.96400 1.000 67.46214  ? 558 VAL   A CG2   1 
ATOM   4394 N  N     . LEU   A  1 567 ? 20.98700 -33.04400  -20.95400 1.000 67.89999  ? 559 LEU   A N     1 
ATOM   4395 C  CA    . LEU   A  1 567 ? 21.43800 -32.24400  -19.78700 1.000 66.13117  ? 559 LEU   A CA    1 
ATOM   4396 C  C     . LEU   A  1 567 ? 21.37000 -30.77000  -20.19300 1.000 68.59130  ? 559 LEU   A C     1 
ATOM   4397 O  O     . LEU   A  1 567 ? 20.65700 -29.99500  -19.53000 1.000 75.72148  ? 559 LEU   A O     1 
ATOM   4398 C  CB    . LEU   A  1 567 ? 22.86100 -32.65100  -19.38500 1.000 67.13984  ? 559 LEU   A CB    1 
ATOM   4399 C  CG    . LEU   A  1 567 ? 23.07700 -34.12300  -19.03000 1.000 70.21881  ? 559 LEU   A CG    1 
ATOM   4400 C  CD1   . LEU   A  1 567 ? 24.50500 -34.35200  -18.56100 1.000 69.85559  ? 559 LEU   A CD1   1 
ATOM   4401 C  CD2   . LEU   A  1 567 ? 22.09200 -34.59800  -17.97100 1.000 65.76335  ? 559 LEU   A CD2   1 
ATOM   4402 N  N     . TYR   A  1 568 ? 22.05700 -30.42400  -21.28200 1.000 77.15096  ? 560 TYR   A N     1 
ATOM   4403 C  CA    . TYR   A  1 568 ? 22.05000 -29.07700  -21.90900 1.000 83.50980  ? 560 TYR   A CA    1 
ATOM   4404 C  C     . TYR   A  1 568 ? 22.51500 -29.21100  -23.36500 1.000 80.22236  ? 560 TYR   A C     1 
ATOM   4405 O  O     . TYR   A  1 568 ? 23.56600 -29.83400  -23.59600 1.000 79.33693  ? 560 TYR   A O     1 
ATOM   4406 C  CB    . TYR   A  1 568 ? 22.92400 -28.11800  -21.09600 1.000 79.60196  ? 560 TYR   A CB    1 
ATOM   4407 C  CG    . TYR   A  1 568 ? 22.79000 -26.66400  -21.47000 1.000 80.64650  ? 560 TYR   A CG    1 
ATOM   4408 C  CD1   . TYR   A  1 568 ? 21.57300 -26.00900  -21.37100 1.000 78.89914  ? 560 TYR   A CD1   1 
ATOM   4409 C  CD2   . TYR   A  1 568 ? 23.88500 -25.93500  -21.90600 1.000 81.48413  ? 560 TYR   A CD2   1 
ATOM   4410 C  CE1   . TYR   A  1 568 ? 21.44300 -24.67100  -21.70700 1.000 80.50106  ? 560 TYR   A CE1   1 
ATOM   4411 C  CE2   . TYR   A  1 568 ? 23.77300 -24.59700  -22.24700 1.000 82.82253  ? 560 TYR   A CE2   1 
ATOM   4412 C  CZ    . TYR   A  1 568 ? 22.54800 -23.96200  -22.14800 1.000 83.03151  ? 560 TYR   A CZ    1 
ATOM   4413 O  OH    . TYR   A  1 568 ? 22.43200 -22.64300  -22.48300 1.000 85.90913  ? 560 TYR   A OH    1 
ATOM   4414 N  N     . GLN   A  1 569 ? 21.71800 -28.69200  -24.30600 1.000 81.63753  ? 561 GLN   A N     1 
ATOM   4415 C  CA    . GLN   A  1 569 ? 22.03800 -28.58000  -25.75900 1.000 86.00392  ? 561 GLN   A CA    1 
ATOM   4416 C  C     . GLN   A  1 569 ? 22.56900 -29.91800  -26.30600 1.000 83.86613  ? 561 GLN   A C     1 
ATOM   4417 O  O     . GLN   A  1 569 ? 21.75100 -30.85100  -26.44300 1.000 78.97291  ? 561 GLN   A O     1 
ATOM   4418 C  CB    . GLN   A  1 569 ? 22.98700 -27.39900  -25.97300 1.000 80.36155  ? 561 GLN   A CB    1 
ATOM   4419 C  CG    . GLN   A  1 569 ? 22.30700 -26.05400  -25.75700 1.000 82.02614  ? 561 GLN   A CG    1 
ATOM   4420 C  CD    . GLN   A  1 569 ? 23.26200 -24.88700  -25.77300 1.000 85.06703  ? 561 GLN   A CD    1 
ATOM   4421 O  OE1   . GLN   A  1 569 ? 24.44300 -25.02000  -26.08900 1.000 86.20506  ? 561 GLN   A OE1   1 
ATOM   4422 N  NE2   . GLN   A  1 569 ? 22.74600 -23.71700  -25.43600 1.000 86.60923  ? 561 GLN   A NE2   1 
ATOM   4423 N  N     . ASP   A  1 570 ? 23.86900 -30.01000  -26.62200 1.000 77.44167  ? 562 ASP   A N     1 
ATOM   4424 C  CA    . ASP   A  1 570 ? 24.48100 -31.17600  -27.31900 1.000 81.50798  ? 562 ASP   A CA    1 
ATOM   4425 C  C     . ASP   A  1 570 ? 25.08300 -32.15100  -26.30100 1.000 79.94708  ? 562 ASP   A C     1 
ATOM   4426 O  O     . ASP   A  1 570 ? 25.43400 -33.27300  -26.71000 1.000 84.07629  ? 562 ASP   A O     1 
ATOM   4427 C  CB    . ASP   A  1 570 ? 25.54900 -30.75200  -28.33200 1.000 83.19275  ? 562 ASP   A CB    1 
ATOM   4428 C  CG    . ASP   A  1 570 ? 26.72300 -30.00200  -27.72800 1.000 85.23023  ? 562 ASP   A CG    1 
ATOM   4429 O  OD1   . ASP   A  1 570 ? 26.50000 -29.24900  -26.76000 1.000 86.26156  ? 562 ASP   A OD1   1 
ATOM   4430 O  OD2   . ASP   A  1 570 ? 27.84900 -30.18200  -28.22800 1.000 84.96761  ? 562 ASP   A OD2   1 
ATOM   4431 N  N     . ILE   A  1 571 ? 25.19700 -31.74700  -25.03300 1.000 79.85346  ? 563 ILE   A N     1 
ATOM   4432 C  CA    . ILE   A  1 571 ? 25.73000 -32.61100  -23.93900 1.000 75.39431  ? 563 ILE   A CA    1 
ATOM   4433 C  C     . ILE   A  1 571 ? 24.58000 -33.50800  -23.47500 1.000 74.50383  ? 563 ILE   A C     1 
ATOM   4434 O  O     . ILE   A  1 571 ? 23.55800 -32.96000  -23.01800 1.000 75.65045  ? 563 ILE   A O     1 
ATOM   4435 C  CB    . ILE   A  1 571 ? 26.33200 -31.77900  -22.78700 1.000 76.92042  ? 563 ILE   A CB    1 
ATOM   4436 C  CG1   . ILE   A  1 571 ? 27.18700 -30.61400  -23.29700 1.000 80.85459  ? 563 ILE   A CG1   1 
ATOM   4437 C  CG2   . ILE   A  1 571 ? 27.12500 -32.66900  -21.84400 1.000 73.88845  ? 563 ILE   A CG2   1 
ATOM   4438 C  CD1   . ILE   A  1 571 ? 26.49700 -29.27000  -23.24600 1.000 82.19488  ? 563 ILE   A CD1   1 
ATOM   4439 N  N     . THR   A  1 572 ? 24.73100 -34.82600  -23.63300 1.000 72.90595  ? 564 THR   A N     1 
ATOM   4440 C  CA    . THR   A  1 572 ? 23.68000 -35.84200  -23.36100 1.000 69.51388  ? 564 THR   A CA    1 
ATOM   4441 C  C     . THR   A  1 572 ? 24.26500 -37.02100  -22.57600 1.000 65.30103  ? 564 THR   A C     1 
ATOM   4442 O  O     . THR   A  1 572 ? 25.50100 -37.18300  -22.56800 1.000 66.28345  ? 564 THR   A O     1 
ATOM   4443 C  CB    . THR   A  1 572 ? 23.05900 -36.35000  -24.66700 1.000 71.99067  ? 564 THR   A CB    1 
ATOM   4444 O  OG1   . THR   A  1 572 ? 24.08700 -37.01000  -25.40600 1.000 71.74962  ? 564 THR   A OG1   1 
ATOM   4445 C  CG2   . THR   A  1 572 ? 22.44700 -35.24400  -25.49900 1.000 71.38412  ? 564 THR   A CG2   1 
ATOM   4446 N  N     . LEU   A  1 573 ? 23.39100 -37.80200  -21.93900 1.000 62.02531  ? 565 LEU   A N     1 
ATOM   4447 C  CA    . LEU   A  1 573 ? 23.70600 -39.14500  -21.38500 1.000 63.51738  ? 565 LEU   A CA    1 
ATOM   4448 C  C     . LEU   A  1 573 ? 22.72800 -40.15000  -21.99500 1.000 62.19796  ? 565 LEU   A C     1 
ATOM   4449 O  O     . LEU   A  1 573 ? 21.58500 -39.75600  -22.30500 1.000 60.45611  ? 565 LEU   A O     1 
ATOM   4450 C  CB    . LEU   A  1 573 ? 23.60000 -39.11600  -19.85800 1.000 65.84329  ? 565 LEU   A CB    1 
ATOM   4451 C  CG    . LEU   A  1 573 ? 24.57600 -38.17900  -19.14800 1.000 66.75298  ? 565 LEU   A CG    1 
ATOM   4452 C  CD1   . LEU   A  1 573 ? 24.22300 -38.05000  -17.67500 1.000 69.57470  ? 565 LEU   A CD1   1 
ATOM   4453 C  CD2   . LEU   A  1 573 ? 26.01200 -38.65200  -19.31700 1.000 64.13950  ? 565 LEU   A CD2   1 
ATOM   4454 N  N     . SER   A  1 574 ? 23.17500 -41.39100  -22.17700 1.000 61.38999  ? 566 SER   A N     1 
ATOM   4455 C  CA    . SER   A  1 574 ? 22.38000 -42.48700  -22.78300 1.000 62.66508  ? 566 SER   A CA    1 
ATOM   4456 C  C     . SER   A  1 574 ? 22.90000 -43.84200  -22.29300 1.000 61.02017  ? 566 SER   A C     1 
ATOM   4457 O  O     . SER   A  1 574 ? 24.13300 -43.98900  -22.14900 1.000 62.63899  ? 566 SER   A O     1 
ATOM   4458 C  CB    . SER   A  1 574 ? 22.41200 -42.38700  -24.28400 1.000 62.52109  ? 566 SER   A CB    1 
ATOM   4459 O  OG    . SER   A  1 574 ? 21.88100 -43.55800  -24.88600 1.000 65.04158  ? 566 SER   A OG    1 
ATOM   4460 N  N     . ILE   A  1 575 ? 21.98000 -44.77100  -22.01800 1.000 59.38419  ? 567 ILE   A N     1 
ATOM   4461 C  CA    . ILE   A  1 575 ? 22.26500 -46.22800  -21.86000 1.000 60.31113  ? 567 ILE   A CA    1 
ATOM   4462 C  C     . ILE   A  1 575 ? 21.56600 -46.99400  -22.99000 1.000 60.13103  ? 567 ILE   A C     1 
ATOM   4463 O  O     . ILE   A  1 575 ? 21.57200 -48.23900  -22.94700 1.000 60.24879  ? 567 ILE   A O     1 
ATOM   4464 C  CB    . ILE   A  1 575 ? 21.84300 -46.73300  -20.46800 1.000 56.99943  ? 567 ILE   A CB    1 
ATOM   4465 C  CG1   . ILE   A  1 575 ? 20.33300 -46.62000  -20.24100 1.000 52.43030  ? 567 ILE   A CG1   1 
ATOM   4466 C  CG2   . ILE   A  1 575 ? 22.63600 -46.01100  -19.39100 1.000 58.81686  ? 567 ILE   A CG2   1 
ATOM   4467 C  CD1   . ILE   A  1 575 ? 19.82100 -47.48100  -19.11100 1.000 53.36381  ? 567 ILE   A CD1   1 
ATOM   4468 N  N     . ARG   A  1 576 ? 20.97600 -46.27000  -23.94800 1.000 57.59093  ? 568 ARG   A N     1 
ATOM   4469 C  CA    . ARG   A  1 576 ? 20.46100 -46.81600  -25.23300 1.000 63.38286  ? 568 ARG   A CA    1 
ATOM   4470 C  C     . ARG   A  1 576 ? 21.64200 -47.44800  -25.96700 1.000 63.25824  ? 568 ARG   A C     1 
ATOM   4471 O  O     . ARG   A  1 576 ? 22.57800 -46.74100  -26.33000 1.000 62.77110  ? 568 ARG   A O     1 
ATOM   4472 C  CB    . ARG   A  1 576 ? 19.80600 -45.68800  -26.03800 1.000 62.65701  ? 568 ARG   A CB    1 
ATOM   4473 C  CG    . ARG   A  1 576 ? 19.05800 -46.13700  -27.28300 1.000 66.11762  ? 568 ARG   A CG    1 
ATOM   4474 C  CD    . ARG   A  1 576 ? 18.42200 -44.94500  -27.97400 1.000 69.19093  ? 568 ARG   A CD    1 
ATOM   4475 N  NE    . ARG   A  1 576 ? 18.11900 -45.19100  -29.37800 1.000 68.92729  ? 568 ARG   A NE    1 
ATOM   4476 C  CZ    . ARG   A  1 576 ? 17.98200 -44.24400  -30.30400 1.000 69.36528  ? 568 ARG   A CZ    1 
ATOM   4477 N  NH1   . ARG   A  1 576 ? 18.13300 -42.96700  -29.99200 1.000 69.60092  ? 568 ARG   A NH1   1 
ATOM   4478 N  NH2   . ARG   A  1 576 ? 17.70300 -44.57900  -31.55200 1.000 73.13229  ? 568 ARG   A NH2   1 
ATOM   4479 N  N     . PRO   A  1 577 ? 21.66000 -48.78700  -26.17600 1.000 61.11008  ? 569 PRO   A N     1 
ATOM   4480 C  CA    . PRO   A  1 577 ? 22.86800 -49.47900  -26.63100 1.000 60.91991  ? 569 PRO   A CA    1 
ATOM   4481 C  C     . PRO   A  1 577 ? 23.52200 -48.82200  -27.85600 1.000 68.58338  ? 569 PRO   A C     1 
ATOM   4482 O  O     . PRO   A  1 577 ? 24.73900 -48.75700  -27.88900 1.000 72.46689  ? 569 PRO   A O     1 
ATOM   4483 C  CB    . PRO   A  1 577 ? 22.37400 -50.89300  -26.96800 1.000 56.39357  ? 569 PRO   A CB    1 
ATOM   4484 C  CG    . PRO   A  1 577 ? 21.16500 -51.08100  -26.08100 1.000 54.31937  ? 569 PRO   A CG    1 
ATOM   4485 C  CD    . PRO   A  1 577 ? 20.52700 -49.71000  -26.00100 1.000 53.94669  ? 569 PRO   A CD    1 
ATOM   4486 N  N     . GLU   A  1 578 ? 22.70700 -48.34200  -28.80300 1.000 63.87836  ? 570 GLU   A N     1 
ATOM   4487 C  CA    . GLU   A  1 578 ? 23.16200 -47.68100  -30.05700 1.000 70.38807  ? 570 GLU   A CA    1 
ATOM   4488 C  C     . GLU   A  1 578 ? 24.01800 -46.45500  -29.71100 1.000 71.79891  ? 570 GLU   A C     1 
ATOM   4489 O  O     . GLU   A  1 578 ? 25.13400 -46.33900  -30.26100 1.000 76.76265  ? 570 GLU   A O     1 
ATOM   4490 C  CB    . GLU   A  1 578 ? 21.98100 -47.23100  -30.92400 1.000 71.97984  ? 570 GLU   A CB    1 
ATOM   4491 C  CG    . GLU   A  1 578 ? 20.97000 -48.31900  -31.24200 1.000 68.63640  ? 570 GLU   A CG    1 
ATOM   4492 C  CD    . GLU   A  1 578 ? 19.76300 -48.31600  -30.32100 1.000 69.24966  ? 570 GLU   A CD    1 
ATOM   4493 O  OE1   . GLU   A  1 578 ? 19.92800 -48.70000  -29.14800 1.000 67.29857  ? 570 GLU   A OE1   1 
ATOM   4494 O  OE2   . GLU   A  1 578 ? 18.67200 -47.90400  -30.76700 1.000 67.58325  ? 570 GLU   A OE2   1 
ATOM   4495 N  N     . THR   A  1 579 ? 23.50700 -45.58900  -28.82900 1.000 66.56184  ? 571 THR   A N     1 
ATOM   4496 C  CA    . THR   A  1 579 ? 24.05800 -44.24200  -28.51900 1.000 68.92176  ? 571 THR   A CA    1 
ATOM   4497 C  C     . THR   A  1 579 ? 24.63700 -44.21900  -27.09800 1.000 69.87299  ? 571 THR   A C     1 
ATOM   4498 O  O     . THR   A  1 579 ? 24.78900 -43.10500  -26.54800 1.000 69.56420  ? 571 THR   A O     1 
ATOM   4499 C  CB    . THR   A  1 579 ? 22.97600 -43.16400  -28.67800 1.000 68.84031  ? 571 THR   A CB    1 
ATOM   4500 O  OG1   . THR   A  1 579 ? 22.18600 -43.13900  -27.49000 1.000 69.44506  ? 571 THR   A OG1   1 
ATOM   4501 C  CG2   . THR   A  1 579 ? 22.07500 -43.39200  -29.87200 1.000 71.63103  ? 571 THR   A CG2   1 
ATOM   4502 N  N     . HIS   A  1 580 ? 24.96000 -45.39200  -26.53900 1.000 68.31860  ? 572 HIS   A N     1 
ATOM   4503 C  CA    . HIS   A  1 580 ? 25.36800 -45.58000  -25.12000 1.000 64.07712  ? 572 HIS   A CA    1 
ATOM   4504 C  C     . HIS   A  1 580 ? 26.59300 -44.71200  -24.81500 1.000 69.26599  ? 572 HIS   A C     1 
ATOM   4505 O  O     . HIS   A  1 580 ? 27.58200 -44.80800  -25.56300 1.000 66.16018  ? 572 HIS   A O     1 
ATOM   4506 C  CB    . HIS   A  1 580 ? 25.64600 -47.06000  -24.81700 1.000 68.31738  ? 572 HIS   A CB    1 
ATOM   4507 C  CG    . HIS   A  1 580 ? 25.53300 -47.40500  -23.36800 1.000 71.39722  ? 572 HIS   A CG    1 
ATOM   4508 N  ND1   . HIS   A  1 580 ? 26.26500 -46.75600  -22.39200 1.000 70.30704  ? 572 HIS   A ND1   1 
ATOM   4509 C  CD2   . HIS   A  1 580 ? 24.77900 -48.32200  -22.72500 1.000 66.19778  ? 572 HIS   A CD2   1 
ATOM   4510 C  CE1   . HIS   A  1 580 ? 25.96100 -47.25600  -21.21200 1.000 64.89450  ? 572 HIS   A CE1   1 
ATOM   4511 N  NE2   . HIS   A  1 580 ? 25.05100 -48.21500  -21.38800 1.000 65.85221  ? 572 HIS   A NE2   1 
ATOM   4512 N  N     . SER   A  1 581 ? 26.51700 -43.90200  -23.75300 1.000 70.22990  ? 573 SER   A N     1 
ATOM   4513 C  CA    . SER   A  1 581 ? 27.63400 -43.07500  -23.22500 1.000 70.78365  ? 573 SER   A CA    1 
ATOM   4514 C  C     . SER   A  1 581 ? 28.81700 -43.98700  -22.90500 1.000 69.84447  ? 573 SER   A C     1 
ATOM   4515 O  O     . SER   A  1 581 ? 28.65200 -44.97400  -22.19200 1.000 69.00449  ? 573 SER   A O     1 
ATOM   4516 C  CB    . SER   A  1 581 ? 27.19700 -42.28700  -22.01700 1.000 66.55530  ? 573 SER   A CB    1 
ATOM   4517 O  OG    . SER   A  1 581 ? 25.99600 -41.57600  -22.28200 1.000 65.93073  ? 573 SER   A OG    1 
ATOM   4518 N  N     . PRO   A  1 582 ? 30.03700 -43.70800  -23.42300 1.000 76.27985  ? 574 PRO   A N     1 
ATOM   4519 C  CA    . PRO   A  1 582 ? 31.15200 -44.65100  -23.31600 1.000 79.26056  ? 574 PRO   A CA    1 
ATOM   4520 C  C     . PRO   A  1 582 ? 31.59500 -44.91200  -21.86700 1.000 81.72588  ? 574 PRO   A C     1 
ATOM   4521 O  O     . PRO   A  1 582 ? 31.96300 -43.96900  -21.18700 1.000 79.11248  ? 574 PRO   A O     1 
ATOM   4522 C  CB    . PRO   A  1 582 ? 32.29500 -43.98800  -24.10700 1.000 80.59840  ? 574 PRO   A CB    1 
ATOM   4523 C  CG    . PRO   A  1 582 ? 31.62200 -42.91400  -24.93800 1.000 88.26923  ? 574 PRO   A CG    1 
ATOM   4524 C  CD    . PRO   A  1 582 ? 30.42000 -42.47600  -24.12800 1.000 79.96951  ? 574 PRO   A CD    1 
ATOM   4525 N  N     . GLY   A  1 583 ? 31.53700 -46.17900  -21.44200 1.000 79.78789  ? 575 GLY   A N     1 
ATOM   4526 C  CA    . GLY   A  1 583 ? 32.01900 -46.66300  -20.13200 1.000 81.49686  ? 575 GLY   A CA    1 
ATOM   4527 C  C     . GLY   A  1 583 ? 31.27400 -46.04600  -18.95800 1.000 74.03345  ? 575 GLY   A C     1 
ATOM   4528 O  O     . GLY   A  1 583 ? 31.92500 -45.79700  -17.92200 1.000 75.77159  ? 575 GLY   A O     1 
ATOM   4529 N  N     . MET   A  1 584 ? 29.96100 -45.82300  -19.09600 1.000 67.42490  ? 576 MET   A N     1 
ATOM   4530 C  CA    . MET   A  1 584 ? 29.09300 -45.25600  -18.02700 1.000 69.96762  ? 576 MET   A CA    1 
ATOM   4531 C  C     . MET   A  1 584 ? 28.30900 -46.38700  -17.34700 1.000 71.41225  ? 576 MET   A C     1 
ATOM   4532 O  O     . MET   A  1 584 ? 27.39600 -46.95500  -17.98400 1.000 67.48487  ? 576 MET   A O     1 
ATOM   4533 C  CB    . MET   A  1 584 ? 28.11400 -44.21800  -18.58300 1.000 68.26844  ? 576 MET   A CB    1 
ATOM   4534 C  CG    . MET   A  1 584 ? 27.41100 -43.42300  -17.49500 1.000 63.53230  ? 576 MET   A CG    1 
ATOM   4535 S  SD    . MET   A  1 584 ? 26.17600 -42.27000  -18.13600 1.000 67.41248  ? 576 MET   A SD    1 
ATOM   4536 C  CE    . MET   A  1 584 ? 24.98500 -43.40700  -18.84400 1.000 56.36742  ? 576 MET   A CE    1 
ATOM   4537 N  N     . PHE   A  1 585 ? 28.63100 -46.65900  -16.08000 1.000 69.71516  ? 577 PHE   A N     1 
ATOM   4538 C  CA    . PHE   A  1 585 ? 28.13300 -47.82200  -15.29700 1.000 68.03355  ? 577 PHE   A CA    1 
ATOM   4539 C  C     . PHE   A  1 585 ? 27.01900 -47.39700  -14.32700 1.000 62.67466  ? 577 PHE   A C     1 
ATOM   4540 O  O     . PHE   A  1 585 ? 26.55200 -48.25500  -13.55300 1.000 60.67754  ? 577 PHE   A O     1 
ATOM   4541 C  CB    . PHE   A  1 585 ? 29.29900 -48.48000  -14.55300 1.000 71.49810  ? 577 PHE   A CB    1 
ATOM   4542 C  CG    . PHE   A  1 585 ? 30.04400 -47.57500  -13.60200 1.000 79.20285  ? 577 PHE   A CG    1 
ATOM   4543 C  CD1   . PHE   A  1 585 ? 29.50800 -47.24000  -12.36600 1.000 75.28950  ? 577 PHE   A CD1   1 
ATOM   4544 C  CD2   . PHE   A  1 585 ? 31.28900 -47.06400  -13.94200 1.000 80.03072  ? 577 PHE   A CD2   1 
ATOM   4545 C  CE1   . PHE   A  1 585 ? 30.19800 -46.40900  -11.49700 1.000 77.64788  ? 577 PHE   A CE1   1 
ATOM   4546 C  CE2   . PHE   A  1 585 ? 31.97800 -46.23500  -13.06900 1.000 83.10757  ? 577 PHE   A CE2   1 
ATOM   4547 C  CZ    . PHE   A  1 585 ? 31.43100 -45.90900  -11.84900 1.000 82.61519  ? 577 PHE   A CZ    1 
ATOM   4548 N  N     . SER   A  1 586 ? 26.60400 -46.12800  -14.36300 1.000 62.14972  ? 578 SER   A N     1 
ATOM   4549 C  CA    . SER   A  1 586 ? 25.60100 -45.54300  -13.43500 1.000 57.42502  ? 578 SER   A CA    1 
ATOM   4550 C  C     . SER   A  1 586 ? 24.25800 -46.27400  -13.56700 1.000 57.68510  ? 578 SER   A C     1 
ATOM   4551 O  O     . SER   A  1 586 ? 23.63400 -46.53000  -12.52200 1.000 63.05162  ? 578 SER   A O     1 
ATOM   4552 C  CB    . SER   A  1 586 ? 25.45200 -44.05900  -13.64600 1.000 63.36447  ? 578 SER   A CB    1 
ATOM   4553 O  OG    . SER   A  1 586 ? 26.50100 -43.35600  -12.99400 1.000 67.13805  ? 578 SER   A OG    1 
ATOM   4554 N  N     . TRP   A  1 587 ? 23.83800 -46.61600  -14.78900 1.000 57.13725  ? 579 TRP   A N     1 
ATOM   4555 C  CA    . TRP   A  1 587 ? 22.54600 -47.30600  -15.05700 1.000 59.85099  ? 579 TRP   A CA    1 
ATOM   4556 C  C     . TRP   A  1 587 ? 22.76400 -48.58600  -15.87000 1.000 53.77147  ? 579 TRP   A C     1 
ATOM   4557 O  O     . TRP   A  1 587 ? 23.46000 -48.51300  -16.89900 1.000 61.80606  ? 579 TRP   A O     1 
ATOM   4558 C  CB    . TRP   A  1 587 ? 21.57700 -46.38100  -15.79700 1.000 58.64474  ? 579 TRP   A CB    1 
ATOM   4559 C  CG    . TRP   A  1 587 ? 21.18500 -45.14100  -15.06000 1.000 57.57821  ? 579 TRP   A CG    1 
ATOM   4560 C  CD1   . TRP   A  1 587 ? 20.13700 -44.99400  -14.20000 1.000 59.54139  ? 579 TRP   A CD1   1 
ATOM   4561 C  CD2   . TRP   A  1 587 ? 21.80400 -43.84800  -15.16200 1.000 54.72619  ? 579 TRP   A CD2   1 
ATOM   4562 N  NE1   . TRP   A  1 587 ? 20.07200 -43.70400  -13.74800 1.000 57.37072  ? 579 TRP   A NE1   1 
ATOM   4563 C  CE2   . TRP   A  1 587 ? 21.08100 -42.97700  -14.32100 1.000 56.96263  ? 579 TRP   A CE2   1 
ATOM   4564 C  CE3   . TRP   A  1 587 ? 22.89800 -43.34400  -15.87200 1.000 54.64876  ? 579 TRP   A CE3   1 
ATOM   4565 C  CZ2   . TRP   A  1 587 ? 21.42100 -41.63400  -14.17000 1.000 59.44645  ? 579 TRP   A CZ2   1 
ATOM   4566 C  CZ3   . TRP   A  1 587 ? 23.23300 -42.01700  -15.72300 1.000 57.94803  ? 579 TRP   A CZ3   1 
ATOM   4567 C  CH2   . TRP   A  1 587 ? 22.50200 -41.17500  -14.88400 1.000 55.78273  ? 579 TRP   A CH2   1 
ATOM   4568 N  N     . PHE   A  1 588 ? 22.16600 -49.69500  -15.42000 1.000 52.85292  ? 580 PHE   A N     1 
ATOM   4569 C  CA    . PHE   A  1 588 ? 21.88700 -50.92100  -16.21300 1.000 53.65891  ? 580 PHE   A CA    1 
ATOM   4570 C  C     . PHE   A  1 588 ? 20.48100 -50.81600  -16.79500 1.000 54.33455  ? 580 PHE   A C     1 
ATOM   4571 O  O     . PHE   A  1 588 ? 19.67100 -50.03900  -16.29500 1.000 52.31035  ? 580 PHE   A O     1 
ATOM   4572 C  CB    . PHE   A  1 588 ? 21.96200 -52.18200  -15.34800 1.000 56.49862  ? 580 PHE   A CB    1 
ATOM   4573 C  CG    . PHE   A  1 588 ? 23.34000 -52.61800  -14.92000 1.000 56.61813  ? 580 PHE   A CG    1 
ATOM   4574 C  CD1   . PHE   A  1 588 ? 24.43300 -52.49600  -15.76500 1.000 59.48621  ? 580 PHE   A CD1   1 
ATOM   4575 C  CD2   . PHE   A  1 588 ? 23.52900 -53.20800  -13.68100 1.000 53.70932  ? 580 PHE   A CD2   1 
ATOM   4576 C  CE1   . PHE   A  1 588 ? 25.69000 -52.92100  -15.36400 1.000 62.41953  ? 580 PHE   A CE1   1 
ATOM   4577 C  CE2   . PHE   A  1 588 ? 24.78500 -53.63600  -13.28500 1.000 56.87975  ? 580 PHE   A CE2   1 
ATOM   4578 C  CZ    . PHE   A  1 588 ? 25.86300 -53.49000  -14.12400 1.000 60.99976  ? 580 PHE   A CZ    1 
ATOM   4579 N  N     . PRO   A  1 589 ? 20.13200 -51.59700  -17.84500 1.000 51.09481  ? 581 PRO   A N     1 
ATOM   4580 C  CA    . PRO   A  1 589 ? 18.78200 -51.56500  -18.40800 1.000 50.67652  ? 581 PRO   A CA    1 
ATOM   4581 C  C     . PRO   A  1 589 ? 17.73400 -52.16100  -17.45600 1.000 55.43512  ? 581 PRO   A C     1 
ATOM   4582 O  O     . PRO   A  1 589 ? 18.08900 -52.95200  -16.59600 1.000 51.96357  ? 581 PRO   A O     1 
ATOM   4583 C  CB    . PRO   A  1 589 ? 18.85400 -52.42300  -19.68000 1.000 46.74250  ? 581 PRO   A CB    1 
ATOM   4584 C  CG    . PRO   A  1 589 ? 20.33200 -52.67700  -19.91100 1.000 51.73522  ? 581 PRO   A CG    1 
ATOM   4585 C  CD    . PRO   A  1 589 ? 21.00600 -52.53600  -18.56200 1.000 51.75175  ? 581 PRO   A CD    1 
ATOM   4586 N  N     . ILE   A  1 590 ? 16.47400 -51.76300  -17.64000 1.000 53.32822  ? 582 ILE   A N     1 
ATOM   4587 C  CA    . ILE   A  1 590 ? 15.29900 -52.27800  -16.87800 1.000 49.79464  ? 582 ILE   A CA    1 
ATOM   4588 C  C     . ILE   A  1 590 ? 14.62500 -53.35300  -17.73800 1.000 49.17839  ? 582 ILE   A C     1 
ATOM   4589 O  O     . ILE   A  1 590 ? 14.80200 -53.30900  -18.96600 1.000 45.40007  ? 582 ILE   A O     1 
ATOM   4590 C  CB    . ILE   A  1 590 ? 14.34900 -51.12000  -16.50600 1.000 48.78006  ? 582 ILE   A CB    1 
ATOM   4591 C  CG1   . ILE   A  1 590 ? 13.54000 -51.42200  -15.24300 1.000 48.17180  ? 582 ILE   A CG1   1 
ATOM   4592 C  CG2   . ILE   A  1 590 ? 13.45000 -50.74400  -17.67300 1.000 49.36035  ? 582 ILE   A CG2   1 
ATOM   4593 C  CD1   . ILE   A  1 590 ? 12.86800 -50.20700  -14.64500 1.000 53.34532  ? 582 ILE   A CD1   1 
ATOM   4594 N  N     . LEU   A  1 591 ? 13.90600 -54.28700  -17.10900 1.000 50.88196  ? 583 LEU   A N     1 
ATOM   4595 C  CA    . LEU   A  1 591 ? 13.17800 -55.39400  -17.78600 1.000 46.37947  ? 583 LEU   A CA    1 
ATOM   4596 C  C     . LEU   A  1 591 ? 11.72300 -55.40500  -17.31100 1.000 44.32951  ? 583 LEU   A C     1 
ATOM   4597 O  O     . LEU   A  1 591 ? 11.50600 -55.61700  -16.11000 1.000 45.39954  ? 583 LEU   A O     1 
ATOM   4598 C  CB    . LEU   A  1 591 ? 13.85900 -56.72800  -17.46300 1.000 49.57874  ? 583 LEU   A CB    1 
ATOM   4599 C  CG    . LEU   A  1 591 ? 13.11300 -57.97800  -17.93600 1.000 50.94165  ? 583 LEU   A CG    1 
ATOM   4600 C  CD1   . LEU   A  1 591 ? 12.90800 -57.95700  -19.44500 1.000 47.22003  ? 583 LEU   A CD1   1 
ATOM   4601 C  CD2   . LEU   A  1 591 ? 13.84900 -59.24100  -17.51900 1.000 48.42615  ? 583 LEU   A CD2   1 
ATOM   4602 N  N     . PHE   A  1 592 ? 10.78000 -55.18800  -18.22900 1.000 48.80215  ? 584 PHE   A N     1 
ATOM   4603 C  CA    . PHE   A  1 592 ? 9.31900  -55.36500  -18.01600 1.000 49.96913  ? 584 PHE   A CA    1 
ATOM   4604 C  C     . PHE   A  1 592 ? 8.93800  -56.76400  -18.49200 1.000 52.42874  ? 584 PHE   A C     1 
ATOM   4605 O  O     . PHE   A  1 592 ? 8.80500  -56.98800  -19.69300 1.000 53.26555  ? 584 PHE   A O     1 
ATOM   4606 C  CB    . PHE   A  1 592 ? 8.52600  -54.27900  -18.74800 1.000 43.61209  ? 584 PHE   A CB    1 
ATOM   4607 C  CG    . PHE   A  1 592 ? 8.67600  -52.90300  -18.15300 1.000 50.19546  ? 584 PHE   A CG    1 
ATOM   4608 C  CD1   . PHE   A  1 592 ? 9.71600  -52.07100  -18.53800 1.000 50.13968  ? 584 PHE   A CD1   1 
ATOM   4609 C  CD2   . PHE   A  1 592 ? 7.78400  -52.44500  -17.19500 1.000 48.99544  ? 584 PHE   A CD2   1 
ATOM   4610 C  CE1   . PHE   A  1 592 ? 9.85600  -50.80800  -17.98100 1.000 53.93569  ? 584 PHE   A CE1   1 
ATOM   4611 C  CE2   . PHE   A  1 592 ? 7.92600  -51.18300  -16.63700 1.000 46.30852  ? 584 PHE   A CE2   1 
ATOM   4612 C  CZ    . PHE   A  1 592 ? 8.96200  -50.36700  -17.03100 1.000 50.33639  ? 584 PHE   A CZ    1 
ATOM   4613 N  N     . PRO   A  1 593 ? 8.77400  -57.75000  -17.57900 1.000 49.79474  ? 585 PRO   A N     1 
ATOM   4614 C  CA    . PRO   A  1 593 ? 8.42800  -59.11200  -17.97600 1.000 45.45051  ? 585 PRO   A CA    1 
ATOM   4615 C  C     . PRO   A  1 593 ? 6.99500  -59.20100  -18.51600 1.000 47.28858  ? 585 PRO   A C     1 
ATOM   4616 O  O     . PRO   A  1 593 ? 6.30400  -58.20400  -18.51400 1.000 45.21597  ? 585 PRO   A O     1 
ATOM   4617 C  CB    . PRO   A  1 593 ? 8.53700  -59.94200  -16.68500 1.000 47.47343  ? 585 PRO   A CB    1 
ATOM   4618 C  CG    . PRO   A  1 593 ? 9.19900  -59.02800  -15.66900 1.000 48.08711  ? 585 PRO   A CG    1 
ATOM   4619 C  CD    . PRO   A  1 593 ? 8.90200  -57.61500  -16.12200 1.000 47.53117  ? 585 PRO   A CD    1 
ATOM   4620 N  N     . ILE   A  1 594 ? 6.59600  -60.39200  -18.96700 1.000 52.16230  ? 586 ILE   A N     1 
ATOM   4621 C  CA    . ILE   A  1 594 ? 5.17900  -60.75000  -19.27200 1.000 49.55410  ? 586 ILE   A CA    1 
ATOM   4622 C  C     . ILE   A  1 594 ? 4.92000  -62.16100  -18.73200 1.000 48.86079  ? 586 ILE   A C     1 
ATOM   4623 O  O     . ILE   A  1 594 ? 5.85400  -62.99000  -18.77200 1.000 46.01008  ? 586 ILE   A O     1 
ATOM   4624 C  CB    . ILE   A  1 594 ? 4.86500  -60.61900  -20.77800 1.000 52.27480  ? 586 ILE   A CB    1 
ATOM   4625 C  CG1   . ILE   A  1 594 ? 5.92800  -61.28300  -21.65600 1.000 49.48254  ? 586 ILE   A CG1   1 
ATOM   4626 C  CG2   . ILE   A  1 594 ? 4.66700  -59.16100  -21.16400 1.000 46.90231  ? 586 ILE   A CG2   1 
ATOM   4627 C  CD1   . ILE   A  1 594 ? 5.43600  -61.63300  -23.03900 1.000 51.11929  ? 586 ILE   A CD1   1 
ATOM   4628 N  N     . LYS   A  1 595 ? 3.70300  -62.39900  -18.22700 1.000 51.09907  ? 587 LYS   A N     1 
ATOM   4629 C  CA    . LYS   A  1 595 ? 3.28800  -63.64400  -17.52700 1.000 51.27476  ? 587 LYS   A CA    1 
ATOM   4630 C  C     . LYS   A  1 595 ? 3.61400  -64.84400  -18.41700 1.000 53.26793  ? 587 LYS   A C     1 
ATOM   4631 O  O     . LYS   A  1 595 ? 4.34100  -65.74800  -17.95700 1.000 53.73186  ? 587 LYS   A O     1 
ATOM   4632 C  CB    . LYS   A  1 595 ? 1.78500  -63.63900  -17.22800 1.000 50.65075  ? 587 LYS   A CB    1 
ATOM   4633 C  CG    . LYS   A  1 595 ? 1.30900  -62.64300  -16.18000 1.000 48.44248  ? 587 LYS   A CG    1 
ATOM   4634 C  CD    . LYS   A  1 595 ? -0.19800 -62.44800  -16.20800 1.000 54.43432  ? 587 LYS   A CD    1 
ATOM   4635 C  CE    . LYS   A  1 595 ? -0.71700 -61.53300  -15.11700 1.000 54.64404  ? 587 LYS   A CE    1 
ATOM   4636 N  NZ    . LYS   A  1 595 ? -0.79700 -62.22900  -13.81200 1.000 51.42278  ? 587 LYS   A NZ    1 
ATOM   4637 N  N     . GLN   A  1 596 ? 3.09400  -64.82400  -19.64800 1.000 47.12439  ? 588 GLN   A N     1 
ATOM   4638 C  CA    . GLN   A  1 596 ? 3.13300  -65.95800  -20.60500 1.000 51.08475  ? 588 GLN   A CA    1 
ATOM   4639 C  C     . GLN   A  1 596 ? 3.92100  -65.54900  -21.84400 1.000 52.56755  ? 588 GLN   A C     1 
ATOM   4640 O  O     . GLN   A  1 596 ? 3.59600  -64.54800  -22.47700 1.000 54.96235  ? 588 GLN   A O     1 
ATOM   4641 C  CB    . GLN   A  1 596 ? 1.70400  -66.36400  -20.95900 1.000 52.36741  ? 588 GLN   A CB    1 
ATOM   4642 C  CG    . GLN   A  1 596 ? 0.98300  -67.05200  -19.81200 1.000 54.39881  ? 588 GLN   A CG    1 
ATOM   4643 C  CD    . GLN   A  1 596 ? 1.59800  -68.39000  -19.48200 1.000 57.83190  ? 588 GLN   A CD    1 
ATOM   4644 O  OE1   . GLN   A  1 596 ? 2.06300  -69.11500  -20.36000 1.000 65.85349  ? 588 GLN   A OE1   1 
ATOM   4645 N  NE2   . GLN   A  1 596 ? 1.60800  -68.73000  -18.20400 1.000 65.62564  ? 588 GLN   A NE2   1 
ATOM   4646 N  N     . PRO   A  1 597 ? 4.97300  -66.30900  -22.23100 1.000 48.41260  ? 589 PRO   A N     1 
ATOM   4647 C  CA    . PRO   A  1 597 ? 5.72000  -66.01700  -23.45200 1.000 51.26785  ? 589 PRO   A CA    1 
ATOM   4648 C  C     . PRO   A  1 597 ? 4.78800  -66.04700  -24.67200 1.000 51.85047  ? 589 PRO   A C     1 
ATOM   4649 O  O     . PRO   A  1 597 ? 3.88600  -66.86400  -24.69400 1.000 57.17743  ? 589 PRO   A O     1 
ATOM   4650 C  CB    . PRO   A  1 597 ? 6.78500  -67.12300  -23.53800 1.000 54.98270  ? 589 PRO   A CB    1 
ATOM   4651 C  CG    . PRO   A  1 597 ? 6.86600  -67.69400  -22.13600 1.000 54.60093  ? 589 PRO   A CG    1 
ATOM   4652 C  CD    . PRO   A  1 597 ? 5.49300  -67.49200  -21.53000 1.000 53.45628  ? 589 PRO   A CD    1 
ATOM   4653 N  N     . ILE   A  1 598 ? 5.01100  -65.14200  -25.62900 1.000 51.51771  ? 590 ILE   A N     1 
ATOM   4654 C  CA    . ILE   A  1 598 ? 4.19300  -64.99800  -26.87000 1.000 55.43897  ? 590 ILE   A CA    1 
ATOM   4655 C  C     . ILE   A  1 598 ? 5.06000  -65.39500  -28.07200 1.000 57.66210  ? 590 ILE   A C     1 
ATOM   4656 O  O     . ILE   A  1 598 ? 6.11400  -64.75600  -28.28400 1.000 55.31581  ? 590 ILE   A O     1 
ATOM   4657 C  CB    . ILE   A  1 598 ? 3.62900  -63.56500  -26.98500 1.000 50.80824  ? 590 ILE   A CB    1 
ATOM   4658 C  CG1   . ILE   A  1 598 ? 2.66000  -63.26000  -25.83900 1.000 45.31052  ? 590 ILE   A CG1   1 
ATOM   4659 C  CG2   . ILE   A  1 598 ? 2.98100  -63.33600  -28.34600 1.000 55.70710  ? 590 ILE   A CG2   1 
ATOM   4660 C  CD1   . ILE   A  1 598 ? 2.25100  -61.80800  -25.73700 1.000 52.37357  ? 590 ILE   A CD1   1 
ATOM   4661 N  N     . THR   A  1 599 ? 4.63500  -66.42500  -28.81200 1.000 53.80509  ? 591 THR   A N     1 
ATOM   4662 C  CA    . THR   A  1 599 ? 5.28500  -66.89400  -30.06400 1.000 54.24992  ? 591 THR   A CA    1 
ATOM   4663 C  C     . THR   A  1 599 ? 5.16600  -65.78800  -31.11800 1.000 58.11265  ? 591 THR   A C     1 
ATOM   4664 O  O     . THR   A  1 599 ? 4.02600  -65.38400  -31.42100 1.000 59.01421  ? 591 THR   A O     1 
ATOM   4665 C  CB    . THR   A  1 599 ? 4.67000  -68.21300  -30.54900 1.000 50.48625  ? 591 THR   A CB    1 
ATOM   4666 O  OG1   . THR   A  1 599 ? 4.96900  -69.21000  -29.57200 1.000 53.95289  ? 591 THR   A OG1   1 
ATOM   4667 C  CG2   . THR   A  1 599 ? 5.19000  -68.65700  -31.89900 1.000 52.36525  ? 591 THR   A CG2   1 
ATOM   4668 N  N     . VAL   A  1 600 ? 6.30200  -65.31000  -31.63100 1.000 53.14343  ? 592 VAL   A N     1 
ATOM   4669 C  CA    . VAL   A  1 600 ? 6.37300  -64.29600  -32.72400 1.000 57.03373  ? 592 VAL   A CA    1 
ATOM   4670 C  C     . VAL   A  1 600 ? 7.01700  -64.96100  -33.94400 1.000 57.54850  ? 592 VAL   A C     1 
ATOM   4671 O  O     . VAL   A  1 600 ? 8.21500  -65.29400  -33.86800 1.000 58.62684  ? 592 VAL   A O     1 
ATOM   4672 C  CB    . VAL   A  1 600 ? 7.14700  -63.04000  -32.28200 1.000 57.48307  ? 592 VAL   A CB    1 
ATOM   4673 C  CG1   . VAL   A  1 600 ? 7.18000  -61.98100  -33.37500 1.000 57.80346  ? 592 VAL   A CG1   1 
ATOM   4674 C  CG2   . VAL   A  1 600 ? 6.57700  -62.45800  -30.99700 1.000 56.68542  ? 592 VAL   A CG2   1 
ATOM   4675 N  N     . ARG   A  1 601 ? 6.23700  -65.16300  -35.01000 1.000 59.31181  ? 593 ARG   A N     1 
ATOM   4676 C  CA    . ARG   A  1 601 ? 6.70900  -65.73800  -36.29800 1.000 63.74288  ? 593 ARG   A CA    1 
ATOM   4677 C  C     . ARG   A  1 601 ? 7.31600  -64.62200  -37.15600 1.000 58.36843  ? 593 ARG   A C     1 
ATOM   4678 O  O     . ARG   A  1 601 ? 6.82900  -63.48100  -37.07600 1.000 61.01427  ? 593 ARG   A O     1 
ATOM   4679 C  CB    . ARG   A  1 601 ? 5.57400  -66.45100  -37.04200 1.000 57.92624  ? 593 ARG   A CB    1 
ATOM   4680 C  CG    . ARG   A  1 601 ? 5.32700  -67.87800  -36.57400 1.000 65.63968  ? 593 ARG   A CG    1 
ATOM   4681 C  CD    . ARG   A  1 601 ? 5.27600  -68.85300  -37.73600 1.000 87.26583  ? 593 ARG   A CD    1 
ATOM   4682 N  NE    . ARG   A  1 601 ? 4.12300  -68.63000  -38.60000 1.000 93.06339  ? 593 ARG   A NE    1 
ATOM   4683 C  CZ    . ARG   A  1 601 ? 3.95600  -69.17000  -39.80600 1.000 101.87276 ? 593 ARG   A CZ    1 
ATOM   4684 N  NH1   . ARG   A  1 601 ? 4.87700  -69.97200  -40.31900 1.000 97.86865  ? 593 ARG   A NH1   1 
ATOM   4685 N  NH2   . ARG   A  1 601 ? 2.86300  -68.89900  -40.50200 1.000 103.39457 ? 593 ARG   A NH2   1 
ATOM   4686 N  N     . GLU   A  1 602 ? 8.33900  -64.96100  -37.94300 1.000 62.60379  ? 594 GLU   A N     1 
ATOM   4687 C  CA    . GLU   A  1 602 ? 9.07800  -64.03900  -38.84600 1.000 67.60757  ? 594 GLU   A CA    1 
ATOM   4688 C  C     . GLU   A  1 602 ? 8.08700  -63.22300  -39.68700 1.000 67.87295  ? 594 GLU   A C     1 
ATOM   4689 O  O     . GLU   A  1 602 ? 7.17900  -63.83100  -40.28900 1.000 64.99537  ? 594 GLU   A O     1 
ATOM   4690 C  CB    . GLU   A  1 602 ? 10.01500 -64.85000  -39.74200 1.000 69.90025  ? 594 GLU   A CB    1 
ATOM   4691 C  CG    . GLU   A  1 602 ? 10.75000 -64.02400  -40.78000 1.000 77.18502  ? 594 GLU   A CG    1 
ATOM   4692 C  CD    . GLU   A  1 602 ? 10.75200 -64.66300  -42.15400 1.000 81.78803  ? 594 GLU   A CD    1 
ATOM   4693 O  OE1   . GLU   A  1 602 ? 9.65100  -64.84700  -42.71200 1.000 82.66074  ? 594 GLU   A OE1   1 
ATOM   4694 O  OE2   . GLU   A  1 602 ? 11.84900 -64.99500  -42.64700 1.000 89.60544  ? 594 GLU   A OE2   1 
ATOM   4695 N  N     . GLY   A  1 603 ? 8.26900  -61.89800  -39.72100 1.000 63.70048  ? 595 GLY   A N     1 
ATOM   4696 C  CA    . GLY   A  1 603 ? 7.43400  -60.95700  -40.49300 1.000 62.51774  ? 595 GLY   A CA    1 
ATOM   4697 C  C     . GLY   A  1 603 ? 6.42300  -60.23800  -39.61700 1.000 60.44793  ? 595 GLY   A C     1 
ATOM   4698 O  O     . GLY   A  1 603 ? 6.13900  -59.06000  -39.90400 1.000 65.48016  ? 595 GLY   A O     1 
ATOM   4699 N  N     . GLN   A  1 604 ? 5.90200  -60.91200  -38.58600 1.000 58.64296  ? 596 GLN   A N     1 
ATOM   4700 C  CA    . GLN   A  1 604 ? 4.84300  -60.38300  -37.68700 1.000 56.81479  ? 596 GLN   A CA    1 
ATOM   4701 C  C     . GLN   A  1 604 ? 5.36700  -59.16300  -36.91900 1.000 60.16315  ? 596 GLN   A C     1 
ATOM   4702 O  O     . GLN   A  1 604 ? 6.60200  -59.01500  -36.78700 1.000 56.26166  ? 596 GLN   A O     1 
ATOM   4703 C  CB    . GLN   A  1 604 ? 4.37500  -61.45300  -36.70000 1.000 55.36730  ? 596 GLN   A CB    1 
ATOM   4704 C  CG    . GLN   A  1 604 ? 3.60800  -62.59700  -37.34400 1.000 56.32196  ? 596 GLN   A CG    1 
ATOM   4705 C  CD    . GLN   A  1 604 ? 2.95600  -63.47500  -36.30400 1.000 60.72702  ? 596 GLN   A CD    1 
ATOM   4706 O  OE1   . GLN   A  1 604 ? 3.61000  -63.99600  -35.40100 1.000 57.45201  ? 596 GLN   A OE1   1 
ATOM   4707 N  NE2   . GLN   A  1 604 ? 1.64800  -63.63800  -36.41700 1.000 61.05818  ? 596 GLN   A NE2   1 
ATOM   4708 N  N     . THR   A  1 605 ? 4.44600  -58.33300  -36.42700 1.000 54.79193  ? 597 THR   A N     1 
ATOM   4709 C  CA    . THR   A  1 605 ? 4.72600  -57.11100  -35.63000 1.000 57.67948  ? 597 THR   A CA    1 
ATOM   4710 C  C     . THR   A  1 605 ? 4.37000  -57.37400  -34.16400 1.000 52.02806  ? 597 THR   A C     1 
ATOM   4711 O  O     . THR   A  1 605 ? 3.25500  -57.87000  -33.91600 1.000 51.75562  ? 597 THR   A O     1 
ATOM   4712 C  CB    . THR   A  1 605 ? 3.93600  -55.91300  -36.16800 1.000 54.59397  ? 597 THR   A CB    1 
ATOM   4713 O  OG1   . THR   A  1 605 ? 4.16800  -55.83300  -37.57500 1.000 60.52075  ? 597 THR   A OG1   1 
ATOM   4714 C  CG2   . THR   A  1 605 ? 4.31400  -54.61000  -35.49700 1.000 54.03885  ? 597 THR   A CG2   1 
ATOM   4715 N  N     . ILE   A  1 606 ? 5.28700  -57.06600  -33.24300 1.000 52.66936  ? 598 ILE   A N     1 
ATOM   4716 C  CA    . ILE   A  1 606 ? 4.99900  -56.97300  -31.78100 1.000 56.94997  ? 598 ILE   A CA    1 
ATOM   4717 C  C     . ILE   A  1 606 ? 4.42100  -55.57800  -31.52200 1.000 51.89764  ? 598 ILE   A C     1 
ATOM   4718 O  O     . ILE   A  1 606 ? 5.15900  -54.59300  -31.72000 1.000 49.50959  ? 598 ILE   A O     1 
ATOM   4719 C  CB    . ILE   A  1 606 ? 6.25900  -57.25500  -30.93300 1.000 50.95449  ? 598 ILE   A CB    1 
ATOM   4720 C  CG1   . ILE   A  1 606 ? 6.72600  -58.70600  -31.08500 1.000 49.39446  ? 598 ILE   A CG1   1 
ATOM   4721 C  CG2   . ILE   A  1 606 ? 6.02600  -56.89100  -29.47300 1.000 46.90065  ? 598 ILE   A CG2   1 
ATOM   4722 C  CD1   . ILE   A  1 606 ? 8.10100  -58.97500  -30.51500 1.000 51.13001  ? 598 ILE   A CD1   1 
ATOM   4723 N  N     . CYS   A  1 607 ? 3.14200  -55.50300  -31.14400 1.000 48.45027  ? 599 CYS   A N     1 
ATOM   4724 C  CA    . CYS   A  1 607 ? 2.46000  -54.25700  -30.70400 1.000 48.94884  ? 599 CYS   A CA    1 
ATOM   4725 C  C     . CYS   A  1 607 ? 2.36100  -54.25700  -29.17500 1.000 53.67635  ? 599 CYS   A C     1 
ATOM   4726 O  O     . CYS   A  1 607 ? 1.58800  -55.07800  -28.63700 1.000 51.19863  ? 599 CYS   A O     1 
ATOM   4727 C  CB    . CYS   A  1 607 ? 1.06900  -54.12700  -31.31200 1.000 49.06278  ? 599 CYS   A CB    1 
ATOM   4728 S  SG    . CYS   A  1 607 ? 0.20100  -52.62500  -30.79200 1.000 50.50148  ? 599 CYS   A SG    1 
ATOM   4729 N  N     . VAL   A  1 608 ? 3.12800  -53.38700  -28.50900 1.000 50.24925  ? 600 VAL   A N     1 
ATOM   4730 C  CA    . VAL   A  1 608 ? 3.13200  -53.23900  -27.02300 1.000 52.25688  ? 600 VAL   A CA    1 
ATOM   4731 C  C     . VAL   A  1 608 ? 2.47700  -51.90100  -26.66100 1.000 51.97589  ? 600 VAL   A C     1 
ATOM   4732 O  O     . VAL   A  1 608 ? 2.62100  -50.93200  -27.43700 1.000 47.85115  ? 600 VAL   A O     1 
ATOM   4733 C  CB    . VAL   A  1 608 ? 4.55000  -53.36200  -26.43300 1.000 49.05490  ? 600 VAL   A CB    1 
ATOM   4734 C  CG1   . VAL   A  1 608 ? 5.41200  -52.14500  -26.72900 1.000 48.19594  ? 600 VAL   A CG1   1 
ATOM   4735 C  CG2   . VAL   A  1 608 ? 4.51200  -53.63600  -24.93900 1.000 48.30544  ? 600 VAL   A CG2   1 
ATOM   4736 N  N     . ARG   A  1 609 ? 1.78300  -51.87500  -25.52100 1.000 51.34817  ? 601 ARG   A N     1 
ATOM   4737 C  CA    . ARG   A  1 609 ? 1.08400  -50.69100  -24.96000 1.000 49.79919  ? 601 ARG   A CA    1 
ATOM   4738 C  C     . ARG   A  1 609 ? 1.68600  -50.38500  -23.58800 1.000 50.83740  ? 601 ARG   A C     1 
ATOM   4739 O  O     . ARG   A  1 609 ? 1.74100  -51.31200  -22.76100 1.000 57.49267  ? 601 ARG   A O     1 
ATOM   4740 C  CB    . ARG   A  1 609 ? -0.41300 -50.97200  -24.80700 1.000 50.23081  ? 601 ARG   A CB    1 
ATOM   4741 C  CG    . ARG   A  1 609 ? -1.05000 -51.65700  -26.00600 1.000 58.01485  ? 601 ARG   A CG    1 
ATOM   4742 C  CD    . ARG   A  1 609 ? -1.47500 -50.67700  -27.08000 1.000 56.23249  ? 601 ARG   A CD    1 
ATOM   4743 N  NE    . ARG   A  1 609 ? -2.13800 -51.36700  -28.18000 1.000 56.74860  ? 601 ARG   A NE    1 
ATOM   4744 C  CZ    . ARG   A  1 609 ? -2.94900 -50.79700  -29.06400 1.000 55.40203  ? 601 ARG   A CZ    1 
ATOM   4745 N  NH1   . ARG   A  1 609 ? -3.21800 -49.50300  -28.99900 1.000 57.60089  ? 601 ARG   A NH1   1 
ATOM   4746 N  NH2   . ARG   A  1 609 ? -3.49600 -51.53100  -30.01500 1.000 59.07698  ? 601 ARG   A NH2   1 
ATOM   4747 N  N     . PHE   A  1 610 ? 2.10800  -49.14100  -23.35400 1.000 49.43289  ? 602 PHE   A N     1 
ATOM   4748 C  CA    . PHE   A  1 610 ? 2.66700  -48.68300  -22.05700 1.000 51.93215  ? 602 PHE   A CA    1 
ATOM   4749 C  C     . PHE   A  1 610 ? 1.88500  -47.46300  -21.56800 1.000 55.89351  ? 602 PHE   A C     1 
ATOM   4750 O  O     . PHE   A  1 610 ? 1.72200  -46.49300  -22.33800 1.000 58.46057  ? 602 PHE   A O     1 
ATOM   4751 C  CB    . PHE   A  1 610 ? 4.16600  -48.40600  -22.18400 1.000 50.90784  ? 602 PHE   A CB    1 
ATOM   4752 C  CG    . PHE   A  1 610 ? 5.03700  -49.54500  -21.72300 1.000 51.36412  ? 602 PHE   A CG    1 
ATOM   4753 C  CD1   . PHE   A  1 610 ? 5.14600  -50.70400  -22.47600 1.000 52.33364  ? 602 PHE   A CD1   1 
ATOM   4754 C  CD2   . PHE   A  1 610 ? 5.73400  -49.46600  -20.52700 1.000 52.89507  ? 602 PHE   A CD2   1 
ATOM   4755 C  CE1   . PHE   A  1 610 ? 5.94400  -51.75400  -22.04900 1.000 50.46756  ? 602 PHE   A CE1   1 
ATOM   4756 C  CE2   . PHE   A  1 610 ? 6.53000  -50.51700  -20.10000 1.000 51.71665  ? 602 PHE   A CE2   1 
ATOM   4757 C  CZ    . PHE   A  1 610 ? 6.63500  -51.65900  -20.86200 1.000 49.81777  ? 602 PHE   A CZ    1 
ATOM   4758 N  N     . TRP   A  1 611 ? 1.40200  -47.54100  -20.32500 1.000 53.59559  ? 603 TRP   A N     1 
ATOM   4759 C  CA    . TRP   A  1 611 ? 0.77500  -46.42800  -19.56800 1.000 52.15434  ? 603 TRP   A CA    1 
ATOM   4760 C  C     . TRP   A  1 611 ? 1.71100  -46.00300  -18.43400 1.000 52.45268  ? 603 TRP   A C     1 
ATOM   4761 O  O     . TRP   A  1 611 ? 2.30500  -46.89600  -17.79800 1.000 47.95495  ? 603 TRP   A O     1 
ATOM   4762 C  CB    . TRP   A  1 611 ? -0.58300 -46.85100  -18.99800 1.000 53.60713  ? 603 TRP   A CB    1 
ATOM   4763 C  CG    . TRP   A  1 611 ? -1.63500 -47.19600  -20.00600 1.000 56.62030  ? 603 TRP   A CG    1 
ATOM   4764 C  CD1   . TRP   A  1 611 ? -2.63400 -46.38600  -20.46200 1.000 56.26957  ? 603 TRP   A CD1   1 
ATOM   4765 C  CD2   . TRP   A  1 611 ? -1.83300 -48.47200  -20.63900 1.000 54.60418  ? 603 TRP   A CD2   1 
ATOM   4766 N  NE1   . TRP   A  1 611 ? -3.42800 -47.06400  -21.34700 1.000 52.73253  ? 603 TRP   A NE1   1 
ATOM   4767 C  CE2   . TRP   A  1 611 ? -2.95900 -48.34400  -21.47700 1.000 54.76489  ? 603 TRP   A CE2   1 
ATOM   4768 C  CE3   . TRP   A  1 611 ? -1.16700 -49.70100  -20.58900 1.000 52.86058  ? 603 TRP   A CE3   1 
ATOM   4769 C  CZ2   . TRP   A  1 611 ? -3.43000 -49.40200  -22.25200 1.000 57.09246  ? 603 TRP   A CZ2   1 
ATOM   4770 C  CZ3   . TRP   A  1 611 ? -1.63000 -50.74500  -21.35900 1.000 50.42859  ? 603 TRP   A CZ3   1 
ATOM   4771 C  CH2   . TRP   A  1 611 ? -2.74900 -50.59500  -22.17700 1.000 53.94770  ? 603 TRP   A CH2   1 
ATOM   4772 N  N     . ARG   A  1 612 ? 1.83500  -44.69400  -18.19800 1.000 56.87278  ? 604 ARG   A N     1 
ATOM   4773 C  CA    . ARG   A  1 612 ? 2.32100  -44.12500  -16.91500 1.000 54.31473  ? 604 ARG   A CA    1 
ATOM   4774 C  C     . ARG   A  1 612 ? 1.08600  -43.65700  -16.14500 1.000 54.21528  ? 604 ARG   A C     1 
ATOM   4775 O  O     . ARG   A  1 612 ? 0.37600  -42.77700  -16.66200 1.000 53.96600  ? 604 ARG   A O     1 
ATOM   4776 C  CB    . ARG   A  1 612 ? 3.32300  -42.99300  -17.15400 1.000 53.70115  ? 604 ARG   A CB    1 
ATOM   4777 C  CG    . ARG   A  1 612 ? 4.19000  -42.67300  -15.94500 1.000 51.27692  ? 604 ARG   A CG    1 
ATOM   4778 C  CD    . ARG   A  1 612 ? 5.23900  -41.62900  -16.27300 1.000 52.35374  ? 604 ARG   A CD    1 
ATOM   4779 N  NE    . ARG   A  1 612 ? 6.20300  -41.41500  -15.19800 1.000 53.02020  ? 604 ARG   A NE    1 
ATOM   4780 C  CZ    . ARG   A  1 612 ? 6.08600  -40.52300  -14.21300 1.000 54.31932  ? 604 ARG   A CZ    1 
ATOM   4781 N  NH1   . ARG   A  1 612 ? 5.02400  -39.73600  -14.12900 1.000 53.51635  ? 604 ARG   A NH1   1 
ATOM   4782 N  NH2   . ARG   A  1 612 ? 7.04000  -40.42300  -13.30300 1.000 55.00214  ? 604 ARG   A NH2   1 
ATOM   4783 N  N     . CYS   A  1 613 ? 0.81000  -44.28300  -14.99800 1.000 55.04171  ? 605 CYS   A N     1 
ATOM   4784 C  CA    . CYS   A  1 613 ? -0.38100 -44.02900  -14.14100 1.000 57.29781  ? 605 CYS   A CA    1 
ATOM   4785 C  C     . CYS   A  1 613 ? 0.07300  -43.43000  -12.80600 1.000 52.61462  ? 605 CYS   A C     1 
ATOM   4786 O  O     . CYS   A  1 613 ? 1.22200  -43.69300  -12.39800 1.000 49.94585  ? 605 CYS   A O     1 
ATOM   4787 C  CB    . CYS   A  1 613 ? -1.15900 -45.31700  -13.90000 1.000 53.69509  ? 605 CYS   A CB    1 
ATOM   4788 S  SG    . CYS   A  1 613 ? -1.64500 -46.17300  -15.42200 1.000 50.35509  ? 605 CYS   A SG    1 
ATOM   4789 N  N     . SER   A  1 614 ? -0.79300 -42.65300  -12.15200 1.000 50.57880  ? 606 SER   A N     1 
ATOM   4790 C  CA    . SER   A  1 614 ? -0.48700 -41.99600  -10.85600 1.000 57.14181  ? 606 SER   A CA    1 
ATOM   4791 C  C     . SER   A  1 614 ? -1.76700 -41.52500  -10.16000 1.000 61.03560  ? 606 SER   A C     1 
ATOM   4792 O  O     . SER   A  1 614 ? -2.74800 -41.19800  -10.85700 1.000 64.41711  ? 606 SER   A O     1 
ATOM   4793 C  CB    . SER   A  1 614 ? 0.47400  -40.84400  -11.04200 1.000 55.08317  ? 606 SER   A CB    1 
ATOM   4794 O  OG    . SER   A  1 614 ? -0.17600 -39.71900  -11.61700 1.000 54.82598  ? 606 SER   A OG    1 
ATOM   4795 N  N     . ASN   A  1 615 ? -1.73200 -41.51200  -8.82600  1.000 53.80864  ? 607 ASN   A N     1 
ATOM   4796 C  CA    . ASN   A  1 615 ? -2.61600 -40.69800  -7.95300  1.000 59.20830  ? 607 ASN   A CA    1 
ATOM   4797 C  C     . ASN   A  1 615 ? -1.69600 -39.77700  -7.13700  1.000 65.25198  ? 607 ASN   A C     1 
ATOM   4798 O  O     . ASN   A  1 615 ? -0.52700 -39.60600  -7.55200  1.000 61.95568  ? 607 ASN   A O     1 
ATOM   4799 C  CB    . ASN   A  1 615 ? -3.56200 -41.58300  -7.13100  1.000 62.74586  ? 607 ASN   A CB    1 
ATOM   4800 C  CG    . ASN   A  1 615 ? -2.85700 -42.63600  -6.30300  1.000 63.04107  ? 607 ASN   A CG    1 
ATOM   4801 O  OD1   . ASN   A  1 615 ? -1.79300 -42.39000  -5.73900  1.000 62.99287  ? 607 ASN   A OD1   1 
ATOM   4802 N  ND2   . ASN   A  1 615 ? -3.45200 -43.81400  -6.21300  1.000 60.40802  ? 607 ASN   A ND2   1 
ATOM   4803 N  N     . SER   A  1 616 ? -2.18800 -39.20700  -6.03300  1.000 63.56518  ? 608 SER   A N     1 
ATOM   4804 C  CA    . SER   A  1 616 ? -1.44100 -38.27000  -5.15200  1.000 63.09824  ? 608 SER   A CA    1 
ATOM   4805 C  C     . SER   A  1 616 ? -0.30400 -38.99500  -4.41600  1.000 63.48153  ? 608 SER   A C     1 
ATOM   4806 O  O     . SER   A  1 616 ? 0.66400  -38.31100  -4.03300  1.000 63.06302  ? 608 SER   A O     1 
ATOM   4807 C  CB    . SER   A  1 616 ? -2.37600 -37.60700  -4.18100  1.000 67.39214  ? 608 SER   A CB    1 
ATOM   4808 O  OG    . SER   A  1 616 ? -3.13600 -38.58000  -3.47900  1.000 70.61301  ? 608 SER   A OG    1 
ATOM   4809 N  N     . LYS   A  1 617 ? -0.41300 -40.31800  -4.23700  1.000 64.15966  ? 609 LYS   A N     1 
ATOM   4810 C  CA    . LYS   A  1 617 ? 0.45900  -41.13300  -3.34400  1.000 63.16842  ? 609 LYS   A CA    1 
ATOM   4811 C  C     . LYS   A  1 617 ? 1.44600  -42.00400  -4.13700  1.000 63.48719  ? 609 LYS   A C     1 
ATOM   4812 O  O     . LYS   A  1 617 ? 2.59900  -42.12000  -3.67200  1.000 59.34819  ? 609 LYS   A O     1 
ATOM   4813 C  CB    . LYS   A  1 617 ? -0.41100 -42.01400  -2.44500  1.000 61.90510  ? 609 LYS   A CB    1 
ATOM   4814 C  CG    . LYS   A  1 617 ? -1.26000 -41.25400  -1.43600  1.000 67.12132  ? 609 LYS   A CG    1 
ATOM   4815 C  CD    . LYS   A  1 617 ? -2.32400 -42.10700  -0.79000  1.000 67.94434  ? 609 LYS   A CD    1 
ATOM   4816 C  CE    . LYS   A  1 617 ? -3.30400 -41.30800  0.04000   1.000 71.55565  ? 609 LYS   A CE    1 
ATOM   4817 N  NZ    . LYS   A  1 617 ? -4.30700 -42.19200  0.68000   1.000 72.63004  ? 609 LYS   A NZ    1 
ATOM   4818 N  N     . LYS   A  1 618 ? 1.01200  -42.60900  -5.25400  1.000 62.83895  ? 610 LYS   A N     1 
ATOM   4819 C  CA    . LYS   A  1 618 ? 1.78700  -43.62400  -6.02700  1.000 55.01535  ? 610 LYS   A CA    1 
ATOM   4820 C  C     . LYS   A  1 618 ? 1.92900  -43.20800  -7.49700  1.000 60.35601  ? 610 LYS   A C     1 
ATOM   4821 O  O     . LYS   A  1 618 ? 1.01500  -42.54700  -8.02600  1.000 60.95962  ? 610 LYS   A O     1 
ATOM   4822 C  CB    . LYS   A  1 618 ? 1.09400  -44.99100  -6.00200  1.000 51.81134  ? 610 LYS   A CB    1 
ATOM   4823 C  CG    . LYS   A  1 618 ? 0.94000  -45.64400  -4.63600  1.000 61.00210  ? 610 LYS   A CG    1 
ATOM   4824 C  CD    . LYS   A  1 618 ? 2.23800  -45.77300  -3.86100  1.000 69.89212  ? 610 LYS   A CD    1 
ATOM   4825 C  CE    . LYS   A  1 618 ? 2.11200  -46.62300  -2.61400  1.000 66.30364  ? 610 LYS   A CE    1 
ATOM   4826 N  NZ    . LYS   A  1 618 ? 3.21100  -46.34600  -1.65900  1.000 58.12738  ? 610 LYS   A NZ    1 
ATOM   4827 N  N     . VAL   A  1 619 ? 3.03800  -43.61500  -8.12100  1.000 55.90386  ? 611 VAL   A N     1 
ATOM   4828 C  CA    . VAL   A  1 619 ? 3.26300  -43.62500  -9.59700  1.000 54.25772  ? 611 VAL   A CA    1 
ATOM   4829 C  C     . VAL   A  1 619 ? 3.61000  -45.06400  -9.99500  1.000 53.88977  ? 611 VAL   A C     1 
ATOM   4830 O  O     . VAL   A  1 619 ? 4.40200  -45.69600  -9.27100  1.000 56.60471  ? 611 VAL   A O     1 
ATOM   4831 C  CB    . VAL   A  1 619 ? 4.37500  -42.63700  -10.00100 1.000 54.84233  ? 611 VAL   A CB    1 
ATOM   4832 C  CG1   . VAL   A  1 619 ? 4.78800  -42.79500  -11.46000 1.000 50.01543  ? 611 VAL   A CG1   1 
ATOM   4833 C  CG2   . VAL   A  1 619 ? 3.97400  -41.20000  -9.71300  1.000 55.11382  ? 611 VAL   A CG2   1 
ATOM   4834 N  N     . TRP   A  1 620 ? 3.03900  -45.56600  -11.09300 1.000 49.14554  ? 612 TRP   A N     1 
ATOM   4835 C  CA    . TRP   A  1 620 ? 3.27600  -46.95400  -11.57400 1.000 51.94201  ? 612 TRP   A CA    1 
ATOM   4836 C  C     . TRP   A  1 620 ? 3.11400  -47.03700  -13.09500 1.000 48.02332  ? 612 TRP   A C     1 
ATOM   4837 O  O     . TRP   A  1 620 ? 2.46300  -46.15100  -13.68100 1.000 50.68906  ? 612 TRP   A O     1 
ATOM   4838 C  CB    . TRP   A  1 620 ? 2.35400  -47.94000  -10.84600 1.000 50.96100  ? 612 TRP   A CB    1 
ATOM   4839 C  CG    . TRP   A  1 620 ? 0.89500  -47.80700  -11.16200 1.000 49.38267  ? 612 TRP   A CG    1 
ATOM   4840 C  CD1   . TRP   A  1 620 ? 0.18300  -48.54300  -12.06400 1.000 46.58930  ? 612 TRP   A CD1   1 
ATOM   4841 C  CD2   . TRP   A  1 620 ? -0.04800 -46.90700  -10.54800 1.000 51.92561  ? 612 TRP   A CD2   1 
ATOM   4842 N  NE1   . TRP   A  1 620 ? -1.12900 -48.15700  -12.06400 1.000 48.55074  ? 612 TRP   A NE1   1 
ATOM   4843 C  CE2   . TRP   A  1 620 ? -1.30400 -47.15800  -11.14300 1.000 49.51675  ? 612 TRP   A CE2   1 
ATOM   4844 C  CE3   . TRP   A  1 620 ? 0.04300  -45.91700  -9.56300  1.000 53.23759  ? 612 TRP   A CE3   1 
ATOM   4845 C  CZ2   . TRP   A  1 620 ? -2.45200 -46.45000  -10.78800 1.000 48.53084  ? 612 TRP   A CZ2   1 
ATOM   4846 C  CZ3   . TRP   A  1 620 ? -1.09200 -45.21800  -9.21300  1.000 53.26139  ? 612 TRP   A CZ3   1 
ATOM   4847 C  CH2   . TRP   A  1 620 ? -2.32200 -45.48400  -9.81700  1.000 50.69090  ? 612 TRP   A CH2   1 
ATOM   4848 N  N     . TYR   A  1 621 ? 3.71300  -48.06500  -13.69900 1.000 47.10666  ? 613 TYR   A N     1 
ATOM   4849 C  CA    . TYR   A  1 621 ? 3.54500  -48.43000  -15.12800 1.000 47.48700  ? 613 TYR   A CA    1 
ATOM   4850 C  C     . TYR   A  1 621 ? 2.57200  -49.60900  -15.23800 1.000 47.95866  ? 613 TYR   A C     1 
ATOM   4851 O  O     . TYR   A  1 621 ? 2.64100  -50.53800  -14.40500 1.000 47.25285  ? 613 TYR   A O     1 
ATOM   4852 C  CB    . TYR   A  1 621 ? 4.88700  -48.79600  -15.76300 1.000 43.97785  ? 613 TYR   A CB    1 
ATOM   4853 C  CG    . TYR   A  1 621 ? 5.94100  -47.72000  -15.70400 1.000 47.21665  ? 613 TYR   A CG    1 
ATOM   4854 C  CD1   . TYR   A  1 621 ? 5.89400  -46.62500  -16.54900 1.000 45.31338  ? 613 TYR   A CD1   1 
ATOM   4855 C  CD2   . TYR   A  1 621 ? 7.00500  -47.81300  -14.82300 1.000 48.60724  ? 613 TYR   A CD2   1 
ATOM   4856 C  CE1   . TYR   A  1 621 ? 6.86800  -45.64000  -16.50800 1.000 48.38331  ? 613 TYR   A CE1   1 
ATOM   4857 C  CE2   . TYR   A  1 621 ? 7.98700  -46.83900  -14.76900 1.000 45.24754  ? 613 TYR   A CE2   1 
ATOM   4858 C  CZ    . TYR   A  1 621 ? 7.91800  -45.74800  -15.61400 1.000 45.60307  ? 613 TYR   A CZ    1 
ATOM   4859 O  OH    . TYR   A  1 621 ? 8.88600  -44.78800  -15.56900 1.000 50.97793  ? 613 TYR   A OH    1 
ATOM   4860 N  N     . GLU   A  1 622 ? 1.67500  -49.54500  -16.22600 1.000 49.28696  ? 614 GLU   A N     1 
ATOM   4861 C  CA    . GLU   A  1 622 ? 0.87000  -50.69000  -16.72600 1.000 51.13244  ? 614 GLU   A CA    1 
ATOM   4862 C  C     . GLU   A  1 622 ? 1.30200  -50.95300  -18.17100 1.000 44.45925  ? 614 GLU   A C     1 
ATOM   4863 O  O     . GLU   A  1 622 ? 1.71400  -49.98500  -18.83700 1.000 49.42744  ? 614 GLU   A O     1 
ATOM   4864 C  CB    . GLU   A  1 622 ? -0.62800 -50.38800  -16.64800 1.000 50.89506  ? 614 GLU   A CB    1 
ATOM   4865 C  CG    . GLU   A  1 622 ? -1.07600 -49.81000  -15.31600 1.000 49.42627  ? 614 GLU   A CG    1 
ATOM   4866 C  CD    . GLU   A  1 622 ? -2.58400 -49.73900  -15.12700 1.000 54.69845  ? 614 GLU   A CD    1 
ATOM   4867 O  OE1   . GLU   A  1 622 ? -3.29500 -50.59600  -15.68900 1.000 57.44248  ? 614 GLU   A OE1   1 
ATOM   4868 O  OE2   . GLU   A  1 622 ? -3.05100 -48.82400  -14.42200 1.000 56.61767  ? 614 GLU   A OE2   1 
ATOM   4869 N  N     . TRP   A  1 623 ? 1.22700  -52.20200  -18.63700 1.000 46.55780  ? 615 TRP   A N     1 
ATOM   4870 C  CA    . TRP   A  1 623 ? 1.64400  -52.57900  -20.01500 1.000 47.66443  ? 615 TRP   A CA    1 
ATOM   4871 C  C     . TRP   A  1 623 ? 0.91900  -53.84400  -20.48400 1.000 47.95304  ? 615 TRP   A C     1 
ATOM   4872 O  O     . TRP   A  1 623 ? 0.57900  -54.68700  -19.63900 1.000 48.47143  ? 615 TRP   A O     1 
ATOM   4873 C  CB    . TRP   A  1 623 ? 3.16900  -52.73300  -20.09600 1.000 45.15808  ? 615 TRP   A CB    1 
ATOM   4874 C  CG    . TRP   A  1 623 ? 3.72300  -53.83000  -19.24000 1.000 50.16911  ? 615 TRP   A CG    1 
ATOM   4875 C  CD1   . TRP   A  1 623 ? 3.98300  -55.11300  -19.62100 1.000 46.83889  ? 615 TRP   A CD1   1 
ATOM   4876 C  CD2   . TRP   A  1 623 ? 4.09200  -53.74100  -17.85100 1.000 52.86950  ? 615 TRP   A CD2   1 
ATOM   4877 N  NE1   . TRP   A  1 623 ? 4.49300  -55.82600  -18.57200 1.000 48.17233  ? 615 TRP   A NE1   1 
ATOM   4878 C  CE2   . TRP   A  1 623 ? 4.57100  -55.01300  -17.47200 1.000 49.49413  ? 615 TRP   A CE2   1 
ATOM   4879 C  CE3   . TRP   A  1 623 ? 4.06700  -52.71800  -16.89400 1.000 49.91910  ? 615 TRP   A CE3   1 
ATOM   4880 C  CZ2   . TRP   A  1 623 ? 5.01100  -55.28600  -16.17600 1.000 47.18751  ? 615 TRP   A CZ2   1 
ATOM   4881 C  CZ3   . TRP   A  1 623 ? 4.50900  -52.98700  -15.61600 1.000 48.92644  ? 615 TRP   A CZ3   1 
ATOM   4882 C  CH2   . TRP   A  1 623 ? 4.97300  -54.25500  -15.26500 1.000 48.51665  ? 615 TRP   A CH2   1 
ATOM   4883 N  N     . ALA   A  1 624 ? 0.69700  -53.95100  -21.79600 1.000 50.76097  ? 616 ALA   A N     1 
ATOM   4884 C  CA    . ALA   A  1 624 ? 0.07300  -55.11400  -22.46900 1.000 48.14649  ? 616 ALA   A CA    1 
ATOM   4885 C  C     . ALA   A  1 624 ? 0.64000  -55.24900  -23.88400 1.000 50.62673  ? 616 ALA   A C     1 
ATOM   4886 O  O     . ALA   A  1 624 ? 0.96300  -54.21300  -24.49500 1.000 52.72406  ? 616 ALA   A O     1 
ATOM   4887 C  CB    . ALA   A  1 624 ? -1.42600 -54.95200  -22.49600 1.000 46.22081  ? 616 ALA   A CB    1 
ATOM   4888 N  N     . VAL   A  1 625 ? 0.76600  -56.48900  -24.36300 1.000 50.73607  ? 617 VAL   A N     1 
ATOM   4889 C  CA    . VAL   A  1 625 ? 1.02700  -56.83600  -25.79000 1.000 46.43601  ? 617 VAL   A CA    1 
ATOM   4890 C  C     . VAL   A  1 625 ? -0.33800 -57.04500  -26.45300 1.000 48.24986  ? 617 VAL   A C     1 
ATOM   4891 O  O     . VAL   A  1 625 ? -1.18000 -57.71400  -25.83300 1.000 44.13507  ? 617 VAL   A O     1 
ATOM   4892 C  CB    . VAL   A  1 625 ? 1.93100  -58.08100  -25.89700 1.000 48.54851  ? 617 VAL   A CB    1 
ATOM   4893 C  CG1   . VAL   A  1 625 ? 2.22400  -58.46800  -27.33800 1.000 51.22479  ? 617 VAL   A CG1   1 
ATOM   4894 C  CG2   . VAL   A  1 625 ? 3.23100  -57.88900  -25.13200 1.000 49.48026  ? 617 VAL   A CG2   1 
ATOM   4895 N  N     . THR   A  1 626 ? -0.56100 -56.45700  -27.63600 1.000 54.75380  ? 618 THR   A N     1 
ATOM   4896 C  CA    . THR   A  1 626 ? -1.83800 -56.53600  -28.40300 1.000 52.19695  ? 618 THR   A CA    1 
ATOM   4897 C  C     . THR   A  1 626 ? -1.62700 -57.21600  -29.76300 1.000 54.82998  ? 618 THR   A C     1 
ATOM   4898 O  O     . THR   A  1 626 ? -2.64100 -57.45400  -30.45200 1.000 62.71227  ? 618 THR   A O     1 
ATOM   4899 C  CB    . THR   A  1 626 ? -2.46800 -55.14800  -28.58000 1.000 54.18550  ? 618 THR   A CB    1 
ATOM   4900 O  OG1   . THR   A  1 626 ? -1.44300 -54.21600  -28.92700 1.000 54.98878  ? 618 THR   A OG1   1 
ATOM   4901 C  CG2   . THR   A  1 626 ? -3.18400 -54.67100  -27.33700 1.000 54.96022  ? 618 THR   A CG2   1 
ATOM   4902 N  N     . ALA   A  1 627 ? -0.37800 -57.51000  -30.14400 1.000 54.54271  ? 619 ALA   A N     1 
ATOM   4903 C  CA    . ALA   A  1 627 ? -0.03000 -58.22900  -31.39400 1.000 55.54663  ? 619 ALA   A CA    1 
ATOM   4904 C  C     . ALA   A  1 627 ? 1.33500  -58.89400  -31.24300 1.000 55.34247  ? 619 ALA   A C     1 
ATOM   4905 O  O     . ALA   A  1 627 ? 2.21700  -58.34200  -30.58700 1.000 49.63417  ? 619 ALA   A O     1 
ATOM   4906 C  CB    . ALA   A  1 627 ? -0.05100 -57.27300  -32.55900 1.000 49.94785  ? 619 ALA   A CB    1 
ATOM   4907 N  N     . PRO   A  1 628 ? 1.56600  -60.08900  -31.84000 1.000 55.34611  ? 620 PRO   A N     1 
ATOM   4908 C  CA    . PRO   A  1 628 ? 0.57300  -60.77400  -32.67200 1.000 56.15514  ? 620 PRO   A CA    1 
ATOM   4909 C  C     . PRO   A  1 628 ? -0.56400 -61.43700  -31.87800 1.000 60.56493  ? 620 PRO   A C     1 
ATOM   4910 O  O     . PRO   A  1 628 ? -1.54400 -61.83200  -32.49000 1.000 64.44154  ? 620 PRO   A O     1 
ATOM   4911 C  CB    . PRO   A  1 628 ? 1.40400  -61.85400  -33.37800 1.000 55.72968  ? 620 PRO   A CB    1 
ATOM   4912 C  CG    . PRO   A  1 628 ? 2.49100  -62.18000  -32.38200 1.000 55.37391  ? 620 PRO   A CG    1 
ATOM   4913 C  CD    . PRO   A  1 628 ? 2.81900  -60.85200  -31.73100 1.000 55.25886  ? 620 PRO   A CD    1 
ATOM   4914 N  N     . VAL   A  1 629 ? -0.39100 -61.55700  -30.55800 1.000 58.76008  ? 621 VAL   A N     1 
ATOM   4915 C  CA    . VAL   A  1 629 ? -1.40500 -62.06900  -29.58800 1.000 55.88263  ? 621 VAL   A CA    1 
ATOM   4916 C  C     . VAL   A  1 629 ? -1.59500 -61.00700  -28.49800 1.000 60.92745  ? 621 VAL   A C     1 
ATOM   4917 O  O     . VAL   A  1 629 ? -0.66100 -60.20200  -28.28800 1.000 60.62111  ? 621 VAL   A O     1 
ATOM   4918 C  CB    . VAL   A  1 629 ? -0.96000 -63.42500  -29.00400 1.000 54.51835  ? 621 VAL   A CB    1 
ATOM   4919 C  CG1   . VAL   A  1 629 ? -1.71800 -63.80300  -27.73900 1.000 55.91902  ? 621 VAL   A CG1   1 
ATOM   4920 C  CG2   . VAL   A  1 629 ? -1.07200 -64.53200  -30.03800 1.000 65.75034  ? 621 VAL   A CG2   1 
ATOM   4921 N  N     . CYS   A  1 630 ? -2.76200 -61.00000  -27.84400 1.000 57.31641  ? 622 CYS   A N     1 
ATOM   4922 C  CA    . CYS   A  1 630 ? -3.05900 -60.15200  -26.65900 1.000 50.60989  ? 622 CYS   A CA    1 
ATOM   4923 C  C     . CYS   A  1 630 ? -2.52900 -60.83400  -25.39700 1.000 52.18023  ? 622 CYS   A C     1 
ATOM   4924 O  O     . CYS   A  1 630 ? -2.88600 -62.00500  -25.16300 1.000 50.10473  ? 622 CYS   A O     1 
ATOM   4925 C  CB    . CYS   A  1 630 ? -4.54900 -59.88400  -26.49700 1.000 50.45647  ? 622 CYS   A CB    1 
ATOM   4926 S  SG    . CYS   A  1 630 ? -5.06800 -58.31300  -27.23200 1.000 63.41133  ? 622 CYS   A SG    1 
ATOM   4927 N  N     . SER   A  1 631 ? -1.69500 -60.12400  -24.63500 1.000 54.57215  ? 623 SER   A N     1 
ATOM   4928 C  CA    . SER   A  1 631 ? -1.33700 -60.44500  -23.23000 1.000 48.03972  ? 623 SER   A CA    1 
ATOM   4929 C  C     . SER   A  1 631 ? -2.38700 -59.82100  -22.31100 1.000 46.30240  ? 623 SER   A C     1 
ATOM   4930 O  O     . SER   A  1 631 ? -3.17400 -58.98500  -22.79300 1.000 48.74841  ? 623 SER   A O     1 
ATOM   4931 C  CB    . SER   A  1 631 ? 0.03900  -59.94600  -22.88800 1.000 46.43281  ? 623 SER   A CB    1 
ATOM   4932 O  OG    . SER   A  1 631 ? 0.03600  -58.53800  -22.72000 1.000 46.38381  ? 623 SER   A OG    1 
ATOM   4933 N  N     . ALA   A  1 632 ? -2.39200 -60.21100  -21.03500 1.000 53.45586  ? 624 ALA   A N     1 
ATOM   4934 C  CA    . ALA   A  1 632 ? -3.14600 -59.52200  -19.96500 1.000 48.74323  ? 624 ALA   A CA    1 
ATOM   4935 C  C     . ALA   A  1 632 ? -2.50000 -58.15300  -19.74700 1.000 48.14276  ? 624 ALA   A C     1 
ATOM   4936 O  O     . ALA   A  1 632 ? -1.28900 -58.02800  -20.01100 1.000 46.50804  ? 624 ALA   A O     1 
ATOM   4937 C  CB    . ALA   A  1 632 ? -3.14700 -60.34600  -18.70200 1.000 43.49859  ? 624 ALA   A CB    1 
ATOM   4938 N  N     . ILE   A  1 633 ? -3.28200 -57.15900  -19.32200 1.000 45.49945  ? 625 ILE   A N     1 
ATOM   4939 C  CA    . ILE   A  1 633 ? -2.73700 -55.86100  -18.82900 1.000 48.63503  ? 625 ILE   A CA    1 
ATOM   4940 C  C     . ILE   A  1 633 ? -1.98000 -56.16400  -17.53000 1.000 49.18048  ? 625 ILE   A C     1 
ATOM   4941 O  O     . ILE   A  1 633 ? -2.58900 -56.74000  -16.60800 1.000 43.58480  ? 625 ILE   A O     1 
ATOM   4942 C  CB    . ILE   A  1 633 ? -3.84900 -54.80800  -18.65900 1.000 46.74288  ? 625 ILE   A CB    1 
ATOM   4943 C  CG1   . ILE   A  1 633 ? -4.50500 -54.47600  -20.00100 1.000 51.16741  ? 625 ILE   A CG1   1 
ATOM   4944 C  CG2   . ILE   A  1 633 ? -3.31500 -53.55600  -17.97800 1.000 50.72274  ? 625 ILE   A CG2   1 
ATOM   4945 C  CD1   . ILE   A  1 633 ? -5.84000 -53.78700  -19.87600 1.000 56.03401  ? 625 ILE   A CD1   1 
ATOM   4946 N  N     . HIS   A  1 634 ? -0.68500 -55.84500  -17.50000 1.000 45.79821  ? 626 HIS   A N     1 
ATOM   4947 C  CA    . HIS   A  1 634 ? 0.24500  -56.13600  -16.37900 1.000 48.01272  ? 626 HIS   A CA    1 
ATOM   4948 C  C     . HIS   A  1 634 ? 0.24100  -54.96200  -15.39500 1.000 53.94417  ? 626 HIS   A C     1 
ATOM   4949 O  O     . HIS   A  1 634 ? 0.31400  -53.80500  -15.85500 1.000 52.75163  ? 626 HIS   A O     1 
ATOM   4950 C  CB    . HIS   A  1 634 ? 1.64900  -56.44500  -16.91700 1.000 47.03368  ? 626 HIS   A CB    1 
ATOM   4951 C  CG    . HIS   A  1 634 ? 1.76200  -57.79200  -17.54700 1.000 49.02570  ? 626 HIS   A CG    1 
ATOM   4952 N  ND1   . HIS   A  1 634 ? 1.07200  -58.13100  -18.69200 1.000 51.60102  ? 626 HIS   A ND1   1 
ATOM   4953 C  CD2   . HIS   A  1 634 ? 2.48100  -58.88200  -17.20400 1.000 46.62672  ? 626 HIS   A CD2   1 
ATOM   4954 C  CE1   . HIS   A  1 634 ? 1.34900  -59.37700  -19.01800 1.000 50.38517  ? 626 HIS   A CE1   1 
ATOM   4955 N  NE2   . HIS   A  1 634 ? 2.21400  -59.85700  -18.12500 1.000 44.20546  ? 626 HIS   A NE2   1 
ATOM   4956 N  N     . ASN   A  1 635 ? 0.13900  -55.26900  -14.09800 1.000 46.79263  ? 627 ASN   A N     1 
ATOM   4957 C  CA    . ASN   A  1 635 ? 0.19200  -54.30500  -12.96700 1.000 50.04798  ? 627 ASN   A CA    1 
ATOM   4958 C  C     . ASN   A  1 635 ? -1.00000 -53.34800  -13.02700 1.000 49.88261  ? 627 ASN   A C     1 
ATOM   4959 O  O     . ASN   A  1 635 ? -0.83700 -52.15000  -12.81100 1.000 46.15809  ? 627 ASN   A O     1 
ATOM   4960 C  CB    . ASN   A  1 635 ? 1.52900  -53.55600  -12.94900 1.000 49.02806  ? 627 ASN   A CB    1 
ATOM   4961 C  CG    . ASN   A  1 635 ? 1.81200  -52.86100  -11.63400 1.000 47.77334  ? 627 ASN   A CG    1 
ATOM   4962 O  OD1   . ASN   A  1 635 ? 1.49000  -53.38100  -10.56900 1.000 47.18432  ? 627 ASN   A OD1   1 
ATOM   4963 N  ND2   . ASN   A  1 635 ? 2.42200  -51.68800  -11.69800 1.000 45.73249  ? 627 ASN   A ND2   1 
ATOM   4964 N  N     . PRO   A  1 636 ? -2.24200 -53.83100  -13.27700 1.000 48.40718  ? 628 PRO   A N     1 
ATOM   4965 C  CA    . PRO   A  1 636 ? -3.41100 -52.95200  -13.28200 1.000 49.93434  ? 628 PRO   A CA    1 
ATOM   4966 C  C     . PRO   A  1 636 ? -3.63700 -52.32100  -11.89900 1.000 52.59091  ? 628 PRO   A C     1 
ATOM   4967 O  O     . PRO   A  1 636 ? -3.67700 -53.05500  -10.92700 1.000 55.96514  ? 628 PRO   A O     1 
ATOM   4968 C  CB    . PRO   A  1 636 ? -4.57600 -53.87300  -13.67500 1.000 50.76589  ? 628 PRO   A CB    1 
ATOM   4969 C  CG    . PRO   A  1 636 ? -4.10100 -55.26100  -13.30300 1.000 49.36179  ? 628 PRO   A CG    1 
ATOM   4970 C  CD    . PRO   A  1 636 ? -2.60300 -55.23600  -13.52700 1.000 46.51871  ? 628 PRO   A CD    1 
ATOM   4971 N  N     . THR   A  1 637 ? -3.74700 -50.98900  -11.85100 1.000 50.71363  ? 629 THR   A N     1 
ATOM   4972 C  CA    . THR   A  1 637 ? -3.99300 -50.17800  -10.62400 1.000 50.82426  ? 629 THR   A CA    1 
ATOM   4973 C  C     . THR   A  1 637 ? -2.79600 -50.28700  -9.66600  1.000 49.43511  ? 629 THR   A C     1 
ATOM   4974 O  O     . THR   A  1 637 ? -2.97800 -50.01300  -8.46700  1.000 55.33165  ? 629 THR   A O     1 
ATOM   4975 C  CB    . THR   A  1 637 ? -5.30900 -50.60000  -9.95500  1.000 60.64220  ? 629 THR   A CB    1 
ATOM   4976 O  OG1   . THR   A  1 637 ? -6.24900 -50.89700  -10.98600 1.000 62.93178  ? 629 THR   A OG1   1 
ATOM   4977 C  CG2   . THR   A  1 637 ? -5.88800 -49.53700  -9.04600  1.000 65.46722  ? 629 THR   A CG2   1 
ATOM   4978 N  N     . GLY   A  1 638 ? -1.61400 -50.64800  -10.17800 1.000 49.50733  ? 630 GLY   A N     1 
ATOM   4979 C  CA    . GLY   A  1 638 ? -0.36800 -50.79700  -9.39900  1.000 49.22187  ? 630 GLY   A CA    1 
ATOM   4980 C  C     . GLY   A  1 638 ? -0.45000 -51.88900  -8.33700  1.000 52.39925  ? 630 GLY   A C     1 
ATOM   4981 O  O     . GLY   A  1 638 ? 0.32600  -51.81600  -7.37200  1.000 53.21492  ? 630 GLY   A O     1 
ATOM   4982 N  N     . ARG   A  1 639 ? -1.32100 -52.88700  -8.52000  1.000 46.69715  ? 631 ARG   A N     1 
ATOM   4983 C  CA    . ARG   A  1 639 ? -1.61200 -53.94400  -7.51200  1.000 47.30980  ? 631 ARG   A CA    1 
ATOM   4984 C  C     . ARG   A  1 639 ? -0.33300 -54.71200  -7.15100  1.000 47.05102  ? 631 ARG   A C     1 
ATOM   4985 O  O     . ARG   A  1 639 ? -0.23800 -55.17100  -5.99600  1.000 60.21785  ? 631 ARG   A O     1 
ATOM   4986 C  CB    . ARG   A  1 639 ? -2.69200 -54.90200  -8.02500  1.000 45.17234  ? 631 ARG   A CB    1 
ATOM   4987 C  CG    . ARG   A  1 639 ? -2.26700 -55.75100  -9.21500  1.000 55.47675  ? 631 ARG   A CG    1 
ATOM   4988 C  CD    . ARG   A  1 639 ? -3.34900 -56.72700  -9.63000  1.000 55.15265  ? 631 ARG   A CD    1 
ATOM   4989 N  NE    . ARG   A  1 639 ? -3.01900 -57.43800  -10.85500 1.000 48.37417  ? 631 ARG   A NE    1 
ATOM   4990 C  CZ    . ARG   A  1 639 ? -3.84600 -58.25800  -11.49500 1.000 57.85474  ? 631 ARG   A CZ    1 
ATOM   4991 N  NH1   . ARG   A  1 639 ? -5.06100 -58.48100  -11.02000 1.000 60.62889  ? 631 ARG   A NH1   1 
ATOM   4992 N  NH2   . ARG   A  1 639 ? -3.45700 -58.85400  -12.61000 1.000 54.78690  ? 631 ARG   A NH2   1 
ATOM   4993 N  N     . SER   A  1 640 ? 0.60300  -54.85300  -8.09300  1.000 47.44306  ? 632 SER   A N     1 
ATOM   4994 C  CA    . SER   A  1 640 ? 1.86100  -55.63300  -7.93900  1.000 48.81114  ? 632 SER   A CA    1 
ATOM   4995 C  C     . SER   A  1 640 ? 3.05500  -54.70800  -7.66500  1.000 48.81002  ? 632 SER   A C     1 
ATOM   4996 O  O     . SER   A  1 640 ? 3.98900  -55.15700  -6.98000  1.000 52.16235  ? 632 SER   A O     1 
ATOM   4997 C  CB    . SER   A  1 640 ? 2.11800  -56.49200  -9.15400  1.000 51.93603  ? 632 SER   A CB    1 
ATOM   4998 O  OG    . SER   A  1 640 ? 1.20400  -57.57600  -9.21600  1.000 52.95674  ? 632 SER   A OG    1 
ATOM   4999 N  N     . TYR   A  1 641 ? 3.04200  -53.48000  -8.19100  1.000 49.87563  ? 633 TYR   A N     1 
ATOM   5000 C  CA    . TYR   A  1 641 ? 4.21000  -52.56000  -8.17700  1.000 50.43300  ? 633 TYR   A CA    1 
ATOM   5001 C  C     . TYR   A  1 641 ? 3.75700  -51.09700  -8.24600  1.000 50.78833  ? 633 TYR   A C     1 
ATOM   5002 O  O     . TYR   A  1 641 ? 3.04700  -50.72500  -9.19800  1.000 51.05677  ? 633 TYR   A O     1 
ATOM   5003 C  CB    . TYR   A  1 641 ? 5.14100  -52.87600  -9.34900  1.000 49.48760  ? 633 TYR   A CB    1 
ATOM   5004 C  CG    . TYR   A  1 641 ? 6.40400  -52.05400  -9.39500  1.000 52.12820  ? 633 TYR   A CG    1 
ATOM   5005 C  CD1   . TYR   A  1 641 ? 7.51900  -52.41800  -8.65600  1.000 51.20817  ? 633 TYR   A CD1   1 
ATOM   5006 C  CD2   . TYR   A  1 641 ? 6.49300  -50.92000  -10.18800 1.000 48.71714  ? 633 TYR   A CD2   1 
ATOM   5007 C  CE1   . TYR   A  1 641 ? 8.68800  -51.67500  -8.69700  1.000 51.70620  ? 633 TYR   A CE1   1 
ATOM   5008 C  CE2   . TYR   A  1 641 ? 7.65500  -50.16600  -10.24300 1.000 50.29301  ? 633 TYR   A CE2   1 
ATOM   5009 C  CZ    . TYR   A  1 641 ? 8.75600  -50.54500  -9.49400  1.000 54.13078  ? 633 TYR   A CZ    1 
ATOM   5010 O  OH    . TYR   A  1 641 ? 9.90500  -49.81100  -9.54100  1.000 55.67746  ? 633 TYR   A OH    1 
ATOM   5011 N  N     . THR   A  1 642 ? 4.18600  -50.29600  -7.26600  1.000 53.35007  ? 634 THR   A N     1 
ATOM   5012 C  CA    . THR   A  1 642 ? 4.00900  -48.82000  -7.22200  1.000 54.07603  ? 634 THR   A CA    1 
ATOM   5013 C  C     . THR   A  1 642 ? 5.32800  -48.16300  -6.81300  1.000 53.25326  ? 634 THR   A C     1 
ATOM   5014 O  O     . THR   A  1 642 ? 6.14400  -48.83400  -6.15300  1.000 56.39663  ? 634 THR   A O     1 
ATOM   5015 C  CB    . THR   A  1 642 ? 2.89000  -48.39900  -6.26300  1.000 52.09043  ? 634 THR   A CB    1 
ATOM   5016 O  OG1   . THR   A  1 642 ? 3.17500  -48.93000  -4.96900  1.000 51.33527  ? 634 THR   A OG1   1 
ATOM   5017 C  CG2   . THR   A  1 642 ? 1.52400  -48.85800  -6.72400  1.000 58.21015  ? 634 THR   A CG2   1 
ATOM   5018 N  N     . ILE   A  1 643 ? 5.51100  -46.90400  -7.21100  1.000 51.70133  ? 635 ILE   A N     1 
ATOM   5019 C  CA    . ILE   A  1 643 ? 6.68300  -46.05100  -6.86300  1.000 56.62212  ? 635 ILE   A CA    1 
ATOM   5020 C  C     . ILE   A  1 643 ? 6.15800  -44.90500  -5.98800  1.000 61.31878  ? 635 ILE   A C     1 
ATOM   5021 O  O     . ILE   A  1 643 ? 5.25400  -44.18000  -6.44800  1.000 61.05804  ? 635 ILE   A O     1 
ATOM   5022 C  CB    . ILE   A  1 643 ? 7.39600  -45.56400  -8.14200  1.000 54.50435  ? 635 ILE   A CB    1 
ATOM   5023 C  CG1   . ILE   A  1 643 ? 7.52400  -46.68000  -9.18500  1.000 57.79328  ? 635 ILE   A CG1   1 
ATOM   5024 C  CG2   . ILE   A  1 643 ? 8.74800  -44.96000  -7.80500  1.000 57.12687  ? 635 ILE   A CG2   1 
ATOM   5025 C  CD1   . ILE   A  1 643 ? 7.73500  -46.19300  -10.60400 1.000 52.26430  ? 635 ILE   A CD1   1 
ATOM   5026 N  N     . GLY   A  1 644 ? 6.66400  -44.78600  -4.75500  1.000 60.53780  ? 636 GLY   A N     1 
ATOM   5027 C  CA    . GLY   A  1 644 ? 6.11200  -43.89500  -3.71700  1.000 56.11169  ? 636 GLY   A CA    1 
ATOM   5028 C  C     . GLY   A  1 644 ? 6.41600  -42.43200  -3.99000  1.000 55.93717  ? 636 GLY   A C     1 
ATOM   5029 O  O     . GLY   A  1 644 ? 7.57300  -42.12900  -4.34300  1.000 55.26981  ? 636 GLY   A O     1 
ATOM   5030 N  N     . LEU   A  1 645 ? 5.41300  -41.56200  -3.82900  1.000 54.98171  ? 637 LEU   A N     1 
ATOM   5031 C  CA    . LEU   A  1 645 ? 5.55800  -40.07900  -3.86000  1.000 65.95614  ? 637 LEU   A CA    1 
ATOM   5032 C  C     . LEU   A  1 645 ? 5.66700  -39.55800  -2.42300  1.000 60.30524  ? 637 LEU   A C     1 
ATOM   5033 O  O     . LEU   A  1 645 ? 6.12700  -40.28400  -1.55000  1.000 68.08148  ? 637 LEU   A O     1 
ATOM   5034 C  CB    . LEU   A  1 645 ? 4.35900  -39.45000  -4.58100  1.000 66.51829  ? 637 LEU   A CB    1 
ATOM   5035 C  CG    . LEU   A  1 645 ? 4.35200  -39.58100  -6.10300  1.000 58.62926  ? 637 LEU   A CG    1 
ATOM   5036 C  CD1   . LEU   A  1 645 ? 3.01200  -39.14400  -6.67800  1.000 56.70196  ? 637 LEU   A CD1   1 
ATOM   5037 C  CD2   . LEU   A  1 645 ? 5.48100  -38.77300  -6.72200  1.000 57.60251  ? 637 LEU   A CD2   1 
ATOM   5038 N  N     . GLU   B  2 36  ? 35.25400 -112.93700 -20.33100 1.000 111.51023 ? 28  GLU   B N     1 
ATOM   5039 C  CA    . GLU   B  2 36  ? 34.10700 -111.98500 -20.45700 1.000 97.71005  ? 28  GLU   B CA    1 
ATOM   5040 C  C     . GLU   B  2 36  ? 32.79800 -112.77700 -20.57900 1.000 99.68356  ? 28  GLU   B C     1 
ATOM   5041 O  O     . GLU   B  2 36  ? 32.73600 -113.68500 -21.43100 1.000 103.16603 ? 28  GLU   B O     1 
ATOM   5042 C  CB    . GLU   B  2 36  ? 34.30200 -111.05500 -21.65600 1.000 98.16097  ? 28  GLU   B CB    1 
ATOM   5043 C  CG    . GLU   B  2 36  ? 35.34800 -109.97400 -21.43100 1.000 99.59344  ? 28  GLU   B CG    1 
ATOM   5044 C  CD    . GLU   B  2 36  ? 36.78500 -110.36600 -21.73100 1.000 102.64235 ? 28  GLU   B CD    1 
ATOM   5045 O  OE1   . GLU   B  2 36  ? 37.04600 -111.57100 -21.92100 1.000 104.81702 ? 28  GLU   B OE1   1 
ATOM   5046 O  OE2   . GLU   B  2 36  ? 37.64200 -109.46200 -21.77300 1.000 103.78194 ? 28  GLU   B OE2   1 
ATOM   5047 N  N     . ARG   B  2 37  ? 31.79600 -112.42200 -19.76500 1.000 106.24220 ? 29  ARG   B N     1 
ATOM   5048 C  CA    . ARG   B  2 37  ? 30.51100 -113.15900 -19.59400 1.000 104.17331 ? 29  ARG   B CA    1 
ATOM   5049 C  C     . ARG   B  2 37  ? 29.68000 -113.08900 -20.88400 1.000 104.96693 ? 29  ARG   B C     1 
ATOM   5050 O  O     . ARG   B  2 37  ? 29.13600 -114.13600 -21.28500 1.000 105.19092 ? 29  ARG   B O     1 
ATOM   5051 C  CB    . ARG   B  2 37  ? 29.73800 -112.58000 -18.40300 1.000 106.08573 ? 29  ARG   B CB    1 
ATOM   5052 C  CG    . ARG   B  2 37  ? 28.36900 -113.20100 -18.15100 1.000 106.83939 ? 29  ARG   B CG    1 
ATOM   5053 C  CD    . ARG   B  2 37  ? 28.41800 -114.52500 -17.41000 1.000 112.79938 ? 29  ARG   B CD    1 
ATOM   5054 N  NE    . ARG   B  2 37  ? 27.10100 -114.91100 -16.91300 1.000 116.87499 ? 29  ARG   B NE    1 
ATOM   5055 C  CZ    . ARG   B  2 37  ? 26.79100 -116.10200 -16.40200 1.000 120.10757 ? 29  ARG   B CZ    1 
ATOM   5056 N  NH1   . ARG   B  2 37  ? 27.70200 -117.05600 -16.31400 1.000 118.87154 ? 29  ARG   B NH1   1 
ATOM   5057 N  NH2   . ARG   B  2 37  ? 25.55700 -116.33400 -15.98100 1.000 118.91222 ? 29  ARG   B NH2   1 
ATOM   5058 N  N     . GLN   B  2 38  ? 29.58100 -111.90700 -21.50000 1.000 99.31770  ? 30  GLN   B N     1 
ATOM   5059 C  CA    . GLN   B  2 38  ? 28.65600 -111.63000 -22.63400 1.000 97.26493  ? 30  GLN   B CA    1 
ATOM   5060 C  C     . GLN   B  2 38  ? 29.34300 -111.98100 -23.96200 1.000 97.09727  ? 30  GLN   B C     1 
ATOM   5061 O  O     . GLN   B  2 38  ? 30.29600 -111.27100 -24.33800 1.000 100.63786 ? 30  GLN   B O     1 
ATOM   5062 C  CB    . GLN   B  2 38  ? 28.20400 -110.16800 -22.60700 1.000 92.35619  ? 30  GLN   B CB    1 
ATOM   5063 C  CG    . GLN   B  2 38  ? 27.28600 -109.82900 -21.43900 1.000 93.20588  ? 30  GLN   B CG    1 
ATOM   5064 C  CD    . GLN   B  2 38  ? 28.01700 -109.62200 -20.13300 1.000 94.24808  ? 30  GLN   B CD    1 
ATOM   5065 O  OE1   . GLN   B  2 38  ? 29.17100 -109.20000 -20.09600 1.000 93.56642  ? 30  GLN   B OE1   1 
ATOM   5066 N  NE2   . GLN   B  2 38  ? 27.33500 -109.91300 -19.03800 1.000 96.31649  ? 30  GLN   B NE2   1 
ATOM   5067 N  N     . LEU   B  2 39  ? 28.86400 -113.02900 -24.64200 1.000 93.73051  ? 31  LEU   B N     1 
ATOM   5068 C  CA    . LEU   B  2 39  ? 29.35600 -113.47500 -25.97600 1.000 93.26676  ? 31  LEU   B CA    1 
ATOM   5069 C  C     . LEU   B  2 39  ? 28.57600 -112.72900 -27.06400 1.000 93.46674  ? 31  LEU   B C     1 
ATOM   5070 O  O     . LEU   B  2 39  ? 27.33300 -112.77200 -27.01900 1.000 93.85714  ? 31  LEU   B O     1 
ATOM   5071 C  CB    . LEU   B  2 39  ? 29.16500 -114.98900 -26.11000 1.000 95.40276  ? 31  LEU   B CB    1 
ATOM   5072 C  CG    . LEU   B  2 39  ? 29.81400 -115.84000 -25.01900 1.000 97.74264  ? 31  LEU   B CG    1 
ATOM   5073 C  CD1   . LEU   B  2 39  ? 29.24200 -117.25000 -25.01500 1.000 100.35612 ? 31  LEU   B CD1   1 
ATOM   5074 C  CD2   . LEU   B  2 39  ? 31.32500 -115.87600 -25.18400 1.000 97.79345  ? 31  LEU   B CD2   1 
ATOM   5075 N  N     . GLU   B  2 40  ? 29.28300 -112.09100 -28.00200 1.000 90.52054  ? 32  GLU   B N     1 
ATOM   5076 C  CA    . GLU   B  2 40  ? 28.70200 -111.23100 -29.07100 1.000 90.06259  ? 32  GLU   B CA    1 
ATOM   5077 C  C     . GLU   B  2 40  ? 28.64400 -111.99700 -30.39600 1.000 92.26818  ? 32  GLU   B C     1 
ATOM   5078 O  O     . GLU   B  2 40  ? 27.56200 -112.03000 -31.00900 1.000 96.12134  ? 32  GLU   B O     1 
ATOM   5079 C  CB    . GLU   B  2 40  ? 29.54200 -109.96500 -29.24700 1.000 89.53225  ? 32  GLU   B CB    1 
ATOM   5080 C  CG    . GLU   B  2 40  ? 29.61300 -109.11600 -27.99400 1.000 95.63293  ? 32  GLU   B CG    1 
ATOM   5081 C  CD    . GLU   B  2 40  ? 28.35000 -108.33600 -27.68000 1.000 90.14616  ? 32  GLU   B CD    1 
ATOM   5082 O  OE1   . GLU   B  2 40  ? 27.43300 -108.31000 -28.52900 1.000 88.36732  ? 32  GLU   B OE1   1 
ATOM   5083 O  OE2   . GLU   B  2 40  ? 28.29300 -107.74900 -26.58600 1.000 92.86393  ? 32  GLU   B OE2   1 
ATOM   5084 N  N     . ALA   B  2 41  ? 29.77500 -112.56600 -30.82500 1.000 90.53720  ? 33  ALA   B N     1 
ATOM   5085 C  CA    . ALA   B  2 41  ? 29.95600 -113.18400 -32.15800 1.000 92.57393  ? 33  ALA   B CA    1 
ATOM   5086 C  C     . ALA   B  2 41  ? 30.27300 -114.67600 -32.01700 1.000 94.90671  ? 33  ALA   B C     1 
ATOM   5087 O  O     . ALA   B  2 41  ? 30.88500 -115.06400 -31.00400 1.000 98.77159  ? 33  ALA   B O     1 
ATOM   5088 C  CB    . ALA   B  2 41  ? 31.04600 -112.46100 -32.90900 1.000 92.92299  ? 33  ALA   B CB    1 
ATOM   5089 N  N     . ALA   B  2 42  ? 29.85800 -115.46700 -33.01100 1.000 98.61948  ? 34  ALA   B N     1 
ATOM   5090 C  CA    . ALA   B  2 42  ? 30.17500 -116.90500 -33.17700 1.000 96.72414  ? 34  ALA   B CA    1 
ATOM   5091 C  C     . ALA   B  2 42  ? 30.12100 -117.25100 -34.66900 1.000 96.48191  ? 34  ALA   B C     1 
ATOM   5092 O  O     . ALA   B  2 42  ? 29.02000 -117.18100 -35.24900 1.000 96.47708  ? 34  ALA   B O     1 
ATOM   5093 C  CB    . ALA   B  2 42  ? 29.21600 -117.75300 -32.38000 1.000 96.97093  ? 34  ALA   B CB    1 
ATOM   5094 N  N     . ARG   B  2 43  ? 31.27200 -117.58300 -35.26200 1.000 97.34183  ? 35  ARG   B N     1 
ATOM   5095 C  CA    . ARG   B  2 43  ? 31.41800 -117.87900 -36.71300 1.000 98.37786  ? 35  ARG   B CA    1 
ATOM   5096 C  C     . ARG   B  2 43  ? 32.24900 -119.15300 -36.89100 1.000 100.53476 ? 35  ARG   B C     1 
ATOM   5097 O  O     . ARG   B  2 43  ? 33.37500 -119.19800 -36.36200 1.000 100.92269 ? 35  ARG   B O     1 
ATOM   5098 C  CB    . ARG   B  2 43  ? 32.08900 -116.70700 -37.43700 1.000 97.62997  ? 35  ARG   B CB    1 
ATOM   5099 C  CG    . ARG   B  2 43  ? 31.43500 -115.35400 -37.19000 1.000 96.25505  ? 35  ARG   B CG    1 
ATOM   5100 C  CD    . ARG   B  2 43  ? 30.05600 -115.22800 -37.81300 1.000 95.85651  ? 35  ARG   B CD    1 
ATOM   5101 N  NE    . ARG   B  2 43  ? 29.36500 -114.04100 -37.33100 1.000 94.41310  ? 35  ARG   B NE    1 
ATOM   5102 C  CZ    . ARG   B  2 43  ? 29.62200 -112.79500 -37.71800 1.000 93.93691  ? 35  ARG   B CZ    1 
ATOM   5103 N  NH1   . ARG   B  2 43  ? 30.56600 -112.54500 -38.61100 1.000 96.78356  ? 35  ARG   B NH1   1 
ATOM   5104 N  NH2   . ARG   B  2 43  ? 28.92900 -111.79300 -37.20400 1.000 100.15789 ? 35  ARG   B NH2   1 
ATOM   5105 N  N     . TYR   B  2 44  ? 31.70300 -120.14200 -37.60500 1.000 102.15290 ? 36  TYR   B N     1 
ATOM   5106 C  CA    . TYR   B  2 44  ? 32.41700 -121.37400 -38.03000 1.000 104.64600 ? 36  TYR   B CA    1 
ATOM   5107 C  C     . TYR   B  2 44  ? 33.29900 -121.04100 -39.23700 1.000 105.24611 ? 36  TYR   B C     1 
ATOM   5108 O  O     . TYR   B  2 44  ? 32.77900 -120.48100 -40.22000 1.000 105.86668 ? 36  TYR   B O     1 
ATOM   5109 C  CB    . TYR   B  2 44  ? 31.44500 -122.50200 -38.39000 1.000 106.41003 ? 36  TYR   B CB    1 
ATOM   5110 C  CG    . TYR   B  2 44  ? 30.97300 -123.35200 -37.23600 1.000 107.49491 ? 36  TYR   B CG    1 
ATOM   5111 C  CD1   . TYR   B  2 44  ? 31.87400 -124.03500 -36.43300 1.000 109.06083 ? 36  TYR   B CD1   1 
ATOM   5112 C  CD2   . TYR   B  2 44  ? 29.62200 -123.50900 -36.96600 1.000 107.50962 ? 36  TYR   B CD2   1 
ATOM   5113 C  CE1   . TYR   B  2 44  ? 31.44900 -124.82800 -35.37900 1.000 110.68146 ? 36  TYR   B CE1   1 
ATOM   5114 C  CE2   . TYR   B  2 44  ? 29.18000 -124.30100 -35.91900 1.000 109.07561 ? 36  TYR   B CE2   1 
ATOM   5115 C  CZ    . TYR   B  2 44  ? 30.09600 -124.96300 -35.12100 1.000 110.72705 ? 36  TYR   B CZ    1 
ATOM   5116 O  OH    . TYR   B  2 44  ? 29.67400 -125.74500 -34.08600 1.000 112.83619 ? 36  TYR   B OH    1 
ATOM   5117 N  N     . ARG   B  2 45  ? 34.59100 -121.36800 -39.15600 1.000 106.55450 ? 37  ARG   B N     1 
ATOM   5118 C  CA    . ARG   B  2 45  ? 35.54200 -121.30500 -40.29800 1.000 108.04861 ? 37  ARG   B CA    1 
ATOM   5119 C  C     . ARG   B  2 45  ? 35.29900 -122.52200 -41.19900 1.000 110.54731 ? 37  ARG   B C     1 
ATOM   5120 O  O     . ARG   B  2 45  ? 34.71800 -123.51000 -40.70900 1.000 111.40335 ? 37  ARG   B O     1 
ATOM   5121 C  CB    . ARG   B  2 45  ? 36.98600 -121.25200 -39.78800 1.000 108.92172 ? 37  ARG   B CB    1 
ATOM   5122 C  CG    . ARG   B  2 45  ? 38.03300 -121.08300 -40.88000 1.000 110.74384 ? 37  ARG   B CG    1 
ATOM   5123 C  CD    . ARG   B  2 45  ? 39.41900 -120.82700 -40.32300 1.000 111.58773 ? 37  ARG   B CD    1 
ATOM   5124 N  NE    . ARG   B  2 45  ? 39.92600 -121.95200 -39.54800 1.000 113.42764 ? 37  ARG   B NE    1 
ATOM   5125 C  CZ    . ARG   B  2 45  ? 41.13000 -122.00800 -38.98600 1.000 114.88980 ? 37  ARG   B CZ    1 
ATOM   5126 N  NH1   . ARG   B  2 45  ? 41.97100 -120.99300 -39.10300 1.000 114.62826 ? 37  ARG   B NH1   1 
ATOM   5127 N  NH2   . ARG   B  2 45  ? 41.49100 -123.08400 -38.30700 1.000 117.00260 ? 37  ARG   B NH2   1 
ATOM   5128 N  N     . SER   B  2 46  ? 35.72000 -122.43800 -42.46600 1.000 111.98788 ? 38  SER   B N     1 
ATOM   5129 C  CA    . SER   B  2 46  ? 35.57700 -123.49100 -43.50800 1.000 114.67573 ? 38  SER   B CA    1 
ATOM   5130 C  C     . SER   B  2 46  ? 35.90000 -124.87800 -42.93500 1.000 116.79924 ? 38  SER   B C     1 
ATOM   5131 O  O     . SER   B  2 46  ? 35.08600 -125.80100 -43.14200 1.000 118.04666 ? 38  SER   B O     1 
ATOM   5132 C  CB    . SER   B  2 46  ? 36.44800 -123.17900 -44.69700 1.000 116.45512 ? 38  SER   B CB    1 
ATOM   5133 O  OG    . SER   B  2 46  ? 37.81100 -123.09200 -44.31100 1.000 117.85739 ? 38  SER   B OG    1 
ATOM   5134 N  N     . ASP   B  2 47  ? 37.03400 -125.01100 -42.23500 1.000 117.53386 ? 39  ASP   B N     1 
ATOM   5135 C  CA    . ASP   B  2 47  ? 37.57500 -126.30700 -41.73500 1.000 120.34007 ? 39  ASP   B CA    1 
ATOM   5136 C  C     . ASP   B  2 47  ? 36.72900 -126.83100 -40.56300 1.000 119.84814 ? 39  ASP   B C     1 
ATOM   5137 O  O     . ASP   B  2 47  ? 36.78500 -128.05000 -40.31000 1.000 122.64684 ? 39  ASP   B O     1 
ATOM   5138 C  CB    . ASP   B  2 47  ? 39.05700 -126.18800 -41.36200 1.000 121.61162 ? 39  ASP   B CB    1 
ATOM   5139 C  CG    . ASP   B  2 47  ? 39.33800 -125.40600 -40.09000 1.000 119.50930 ? 39  ASP   B CG    1 
ATOM   5140 O  OD1   . ASP   B  2 47  ? 38.52400 -124.52700 -39.74300 1.000 116.47085 ? 39  ASP   B OD1   1 
ATOM   5141 O  OD2   . ASP   B  2 47  ? 40.37500 -125.68200 -39.45600 1.000 121.19142 ? 39  ASP   B OD2   1 
ATOM   5142 N  N     . GLY   B  2 48  ? 35.99200 -125.95200 -39.87100 1.000 116.83642 ? 40  GLY   B N     1 
ATOM   5143 C  CA    . GLY   B  2 48  ? 35.04000 -126.31900 -38.80000 1.000 117.70922 ? 40  GLY   B CA    1 
ATOM   5144 C  C     . GLY   B  2 48  ? 35.43700 -125.78700 -37.42800 1.000 115.19813 ? 40  GLY   B C     1 
ATOM   5145 O  O     . GLY   B  2 48  ? 34.82300 -126.22800 -36.43500 1.000 115.69271 ? 40  GLY   B O     1 
ATOM   5146 N  N     . ALA   B  2 49  ? 36.41500 -124.87600 -37.36500 1.000 113.98907 ? 41  ALA   B N     1 
ATOM   5147 C  CA    . ALA   B  2 49  ? 36.85900 -124.18600 -36.13000 1.000 112.71146 ? 41  ALA   B CA    1 
ATOM   5148 C  C     . ALA   B  2 49  ? 35.86300 -123.07100 -35.79100 1.000 109.40856 ? 41  ALA   B C     1 
ATOM   5149 O  O     . ALA   B  2 49  ? 35.27400 -122.50300 -36.73000 1.000 107.97218 ? 41  ALA   B O     1 
ATOM   5150 C  CB    . ALA   B  2 49  ? 38.25500 -123.64500 -36.31200 1.000 113.06321 ? 41  ALA   B CB    1 
ATOM   5151 N  N     . LEU   B  2 50  ? 35.69400 -122.77100 -34.49800 1.000 109.50295 ? 42  LEU   B N     1 
ATOM   5152 C  CA    . LEU   B  2 50  ? 34.67400 -121.82100 -33.97600 1.000 105.93365 ? 42  LEU   B CA    1 
ATOM   5153 C  C     . LEU   B  2 50  ? 35.36800 -120.57300 -33.41700 1.000 104.06925 ? 42  LEU   B C     1 
ATOM   5154 O  O     . LEU   B  2 50  ? 36.13200 -120.71100 -32.44500 1.000 105.07857 ? 42  LEU   B O     1 
ATOM   5155 C  CB    . LEU   B  2 50  ? 33.84200 -122.53800 -32.90600 1.000 107.07973 ? 42  LEU   B CB    1 
ATOM   5156 C  CG    . LEU   B  2 50  ? 32.69900 -121.73800 -32.28200 1.000 105.51878 ? 42  LEU   B CG    1 
ATOM   5157 C  CD1   . LEU   B  2 50  ? 31.83100 -121.07700 -33.34500 1.000 103.08952 ? 42  LEU   B CD1   1 
ATOM   5158 C  CD2   . LEU   B  2 50  ? 31.85000 -122.62900 -31.38900 1.000 107.68824 ? 42  LEU   B CD2   1 
ATOM   5159 N  N     . LEU   B  2 51  ? 35.10800 -119.40900 -34.02600 1.000 103.19864 ? 43  LEU   B N     1 
ATOM   5160 C  CA    . LEU   B  2 51  ? 35.61900 -118.07500 -33.60000 1.000 101.14349 ? 43  LEU   B CA    1 
ATOM   5161 C  C     . LEU   B  2 51  ? 34.56400 -117.39600 -32.72000 1.000 101.16146 ? 43  LEU   B C     1 
ATOM   5162 O  O     . LEU   B  2 51  ? 33.43500 -117.20800 -33.21000 1.000 101.27986 ? 43  LEU   B O     1 
ATOM   5163 C  CB    . LEU   B  2 51  ? 35.91800 -117.22900 -34.84300 1.000 99.35474  ? 43  LEU   B CB    1 
ATOM   5164 C  CG    . LEU   B  2 51  ? 36.17400 -115.74000 -34.60200 1.000 97.63590  ? 43  LEU   B CG    1 
ATOM   5165 C  CD1   . LEU   B  2 51  ? 37.31900 -115.52800 -33.62500 1.000 98.13525  ? 43  LEU   B CD1   1 
ATOM   5166 C  CD2   . LEU   B  2 51  ? 36.45700 -115.01900 -35.91000 1.000 97.78288  ? 43  LEU   B CD2   1 
ATOM   5167 N  N     . LEU   B  2 52  ? 34.92800 -117.03500 -31.48400 1.000 100.92771 ? 44  LEU   B N     1 
ATOM   5168 C  CA    . LEU   B  2 52  ? 34.02600 -116.37500 -30.50100 1.000 98.31732  ? 44  LEU   B CA    1 
ATOM   5169 C  C     . LEU   B  2 52  ? 34.55300 -114.97700 -30.16600 1.000 100.86705 ? 44  LEU   B C     1 
ATOM   5170 O  O     . LEU   B  2 52  ? 35.68500 -114.88000 -29.65000 1.000 101.96408 ? 44  LEU   B O     1 
ATOM   5171 C  CB    . LEU   B  2 52  ? 33.93000 -117.23000 -29.23200 1.000 99.61369  ? 44  LEU   B CB    1 
ATOM   5172 C  CG    . LEU   B  2 52  ? 33.23200 -118.58100 -29.38000 1.000 109.15148 ? 44  LEU   B CG    1 
ATOM   5173 C  CD1   . LEU   B  2 52  ? 32.99800 -119.21500 -28.01700 1.000 105.09230 ? 44  LEU   B CD1   1 
ATOM   5174 C  CD2   . LEU   B  2 52  ? 31.91600 -118.45000 -30.13300 1.000 102.91279 ? 44  LEU   B CD2   1 
ATOM   5175 N  N     . GLY   B  2 53  ? 33.75000 -113.94900 -30.46100 1.000 101.32427 ? 45  GLY   B N     1 
ATOM   5176 C  CA    . GLY   B  2 53  ? 33.92000 -112.57500 -29.95400 1.000 94.79492  ? 45  GLY   B CA    1 
ATOM   5177 C  C     . GLY   B  2 53  ? 33.12000 -112.38000 -28.68000 1.000 91.41974  ? 45  GLY   B C     1 
ATOM   5178 O  O     . GLY   B  2 53  ? 31.94600 -112.79700 -28.65600 1.000 91.94984  ? 45  GLY   B O     1 
ATOM   5179 N  N     . ALA   B  2 54  ? 33.73500 -111.78700 -27.65400 1.000 94.59478  ? 46  ALA   B N     1 
ATOM   5180 C  CA    . ALA   B  2 54  ? 33.12800 -111.56200 -26.32100 1.000 93.78268  ? 46  ALA   B CA    1 
ATOM   5181 C  C     . ALA   B  2 54  ? 33.48100 -110.16100 -25.81400 1.000 93.33844  ? 46  ALA   B C     1 
ATOM   5182 O  O     . ALA   B  2 54  ? 34.44100 -109.55900 -26.33600 1.000 94.58210  ? 46  ALA   B O     1 
ATOM   5183 C  CB    . ALA   B  2 54  ? 33.59300 -112.62800 -25.36100 1.000 93.46278  ? 46  ALA   B CB    1 
ATOM   5184 N  N     . SER   B  2 55  ? 32.71900 -109.67700 -24.82900 1.000 93.72867  ? 47  SER   B N     1 
ATOM   5185 C  CA    . SER   B  2 55  ? 32.89300 -108.35700 -24.16900 1.000 93.52292  ? 47  SER   B CA    1 
ATOM   5186 C  C     . SER   B  2 55  ? 32.29800 -108.40100 -22.75700 1.000 95.75849  ? 47  SER   B C     1 
ATOM   5187 O  O     . SER   B  2 55  ? 31.36000 -109.19100 -22.53500 1.000 91.00942  ? 47  SER   B O     1 
ATOM   5188 C  CB    . SER   B  2 55  ? 32.27600 -107.25800 -25.00100 1.000 91.95043  ? 47  SER   B CB    1 
ATOM   5189 O  OG    . SER   B  2 55  ? 30.98500 -107.62800 -25.46400 1.000 90.73321  ? 47  SER   B OG    1 
ATOM   5190 N  N     . SER   B  2 56  ? 32.85600 -107.60900 -21.83600 1.000 103.06001 ? 48  SER   B N     1 
ATOM   5191 C  CA    . SER   B  2 56  ? 32.29000 -107.32800 -20.48900 1.000 91.40639  ? 48  SER   B CA    1 
ATOM   5192 C  C     . SER   B  2 56  ? 31.38200 -106.09700 -20.58100 1.000 90.13477  ? 48  SER   B C     1 
ATOM   5193 O  O     . SER   B  2 56  ? 31.91500 -104.97900 -20.73900 1.000 89.36787  ? 48  SER   B O     1 
ATOM   5194 C  CB    . SER   B  2 56  ? 33.37000 -107.13500 -19.45600 1.000 92.71426  ? 48  SER   B CB    1 
ATOM   5195 O  OG    . SER   B  2 56  ? 33.86600 -108.38300 -19.00200 1.000 104.30548 ? 48  SER   B OG    1 
ATOM   5196 N  N     . LEU   B  2 57  ? 30.06400 -106.30800 -20.50700 1.000 90.27271  ? 49  LEU   B N     1 
ATOM   5197 C  CA    . LEU   B  2 57  ? 29.02700 -105.24200 -20.57200 1.000 89.56105  ? 49  LEU   B CA    1 
ATOM   5198 C  C     . LEU   B  2 57  ? 28.56400 -104.88400 -19.15300 1.000 90.90381  ? 49  LEU   B C     1 
ATOM   5199 O  O     . LEU   B  2 57  ? 27.61000 -104.09000 -19.02400 1.000 95.29937  ? 49  LEU   B O     1 
ATOM   5200 C  CB    . LEU   B  2 57  ? 27.86300 -105.73400 -21.43800 1.000 89.32548  ? 49  LEU   B CB    1 
ATOM   5201 C  CG    . LEU   B  2 57  ? 28.23500 -106.27100 -22.82200 1.000 88.48359  ? 49  LEU   B CG    1 
ATOM   5202 C  CD1   . LEU   B  2 57  ? 26.98300 -106.58100 -23.62700 1.000 88.49524  ? 49  LEU   B CD1   1 
ATOM   5203 C  CD2   . LEU   B  2 57  ? 29.12500 -105.29500 -23.57900 1.000 87.36768  ? 49  LEU   B CD2   1 
ATOM   5204 N  N     . SER   B  2 58  ? 29.21500 -105.45200 -18.13200 1.000 92.38146  ? 50  SER   B N     1 
ATOM   5205 C  CA    . SER   B  2 58  ? 29.03100 -105.11200 -16.69700 1.000 94.09428  ? 50  SER   B CA    1 
ATOM   5206 C  C     . SER   B  2 58  ? 30.26900 -105.55500 -15.91000 1.000 95.54419  ? 50  SER   B C     1 
ATOM   5207 O  O     . SER   B  2 58  ? 30.94100 -106.50800 -16.35900 1.000 95.78371  ? 50  SER   B O     1 
ATOM   5208 C  CB    . SER   B  2 58  ? 27.77300 -105.73100 -16.15000 1.000 95.79205  ? 50  SER   B CB    1 
ATOM   5209 O  OG    . SER   B  2 58  ? 27.47000 -105.20000 -14.87100 1.000 97.50640  ? 50  SER   B OG    1 
ATOM   5210 N  N     . GLY   B  2 59  ? 30.55900 -104.87500 -14.79500 1.000 96.72416  ? 51  GLY   B N     1 
ATOM   5211 C  CA    . GLY   B  2 59  ? 31.71000 -105.15400 -13.91400 1.000 98.59112  ? 51  GLY   B CA    1 
ATOM   5212 C  C     . GLY   B  2 59  ? 32.75000 -104.04700 -13.96000 1.000 97.68045  ? 51  GLY   B C     1 
ATOM   5213 O  O     . GLY   B  2 59  ? 32.52000 -103.04200 -14.65800 1.000 95.71032  ? 51  GLY   B O     1 
ATOM   5214 N  N     . ARG   B  2 60  ? 33.86000 -104.23300 -13.23800 1.000 104.73004 ? 52  ARG   B N     1 
ATOM   5215 C  CA    . ARG   B  2 60  ? 34.96300 -103.24400 -13.08200 1.000 101.12039 ? 52  ARG   B CA    1 
ATOM   5216 C  C     . ARG   B  2 60  ? 35.56300 -102.91000 -14.45500 1.000 98.56269  ? 52  ARG   B C     1 
ATOM   5217 O  O     . ARG   B  2 60  ? 35.70400 -101.71300 -14.76700 1.000 96.84179  ? 52  ARG   B O     1 
ATOM   5218 C  CB    . ARG   B  2 60  ? 36.03300 -103.79600 -12.13100 1.000 102.24186 ? 52  ARG   B CB    1 
ATOM   5219 C  CG    . ARG   B  2 60  ? 37.15300 -102.81800 -11.80400 1.000 102.79740 ? 52  ARG   B CG    1 
ATOM   5220 C  CD    . ARG   B  2 60  ? 38.36500 -103.50200 -11.20200 1.000 105.59356 ? 52  ARG   B CD    1 
ATOM   5221 N  NE    . ARG   B  2 60  ? 38.14800 -103.90500 -9.81700  1.000 108.73179 ? 52  ARG   B NE    1 
ATOM   5222 C  CZ    . ARG   B  2 60  ? 38.37300 -103.14500 -8.74500  1.000 110.54858 ? 52  ARG   B CZ    1 
ATOM   5223 N  NH1   . ARG   B  2 60  ? 38.82700 -101.90800 -8.87100  1.000 109.48974 ? 52  ARG   B NH1   1 
ATOM   5224 N  NH2   . ARG   B  2 60  ? 38.13800 -103.63200 -7.53800  1.000 113.79805 ? 52  ARG   B NH2   1 
ATOM   5225 N  N     A CYS   B  2 61  ? 35.90000 -103.94200 -15.23700 0.500 107.60729 ? 53  CYS   B N     1 
ATOM   5226 N  N     B CYS   B  2 61  ? 35.90700 -103.94300 -15.23400 0.500 104.14256 ? 53  CYS   B N     1 
ATOM   5227 C  CA    A CYS   B  2 61  ? 36.55600 -103.84400 -16.57100 0.500 102.02010 ? 53  CYS   B CA    1 
ATOM   5228 C  CA    B CYS   B  2 61  ? 36.55700 -103.84500 -16.57100 0.500 101.59088 ? 53  CYS   B CA    1 
ATOM   5229 C  C     A CYS   B  2 61  ? 35.51600 -104.04400 -17.68100 0.500 94.96375  ? 53  CYS   B C     1 
ATOM   5230 C  C     B CYS   B  2 61  ? 35.50900 -104.03700 -17.67500 0.500 101.49862 ? 53  CYS   B C     1 
ATOM   5231 O  O     A CYS   B  2 61  ? 34.72000 -104.99700 -17.56800 0.500 95.53539  ? 53  CYS   B O     1 
ATOM   5232 O  O     B CYS   B  2 61  ? 34.70200 -104.97900 -17.55500 0.500 100.31591 ? 53  CYS   B O     1 
ATOM   5233 C  CB    A CYS   B  2 61  ? 37.66900 -104.87700 -16.69600 0.500 101.66599 ? 53  CYS   B CB    1 
ATOM   5234 C  CB    B CYS   B  2 61  ? 37.65700 -104.89000 -16.72100 0.500 96.91507  ? 53  CYS   B CB    1 
ATOM   5235 S  SG    A CYS   B  2 61  ? 38.48900 -104.87300 -18.31200 0.500 102.09574 ? 53  CYS   B SG    1 
ATOM   5236 S  SG    B CYS   B  2 61  ? 38.67800 -105.09200 -15.23700 0.500 100.19608 ? 53  CYS   B SG    1 
ATOM   5237 N  N     . TRP   B  2 62  ? 35.53400 -103.18100 -18.70600 1.000 91.90456  ? 54  TRP   B N     1 
ATOM   5238 C  CA    . TRP   B  2 62  ? 34.58500 -103.20400 -19.85800 1.000 91.92477  ? 54  TRP   B CA    1 
ATOM   5239 C  C     . TRP   B  2 62  ? 35.35000 -103.46600 -21.16400 1.000 92.83408  ? 54  TRP   B C     1 
ATOM   5240 O  O     . TRP   B  2 62  ? 35.08700 -102.76100 -22.16000 1.000 89.62261  ? 54  TRP   B O     1 
ATOM   5241 C  CB    . TRP   B  2 62  ? 33.79600 -101.88700 -19.93200 1.000 89.45720  ? 54  TRP   B CB    1 
ATOM   5242 C  CG    . TRP   B  2 62  ? 32.65000 -101.75800 -18.97300 1.000 90.00373  ? 54  TRP   B CG    1 
ATOM   5243 C  CD1   . TRP   B  2 62  ? 32.27400 -102.63100 -17.99200 1.000 91.63448  ? 54  TRP   B CD1   1 
ATOM   5244 C  CD2   . TRP   B  2 62  ? 31.73500 -100.65100 -18.88800 1.000 89.48571  ? 54  TRP   B CD2   1 
ATOM   5245 N  NE1   . TRP   B  2 62  ? 31.18300 -102.15200 -17.31900 1.000 91.37805  ? 54  TRP   B NE1   1 
ATOM   5246 C  CE2   . TRP   B  2 62  ? 30.83100 -100.93700 -17.84300 1.000 90.41145  ? 54  TRP   B CE2   1 
ATOM   5247 C  CE3   . TRP   B  2 62  ? 31.58700 -99.45200  -19.59700 1.000 88.90652  ? 54  TRP   B CE3   1 
ATOM   5248 C  CZ2   . TRP   B  2 62  ? 29.80000 -100.06700 -17.49200 1.000 90.64623  ? 54  TRP   B CZ2   1 
ATOM   5249 C  CZ3   . TRP   B  2 62  ? 30.57100 -98.59000  -19.24700 1.000 89.17234  ? 54  TRP   B CZ3   1 
ATOM   5250 C  CH2   . TRP   B  2 62  ? 29.69000 -98.89700  -18.20900 1.000 89.96115  ? 54  TRP   B CH2   1 
ATOM   5251 N  N     . ALA   B  2 63  ? 36.25200 -104.45300 -21.16300 1.000 91.74676  ? 55  ALA   B N     1 
ATOM   5252 C  CA    . ALA   B  2 63  ? 37.09700 -104.83700 -22.32000 1.000 96.26588  ? 55  ALA   B CA    1 
ATOM   5253 C  C     . ALA   B  2 63  ? 36.42100 -105.97400 -23.09800 1.000 96.66760  ? 55  ALA   B C     1 
ATOM   5254 O  O     . ALA   B  2 63  ? 35.25400 -106.28900 -22.78900 1.000 95.37436  ? 55  ALA   B O     1 
ATOM   5255 C  CB    . ALA   B  2 63  ? 38.47500 -105.22200 -21.83700 1.000 100.86209 ? 55  ALA   B CB    1 
ATOM   5256 N  N     . GLY   B  2 64  ? 37.11900 -106.53900 -24.09100 1.000 100.61096 ? 56  GLY   B N     1 
ATOM   5257 C  CA    . GLY   B  2 64  ? 36.63900 -107.65700 -24.92800 1.000 100.46461 ? 56  GLY   B CA    1 
ATOM   5258 C  C     . GLY   B  2 64  ? 37.72900 -108.68200 -25.18400 1.000 103.48076 ? 56  GLY   B C     1 
ATOM   5259 O  O     . GLY   B  2 64  ? 38.86900 -108.46300 -24.72700 1.000 105.42122 ? 56  GLY   B O     1 
ATOM   5260 N  N     . SER   B  2 65  ? 37.39600 -109.75900 -25.90200 1.000 100.98644 ? 57  SER   B N     1 
ATOM   5261 C  CA    . SER   B  2 65  ? 38.31200 -110.89200 -26.19300 1.000 102.43893 ? 57  SER   B CA    1 
ATOM   5262 C  C     . SER   B  2 65  ? 37.88600 -111.62700 -27.46900 1.000 101.37046 ? 57  SER   B C     1 
ATOM   5263 O  O     . SER   B  2 65  ? 36.69000 -111.57700 -27.82600 1.000 98.96762  ? 57  SER   B O     1 
ATOM   5264 C  CB    . SER   B  2 65  ? 38.37200 -111.83300 -25.02200 1.000 103.52331 ? 57  SER   B CB    1 
ATOM   5265 O  OG    . SER   B  2 65  ? 37.07000 -112.27200 -24.66600 1.000 104.65558 ? 57  SER   B OG    1 
ATOM   5266 N  N     . LEU   B  2 66  ? 38.85200 -112.28700 -28.11600 1.000 101.09505 ? 58  LEU   B N     1 
ATOM   5267 C  CA    . LEU   B  2 66  ? 38.66300 -113.14500 -29.31500 1.000 99.30130  ? 58  LEU   B CA    1 
ATOM   5268 C  C     . LEU   B  2 66  ? 39.26300 -114.52200 -29.01300 1.000 101.09687 ? 58  LEU   B C     1 
ATOM   5269 O  O     . LEU   B  2 66  ? 40.43700 -114.55900 -28.60000 1.000 108.03328 ? 58  LEU   B O     1 
ATOM   5270 C  CB    . LEU   B  2 66  ? 39.35500 -112.48800 -30.51500 1.000 101.32957 ? 58  LEU   B CB    1 
ATOM   5271 C  CG    . LEU   B  2 66  ? 38.90300 -111.06500 -30.84800 1.000 99.82892  ? 58  LEU   B CG    1 
ATOM   5272 C  CD1   . LEU   B  2 66  ? 39.93200 -110.35700 -31.71600 1.000 103.47600 ? 58  LEU   B CD1   1 
ATOM   5273 C  CD2   . LEU   B  2 66  ? 37.54100 -111.06800 -31.52700 1.000 93.52749  ? 58  LEU   B CD2   1 
ATOM   5274 N  N     . TRP   B  2 67  ? 38.47900 -115.59400 -29.18200 1.000 102.33072 ? 59  TRP   B N     1 
ATOM   5275 C  CA    . TRP   B  2 67  ? 38.90100 -117.00700 -28.96900 1.000 107.63699 ? 59  TRP   B CA    1 
ATOM   5276 C  C     . TRP   B  2 67  ? 38.84600 -117.77100 -30.29600 1.000 105.32678 ? 59  TRP   B C     1 
ATOM   5277 O  O     . TRP   B  2 67  ? 38.18300 -117.28600 -31.22900 1.000 105.97658 ? 59  TRP   B O     1 
ATOM   5278 C  CB    . TRP   B  2 67  ? 38.01900 -117.69600 -27.91900 1.000 109.37387 ? 59  TRP   B CB    1 
ATOM   5279 C  CG    . TRP   B  2 67  ? 37.75800 -116.88400 -26.68800 1.000 108.56224 ? 59  TRP   B CG    1 
ATOM   5280 C  CD1   . TRP   B  2 67  ? 36.69000 -116.06700 -26.45800 1.000 108.59686 ? 59  TRP   B CD1   1 
ATOM   5281 C  CD2   . TRP   B  2 67  ? 38.57200 -116.82400 -25.50300 1.000 113.91011 ? 59  TRP   B CD2   1 
ATOM   5282 N  NE1   . TRP   B  2 67  ? 36.78600 -115.49600 -25.21700 1.000 112.96100 ? 59  TRP   B NE1   1 
ATOM   5283 C  CE2   . TRP   B  2 67  ? 37.92900 -115.94200 -24.60700 1.000 114.86533 ? 59  TRP   B CE2   1 
ATOM   5284 C  CE3   . TRP   B  2 67  ? 39.77600 -117.42200 -25.11200 1.000 117.05237 ? 59  TRP   B CE3   1 
ATOM   5285 C  CZ2   . TRP   B  2 67  ? 38.45400 -115.64700 -23.34900 1.000 114.53105 ? 59  TRP   B CZ2   1 
ATOM   5286 C  CZ3   . TRP   B  2 67  ? 40.29400 -117.13000 -23.86900 1.000 112.78583 ? 59  TRP   B CZ3   1 
ATOM   5287 C  CH2   . TRP   B  2 67  ? 39.64100 -116.25200 -23.00200 1.000 116.34360 ? 59  TRP   B CH2   1 
ATOM   5288 N  N     . LEU   B  2 68  ? 39.51500 -118.92700 -30.36400 1.000 114.84314 ? 60  LEU   B N     1 
ATOM   5289 C  CA    . LEU   B  2 68  ? 39.32400 -119.94500 -31.43200 1.000 111.30960 ? 60  LEU   B CA    1 
ATOM   5290 C  C     . LEU   B  2 68  ? 39.19700 -121.32700 -30.78200 1.000 116.70143 ? 60  LEU   B C     1 
ATOM   5291 O  O     . LEU   B  2 68  ? 40.03900 -121.65500 -29.92400 1.000 120.92714 ? 60  LEU   B O     1 
ATOM   5292 C  CB    . LEU   B  2 68  ? 40.49400 -119.90100 -32.42000 1.000 109.26998 ? 60  LEU   B CB    1 
ATOM   5293 C  CG    . LEU   B  2 68  ? 40.37000 -120.84400 -33.61900 1.000 114.98544 ? 60  LEU   B CG    1 
ATOM   5294 C  CD1   . LEU   B  2 68  ? 39.18600 -120.46700 -34.49600 1.000 107.74734 ? 60  LEU   B CD1   1 
ATOM   5295 C  CD2   . LEU   B  2 68  ? 41.65100 -120.85700 -34.43700 1.000 111.88844 ? 60  LEU   B CD2   1 
ATOM   5296 N  N     . PHE   B  2 69  ? 38.18000 -122.09500 -31.18800 1.000 118.72329 ? 61  PHE   B N     1 
ATOM   5297 C  CA    . PHE   B  2 69  ? 37.85900 -123.45400 -30.67800 1.000 119.97797 ? 61  PHE   B CA    1 
ATOM   5298 C  C     . PHE   B  2 69  ? 37.87000 -124.45400 -31.83900 1.000 121.40909 ? 61  PHE   B C     1 
ATOM   5299 O  O     . PHE   B  2 69  ? 36.90300 -124.46800 -32.63000 1.000 118.30939 ? 61  PHE   B O     1 
ATOM   5300 C  CB    . PHE   B  2 69  ? 36.50100 -123.45100 -29.97300 1.000 119.75621 ? 61  PHE   B CB    1 
ATOM   5301 C  CG    . PHE   B  2 69  ? 36.50600 -122.83400 -28.59800 1.000 124.49305 ? 61  PHE   B CG    1 
ATOM   5302 C  CD1   . PHE   B  2 69  ? 36.44900 -121.45800 -28.43600 1.000 122.40487 ? 61  PHE   B CD1   1 
ATOM   5303 C  CD2   . PHE   B  2 69  ? 36.56500 -123.63100 -27.46600 1.000 126.66041 ? 61  PHE   B CD2   1 
ATOM   5304 C  CE1   . PHE   B  2 69  ? 36.45400 -120.89100 -27.17100 1.000 120.33899 ? 61  PHE   B CE1   1 
ATOM   5305 C  CE2   . PHE   B  2 69  ? 36.56900 -123.06300 -26.20100 1.000 131.96603 ? 61  PHE   B CE2   1 
ATOM   5306 C  CZ    . PHE   B  2 69  ? 36.51400 -121.69500 -26.05600 1.000 130.16349 ? 61  PHE   B CZ    1 
ATOM   5307 N  N     . LYS   B  2 70  ? 38.93200 -125.26100 -31.93000 1.000 125.62312 ? 62  LYS   B N     1 
ATOM   5308 C  CA    . LYS   B  2 70  ? 39.08400 -126.34900 -32.93500 1.000 128.08558 ? 62  LYS   B CA    1 
ATOM   5309 C  C     . LYS   B  2 70  ? 38.19400 -127.53300 -32.53200 1.000 130.21565 ? 62  LYS   B C     1 
ATOM   5310 O  O     . LYS   B  2 70  ? 37.80600 -128.31000 -33.43000 1.000 131.45037 ? 62  LYS   B O     1 
ATOM   5311 C  CB    . LYS   B  2 70  ? 40.55800 -126.74000 -33.07300 1.000 128.27886 ? 62  LYS   B CB    1 
ATOM   5312 C  CG    . LYS   B  2 70  ? 41.42600 -125.69000 -33.75700 1.000 128.93967 ? 62  LYS   B CG    1 
ATOM   5313 C  CD    . LYS   B  2 70  ? 42.90900 -125.97300 -33.68500 1.000 133.76010 ? 62  LYS   B CD    1 
ATOM   5314 C  CE    . LYS   B  2 70  ? 43.75000 -124.86900 -34.29000 1.000 130.19893 ? 62  LYS   B CE    1 
ATOM   5315 N  NZ    . LYS   B  2 70  ? 45.17600 -125.00300 -33.91200 1.000 126.94339 ? 62  LYS   B NZ    1 
ATOM   5316 N  N     . ASP   B  2 71  ? 37.89400 -127.65900 -31.23400 1.000 133.11778 ? 63  ASP   B N     1 
ATOM   5317 C  CA    . ASP   B  2 71  ? 36.83500 -128.54900 -30.68200 1.000 139.78475 ? 63  ASP   B CA    1 
ATOM   5318 C  C     . ASP   B  2 71  ? 35.62700 -127.67800 -30.33900 1.000 143.25576 ? 63  ASP   B C     1 
ATOM   5319 O  O     . ASP   B  2 71  ? 35.66900 -126.92200 -29.36900 1.000 142.72278 ? 63  ASP   B O     1 
ATOM   5320 C  CB    . ASP   B  2 71  ? 37.35500 -129.33400 -29.47400 1.000 140.78638 ? 63  ASP   B CB    1 
ATOM   5321 C  CG    . ASP   B  2 71  ? 36.57300 -130.60100 -29.16800 1.000 145.42602 ? 63  ASP   B CG    1 
ATOM   5322 O  OD1   . ASP   B  2 71  ? 35.35500 -130.62300 -29.43700 1.000 143.58024 ? 63  ASP   B OD1   1 
ATOM   5323 O  OD2   . ASP   B  2 71  ? 37.19200 -131.56000 -28.66500 1.000 149.01306 ? 63  ASP   B OD2   1 
ATOM   5324 N  N     . PRO   B  2 72  ? 34.52100 -127.73800 -31.12100 1.000 146.39886 ? 64  PRO   B N     1 
ATOM   5325 C  CA    . PRO   B  2 72  ? 33.38400 -126.83600 -30.92300 1.000 138.89710 ? 64  PRO   B CA    1 
ATOM   5326 C  C     . PRO   B  2 72  ? 32.52700 -127.18900 -29.69500 1.000 140.28296 ? 64  PRO   B C     1 
ATOM   5327 O  O     . PRO   B  2 72  ? 31.95400 -126.28300 -29.11300 1.000 132.37244 ? 64  PRO   B O     1 
ATOM   5328 C  CB    . PRO   B  2 72  ? 32.57900 -127.00400 -32.22100 1.000 129.30988 ? 64  PRO   B CB    1 
ATOM   5329 C  CG    . PRO   B  2 72  ? 32.86100 -128.43100 -32.64300 1.000 141.12917 ? 64  PRO   B CG    1 
ATOM   5330 C  CD    . PRO   B  2 72  ? 34.29500 -128.68700 -32.22500 1.000 145.77954 ? 64  PRO   B CD    1 
ATOM   5331 N  N     . CYS   B  2 73  ? 32.47900 -128.47700 -29.32700 1.000 144.73227 ? 65  CYS   B N     1 
ATOM   5332 C  CA    . CYS   B  2 73  ? 31.70600 -129.02500 -28.17700 1.000 142.27262 ? 65  CYS   B CA    1 
ATOM   5333 C  C     . CYS   B  2 73  ? 32.45800 -128.80000 -26.85500 1.000 142.16700 ? 65  CYS   B C     1 
ATOM   5334 O  O     . CYS   B  2 73  ? 32.01700 -129.35900 -25.83000 1.000 143.89697 ? 65  CYS   B O     1 
ATOM   5335 C  CB    . CYS   B  2 73  ? 31.42800 -130.51200 -28.37100 1.000 142.30616 ? 65  CYS   B CB    1 
ATOM   5336 S  SG    . CYS   B  2 73  ? 30.51800 -130.88200 -29.89400 1.000 142.73122 ? 65  CYS   B SG    1 
ATOM   5337 N  N     . ALA   B  2 74  ? 33.54700 -128.01900 -26.87700 1.000 141.73668 ? 66  ALA   B N     1 
ATOM   5338 C  CA    . ALA   B  2 74  ? 34.33600 -127.60300 -25.69300 1.000 138.74643 ? 66  ALA   B CA    1 
ATOM   5339 C  C     . ALA   B  2 74  ? 33.85600 -126.23400 -25.19000 1.000 139.60990 ? 66  ALA   B C     1 
ATOM   5340 O  O     . ALA   B  2 74  ? 33.91300 -126.01000 -23.96400 1.000 139.81698 ? 66  ALA   B O     1 
ATOM   5341 C  CB    . ALA   B  2 74  ? 35.80500 -127.57400 -26.03900 1.000 139.62629 ? 66  ALA   B CB    1 
ATOM   5342 N  N     . ALA   B  2 75  ? 33.40800 -125.36200 -26.10400 1.000 132.37840 ? 67  ALA   B N     1 
ATOM   5343 C  CA    . ALA   B  2 75  ? 32.97000 -123.97000 -25.83600 1.000 128.82722 ? 67  ALA   B CA    1 
ATOM   5344 C  C     . ALA   B  2 75  ? 31.80000 -123.96500 -24.85200 1.000 131.24169 ? 67  ALA   B C     1 
ATOM   5345 O  O     . ALA   B  2 75  ? 31.00400 -124.90200 -24.84100 1.000 128.61095 ? 67  ALA   B O     1 
ATOM   5346 C  CB    . ALA   B  2 75  ? 32.59900 -123.29900 -27.13700 1.000 125.62743 ? 67  ALA   B CB    1 
ATOM   5347 N  N     . PRO   B  2 76  ? 31.64200 -122.92100 -24.00000 1.000 130.43556 ? 68  PRO   B N     1 
ATOM   5348 C  CA    . PRO   B  2 76  ? 32.50400 -121.73500 -24.00600 1.000 127.23804 ? 68  PRO   B CA    1 
ATOM   5349 C  C     . PRO   B  2 76  ? 33.80400 -121.85100 -23.19200 1.000 135.47180 ? 68  PRO   B C     1 
ATOM   5350 O  O     . PRO   B  2 76  ? 34.58700 -120.91600 -23.22500 1.000 134.30421 ? 68  PRO   B O     1 
ATOM   5351 C  CB    . PRO   B  2 76  ? 31.60300 -120.69700 -23.32200 1.000 116.26546 ? 68  PRO   B CB    1 
ATOM   5352 C  CG    . PRO   B  2 76  ? 30.86600 -121.51200 -22.28100 1.000 120.93982 ? 68  PRO   B CG    1 
ATOM   5353 C  CD    . PRO   B  2 76  ? 30.60000 -122.84000 -22.96100 1.000 125.25116 ? 68  PRO   B CD    1 
ATOM   5354 N  N     . ASN   B  2 77  ? 33.99600 -122.97800 -22.49500 1.000 148.99782 ? 69  ASN   B N     1 
ATOM   5355 C  CA    . ASN   B  2 77  ? 35.03500 -123.18400 -21.44600 1.000 148.70733 ? 69  ASN   B CA    1 
ATOM   5356 C  C     . ASN   B  2 77  ? 36.41500 -122.76800 -21.97500 1.000 152.90772 ? 69  ASN   B C     1 
ATOM   5357 O  O     . ASN   B  2 77  ? 36.92100 -123.43800 -22.90000 1.000 149.59487 ? 69  ASN   B O     1 
ATOM   5358 C  CB    . ASN   B  2 77  ? 35.05000 -124.63300 -20.94500 1.000 152.12316 ? 69  ASN   B CB    1 
ATOM   5359 C  CG    . ASN   B  2 77  ? 35.67100 -124.78400 -19.57200 1.000 158.18785 ? 69  ASN   B CG    1 
ATOM   5360 O  OD1   . ASN   B  2 77  ? 36.42600 -125.72200 -19.32500 1.000 158.41364 ? 69  ASN   B OD1   1 
ATOM   5361 N  ND2   . ASN   B  2 77  ? 35.35600 -123.87100 -18.66700 1.000 160.94658 ? 69  ASN   B ND2   1 
ATOM   5362 N  N     . GLU   B  2 78  ? 37.00100 -121.72000 -21.38100 1.000 161.13429 ? 70  GLU   B N     1 
ATOM   5363 C  CA    . GLU   B  2 78  ? 38.31500 -121.12800 -21.76600 1.000 155.38952 ? 70  GLU   B CA    1 
ATOM   5364 C  C     . GLU   B  2 78  ? 39.42800 -122.18100 -21.64400 1.000 162.69052 ? 70  GLU   B C     1 
ATOM   5365 O  O     . GLU   B  2 78  ? 40.35400 -122.15600 -22.48000 1.000 160.04507 ? 70  GLU   B O     1 
ATOM   5366 C  CB    . GLU   B  2 78  ? 38.64400 -119.91400 -20.89100 1.000 146.20177 ? 70  GLU   B CB    1 
ATOM   5367 C  CG    . GLU   B  2 78  ? 37.76700 -118.70000 -21.16100 1.000 150.47626 ? 70  GLU   B CG    1 
ATOM   5368 C  CD    . GLU   B  2 78  ? 36.51300 -118.57300 -20.30900 1.000 154.18746 ? 70  GLU   B CD    1 
ATOM   5369 O  OE1   . GLU   B  2 78  ? 36.49700 -119.12000 -19.18400 1.000 151.57254 ? 70  GLU   B OE1   1 
ATOM   5370 O  OE2   . GLU   B  2 78  ? 35.55400 -117.91500 -20.76900 1.000 154.37043 ? 70  GLU   B OE2   1 
ATOM   5371 N  N     . GLY   B  2 79  ? 39.33200 -123.07200 -20.64900 1.000 161.75107 ? 71  GLY   B N     1 
ATOM   5372 C  CA    . GLY   B  2 79  ? 40.35700 -124.08400 -20.32300 1.000 164.92117 ? 71  GLY   B CA    1 
ATOM   5373 C  C     . GLY   B  2 79  ? 40.59700 -125.08400 -21.44700 1.000 171.05897 ? 71  GLY   B C     1 
ATOM   5374 O  O     . GLY   B  2 79  ? 41.66300 -125.73800 -21.42000 1.000 173.27067 ? 71  GLY   B O     1 
ATOM   5375 N  N     . PHE   B  2 80  ? 39.65100 -125.21800 -22.38600 1.000 168.26877 ? 72  PHE   B N     1 
ATOM   5376 C  CA    . PHE   B  2 80  ? 39.68700 -126.19200 -23.51200 1.000 163.53807 ? 72  PHE   B CA    1 
ATOM   5377 C  C     . PHE   B  2 80  ? 39.57600 -125.44600 -24.85100 1.000 162.15761 ? 72  PHE   B C     1 
ATOM   5378 O  O     . PHE   B  2 80  ? 38.70300 -125.80900 -25.67100 1.000 159.41331 ? 72  PHE   B O     1 
ATOM   5379 C  CB    . PHE   B  2 80  ? 38.57000 -127.23000 -23.35000 1.000 164.00011 ? 72  PHE   B CB    1 
ATOM   5380 C  CG    . PHE   B  2 80  ? 38.69600 -128.12400 -22.14000 1.000 170.76623 ? 72  PHE   B CG    1 
ATOM   5381 C  CD1   . PHE   B  2 80  ? 38.45800 -127.63400 -20.86400 1.000 171.47182 ? 72  PHE   B CD1   1 
ATOM   5382 C  CD2   . PHE   B  2 80  ? 39.03800 -129.46200 -22.27800 1.000 173.27879 ? 72  PHE   B CD2   1 
ATOM   5383 C  CE1   . PHE   B  2 80  ? 38.57200 -128.45700 -19.75300 1.000 172.53143 ? 72  PHE   B CE1   1 
ATOM   5384 C  CE2   . PHE   B  2 80  ? 39.14800 -130.28500 -21.16600 1.000 172.24946 ? 72  PHE   B CE2   1 
ATOM   5385 C  CZ    . PHE   B  2 80  ? 38.91500 -129.78100 -19.90600 1.000 176.90002 ? 72  PHE   B CZ    1 
ATOM   5386 N  N     . CYS   B  2 81  ? 40.43900 -124.44400 -25.06700 1.000 165.77276 ? 73  CYS   B N     1 
ATOM   5387 C  CA    . CYS   B  2 81  ? 40.51200 -123.61800 -26.30800 1.000 155.52234 ? 73  CYS   B CA    1 
ATOM   5388 C  C     . CYS   B  2 81  ? 41.86400 -123.82400 -27.00300 1.000 153.75736 ? 73  CYS   B C     1 
ATOM   5389 O  O     . CYS   B  2 81  ? 42.79800 -124.33500 -26.35100 1.000 157.84154 ? 73  CYS   B O     1 
ATOM   5390 C  CB    . CYS   B  2 81  ? 40.31700 -122.13500 -26.00900 1.000 147.71555 ? 73  CYS   B CB    1 
ATOM   5391 S  SG    . CYS   B  2 81  ? 41.84400 -121.27700 -25.54500 1.000 145.59137 ? 73  CYS   B SG    1 
ATOM   5392 N  N     . SER   B  2 82  ? 41.95600 -123.42100 -28.27500 1.000 142.18283 ? 74  SER   B N     1 
ATOM   5393 C  CA    . SER   B  2 82  ? 43.17400 -123.50200 -29.12600 1.000 138.09906 ? 74  SER   B CA    1 
ATOM   5394 C  C     . SER   B  2 82  ? 44.02000 -122.23300 -28.95500 1.000 139.93457 ? 74  SER   B C     1 
ATOM   5395 O  O     . SER   B  2 82  ? 45.25500 -122.36300 -28.83400 1.000 146.14174 ? 74  SER   B O     1 
ATOM   5396 C  CB    . SER   B  2 82  ? 42.81000 -123.72300 -30.57300 1.000 134.28793 ? 74  SER   B CB    1 
ATOM   5397 O  OG    . SER   B  2 82  ? 41.99800 -124.87800 -30.72200 1.000 135.81535 ? 74  SER   B OG    1 
ATOM   5398 N  N     . ALA   B  2 83  ? 43.37600 -121.05900 -28.95800 1.000 132.94184 ? 75  ALA   B N     1 
ATOM   5399 C  CA    . ALA   B  2 83  ? 44.01500 -119.72900 -28.81100 1.000 119.69188 ? 75  ALA   B CA    1 
ATOM   5400 C  C     . ALA   B  2 83  ? 42.98900 -118.69700 -28.32900 1.000 121.96577 ? 75  ALA   B C     1 
ATOM   5401 O  O     . ALA   B  2 83  ? 41.77500 -118.93100 -28.50900 1.000 122.01542 ? 75  ALA   B O     1 
ATOM   5402 C  CB    . ALA   B  2 83  ? 44.62900 -119.30600 -30.12100 1.000 116.48776 ? 75  ALA   B CB    1 
ATOM   5403 N  N     . GLY   B  2 84  ? 43.47500 -117.59400 -27.74800 1.000 119.08375 ? 76  GLY   B N     1 
ATOM   5404 C  CA    . GLY   B  2 84  ? 42.65900 -116.46100 -27.26600 1.000 108.90520 ? 76  GLY   B CA    1 
ATOM   5405 C  C     . GLY   B  2 84  ? 43.50100 -115.21400 -27.04900 1.000 106.85183 ? 76  GLY   B C     1 
ATOM   5406 O  O     . GLY   B  2 84  ? 44.72300 -115.36000 -26.83900 1.000 109.35855 ? 76  GLY   B O     1 
ATOM   5407 N  N     . VAL   B  2 85  ? 42.88000 -114.03100 -27.10100 1.000 104.06720 ? 77  VAL   B N     1 
ATOM   5408 C  CA    . VAL   B  2 85  ? 43.56000 -112.71900 -26.87600 1.000 103.58806 ? 77  VAL   B CA    1 
ATOM   5409 C  C     . VAL   B  2 85  ? 42.55400 -111.71500 -26.29900 1.000 110.07272 ? 77  VAL   B C     1 
ATOM   5410 O  O     . VAL   B  2 85  ? 41.34900 -111.84000 -26.59900 1.000 107.34648 ? 77  VAL   B O     1 
ATOM   5411 C  CB    . VAL   B  2 85  ? 44.20600 -112.18500 -28.17000 1.000 103.73575 ? 77  VAL   B CB    1 
ATOM   5412 C  CG1   . VAL   B  2 85  ? 43.17100 -111.66800 -29.16000 1.000 105.00903 ? 77  VAL   B CG1   1 
ATOM   5413 C  CG2   . VAL   B  2 85  ? 45.24900 -111.11600 -27.87900 1.000 104.64321 ? 77  VAL   B CG2   1 
ATOM   5414 N  N     . GLN   B  2 86  ? 43.05500 -110.75400 -25.51400 1.000 107.86394 ? 78  GLN   B N     1 
ATOM   5415 C  CA    . GLN   B  2 86  ? 42.28300 -109.63800 -24.90400 1.000 103.18132 ? 78  GLN   B CA    1 
ATOM   5416 C  C     . GLN   B  2 86  ? 42.43900 -108.38500 -25.77600 1.000 101.51037 ? 78  GLN   B C     1 
ATOM   5417 O  O     . GLN   B  2 86  ? 43.59100 -108.02500 -26.09100 1.000 104.74958 ? 78  GLN   B O     1 
ATOM   5418 C  CB    . GLN   B  2 86  ? 42.79200 -109.36900 -23.48500 1.000 105.53399 ? 78  GLN   B CB    1 
ATOM   5419 C  CG    . GLN   B  2 86  ? 41.88900 -108.45900 -22.65900 1.000 106.84662 ? 78  GLN   B CG    1 
ATOM   5420 C  CD    . GLN   B  2 86  ? 41.01300 -109.19700 -21.67500 1.000 107.70363 ? 78  GLN   B CD    1 
ATOM   5421 O  OE1   . GLN   B  2 86  ? 41.21100 -110.37500 -21.38700 1.000 110.89144 ? 78  GLN   B OE1   1 
ATOM   5422 N  NE2   . GLN   B  2 86  ? 40.03200 -108.49300 -21.13500 1.000 107.18399 ? 78  GLN   B NE2   1 
ATOM   5423 N  N     . THR   B  2 87  ? 41.32200 -107.75700 -26.15400 1.000 100.97756 ? 79  THR   B N     1 
ATOM   5424 C  CA    . THR   B  2 87  ? 41.27700 -106.42300 -26.81300 1.000 100.74201 ? 79  THR   B CA    1 
ATOM   5425 C  C     . THR   B  2 87  ? 41.22200 -105.34500 -25.72100 1.000 106.14419 ? 79  THR   B C     1 
ATOM   5426 O  O     . THR   B  2 87  ? 40.89100 -105.69300 -24.56500 1.000 103.22059 ? 79  THR   B O     1 
ATOM   5427 C  CB    . THR   B  2 87  ? 40.09700 -106.32600 -27.78900 1.000 102.26237 ? 79  THR   B CB    1 
ATOM   5428 O  OG1   . THR   B  2 87  ? 38.88600 -106.50700 -27.05500 1.000 104.47306 ? 79  THR   B OG1   1 
ATOM   5429 C  CG2   . THR   B  2 87  ? 40.16400 -107.34900 -28.90100 1.000 98.86566  ? 79  THR   B CG2   1 
ATOM   5430 N  N     . GLU   B  2 88  ? 41.53500 -104.09300 -26.06600 1.000 102.80514 ? 80  GLU   B N     1 
ATOM   5431 C  CA    . GLU   B  2 88  ? 41.57700 -102.96200 -25.09900 1.000 97.35608  ? 80  GLU   B CA    1 
ATOM   5432 C  C     . GLU   B  2 88  ? 40.13900 -102.57800 -24.71800 1.000 97.51403  ? 80  GLU   B C     1 
ATOM   5433 O  O     . GLU   B  2 88  ? 39.94800 -102.09200 -23.58300 1.000 98.51086  ? 80  GLU   B O     1 
ATOM   5434 C  CB    . GLU   B  2 88  ? 42.39700 -101.79500 -25.66200 1.000 96.04987  ? 80  GLU   B CB    1 
ATOM   5435 C  CG    . GLU   B  2 88  ? 41.60100 -100.78700 -26.47300 1.000 100.60859 ? 80  GLU   B CG    1 
ATOM   5436 C  CD    . GLU   B  2 88  ? 42.40100 -99.56300  -26.88800 1.000 109.24692 ? 80  GLU   B CD    1 
ATOM   5437 O  OE1   . GLU   B  2 88  ? 43.41700 -99.73600  -27.59200 1.000 112.69332 ? 80  GLU   B OE1   1 
ATOM   5438 O  OE2   . GLU   B  2 88  ? 42.01500 -98.44100  -26.48900 1.000 108.36165 ? 80  GLU   B OE2   1 
ATOM   5439 N  N     . ALA   B  2 89  ? 39.17300 -102.80900 -25.61800 1.000 96.78110  ? 81  ALA   B N     1 
ATOM   5440 C  CA    . ALA   B  2 89  ? 37.73300 -102.50500 -25.42500 1.000 97.60755  ? 81  ALA   B CA    1 
ATOM   5441 C  C     . ALA   B  2 89  ? 36.86500 -103.63900 -25.98700 1.000 93.43206  ? 81  ALA   B C     1 
ATOM   5442 O  O     . ALA   B  2 89  ? 37.40100 -104.49600 -26.71500 1.000 94.80931  ? 81  ALA   B O     1 
ATOM   5443 C  CB    . ALA   B  2 89  ? 37.39600 -101.18500 -26.07500 1.000 89.99621  ? 81  ALA   B CB    1 
ATOM   5444 N  N     . GLY   B  2 90  ? 35.56700 -103.61800 -25.66300 1.000 88.26609  ? 82  GLY   B N     1 
ATOM   5445 C  CA    . GLY   B  2 90  ? 34.57900 -104.64500 -26.04700 1.000 87.73068  ? 82  GLY   B CA    1 
ATOM   5446 C  C     . GLY   B  2 90  ? 34.38600 -104.71900 -27.55200 1.000 87.93977  ? 82  GLY   B C     1 
ATOM   5447 O  O     . GLY   B  2 90  ? 34.65500 -103.70800 -28.23200 1.000 87.86111  ? 82  GLY   B O     1 
ATOM   5448 N  N     . VAL   B  2 91  ? 33.95200 -105.88000 -28.05300 1.000 89.64755  ? 83  VAL   B N     1 
ATOM   5449 C  CA    . VAL   B  2 91  ? 33.61900 -106.12700 -29.48800 1.000 87.74878  ? 83  VAL   B CA    1 
ATOM   5450 C  C     . VAL   B  2 91  ? 32.09400 -106.06700 -29.65100 1.000 87.14145  ? 83  VAL   B C     1 
ATOM   5451 O  O     . VAL   B  2 91  ? 31.39200 -106.66600 -28.81900 1.000 89.10885  ? 83  VAL   B O     1 
ATOM   5452 C  CB    . VAL   B  2 91  ? 34.19800 -107.47100 -29.97800 1.000 89.53981  ? 83  VAL   B CB    1 
ATOM   5453 C  CG1   . VAL   B  2 91  ? 35.65300 -107.64000 -29.56500 1.000 95.12923  ? 83  VAL   B CG1   1 
ATOM   5454 C  CG2   . VAL   B  2 91  ? 33.38000 -108.67000 -29.51900 1.000 88.59211  ? 83  VAL   B CG2   1 
ATOM   5455 N  N     . ALA   B  2 92  ? 31.61100 -105.36000 -30.67800 1.000 90.30544  ? 84  ALA   B N     1 
ATOM   5456 C  CA    . ALA   B  2 92  ? 30.17200 -105.18600 -31.00100 1.000 90.18200  ? 84  ALA   B CA    1 
ATOM   5457 C  C     . ALA   B  2 92  ? 29.76900 -106.13000 -32.14000 1.000 92.51542  ? 84  ALA   B C     1 
ATOM   5458 O  O     . ALA   B  2 92  ? 28.63900 -106.65100 -32.10000 1.000 98.02187  ? 84  ALA   B O     1 
ATOM   5459 C  CB    . ALA   B  2 92  ? 29.89500 -103.74900 -31.36300 1.000 90.54958  ? 84  ALA   B CB    1 
ATOM   5460 N  N     . ASP   B  2 93  ? 30.65200 -106.31400 -33.12600 1.000 88.49274  ? 85  ASP   B N     1 
ATOM   5461 C  CA    . ASP   B  2 93  ? 30.46700 -107.24900 -34.26700 1.000 89.34246  ? 85  ASP   B CA    1 
ATOM   5462 C  C     . ASP   B  2 93  ? 31.83700 -107.80900 -34.66600 1.000 90.95336  ? 85  ASP   B C     1 
ATOM   5463 O  O     . ASP   B  2 93  ? 32.86300 -107.21800 -34.26700 1.000 90.10774  ? 85  ASP   B O     1 
ATOM   5464 C  CB    . ASP   B  2 93  ? 29.76600 -106.56300 -35.44400 1.000 90.33065  ? 85  ASP   B CB    1 
ATOM   5465 C  CG    . ASP   B  2 93  ? 29.34000 -107.50300 -36.56300 1.000 91.38395  ? 85  ASP   B CG    1 
ATOM   5466 O  OD1   . ASP   B  2 93  ? 29.28600 -108.72700 -36.32000 1.000 91.16780  ? 85  ASP   B OD1   1 
ATOM   5467 O  OD2   . ASP   B  2 93  ? 29.07000 -107.00500 -37.67200 1.000 92.73779  ? 85  ASP   B OD2   1 
ATOM   5468 N  N     . LEU   B  2 94  ? 31.83700 -108.91100 -35.42000 1.000 92.87147  ? 86  LEU   B N     1 
ATOM   5469 C  CA    . LEU   B  2 94  ? 33.04900 -109.68100 -35.80000 1.000 92.17477  ? 86  LEU   B CA    1 
ATOM   5470 C  C     . LEU   B  2 94  ? 32.82100 -110.32600 -37.17000 1.000 94.14906  ? 86  LEU   B C     1 
ATOM   5471 O  O     . LEU   B  2 94  ? 31.65100 -110.57900 -37.50500 1.000 97.14406  ? 86  LEU   B O     1 
ATOM   5472 C  CB    . LEU   B  2 94  ? 33.28400 -110.74300 -34.72200 1.000 91.59014  ? 86  LEU   B CB    1 
ATOM   5473 C  CG    . LEU   B  2 94  ? 34.71100 -111.26400 -34.58000 1.000 93.37539  ? 86  LEU   B CG    1 
ATOM   5474 C  CD1   . LEU   B  2 94  ? 35.69500 -110.12700 -34.35700 1.000 92.67249  ? 86  LEU   B CD1   1 
ATOM   5475 C  CD2   . LEU   B  2 94  ? 34.79800 -112.26200 -33.43600 1.000 97.10016  ? 86  LEU   B CD2   1 
ATOM   5476 N  N     . THR   B  2 95  ? 33.89300 -110.57200 -37.92600 1.000 94.78376  ? 87  THR   B N     1 
ATOM   5477 C  CA    . THR   B  2 95  ? 33.85800 -111.32500 -39.20800 1.000 97.69284  ? 87  THR   B CA    1 
ATOM   5478 C  C     . THR   B  2 95  ? 35.21900 -111.98000 -39.46400 1.000 98.02333  ? 87  THR   B C     1 
ATOM   5479 O  O     . THR   B  2 95  ? 36.25500 -111.35600 -39.15000 1.000 98.31977  ? 87  THR   B O     1 
ATOM   5480 C  CB    . THR   B  2 95  ? 33.42700 -110.43600 -40.38600 1.000 99.94719  ? 87  THR   B CB    1 
ATOM   5481 O  OG1   . THR   B  2 95  ? 33.29200 -111.26500 -41.54200 1.000 99.44580  ? 87  THR   B OG1   1 
ATOM   5482 C  CG2   . THR   B  2 95  ? 34.39400 -109.31400 -40.69500 1.000 98.75810  ? 87  THR   B CG2   1 
ATOM   5483 N  N     . TRP   B  2 96  ? 35.19400 -113.20200 -39.99900 1.000 99.20064  ? 88  TRP   B N     1 
ATOM   5484 C  CA    . TRP   B  2 96  ? 36.36800 -113.88600 -40.59900 1.000 101.36784 ? 88  TRP   B CA    1 
ATOM   5485 C  C     . TRP   B  2 96  ? 36.79400 -113.11100 -41.85100 1.000 103.22338 ? 88  TRP   B C     1 
ATOM   5486 O  O     . TRP   B  2 96  ? 35.91300 -112.80100 -42.67800 1.000 107.59686 ? 88  TRP   B O     1 
ATOM   5487 C  CB    . TRP   B  2 96  ? 36.03700 -115.34500 -40.93800 1.000 102.41565 ? 88  TRP   B CB    1 
ATOM   5488 C  CG    . TRP   B  2 96  ? 36.21300 -116.32600 -39.81800 1.000 102.07305 ? 88  TRP   B CG    1 
ATOM   5489 C  CD1   . TRP   B  2 96  ? 35.24000 -117.07800 -39.22600 1.000 101.37588 ? 88  TRP   B CD1   1 
ATOM   5490 C  CD2   . TRP   B  2 96  ? 37.44800 -116.70100 -39.18200 1.000 103.02977 ? 88  TRP   B CD2   1 
ATOM   5491 N  NE1   . TRP   B  2 96  ? 35.78100 -117.88400 -38.26100 1.000 101.93038 ? 88  TRP   B NE1   1 
ATOM   5492 C  CE2   . TRP   B  2 96  ? 37.13400 -117.67600 -38.21100 1.000 102.92412 ? 88  TRP   B CE2   1 
ATOM   5493 C  CE3   . TRP   B  2 96  ? 38.78300 -116.31000 -39.33300 1.000 104.34920 ? 88  TRP   B CE3   1 
ATOM   5494 C  CZ2   . TRP   B  2 96  ? 38.10800 -118.25900 -37.40000 1.000 104.14090 ? 88  TRP   B CZ2   1 
ATOM   5495 C  CZ3   . TRP   B  2 96  ? 39.74400 -116.88400 -38.52900 1.000 105.40462 ? 88  TRP   B CZ3   1 
ATOM   5496 C  CH2   . TRP   B  2 96  ? 39.40800 -117.84500 -37.57500 1.000 105.31488 ? 88  TRP   B CH2   1 
ATOM   5497 N  N     . VAL   B  2 97  ? 38.08300 -112.78300 -41.96500 1.000 104.71188 ? 89  VAL   B N     1 
ATOM   5498 C  CA    . VAL   B  2 97  ? 38.72600 -112.31100 -43.22700 1.000 107.51460 ? 89  VAL   B CA    1 
ATOM   5499 C  C     . VAL   B  2 97  ? 39.48200 -113.50600 -43.81700 1.000 111.37459 ? 89  VAL   B C     1 
ATOM   5500 O  O     . VAL   B  2 97  ? 40.68300 -113.66300 -43.51500 1.000 111.10782 ? 89  VAL   B O     1 
ATOM   5501 C  CB    . VAL   B  2 97  ? 39.64100 -111.09300 -42.99200 1.000 108.17732 ? 89  VAL   B CB    1 
ATOM   5502 C  CG1   . VAL   B  2 97  ? 40.34800 -110.64900 -44.26600 1.000 111.68350 ? 89  VAL   B CG1   1 
ATOM   5503 C  CG2   . VAL   B  2 97  ? 38.87300 -109.93100 -42.38200 1.000 106.06837 ? 89  VAL   B CG2   1 
ATOM   5504 N  N     . GLY   B  2 98  ? 38.77900 -114.33200 -44.59800 1.000 112.62874 ? 90  GLY   B N     1 
ATOM   5505 C  CA    . GLY   B  2 98  ? 39.30700 -115.58500 -45.16900 1.000 110.35876 ? 90  GLY   B CA    1 
ATOM   5506 C  C     . GLY   B  2 98  ? 39.42500 -116.66700 -44.10900 1.000 117.20384 ? 90  GLY   B C     1 
ATOM   5507 O  O     . GLY   B  2 98  ? 38.37100 -117.13500 -43.62600 1.000 113.08038 ? 90  GLY   B O     1 
ATOM   5508 N  N     . GLU   B  2 99  ? 40.65900 -117.01800 -43.73000 1.000 108.30090 ? 91  GLU   B N     1 
ATOM   5509 C  CA    . GLU   B  2 99  ? 40.98100 -118.21800 -42.90900 1.000 108.25090 ? 91  GLU   B CA    1 
ATOM   5510 C  C     . GLU   B  2 99  ? 41.74500 -117.84700 -41.62700 1.000 107.19252 ? 91  GLU   B C     1 
ATOM   5511 O  O     . GLU   B  2 99  ? 41.52500 -118.53600 -40.61300 1.000 103.78897 ? 91  GLU   B O     1 
ATOM   5512 C  CB    . GLU   B  2 99  ? 41.78300 -119.20800 -43.75600 1.000 109.58013 ? 91  GLU   B CB    1 
ATOM   5513 C  CG    . GLU   B  2 99  ? 41.01600 -119.73100 -44.95900 1.000 105.69978 ? 91  GLU   B CG    1 
ATOM   5514 C  CD    . GLU   B  2 99  ? 39.79300 -120.56500 -44.61400 1.000 109.11213 ? 91  GLU   B CD    1 
ATOM   5515 O  OE1   . GLU   B  2 99  ? 39.94700 -121.54800 -43.86000 1.000 111.34013 ? 91  GLU   B OE1   1 
ATOM   5516 O  OE2   . GLU   B  2 99  ? 38.68900 -120.22200 -45.08700 1.000 105.90167 ? 91  GLU   B OE2   1 
ATOM   5517 N  N     . ARG   B  2 100 ? 42.62600 -116.83800 -41.66700 1.000 107.05863 ? 92  ARG   B N     1 
ATOM   5518 C  CA    . ARG   B  2 100 ? 43.50500 -116.45300 -40.52500 1.000 106.78010 ? 92  ARG   B CA    1 
ATOM   5519 C  C     . ARG   B  2 100 ? 43.22200 -115.02000 -40.04500 1.000 109.31349 ? 92  ARG   B C     1 
ATOM   5520 O  O     . ARG   B  2 100 ? 43.78100 -114.64100 -38.99800 1.000 108.95475 ? 92  ARG   B O     1 
ATOM   5521 C  CB    . ARG   B  2 100 ? 44.97500 -116.60900 -40.92600 1.000 105.91491 ? 92  ARG   B CB    1 
ATOM   5522 C  CG    . ARG   B  2 100 ? 45.49900 -118.03300 -40.80800 1.000 111.91407 ? 92  ARG   B CG    1 
ATOM   5523 C  CD    . ARG   B  2 100 ? 47.00200 -118.11600 -40.99400 1.000 113.51562 ? 92  ARG   B CD    1 
ATOM   5524 N  NE    . ARG   B  2 100 ? 47.56100 -119.34600 -40.44500 1.000 119.39894 ? 92  ARG   B NE    1 
ATOM   5525 C  CZ    . ARG   B  2 100 ? 47.51700 -120.54400 -41.03000 1.000 122.73680 ? 92  ARG   B CZ    1 
ATOM   5526 N  NH1   . ARG   B  2 100 ? 46.92800 -120.70300 -42.20500 1.000 116.40424 ? 92  ARG   B NH1   1 
ATOM   5527 N  NH2   . ARG   B  2 100 ? 48.06500 -121.58800 -40.43000 1.000 121.21334 ? 92  ARG   B NH2   1 
ATOM   5528 N  N     . GLY   B  2 101 ? 42.39600 -114.25000 -40.76100 1.000 110.81520 ? 93  GLY   B N     1 
ATOM   5529 C  CA    . GLY   B  2 101 ? 42.09900 -112.84100 -40.43400 1.000 103.19660 ? 93  GLY   B CA    1 
ATOM   5530 C  C     . GLY   B  2 101 ? 40.82800 -112.70500 -39.61200 1.000 99.53247  ? 93  GLY   B C     1 
ATOM   5531 O  O     . GLY   B  2 101 ? 39.86600 -113.44200 -39.89000 1.000 101.14296 ? 93  GLY   B O     1 
ATOM   5532 N  N     . ILE   B  2 102 ? 40.82200 -111.79500 -38.63300 1.000 96.76526  ? 94  ILE   B N     1 
ATOM   5533 C  CA    . ILE   B  2 102 ? 39.64100 -111.48300 -37.77000 1.000 101.11561 ? 94  ILE   B CA    1 
ATOM   5534 C  C     . ILE   B  2 102 ? 39.46400 -109.96000 -37.72200 1.000 95.53320  ? 94  ILE   B C     1 
ATOM   5535 O  O     . ILE   B  2 102 ? 40.28800 -109.29500 -37.06500 1.000 96.11287  ? 94  ILE   B O     1 
ATOM   5536 C  CB    . ILE   B  2 102 ? 39.80100 -112.08700 -36.35700 1.000 95.98149  ? 94  ILE   B CB    1 
ATOM   5537 C  CG1   . ILE   B  2 102 ? 40.00800 -113.60400 -36.39700 1.000 92.07211  ? 94  ILE   B CG1   1 
ATOM   5538 C  CG2   . ILE   B  2 102 ? 38.61600 -111.71100 -35.48100 1.000 91.91553  ? 94  ILE   B CG2   1 
ATOM   5539 C  CD1   . ILE   B  2 102 ? 40.43100 -114.20900 -35.07600 1.000 93.64998  ? 94  ILE   B CD1   1 
ATOM   5540 N  N     . LEU   B  2 103 ? 38.42500 -109.44100 -38.38600 1.000 88.31590  ? 95  LEU   B N     1 
ATOM   5541 C  CA    . LEU   B  2 103 ? 38.08500 -107.99200 -38.42700 1.000 91.51977  ? 95  LEU   B CA    1 
ATOM   5542 C  C     . LEU   B  2 103 ? 37.05800 -107.68500 -37.33000 1.000 90.37200  ? 95  LEU   B C     1 
ATOM   5543 O  O     . LEU   B  2 103 ? 35.99000 -108.33100 -37.32700 1.000 91.47645  ? 95  LEU   B O     1 
ATOM   5544 C  CB    . LEU   B  2 103 ? 37.53700 -107.64800 -39.81500 1.000 84.80108  ? 95  LEU   B CB    1 
ATOM   5545 C  CG    . LEU   B  2 103 ? 37.33400 -106.16000 -40.09400 1.000 85.39833  ? 95  LEU   B CG    1 
ATOM   5546 C  CD1   . LEU   B  2 103 ? 38.66900 -105.45000 -40.25800 1.000 88.93470  ? 95  LEU   B CD1   1 
ATOM   5547 C  CD2   . LEU   B  2 103 ? 36.46800 -105.95600 -41.32900 1.000 93.05114  ? 95  LEU   B CD2   1 
ATOM   5548 N  N     . VAL   B  2 104 ? 37.36700 -106.72300 -36.45200 1.000 87.60178  ? 96  VAL   B N     1 
ATOM   5549 C  CA    . VAL   B  2 104 ? 36.59900 -106.43000 -35.20300 1.000 83.46248  ? 96  VAL   B CA    1 
ATOM   5550 C  C     . VAL   B  2 104 ? 36.02500 -105.01100 -35.27800 1.000 79.53017  ? 96  VAL   B C     1 
ATOM   5551 O  O     . VAL   B  2 104 ? 36.73300 -104.10700 -35.76500 1.000 80.63934  ? 96  VAL   B O     1 
ATOM   5552 C  CB    . VAL   B  2 104 ? 37.48100 -106.58500 -33.94900 1.000 90.16338  ? 96  VAL   B CB    1 
ATOM   5553 C  CG1   . VAL   B  2 104 ? 36.65000 -106.64500 -32.67600 1.000 91.57095  ? 96  VAL   B CG1   1 
ATOM   5554 C  CG2   . VAL   B  2 104 ? 38.40200 -107.79100 -34.03600 1.000 84.29423  ? 96  VAL   B CG2   1 
ATOM   5555 N  N     . ALA   B  2 105 ? 34.79700 -104.83500 -34.78200 1.000 78.87177  ? 97  ALA   B N     1 
ATOM   5556 C  CA    . ALA   B  2 105 ? 34.11700 -103.53300 -34.59200 1.000 75.98168  ? 97  ALA   B CA    1 
ATOM   5557 C  C     . ALA   B  2 105 ? 34.10800 -103.20000 -33.09600 1.000 78.43714  ? 97  ALA   B C     1 
ATOM   5558 O  O     . ALA   B  2 105 ? 33.30900 -103.81800 -32.36500 1.000 83.58023  ? 97  ALA   B O     1 
ATOM   5559 C  CB    . ALA   B  2 105 ? 32.72100 -103.60600 -35.15900 1.000 77.75515  ? 97  ALA   B CB    1 
ATOM   5560 N  N     . SER   B  2 106 ? 34.97200 -102.27100 -32.66600 1.000 77.56351  ? 98  SER   B N     1 
ATOM   5561 C  CA    . SER   B  2 106 ? 35.26900 -101.96100 -31.23900 1.000 78.42143  ? 98  SER   B CA    1 
ATOM   5562 C  C     . SER   B  2 106 ? 34.34600 -100.85600 -30.70800 1.000 77.51204  ? 98  SER   B C     1 
ATOM   5563 O  O     . SER   B  2 106 ? 33.88900 -100.01600 -31.51000 1.000 81.12184  ? 98  SER   B O     1 
ATOM   5564 C  CB    . SER   B  2 106 ? 36.71700 -101.57700 -31.06200 1.000 82.27904  ? 98  SER   B CB    1 
ATOM   5565 O  OG    . SER   B  2 106 ? 37.03900 -101.41900 -29.68900 1.000 80.38212  ? 98  SER   B OG    1 
ATOM   5566 N  N     . ASP   B  2 107 ? 34.09800 -100.86400 -29.39400 1.000 80.82757  ? 99  ASP   B N     1 
ATOM   5567 C  CA    . ASP   B  2 107 ? 33.41400 -99.77500  -28.64300 1.000 77.00698  ? 99  ASP   B CA    1 
ATOM   5568 C  C     . ASP   B  2 107 ? 34.25500 -98.49700  -28.73800 1.000 75.40505  ? 99  ASP   B C     1 
ATOM   5569 O  O     . ASP   B  2 107 ? 33.65800 -97.40500  -28.80600 1.000 77.23236  ? 99  ASP   B O     1 
ATOM   5570 C  CB    . ASP   B  2 107 ? 33.20500 -100.14100 -27.17000 1.000 78.72909  ? 99  ASP   B CB    1 
ATOM   5571 C  CG    . ASP   B  2 107 ? 32.08900 -101.14000 -26.92000 1.000 74.01818  ? 99  ASP   B CG    1 
ATOM   5572 O  OD1   . ASP   B  2 107 ? 30.95700 -100.87700 -27.37100 1.000 72.74719  ? 99  ASP   B OD1   1 
ATOM   5573 O  OD2   . ASP   B  2 107 ? 32.36000 -102.17100 -26.27200 1.000 74.96413  ? 99  ASP   B OD2   1 
ATOM   5574 N  N     . SER   B  2 108 ? 35.58700 -98.64600  -28.74400 1.000 76.83338  ? 100 SER   B N     1 
ATOM   5575 C  CA    . SER   B  2 108 ? 36.60200 -97.55600  -28.78900 1.000 78.66838  ? 100 SER   B CA    1 
ATOM   5576 C  C     . SER   B  2 108 ? 36.36700 -96.63800  -29.99500 1.000 81.20923  ? 100 SER   B C     1 
ATOM   5577 O  O     . SER   B  2 108 ? 36.82000 -95.47400  -29.94300 1.000 84.72226  ? 100 SER   B O     1 
ATOM   5578 C  CB    . SER   B  2 108 ? 38.00200 -98.12500  -28.81300 1.000 83.26105  ? 100 SER   B CB    1 
ATOM   5579 O  OG    . SER   B  2 108 ? 38.20900 -98.92400  -29.97000 1.000 81.38570  ? 100 SER   B OG    1 
ATOM   5580 N  N     . GLY   B  2 109 ? 35.69400 -97.14600  -31.03300 1.000 77.22625  ? 101 GLY   B N     1 
ATOM   5581 C  CA    . GLY   B  2 109 ? 35.46800 -96.44600  -32.31100 1.000 78.34831  ? 101 GLY   B CA    1 
ATOM   5582 C  C     . GLY   B  2 109 ? 36.51900 -96.83000  -33.33300 1.000 85.08834  ? 101 GLY   B C     1 
ATOM   5583 O  O     . GLY   B  2 109 ? 36.64400 -96.12400  -34.35300 1.000 86.99276  ? 101 GLY   B O     1 
ATOM   5584 N  N     . ALA   B  2 110 ? 37.25000 -97.91700  -33.06400 1.000 85.75037  ? 102 ALA   B N     1 
ATOM   5585 C  CA    . ALA   B  2 110 ? 38.29900 -98.48000  -33.94200 1.000 85.70544  ? 102 ALA   B CA    1 
ATOM   5586 C  C     . ALA   B  2 110 ? 37.73800 -99.69700  -34.68200 1.000 84.94628  ? 102 ALA   B C     1 
ATOM   5587 O  O     . ALA   B  2 110 ? 36.93700 -100.44300 -34.08200 1.000 80.32713  ? 102 ALA   B O     1 
ATOM   5588 C  CB    . ALA   B  2 110 ? 39.51500 -98.84500  -33.12600 1.000 84.06159  ? 102 ALA   B CB    1 
ATOM   5589 N  N     . VAL   B  2 111 ? 38.11700 -99.84800  -35.95300 1.000 87.94067  ? 103 VAL   B N     1 
ATOM   5590 C  CA    . VAL   B  2 111 ? 38.07100 -101.13300 -36.70900 1.000 87.12603  ? 103 VAL   B CA    1 
ATOM   5591 C  C     . VAL   B  2 111 ? 39.48000 -101.72300 -36.62900 1.000 90.23796  ? 103 VAL   B C     1 
ATOM   5592 O  O     . VAL   B  2 111 ? 40.43300 -100.99600 -36.97700 1.000 92.50697  ? 103 VAL   B O     1 
ATOM   5593 C  CB    . VAL   B  2 111 ? 37.61600 -100.92400 -38.16800 1.000 91.13664  ? 103 VAL   B CB    1 
ATOM   5594 C  CG1   . VAL   B  2 111 ? 37.58800 -102.22700 -38.95400 1.000 91.97606  ? 103 VAL   B CG1   1 
ATOM   5595 C  CG2   . VAL   B  2 111 ? 36.26200 -100.23500 -38.24100 1.000 90.55913  ? 103 VAL   B CG2   1 
ATOM   5596 N  N     . GLU   B  2 112 ? 39.61300 -102.96500 -36.15500 1.000 92.82089  ? 104 GLU   B N     1 
ATOM   5597 C  CA    . GLU   B  2 112 ? 40.93000 -103.63000 -35.96500 1.000 99.78736  ? 104 GLU   B CA    1 
ATOM   5598 C  C     . GLU   B  2 112 ? 40.90600 -105.02200 -36.61000 1.000 94.88594  ? 104 GLU   B C     1 
ATOM   5599 O  O     . GLU   B  2 112 ? 39.86600 -105.70500 -36.52900 1.000 93.10091  ? 104 GLU   B O     1 
ATOM   5600 C  CB    . GLU   B  2 112 ? 41.33100 -103.65800 -34.48400 1.000 100.03711 ? 104 GLU   B CB    1 
ATOM   5601 C  CG    . GLU   B  2 112 ? 40.23900 -104.10100 -33.52400 1.000 98.51715  ? 104 GLU   B CG    1 
ATOM   5602 C  CD    . GLU   B  2 112 ? 40.57600 -103.93000 -32.04900 1.000 105.73446 ? 104 GLU   B CD    1 
ATOM   5603 O  OE1   . GLU   B  2 112 ? 41.64000 -103.35200 -31.74100 1.000 112.33921 ? 104 GLU   B OE1   1 
ATOM   5604 O  OE2   . GLU   B  2 112 ? 39.77700 -104.38600 -31.20500 1.000 110.26581 ? 104 GLU   B OE2   1 
ATOM   5605 N  N     . LEU   B  2 113 ? 42.01500 -105.39000 -37.26000 1.000 99.46636  ? 105 LEU   B N     1 
ATOM   5606 C  CA    . LEU   B  2 113 ? 42.25100 -106.71400 -37.89500 1.000 103.28821 ? 105 LEU   B CA    1 
ATOM   5607 C  C     . LEU   B  2 113 ? 43.29500 -107.46800 -37.06500 1.000 108.50184 ? 105 LEU   B C     1 
ATOM   5608 O  O     . LEU   B  2 113 ? 44.44900 -106.99600 -36.99500 1.000 102.96873 ? 105 LEU   B O     1 
ATOM   5609 C  CB    . LEU   B  2 113 ? 42.73300 -106.49600 -39.33300 1.000 103.03607 ? 105 LEU   B CB    1 
ATOM   5610 C  CG    . LEU   B  2 113 ? 43.17000 -107.74500 -40.09900 1.000 94.56079  ? 105 LEU   B CG    1 
ATOM   5611 C  CD1   . LEU   B  2 113 ? 41.98400 -108.64700 -40.39800 1.000 92.90011  ? 105 LEU   B CD1   1 
ATOM   5612 C  CD2   . LEU   B  2 113 ? 43.88300 -107.36100 -41.38600 1.000 96.50316  ? 105 LEU   B CD2   1 
ATOM   5613 N  N     . TRP   B  2 114 ? 42.89100 -108.57900 -36.44300 1.000 109.70256 ? 106 TRP   B N     1 
ATOM   5614 C  CA    . TRP   B  2 114 ? 43.78100 -109.48100 -35.66500 1.000 113.45136 ? 106 TRP   B CA    1 
ATOM   5615 C  C     . TRP   B  2 114 ? 44.18700 -110.66600 -36.54900 1.000 115.25720 ? 106 TRP   B C     1 
ATOM   5616 O  O     . TRP   B  2 114 ? 43.30600 -111.21500 -37.24300 1.000 113.05895 ? 106 TRP   B O     1 
ATOM   5617 C  CB    . TRP   B  2 114 ? 43.09800 -109.93200 -34.36800 1.000 114.72768 ? 106 TRP   B CB    1 
ATOM   5618 C  CG    . TRP   B  2 114 ? 42.81700 -108.81400 -33.41000 1.000 115.73546 ? 106 TRP   B CG    1 
ATOM   5619 C  CD1   . TRP   B  2 114 ? 41.75900 -107.95300 -33.44500 1.000 112.04929 ? 106 TRP   B CD1   1 
ATOM   5620 C  CD2   . TRP   B  2 114 ? 43.60600 -108.42900 -32.26900 1.000 113.23765 ? 106 TRP   B CD2   1 
ATOM   5621 N  NE1   . TRP   B  2 114 ? 41.83500 -107.06100 -32.41000 1.000 109.98370 ? 106 TRP   B NE1   1 
ATOM   5622 C  CE2   . TRP   B  2 114 ? 42.95700 -107.32700 -31.67100 1.000 111.19790 ? 106 TRP   B CE2   1 
ATOM   5623 C  CE3   . TRP   B  2 114 ? 44.79200 -108.90200 -31.69600 1.000 109.03506 ? 106 TRP   B CE3   1 
ATOM   5624 C  CZ2   . TRP   B  2 114 ? 43.45800 -106.69600 -30.53300 1.000 114.75498 ? 106 TRP   B CZ2   1 
ATOM   5625 C  CZ3   . TRP   B  2 114 ? 45.28600 -108.27900 -30.57100 1.000 110.80262 ? 106 TRP   B CZ3   1 
ATOM   5626 C  CH2   . TRP   B  2 114 ? 44.62500 -107.19200 -29.99800 1.000 114.92371 ? 106 TRP   B CH2   1 
ATOM   5627 N  N     . GLU   B  2 115 ? 45.47500 -111.02300 -36.53300 1.000 128.16789 ? 107 GLU   B N     1 
ATOM   5628 C  CA    . GLU   B  2 115 ? 46.07700 -112.08800 -37.38300 1.000 128.60900 ? 107 GLU   B CA    1 
ATOM   5629 C  C     . GLU   B  2 115 ? 46.24500 -113.36800 -36.55700 1.000 128.19508 ? 107 GLU   B C     1 
ATOM   5630 O  O     . GLU   B  2 115 ? 46.96500 -113.32700 -35.53800 1.000 123.81978 ? 107 GLU   B O     1 
ATOM   5631 C  CB    . GLU   B  2 115 ? 47.43200 -111.63200 -37.92700 1.000 129.88197 ? 107 GLU   B CB    1 
ATOM   5632 C  CG    . GLU   B  2 115 ? 47.93800 -112.45600 -39.09900 1.000 128.69695 ? 107 GLU   B CG    1 
ATOM   5633 C  CD    . GLU   B  2 115 ? 47.43600 -112.00200 -40.45900 1.000 129.13628 ? 107 GLU   B CD    1 
ATOM   5634 O  OE1   . GLU   B  2 115 ? 46.33800 -111.41400 -40.52100 1.000 129.86640 ? 107 GLU   B OE1   1 
ATOM   5635 O  OE2   . GLU   B  2 115 ? 48.15000 -112.23400 -41.45300 1.000 132.15938 ? 107 GLU   B OE2   1 
ATOM   5636 N  N     . LEU   B  2 116 ? 45.61200 -114.46000 -36.99300 1.000 120.24816 ? 108 LEU   B N     1 
ATOM   5637 C  CA    . LEU   B  2 116 ? 45.80300 -115.81800 -36.42000 1.000 117.83700 ? 108 LEU   B CA    1 
ATOM   5638 C  C     . LEU   B  2 116 ? 47.21500 -116.29400 -36.78600 1.000 118.59632 ? 108 LEU   B C     1 
ATOM   5639 O  O     . LEU   B  2 116 ? 47.64500 -116.03700 -37.92800 1.000 120.45862 ? 108 LEU   B O     1 
ATOM   5640 C  CB    . LEU   B  2 116 ? 44.71300 -116.74500 -36.97100 1.000 117.22473 ? 108 LEU   B CB    1 
ATOM   5641 C  CG    . LEU   B  2 116 ? 44.48400 -118.04900 -36.20900 1.000 117.06055 ? 108 LEU   B CG    1 
ATOM   5642 C  CD1   . LEU   B  2 116 ? 44.04500 -117.78500 -34.77500 1.000 112.41399 ? 108 LEU   B CD1   1 
ATOM   5643 C  CD2   . LEU   B  2 116 ? 43.45400 -118.90800 -36.92500 1.000 113.24960 ? 108 LEU   B CD2   1 
ATOM   5644 N  N     . ASP   B  2 117 ? 47.90500 -116.94500 -35.84400 1.000 118.29696 ? 109 ASP   B N     1 
ATOM   5645 C  CA    . ASP   B  2 117 ? 49.35500 -117.28100 -35.92000 1.000 121.75707 ? 109 ASP   B CA    1 
ATOM   5646 C  C     . ASP   B  2 117 ? 49.59600 -118.28700 -37.05400 1.000 124.56814 ? 109 ASP   B C     1 
ATOM   5647 O  O     . ASP   B  2 117 ? 48.60700 -118.80700 -37.61300 1.000 121.63430 ? 109 ASP   B O     1 
ATOM   5648 C  CB    . ASP   B  2 117 ? 49.86300 -117.83000 -34.57900 1.000 120.29068 ? 109 ASP   B CB    1 
ATOM   5649 C  CG    . ASP   B  2 117 ? 51.29700 -117.46000 -34.23300 1.000 125.11284 ? 109 ASP   B CG    1 
ATOM   5650 O  OD1   . ASP   B  2 117 ? 51.72400 -116.34600 -34.59700 1.000 130.70259 ? 109 ASP   B OD1   1 
ATOM   5651 O  OD2   . ASP   B  2 117 ? 51.97000 -118.28500 -33.58400 1.000 127.55669 ? 109 ASP   B OD2   1 
ATOM   5652 N  N     . GLU   B  2 118 ? 50.87000 -118.55200 -37.36900 1.000 128.11299 ? 110 GLU   B N     1 
ATOM   5653 C  CA    . GLU   B  2 118 ? 51.31100 -119.60800 -38.32400 1.000 130.11360 ? 110 GLU   B CA    1 
ATOM   5654 C  C     . GLU   B  2 118 ? 50.92100 -120.98400 -37.76500 1.000 130.49529 ? 110 GLU   B C     1 
ATOM   5655 O  O     . GLU   B  2 118 ? 50.64100 -121.89000 -38.57700 1.000 130.98113 ? 110 GLU   B O     1 
ATOM   5656 C  CB    . GLU   B  2 118 ? 52.82000 -119.50500 -38.56600 1.000 134.32148 ? 110 GLU   B CB    1 
ATOM   5657 C  CG    . GLU   B  2 118 ? 53.33200 -120.37000 -39.70800 1.000 136.95136 ? 110 GLU   B CG    1 
ATOM   5658 C  CD    . GLU   B  2 118 ? 52.95700 -119.91500 -41.11100 1.000 148.23607 ? 110 GLU   B CD    1 
ATOM   5659 O  OE1   . GLU   B  2 118 ? 52.32000 -118.85200 -41.24400 1.000 150.22968 ? 110 GLU   B OE1   1 
ATOM   5660 O  OE2   . GLU   B  2 118 ? 53.31000 -120.62800 -42.07300 1.000 145.28003 ? 110 GLU   B OE2   1 
ATOM   5661 N  N     . ASN   B  2 119 ? 50.90900 -121.12700 -36.43200 1.000 129.17233 ? 111 ASN   B N     1 
ATOM   5662 C  CA    . ASN   B  2 119 ? 50.49700 -122.35700 -35.69900 1.000 124.46957 ? 111 ASN   B CA    1 
ATOM   5663 C  C     . ASN   B  2 119 ? 49.02400 -122.26000 -35.28000 1.000 119.27811 ? 111 ASN   B C     1 
ATOM   5664 O  O     . ASN   B  2 119 ? 48.45800 -123.30300 -34.89400 1.000 119.87182 ? 111 ASN   B O     1 
ATOM   5665 C  CB    . ASN   B  2 119 ? 51.37500 -122.60200 -34.46700 1.000 122.27031 ? 111 ASN   B CB    1 
ATOM   5666 C  CG    . ASN   B  2 119 ? 52.68800 -123.28300 -34.78900 1.000 125.94022 ? 111 ASN   B CG    1 
ATOM   5667 O  OD1   . ASN   B  2 119 ? 53.11200 -123.31800 -35.94300 1.000 126.68408 ? 111 ASN   B OD1   1 
ATOM   5668 N  ND2   . ASN   B  2 119 ? 53.34000 -123.82400 -33.77400 1.000 128.41575 ? 111 ASN   B ND2   1 
ATOM   5669 N  N     . GLU   B  2 120 ? 48.43400 -121.06200 -35.35600 1.000 118.17863 ? 112 GLU   B N     1 
ATOM   5670 C  CA    . GLU   B  2 120 ? 47.05500 -120.74300 -34.89100 1.000 117.44264 ? 112 GLU   B CA    1 
ATOM   5671 C  C     . GLU   B  2 120 ? 46.97500 -120.95700 -33.37300 1.000 116.08887 ? 112 GLU   B C     1 
ATOM   5672 O  O     . GLU   B  2 120 ? 45.99100 -121.57000 -32.90900 1.000 118.03263 ? 112 GLU   B O     1 
ATOM   5673 C  CB    . GLU   B  2 120 ? 46.02200 -121.58800 -35.64300 1.000 115.60694 ? 112 GLU   B CB    1 
ATOM   5674 C  CG    . GLU   B  2 120 ? 46.12600 -121.48500 -37.15500 1.000 117.43161 ? 112 GLU   B CG    1 
ATOM   5675 C  CD    . GLU   B  2 120 ? 45.05400 -122.24900 -37.91500 1.000 120.09839 ? 112 GLU   B CD    1 
ATOM   5676 O  OE1   . GLU   B  2 120 ? 44.35200 -123.06800 -37.28500 1.000 121.76963 ? 112 GLU   B OE1   1 
ATOM   5677 O  OE2   . GLU   B  2 120 ? 44.91500 -122.01800 -39.13400 1.000 115.63878 ? 112 GLU   B OE2   1 
ATOM   5678 N  N     . THR   B  2 121 ? 47.97700 -120.46300 -32.63700 1.000 114.20362 ? 113 THR   B N     1 
ATOM   5679 C  CA    . THR   B  2 121 ? 48.10900 -120.59600 -31.16000 1.000 115.83860 ? 113 THR   B CA    1 
ATOM   5680 C  C     . THR   B  2 121 ? 48.34200 -119.21700 -30.52500 1.000 115.96101 ? 113 THR   B C     1 
ATOM   5681 O  O     . THR   B  2 121 ? 48.76000 -119.17200 -29.35000 1.000 116.28752 ? 113 THR   B O     1 
ATOM   5682 C  CB    . THR   B  2 121 ? 49.23500 -121.57800 -30.81000 1.000 117.73302 ? 113 THR   B CB    1 
ATOM   5683 O  OG1   . THR   B  2 121 ? 50.45400 -121.07300 -31.35600 1.000 119.43571 ? 113 THR   B OG1   1 
ATOM   5684 C  CG2   . THR   B  2 121 ? 48.98200 -122.97400 -31.33600 1.000 118.83967 ? 113 THR   B CG2   1 
ATOM   5685 N  N     . LEU   B  2 122 ? 48.05700 -118.13800 -31.26100 1.000 115.01786 ? 114 LEU   B N     1 
ATOM   5686 C  CA    . LEU   B  2 122 ? 48.33500 -116.73600 -30.84700 1.000 118.72401 ? 114 LEU   B CA    1 
ATOM   5687 C  C     . LEU   B  2 122 ? 47.64800 -115.77900 -31.83200 1.000 112.76225 ? 114 LEU   B C     1 
ATOM   5688 O  O     . LEU   B  2 122 ? 47.75300 -116.00600 -33.05200 1.000 116.11590 ? 114 LEU   B O     1 
ATOM   5689 C  CB    . LEU   B  2 122 ? 49.85600 -116.53600 -30.80300 1.000 117.76535 ? 114 LEU   B CB    1 
ATOM   5690 C  CG    . LEU   B  2 122 ? 50.35900 -115.09400 -30.72800 1.000 121.19054 ? 114 LEU   B CG    1 
ATOM   5691 C  CD1   . LEU   B  2 122 ? 49.95900 -114.43500 -29.41400 1.000 118.69397 ? 114 LEU   B CD1   1 
ATOM   5692 C  CD2   . LEU   B  2 122 ? 51.86900 -115.04400 -30.91200 1.000 116.55952 ? 114 LEU   B CD2   1 
ATOM   5693 N  N     . ILE   B  2 123 ? 46.95500 -114.76200 -31.31400 1.000 109.08662 ? 115 ILE   B N     1 
ATOM   5694 C  CA    . ILE   B  2 123 ? 46.18200 -113.76400 -32.11200 1.000 110.46416 ? 115 ILE   B CA    1 
ATOM   5695 C  C     . ILE   B  2 123 ? 46.80600 -112.38300 -31.86800 1.000 110.53624 ? 115 ILE   B C     1 
ATOM   5696 O  O     . ILE   B  2 123 ? 46.76800 -111.92300 -30.71100 1.000 112.69560 ? 115 ILE   B O     1 
ATOM   5697 C  CB    . ILE   B  2 123 ? 44.68300 -113.82800 -31.74200 1.000 108.92223 ? 115 ILE   B CB    1 
ATOM   5698 C  CG1   . ILE   B  2 123 ? 44.14400 -115.26200 -31.78300 1.000 107.01770 ? 115 ILE   B CG1   1 
ATOM   5699 C  CG2   . ILE   B  2 123 ? 43.86600 -112.89900 -32.62800 1.000 107.67326 ? 115 ILE   B CG2   1 
ATOM   5700 C  CD1   . ILE   B  2 123 ? 42.82300 -115.45400 -31.07100 1.000 99.15549  ? 115 ILE   B CD1   1 
ATOM   5701 N  N     . VAL   B  2 124 ? 47.38100 -111.76700 -32.90900 1.000 113.73815 ? 116 VAL   B N     1 
ATOM   5702 C  CA    . VAL   B  2 124 ? 48.14600 -110.48300 -32.82500 1.000 112.63237 ? 116 VAL   B CA    1 
ATOM   5703 C  C     . VAL   B  2 124 ? 47.46000 -109.43000 -33.70400 1.000 119.80267 ? 116 VAL   B C     1 
ATOM   5704 O  O     . VAL   B  2 124 ? 46.92800 -109.79900 -34.77100 1.000 117.79834 ? 116 VAL   B O     1 
ATOM   5705 C  CB    . VAL   B  2 124 ? 49.62900 -110.66900 -33.21500 1.000 107.79618 ? 116 VAL   B CB    1 
ATOM   5706 C  CG1   . VAL   B  2 124 ? 50.13300 -112.06900 -32.89300 1.000 109.81061 ? 116 VAL   B CG1   1 
ATOM   5707 C  CG2   . VAL   B  2 124 ? 49.90300 -110.33900 -34.67500 1.000 108.15597 ? 116 VAL   B CG2   1 
ATOM   5708 N  N     . SER   B  2 125 ? 47.49000 -108.16500 -33.26800 1.000 119.40373 ? 117 SER   B N     1 
ATOM   5709 C  CA    . SER   B  2 125 ? 46.87200 -107.00000 -33.95600 1.000 116.14600 ? 117 SER   B CA    1 
ATOM   5710 C  C     . SER   B  2 125 ? 47.72400 -106.60300 -35.16800 1.000 111.07683 ? 117 SER   B C     1 
ATOM   5711 O  O     . SER   B  2 125 ? 48.94400 -106.41100 -34.99100 1.000 113.36073 ? 117 SER   B O     1 
ATOM   5712 C  CB    . SER   B  2 125 ? 46.70000 -105.84200 -33.00600 1.000 112.58629 ? 117 SER   B CB    1 
ATOM   5713 O  OG    . SER   B  2 125 ? 46.04500 -104.75400 -33.64100 1.000 115.49983 ? 117 SER   B OG    1 
ATOM   5714 N  N     . LYS   B  2 126 ? 47.10100 -106.49500 -36.34700 1.000 108.03665 ? 118 LYS   B N     1 
ATOM   5715 C  CA    . LYS   B  2 126 ? 47.73900 -106.00200 -37.59800 1.000 110.32764 ? 118 LYS   B CA    1 
ATOM   5716 C  C     . LYS   B  2 126 ? 47.49900 -104.49400 -37.70600 1.000 104.89581 ? 118 LYS   B C     1 
ATOM   5717 O  O     . LYS   B  2 126 ? 48.49000 -103.73800 -37.71500 1.000 104.49150 ? 118 LYS   B O     1 
ATOM   5718 C  CB    . LYS   B  2 126 ? 47.18900 -106.73600 -38.82600 1.000 110.22885 ? 118 LYS   B CB    1 
ATOM   5719 C  CG    . LYS   B  2 126 ? 47.45600 -108.23400 -38.86100 1.000 113.35876 ? 118 LYS   B CG    1 
ATOM   5720 C  CD    . LYS   B  2 126 ? 48.91400 -108.60500 -39.07400 1.000 119.58299 ? 118 LYS   B CD    1 
ATOM   5721 C  CE    . LYS   B  2 126 ? 49.67300 -108.84900 -37.78600 1.000 113.69618 ? 118 LYS   B CE    1 
ATOM   5722 N  NZ    . LYS   B  2 126 ? 51.00600 -109.44600 -38.04200 1.000 116.67494 ? 118 LYS   B NZ    1 
ATOM   5723 N  N     . PHE   B  2 127 ? 46.23000 -104.08000 -37.78100 1.000 101.00430 ? 119 PHE   B N     1 
ATOM   5724 C  CA    . PHE   B  2 127 ? 45.80600 -102.65700 -37.72400 1.000 102.85070 ? 119 PHE   B CA    1 
ATOM   5725 C  C     . PHE   B  2 127 ? 44.70100 -102.50200 -36.67300 1.000 102.66176 ? 119 PHE   B C     1 
ATOM   5726 O  O     . PHE   B  2 127 ? 43.91300 -103.44700 -36.47600 1.000 99.75356  ? 119 PHE   B O     1 
ATOM   5727 C  CB    . PHE   B  2 127 ? 45.42000 -102.14000 -39.11600 1.000 105.52323 ? 119 PHE   B CB    1 
ATOM   5728 C  CG    . PHE   B  2 127 ? 44.07800 -102.56400 -39.66200 1.000 102.27386 ? 119 PHE   B CG    1 
ATOM   5729 C  CD1   . PHE   B  2 127 ? 42.90600 -101.96000 -39.23000 1.000 96.55195  ? 119 PHE   B CD1   1 
ATOM   5730 C  CD2   . PHE   B  2 127 ? 43.99100 -103.52300 -40.66100 1.000 101.70249 ? 119 PHE   B CD2   1 
ATOM   5731 C  CE1   . PHE   B  2 127 ? 41.67800 -102.33600 -39.75400 1.000 95.51707  ? 119 PHE   B CE1   1 
ATOM   5732 C  CE2   . PHE   B  2 127 ? 42.76200 -103.89400 -41.18700 1.000 97.90121  ? 119 PHE   B CE2   1 
ATOM   5733 C  CZ    . PHE   B  2 127 ? 41.60800 -103.30400 -40.73000 1.000 95.94777  ? 119 PHE   B CZ    1 
ATOM   5734 N  N     . CYS   B  2 128 ? 44.69800 -101.35200 -35.99200 1.000 98.54418  ? 120 CYS   B N     1 
ATOM   5735 C  CA    . CYS   B  2 128 ? 43.63500 -100.87200 -35.06700 1.000 98.76684  ? 120 CYS   B CA    1 
ATOM   5736 C  C     . CYS   B  2 128 ? 43.43100 -99.37400  -35.32000 1.000 97.93262  ? 120 CYS   B C     1 
ATOM   5737 O  O     . CYS   B  2 128 ? 44.15700 -98.56600  -34.70300 1.000 98.42103  ? 120 CYS   B O     1 
ATOM   5738 C  CB    . CYS   B  2 128 ? 44.00000 -101.14500 -33.61100 1.000 100.76158 ? 120 CYS   B CB    1 
ATOM   5739 S  SG    . CYS   B  2 128 ? 42.85500 -100.40300 -32.41600 1.000 95.23396  ? 120 CYS   B SG    1 
ATOM   5740 N  N     . LYS   B  2 129 ? 42.50100 -99.03100  -36.21700 1.000 91.24563  ? 121 LYS   B N     1 
ATOM   5741 C  CA    . LYS   B  2 129 ? 42.36500 -97.67500  -36.81300 1.000 90.96308  ? 121 LYS   B CA    1 
ATOM   5742 C  C     . LYS   B  2 129 ? 41.17200 -96.94100  -36.19200 1.000 91.50307  ? 121 LYS   B C     1 
ATOM   5743 O  O     . LYS   B  2 129 ? 40.02200 -97.33400  -36.47200 1.000 92.81999  ? 121 LYS   B O     1 
ATOM   5744 C  CB    . LYS   B  2 129 ? 42.22500 -97.78800  -38.33400 1.000 96.11524  ? 121 LYS   B CB    1 
ATOM   5745 C  CG    . LYS   B  2 129 ? 43.48300 -98.24800  -39.05800 1.000 100.37386 ? 121 LYS   B CG    1 
ATOM   5746 C  CD    . LYS   B  2 129 ? 44.58000 -97.20300  -39.08700 1.000 99.49333  ? 121 LYS   B CD    1 
ATOM   5747 C  CE    . LYS   B  2 129 ? 45.93100 -97.76700  -39.47300 1.000 100.16518 ? 121 LYS   B CE    1 
ATOM   5748 N  NZ    . LYS   B  2 129 ? 46.95500 -96.70100  -39.58500 1.000 102.80038 ? 121 LYS   B NZ    1 
ATOM   5749 N  N     . TYR   B  2 130 ? 41.45500 -95.90300  -35.39700 1.000 92.81697  ? 122 TYR   B N     1 
ATOM   5750 C  CA    . TYR   B  2 130 ? 40.45700 -95.03100  -34.72200 1.000 91.49922  ? 122 TYR   B CA    1 
ATOM   5751 C  C     . TYR   B  2 130 ? 39.95500 -93.98200  -35.72200 1.000 86.95847  ? 122 TYR   B C     1 
ATOM   5752 O  O     . TYR   B  2 130 ? 40.39700 -92.81800  -35.64400 1.000 88.33941  ? 122 TYR   B O     1 
ATOM   5753 C  CB    . TYR   B  2 130 ? 41.07200 -94.36600  -33.48500 1.000 91.71947  ? 122 TYR   B CB    1 
ATOM   5754 C  CG    . TYR   B  2 130 ? 41.65100 -95.31700  -32.46600 1.000 90.86042  ? 122 TYR   B CG    1 
ATOM   5755 C  CD1   . TYR   B  2 130 ? 40.83800 -95.96700  -31.55000 1.000 90.66450  ? 122 TYR   B CD1   1 
ATOM   5756 C  CD2   . TYR   B  2 130 ? 43.01500 -95.55500  -32.40300 1.000 91.55767  ? 122 TYR   B CD2   1 
ATOM   5757 C  CE1   . TYR   B  2 130 ? 41.36100 -96.83900  -30.60800 1.000 92.34820  ? 122 TYR   B CE1   1 
ATOM   5758 C  CE2   . TYR   B  2 130 ? 43.55500 -96.42200  -31.46600 1.000 92.35871  ? 122 TYR   B CE2   1 
ATOM   5759 C  CZ    . TYR   B  2 130 ? 42.72500 -97.06600  -30.56500 1.000 95.68523  ? 122 TYR   B CZ    1 
ATOM   5760 O  OH    . TYR   B  2 130 ? 43.24300 -97.92200  -29.63900 1.000 94.53158  ? 122 TYR   B OH    1 
ATOM   5761 N  N     . GLU   B  2 131 ? 39.06500 -94.38800  -36.63400 1.000 85.54802  ? 123 GLU   B N     1 
ATOM   5762 C  CA    . GLU   B  2 131 ? 38.54500 -93.53100  -37.73700 1.000 87.14826  ? 123 GLU   B CA    1 
ATOM   5763 C  C     . GLU   B  2 131 ? 37.08800 -93.12400  -37.47100 1.000 82.99778  ? 123 GLU   B C     1 
ATOM   5764 O  O     . GLU   B  2 131 ? 36.69200 -92.04900  -37.96400 1.000 83.17747  ? 123 GLU   B O     1 
ATOM   5765 C  CB    . GLU   B  2 131 ? 38.69800 -94.24700  -39.08000 1.000 86.46930  ? 123 GLU   B CB    1 
ATOM   5766 C  CG    . GLU   B  2 131 ? 40.10200 -94.14900  -39.65000 1.000 89.55325  ? 123 GLU   B CG    1 
ATOM   5767 C  CD    . GLU   B  2 131 ? 40.47100 -92.77000  -40.17000 1.000 92.58671  ? 123 GLU   B CD    1 
ATOM   5768 O  OE1   . GLU   B  2 131 ? 39.79700 -92.29300  -41.10400 1.000 94.46702  ? 123 GLU   B OE1   1 
ATOM   5769 O  OE2   . GLU   B  2 131 ? 41.41900 -92.16900  -39.62800 1.000 99.14405  ? 123 GLU   B OE2   1 
ATOM   5770 N  N     . HIS   B  2 132 ? 36.32100 -93.94200  -36.74000 1.000 83.02331  ? 124 HIS   B N     1 
ATOM   5771 C  CA    . HIS   B  2 132 ? 34.92300 -93.64100  -36.32100 1.000 80.45140  ? 124 HIS   B CA    1 
ATOM   5772 C  C     . HIS   B  2 132 ? 34.93000 -92.76900  -35.05600 1.000 80.88860  ? 124 HIS   B C     1 
ATOM   5773 O  O     . HIS   B  2 132 ? 35.92300 -92.81800  -34.30300 1.000 79.40056  ? 124 HIS   B O     1 
ATOM   5774 C  CB    . HIS   B  2 132 ? 34.11600 -94.93300  -36.12200 1.000 76.53417  ? 124 HIS   B CB    1 
ATOM   5775 C  CG    . HIS   B  2 132 ? 33.61500 -95.53600  -37.39100 1.000 79.27843  ? 124 HIS   B CG    1 
ATOM   5776 N  ND1   . HIS   B  2 132 ? 32.73000 -94.87500  -38.22000 1.000 77.37479  ? 124 HIS   B ND1   1 
ATOM   5777 C  CD2   . HIS   B  2 132 ? 33.84800 -96.73600  -37.96300 1.000 80.48714  ? 124 HIS   B CD2   1 
ATOM   5778 C  CE1   . HIS   B  2 132 ? 32.44700 -95.64000  -39.25300 1.000 78.06297  ? 124 HIS   B CE1   1 
ATOM   5779 N  NE2   . HIS   B  2 132 ? 33.12000 -96.78700  -39.11900 1.000 78.85620  ? 124 HIS   B NE2   1 
ATOM   5780 N  N     . ASP   B  2 133 ? 33.85000 -92.01100  -34.83900 1.000 76.50702  ? 125 ASP   B N     1 
ATOM   5781 C  CA    . ASP   B  2 133 ? 33.69900 -91.04000  -33.72200 1.000 76.19032  ? 125 ASP   B CA    1 
ATOM   5782 C  C     . ASP   B  2 133 ? 32.79000 -91.61800  -32.63100 1.000 74.01983  ? 125 ASP   B C     1 
ATOM   5783 O  O     . ASP   B  2 133 ? 32.51900 -90.89600  -31.65100 1.000 73.57563  ? 125 ASP   B O     1 
ATOM   5784 C  CB    . ASP   B  2 133 ? 33.16500 -89.70200  -34.24000 1.000 76.27287  ? 125 ASP   B CB    1 
ATOM   5785 C  CG    . ASP   B  2 133 ? 34.22300 -88.87000  -34.93900 1.000 78.92118  ? 125 ASP   B CG    1 
ATOM   5786 O  OD1   . ASP   B  2 133 ? 35.27600 -89.43800  -35.28500 1.000 80.55802  ? 125 ASP   B OD1   1 
ATOM   5787 O  OD2   . ASP   B  2 133 ? 33.99100 -87.65800  -35.11300 1.000 84.61831  ? 125 ASP   B OD2   1 
ATOM   5788 N  N     . ASP   B  2 134 ? 32.34200 -92.86600  -32.78600 1.000 72.90083  ? 126 ASP   B N     1 
ATOM   5789 C  CA    . ASP   B  2 134 ? 31.47800 -93.56300  -31.79700 1.000 71.17904  ? 126 ASP   B CA    1 
ATOM   5790 C  C     . ASP   B  2 134 ? 31.66300 -95.07500  -31.96700 1.000 75.61800  ? 126 ASP   B C     1 
ATOM   5791 O  O     . ASP   B  2 134 ? 32.42200 -95.47500  -32.86900 1.000 80.89650  ? 126 ASP   B O     1 
ATOM   5792 C  CB    . ASP   B  2 134 ? 30.01700 -93.13100  -31.95800 1.000 70.39741  ? 126 ASP   B CB    1 
ATOM   5793 C  CG    . ASP   B  2 134 ? 29.16700 -93.26700  -30.70400 1.000 70.64403  ? 126 ASP   B CG    1 
ATOM   5794 O  OD1   . ASP   B  2 134 ? 29.63200 -93.91000  -29.74000 1.000 67.88120  ? 126 ASP   B OD1   1 
ATOM   5795 O  OD2   . ASP   B  2 134 ? 28.04100 -92.73000  -30.70400 1.000 70.05361  ? 126 ASP   B OD2   1 
ATOM   5796 N  N     . ILE   B  2 135 ? 30.99700 -95.87100  -31.12600 1.000 77.60530  ? 127 ILE   B N     1 
ATOM   5797 C  CA    . ILE   B  2 135 ? 31.00200 -97.36400  -31.16600 1.000 72.69348  ? 127 ILE   B CA    1 
ATOM   5798 C  C     . ILE   B  2 135 ? 30.83900 -97.81700  -32.62100 1.000 77.69314  ? 127 ILE   B C     1 
ATOM   5799 O  O     . ILE   B  2 135 ? 29.86600 -97.37900  -33.26900 1.000 72.79989  ? 127 ILE   B O     1 
ATOM   5800 C  CB    . ILE   B  2 135 ? 29.89000 -97.94600  -30.26500 1.000 71.79273  ? 127 ILE   B CB    1 
ATOM   5801 C  CG1   . ILE   B  2 135 ? 30.15100 -97.67700  -28.77800 1.000 70.84246  ? 127 ILE   B CG1   1 
ATOM   5802 C  CG2   . ILE   B  2 135 ? 29.68900 -99.43100  -30.53600 1.000 68.07168  ? 127 ILE   B CG2   1 
ATOM   5803 C  CD1   . ILE   B  2 135 ? 28.94600 -97.89300  -27.88800 1.000 66.79760  ? 127 ILE   B CD1   1 
ATOM   5804 N  N     . VAL   B  2 136 ? 31.76000 -98.65400  -33.10800 1.000 79.80649  ? 128 VAL   B N     1 
ATOM   5805 C  CA    . VAL   B  2 136 ? 31.59200 -99.42300  -34.37700 1.000 76.88924  ? 128 VAL   B CA    1 
ATOM   5806 C  C     . VAL   B  2 136 ? 30.70500 -100.62200 -34.02800 1.000 75.83507  ? 128 VAL   B C     1 
ATOM   5807 O  O     . VAL   B  2 136 ? 31.11200 -101.40700 -33.15500 1.000 76.55621  ? 128 VAL   B O     1 
ATOM   5808 C  CB    . VAL   B  2 136 ? 32.93300 -99.86100  -35.00000 1.000 73.94209  ? 128 VAL   B CB    1 
ATOM   5809 C  CG1   . VAL   B  2 136 ? 32.74600 -100.33100 -36.43400 1.000 74.09942  ? 128 VAL   B CG1   1 
ATOM   5810 C  CG2   . VAL   B  2 136 ? 33.99000 -98.76600  -34.94600 1.000 75.46219  ? 128 VAL   B CG2   1 
ATOM   5811 N  N     . SER   B  2 137 ? 29.52600 -100.72200 -34.64700 1.000 73.06269  ? 129 SER   B N     1 
ATOM   5812 C  CA    . SER   B  2 137 ? 28.44000 -101.66200 -34.26000 1.000 74.68719  ? 129 SER   B CA    1 
ATOM   5813 C  C     . SER   B  2 137 ? 28.32700 -102.83300 -35.24600 1.000 79.98284  ? 129 SER   B C     1 
ATOM   5814 O  O     . SER   B  2 137 ? 27.80700 -103.88500 -34.82300 1.000 82.92893  ? 129 SER   B O     1 
ATOM   5815 C  CB    . SER   B  2 137 ? 27.13100 -100.93300 -34.13300 1.000 71.01049  ? 129 SER   B CB    1 
ATOM   5816 O  OG    . SER   B  2 137 ? 26.82900 -100.23300 -35.32900 1.000 82.69649  ? 129 SER   B OG    1 
ATOM   5817 N  N     . THR   B  2 138 ? 28.77300 -102.67100 -36.49900 1.000 76.13710  ? 130 THR   B N     1 
ATOM   5818 C  CA    . THR   B  2 138 ? 28.64400 -103.70400 -37.56500 1.000 84.63104  ? 130 THR   B CA    1 
ATOM   5819 C  C     . THR   B  2 138 ? 29.85200 -103.66900 -38.51400 1.000 81.46345  ? 130 THR   B C     1 
ATOM   5820 O  O     . THR   B  2 138 ? 30.35200 -102.56300 -38.80300 1.000 81.10529  ? 130 THR   B O     1 
ATOM   5821 C  CB    . THR   B  2 138 ? 27.32000 -103.54500 -38.32600 1.000 80.05933  ? 130 THR   B CB    1 
ATOM   5822 O  OG1   . THR   B  2 138 ? 27.29100 -104.50000 -39.38700 1.000 79.73417  ? 130 THR   B OG1   1 
ATOM   5823 C  CG2   . THR   B  2 138 ? 27.11900 -102.15400 -38.88500 1.000 79.82942  ? 130 THR   B CG2   1 
ATOM   5824 N  N     . VAL   B  2 139 ? 30.29100 -104.85100 -38.96400 1.000 80.68150  ? 131 VAL   B N     1 
ATOM   5825 C  CA    . VAL   B  2 139 ? 31.33800 -105.05400 -40.01100 1.000 81.67355  ? 131 VAL   B CA    1 
ATOM   5826 C  C     . VAL   B  2 139 ? 30.89800 -106.20100 -40.92300 1.000 79.64192  ? 131 VAL   B C     1 
ATOM   5827 O  O     . VAL   B  2 139 ? 30.15900 -107.09200 -40.45600 1.000 79.19449  ? 131 VAL   B O     1 
ATOM   5828 C  CB    . VAL   B  2 139 ? 32.73200 -105.34400 -39.41900 1.000 84.04435  ? 131 VAL   B CB    1 
ATOM   5829 C  CG1   . VAL   B  2 139 ? 33.45200 -104.06700 -39.01500 1.000 86.14876  ? 131 VAL   B CG1   1 
ATOM   5830 C  CG2   . VAL   B  2 139 ? 32.67400 -106.32900 -38.26000 1.000 87.72206  ? 131 VAL   B CG2   1 
ATOM   5831 N  N     . SER   B  2 140 ? 31.35800 -106.16900 -42.17400 1.000 81.36602  ? 132 SER   B N     1 
ATOM   5832 C  CA    . SER   B  2 140 ? 31.12100 -107.20900 -43.20600 1.000 82.86795  ? 132 SER   B CA    1 
ATOM   5833 C  C     . SER   B  2 140 ? 32.23000 -107.11700 -44.25800 1.000 81.56028  ? 132 SER   B C     1 
ATOM   5834 O  O     . SER   B  2 140 ? 32.45600 -106.00200 -44.77100 1.000 81.08122  ? 132 SER   B O     1 
ATOM   5835 C  CB    . SER   B  2 140 ? 29.75300 -107.05100 -43.81300 1.000 77.47179  ? 132 SER   B CB    1 
ATOM   5836 O  OG    . SER   B  2 140 ? 29.42700 -108.16600 -44.62900 1.000 84.01115  ? 132 SER   B OG    1 
ATOM   5837 N  N     . VAL   B  2 141 ? 32.91800 -108.23100 -44.52700 1.000 82.25777  ? 133 VAL   B N     1 
ATOM   5838 C  CA    . VAL   B  2 141 ? 33.99800 -108.31800 -45.55400 1.000 84.63436  ? 133 VAL   B CA    1 
ATOM   5839 C  C     . VAL   B  2 141 ? 33.33100 -108.46000 -46.92800 1.000 85.33412  ? 133 VAL   B C     1 
ATOM   5840 O  O     . VAL   B  2 141 ? 32.35600 -109.23300 -47.02800 1.000 84.65736  ? 133 VAL   B O     1 
ATOM   5841 C  CB    . VAL   B  2 141 ? 34.98800 -109.46300 -45.25300 1.000 86.12982  ? 133 VAL   B CB    1 
ATOM   5842 C  CG1   . VAL   B  2 141 ? 34.39500 -110.84500 -45.50100 1.000 88.34583  ? 133 VAL   B CG1   1 
ATOM   5843 C  CG2   . VAL   B  2 141 ? 36.28600 -109.29300 -46.02600 1.000 88.54243  ? 133 VAL   B CG2   1 
ATOM   5844 N  N     . LEU   B  2 142 ? 33.82000 -107.71800 -47.92800 1.000 86.80140  ? 134 LEU   B N     1 
ATOM   5845 C  CA    . LEU   B  2 142 ? 33.29800 -107.73300 -49.32300 1.000 87.92225  ? 134 LEU   B CA    1 
ATOM   5846 C  C     . LEU   B  2 142 ? 33.78400 -109.00400 -50.03500 1.000 89.90124  ? 134 LEU   B C     1 
ATOM   5847 O  O     . LEU   B  2 142 ? 34.77300 -109.60900 -49.56600 1.000 90.73825  ? 134 LEU   B O     1 
ATOM   5848 C  CB    . LEU   B  2 142 ? 33.74700 -106.46100 -50.05200 1.000 89.08355  ? 134 LEU   B CB    1 
ATOM   5849 C  CG    . LEU   B  2 142 ? 33.21800 -105.14800 -49.47000 1.000 89.13724  ? 134 LEU   B CG    1 
ATOM   5850 C  CD1   . LEU   B  2 142 ? 33.89300 -103.94900 -50.11900 1.000 88.99059  ? 134 LEU   B CD1   1 
ATOM   5851 C  CD2   . LEU   B  2 142 ? 31.70800 -105.04500 -49.62400 1.000 85.79756  ? 134 LEU   B CD2   1 
ATOM   5852 N  N     . SER   B  2 143 ? 33.10500 -109.38000 -51.12500 1.000 90.76328  ? 135 SER   B N     1 
ATOM   5853 C  CA    . SER   B  2 143 ? 33.25900 -110.66600 -51.86200 1.000 92.56260  ? 135 SER   B CA    1 
ATOM   5854 C  C     . SER   B  2 143 ? 34.73500 -110.97500 -52.15100 1.000 94.82164  ? 135 SER   B C     1 
ATOM   5855 O  O     . SER   B  2 143 ? 35.09700 -112.16800 -52.11900 1.000 95.81255  ? 135 SER   B O     1 
ATOM   5856 C  CB    . SER   B  2 143 ? 32.44500 -110.65800 -53.13000 1.000 93.57690  ? 135 SER   B CB    1 
ATOM   5857 O  OG    . SER   B  2 143 ? 32.74900 -109.52000 -53.92100 1.000 94.66978  ? 135 SER   B OG    1 
ATOM   5858 N  N     . SER   B  2 144 ? 35.54700 -109.94900 -52.43200 1.000 95.77836  ? 136 SER   B N     1 
ATOM   5859 C  CA    . SER   B  2 144 ? 37.01000 -110.05900 -52.68200 1.000 98.07107  ? 136 SER   B CA    1 
ATOM   5860 C  C     . SER   B  2 144 ? 37.71500 -110.67100 -51.46500 1.000 97.53494  ? 136 SER   B C     1 
ATOM   5861 O  O     . SER   B  2 144 ? 38.47000 -111.64500 -51.65500 1.000 99.26845  ? 136 SER   B O     1 
ATOM   5862 C  CB    . SER   B  2 144 ? 37.60900 -108.71900 -53.03500 1.000 98.98594  ? 136 SER   B CB    1 
ATOM   5863 O  OG    . SER   B  2 144 ? 37.25300 -107.73100 -52.07800 1.000 96.82608  ? 136 SER   B OG    1 
ATOM   5864 N  N     . GLY   B  2 145 ? 37.46800 -110.11600 -50.27100 1.000 95.38216  ? 137 GLY   B N     1 
ATOM   5865 C  CA    . GLY   B  2 145 ? 38.18500 -110.45100 -49.02400 1.000 94.98874  ? 137 GLY   B CA    1 
ATOM   5866 C  C     . GLY   B  2 145 ? 39.38300 -109.54000 -48.80100 1.000 96.12562  ? 137 GLY   B C     1 
ATOM   5867 O  O     . GLY   B  2 145 ? 40.12900 -109.77900 -47.83100 1.000 96.27086  ? 137 GLY   B O     1 
ATOM   5868 N  N     . THR   B  2 146 ? 39.56600 -108.54400 -49.67900 1.000 97.14584  ? 138 THR   B N     1 
ATOM   5869 C  CA    . THR   B  2 146 ? 40.66300 -107.53600 -49.65100 1.000 98.59450  ? 138 THR   B CA    1 
ATOM   5870 C  C     . THR   B  2 146 ? 40.12400 -106.18200 -49.17200 1.000 96.90868  ? 138 THR   B C     1 
ATOM   5871 O  O     . THR   B  2 146 ? 40.94800 -105.26800 -48.96200 1.000 97.91494  ? 138 THR   B O     1 
ATOM   5872 C  CB    . THR   B  2 146 ? 41.29400 -107.36300 -51.03900 1.000 101.39621 ? 138 THR   B CB    1 
ATOM   5873 O  OG1   . THR   B  2 146 ? 40.34600 -106.68000 -51.86100 1.000 100.92642 ? 138 THR   B OG1   1 
ATOM   5874 C  CG2   . THR   B  2 146 ? 41.68900 -108.67300 -51.68700 1.000 103.16793 ? 138 THR   B CG2   1 
ATOM   5875 N  N     . GLN   B  2 147 ? 38.79800 -106.05700 -49.04200 1.000 96.46038  ? 139 GLN   B N     1 
ATOM   5876 C  CA    . GLN   B  2 147 ? 38.09100 -104.82800 -48.59100 1.000 92.86625  ? 139 GLN   B CA    1 
ATOM   5877 C  C     . GLN   B  2 147 ? 36.95100 -105.21600 -47.64100 1.000 90.14768  ? 139 GLN   B C     1 
ATOM   5878 O  O     . GLN   B  2 147 ? 36.43900 -106.34700 -47.75400 1.000 89.66165  ? 139 GLN   B O     1 
ATOM   5879 C  CB    . GLN   B  2 147 ? 37.54000 -104.05700 -49.79200 1.000 93.56693  ? 139 GLN   B CB    1 
ATOM   5880 C  CG    . GLN   B  2 147 ? 38.61100 -103.48700 -50.71100 1.000 98.43721  ? 139 GLN   B CG    1 
ATOM   5881 C  CD    . GLN   B  2 147 ? 38.03100 -102.74300 -51.89000 1.000 97.39388  ? 139 GLN   B CD    1 
ATOM   5882 O  OE1   . GLN   B  2 147 ? 36.82500 -102.75700 -52.13200 1.000 95.98836  ? 139 GLN   B OE1   1 
ATOM   5883 N  NE2   . GLN   B  2 147 ? 38.89600 -102.08300 -52.64100 1.000 99.99096  ? 139 GLN   B NE2   1 
ATOM   5884 N  N     . ALA   B  2 148 ? 36.57200 -104.30100 -46.74600 1.000 91.81711  ? 140 ALA   B N     1 
ATOM   5885 C  CA    . ALA   B  2 148 ? 35.45100 -104.45700 -45.78900 1.000 88.23026  ? 140 ALA   B CA    1 
ATOM   5886 C  C     . ALA   B  2 148 ? 34.75100 -103.10900 -45.58900 1.000 84.87384  ? 140 ALA   B C     1 
ATOM   5887 O  O     . ALA   B  2 148 ? 35.38400 -102.06500 -45.85300 1.000 86.77530  ? 140 ALA   B O     1 
ATOM   5888 C  CB    . ALA   B  2 148 ? 35.96200 -105.01400 -44.48300 1.000 85.19471  ? 140 ALA   B CB    1 
ATOM   5889 N  N     . VAL   B  2 149 ? 33.49100 -103.14400 -45.14400 1.000 82.18538  ? 141 VAL   B N     1 
ATOM   5890 C  CA    . VAL   B  2 149 ? 32.66500 -101.93900 -44.83200 1.000 82.29969  ? 141 VAL   B CA    1 
ATOM   5891 C  C     . VAL   B  2 149 ? 32.19000 -102.04100 -43.37700 1.000 80.14088  ? 141 VAL   B C     1 
ATOM   5892 O  O     . VAL   B  2 149 ? 31.81500 -103.15300 -42.95100 1.000 82.88214  ? 141 VAL   B O     1 
ATOM   5893 C  CB    . VAL   B  2 149 ? 31.49000 -101.77800 -45.82000 1.000 82.40935  ? 141 VAL   B CB    1 
ATOM   5894 C  CG1   . VAL   B  2 149 ? 30.50700 -102.93900 -45.76000 1.000 83.40149  ? 141 VAL   B CG1   1 
ATOM   5895 C  CG2   . VAL   B  2 149 ? 30.76100 -100.45800 -45.61800 1.000 81.69939  ? 141 VAL   B CG2   1 
ATOM   5896 N  N     . SER   B  2 150 ? 32.22100 -100.92100 -42.64800 1.000 83.45902  ? 142 SER   B N     1 
ATOM   5897 C  CA    . SER   B  2 150 ? 31.84100 -100.81400 -41.21400 1.000 79.41718  ? 142 SER   B CA    1 
ATOM   5898 C  C     . SER   B  2 150 ? 30.67000 -99.84000  -41.05900 1.000 77.04835  ? 142 SER   B C     1 
ATOM   5899 O  O     . SER   B  2 150 ? 30.52000 -98.95500  -41.92300 1.000 76.20989  ? 142 SER   B O     1 
ATOM   5900 C  CB    . SER   B  2 150 ? 33.01500 -100.38200 -40.38300 1.000 76.97367  ? 142 SER   B CB    1 
ATOM   5901 O  OG    . SER   B  2 150 ? 33.42900 -99.07500  -40.74800 1.000 77.89293  ? 142 SER   B OG    1 
ATOM   5902 N  N     . GLY   B  2 151 ? 29.88300 -100.00800 -39.99300 1.000 77.98383  ? 143 GLY   B N     1 
ATOM   5903 C  CA    . GLY   B  2 151 ? 28.75000 -99.13400  -39.62900 1.000 77.10284  ? 143 GLY   B CA    1 
ATOM   5904 C  C     . GLY   B  2 151 ? 28.79300 -98.76000  -38.15700 1.000 79.86728  ? 143 GLY   B C     1 
ATOM   5905 O  O     . GLY   B  2 151 ? 28.64600 -99.66900  -37.31500 1.000 82.35883  ? 143 GLY   B O     1 
ATOM   5906 N  N     . SER   B  2 152 ? 28.98700 -97.47200  -37.85500 1.000 74.58580  ? 144 SER   B N     1 
ATOM   5907 C  CA    . SER   B  2 152 ? 29.16900 -96.93700  -36.47900 1.000 77.65204  ? 144 SER   B CA    1 
ATOM   5908 C  C     . SER   B  2 152 ? 27.92400 -96.16500  -36.02700 1.000 73.30029  ? 144 SER   B C     1 
ATOM   5909 O  O     . SER   B  2 152 ? 27.12400 -95.75800  -36.89300 1.000 72.81714  ? 144 SER   B O     1 
ATOM   5910 C  CB    . SER   B  2 152 ? 30.40600 -96.08000  -36.40200 1.000 76.01759  ? 144 SER   B CB    1 
ATOM   5911 O  OG    . SER   B  2 152 ? 30.47000 -95.38200  -35.16700 1.000 77.53038  ? 144 SER   B OG    1 
ATOM   5912 N  N     . LYS   B  2 153 ? 27.78800 -95.96900  -34.71000 1.000 75.46588  ? 145 LYS   B N     1 
ATOM   5913 C  CA    . LYS   B  2 153 ? 26.69700 -95.18400  -34.06800 1.000 73.63627  ? 145 LYS   B CA    1 
ATOM   5914 C  C     . LYS   B  2 153 ? 26.87000 -93.69300  -34.39100 1.000 72.75411  ? 145 LYS   B C     1 
ATOM   5915 O  O     . LYS   B  2 153 ? 25.90100 -92.93600  -34.18800 1.000 72.00228  ? 145 LYS   B O     1 
ATOM   5916 C  CB    . LYS   B  2 153 ? 26.67600 -95.41800  -32.55300 1.000 71.08986  ? 145 LYS   B CB    1 
ATOM   5917 C  CG    . LYS   B  2 153 ? 26.03800 -96.72800  -32.11000 1.000 75.32649  ? 145 LYS   B CG    1 
ATOM   5918 C  CD    . LYS   B  2 153 ? 26.01600 -96.91800  -30.60600 1.000 67.81497  ? 145 LYS   B CD    1 
ATOM   5919 C  CE    . LYS   B  2 153 ? 25.42100 -98.24500  -30.18500 1.000 67.54211  ? 145 LYS   B CE    1 
ATOM   5920 N  NZ    . LYS   B  2 153 ? 23.94000 -98.20900  -30.20500 1.000 66.57524  ? 145 LYS   B NZ    1 
ATOM   5921 N  N     . ASP   B  2 154 ? 28.05200 -93.29500  -34.88000 1.000 69.31246  ? 146 ASP   B N     1 
ATOM   5922 C  CA    . ASP   B  2 154 ? 28.34700 -91.92200  -35.37200 1.000 68.76859  ? 146 ASP   B CA    1 
ATOM   5923 C  C     . ASP   B  2 154 ? 27.64000 -91.67700  -36.71400 1.000 69.25121  ? 146 ASP   B C     1 
ATOM   5924 O  O     . ASP   B  2 154 ? 27.85200 -90.59400  -37.28700 1.000 70.02247  ? 146 ASP   B O     1 
ATOM   5925 C  CB    . ASP   B  2 154 ? 29.85500 -91.68700  -35.49300 1.000 73.70560  ? 146 ASP   B CB    1 
ATOM   5926 C  CG    . ASP   B  2 154 ? 30.53400 -92.47400  -36.60400 1.000 77.82445  ? 146 ASP   B CG    1 
ATOM   5927 O  OD1   . ASP   B  2 154 ? 29.81700 -93.04100  -37.45200 1.000 75.55271  ? 146 ASP   B OD1   1 
ATOM   5928 O  OD2   . ASP   B  2 154 ? 31.78000 -92.51200  -36.61000 1.000 81.13490  ? 146 ASP   B OD2   1 
ATOM   5929 N  N     . ILE   B  2 155 ? 26.88400 -92.66700  -37.21200 1.000 71.63371  ? 147 ILE   B N     1 
ATOM   5930 C  CA    . ILE   B  2 155 ? 25.91600 -92.55900  -38.35000 1.000 77.75845  ? 147 ILE   B CA    1 
ATOM   5931 C  C     . ILE   B  2 155 ? 26.64800 -92.77800  -39.68400 1.000 77.72706  ? 147 ILE   B C     1 
ATOM   5932 O  O     . ILE   B  2 155 ? 25.95600 -92.94700  -40.70600 1.000 76.25830  ? 147 ILE   B O     1 
ATOM   5933 C  CB    . ILE   B  2 155 ? 25.14000 -91.22100  -38.30600 1.000 72.62725  ? 147 ILE   B CB    1 
ATOM   5934 C  CG1   . ILE   B  2 155 ? 24.44900 -91.01800  -36.95200 1.000 65.57157  ? 147 ILE   B CG1   1 
ATOM   5935 C  CG2   . ILE   B  2 155 ? 24.15200 -91.11800  -39.46300 1.000 67.40975  ? 147 ILE   B CG2   1 
ATOM   5936 C  CD1   . ILE   B  2 155 ? 23.80700 -89.66100  -36.76800 1.000 65.33433  ? 147 ILE   B CD1   1 
ATOM   5937 N  N     . CYS   B  2 156 ? 27.98500 -92.82700  -39.68000 1.000 73.89162  ? 148 CYS   B N     1 
ATOM   5938 C  CA    . CYS   B  2 156 ? 28.82600 -92.95400  -40.90200 1.000 73.38071  ? 148 CYS   B CA    1 
ATOM   5939 C  C     . CYS   B  2 156 ? 29.01200 -94.43100  -41.27100 1.000 76.45111  ? 148 CYS   B C     1 
ATOM   5940 O  O     . CYS   B  2 156 ? 29.07400 -95.27400  -40.35400 1.000 75.12894  ? 148 CYS   B O     1 
ATOM   5941 C  CB    . CYS   B  2 156 ? 30.18200 -92.28400  -40.71200 1.000 75.25491  ? 148 CYS   B CB    1 
ATOM   5942 S  SG    . CYS   B  2 156 ? 30.08400 -90.47400  -40.70000 1.000 81.72799  ? 148 CYS   B SG    1 
ATOM   5943 N  N     . ILE   B  2 157 ? 29.06600 -94.71500  -42.57600 1.000 79.62124  ? 149 ILE   B N     1 
ATOM   5944 C  CA    . ILE   B  2 157 ? 29.52500 -96.00600  -43.16800 1.000 75.57816  ? 149 ILE   B CA    1 
ATOM   5945 C  C     . ILE   B  2 157 ? 30.83800 -95.72100  -43.90800 1.000 78.14094  ? 149 ILE   B C     1 
ATOM   5946 O  O     . ILE   B  2 157 ? 30.86900 -94.75300  -44.69000 1.000 79.44640  ? 149 ILE   B O     1 
ATOM   5947 C  CB    . ILE   B  2 157 ? 28.44400 -96.61200  -44.08800 1.000 75.19489  ? 149 ILE   B CB    1 
ATOM   5948 C  CG1   . ILE   B  2 157 ? 27.18300 -96.97600  -43.29800 1.000 72.82994  ? 149 ILE   B CG1   1 
ATOM   5949 C  CG2   . ILE   B  2 157 ? 28.99000 -97.80500  -44.86100 1.000 76.49816  ? 149 ILE   B CG2   1 
ATOM   5950 C  CD1   . ILE   B  2 157 ? 26.04800 -97.53100  -44.13200 1.000 72.53947  ? 149 ILE   B CD1   1 
ATOM   5951 N  N     . LYS   B  2 158 ? 31.88000 -96.51500  -43.64300 1.000 78.98415  ? 150 LYS   B N     1 
ATOM   5952 C  CA    . LYS   B  2 158 ? 33.23500 -96.35600  -44.23700 1.000 81.56514  ? 150 LYS   B CA    1 
ATOM   5953 C  C     . LYS   B  2 158 ? 33.65000 -97.66400  -44.92000 1.000 84.05107  ? 150 LYS   B C     1 
ATOM   5954 O  O     . LYS   B  2 158 ? 33.34300 -98.73700  -44.36700 1.000 82.69475  ? 150 LYS   B O     1 
ATOM   5955 C  CB    . LYS   B  2 158 ? 34.25500 -95.98000  -43.15800 1.000 82.00846  ? 150 LYS   B CB    1 
ATOM   5956 C  CG    . LYS   B  2 158 ? 34.10000 -94.58900  -42.55500 1.000 81.67429  ? 150 LYS   B CG    1 
ATOM   5957 C  CD    . LYS   B  2 158 ? 35.35900 -94.10900  -41.85500 1.000 83.15108  ? 150 LYS   B CD    1 
ATOM   5958 C  CE    . LYS   B  2 158 ? 35.09300 -93.31700  -40.59300 1.000 81.92215  ? 150 LYS   B CE    1 
ATOM   5959 N  NZ    . LYS   B  2 158 ? 34.76700 -91.90100  -40.88600 1.000 85.68578  ? 150 LYS   B NZ    1 
ATOM   5960 N  N     . VAL   B  2 159 ? 34.32700 -97.56300  -46.07100 1.000 89.25792  ? 151 VAL   B N     1 
ATOM   5961 C  CA    . VAL   B  2 159 ? 34.89100 -98.71200  -46.84300 1.000 90.02046  ? 151 VAL   B CA    1 
ATOM   5962 C  C     . VAL   B  2 159 ? 36.39800 -98.78500  -46.56900 1.000 92.31754  ? 151 VAL   B C     1 
ATOM   5963 O  O     . VAL   B  2 159 ? 37.06700 -97.73300  -46.65500 1.000 93.32242  ? 151 VAL   B O     1 
ATOM   5964 C  CB    . VAL   B  2 159 ? 34.59400 -98.58400  -48.35100 1.000 87.99899  ? 151 VAL   B CB    1 
ATOM   5965 C  CG1   . VAL   B  2 159 ? 35.32200 -99.64400  -49.16600 1.000 89.91495  ? 151 VAL   B CG1   1 
ATOM   5966 C  CG2   . VAL   B  2 159 ? 33.10100 -98.63000  -48.63600 1.000 86.33726  ? 151 VAL   B CG2   1 
ATOM   5967 N  N     . TRP   B  2 160 ? 36.90200 -99.98800  -46.27600 1.000 88.46383  ? 152 TRP   B N     1 
ATOM   5968 C  CA    . TRP   B  2 160 ? 38.29700 -100.24700 -45.83000 1.000 90.12723  ? 152 TRP   B CA    1 
ATOM   5969 C  C     . TRP   B  2 160 ? 39.08800 -100.96800 -46.92300 1.000 97.03518  ? 152 TRP   B C     1 
ATOM   5970 O  O     . TRP   B  2 160 ? 38.48300 -101.76300 -47.66700 1.000 98.97534  ? 152 TRP   B O     1 
ATOM   5971 C  CB    . TRP   B  2 160 ? 38.29300 -101.06600 -44.53600 1.000 89.66599  ? 152 TRP   B CB    1 
ATOM   5972 C  CG    . TRP   B  2 160 ? 37.70700 -100.33700 -43.37100 1.000 86.91011  ? 152 TRP   B CG    1 
ATOM   5973 C  CD1   . TRP   B  2 160 ? 36.39600 -100.30600 -42.99600 1.000 84.50592  ? 152 TRP   B CD1   1 
ATOM   5974 C  CD2   . TRP   B  2 160 ? 38.41700 -99.51800  -42.42700 1.000 89.25553  ? 152 TRP   B CD2   1 
ATOM   5975 N  NE1   . TRP   B  2 160 ? 36.24200 -99.52700  -41.88100 1.000 89.47906  ? 152 TRP   B NE1   1 
ATOM   5976 C  CE2   . TRP   B  2 160 ? 37.46300 -99.03000  -41.50800 1.000 91.62693  ? 152 TRP   B CE2   1 
ATOM   5977 C  CE3   . TRP   B  2 160 ? 39.75900 -99.15300  -42.26500 1.000 90.29008  ? 152 TRP   B CE3   1 
ATOM   5978 C  CZ2   . TRP   B  2 160 ? 37.81300 -98.19700  -40.44500 1.000 88.56433  ? 152 TRP   B CZ2   1 
ATOM   5979 C  CZ3   . TRP   B  2 160 ? 40.10300 -98.32900  -41.21500 1.000 91.65801  ? 152 TRP   B CZ3   1 
ATOM   5980 C  CH2   . TRP   B  2 160 ? 39.14200 -97.86000  -40.31800 1.000 87.97555  ? 152 TRP   B CH2   1 
ATOM   5981 N  N     . ASP   B  2 161 ? 40.39200 -100.68600 -46.99600 1.000 102.29626 ? 153 ASP   B N     1 
ATOM   5982 C  CA    . ASP   B  2 161 ? 41.40400 -101.47600 -47.74600 1.000 98.75882  ? 153 ASP   B CA    1 
ATOM   5983 C  C     . ASP   B  2 161 ? 42.23200 -102.24400 -46.70900 1.000 103.72506 ? 153 ASP   B C     1 
ATOM   5984 O  O     . ASP   B  2 161 ? 43.08600 -101.61400 -46.05300 1.000 101.95457 ? 153 ASP   B O     1 
ATOM   5985 C  CB    . ASP   B  2 161 ? 42.25800 -100.57000 -48.64000 1.000 103.42278 ? 153 ASP   B CB    1 
ATOM   5986 C  CG    . ASP   B  2 161 ? 43.10200 -101.30800 -49.66800 1.000 115.45294 ? 153 ASP   B CG    1 
ATOM   5987 O  OD1   . ASP   B  2 161 ? 43.34300 -102.51900 -49.48100 1.000 113.29409 ? 153 ASP   B OD1   1 
ATOM   5988 O  OD2   . ASP   B  2 161 ? 43.51200 -100.66200 -50.65400 1.000 120.02139 ? 153 ASP   B OD2   1 
ATOM   5989 N  N     . LEU   B  2 162 ? 41.96100 -103.54400 -46.54700 1.000 104.34248 ? 154 LEU   B N     1 
ATOM   5990 C  CA    . LEU   B  2 162 ? 42.58300 -104.41100 -45.50700 1.000 99.15161  ? 154 LEU   B CA    1 
ATOM   5991 C  C     . LEU   B  2 162 ? 44.07000 -104.61000 -45.82700 1.000 106.91962 ? 154 LEU   B C     1 
ATOM   5992 O  O     . LEU   B  2 162 ? 44.85500 -104.80400 -44.87800 1.000 109.80483 ? 154 LEU   B O     1 
ATOM   5993 C  CB    . LEU   B  2 162 ? 41.84400 -105.75400 -45.44300 1.000 95.63142  ? 154 LEU   B CB    1 
ATOM   5994 C  CG    . LEU   B  2 162 ? 40.34500 -105.69200 -45.14300 1.000 96.37115  ? 154 LEU   B CG    1 
ATOM   5995 C  CD1   . LEU   B  2 162 ? 39.76000 -107.09200 -45.03700 1.000 94.25615  ? 154 LEU   B CD1   1 
ATOM   5996 C  CD2   . LEU   B  2 162 ? 40.05700 -104.90600 -43.87200 1.000 91.00131  ? 154 LEU   B CD2   1 
ATOM   5997 N  N     . ALA   B  2 163 ? 44.43600 -104.56400 -47.11200 1.000 108.15786 ? 155 ALA   B N     1 
ATOM   5998 C  CA    . ALA   B  2 163 ? 45.82800 -104.67200 -47.60700 1.000 109.73076 ? 155 ALA   B CA    1 
ATOM   5999 C  C     . ALA   B  2 163 ? 46.63700 -103.44300 -47.16900 1.000 112.21415 ? 155 ALA   B C     1 
ATOM   6000 O  O     . ALA   B  2 163 ? 47.78000 -103.62700 -46.70500 1.000 110.93450 ? 155 ALA   B O     1 
ATOM   6001 C  CB    . ALA   B  2 163 ? 45.82900 -104.82600 -49.10900 1.000 118.28277 ? 155 ALA   B CB    1 
ATOM   6002 N  N     . GLN   B  2 164 ? 46.06000 -102.24300 -47.31000 1.000 113.96353 ? 156 GLN   B N     1 
ATOM   6003 C  CA    . GLN   B  2 164 ? 46.73500 -100.93500 -47.07300 1.000 111.99339 ? 156 GLN   B CA    1 
ATOM   6004 C  C     . GLN   B  2 164 ? 46.41300 -100.39900 -45.66900 1.000 107.26761 ? 156 GLN   B C     1 
ATOM   6005 O  O     . GLN   B  2 164 ? 47.16900 -99.52800  -45.19700 1.000 106.49336 ? 156 GLN   B O     1 
ATOM   6006 C  CB    . GLN   B  2 164 ? 46.31600 -99.93000  -48.14700 1.000 108.72158 ? 156 GLN   B CB    1 
ATOM   6007 C  CG    . GLN   B  2 164 ? 46.67900 -100.36700 -49.56000 1.000 118.70039 ? 156 GLN   B CG    1 
ATOM   6008 C  CD    . GLN   B  2 164 ? 46.43800 -99.28900  -50.58900 1.000 124.08033 ? 156 GLN   B CD    1 
ATOM   6009 O  OE1   . GLN   B  2 164 ? 45.69100 -98.33700  -50.36600 1.000 115.57110 ? 156 GLN   B OE1   1 
ATOM   6010 N  NE2   . GLN   B  2 164 ? 47.07200 -99.43700  -51.74200 1.000 120.78723 ? 156 GLN   B NE2   1 
ATOM   6011 N  N     . GLN   B  2 165 ? 45.33300 -100.88300 -45.04300 1.000 103.07273 ? 157 GLN   B N     1 
ATOM   6012 C  CA    . GLN   B  2 165 ? 44.91500 -100.55400 -43.65000 1.000 106.98152 ? 157 GLN   B CA    1 
ATOM   6013 C  C     . GLN   B  2 165 ? 44.49300 -99.07900  -43.55100 1.000 109.42098 ? 157 GLN   B C     1 
ATOM   6014 O  O     . GLN   B  2 165 ? 44.69100 -98.48300  -42.47200 1.000 107.97899 ? 157 GLN   B O     1 
ATOM   6015 C  CB    . GLN   B  2 165 ? 46.04100 -100.86700 -42.65700 1.000 104.17104 ? 157 GLN   B CB    1 
ATOM   6016 C  CG    . GLN   B  2 165 ? 46.63300 -102.26200 -42.81300 1.000 106.74710 ? 157 GLN   B CG    1 
ATOM   6017 C  CD    . GLN   B  2 165 ? 47.80100 -102.50200 -41.88800 1.000 104.41467 ? 157 GLN   B CD    1 
ATOM   6018 O  OE1   . GLN   B  2 165 ? 48.21400 -101.62400 -41.13400 1.000 104.94578 ? 157 GLN   B OE1   1 
ATOM   6019 N  NE2   . GLN   B  2 165 ? 48.34600 -103.70600 -41.94200 1.000 105.55926 ? 157 GLN   B NE2   1 
ATOM   6020 N  N     . VAL   B  2 166 ? 43.91400 -98.52000  -44.62300 1.000 107.70600 ? 158 VAL   B N     1 
ATOM   6021 C  CA    . VAL   B  2 166 ? 43.38600 -97.12100  -44.67100 1.000 101.21473 ? 158 VAL   B CA    1 
ATOM   6022 C  C     . VAL   B  2 166 ? 41.91800 -97.16200  -45.11000 1.000 96.64142  ? 158 VAL   B C     1 
ATOM   6023 O  O     . VAL   B  2 166 ? 41.45600 -98.23400  -45.55300 1.000 95.84739  ? 158 VAL   B O     1 
ATOM   6024 C  CB    . VAL   B  2 166 ? 44.21600 -96.21900  -45.60700 1.000 102.16003 ? 158 VAL   B CB    1 
ATOM   6025 C  CG1   . VAL   B  2 166 ? 45.69800 -96.24700  -45.26100 1.000 104.86028 ? 158 VAL   B CG1   1 
ATOM   6026 C  CG2   . VAL   B  2 166 ? 44.00500 -96.56200  -47.07600 1.000 103.26115 ? 158 VAL   B CG2   1 
ATOM   6027 N  N     . VAL   B  2 167 ? 41.22900 -96.02100  -45.01200 1.000 95.74578  ? 159 VAL   B N     1 
ATOM   6028 C  CA    . VAL   B  2 167 ? 39.81400 -95.84200  -45.45300 1.000 94.43613  ? 159 VAL   B CA    1 
ATOM   6029 C  C     . VAL   B  2 167 ? 39.83000 -95.29000  -46.88400 1.000 96.53602  ? 159 VAL   B C     1 
ATOM   6030 O  O     . VAL   B  2 167 ? 40.53000 -94.28600  -47.11300 1.000 99.62611  ? 159 VAL   B O     1 
ATOM   6031 C  CB    . VAL   B  2 167 ? 39.03200 -94.91000  -44.50700 1.000 91.72364  ? 159 VAL   B CB    1 
ATOM   6032 C  CG1   . VAL   B  2 167 ? 37.53500 -95.01500  -44.74300 1.000 89.34842  ? 159 VAL   B CG1   1 
ATOM   6033 C  CG2   . VAL   B  2 167 ? 39.35700 -95.16400  -43.04200 1.000 90.64096  ? 159 VAL   B CG2   1 
ATOM   6034 N  N     . LEU   B  2 168 ? 39.09600 -95.92500  -47.80400 1.000 96.53809  ? 160 LEU   B N     1 
ATOM   6035 C  CA    . LEU   B  2 168 ? 38.95500 -95.47600  -49.21700 1.000 97.31309  ? 160 LEU   B CA    1 
ATOM   6036 C  C     . LEU   B  2 168 ? 37.82400 -94.44600  -49.30700 1.000 100.01678 ? 160 LEU   B C     1 
ATOM   6037 O  O     . LEU   B  2 168 ? 38.08500 -93.31900  -49.78000 1.000 98.01610  ? 160 LEU   B O     1 
ATOM   6038 C  CB    . LEU   B  2 168 ? 38.66800 -96.68400  -50.11600 1.000 97.52646  ? 160 LEU   B CB    1 
ATOM   6039 C  CG    . LEU   B  2 168 ? 39.75800 -97.75300  -50.17400 1.000 98.95918  ? 160 LEU   B CG    1 
ATOM   6040 C  CD1   . LEU   B  2 168 ? 39.32900 -98.90700  -51.06600 1.000 99.10992  ? 160 LEU   B CD1   1 
ATOM   6041 C  CD2   . LEU   B  2 168 ? 41.08000 -97.17400  -50.65900 1.000 102.26316 ? 160 LEU   B CD2   1 
ATOM   6042 N  N     . SER   B  2 169 ? 36.62300 -94.82800  -48.85800 1.000 95.16732  ? 161 SER   B N     1 
ATOM   6043 C  CA    . SER   B  2 169 ? 35.38000 -94.01300  -48.90500 1.000 93.58286  ? 161 SER   B CA    1 
ATOM   6044 C  C     . SER   B  2 169 ? 34.83400 -93.79600  -47.48800 1.000 89.14853  ? 161 SER   B C     1 
ATOM   6045 O  O     . SER   B  2 169 ? 34.99600 -94.70000  -46.64400 1.000 87.76991  ? 161 SER   B O     1 
ATOM   6046 C  CB    . SER   B  2 169 ? 34.35000 -94.66800  -49.78800 1.000 91.34165  ? 161 SER   B CB    1 
ATOM   6047 O  OG    . SER   B  2 169 ? 34.91300 -95.04100  -51.03600 1.000 93.94922  ? 161 SER   B OG    1 
ATOM   6048 N  N     . SER   B  2 170 ? 34.21500 -92.63500  -47.25100 1.000 88.69750  ? 162 SER   B N     1 
ATOM   6049 C  CA    . SER   B  2 170 ? 33.49000 -92.27300  -46.00400 1.000 87.53085  ? 162 SER   B CA    1 
ATOM   6050 C  C     . SER   B  2 170 ? 32.10300 -91.73300  -46.37200 1.000 87.66542  ? 162 SER   B C     1 
ATOM   6051 O  O     . SER   B  2 170 ? 32.03400 -90.61900  -46.92900 1.000 90.77605  ? 162 SER   B O     1 
ATOM   6052 C  CB    . SER   B  2 170 ? 34.27700 -91.27700  -45.19000 1.000 88.80533  ? 162 SER   B CB    1 
ATOM   6053 O  OG    . SER   B  2 170 ? 33.63600 -91.01700  -43.95100 1.000 85.57016  ? 162 SER   B OG    1 
ATOM   6054 N  N     . TYR   B  2 171 ? 31.04800 -92.50400  -46.08500 1.000 82.55589  ? 163 TYR   B N     1 
ATOM   6055 C  CA    . TYR   B  2 171 ? 29.64600 -92.22100  -46.49100 1.000 81.46519  ? 163 TYR   B CA    1 
ATOM   6056 C  C     . TYR   B  2 171 ? 28.79400 -91.87200  -45.26600 1.000 80.59962  ? 163 TYR   B C     1 
ATOM   6057 O  O     . TYR   B  2 171 ? 28.52900 -92.76700  -44.43600 1.000 82.30522  ? 163 TYR   B O     1 
ATOM   6058 C  CB    . TYR   B  2 171 ? 29.03700 -93.42300  -47.21500 1.000 81.11455  ? 163 TYR   B CB    1 
ATOM   6059 C  CG    . TYR   B  2 171 ? 29.76000 -93.85900  -48.46400 1.000 83.61998  ? 163 TYR   B CG    1 
ATOM   6060 C  CD1   . TYR   B  2 171 ? 30.00400 -92.96900  -49.49800 1.000 86.01827  ? 163 TYR   B CD1   1 
ATOM   6061 C  CD2   . TYR   B  2 171 ? 30.17500 -95.17100  -48.62900 1.000 83.76758  ? 163 TYR   B CD2   1 
ATOM   6062 C  CE1   . TYR   B  2 171 ? 30.65900 -93.36400  -50.65400 1.000 88.50389  ? 163 TYR   B CE1   1 
ATOM   6063 C  CE2   . TYR   B  2 171 ? 30.83000 -95.58300  -49.77900 1.000 86.16725  ? 163 TYR   B CE2   1 
ATOM   6064 C  CZ    . TYR   B  2 171 ? 31.07100 -94.67700  -50.79600 1.000 88.53935  ? 163 TYR   B CZ    1 
ATOM   6065 O  OH    . TYR   B  2 171 ? 31.71600 -95.07700  -51.93000 1.000 95.28260  ? 163 TYR   B OH    1 
ATOM   6066 N  N     . ARG   B  2 172 ? 28.37200 -90.60800  -45.16700 1.000 77.26633  ? 164 ARG   B N     1 
ATOM   6067 C  CA    . ARG   B  2 172 ? 27.33800 -90.14000  -44.20700 1.000 75.99068  ? 164 ARG   B CA    1 
ATOM   6068 C  C     . ARG   B  2 172 ? 25.99700 -90.08300  -44.94900 1.000 74.51821  ? 164 ARG   B C     1 
ATOM   6069 O  O     . ARG   B  2 172 ? 25.54500 -88.97500  -45.28500 1.000 75.12642  ? 164 ARG   B O     1 
ATOM   6070 C  CB    . ARG   B  2 172 ? 27.73900 -88.79000  -43.60400 1.000 77.68894  ? 164 ARG   B CB    1 
ATOM   6071 C  CG    . ARG   B  2 172 ? 26.82100 -88.30600  -42.49000 1.000 76.68320  ? 164 ARG   B CG    1 
ATOM   6072 C  CD    . ARG   B  2 172 ? 27.21200 -86.93100  -41.98800 1.000 81.10568  ? 164 ARG   B CD    1 
ATOM   6073 N  NE    . ARG   B  2 172 ? 28.38800 -86.97100  -41.13000 1.000 83.47723  ? 164 ARG   B NE    1 
ATOM   6074 C  CZ    . ARG   B  2 172 ? 28.38300 -87.30400  -39.84200 1.000 84.96141  ? 164 ARG   B CZ    1 
ATOM   6075 N  NH1   . ARG   B  2 172 ? 27.25600 -87.64100  -39.23600 1.000 80.98098  ? 164 ARG   B NH1   1 
ATOM   6076 N  NH2   . ARG   B  2 172 ? 29.51800 -87.30400  -39.16200 1.000 87.41832  ? 164 ARG   B NH2   1 
ATOM   6077 N  N     . ALA   B  2 173 ? 25.40200 -91.24800  -45.21100 1.000 73.01906  ? 165 ALA   B N     1 
ATOM   6078 C  CA    . ALA   B  2 173 ? 24.12200 -91.39900  -45.94000 1.000 71.94121  ? 165 ALA   B CA    1 
ATOM   6079 C  C     . ALA   B  2 173 ? 22.95400 -91.31600  -44.95200 1.000 70.65044  ? 165 ALA   B C     1 
ATOM   6080 O  O     . ALA   B  2 173 ? 21.96800 -90.62300  -45.26400 1.000 73.20863  ? 165 ALA   B O     1 
ATOM   6081 C  CB    . ALA   B  2 173 ? 24.10600 -92.70200  -46.70100 1.000 71.42433  ? 165 ALA   B CB    1 
ATOM   6082 N  N     . HIS   B  2 174 ? 23.07600 -91.99400  -43.80700 1.000 69.94504  ? 166 HIS   B N     1 
ATOM   6083 C  CA    . HIS   B  2 174 ? 22.00000 -92.16200  -42.79300 1.000 68.78457  ? 166 HIS   B CA    1 
ATOM   6084 C  C     . HIS   B  2 174 ? 21.87000 -90.91700  -41.90900 1.000 70.08250  ? 166 HIS   B C     1 
ATOM   6085 O  O     . HIS   B  2 174 ? 22.76500 -90.04800  -41.95800 1.000 71.66767  ? 166 HIS   B O     1 
ATOM   6086 C  CB    . HIS   B  2 174 ? 22.25900 -93.40700  -41.94100 1.000 68.28101  ? 166 HIS   B CB    1 
ATOM   6087 C  CG    . HIS   B  2 174 ? 22.09100 -94.68000  -42.69300 1.000 67.97675  ? 166 HIS   B CG    1 
ATOM   6088 N  ND1   . HIS   B  2 174 ? 20.84600 -95.19100  -42.99700 1.000 67.55906  ? 166 HIS   B ND1   1 
ATOM   6089 C  CD2   . HIS   B  2 174 ? 22.99700 -95.54100  -43.20300 1.000 68.47311  ? 166 HIS   B CD2   1 
ATOM   6090 C  CE1   . HIS   B  2 174 ? 20.99100 -96.32000  -43.65800 1.000 67.76450  ? 166 HIS   B CE1   1 
ATOM   6091 N  NE2   . HIS   B  2 174 ? 22.30100 -96.55600  -43.79800 1.000 68.23122  ? 166 HIS   B NE2   1 
ATOM   6092 N  N     . ALA   B  2 175 ? 20.79100 -90.86300  -41.12200 1.000 69.22730  ? 167 ALA   B N     1 
ATOM   6093 C  CA    . ALA   B  2 175 ? 20.44400 -89.76000  -40.19700 1.000 68.65726  ? 167 ALA   B CA    1 
ATOM   6094 C  C     . ALA   B  2 175 ? 20.40100 -90.26800  -38.74800 1.000 69.73125  ? 167 ALA   B C     1 
ATOM   6095 O  O     . ALA   B  2 175 ? 19.94400 -89.49900  -37.87300 1.000 68.31396  ? 167 ALA   B O     1 
ATOM   6096 C  CB    . ALA   B  2 175 ? 19.12100 -89.16300  -40.60900 1.000 68.45102  ? 167 ALA   B CB    1 
ATOM   6097 N  N     . ALA   B  2 176 ? 20.86000 -91.50100  -38.49700 1.000 67.84070  ? 168 ALA   B N     1 
ATOM   6098 C  CA    . ALA   B  2 176 ? 20.86900 -92.13700  -37.15500 1.000 71.53263  ? 168 ALA   B CA    1 
ATOM   6099 C  C     . ALA   B  2 176 ? 21.86100 -93.30700  -37.12000 1.000 75.28737  ? 168 ALA   B C     1 
ATOM   6100 O  O     . ALA   B  2 176 ? 22.48500 -93.59000  -38.16100 1.000 77.74026  ? 168 ALA   B O     1 
ATOM   6101 C  CB    . ALA   B  2 176 ? 19.47100 -92.58000  -36.79200 1.000 67.53258  ? 168 ALA   B CB    1 
ATOM   6102 N  N     . GLN   B  2 177 ? 21.99900 -93.95000  -35.95500 1.000 82.12171  ? 169 GLN   B N     1 
ATOM   6103 C  CA    . GLN   B  2 177 ? 22.95500 -95.06100  -35.69000 1.000 79.47020  ? 169 GLN   B CA    1 
ATOM   6104 C  C     . GLN   B  2 177 ? 22.86100 -96.09900  -36.81500 1.000 83.19068  ? 169 GLN   B C     1 
ATOM   6105 O  O     . GLN   B  2 177 ? 21.73700 -96.56000  -37.09800 1.000 84.26310  ? 169 GLN   B O     1 
ATOM   6106 C  CB    . GLN   B  2 177 ? 22.66700 -95.70000  -34.32800 1.000 77.88573  ? 169 GLN   B CB    1 
ATOM   6107 C  CG    . GLN   B  2 177 ? 23.08400 -94.82200  -33.15600 1.000 88.69270  ? 169 GLN   B CG    1 
ATOM   6108 C  CD    . GLN   B  2 177 ? 22.63500 -95.32900  -31.80500 1.000 89.13328  ? 169 GLN   B CD    1 
ATOM   6109 O  OE1   . GLN   B  2 177 ? 22.20200 -96.47000  -31.65200 1.000 92.22794  ? 169 GLN   B OE1   1 
ATOM   6110 N  NE2   . GLN   B  2 177 ? 22.75200 -94.47500  -30.80000 1.000 78.47804  ? 169 GLN   B NE2   1 
ATOM   6111 N  N     . VAL   B  2 178 ? 23.99900 -96.43600  -37.43300 1.000 75.47159  ? 170 VAL   B N     1 
ATOM   6112 C  CA    . VAL   B  2 178 ? 24.11100 -97.51900  -38.45700 1.000 78.15805  ? 170 VAL   B CA    1 
ATOM   6113 C  C     . VAL   B  2 178 ? 24.05100 -98.85900  -37.71300 1.000 78.60141  ? 170 VAL   B C     1 
ATOM   6114 O  O     . VAL   B  2 178 ? 25.02300 -99.18500  -37.00300 1.000 74.89416  ? 170 VAL   B O     1 
ATOM   6115 C  CB    . VAL   B  2 178 ? 25.39100 -97.39800  -39.30900 1.000 72.91021  ? 170 VAL   B CB    1 
ATOM   6116 C  CG1   . VAL   B  2 178 ? 25.44800 -98.47200  -40.38300 1.000 73.25978  ? 170 VAL   B CG1   1 
ATOM   6117 C  CG2   . VAL   B  2 178 ? 25.53900 -96.02100  -39.94000 1.000 71.08955  ? 170 VAL   B CG2   1 
ATOM   6118 N  N     . THR   B  2 179 ? 22.94300 -99.59100  -37.86900 1.000 72.80276  ? 171 THR   B N     1 
ATOM   6119 C  CA    . THR   B  2 179 ? 22.62400 -100.83200 -37.11600 1.000 70.50788  ? 171 THR   B CA    1 
ATOM   6120 C  C     . THR   B  2 179 ? 23.39100 -102.01500 -37.71700 1.000 75.53863  ? 171 THR   B C     1 
ATOM   6121 O  O     . THR   B  2 179 ? 24.17700 -102.64100 -36.98200 1.000 79.49053  ? 171 THR   B O     1 
ATOM   6122 C  CB    . THR   B  2 179 ? 21.11300 -101.09400 -37.10800 1.000 70.11150  ? 171 THR   B CB    1 
ATOM   6123 O  OG1   . THR   B  2 179 ? 20.45800 -99.90000  -36.67700 1.000 74.25895  ? 171 THR   B OG1   1 
ATOM   6124 C  CG2   . THR   B  2 179 ? 20.72400 -102.24400 -36.20600 1.000 70.97265  ? 171 THR   B CG2   1 
ATOM   6125 N  N     . CYS   B  2 180 ? 23.16000 -102.30500 -39.00100 1.000 73.50465  ? 172 CYS   B N     1 
ATOM   6126 C  CA    . CYS   B  2 180 ? 23.72000 -103.47500 -39.73000 1.000 72.85456  ? 172 CYS   B CA    1 
ATOM   6127 C  C     . CYS   B  2 180 ? 24.24800 -103.03400 -41.09900 1.000 76.31014  ? 172 CYS   B C     1 
ATOM   6128 O  O     . CYS   B  2 180 ? 23.60200 -102.17500 -41.72800 1.000 73.01134  ? 172 CYS   B O     1 
ATOM   6129 C  CB    . CYS   B  2 180 ? 22.65900 -104.55500 -39.90600 1.000 72.45670  ? 172 CYS   B CB    1 
ATOM   6130 S  SG    . CYS   B  2 180 ? 23.32200 -106.12900 -40.50900 1.000 74.13569  ? 172 CYS   B SG    1 
ATOM   6131 N  N     . VAL   B  2 181 ? 25.39200 -103.58800 -41.51800 1.000 80.20077  ? 173 VAL   B N     1 
ATOM   6132 C  CA    . VAL   B  2 181 ? 25.93700 -103.47800 -42.90500 1.000 79.45164  ? 173 VAL   B CA    1 
ATOM   6133 C  C     . VAL   B  2 181 ? 26.31500 -104.88900 -43.37500 1.000 82.53048  ? 173 VAL   B C     1 
ATOM   6134 O  O     . VAL   B  2 181 ? 27.17200 -105.52000 -42.72900 1.000 86.31322  ? 173 VAL   B O     1 
ATOM   6135 C  CB    . VAL   B  2 181 ? 27.12400 -102.49600 -42.99800 1.000 77.95707  ? 173 VAL   B CB    1 
ATOM   6136 C  CG1   . VAL   B  2 181 ? 26.73800 -101.10900 -42.50900 1.000 78.74502  ? 173 VAL   B CG1   1 
ATOM   6137 C  CG2   . VAL   B  2 181 ? 28.36800 -102.98400 -42.26800 1.000 81.53401  ? 173 VAL   B CG2   1 
ATOM   6138 N  N     . ALA   B  2 182 ? 25.67100 -105.37100 -44.44100 1.000 77.64505  ? 174 ALA   B N     1 
ATOM   6139 C  CA    . ALA   B  2 182 ? 25.88100 -106.71700 -45.02200 1.000 75.53291  ? 174 ALA   B CA    1 
ATOM   6140 C  C     . ALA   B  2 182 ? 26.46200 -106.57000 -46.43300 1.000 85.47484  ? 174 ALA   B C     1 
ATOM   6141 O  O     . ALA   B  2 182 ? 25.78800 -105.97100 -47.29500 1.000 81.83313  ? 174 ALA   B O     1 
ATOM   6142 C  CB    . ALA   B  2 182 ? 24.58100 -107.48200 -45.02800 1.000 75.51626  ? 174 ALA   B CB    1 
ATOM   6143 N  N     . ALA   B  2 183 ? 27.67400 -107.08900 -46.64400 1.000 85.38757  ? 175 ALA   B N     1 
ATOM   6144 C  CA    . ALA   B  2 183 ? 28.37500 -107.11900 -47.94700 1.000 78.28392  ? 175 ALA   B CA    1 
ATOM   6145 C  C     . ALA   B  2 183 ? 27.60600 -108.03400 -48.90300 1.000 80.70502  ? 175 ALA   B C     1 
ATOM   6146 O  O     . ALA   B  2 183 ? 27.09400 -109.06700 -48.43100 1.000 79.09569  ? 175 ALA   B O     1 
ATOM   6147 C  CB    . ALA   B  2 183 ? 29.79400 -107.59400 -47.75900 1.000 80.42598  ? 175 ALA   B CB    1 
ATOM   6148 N  N     . SER   B  2 184 ? 27.51900 -107.66000 -50.18400 1.000 80.46809  ? 176 SER   B N     1 
ATOM   6149 C  CA    . SER   B  2 184 ? 26.99200 -108.52400 -51.27200 1.000 78.85743  ? 176 SER   B CA    1 
ATOM   6150 C  C     . SER   B  2 184 ? 27.84200 -109.78700 -51.32800 1.000 80.92572  ? 176 SER   B C     1 
ATOM   6151 O  O     . SER   B  2 184 ? 29.06700 -109.70000 -51.26800 1.000 81.97341  ? 176 SER   B O     1 
ATOM   6152 C  CB    . SER   B  2 184 ? 26.97800 -107.81300 -52.60000 1.000 83.16439  ? 176 SER   B CB    1 
ATOM   6153 O  OG    . SER   B  2 184 ? 26.53100 -108.67700 -53.63600 1.000 82.87804  ? 176 SER   B OG    1 
ATOM   6154 N  N     . PRO   B  2 185 ? 27.22500 -110.99000 -51.39900 1.000 84.76445  ? 177 PRO   B N     1 
ATOM   6155 C  CA    . PRO   B  2 185 ? 27.97800 -112.24200 -51.49500 1.000 84.19252  ? 177 PRO   B CA    1 
ATOM   6156 C  C     . PRO   B  2 185 ? 29.05400 -112.26900 -52.59300 1.000 85.39999  ? 177 PRO   B C     1 
ATOM   6157 O  O     . PRO   B  2 185 ? 30.12800 -112.77500 -52.32300 1.000 87.13155  ? 177 PRO   B O     1 
ATOM   6158 C  CB    . PRO   B  2 185 ? 26.89200 -113.28200 -51.81300 1.000 84.96233  ? 177 PRO   B CB    1 
ATOM   6159 C  CG    . PRO   B  2 185 ? 25.63400 -112.71300 -51.19600 1.000 83.48845  ? 177 PRO   B CG    1 
ATOM   6160 C  CD    . PRO   B  2 185 ? 25.77100 -111.21200 -51.34700 1.000 81.49460  ? 177 PRO   B CD    1 
ATOM   6161 N  N     . HIS   B  2 186 ? 28.75300 -111.72600 -53.78100 1.000 84.74276  ? 178 HIS   B N     1 
ATOM   6162 C  CA    . HIS   B  2 186 ? 29.54500 -111.93700 -55.02600 1.000 86.16580  ? 178 HIS   B CA    1 
ATOM   6163 C  C     . HIS   B  2 186 ? 29.95900 -110.61900 -55.70300 1.000 85.30114  ? 178 HIS   B C     1 
ATOM   6164 O  O     . HIS   B  2 186 ? 30.59300 -110.70900 -56.77100 1.000 86.70063  ? 178 HIS   B O     1 
ATOM   6165 C  CB    . HIS   B  2 186 ? 28.75200 -112.83500 -55.98600 1.000 87.08577  ? 178 HIS   B CB    1 
ATOM   6166 C  CG    . HIS   B  2 186 ? 28.30700 -114.11700 -55.36500 1.000 88.31220  ? 178 HIS   B CG    1 
ATOM   6167 N  ND1   . HIS   B  2 186 ? 29.20300 -115.07000 -54.92100 1.000 90.31975  ? 178 HIS   B ND1   1 
ATOM   6168 C  CD2   . HIS   B  2 186 ? 27.07400 -114.60200 -55.10400 1.000 88.35386  ? 178 HIS   B CD2   1 
ATOM   6169 C  CE1   . HIS   B  2 186 ? 28.53900 -116.09000 -54.41600 1.000 91.36001  ? 178 HIS   B CE1   1 
ATOM   6170 N  NE2   . HIS   B  2 186 ? 27.23100 -115.82800 -54.51800 1.000 90.12035  ? 178 HIS   B NE2   1 
ATOM   6171 N  N     . LYS   B  2 187 ? 29.65500 -109.45400 -55.11700 1.000 83.53581  ? 179 LYS   B N     1 
ATOM   6172 C  CA    . LYS   B  2 187 ? 29.96500 -108.12300 -55.71200 1.000 82.94403  ? 179 LYS   B CA    1 
ATOM   6173 C  C     . LYS   B  2 187 ? 30.62000 -107.21700 -54.66200 1.000 87.10344  ? 179 LYS   B C     1 
ATOM   6174 O  O     . LYS   B  2 187 ? 30.00800 -107.01300 -53.59900 1.000 89.69630  ? 179 LYS   B O     1 
ATOM   6175 C  CB    . LYS   B  2 187 ? 28.69000 -107.47100 -56.25700 1.000 86.33096  ? 179 LYS   B CB    1 
ATOM   6176 C  CG    . LYS   B  2 187 ? 27.82500 -108.35900 -57.14000 1.000 82.97142  ? 179 LYS   B CG    1 
ATOM   6177 C  CD    . LYS   B  2 187 ? 26.88400 -107.57900 -58.03100 1.000 82.03716  ? 179 LYS   B CD    1 
ATOM   6178 C  CE    . LYS   B  2 187 ? 25.72600 -108.40600 -58.54500 1.000 82.96801  ? 179 LYS   B CE    1 
ATOM   6179 N  NZ    . LYS   B  2 187 ? 24.93800 -107.66500 -59.55800 1.000 83.28183  ? 179 LYS   B NZ    1 
ATOM   6180 N  N     . ASP   B  2 188 ? 31.80900 -106.68000 -54.96600 1.000 83.65803  ? 180 ASP   B N     1 
ATOM   6181 C  CA    . ASP   B  2 188 ? 32.59400 -105.79100 -54.06500 1.000 84.62728  ? 180 ASP   B CA    1 
ATOM   6182 C  C     . ASP   B  2 188 ? 31.88100 -104.44500 -53.90100 1.000 82.17014  ? 180 ASP   B C     1 
ATOM   6183 O  O     . ASP   B  2 188 ? 31.79000 -103.95700 -52.76100 1.000 92.84175  ? 180 ASP   B O     1 
ATOM   6184 C  CB    . ASP   B  2 188 ? 34.00700 -105.53900 -54.59700 1.000 86.06556  ? 180 ASP   B CB    1 
ATOM   6185 C  CG    . ASP   B  2 188 ? 34.96500 -106.69900 -54.40200 1.000 90.46637  ? 180 ASP   B CG    1 
ATOM   6186 O  OD1   . ASP   B  2 188 ? 34.90000 -107.34500 -53.33500 1.000 88.30804  ? 180 ASP   B OD1   1 
ATOM   6187 O  OD2   . ASP   B  2 188 ? 35.77400 -106.94100 -55.32000 1.000 106.09598 ? 180 ASP   B OD2   1 
ATOM   6188 N  N     . SER   B  2 189 ? 31.41300 -103.86400 -55.00600 1.000 84.18939  ? 181 SER   B N     1 
ATOM   6189 C  CA    . SER   B  2 189 ? 30.84900 -102.49000 -55.07300 1.000 85.83251  ? 181 SER   B CA    1 
ATOM   6190 C  C     . SER   B  2 189 ? 29.45600 -102.43600 -54.43400 1.000 84.34950  ? 181 SER   B C     1 
ATOM   6191 O  O     . SER   B  2 189 ? 28.99700 -101.31000 -54.15200 1.000 88.05666  ? 181 SER   B O     1 
ATOM   6192 C  CB    . SER   B  2 189 ? 30.80700 -101.99300 -56.49500 1.000 82.18399  ? 181 SER   B CB    1 
ATOM   6193 O  OG    . SER   B  2 189 ? 29.96900 -102.81500 -57.29300 1.000 87.10739  ? 181 SER   B OG    1 
ATOM   6194 N  N     . VAL   B  2 190 ? 28.80900 -103.59100 -54.22400 1.000 78.31894  ? 182 VAL   B N     1 
ATOM   6195 C  CA    . VAL   B  2 190 ? 27.41000 -103.69000 -53.70700 1.000 83.82889  ? 182 VAL   B CA    1 
ATOM   6196 C  C     . VAL   B  2 190 ? 27.42900 -104.20900 -52.25900 1.000 86.34606  ? 182 VAL   B C     1 
ATOM   6197 O  O     . VAL   B  2 190 ? 28.26100 -105.08800 -51.95100 1.000 87.84968  ? 182 VAL   B O     1 
ATOM   6198 C  CB    . VAL   B  2 190 ? 26.54700 -104.57600 -54.62600 1.000 81.55009  ? 182 VAL   B CB    1 
ATOM   6199 C  CG1   . VAL   B  2 190 ? 25.12300 -104.73500 -54.11100 1.000 77.45675  ? 182 VAL   B CG1   1 
ATOM   6200 C  CG2   . VAL   B  2 190 ? 26.53600 -104.05100 -56.05200 1.000 80.97419  ? 182 VAL   B CG2   1 
ATOM   6201 N  N     . PHE   B  2 191 ? 26.54500 -103.66700 -51.41000 1.000 79.77733  ? 183 PHE   B N     1 
ATOM   6202 C  CA    . PHE   B  2 191 ? 26.30400 -104.10200 -50.00700 1.000 78.74717  ? 183 PHE   B CA    1 
ATOM   6203 C  C     . PHE   B  2 191 ? 25.03600 -103.43200 -49.46400 1.000 75.21077  ? 183 PHE   B C     1 
ATOM   6204 O  O     . PHE   B  2 191 ? 24.65200 -102.36900 -49.97400 1.000 78.86175  ? 183 PHE   B O     1 
ATOM   6205 C  CB    . PHE   B  2 191 ? 27.51300 -103.79300 -49.11800 1.000 78.60755  ? 183 PHE   B CB    1 
ATOM   6206 C  CG    . PHE   B  2 191 ? 27.85100 -102.33300 -48.95400 1.000 77.66349  ? 183 PHE   B CG    1 
ATOM   6207 C  CD1   . PHE   B  2 191 ? 27.21400 -101.55800 -47.99800 1.000 76.74505  ? 183 PHE   B CD1   1 
ATOM   6208 C  CD2   . PHE   B  2 191 ? 28.83400 -101.74200 -49.73400 1.000 77.68731  ? 183 PHE   B CD2   1 
ATOM   6209 C  CE1   . PHE   B  2 191 ? 27.53900 -100.21900 -47.83700 1.000 77.86784  ? 183 PHE   B CE1   1 
ATOM   6210 C  CE2   . PHE   B  2 191 ? 29.15800 -100.40300 -49.57300 1.000 81.33597  ? 183 PHE   B CE2   1 
ATOM   6211 C  CZ    . PHE   B  2 191 ? 28.50900 -99.64400  -48.62700 1.000 81.27781  ? 183 PHE   B CZ    1 
ATOM   6212 N  N     . LEU   B  2 192 ? 24.40800 -104.04600 -48.45800 1.000 73.13338  ? 184 LEU   B N     1 
ATOM   6213 C  CA    . LEU   B  2 192 ? 23.19400 -103.51900 -47.77900 1.000 73.39601  ? 184 LEU   B CA    1 
ATOM   6214 C  C     . LEU   B  2 192 ? 23.60700 -102.79600 -46.49500 1.000 76.35608  ? 184 LEU   B C     1 
ATOM   6215 O  O     . LEU   B  2 192 ? 24.67400 -103.12100 -45.94400 1.000 79.14242  ? 184 LEU   B O     1 
ATOM   6216 C  CB    . LEU   B  2 192 ? 22.23900 -104.67200 -47.45700 1.000 75.32574  ? 184 LEU   B CB    1 
ATOM   6217 C  CG    . LEU   B  2 192 ? 21.45600 -105.23600 -48.63900 1.000 79.50759  ? 184 LEU   B CG    1 
ATOM   6218 C  CD1   . LEU   B  2 192 ? 20.89600 -106.61000 -48.30900 1.000 77.50859  ? 184 LEU   B CD1   1 
ATOM   6219 C  CD2   . LEU   B  2 192 ? 20.34200 -104.29000 -49.06100 1.000 77.79466  ? 184 LEU   B CD2   1 
ATOM   6220 N  N     . SER   B  2 193 ? 22.77700 -101.85300 -46.04800 1.000 71.99109  ? 185 SER   B N     1 
ATOM   6221 C  CA    . SER   B  2 193 ? 22.88500 -101.16600 -44.73600 1.000 70.48150  ? 185 SER   B CA    1 
ATOM   6222 C  C     . SER   B  2 193 ? 21.48600 -100.76000 -44.26600 1.000 70.12084  ? 185 SER   B C     1 
ATOM   6223 O  O     . SER   B  2 193 ? 20.63800 -100.46200 -45.13000 1.000 72.57621  ? 185 SER   B O     1 
ATOM   6224 C  CB    . SER   B  2 193 ? 23.79900 -99.97400  -44.81400 1.000 72.60869  ? 185 SER   B CB    1 
ATOM   6225 O  OG    . SER   B  2 193 ? 23.09400 -98.82900  -45.26700 1.000 69.20613  ? 185 SER   B OG    1 
ATOM   6226 N  N     . CYS   B  2 194 ? 21.26100 -100.75600 -42.94900 1.000 70.63141  ? 186 CYS   B N     1 
ATOM   6227 C  CA    . CYS   B  2 194 ? 20.01000 -100.27300 -42.30600 1.000 68.47145  ? 186 CYS   B CA    1 
ATOM   6228 C  C     . CYS   B  2 194 ? 20.35200 -99.50800  -41.02400 1.000 68.13395  ? 186 CYS   B C     1 
ATOM   6229 O  O     . CYS   B  2 194 ? 21.41300 -99.78800  -40.43000 1.000 68.72539  ? 186 CYS   B O     1 
ATOM   6230 C  CB    . CYS   B  2 194 ? 19.05100 -101.42200 -42.02300 1.000 68.99674  ? 186 CYS   B CB    1 
ATOM   6231 S  SG    . CYS   B  2 194 ? 19.69500 -102.63200 -40.84100 1.000 69.87980  ? 186 CYS   B SG    1 
ATOM   6232 N  N     . SER   B  2 195 ? 19.48800 -98.56900  -40.63100 1.000 67.57990  ? 187 SER   B N     1 
ATOM   6233 C  CA    . SER   B  2 195 ? 19.73300 -97.58700  -39.54200 1.000 68.75820  ? 187 SER   B CA    1 
ATOM   6234 C  C     . SER   B  2 195 ? 18.42400 -97.25400  -38.81900 1.000 70.39464  ? 187 SER   B C     1 
ATOM   6235 O  O     . SER   B  2 195 ? 17.34700 -97.64000  -39.31500 1.000 70.25720  ? 187 SER   B O     1 
ATOM   6236 C  CB    . SER   B  2 195 ? 20.38600 -96.34700  -40.09500 1.000 68.72100  ? 187 SER   B CB    1 
ATOM   6237 O  OG    . SER   B  2 195 ? 20.51900 -95.34700  -39.09900 1.000 72.00040  ? 187 SER   B OG    1 
ATOM   6238 N  N     . GLU   B  2 196 ? 18.52900 -96.53100  -37.70100 1.000 73.58096  ? 188 GLU   B N     1 
ATOM   6239 C  CA    . GLU   B  2 196 ? 17.38100 -96.12900  -36.84400 1.000 72.69365  ? 188 GLU   B CA    1 
ATOM   6240 C  C     . GLU   B  2 196 ? 16.64800 -94.94500  -37.49200 1.000 73.52252  ? 188 GLU   B C     1 
ATOM   6241 O  O     . GLU   B  2 196 ? 15.61800 -94.52000  -36.93200 1.000 78.56704  ? 188 GLU   B O     1 
ATOM   6242 C  CB    . GLU   B  2 196 ? 17.85800 -95.80400  -35.42600 1.000 70.23718  ? 188 GLU   B CB    1 
ATOM   6243 C  CG    . GLU   B  2 196 ? 18.79800 -96.85100  -34.85400 1.000 72.20169  ? 188 GLU   B CG    1 
ATOM   6244 C  CD    . GLU   B  2 196 ? 18.94300 -96.86300  -33.34200 1.000 78.93648  ? 188 GLU   B CD    1 
ATOM   6245 O  OE1   . GLU   B  2 196 ? 18.48700 -95.90200  -32.68400 1.000 78.57628  ? 188 GLU   B OE1   1 
ATOM   6246 O  OE2   . GLU   B  2 196 ? 19.51800 -97.84100  -32.82600 1.000 82.12080  ? 188 GLU   B OE2   1 
ATOM   6247 N  N     . ASP   B  2 197 ? 17.15100 -94.44200  -38.62800 1.000 66.42187  ? 189 ASP   B N     1 
ATOM   6248 C  CA    . ASP   B  2 197 ? 16.45300 -93.45400  -39.49700 1.000 68.55174  ? 189 ASP   B CA    1 
ATOM   6249 C  C     . ASP   B  2 197 ? 15.37600 -94.17300  -40.32200 1.000 66.66369  ? 189 ASP   B C     1 
ATOM   6250 O  O     . ASP   B  2 197 ? 14.70900 -93.50000  -41.12500 1.000 67.00246  ? 189 ASP   B O     1 
ATOM   6251 C  CB    . ASP   B  2 197 ? 17.43800 -92.70000  -40.39600 1.000 67.11828  ? 189 ASP   B CB    1 
ATOM   6252 C  CG    . ASP   B  2 197 ? 18.06800 -93.53800  -41.49700 1.000 66.85845  ? 189 ASP   B CG    1 
ATOM   6253 O  OD1   . ASP   B  2 197 ? 17.78900 -94.75200  -41.54800 1.000 66.77957  ? 189 ASP   B OD1   1 
ATOM   6254 O  OD2   . ASP   B  2 197 ? 18.84100 -92.96900  -42.29200 1.000 67.85223  ? 189 ASP   B OD2   1 
ATOM   6255 N  N     . ASN   B  2 198 ? 15.26000 -95.49700  -40.16000 1.000 68.68886  ? 190 ASN   B N     1 
ATOM   6256 C  CA    . ASN   B  2 198 ? 14.19900 -96.36000  -40.74700 1.000 71.17768  ? 190 ASN   B CA    1 
ATOM   6257 C  C     . ASN   B  2 198 ? 14.50500 -96.63600  -42.22600 1.000 68.85073  ? 190 ASN   B C     1 
ATOM   6258 O  O     . ASN   B  2 198 ? 13.59700 -97.11800  -42.92900 1.000 69.84537  ? 190 ASN   B O     1 
ATOM   6259 C  CB    . ASN   B  2 198 ? 12.80500 -95.75300  -40.55600 1.000 67.62779  ? 190 ASN   B CB    1 
ATOM   6260 C  CG    . ASN   B  2 198 ? 11.68400 -96.74700  -40.77800 1.000 71.05790  ? 190 ASN   B CG    1 
ATOM   6261 O  OD1   . ASN   B  2 198 ? 11.87300 -97.95300  -40.63200 1.000 75.45903  ? 190 ASN   B OD1   1 
ATOM   6262 N  ND2   . ASN   B  2 198 ? 10.51200 -96.25100  -41.13500 1.000 86.03790  ? 190 ASN   B ND2   1 
ATOM   6263 N  N     . ARG   B  2 199 ? 15.73800 -96.37200  -42.67300 1.000 67.40937  ? 191 ARG   B N     1 
ATOM   6264 C  CA    . ARG   B  2 199 ? 16.18300 -96.58000  -44.07700 1.000 67.84917  ? 191 ARG   B CA    1 
ATOM   6265 C  C     . ARG   B  2 199 ? 16.91900 -97.91700  -44.19100 1.000 72.13111  ? 191 ARG   B C     1 
ATOM   6266 O  O     . ARG   B  2 199 ? 17.78500 -98.19000  -43.34200 1.000 71.83242  ? 191 ARG   B O     1 
ATOM   6267 C  CB    . ARG   B  2 199 ? 17.12900 -95.46800  -44.54200 1.000 67.76413  ? 191 ARG   B CB    1 
ATOM   6268 C  CG    . ARG   B  2 199 ? 16.47600 -94.10400  -44.71600 1.000 67.99021  ? 191 ARG   B CG    1 
ATOM   6269 C  CD    . ARG   B  2 199 ? 17.40100 -93.15700  -45.45500 1.000 68.38402  ? 191 ARG   B CD    1 
ATOM   6270 N  NE    . ARG   B  2 199 ? 16.78500 -91.86300  -45.71800 1.000 68.96723  ? 191 ARG   B NE    1 
ATOM   6271 C  CZ    . ARG   B  2 199 ? 16.98700 -90.74700  -45.01900 1.000 71.56395  ? 191 ARG   B CZ    1 
ATOM   6272 N  NH1   . ARG   B  2 199 ? 17.80500 -90.73000  -43.97800 1.000 68.43999  ? 191 ARG   B NH1   1 
ATOM   6273 N  NH2   . ARG   B  2 199 ? 16.36300 -89.63700  -45.37400 1.000 69.90200  ? 191 ARG   B NH2   1 
ATOM   6274 N  N     . ILE   B  2 200 ? 16.57800 -98.70600  -45.21200 1.000 77.18874  ? 192 ILE   B N     1 
ATOM   6275 C  CA    . ILE   B  2 200 ? 17.42400 -99.81200  -45.74900 1.000 74.61057  ? 192 ILE   B CA    1 
ATOM   6276 C  C     . ILE   B  2 200 ? 18.00400 -99.30700  -47.07400 1.000 73.27682  ? 192 ILE   B C     1 
ATOM   6277 O  O     . ILE   B  2 200 ? 17.20800 -99.03600  -47.98700 1.000 85.42745  ? 192 ILE   B O     1 
ATOM   6278 C  CB    . ILE   B  2 200 ? 16.61600 -101.11300 -45.92300 1.000 73.98097  ? 192 ILE   B CB    1 
ATOM   6279 C  CG1   . ILE   B  2 200 ? 15.76000 -101.43100 -44.69200 1.000 77.62764  ? 192 ILE   B CG1   1 
ATOM   6280 C  CG2   . ILE   B  2 200 ? 17.53800 -102.27000 -46.27700 1.000 75.72223  ? 192 ILE   B CG2   1 
ATOM   6281 C  CD1   . ILE   B  2 200 ? 14.42700 -102.06700 -45.01600 1.000 80.47640  ? 192 ILE   B CD1   1 
ATOM   6282 N  N     . LEU   B  2 201 ? 19.32600 -99.13300  -47.14600 1.000 70.98446  ? 193 LEU   B N     1 
ATOM   6283 C  CA    . LEU   B  2 201 ? 20.03700 -98.63500  -48.35400 1.000 75.25638  ? 193 LEU   B CA    1 
ATOM   6284 C  C     . LEU   B  2 201 ? 20.68200 -99.81300  -49.08900 1.000 78.40195  ? 193 LEU   B C     1 
ATOM   6285 O  O     . LEU   B  2 201 ? 21.49800 -100.52000 -48.46600 1.000 72.56870  ? 193 LEU   B O     1 
ATOM   6286 C  CB    . LEU   B  2 201 ? 21.10500 -97.61900  -47.93700 1.000 75.55901  ? 193 LEU   B CB    1 
ATOM   6287 C  CG    . LEU   B  2 201 ? 20.61400 -96.39600  -47.16300 1.000 68.95179  ? 193 LEU   B CG    1 
ATOM   6288 C  CD1   . LEU   B  2 201 ? 21.77500 -95.46200  -46.85600 1.000 69.05881  ? 193 LEU   B CD1   1 
ATOM   6289 C  CD2   . LEU   B  2 201 ? 19.52800 -95.65400  -47.92700 1.000 71.79679  ? 193 LEU   B CD2   1 
ATOM   6290 N  N     . LEU   B  2 202 ? 20.32200 -100.01000 -50.36100 1.000 78.61934  ? 194 LEU   B N     1 
ATOM   6291 C  CA    . LEU   B  2 202 ? 21.09100 -100.84400 -51.32400 1.000 77.81521  ? 194 LEU   B CA    1 
ATOM   6292 C  C     . LEU   B  2 202 ? 22.21900 -99.97700  -51.89000 1.000 74.43424  ? 194 LEU   B C     1 
ATOM   6293 O  O     . LEU   B  2 202 ? 21.90800 -98.91500  -52.46300 1.000 78.52104  ? 194 LEU   B O     1 
ATOM   6294 C  CB    . LEU   B  2 202 ? 20.16200 -101.35300 -52.43200 1.000 74.02105  ? 194 LEU   B CB    1 
ATOM   6295 C  CG    . LEU   B  2 202 ? 20.84700 -102.08800 -53.58400 1.000 77.46496  ? 194 LEU   B CG    1 
ATOM   6296 C  CD1   . LEU   B  2 202 ? 21.67100 -103.26200 -53.07600 1.000 81.10268  ? 194 LEU   B CD1   1 
ATOM   6297 C  CD2   . LEU   B  2 202 ? 19.82500 -102.56100 -54.60600 1.000 76.30526  ? 194 LEU   B CD2   1 
ATOM   6298 N  N     . TRP   B  2 203 ? 23.47400 -100.39500 -51.70200 1.000 72.57632  ? 195 TRP   B N     1 
ATOM   6299 C  CA    . TRP   B  2 203 ? 24.68000 -99.63600  -52.12600 1.000 74.36639  ? 195 TRP   B CA    1 
ATOM   6300 C  C     . TRP   B  2 203 ? 25.22800 -100.21300 -53.43300 1.000 84.41994  ? 195 TRP   B C     1 
ATOM   6301 O  O     . TRP   B  2 203 ? 25.08800 -101.43000 -53.65000 1.000 84.48896  ? 195 TRP   B O     1 
ATOM   6302 C  CB    . TRP   B  2 203 ? 25.75000 -99.63700  -51.03000 1.000 77.30572  ? 195 TRP   B CB    1 
ATOM   6303 C  CG    . TRP   B  2 203 ? 25.34900 -98.87600  -49.80600 1.000 78.89920  ? 195 TRP   B CG    1 
ATOM   6304 C  CD1   . TRP   B  2 203 ? 24.50100 -99.28900  -48.82100 1.000 76.31456  ? 195 TRP   B CD1   1 
ATOM   6305 C  CD2   . TRP   B  2 203 ? 25.78300 -97.55600  -49.43500 1.000 77.81128  ? 195 TRP   B CD2   1 
ATOM   6306 N  NE1   . TRP   B  2 203 ? 24.37900 -98.32000  -47.86400 1.000 75.84846  ? 195 TRP   B NE1   1 
ATOM   6307 C  CE2   . TRP   B  2 203 ? 25.15100 -97.24500  -48.21200 1.000 77.14037  ? 195 TRP   B CE2   1 
ATOM   6308 C  CE3   . TRP   B  2 203 ? 26.63900 -96.61100  -50.01200 1.000 79.70670  ? 195 TRP   B CE3   1 
ATOM   6309 C  CZ2   . TRP   B  2 203 ? 25.35200 -96.02900  -47.56000 1.000 75.19322  ? 195 TRP   B CZ2   1 
ATOM   6310 C  CZ3   . TRP   B  2 203 ? 26.83600 -95.40900  -49.36700 1.000 75.34080  ? 195 TRP   B CZ3   1 
ATOM   6311 C  CH2   . TRP   B  2 203 ? 26.20100 -95.12600  -48.15700 1.000 74.60113  ? 195 TRP   B CH2   1 
ATOM   6312 N  N     . ASP   B  2 204 ? 25.81600 -99.34500  -54.25900 1.000 86.79950  ? 196 ASP   B N     1 
ATOM   6313 C  CA    . ASP   B  2 204 ? 26.55900 -99.69200  -55.49700 1.000 79.11845  ? 196 ASP   B CA    1 
ATOM   6314 C  C     . ASP   B  2 204 ? 27.56600 -98.56300  -55.74700 1.000 81.69115  ? 196 ASP   B C     1 
ATOM   6315 O  O     . ASP   B  2 204 ? 27.18700 -97.55200  -56.37200 1.000 81.33872  ? 196 ASP   B O     1 
ATOM   6316 C  CB    . ASP   B  2 204 ? 25.59800 -99.93800  -56.66400 1.000 87.16009  ? 196 ASP   B CB    1 
ATOM   6317 C  CG    . ASP   B  2 204 ? 26.16400 -100.83600 -57.75300 1.000 90.11673  ? 196 ASP   B CG    1 
ATOM   6318 O  OD1   . ASP   B  2 204 ? 27.39000 -100.77800 -57.98400 1.000 87.09381  ? 196 ASP   B OD1   1 
ATOM   6319 O  OD2   . ASP   B  2 204 ? 25.37400 -101.59500 -58.35600 1.000 86.96468  ? 196 ASP   B OD2   1 
ATOM   6320 N  N     . THR   B  2 205 ? 28.79400 -98.72500  -55.24300 1.000 81.47527  ? 197 THR   B N     1 
ATOM   6321 C  CA    . THR   B  2 205 ? 29.85200 -97.67700  -55.20800 1.000 84.91399  ? 197 THR   B CA    1 
ATOM   6322 C  C     . THR   B  2 205 ? 30.32500 -97.34100  -56.62900 1.000 89.46200  ? 197 THR   B C     1 
ATOM   6323 O  O     . THR   B  2 205 ? 31.07400 -96.35500  -56.77200 1.000 88.40734  ? 197 THR   B O     1 
ATOM   6324 C  CB    . THR   B  2 205 ? 31.02300 -98.10100  -54.31200 1.000 86.09477  ? 197 THR   B CB    1 
ATOM   6325 O  OG1   . THR   B  2 205 ? 31.53100 -99.34800  -54.78700 1.000 85.72807  ? 197 THR   B OG1   1 
ATOM   6326 C  CG2   . THR   B  2 205 ? 30.62800 -98.22900  -52.85600 1.000 87.31212  ? 197 THR   B CG2   1 
ATOM   6327 N  N     . ARG   B  2 206 ? 29.91700 -98.12700  -57.63200 1.000 90.04828  ? 198 ARG   B N     1 
ATOM   6328 C  CA    . ARG   B  2 206 ? 30.14400 -97.83600  -59.07500 1.000 86.06735  ? 198 ARG   B CA    1 
ATOM   6329 C  C     . ARG   B  2 206 ? 29.38200 -96.56000  -59.46500 1.000 85.42235  ? 198 ARG   B C     1 
ATOM   6330 O  O     . ARG   B  2 206 ? 29.88700 -95.82300  -60.33100 1.000 95.88802  ? 198 ARG   B O     1 
ATOM   6331 C  CB    . ARG   B  2 206 ? 29.73300 -99.03800  -59.93400 1.000 85.36633  ? 198 ARG   B CB    1 
ATOM   6332 C  CG    . ARG   B  2 206 ? 30.63400 -100.25200 -59.75700 1.000 84.87112  ? 198 ARG   B CG    1 
ATOM   6333 C  CD    . ARG   B  2 206 ? 30.23200 -101.46100 -60.58600 1.000 84.52363  ? 198 ARG   B CD    1 
ATOM   6334 N  NE    . ARG   B  2 206 ? 29.00100 -102.08900 -60.11400 1.000 87.06763  ? 198 ARG   B NE    1 
ATOM   6335 C  CZ    . ARG   B  2 206 ? 28.65500 -103.36100 -60.31600 1.000 84.67645  ? 198 ARG   B CZ    1 
ATOM   6336 N  NH1   . ARG   B  2 206 ? 29.45000 -104.18400 -60.98200 1.000 84.52176  ? 198 ARG   B NH1   1 
ATOM   6337 N  NH2   . ARG   B  2 206 ? 27.50700 -103.81200 -59.83900 1.000 83.75572  ? 198 ARG   B NH2   1 
ATOM   6338 N  N     . CYS   B  2 207 ? 28.22600 -96.30200  -58.83900 1.000 84.54304  ? 199 CYS   B N     1 
ATOM   6339 C  CA    . CYS   B  2 207 ? 27.35000 -95.12500  -59.10200 1.000 87.42207  ? 199 CYS   B CA    1 
ATOM   6340 C  C     . CYS   B  2 207 ? 27.92800 -93.86800  -58.45500 1.000 86.06441  ? 199 CYS   B C     1 
ATOM   6341 O  O     . CYS   B  2 207 ? 28.65200 -93.95300  -57.46600 1.000 86.79096  ? 199 CYS   B O     1 
ATOM   6342 C  CB    . CYS   B  2 207 ? 25.94300 -95.35800  -58.56500 1.000 85.39114  ? 199 CYS   B CB    1 
ATOM   6343 S  SG    . CYS   B  2 207 ? 25.16200 -96.84700  -59.23700 1.000 91.67393  ? 199 CYS   B SG    1 
ATOM   6344 N  N     . PRO   B  2 208 ? 27.61700 -92.66200  -58.98500 1.000 87.47106  ? 200 PRO   B N     1 
ATOM   6345 C  CA    . PRO   B  2 208 ? 28.02800 -91.40900  -58.35000 1.000 87.04858  ? 200 PRO   B CA    1 
ATOM   6346 C  C     . PRO   B  2 208 ? 27.20500 -91.09100  -57.09100 1.000 85.26036  ? 200 PRO   B C     1 
ATOM   6347 O  O     . PRO   B  2 208 ? 27.74000 -90.45900  -56.19600 1.000 88.27125  ? 200 PRO   B O     1 
ATOM   6348 C  CB    . PRO   B  2 208 ? 27.80400 -90.36200  -59.45200 1.000 89.44804  ? 200 PRO   B CB    1 
ATOM   6349 C  CG    . PRO   B  2 208 ? 26.68500 -90.93800  -60.29400 1.000 89.06741  ? 200 PRO   B CG    1 
ATOM   6350 C  CD    . PRO   B  2 208 ? 26.87200 -92.44000  -60.23400 1.000 90.59765  ? 200 PRO   B CD    1 
ATOM   6351 N  N     . LYS   B  2 209 ? 25.93400 -91.51300  -57.06500 1.000 88.21573  ? 201 LYS   B N     1 
ATOM   6352 C  CA    . LYS   B  2 209 ? 25.05700 -91.53000  -55.86000 1.000 80.22717  ? 201 LYS   B CA    1 
ATOM   6353 C  C     . LYS   B  2 209 ? 24.85100 -92.98500  -55.43800 1.000 79.01096  ? 201 LYS   B C     1 
ATOM   6354 O  O     . LYS   B  2 209 ? 23.86900 -93.61300  -55.83100 1.000 77.85329  ? 201 LYS   B O     1 
ATOM   6355 C  CB    . LYS   B  2 209 ? 23.72600 -90.82700  -56.14400 1.000 80.54095  ? 201 LYS   B CB    1 
ATOM   6356 C  CG    . LYS   B  2 209 ? 23.77200 -89.30400  -56.09200 1.000 83.22463  ? 201 LYS   B CG    1 
ATOM   6357 C  CD    . LYS   B  2 209 ? 22.40300 -88.65700  -56.10600 1.000 82.42481  ? 201 LYS   B CD    1 
ATOM   6358 C  CE    . LYS   B  2 209 ? 22.45500 -87.14800  -56.00200 1.000 84.28317  ? 201 LYS   B CE    1 
ATOM   6359 N  NZ    . LYS   B  2 209 ? 21.14400 -86.58500  -55.60200 1.000 84.17570  ? 201 LYS   B NZ    1 
ATOM   6360 N  N     . PRO   B  2 210 ? 25.77100 -93.56100  -54.62600 1.000 77.73577  ? 202 PRO   B N     1 
ATOM   6361 C  CA    . PRO   B  2 210 ? 25.80600 -95.00600  -54.38300 1.000 79.35233  ? 202 PRO   B CA    1 
ATOM   6362 C  C     . PRO   B  2 210 ? 24.59600 -95.63700  -53.67200 1.000 76.15847  ? 202 PRO   B C     1 
ATOM   6363 O  O     . PRO   B  2 210 ? 24.37200 -96.81100  -53.87400 1.000 82.72547  ? 202 PRO   B O     1 
ATOM   6364 C  CB    . PRO   B  2 210 ? 27.04900 -95.19700  -53.49400 1.000 77.08634  ? 202 PRO   B CB    1 
ATOM   6365 C  CG    . PRO   B  2 210 ? 27.28300 -93.84400  -52.86300 1.000 77.31532  ? 202 PRO   B CG    1 
ATOM   6366 C  CD    . PRO   B  2 210 ? 26.84800 -92.85100  -53.91800 1.000 78.48825  ? 202 PRO   B CD    1 
ATOM   6367 N  N     . ALA   B  2 211 ? 23.85800 -94.87500  -52.86200 1.000 74.93085  ? 203 ALA   B N     1 
ATOM   6368 C  CA    . ALA   B  2 211 ? 22.78300 -95.40100  -51.98700 1.000 79.33955  ? 203 ALA   B CA    1 
ATOM   6369 C  C     . ALA   B  2 211 ? 21.42200 -95.29500  -52.68400 1.000 77.11235  ? 203 ALA   B C     1 
ATOM   6370 O  O     . ALA   B  2 211 ? 21.22400 -94.34300  -53.46100 1.000 79.65457  ? 203 ALA   B O     1 
ATOM   6371 C  CB    . ALA   B  2 211 ? 22.78400 -94.67000  -50.66700 1.000 79.18041  ? 203 ALA   B CB    1 
ATOM   6372 N  N     . SER   B  2 212 ? 20.52200 -96.24000  -52.39100 1.000 77.82762  ? 204 SER   B N     1 
ATOM   6373 C  CA    . SER   B  2 212 ? 19.11900 -96.28600  -52.88100 1.000 80.97786  ? 204 SER   B CA    1 
ATOM   6374 C  C     . SER   B  2 212 ? 18.20800 -96.86300  -51.78900 1.000 79.17825  ? 204 SER   B C     1 
ATOM   6375 O  O     . SER   B  2 212 ? 18.47100 -97.99300  -51.34000 1.000 82.54518  ? 204 SER   B O     1 
ATOM   6376 C  CB    . SER   B  2 212 ? 19.02400 -97.08700  -54.15600 1.000 86.78021  ? 204 SER   B CB    1 
ATOM   6377 O  OG    . SER   B  2 212 ? 17.72300 -96.99200  -54.72200 1.000 92.82224  ? 204 SER   B OG    1 
ATOM   6378 N  N     . GLN   B  2 213 ? 17.18300 -96.10900  -51.37700 1.000 80.40682  ? 205 GLN   B N     1 
ATOM   6379 C  CA    . GLN   B  2 213 ? 16.17100 -96.53900  -50.37300 1.000 82.87183  ? 205 GLN   B CA    1 
ATOM   6380 C  C     . GLN   B  2 213 ? 15.24700 -97.58900  -50.99900 1.000 85.91103  ? 205 GLN   B C     1 
ATOM   6381 O  O     . GLN   B  2 213 ? 14.70500 -97.32200  -52.08800 1.000 90.25240  ? 205 GLN   B O     1 
ATOM   6382 C  CB    . GLN   B  2 213 ? 15.35100 -95.34800  -49.87500 1.000 80.98623  ? 205 GLN   B CB    1 
ATOM   6383 C  CG    . GLN   B  2 213 ? 16.12200 -94.43300  -48.93700 1.000 79.31934  ? 205 GLN   B CG    1 
ATOM   6384 C  CD    . GLN   B  2 213 ? 15.23100 -93.39100  -48.30800 1.000 77.22063  ? 205 GLN   B CD    1 
ATOM   6385 O  OE1   . GLN   B  2 213 ? 15.41000 -92.19300  -48.51000 1.000 80.37748  ? 205 GLN   B OE1   1 
ATOM   6386 N  NE2   . GLN   B  2 213 ? 14.25500 -93.84400  -47.53800 1.000 76.12984  ? 205 GLN   B NE2   1 
ATOM   6387 N  N     . ILE   B  2 214 ? 15.05800 -98.72000  -50.31300 1.000 95.30951  ? 206 ILE   B N     1 
ATOM   6388 C  CA    . ILE   B  2 214 ? 14.26200 -99.88800  -50.79500 1.000 96.69361  ? 206 ILE   B CA    1 
ATOM   6389 C  C     . ILE   B  2 214 ? 13.65500 -100.60500 -49.58200 1.000 103.13260 ? 206 ILE   B C     1 
ATOM   6390 O  O     . ILE   B  2 214 ? 14.38200 -100.80000 -48.59200 1.000 104.84662 ? 206 ILE   B O     1 
ATOM   6391 C  CB    . ILE   B  2 214 ? 15.12800 -100.82800 -51.66300 1.000 103.22605 ? 206 ILE   B CB    1 
ATOM   6392 C  CG1   . ILE   B  2 214 ? 16.53500 -101.03300 -51.08800 1.000 91.61668  ? 206 ILE   B CG1   1 
ATOM   6393 C  CG2   . ILE   B  2 214 ? 15.18300 -100.33700 -53.10400 1.000 100.15287 ? 206 ILE   B CG2   1 
ATOM   6394 C  CD1   . ILE   B  2 214 ? 16.71800 -102.34100 -50.36100 1.000 87.42717  ? 206 ILE   B CD1   1 
ATOM   6395 N  N     . GLY   B  2 215 ? 12.36800 -100.96400 -49.65800 1.000 112.07765 ? 207 GLY   B N     1 
ATOM   6396 C  CA    . GLY   B  2 215 ? 11.62600 -101.64300 -48.57500 1.000 112.44891 ? 207 GLY   B CA    1 
ATOM   6397 C  C     . GLY   B  2 215 ? 10.18500 -101.93900 -48.96400 1.000 125.94274 ? 207 GLY   B C     1 
ATOM   6398 O  O     . GLY   B  2 215 ? 9.91100  -102.04700 -50.17800 1.000 132.53925 ? 207 GLY   B O     1 
ATOM   6399 N  N     . CYS   B  2 216 ? 9.29600  -102.06200 -47.97000 1.000 129.10398 ? 208 CYS   B N     1 
ATOM   6400 C  CA    . CYS   B  2 216 ? 7.84600  -102.36500 -48.13900 1.000 137.50513 ? 208 CYS   B CA    1 
ATOM   6401 C  C     . CYS   B  2 216 ? 7.07900  -101.08900 -48.51500 1.000 144.61232 ? 208 CYS   B C     1 
ATOM   6402 O  O     . CYS   B  2 216 ? 7.70100  -100.00500 -48.52900 1.000 144.49745 ? 208 CYS   B O     1 
ATOM   6403 C  CB    . CYS   B  2 216 ? 7.24900  -102.96700 -46.87000 1.000 140.44745 ? 208 CYS   B CB    1 
ATOM   6404 S  SG    . CYS   B  2 216 ? 8.14400  -104.40900 -46.22900 1.000 156.75462 ? 208 CYS   B SG    1 
ATOM   6405 N  N     . SER   B  2 217 ? 5.77900  -101.22400 -48.80300 1.000 149.37175 ? 209 SER   B N     1 
ATOM   6406 C  CA    . SER   B  2 217 ? 4.86700  -100.13700 -49.25600 1.000 152.33454 ? 209 SER   B CA    1 
ATOM   6407 C  C     . SER   B  2 217 ? 4.87500  -98.97600  -48.25200 1.000 152.93605 ? 209 SER   B C     1 
ATOM   6408 O  O     . SER   B  2 217 ? 5.22900  -97.85000  -48.65500 1.000 150.90852 ? 209 SER   B O     1 
ATOM   6409 C  CB    . SER   B  2 217 ? 3.46600  -100.65600 -49.47400 1.000 151.62921 ? 209 SER   B CB    1 
ATOM   6410 O  OG    . SER   B  2 217 ? 3.41300  -101.51600 -50.60300 1.000 151.91787 ? 209 SER   B OG    1 
ATOM   6411 N  N     . ALA   B  2 218 ? 4.49400  -99.24800  -46.99900 1.000 163.54103 ? 210 ALA   B N     1 
ATOM   6412 C  CA    . ALA   B  2 218 ? 4.39400  -98.25600  -45.90100 1.000 157.04310 ? 210 ALA   B CA    1 
ATOM   6413 C  C     . ALA   B  2 218 ? 5.67200  -98.27900  -45.06400 1.000 154.51228 ? 210 ALA   B C     1 
ATOM   6414 O  O     . ALA   B  2 218 ? 6.38700  -99.28200  -45.04700 1.000 146.43651 ? 210 ALA   B O     1 
ATOM   6415 C  CB    . ALA   B  2 218 ? 3.17400  -98.54800  -45.05900 1.000 154.56370 ? 210 ALA   B CB    1 
ATOM   6416 N  N     . PRO   B  2 219 ? 6.00200  -97.17600  -44.34900 1.000 146.19954 ? 211 PRO   B N     1 
ATOM   6417 C  CA    . PRO   B  2 219 ? 7.15400  -97.15700  -43.44600 1.000 138.92380 ? 211 PRO   B CA    1 
ATOM   6418 C  C     . PRO   B  2 219 ? 6.85500  -97.88900  -42.12600 1.000 128.96774 ? 211 PRO   B C     1 
ATOM   6419 O  O     . PRO   B  2 219 ? 6.30500  -97.27900  -41.22500 1.000 125.66114 ? 211 PRO   B O     1 
ATOM   6420 C  CB    . PRO   B  2 219 ? 7.40000  -95.65300  -43.24000 1.000 138.73316 ? 211 PRO   B CB    1 
ATOM   6421 C  CG    . PRO   B  2 219 ? 6.02300  -95.03000  -43.36500 1.000 143.50364 ? 211 PRO   B CG    1 
ATOM   6422 C  CD    . PRO   B  2 219 ? 5.28900  -95.88800  -44.37600 1.000 146.43145 ? 211 PRO   B CD    1 
ATOM   6423 N  N     . GLY   B  2 220 ? 7.21900  -99.17500  -42.05000 1.000 113.38551 ? 212 GLY   B N     1 
ATOM   6424 C  CA    . GLY   B  2 220 ? 6.97200  -100.05000 -40.88600 1.000 105.92780 ? 212 GLY   B CA    1 
ATOM   6425 C  C     . GLY   B  2 220 ? 7.94700  -99.77900  -39.75200 1.000 95.51023  ? 212 GLY   B C     1 
ATOM   6426 O  O     . GLY   B  2 220 ? 8.50700  -98.66400  -39.70800 1.000 98.59878  ? 212 GLY   B O     1 
ATOM   6427 N  N     . TYR   B  2 221 ? 8.14500  -100.76300 -38.86700 1.000 86.48684  ? 213 TYR   B N     1 
ATOM   6428 C  CA    . TYR   B  2 221 ? 9.05500  -100.69200 -37.69000 1.000 79.51499  ? 213 TYR   B CA    1 
ATOM   6429 C  C     . TYR   B  2 221 ? 10.50700 -100.80000 -38.17000 1.000 77.20146  ? 213 TYR   B C     1 
ATOM   6430 O  O     . TYR   B  2 221 ? 10.73400 -101.32700 -39.27500 1.000 83.55560  ? 213 TYR   B O     1 
ATOM   6431 C  CB    . TYR   B  2 221 ? 8.68000  -101.76000 -36.65900 1.000 74.33136  ? 213 TYR   B CB    1 
ATOM   6432 C  CG    . TYR   B  2 221 ? 7.30300  -101.57900 -36.07200 1.000 75.58372  ? 213 TYR   B CG    1 
ATOM   6433 C  CD1   . TYR   B  2 221 ? 7.02300  -100.51300 -35.23200 1.000 74.27612  ? 213 TYR   B CD1   1 
ATOM   6434 C  CD2   . TYR   B  2 221 ? 6.27100  -102.45400 -36.37200 1.000 73.84101  ? 213 TYR   B CD2   1 
ATOM   6435 C  CE1   . TYR   B  2 221 ? 5.75900  -100.32600 -34.69800 1.000 74.65956  ? 213 TYR   B CE1   1 
ATOM   6436 C  CE2   . TYR   B  2 221 ? 5.00100  -102.28300 -35.84400 1.000 75.83405  ? 213 TYR   B CE2   1 
ATOM   6437 C  CZ    . TYR   B  2 221 ? 4.74400  -101.21400 -35.00400 1.000 76.20287  ? 213 TYR   B CZ    1 
ATOM   6438 O  OH    . TYR   B  2 221 ? 3.49700  -101.03300 -34.48100 1.000 78.51700  ? 213 TYR   B OH    1 
ATOM   6439 N  N     . LEU   B  2 222 ? 11.45300 -100.31700 -37.35700 1.000 76.24644  ? 214 LEU   B N     1 
ATOM   6440 C  CA    . LEU   B  2 222 ? 12.86300 -100.05000 -37.75900 1.000 74.71559  ? 214 LEU   B CA    1 
ATOM   6441 C  C     . LEU   B  2 222 ? 13.57200 -101.35100 -38.12200 1.000 69.23879  ? 214 LEU   B C     1 
ATOM   6442 O  O     . LEU   B  2 222 ? 13.40700 -102.35700 -37.44100 1.000 66.71076  ? 214 LEU   B O     1 
ATOM   6443 C  CB    . LEU   B  2 222 ? 13.60900 -99.35100  -36.61800 1.000 71.13675  ? 214 LEU   B CB    1 
ATOM   6444 C  CG    . LEU   B  2 222 ? 13.04800 -98.00700  -36.15400 1.000 70.30285  ? 214 LEU   B CG    1 
ATOM   6445 C  CD1   . LEU   B  2 222 ? 13.98500 -97.37100  -35.14300 1.000 69.95052  ? 214 LEU   B CD1   1 
ATOM   6446 C  CD2   . LEU   B  2 222 ? 12.81700 -97.06000  -37.32100 1.000 73.34787  ? 214 LEU   B CD2   1 
ATOM   6447 N  N     . PRO   B  2 223 ? 14.40100 -101.35400 -39.19200 1.000 69.42325  ? 215 PRO   B N     1 
ATOM   6448 C  CA    . PRO   B  2 223 ? 15.21300 -102.51800 -39.55200 1.000 73.23863  ? 215 PRO   B CA    1 
ATOM   6449 C  C     . PRO   B  2 223 ? 16.43200 -102.69100 -38.63200 1.000 67.33832  ? 215 PRO   B C     1 
ATOM   6450 O  O     . PRO   B  2 223 ? 17.04700 -101.69600 -38.29700 1.000 72.92135  ? 215 PRO   B O     1 
ATOM   6451 C  CB    . PRO   B  2 223 ? 15.65500 -102.19200 -40.98600 1.000 69.90500  ? 215 PRO   B CB    1 
ATOM   6452 C  CG    . PRO   B  2 223 ? 15.74100 -100.68200 -41.00000 1.000 71.47013  ? 215 PRO   B CG    1 
ATOM   6453 C  CD    . PRO   B  2 223 ? 14.59700 -100.22900 -40.12000 1.000 71.19340  ? 215 PRO   B CD    1 
ATOM   6454 N  N     . THR   B  2 224 ? 16.75700 -103.93700 -38.26900 1.000 69.20574  ? 216 THR   B N     1 
ATOM   6455 C  CA    . THR   B  2 224 ? 17.78400 -104.28400 -37.24600 1.000 70.23759  ? 216 THR   B CA    1 
ATOM   6456 C  C     . THR   B  2 224 ? 18.80500 -105.29000 -37.79900 1.000 73.61361  ? 216 THR   B C     1 
ATOM   6457 O  O     . THR   B  2 224 ? 20.01000 -105.06100 -37.57900 1.000 75.84360  ? 216 THR   B O     1 
ATOM   6458 C  CB    . THR   B  2 224 ? 17.11300 -104.78200 -35.96100 1.000 69.59981  ? 216 THR   B CB    1 
ATOM   6459 O  OG1   . THR   B  2 224 ? 16.22400 -105.85000 -36.28500 1.000 72.47060  ? 216 THR   B OG1   1 
ATOM   6460 C  CG2   . THR   B  2 224 ? 16.33900 -103.69200 -35.25400 1.000 70.73652  ? 216 THR   B CG2   1 
ATOM   6461 N  N     . SER   B  2 225 ? 18.35500 -106.35900 -38.46800 1.000 73.85353  ? 217 SER   B N     1 
ATOM   6462 C  CA    . SER   B  2 225 ? 19.21200 -107.43400 -39.04600 1.000 74.90502  ? 217 SER   B CA    1 
ATOM   6463 C  C     . SER   B  2 225 ? 19.03300 -107.50400 -40.56900 1.000 74.10196  ? 217 SER   B C     1 
ATOM   6464 O  O     . SER   B  2 225 ? 17.90600 -107.25500 -41.04000 1.000 74.63345  ? 217 SER   B O     1 
ATOM   6465 C  CB    . SER   B  2 225 ? 18.91500 -108.76500 -38.39800 1.000 73.52334  ? 217 SER   B CB    1 
ATOM   6466 O  OG    . SER   B  2 225 ? 17.51500 -108.97700 -38.28400 1.000 76.84868  ? 217 SER   B OG    1 
ATOM   6467 N  N     . LEU   B  2 226 ? 20.10800 -107.83800 -41.29700 1.000 74.17444  ? 218 LEU   B N     1 
ATOM   6468 C  CA    . LEU   B  2 226 ? 20.13100 -107.97200 -42.78300 1.000 73.82076  ? 218 LEU   B CA    1 
ATOM   6469 C  C     . LEU   B  2 226 ? 20.92400 -109.21800 -43.19000 1.000 74.25516  ? 218 LEU   B C     1 
ATOM   6470 O  O     . LEU   B  2 226 ? 22.09600 -109.33100 -42.78300 1.000 75.58227  ? 218 LEU   B O     1 
ATOM   6471 C  CB    . LEU   B  2 226 ? 20.77900 -106.72900 -43.39900 1.000 72.51256  ? 218 LEU   B CB    1 
ATOM   6472 C  CG    . LEU   B  2 226 ? 20.00800 -105.42000 -43.25100 1.000 72.57011  ? 218 LEU   B CG    1 
ATOM   6473 C  CD1   . LEU   B  2 226 ? 20.86600 -104.25100 -43.70700 1.000 73.12816  ? 218 LEU   B CD1   1 
ATOM   6474 C  CD2   . LEU   B  2 226 ? 18.70100 -105.45900 -44.02800 1.000 75.42161  ? 218 LEU   B CD2   1 
ATOM   6475 N  N     . ALA   B  2 227 ? 20.32000 -110.09000 -44.00200 1.000 73.79666  ? 219 ALA   B N     1 
ATOM   6476 C  CA    . ALA   B  2 227 ? 20.96400 -111.29300 -44.57800 1.000 78.68296  ? 219 ALA   B CA    1 
ATOM   6477 C  C     . ALA   B  2 227 ? 20.65000 -111.38800 -46.07600 1.000 78.00795  ? 219 ALA   B C     1 
ATOM   6478 O  O     . ALA   B  2 227 ? 19.45800 -111.47800 -46.43200 1.000 77.13284  ? 219 ALA   B O     1 
ATOM   6479 C  CB    . ALA   B  2 227 ? 20.50300 -112.52300 -43.83600 1.000 76.32886  ? 219 ALA   B CB    1 
ATOM   6480 N  N     . TRP   B  2 228 ? 21.69000 -111.35000 -46.91500 1.000 78.84556  ? 220 TRP   B N     1 
ATOM   6481 C  CA    . TRP   B  2 228 ? 21.61600 -111.65100 -48.37100 1.000 82.68952  ? 220 TRP   B CA    1 
ATOM   6482 C  C     . TRP   B  2 228 ? 21.22500 -113.12000 -48.55900 1.000 83.75203  ? 220 TRP   B C     1 
ATOM   6483 O  O     . TRP   B  2 228 ? 21.67200 -113.95300 -47.74400 1.000 82.73348  ? 220 TRP   B O     1 
ATOM   6484 C  CB    . TRP   B  2 228 ? 22.95400 -111.35900 -49.06100 1.000 82.68823  ? 220 TRP   B CB    1 
ATOM   6485 C  CG    . TRP   B  2 228 ? 23.21600 -109.92100 -49.38300 1.000 82.58178  ? 220 TRP   B CG    1 
ATOM   6486 C  CD1   . TRP   B  2 228 ? 24.10000 -109.09000 -48.76000 1.000 82.26591  ? 220 TRP   B CD1   1 
ATOM   6487 C  CD2   . TRP   B  2 228 ? 22.63200 -109.15500 -50.45100 1.000 83.67264  ? 220 TRP   B CD2   1 
ATOM   6488 N  NE1   . TRP   B  2 228 ? 24.09400 -107.85600 -49.35300 1.000 83.04225  ? 220 TRP   B NE1   1 
ATOM   6489 C  CE2   . TRP   B  2 228 ? 23.20300 -107.86500 -50.39300 1.000 83.99994  ? 220 TRP   B CE2   1 
ATOM   6490 C  CE3   . TRP   B  2 228 ? 21.67800 -109.42500 -51.44000 1.000 87.70928  ? 220 TRP   B CE3   1 
ATOM   6491 C  CZ2   . TRP   B  2 228 ? 22.84800 -106.85500 -51.28700 1.000 85.74721  ? 220 TRP   B CZ2   1 
ATOM   6492 C  CZ3   . TRP   B  2 228 ? 21.32500 -108.42400 -52.31900 1.000 86.68559  ? 220 TRP   B CZ3   1 
ATOM   6493 C  CH2   . TRP   B  2 228 ? 21.90300 -107.15700 -52.24100 1.000 87.11949  ? 220 TRP   B CH2   1 
ATOM   6494 N  N     . HIS   B  2 229 ? 20.43500 -113.42400 -49.59300 1.000 85.05080  ? 221 HIS   B N     1 
ATOM   6495 C  CA    . HIS   B  2 229 ? 20.13700 -114.81300 -50.03800 1.000 88.60201  ? 221 HIS   B CA    1 
ATOM   6496 C  C     . HIS   B  2 229 ? 21.36500 -115.34300 -50.77500 1.000 90.52433  ? 221 HIS   B C     1 
ATOM   6497 O  O     . HIS   B  2 229 ? 21.91300 -114.64800 -51.62700 1.000 92.19103  ? 221 HIS   B O     1 
ATOM   6498 C  CB    . HIS   B  2 229 ? 18.86300 -114.85700 -50.89000 1.000 88.53032  ? 221 HIS   B CB    1 
ATOM   6499 C  CG    . HIS   B  2 229 ? 18.21300 -116.20000 -50.94000 1.000 93.11650  ? 221 HIS   B CG    1 
ATOM   6500 N  ND1   . HIS   B  2 229 ? 18.76100 -117.26300 -51.63100 1.000 97.56526  ? 221 HIS   B ND1   1 
ATOM   6501 C  CD2   . HIS   B  2 229 ? 17.06300 -116.65600 -50.39600 1.000 94.84004  ? 221 HIS   B CD2   1 
ATOM   6502 C  CE1   . HIS   B  2 229 ? 17.98000 -118.31700 -51.50700 1.000 98.13831  ? 221 HIS   B CE1   1 
ATOM   6503 N  NE2   . HIS   B  2 229 ? 16.93000 -117.97000 -50.75500 1.000 97.24484  ? 221 HIS   B NE2   1 
ATOM   6504 N  N     . PRO   B  2 230 ? 21.86400 -116.56200 -50.45700 1.000 90.36493  ? 222 PRO   B N     1 
ATOM   6505 C  CA    . PRO   B  2 230 ? 23.13600 -117.03700 -51.00600 1.000 95.54002  ? 222 PRO   B CA    1 
ATOM   6506 C  C     . PRO   B  2 230 ? 23.12800 -117.36200 -52.51100 1.000 103.57964 ? 222 PRO   B C     1 
ATOM   6507 O  O     . PRO   B  2 230 ? 24.19900 -117.39100 -53.09200 1.000 97.56890  ? 222 PRO   B O     1 
ATOM   6508 C  CB    . PRO   B  2 230 ? 23.42400 -118.32900 -50.21800 1.000 100.12409 ? 222 PRO   B CB    1 
ATOM   6509 C  CG    . PRO   B  2 230 ? 22.47400 -118.28800 -49.03600 1.000 92.74535  ? 222 PRO   B CG    1 
ATOM   6510 C  CD    . PRO   B  2 230 ? 21.26000 -117.53900 -49.53800 1.000 90.72829  ? 222 PRO   B CD    1 
ATOM   6511 N  N     . GLN   B  2 231 ? 21.94800 -117.60200 -53.09500 1.000 108.18646 ? 223 GLN   B N     1 
ATOM   6512 C  CA    . GLN   B  2 231 ? 21.78200 -118.09000 -54.49300 1.000 112.24201 ? 223 GLN   B CA    1 
ATOM   6513 C  C     . GLN   B  2 231 ? 21.11400 -117.02500 -55.37400 1.000 111.07467 ? 223 GLN   B C     1 
ATOM   6514 O  O     . GLN   B  2 231 ? 21.46000 -116.96700 -56.57300 1.000 113.62622 ? 223 GLN   B O     1 
ATOM   6515 C  CB    . GLN   B  2 231 ? 21.00000 -119.40200 -54.48100 1.000 116.89665 ? 223 GLN   B CB    1 
ATOM   6516 C  CG    . GLN   B  2 231 ? 21.83500 -120.57400 -53.98300 1.000 119.18241 ? 223 GLN   B CG    1 
ATOM   6517 C  CD    . GLN   B  2 231 ? 21.04900 -121.58100 -53.18000 1.000 121.62591 ? 223 GLN   B CD    1 
ATOM   6518 O  OE1   . GLN   B  2 231 ? 20.04200 -121.26400 -52.55100 1.000 115.99787 ? 223 GLN   B OE1   1 
ATOM   6519 N  NE2   . GLN   B  2 231 ? 21.52500 -122.81500 -53.18500 1.000 122.84893 ? 223 GLN   B NE2   1 
ATOM   6520 N  N     . GLN   B  2 232 ? 20.17900 -116.24300 -54.82300 1.000 101.66203 ? 224 GLN   B N     1 
ATOM   6521 C  CA    . GLN   B  2 232 ? 19.62100 -115.02800 -55.47800 1.000 103.24214 ? 224 GLN   B CA    1 
ATOM   6522 C  C     . GLN   B  2 232 ? 20.46600 -113.81800 -55.06600 1.000 107.97152 ? 224 GLN   B C     1 
ATOM   6523 O  O     . GLN   B  2 232 ? 20.40100 -113.42700 -53.88400 1.000 107.19347 ? 224 GLN   B O     1 
ATOM   6524 C  CB    . GLN   B  2 232 ? 18.15800 -114.79900 -55.09400 1.000 98.92703  ? 224 GLN   B CB    1 
ATOM   6525 C  CG    . GLN   B  2 232 ? 17.18100 -115.76200 -55.75100 1.000 100.92406 ? 224 GLN   B CG    1 
ATOM   6526 C  CD    . GLN   B  2 232 ? 16.95500 -116.99400 -54.91100 1.000 105.11320 ? 224 GLN   B CD    1 
ATOM   6527 O  OE1   . GLN   B  2 232 ? 17.89000 -117.71300 -54.56800 1.000 110.85038 ? 224 GLN   B OE1   1 
ATOM   6528 N  NE2   . GLN   B  2 232 ? 15.70100 -117.24500 -54.57200 1.000 100.45300 ? 224 GLN   B NE2   1 
ATOM   6529 N  N     . SER   B  2 233 ? 21.21000 -113.24000 -56.01200 1.000 130.34719 ? 225 SER   B N     1 
ATOM   6530 C  CA    . SER   B  2 233 ? 22.10000 -112.06700 -55.80100 1.000 137.68656 ? 225 SER   B CA    1 
ATOM   6531 C  C     . SER   B  2 233 ? 21.27200 -110.78800 -55.59300 1.000 134.35874 ? 225 SER   B C     1 
ATOM   6532 O  O     . SER   B  2 233 ? 21.86800 -109.77100 -55.17700 1.000 127.39039 ? 225 SER   B O     1 
ATOM   6533 C  CB    . SER   B  2 233 ? 23.06200 -111.91800 -56.95600 1.000 132.60331 ? 225 SER   B CB    1 
ATOM   6534 O  OG    . SER   B  2 233 ? 24.02400 -110.90800 -56.69000 1.000 139.74267 ? 225 SER   B OG    1 
ATOM   6535 N  N     . GLU   B  2 234 ? 19.95900 -110.84000 -55.86000 1.000 117.94666 ? 226 GLU   B N     1 
ATOM   6536 C  CA    . GLU   B  2 234 ? 19.05900 -109.65700 -55.93900 1.000 116.30237 ? 226 GLU   B CA    1 
ATOM   6537 C  C     . GLU   B  2 234 ? 17.94800 -109.70900 -54.87700 1.000 114.40306 ? 226 GLU   B C     1 
ATOM   6538 O  O     . GLU   B  2 234 ? 17.07100 -108.82300 -54.92600 1.000 120.78162 ? 226 GLU   B O     1 
ATOM   6539 C  CB    . GLU   B  2 234 ? 18.44800 -109.57200 -57.34000 1.000 118.77206 ? 226 GLU   B CB    1 
ATOM   6540 C  CG    . GLU   B  2 234 ? 19.43000 -109.12700 -58.40900 1.000 118.00122 ? 226 GLU   B CG    1 
ATOM   6541 C  CD    . GLU   B  2 234 ? 18.77300 -108.63700 -59.68800 1.000 136.12864 ? 226 GLU   B CD    1 
ATOM   6542 O  OE1   . GLU   B  2 234 ? 17.85100 -107.80200 -59.58700 1.000 139.69425 ? 226 GLU   B OE1   1 
ATOM   6543 O  OE2   . GLU   B  2 234 ? 19.18100 -109.09000 -60.78100 1.000 136.73214 ? 226 GLU   B OE2   1 
ATOM   6544 N  N     . VAL   B  2 235 ? 17.96400 -110.68000 -53.95300 1.000 104.67730 ? 227 VAL   B N     1 
ATOM   6545 C  CA    . VAL   B  2 235 ? 16.98000 -110.74900 -52.82600 1.000 98.14234  ? 227 VAL   B CA    1 
ATOM   6546 C  C     . VAL   B  2 235 ? 17.74300 -110.86800 -51.49900 1.000 94.76998  ? 227 VAL   B C     1 
ATOM   6547 O  O     . VAL   B  2 235 ? 18.83300 -111.47400 -51.48600 1.000 94.47235  ? 227 VAL   B O     1 
ATOM   6548 C  CB    . VAL   B  2 235 ? 15.94600 -111.88500 -52.99700 1.000 94.94064  ? 227 VAL   B CB    1 
ATOM   6549 C  CG1   . VAL   B  2 235 ? 15.59300 -112.13000 -54.45700 1.000 102.53953 ? 227 VAL   B CG1   1 
ATOM   6550 C  CG2   . VAL   B  2 235 ? 16.37700 -113.18100 -52.33100 1.000 91.67599  ? 227 VAL   B CG2   1 
ATOM   6551 N  N     . PHE   B  2 236 ? 17.17800 -110.29500 -50.43200 1.000 87.52751  ? 228 PHE   B N     1 
ATOM   6552 C  CA    . PHE   B  2 236 ? 17.68800 -110.37500 -49.03800 1.000 84.07191  ? 228 PHE   B CA    1 
ATOM   6553 C  C     . PHE   B  2 236 ? 16.50400 -110.46700 -48.07000 1.000 81.98304  ? 228 PHE   B C     1 
ATOM   6554 O  O     . PHE   B  2 236 ? 15.35100 -110.26000 -48.50100 1.000 83.77475  ? 228 PHE   B O     1 
ATOM   6555 C  CB    . PHE   B  2 236 ? 18.57900 -109.17000 -48.71800 1.000 82.14501  ? 228 PHE   B CB    1 
ATOM   6556 C  CG    . PHE   B  2 236 ? 17.87500 -107.83600 -48.69100 1.000 81.22160  ? 228 PHE   B CG    1 
ATOM   6557 C  CD1   . PHE   B  2 236 ? 17.29900 -107.36000 -47.52300 1.000 78.52016  ? 228 PHE   B CD1   1 
ATOM   6558 C  CD2   . PHE   B  2 236 ? 17.80900 -107.04400 -49.82800 1.000 85.28402  ? 228 PHE   B CD2   1 
ATOM   6559 C  CE1   . PHE   B  2 236 ? 16.65900 -106.13100 -47.49800 1.000 77.49521  ? 228 PHE   B CE1   1 
ATOM   6560 C  CE2   . PHE   B  2 236 ? 17.17200 -105.81300 -49.79900 1.000 82.23664  ? 228 PHE   B CE2   1 
ATOM   6561 C  CZ    . PHE   B  2 236 ? 16.59900 -105.35800 -48.63400 1.000 80.22543  ? 228 PHE   B CZ    1 
ATOM   6562 N  N     . VAL   B  2 237 ? 16.79200 -110.77400 -46.80300 1.000 76.90689  ? 229 VAL   B N     1 
ATOM   6563 C  CA    . VAL   B  2 237 ? 15.80600 -110.73500 -45.68100 1.000 80.18025  ? 229 VAL   B CA    1 
ATOM   6564 C  C     . VAL   B  2 237 ? 16.25900 -109.66800 -44.67700 1.000 81.53413  ? 229 VAL   B C     1 
ATOM   6565 O  O     . VAL   B  2 237 ? 17.47600 -109.59000 -44.40200 1.000 82.38988  ? 229 VAL   B O     1 
ATOM   6566 C  CB    . VAL   B  2 237 ? 15.62300 -112.11200 -45.00800 1.000 80.32624  ? 229 VAL   B CB    1 
ATOM   6567 C  CG1   . VAL   B  2 237 ? 14.93700 -113.10400 -45.93300 1.000 78.61025  ? 229 VAL   B CG1   1 
ATOM   6568 C  CG2   . VAL   B  2 237 ? 16.92800 -112.69300 -44.48400 1.000 75.87726  ? 229 VAL   B CG2   1 
ATOM   6569 N  N     . PHE   B  2 238 ? 15.31800 -108.86200 -44.17600 1.000 78.08806  ? 230 PHE   B N     1 
ATOM   6570 C  CA    . PHE   B  2 238 ? 15.54400 -107.88300 -43.08200 1.000 77.50318  ? 230 PHE   B CA    1 
ATOM   6571 C  C     . PHE   B  2 238 ? 14.61000 -108.22600 -41.91600 1.000 81.00467  ? 230 PHE   B C     1 
ATOM   6572 O  O     . PHE   B  2 238 ? 13.39700 -108.42000 -42.14600 1.000 81.14091  ? 230 PHE   B O     1 
ATOM   6573 C  CB    . PHE   B  2 238 ? 15.38500 -106.44200 -43.58200 1.000 73.33225  ? 230 PHE   B CB    1 
ATOM   6574 C  CG    . PHE   B  2 238 ? 13.97800 -105.89900 -43.63800 1.000 81.80527  ? 230 PHE   B CG    1 
ATOM   6575 C  CD1   . PHE   B  2 238 ? 13.21500 -106.02000 -44.78900 1.000 82.50282  ? 230 PHE   B CD1   1 
ATOM   6576 C  CD2   . PHE   B  2 238 ? 13.43000 -105.23200 -42.55200 1.000 82.40047  ? 230 PHE   B CD2   1 
ATOM   6577 C  CE1   . PHE   B  2 238 ? 11.92900 -105.50300 -44.84700 1.000 86.04737  ? 230 PHE   B CE1   1 
ATOM   6578 C  CE2   . PHE   B  2 238 ? 12.14200 -104.71800 -42.61100 1.000 86.93821  ? 230 PHE   B CE2   1 
ATOM   6579 C  CZ    . PHE   B  2 238 ? 11.39400 -104.85500 -43.75800 1.000 90.10072  ? 230 PHE   B CZ    1 
ATOM   6580 N  N     . GLY   B  2 239 ? 15.18200 -108.33600 -40.71300 1.000 78.75132  ? 231 GLY   B N     1 
ATOM   6581 C  CA    . GLY   B  2 239 ? 14.44400 -108.44200 -39.44000 1.000 75.83006  ? 231 GLY   B CA    1 
ATOM   6582 C  C     . GLY   B  2 239 ? 14.30000 -107.07200 -38.80500 1.000 74.55058  ? 231 GLY   B C     1 
ATOM   6583 O  O     . GLY   B  2 239 ? 15.29800 -106.32400 -38.80800 1.000 75.77983  ? 231 GLY   B O     1 
ATOM   6584 N  N     . ASP   B  2 240 ? 13.10500 -106.74000 -38.30700 1.000 76.62275  ? 232 ASP   B N     1 
ATOM   6585 C  CA    . ASP   B  2 240 ? 12.79600 -105.41100 -37.71200 1.000 70.89859  ? 232 ASP   B CA    1 
ATOM   6586 C  C     . ASP   B  2 240 ? 12.90900 -105.50800 -36.18400 1.000 73.91054  ? 232 ASP   B C     1 
ATOM   6587 O  O     . ASP   B  2 240 ? 13.33300 -106.56800 -35.68500 1.000 75.34899  ? 232 ASP   B O     1 
ATOM   6588 C  CB    . ASP   B  2 240 ? 11.44100 -104.88600 -38.20100 1.000 73.70740  ? 232 ASP   B CB    1 
ATOM   6589 C  CG    . ASP   B  2 240 ? 10.22200 -105.61600 -37.66200 1.000 72.74749  ? 232 ASP   B CG    1 
ATOM   6590 O  OD1   . ASP   B  2 240 ? 10.40100 -106.66500 -37.02000 1.000 75.65053  ? 232 ASP   B OD1   1 
ATOM   6591 O  OD2   . ASP   B  2 240 ? 9.09900  -105.12500 -37.89300 1.000 73.42885  ? 232 ASP   B OD2   1 
ATOM   6592 N  N     . GLU   B  2 241 ? 12.55200 -104.42900 -35.48100 1.000 74.69649  ? 233 GLU   B N     1 
ATOM   6593 C  CA    . GLU   B  2 241 ? 12.64200 -104.30000 -34.00000 1.000 71.16039  ? 233 GLU   B CA    1 
ATOM   6594 C  C     . GLU   B  2 241 ? 11.36000 -104.82000 -33.33600 1.000 72.82406  ? 233 GLU   B C     1 
ATOM   6595 O  O     . GLU   B  2 241 ? 11.34400 -104.89600 -32.09200 1.000 74.81286  ? 233 GLU   B O     1 
ATOM   6596 C  CB    . GLU   B  2 241 ? 12.88600 -102.84000 -33.61000 1.000 65.08706  ? 233 GLU   B CB    1 
ATOM   6597 C  CG    . GLU   B  2 241 ? 11.74500 -101.90900 -33.97900 1.000 67.06382  ? 233 GLU   B CG    1 
ATOM   6598 C  CD    . GLU   B  2 241 ? 11.99100 -100.44600 -33.66200 1.000 71.04051  ? 233 GLU   B CD    1 
ATOM   6599 O  OE1   . GLU   B  2 241 ? 13.10100 -100.12400 -33.18900 1.000 71.94541  ? 233 GLU   B OE1   1 
ATOM   6600 O  OE2   . GLU   B  2 241 ? 11.07200 -99.63500  -33.89200 1.000 71.72050  ? 233 GLU   B OE2   1 
ATOM   6601 N  N     . ASN   B  2 242 ? 10.33000 -105.14200 -34.12800 1.000 76.15456  ? 234 ASN   B N     1 
ATOM   6602 C  CA    . ASN   B  2 242 ? 9.00900  -105.63700 -33.65200 1.000 70.97106  ? 234 ASN   B CA    1 
ATOM   6603 C  C     . ASN   B  2 242 ? 8.95000  -107.16600 -33.75300 1.000 74.02644  ? 234 ASN   B C     1 
ATOM   6604 O  O     . ASN   B  2 242 ? 7.90400  -107.73400 -33.38700 1.000 77.53183  ? 234 ASN   B O     1 
ATOM   6605 C  CB    . ASN   B  2 242 ? 7.85600  -105.00500 -34.43500 1.000 73.25039  ? 234 ASN   B CB    1 
ATOM   6606 C  CG    . ASN   B  2 242 ? 6.50600  -105.21500 -33.78200 1.000 74.12139  ? 234 ASN   B CG    1 
ATOM   6607 O  OD1   . ASN   B  2 242 ? 6.39600  -105.21300 -32.55700 1.000 75.13684  ? 234 ASN   B OD1   1 
ATOM   6608 N  ND2   . ASN   B  2 242 ? 5.47300  -105.39600 -34.58900 1.000 72.97034  ? 234 ASN   B ND2   1 
ATOM   6609 N  N     . GLY   B  2 243 ? 10.01800 -107.80500 -34.24400 1.000 74.98497  ? 235 GLY   B N     1 
ATOM   6610 C  CA    . GLY   B  2 243 ? 10.15000 -109.27500 -34.30400 1.000 78.87868  ? 235 GLY   B CA    1 
ATOM   6611 C  C     . GLY   B  2 243 ? 9.70600  -109.86400 -35.63600 1.000 79.16619  ? 235 GLY   B C     1 
ATOM   6612 O  O     . GLY   B  2 243 ? 9.69400  -111.10800 -35.74800 1.000 84.35202  ? 235 GLY   B O     1 
ATOM   6613 N  N     . THR   B  2 244 ? 9.35100  -109.02100 -36.61200 1.000 75.58047  ? 236 THR   B N     1 
ATOM   6614 C  CA    . THR   B  2 244 ? 8.94400  -109.43200 -37.98400 1.000 78.08044  ? 236 THR   B CA    1 
ATOM   6615 C  C     . THR   B  2 244 ? 10.19700 -109.63800 -38.84200 1.000 76.40304  ? 236 THR   B C     1 
ATOM   6616 O  O     . THR   B  2 244 ? 11.04500 -108.72500 -38.87500 1.000 78.47082  ? 236 THR   B O     1 
ATOM   6617 C  CB    . THR   B  2 244 ? 7.99700  -108.40400 -38.62000 1.000 77.26131  ? 236 THR   B CB    1 
ATOM   6618 O  OG1   . THR   B  2 244 ? 6.80800  -108.34500 -37.83200 1.000 79.08199  ? 236 THR   B OG1   1 
ATOM   6619 C  CG2   . THR   B  2 244 ? 7.63200  -108.72800 -40.05200 1.000 75.48256  ? 236 THR   B CG2   1 
ATOM   6620 N  N     . VAL   B  2 245 ? 10.30500 -110.79800 -39.49700 1.000 72.90354  ? 237 VAL   B N     1 
ATOM   6621 C  CA    . VAL   B  2 245 ? 11.32200 -111.09000 -40.55200 1.000 82.43960  ? 237 VAL   B CA    1 
ATOM   6622 C  C     . VAL   B  2 245 ? 10.62100 -110.99400 -41.91400 1.000 81.70130  ? 237 VAL   B C     1 
ATOM   6623 O  O     . VAL   B  2 245 ? 9.57200  -111.64800 -42.08300 1.000 80.25095  ? 237 VAL   B O     1 
ATOM   6624 C  CB    . VAL   B  2 245 ? 11.99100 -112.46200 -40.32800 1.000 79.99379  ? 237 VAL   B CB    1 
ATOM   6625 C  CG1   . VAL   B  2 245 ? 12.80200 -112.92000 -41.53200 1.000 77.11330  ? 237 VAL   B CG1   1 
ATOM   6626 C  CG2   . VAL   B  2 245 ? 12.86200 -112.45200 -39.08100 1.000 75.55101  ? 237 VAL   B CG2   1 
ATOM   6627 N  N     . SER   B  2 246 ? 11.17300 -110.19200 -42.83100 1.000 75.10910  ? 238 SER   B N     1 
ATOM   6628 C  CA    . SER   B  2 246 ? 10.59200 -109.88100 -44.16600 1.000 83.31838  ? 238 SER   B CA    1 
ATOM   6629 C  C     . SER   B  2 246 ? 11.54400 -110.32800 -45.28300 1.000 82.84300  ? 238 SER   B C     1 
ATOM   6630 O  O     . SER   B  2 246 ? 12.76200 -110.10900 -45.14200 1.000 79.60237  ? 238 SER   B O     1 
ATOM   6631 C  CB    . SER   B  2 246 ? 10.27600 -108.41400 -44.27800 1.000 83.47823  ? 238 SER   B CB    1 
ATOM   6632 O  OG    . SER   B  2 246 ? 9.25100  -108.04700 -43.36900 1.000 92.67474  ? 238 SER   B OG    1 
ATOM   6633 N  N     . LEU   B  2 247 ? 10.99400 -110.92000 -46.34900 1.000 84.40657  ? 239 LEU   B N     1 
ATOM   6634 C  CA    . LEU   B  2 247 ? 11.73100 -111.33900 -47.57400 1.000 88.40820  ? 239 LEU   B CA    1 
ATOM   6635 C  C     . LEU   B  2 247 ? 11.57500 -110.25400 -48.64600 1.000 85.21154  ? 239 LEU   B C     1 
ATOM   6636 O  O     . LEU   B  2 247 ? 10.43200 -110.02700 -49.08800 1.000 91.40293  ? 239 LEU   B O     1 
ATOM   6637 C  CB    . LEU   B  2 247 ? 11.17600 -112.68400 -48.05400 1.000 88.92004  ? 239 LEU   B CB    1 
ATOM   6638 C  CG    . LEU   B  2 247 ? 11.69100 -113.18200 -49.40500 1.000 88.66282  ? 239 LEU   B CG    1 
ATOM   6639 C  CD1   . LEU   B  2 247 ? 13.21100 -113.24600 -49.43100 1.000 89.96395  ? 239 LEU   B CD1   1 
ATOM   6640 C  CD2   . LEU   B  2 247 ? 11.09700 -114.54100 -49.73500 1.000 90.47737  ? 239 LEU   B CD2   1 
ATOM   6641 N  N     . VAL   B  2 248 ? 12.68400 -109.62400 -49.04900 1.000 83.33624  ? 240 VAL   B N     1 
ATOM   6642 C  CA    . VAL   B  2 248 ? 12.70500 -108.44000 -49.96100 1.000 93.85918  ? 240 VAL   B CA    1 
ATOM   6643 C  C     . VAL   B  2 248 ? 13.29900 -108.84600 -51.31500 1.000 95.56371  ? 240 VAL   B C     1 
ATOM   6644 O  O     . VAL   B  2 248 ? 14.29700 -109.58900 -51.32700 1.000 91.09654  ? 240 VAL   B O     1 
ATOM   6645 C  CB    . VAL   B  2 248 ? 13.49500 -107.27000 -49.34200 1.000 87.41791  ? 240 VAL   B CB    1 
ATOM   6646 C  CG1   . VAL   B  2 248 ? 13.83200 -106.19600 -50.36800 1.000 85.77862  ? 240 VAL   B CG1   1 
ATOM   6647 C  CG2   . VAL   B  2 248 ? 12.75500 -106.66200 -48.16400 1.000 84.93515  ? 240 VAL   B CG2   1 
ATOM   6648 N  N     . ASP   B  2 249 ? 12.70200 -108.34200 -52.40000 1.000 97.30579  ? 241 ASP   B N     1 
ATOM   6649 C  CA    . ASP   B  2 249 ? 13.24300 -108.39100 -53.78500 1.000 105.46086 ? 241 ASP   B CA    1 
ATOM   6650 C  C     . ASP   B  2 249 ? 13.67800 -106.97000 -54.16200 1.000 113.44686 ? 241 ASP   B C     1 
ATOM   6651 O  O     . ASP   B  2 249 ? 12.81400 -106.07100 -54.14000 1.000 120.72471 ? 241 ASP   B O     1 
ATOM   6652 C  CB    . ASP   B  2 249 ? 12.20300 -108.96200 -54.75500 1.000 112.73871 ? 241 ASP   B CB    1 
ATOM   6653 C  CG    . ASP   B  2 249 ? 12.74700 -109.34000 -56.12400 1.000 117.21480 ? 241 ASP   B CG    1 
ATOM   6654 O  OD1   . ASP   B  2 249 ? 13.69700 -108.67700 -56.58600 1.000 119.91755 ? 241 ASP   B OD1   1 
ATOM   6655 O  OD2   . ASP   B  2 249 ? 12.21100 -110.29700 -56.71800 1.000 109.71274 ? 241 ASP   B OD2   1 
ATOM   6656 N  N     . THR   B  2 250 ? 14.96600 -106.77400 -54.46600 1.000 116.22857 ? 242 THR   B N     1 
ATOM   6657 C  CA    . THR   B  2 250 ? 15.54900 -105.47000 -54.88600 1.000 117.87380 ? 242 THR   B CA    1 
ATOM   6658 C  C     . THR   B  2 250 ? 14.94200 -105.06100 -56.23400 1.000 126.67281 ? 242 THR   B C     1 
ATOM   6659 O  O     . THR   B  2 250 ? 14.64100 -103.86200 -56.40800 1.000 125.36431 ? 242 THR   B O     1 
ATOM   6660 C  CB    . THR   B  2 250 ? 17.08100 -105.52900 -54.96900 1.000 108.84773 ? 242 THR   B CB    1 
ATOM   6661 O  OG1   . THR   B  2 250 ? 17.44800 -106.53100 -55.91700 1.000 120.94759 ? 242 THR   B OG1   1 
ATOM   6662 C  CG2   . THR   B  2 250 ? 17.73700 -105.82500 -53.63900 1.000 98.69448  ? 242 THR   B CG2   1 
ATOM   6663 N  N     . LYS   B  2 251 ? 14.76200 -106.03600 -57.13200 1.000 138.96783 ? 243 LYS   B N     1 
ATOM   6664 C  CA    . LYS   B  2 251 ? 14.25300 -105.85100 -58.51900 1.000 142.41608 ? 243 LYS   B CA    1 
ATOM   6665 C  C     . LYS   B  2 251 ? 12.80300 -105.35100 -58.48100 1.000 146.20103 ? 243 LYS   B C     1 
ATOM   6666 O  O     . LYS   B  2 251 ? 12.47800 -104.43700 -59.26600 1.000 149.34002 ? 243 LYS   B O     1 
ATOM   6667 C  CB    . LYS   B  2 251 ? 14.35600 -107.17100 -59.29200 1.000 140.89263 ? 243 LYS   B CB    1 
ATOM   6668 C  CG    . LYS   B  2 251 ? 14.34700 -107.04200 -60.80900 1.000 148.35351 ? 243 LYS   B CG    1 
ATOM   6669 C  CD    . LYS   B  2 251 ? 14.63500 -108.34800 -61.51900 1.000 150.60451 ? 243 LYS   B CD    1 
ATOM   6670 C  CE    . LYS   B  2 251 ? 14.93000 -108.17100 -62.99300 1.000 153.69940 ? 243 LYS   B CE    1 
ATOM   6671 N  NZ    . LYS   B  2 251 ? 15.04200 -109.47500 -63.68800 1.000 151.53192 ? 243 LYS   B NZ    1 
ATOM   6672 N  N     . SER   B  2 252 ? 11.97400 -105.92700 -57.60200 1.000 135.66237 ? 244 SER   B N     1 
ATOM   6673 C  CA    . SER   B  2 252 ? 10.50900 -105.67700 -57.50000 1.000 137.71102 ? 244 SER   B CA    1 
ATOM   6674 C  C     . SER   B  2 252 ? 10.21800 -104.50100 -56.55600 1.000 137.34656 ? 244 SER   B C     1 
ATOM   6675 O  O     . SER   B  2 252 ? 9.10800  -103.94100 -56.65200 1.000 139.19704 ? 244 SER   B O     1 
ATOM   6676 C  CB    . SER   B  2 252 ? 9.78600  -106.92700 -57.05900 1.000 138.58738 ? 244 SER   B CB    1 
ATOM   6677 O  OG    . SER   B  2 252 ? 8.41400  -106.87600 -57.42300 1.000 145.29434 ? 244 SER   B OG    1 
ATOM   6678 N  N     . THR   B  2 253 ? 11.16000 -104.17700 -55.65900 1.000 135.72990 ? 245 THR   B N     1 
ATOM   6679 C  CA    . THR   B  2 253 ? 11.12500 -103.04300 -54.68600 1.000 137.07805 ? 245 THR   B CA    1 
ATOM   6680 C  C     . THR   B  2 253 ? 9.84900  -103.09700 -53.82500 1.000 140.01666 ? 245 THR   B C     1 
ATOM   6681 O  O     . THR   B  2 253 ? 9.46900  -102.04300 -53.27000 1.000 134.97838 ? 245 THR   B O     1 
ATOM   6682 C  CB    . THR   B  2 253 ? 11.34400 -101.69900 -55.40400 1.000 139.27301 ? 245 THR   B CB    1 
ATOM   6683 O  OG1   . THR   B  2 253 ? 11.82600 -100.77100 -54.43100 1.000 136.86531 ? 245 THR   B OG1   1 
ATOM   6684 C  CG2   . THR   B  2 253 ? 10.11600 -101.12400 -56.08100 1.000 132.02335 ? 245 THR   B CG2   1 
ATOM   6685 N  N     . SER   B  2 254 ? 9.24800  -104.28400 -53.67200 1.000 145.09223 ? 246 SER   B N     1 
ATOM   6686 C  CA    . SER   B  2 254 ? 8.01800  -104.53500 -52.87200 1.000 138.91940 ? 246 SER   B CA    1 
ATOM   6687 C  C     . SER   B  2 254 ? 8.18300  -105.83600 -52.07700 1.000 132.72378 ? 246 SER   B C     1 
ATOM   6688 O  O     . SER   B  2 254 ? 8.66900  -106.82800 -52.65700 1.000 138.97357 ? 246 SER   B O     1 
ATOM   6689 C  CB    . SER   B  2 254 ? 6.79500  -104.57400 -53.75600 1.000 139.35989 ? 246 SER   B CB    1 
ATOM   6690 O  OG    . SER   B  2 254 ? 5.61100  -104.68600 -52.97800 1.000 136.71340 ? 246 SER   B OG    1 
ATOM   6691 N  N     . CYS   B  2 255 ? 7.80200  -105.82200 -50.79600 1.000 131.57000 ? 247 CYS   B N     1 
ATOM   6692 C  CA    . CYS   B  2 255 ? 7.96000  -106.95400 -49.84200 1.000 127.79082 ? 247 CYS   B CA    1 
ATOM   6693 C  C     . CYS   B  2 255 ? 6.98200  -108.07800 -50.20500 1.000 125.66758 ? 247 CYS   B C     1 
ATOM   6694 O  O     . CYS   B  2 255 ? 5.76100  -107.87200 -50.05100 1.000 124.85769 ? 247 CYS   B O     1 
ATOM   6695 C  CB    . CYS   B  2 255 ? 7.74300  -106.49200 -48.40600 1.000 127.51297 ? 247 CYS   B CB    1 
ATOM   6696 S  SG    . CYS   B  2 255 ? 8.98200  -105.28800 -47.86200 1.000 128.19791 ? 247 CYS   B SG    1 
ATOM   6697 N  N     . VAL   B  2 256 ? 7.51300  -109.22000 -50.65900 1.000 125.83977 ? 248 VAL   B N     1 
ATOM   6698 C  CA    . VAL   B  2 256 ? 6.72900  -110.36200 -51.22300 1.000 127.37898 ? 248 VAL   B CA    1 
ATOM   6699 C  C     . VAL   B  2 256 ? 6.00100  -111.09500 -50.08600 1.000 121.59464 ? 248 VAL   B C     1 
ATOM   6700 O  O     . VAL   B  2 256 ? 4.83400  -111.48300 -50.29900 1.000 124.87706 ? 248 VAL   B O     1 
ATOM   6701 C  CB    . VAL   B  2 256 ? 7.60900  -111.31800 -52.05800 1.000 121.92728 ? 248 VAL   B CB    1 
ATOM   6702 C  CG1   . VAL   B  2 256 ? 8.25100  -110.60100 -53.23600 1.000 123.86412 ? 248 VAL   B CG1   1 
ATOM   6703 C  CG2   . VAL   B  2 256 ? 8.67000  -112.02900 -51.22800 1.000 115.65898 ? 248 VAL   B CG2   1 
ATOM   6704 N  N     . LEU   B  2 257 ? 6.65600  -111.27800 -48.93300 1.000 110.08238 ? 249 LEU   B N     1 
ATOM   6705 C  CA    . LEU   B  2 257 ? 6.05000  -111.91600 -47.73200 1.000 107.03161 ? 249 LEU   B CA    1 
ATOM   6706 C  C     . LEU   B  2 257 ? 6.87000  -111.58600 -46.47900 1.000 101.63575 ? 249 LEU   B C     1 
ATOM   6707 O  O     . LEU   B  2 257 ? 8.11600  -111.60200 -46.55400 1.000 96.02154  ? 249 LEU   B O     1 
ATOM   6708 C  CB    . LEU   B  2 257 ? 5.96900  -113.43200 -47.94400 1.000 110.07672 ? 249 LEU   B CB    1 
ATOM   6709 C  CG    . LEU   B  2 257 ? 5.40100  -114.24000 -46.77400 1.000 111.38793 ? 249 LEU   B CG    1 
ATOM   6710 C  CD1   . LEU   B  2 257 ? 3.99000  -113.79000 -46.41400 1.000 102.10148 ? 249 LEU   B CD1   1 
ATOM   6711 C  CD2   . LEU   B  2 257 ? 5.41700  -115.73000 -47.09000 1.000 110.32418 ? 249 LEU   B CD2   1 
ATOM   6712 N  N     . SER   B  2 258 ? 6.17000  -111.30700 -45.37400 1.000 98.81054  ? 250 SER   B N     1 
ATOM   6713 C  CA    . SER   B  2 258 ? 6.72300  -111.13300 -44.00600 1.000 93.30010  ? 250 SER   B CA    1 
ATOM   6714 C  C     . SER   B  2 258 ? 5.99400  -112.08100 -43.04700 1.000 93.58609  ? 250 SER   B C     1 
ATOM   6715 O  O     . SER   B  2 258 ? 4.95700  -112.65200 -43.45200 1.000 94.21971  ? 250 SER   B O     1 
ATOM   6716 C  CB    . SER   B  2 258 ? 6.60900  -109.69800 -43.56400 1.000 87.62859  ? 250 SER   B CB    1 
ATOM   6717 O  OG    . SER   B  2 258 ? 5.24900  -109.29400 -43.50000 1.000 94.70701  ? 250 SER   B OG    1 
ATOM   6718 N  N     . SER   B  2 259 ? 6.52400  -112.24500 -41.83000 1.000 93.12548  ? 251 SER   B N     1 
ATOM   6719 C  CA    . SER   B  2 259 ? 5.95300  -113.10400 -40.75700 1.000 89.40632  ? 251 SER   B CA    1 
ATOM   6720 C  C     . SER   B  2 259 ? 6.45200  -112.63700 -39.38400 1.000 85.42040  ? 251 SER   B C     1 
ATOM   6721 O  O     . SER   B  2 259 ? 7.62300  -112.21400 -39.29000 1.000 83.41887  ? 251 SER   B O     1 
ATOM   6722 C  CB    . SER   B  2 259 ? 6.28300  -114.55500 -41.00100 1.000 88.43543  ? 251 SER   B CB    1 
ATOM   6723 O  OG    . SER   B  2 259 ? 5.55200  -115.39600 -40.12200 1.000 96.19730  ? 251 SER   B OG    1 
ATOM   6724 N  N     . ALA   B  2 260 ? 5.58700  -112.70700 -38.36600 1.000 86.96522  ? 252 ALA   B N     1 
ATOM   6725 C  CA    . ALA   B  2 260 ? 5.90900  -112.41900 -36.94700 1.000 86.92478  ? 252 ALA   B CA    1 
ATOM   6726 C  C     . ALA   B  2 260 ? 6.55600  -113.66100 -36.32100 1.000 84.50177  ? 252 ALA   B C     1 
ATOM   6727 O  O     . ALA   B  2 260 ? 5.81400  -114.52100 -35.80500 1.000 85.94298  ? 252 ALA   B O     1 
ATOM   6728 C  CB    . ALA   B  2 260 ? 4.66200  -112.00600 -36.20100 1.000 89.11916  ? 252 ALA   B CB    1 
ATOM   6729 N  N     . VAL   B  2 261 ? 7.88900  -113.74400 -36.37600 1.000 86.78990  ? 253 VAL   B N     1 
ATOM   6730 C  CA    . VAL   B  2 261 ? 8.69000  -114.92300 -35.92500 1.000 89.53836  ? 253 VAL   B CA    1 
ATOM   6731 C  C     . VAL   B  2 261 ? 8.91800  -114.80100 -34.41300 1.000 92.56915  ? 253 VAL   B C     1 
ATOM   6732 O  O     . VAL   B  2 261 ? 8.56300  -115.74700 -33.68100 1.000 92.00214  ? 253 VAL   B O     1 
ATOM   6733 C  CB    . VAL   B  2 261 ? 10.03000 -115.03000 -36.68400 1.000 85.48217  ? 253 VAL   B CB    1 
ATOM   6734 C  CG1   . VAL   B  2 261 ? 10.75700 -116.32800 -36.36500 1.000 88.34144  ? 253 VAL   B CG1   1 
ATOM   6735 C  CG2   . VAL   B  2 261 ? 9.85500  -114.88300 -38.18800 1.000 82.68555  ? 253 VAL   B CG2   1 
ATOM   6736 N  N     . HIS   B  2 262 ? 9.49100  -113.67400 -33.98000 1.000 90.33405  ? 254 HIS   B N     1 
ATOM   6737 C  CA    . HIS   B  2 262 ? 9.85800  -113.37500 -32.56900 1.000 89.93514  ? 254 HIS   B CA    1 
ATOM   6738 C  C     . HIS   B  2 262 ? 8.84700  -112.39900 -31.95700 1.000 87.16817  ? 254 HIS   B C     1 
ATOM   6739 O  O     . HIS   B  2 262 ? 8.15700  -111.69500 -32.72100 1.000 84.38706  ? 254 HIS   B O     1 
ATOM   6740 C  CB    . HIS   B  2 262 ? 11.28400 -112.81500 -32.49900 1.000 87.77883  ? 254 HIS   B CB    1 
ATOM   6741 C  CG    . HIS   B  2 262 ? 12.30700 -113.70000 -33.12700 1.000 86.77018  ? 254 HIS   B CG    1 
ATOM   6742 N  ND1   . HIS   B  2 262 ? 12.81400 -114.81000 -32.48300 1.000 90.88241  ? 254 HIS   B ND1   1 
ATOM   6743 C  CD2   . HIS   B  2 262 ? 12.92800 -113.63800 -34.32300 1.000 86.04354  ? 254 HIS   B CD2   1 
ATOM   6744 C  CE1   . HIS   B  2 262 ? 13.70100 -115.39800 -33.26000 1.000 87.42683  ? 254 HIS   B CE1   1 
ATOM   6745 N  NE2   . HIS   B  2 262 ? 13.78900 -114.69800 -34.39400 1.000 88.89525  ? 254 HIS   B NE2   1 
ATOM   6746 N  N     . SER   B  2 263 ? 8.77400  -112.37000 -30.62400 1.000 89.85061  ? 255 SER   B N     1 
ATOM   6747 C  CA    . SER   B  2 263 ? 7.92700  -111.44400 -29.82900 1.000 90.93291  ? 255 SER   B CA    1 
ATOM   6748 C  C     . SER   B  2 263 ? 8.67100  -110.12200 -29.60500 1.000 93.87825  ? 255 SER   B C     1 
ATOM   6749 O  O     . SER   B  2 263 ? 7.99900  -109.12500 -29.27200 1.000 95.21672  ? 255 SER   B O     1 
ATOM   6750 C  CB    . SER   B  2 263 ? 7.51800  -112.07500 -28.52300 1.000 88.64240  ? 255 SER   B CB    1 
ATOM   6751 O  OG    . SER   B  2 263 ? 8.65700  -112.46400 -27.77000 1.000 91.54851  ? 255 SER   B OG    1 
ATOM   6752 N  N     . GLN   B  2 264 ? 9.99900  -110.11700 -29.78200 1.000 98.42801  ? 256 GLN   B N     1 
ATOM   6753 C  CA    . GLN   B  2 264 ? 10.87700 -108.92700 -29.59900 1.000 90.82247  ? 256 GLN   B CA    1 
ATOM   6754 C  C     . GLN   B  2 264 ? 11.85600 -108.81000 -30.77600 1.000 84.55258  ? 256 GLN   B C     1 
ATOM   6755 O  O     . GLN   B  2 264 ? 11.85300 -109.70700 -31.64000 1.000 85.90483  ? 256 GLN   B O     1 
ATOM   6756 C  CB    . GLN   B  2 264 ? 11.61500 -109.01400 -28.26100 1.000 85.49251  ? 256 GLN   B CB    1 
ATOM   6757 C  CG    . GLN   B  2 264 ? 10.68000 -109.03600 -27.06000 1.000 94.49049  ? 256 GLN   B CG    1 
ATOM   6758 C  CD    . GLN   B  2 264 ? 11.25200 -108.30400 -25.87100 1.000 97.11418  ? 256 GLN   B CD    1 
ATOM   6759 O  OE1   . GLN   B  2 264 ? 12.40900 -108.49500 -25.49900 1.000 97.90879  ? 256 GLN   B OE1   1 
ATOM   6760 N  NE2   . GLN   B  2 264 ? 10.43600 -107.46000 -25.25900 1.000 97.06711  ? 256 GLN   B NE2   1 
ATOM   6761 N  N     . CYS   B  2 265 ? 12.65700 -107.73700 -30.78500 1.000 78.61414  ? 257 CYS   B N     1 
ATOM   6762 C  CA    . CYS   B  2 265 ? 13.57700 -107.30700 -31.87700 1.000 77.31636  ? 257 CYS   B CA    1 
ATOM   6763 C  C     . CYS   B  2 265 ? 14.38800 -108.48400 -32.43100 1.000 79.97190  ? 257 CYS   B C     1 
ATOM   6764 O  O     . CYS   B  2 265 ? 14.82800 -109.32100 -31.62700 1.000 81.06592  ? 257 CYS   B O     1 
ATOM   6765 C  CB    . CYS   B  2 265 ? 14.54000 -106.23400 -31.38000 1.000 77.66027  ? 257 CYS   B CB    1 
ATOM   6766 S  SG    . CYS   B  2 265 ? 16.00200 -106.02600 -32.43000 1.000 81.66641  ? 257 CYS   B SG    1 
ATOM   6767 N  N     . VAL   B  2 266 ? 14.60200 -108.49800 -33.75500 1.000 79.49009  ? 258 VAL   B N     1 
ATOM   6768 C  CA    . VAL   B  2 266 ? 15.39400 -109.52000 -34.50600 1.000 74.86960  ? 258 VAL   B CA    1 
ATOM   6769 C  C     . VAL   B  2 266 ? 16.83100 -109.00300 -34.65800 1.000 74.41083  ? 258 VAL   B C     1 
ATOM   6770 O  O     . VAL   B  2 266 ? 17.04900 -108.11300 -35.50300 1.000 77.50039  ? 258 VAL   B O     1 
ATOM   6771 C  CB    . VAL   B  2 266 ? 14.76800 -109.82100 -35.88200 1.000 76.81080  ? 258 VAL   B CB    1 
ATOM   6772 C  CG1   . VAL   B  2 266 ? 15.42200 -111.02300 -36.54800 1.000 81.61330  ? 258 VAL   B CG1   1 
ATOM   6773 C  CG2   . VAL   B  2 266 ? 13.26200 -110.01700 -35.79900 1.000 78.33890  ? 258 VAL   B CG2   1 
ATOM   6774 N  N     . THR   B  2 267 ? 17.77200 -109.55000 -33.88200 1.000 75.62394  ? 259 THR   B N     1 
ATOM   6775 C  CA    . THR   B  2 267 ? 19.15700 -109.02500 -33.73100 1.000 76.93975  ? 259 THR   B CA    1 
ATOM   6776 C  C     . THR   B  2 267 ? 20.09400 -109.63100 -34.78300 1.000 75.22092  ? 259 THR   B C     1 
ATOM   6777 O  O     . THR   B  2 267 ? 21.14900 -109.02100 -35.03600 1.000 80.05708  ? 259 THR   B O     1 
ATOM   6778 C  CB    . THR   B  2 267 ? 19.69600 -109.28500 -32.31900 1.000 73.98847  ? 259 THR   B CB    1 
ATOM   6779 O  OG1   . THR   B  2 267 ? 19.60500 -110.68700 -32.06500 1.000 81.92901  ? 259 THR   B OG1   1 
ATOM   6780 C  CG2   . THR   B  2 267 ? 18.94200 -108.51400 -31.25800 1.000 75.63216  ? 259 THR   B CG2   1 
ATOM   6781 N  N     . GLY   B  2 268 ? 19.73900 -110.78500 -35.35700 1.000 74.17131  ? 260 GLY   B N     1 
ATOM   6782 C  CA    . GLY   B  2 268 ? 20.57600 -111.48600 -36.35000 1.000 76.29218  ? 260 GLY   B CA    1 
ATOM   6783 C  C     . GLY   B  2 268 ? 19.76000 -112.36000 -37.28700 1.000 77.46008  ? 260 GLY   B C     1 
ATOM   6784 O  O     . GLY   B  2 268 ? 18.72600 -112.90400 -36.84800 1.000 79.43513  ? 260 GLY   B O     1 
ATOM   6785 N  N     . LEU   B  2 269 ? 20.21200 -112.47800 -38.53900 1.000 76.48979  ? 261 LEU   B N     1 
ATOM   6786 C  CA    . LEU   B  2 269 ? 19.64700 -113.39100 -39.56800 1.000 79.35766  ? 261 LEU   B CA    1 
ATOM   6787 C  C     . LEU   B  2 269 ? 20.80600 -114.04100 -40.33100 1.000 84.61153  ? 261 LEU   B C     1 
ATOM   6788 O  O     . LEU   B  2 269 ? 21.61300 -113.29600 -40.92100 1.000 85.26068  ? 261 LEU   B O     1 
ATOM   6789 C  CB    . LEU   B  2 269 ? 18.72800 -112.59900 -40.50500 1.000 75.98123  ? 261 LEU   B CB    1 
ATOM   6790 C  CG    . LEU   B  2 269 ? 17.33600 -112.28800 -39.95600 1.000 75.67650  ? 261 LEU   B CG    1 
ATOM   6791 C  CD1   . LEU   B  2 269 ? 16.68800 -111.15000 -40.72800 1.000 77.21001  ? 261 LEU   B CD1   1 
ATOM   6792 C  CD2   . LEU   B  2 269 ? 16.44700 -113.52100 -39.98600 1.000 79.21200  ? 261 LEU   B CD2   1 
ATOM   6793 N  N     . VAL   B  2 270 ? 20.89200 -115.37400 -40.29400 1.000 81.63867  ? 262 VAL   B N     1 
ATOM   6794 C  CA    . VAL   B  2 270 ? 22.00700 -116.16900 -40.89200 1.000 85.39195  ? 262 VAL   B CA    1 
ATOM   6795 C  C     . VAL   B  2 270 ? 21.40800 -117.33400 -41.68800 1.000 85.85163  ? 262 VAL   B C     1 
ATOM   6796 O  O     . VAL   B  2 270 ? 20.59900 -118.08800 -41.11400 1.000 86.11128  ? 262 VAL   B O     1 
ATOM   6797 C  CB    . VAL   B  2 270 ? 22.98300 -116.66300 -39.80700 1.000 88.75622  ? 262 VAL   B CB    1 
ATOM   6798 C  CG1   . VAL   B  2 270 ? 24.14300 -117.45100 -40.39900 1.000 83.82376  ? 262 VAL   B CG1   1 
ATOM   6799 C  CG2   . VAL   B  2 270 ? 23.49900 -115.51400 -38.95200 1.000 88.07478  ? 262 VAL   B CG2   1 
ATOM   6800 N  N     . PHE   B  2 271 ? 21.80100 -117.46600 -42.95800 1.000 92.66335  ? 263 PHE   B N     1 
ATOM   6801 C  CA    . PHE   B  2 271 ? 21.36000 -118.54500 -43.88000 1.000 89.89350  ? 263 PHE   B CA    1 
ATOM   6802 C  C     . PHE   B  2 271 ? 22.25500 -119.77500 -43.69200 1.000 90.21551  ? 263 PHE   B C     1 
ATOM   6803 O  O     . PHE   B  2 271 ? 23.43900 -119.61600 -43.32900 1.000 89.27575  ? 263 PHE   B O     1 
ATOM   6804 C  CB    . PHE   B  2 271 ? 21.37500 -118.05800 -45.33200 1.000 89.99103  ? 263 PHE   B CB    1 
ATOM   6805 C  CG    . PHE   B  2 271 ? 20.15500 -117.27500 -45.74200 1.000 85.06911  ? 263 PHE   B CG    1 
ATOM   6806 C  CD1   . PHE   B  2 271 ? 18.96200 -117.92300 -46.02600 1.000 86.37749  ? 263 PHE   B CD1   1 
ATOM   6807 C  CD2   . PHE   B  2 271 ? 20.19800 -115.89400 -45.85400 1.000 82.79972  ? 263 PHE   B CD2   1 
ATOM   6808 C  CE1   . PHE   B  2 271 ? 17.83800 -117.20600 -46.40800 1.000 85.39617  ? 263 PHE   B CE1   1 
ATOM   6809 C  CE2   . PHE   B  2 271 ? 19.07300 -115.17800 -46.23600 1.000 81.83321  ? 263 PHE   B CE2   1 
ATOM   6810 C  CZ    . PHE   B  2 271 ? 17.89600 -115.83600 -46.51200 1.000 83.11347  ? 263 PHE   B CZ    1 
ATOM   6811 N  N     . SER   B  2 272 ? 21.69500 -120.96500 -43.93200 1.000 96.34508  ? 264 SER   B N     1 
ATOM   6812 C  CA    . SER   B  2 272 ? 22.40100 -122.27200 -43.86200 1.000 100.59101 ? 264 SER   B CA    1 
ATOM   6813 C  C     . SER   B  2 272 ? 23.18400 -122.50300 -45.15200 1.000 103.87559 ? 264 SER   B C     1 
ATOM   6814 O  O     . SER   B  2 272 ? 22.88600 -121.89100 -46.17600 1.000 102.13163 ? 264 SER   B O     1 
ATOM   6815 C  CB    . SER   B  2 272 ? 21.43800 -123.40400 -43.59900 1.000 100.92246 ? 264 SER   B CB    1 
ATOM   6816 O  OG    . SER   B  2 272 ? 20.74700 -123.77200 -44.78500 1.000 103.38644 ? 264 SER   B OG    1 
ATOM   6817 N  N     . PRO   B  2 273 ? 24.20600 -123.39200 -45.14600 1.000 108.61073 ? 265 PRO   B N     1 
ATOM   6818 C  CA    . PRO   B  2 273 ? 24.97000 -123.70800 -46.35400 1.000 112.58542 ? 265 PRO   B CA    1 
ATOM   6819 C  C     . PRO   B  2 273 ? 24.27100 -124.70700 -47.29200 1.000 111.81976 ? 265 PRO   B C     1 
ATOM   6820 O  O     . PRO   B  2 273 ? 24.80800 -124.95300 -48.35600 1.000 112.15160 ? 265 PRO   B O     1 
ATOM   6821 C  CB    . PRO   B  2 273 ? 26.27700 -124.32100 -45.81400 1.000 116.69876 ? 265 PRO   B CB    1 
ATOM   6822 C  CG    . PRO   B  2 273 ? 26.20100 -124.17100 -44.29900 1.000 108.58342 ? 265 PRO   B CG    1 
ATOM   6823 C  CD    . PRO   B  2 273 ? 24.72400 -124.11300 -43.97700 1.000 104.94129 ? 265 PRO   B CD    1 
ATOM   6824 N  N     . HIS   B  2 274 ? 23.11500 -125.25200 -46.88200 1.000 113.25694 ? 266 HIS   B N     1 
ATOM   6825 C  CA    . HIS   B  2 274 ? 22.28200 -126.22200 -47.64900 1.000 110.54362 ? 266 HIS   B CA    1 
ATOM   6826 C  C     . HIS   B  2 274 ? 22.05400 -125.72100 -49.08100 1.000 110.67829 ? 266 HIS   B C     1 
ATOM   6827 O  O     . HIS   B  2 274 ? 22.03100 -124.48800 -49.27700 1.000 107.98849 ? 266 HIS   B O     1 
ATOM   6828 C  CB    . HIS   B  2 274 ? 20.92900 -126.45400 -46.95600 1.000 109.66484 ? 266 HIS   B CB    1 
ATOM   6829 C  CG    . HIS   B  2 274 ? 20.97900 -127.33700 -45.75500 1.000 112.32680 ? 266 HIS   B CG    1 
ATOM   6830 N  ND1   . HIS   B  2 274 ? 21.03100 -128.71400 -45.85400 1.000 111.81216 ? 266 HIS   B ND1   1 
ATOM   6831 C  CD2   . HIS   B  2 274 ? 20.95100 -127.05100 -44.43500 1.000 111.95399 ? 266 HIS   B CD2   1 
ATOM   6832 C  CE1   . HIS   B  2 274 ? 21.05000 -129.23900 -44.64600 1.000 114.34634 ? 266 HIS   B CE1   1 
ATOM   6833 N  NE2   . HIS   B  2 274 ? 21.00000 -128.23900 -43.75700 1.000 118.91448 ? 266 HIS   B NE2   1 
ATOM   6834 N  N     . SER   B  2 275 ? 21.87000 -126.64600 -50.03200 1.000 113.03864 ? 267 SER   B N     1 
ATOM   6835 C  CA    . SER   B  2 275 ? 21.51100 -126.35500 -51.44700 1.000 112.03283 ? 267 SER   B CA    1 
ATOM   6836 C  C     . SER   B  2 275 ? 20.25000 -125.48100 -51.47500 1.000 113.91547 ? 267 SER   B C     1 
ATOM   6837 O  O     . SER   B  2 275 ? 20.28500 -124.41500 -52.11300 1.000 110.79395 ? 267 SER   B O     1 
ATOM   6838 C  CB    . SER   B  2 275 ? 21.33300 -127.62400 -52.24900 1.000 113.34995 ? 267 SER   B CB    1 
ATOM   6839 O  OG    . SER   B  2 275 ? 22.56900 -128.30600 -52.40500 1.000 115.49902 ? 267 SER   B OG    1 
ATOM   6840 N  N     . VAL   B  2 276 ? 19.18700 -125.91400 -50.78800 1.000 110.86410 ? 268 VAL   B N     1 
ATOM   6841 C  CA    . VAL   B  2 276 ? 17.97000 -125.09100 -50.50700 1.000 108.97654 ? 268 VAL   B CA    1 
ATOM   6842 C  C     . VAL   B  2 276 ? 18.05600 -124.63500 -49.04900 1.000 108.21232 ? 268 VAL   B C     1 
ATOM   6843 O  O     . VAL   B  2 276 ? 17.75800 -125.39600 -48.13200 1.000 111.56917 ? 268 VAL   B O     1 
ATOM   6844 C  CB    . VAL   B  2 276 ? 16.66500 -125.84700 -50.84000 1.000 109.30050 ? 268 VAL   B CB    1 
ATOM   6845 C  CG1   . VAL   B  2 276 ? 16.41000 -127.05300 -49.94300 1.000 109.59147 ? 268 VAL   B CG1   1 
ATOM   6846 C  CG2   . VAL   B  2 276 ? 15.46300 -124.91500 -50.83500 1.000 105.91912 ? 268 VAL   B CG2   1 
ATOM   6847 N  N     . PRO   B  2 277 ? 18.48800 -123.37900 -48.78500 1.000 105.43305 ? 269 PRO   B N     1 
ATOM   6848 C  CA    . PRO   B  2 277 ? 18.97400 -122.99400 -47.45900 1.000 104.27490 ? 269 PRO   B CA    1 
ATOM   6849 C  C     . PRO   B  2 277 ? 17.87200 -122.71200 -46.42800 1.000 102.10513 ? 269 PRO   B C     1 
ATOM   6850 O  O     . PRO   B  2 277 ? 16.81000 -122.25500 -46.81000 1.000 106.53256 ? 269 PRO   B O     1 
ATOM   6851 C  CB    . PRO   B  2 277 ? 19.76400 -121.71300 -47.76300 1.000 101.78249 ? 269 PRO   B CB    1 
ATOM   6852 C  CG    . PRO   B  2 277 ? 19.00100 -121.08300 -48.90700 1.000 101.08291 ? 269 PRO   B CG    1 
ATOM   6853 C  CD    . PRO   B  2 277 ? 18.51400 -122.25600 -49.73600 1.000 107.85402 ? 269 PRO   B CD    1 
ATOM   6854 N  N     . PHE   B  2 278 ? 18.16000 -122.99900 -45.15400 1.000 98.48320  ? 270 PHE   B N     1 
ATOM   6855 C  CA    . PHE   B  2 278 ? 17.33800 -122.61100 -43.97900 1.000 95.03309  ? 270 PHE   B CA    1 
ATOM   6856 C  C     . PHE   B  2 278 ? 17.74600 -121.20600 -43.53000 1.000 91.56177  ? 270 PHE   B C     1 
ATOM   6857 O  O     . PHE   B  2 278 ? 18.92100 -120.83500 -43.71600 1.000 90.74580  ? 270 PHE   B O     1 
ATOM   6858 C  CB    . PHE   B  2 278 ? 17.51500 -123.59800 -42.82200 1.000 97.81904  ? 270 PHE   B CB    1 
ATOM   6859 C  CG    . PHE   B  2 278 ? 16.88300 -124.95000 -43.03000 1.000 104.74898 ? 270 PHE   B CG    1 
ATOM   6860 C  CD1   . PHE   B  2 278 ? 15.54800 -125.06400 -43.39200 1.000 106.16035 ? 270 PHE   B CD1   1 
ATOM   6861 C  CD2   . PHE   B  2 278 ? 17.61600 -126.11300 -42.84100 1.000 109.82138 ? 270 PHE   B CD2   1 
ATOM   6862 C  CE1   . PHE   B  2 278 ? 14.96800 -126.30900 -43.58000 1.000 112.30325 ? 270 PHE   B CE1   1 
ATOM   6863 C  CE2   . PHE   B  2 278 ? 17.03300 -127.35700 -43.02600 1.000 113.68848 ? 270 PHE   B CE2   1 
ATOM   6864 C  CZ    . PHE   B  2 278 ? 15.71000 -127.45300 -43.39500 1.000 116.08737 ? 270 PHE   B CZ    1 
ATOM   6865 N  N     . LEU   B  2 279 ? 16.80100 -120.46300 -42.95000 1.000 90.02256  ? 271 LEU   B N     1 
ATOM   6866 C  CA    . LEU   B  2 279 ? 17.02500 -119.11200 -42.37200 1.000 87.17406  ? 271 LEU   B CA    1 
ATOM   6867 C  C     . LEU   B  2 279 ? 16.92300 -119.20400 -40.84500 1.000 87.03853  ? 271 LEU   B C     1 
ATOM   6868 O  O     . LEU   B  2 279 ? 15.82000 -119.49500 -40.34400 1.000 87.81937  ? 271 LEU   B O     1 
ATOM   6869 C  CB    . LEU   B  2 279 ? 15.98900 -118.14100 -42.94800 1.000 86.29930  ? 271 LEU   B CB    1 
ATOM   6870 C  CG    . LEU   B  2 279 ? 16.06300 -116.70100 -42.43600 1.000 84.02350  ? 271 LEU   B CG    1 
ATOM   6871 C  CD1   . LEU   B  2 279 ? 17.39900 -116.06100 -42.78500 1.000 82.73982  ? 271 LEU   B CD1   1 
ATOM   6872 C  CD2   . LEU   B  2 279 ? 14.91400 -115.87300 -42.99100 1.000 82.76114  ? 271 LEU   B CD2   1 
ATOM   6873 N  N     . ALA   B  2 280 ? 18.04100 -118.98100 -40.14900 1.000 86.31399  ? 272 ALA   B N     1 
ATOM   6874 C  CA    . ALA   B  2 280 ? 18.11800 -118.84600 -38.67600 1.000 85.98708  ? 272 ALA   B CA    1 
ATOM   6875 C  C     . ALA   B  2 280 ? 17.88500 -117.37700 -38.30500 1.000 90.03042  ? 272 ALA   B C     1 
ATOM   6876 O  O     . ALA   B  2 280 ? 18.57500 -116.51500 -38.88600 1.000 83.16927  ? 272 ALA   B O     1 
ATOM   6877 C  CB    . ALA   B  2 280 ? 19.45600 -119.33600 -38.18100 1.000 86.72051  ? 272 ALA   B CB    1 
ATOM   6878 N  N     . SER   B  2 281 ? 16.94200 -117.11400 -37.38900 1.000 90.23522  ? 273 SER   B N     1 
ATOM   6879 C  CA    . SER   B  2 281 ? 16.57500 -115.76200 -36.88500 1.000 87.11126  ? 273 SER   B CA    1 
ATOM   6880 C  C     . SER   B  2 281 ? 16.83700 -115.67700 -35.37600 1.000 83.66111  ? 273 SER   B C     1 
ATOM   6881 O  O     . SER   B  2 281 ? 16.35500 -116.56000 -34.63700 1.000 83.44551  ? 273 SER   B O     1 
ATOM   6882 C  CB    . SER   B  2 281 ? 15.14300 -115.42100 -37.21700 1.000 83.03881  ? 273 SER   B CB    1 
ATOM   6883 O  OG    . SER   B  2 281 ? 14.25200 -116.37100 -36.65500 1.000 87.57280  ? 273 SER   B OG    1 
ATOM   6884 N  N     . LEU   B  2 282 ? 17.59000 -114.65200 -34.95900 1.000 82.25468  ? 274 LEU   B N     1 
ATOM   6885 C  CA    . LEU   B  2 282 ? 17.99900 -114.37500 -33.55500 1.000 82.57102  ? 274 LEU   B CA    1 
ATOM   6886 C  C     . LEU   B  2 282 ? 17.14600 -113.22100 -33.02100 1.000 84.44637  ? 274 LEU   B C     1 
ATOM   6887 O  O     . LEU   B  2 282 ? 16.64800 -112.44300 -33.85400 1.000 86.02626  ? 274 LEU   B O     1 
ATOM   6888 C  CB    . LEU   B  2 282 ? 19.48100 -113.99200 -33.53300 1.000 79.11092  ? 274 LEU   B CB    1 
ATOM   6889 C  CG    . LEU   B  2 282 ? 20.47600 -115.10400 -33.85800 1.000 80.50726  ? 274 LEU   B CG    1 
ATOM   6890 C  CD1   . LEU   B  2 282 ? 20.11100 -115.84000 -35.13800 1.000 81.19761  ? 274 LEU   B CD1   1 
ATOM   6891 C  CD2   . LEU   B  2 282 ? 21.87500 -114.53300 -33.96900 1.000 79.59673  ? 274 LEU   B CD2   1 
ATOM   6892 N  N     . SER   B  2 283 ? 17.00500 -113.09200 -31.69800 1.000 79.38147  ? 275 SER   B N     1 
ATOM   6893 C  CA    . SER   B  2 283 ? 16.13100 -112.06400 -31.07200 1.000 83.77867  ? 275 SER   B CA    1 
ATOM   6894 C  C     . SER   B  2 283 ? 16.48100 -111.82100 -29.59700 1.000 84.79545  ? 275 SER   B C     1 
ATOM   6895 O  O     . SER   B  2 283 ? 17.15700 -112.66900 -28.98200 1.000 89.51376  ? 275 SER   B O     1 
ATOM   6896 C  CB    . SER   B  2 283 ? 14.68200 -112.44800 -31.24000 1.000 83.41436  ? 275 SER   B CB    1 
ATOM   6897 O  OG    . SER   B  2 283 ? 13.83200 -111.62400 -30.45600 1.000 83.74365  ? 275 SER   B OG    1 
ATOM   6898 N  N     . GLU   B  2 284 ? 16.00800 -110.69000 -29.06600 1.000 81.74150  ? 276 GLU   B N     1 
ATOM   6899 C  CA    . GLU   B  2 284 ? 16.14200 -110.27300 -27.64500 1.000 81.34126  ? 276 GLU   B CA    1 
ATOM   6900 C  C     . GLU   B  2 284 ? 15.07000 -110.97300 -26.79700 1.000 85.82803  ? 276 GLU   B C     1 
ATOM   6901 O  O     . GLU   B  2 284 ? 15.07600 -110.77300 -25.56400 1.000 86.50079  ? 276 GLU   B O     1 
ATOM   6902 C  CB    . GLU   B  2 284 ? 16.03500 -108.74900 -27.53000 1.000 78.06686  ? 276 GLU   B CB    1 
ATOM   6903 C  CG    . GLU   B  2 284 ? 17.26300 -108.02100 -28.04600 1.000 76.43294  ? 276 GLU   B CG    1 
ATOM   6904 C  CD    . GLU   B  2 284 ? 17.06900 -106.54100 -28.32600 1.000 84.26548  ? 276 GLU   B CD    1 
ATOM   6905 O  OE1   . GLU   B  2 284 ? 16.20600 -105.91800 -27.67100 1.000 85.43674  ? 276 GLU   B OE1   1 
ATOM   6906 O  OE2   . GLU   B  2 284 ? 17.78200 -106.01300 -29.20300 1.000 91.94625  ? 276 GLU   B OE2   1 
ATOM   6907 N  N     . ASP   B  2 285 ? 14.18600 -111.75800 -27.42700 1.000 82.39426  ? 277 ASP   B N     1 
ATOM   6908 C  CA    . ASP   B  2 285 ? 13.20500 -112.63800 -26.73300 1.000 87.71521  ? 277 ASP   B CA    1 
ATOM   6909 C  C     . ASP   B  2 285 ? 13.90800 -113.92800 -26.28300 1.000 87.88400  ? 277 ASP   B C     1 
ATOM   6910 O  O     . ASP   B  2 285 ? 13.21000 -114.82300 -25.76900 1.000 92.83172  ? 277 ASP   B O     1 
ATOM   6911 C  CB    . ASP   B  2 285 ? 11.98000 -112.92000 -27.61100 1.000 84.98390  ? 277 ASP   B CB    1 
ATOM   6912 C  CG    . ASP   B  2 285 ? 12.22100 -113.89400 -28.75400 1.000 91.40837  ? 277 ASP   B CG    1 
ATOM   6913 O  OD1   . ASP   B  2 285 ? 13.39100 -114.26200 -28.98200 1.000 89.88046  ? 277 ASP   B OD1   1 
ATOM   6914 O  OD2   . ASP   B  2 285 ? 11.23100 -114.27900 -29.40900 1.000 94.18787  ? 277 ASP   B OD2   1 
ATOM   6915 N  N     . CYS   B  2 286 ? 15.22800 -114.02300 -26.49500 1.000 86.94106  ? 278 CYS   B N     1 
ATOM   6916 C  CA    . CYS   B  2 286 ? 16.11600 -115.11600 -26.01000 1.000 89.10333  ? 278 CYS   B CA    1 
ATOM   6917 C  C     . CYS   B  2 286 ? 15.72800 -116.44700 -26.66700 1.000 93.57596  ? 278 CYS   B C     1 
ATOM   6918 O  O     . CYS   B  2 286 ? 15.88400 -117.49900 -26.01300 1.000 97.81192  ? 278 CYS   B O     1 
ATOM   6919 C  CB    . CYS   B  2 286 ? 16.05600 -115.24500 -24.49100 1.000 89.69941  ? 278 CYS   B CB    1 
ATOM   6920 S  SG    . CYS   B  2 286 ? 16.44800 -113.71000 -23.61300 1.000 88.47664  ? 278 CYS   B SG    1 
ATOM   6921 N  N     . SER   B  2 287 ? 15.25200 -116.40500 -27.91500 1.000 93.24160  ? 279 SER   B N     1 
ATOM   6922 C  CA    . SER   B  2 287 ? 14.76800 -117.58900 -28.67200 1.000 89.51896  ? 279 SER   B CA    1 
ATOM   6923 C  C     . SER   B  2 287 ? 15.40500 -117.62200 -30.06500 1.000 88.09991  ? 279 SER   B C     1 
ATOM   6924 O  O     . SER   B  2 287 ? 15.44600 -116.57000 -30.72600 1.000 90.67419  ? 279 SER   B O     1 
ATOM   6925 C  CB    . SER   B  2 287 ? 13.26100 -117.60600 -28.75400 1.000 96.96220  ? 279 SER   B CB    1 
ATOM   6926 O  OG    . SER   B  2 287 ? 12.79200 -116.77800 -29.80700 1.000 94.39825  ? 279 SER   B OG    1 
ATOM   6927 N  N     . LEU   B  2 288 ? 15.89500 -118.79700 -30.47100 1.000 104.33183 ? 280 LEU   B N     1 
ATOM   6928 C  CA    . LEU   B  2 288 ? 16.32700 -119.10200 -31.86100 1.000 101.46691 ? 280 LEU   B CA    1 
ATOM   6929 C  C     . LEU   B  2 288 ? 15.12300 -119.65300 -32.63000 1.000 102.08288 ? 280 LEU   B C     1 
ATOM   6930 O  O     . LEU   B  2 288 ? 14.31500 -120.38200 -32.01900 1.000 101.32178 ? 280 LEU   B O     1 
ATOM   6931 C  CB    . LEU   B  2 288 ? 17.46900 -120.12400 -31.83000 1.000 95.05958  ? 280 LEU   B CB    1 
ATOM   6932 C  CG    . LEU   B  2 288 ? 17.99600 -120.56000 -33.19600 1.000 96.16329  ? 280 LEU   B CG    1 
ATOM   6933 C  CD1   . LEU   B  2 288 ? 18.81400 -119.45100 -33.84000 1.000 95.28871  ? 280 LEU   B CD1   1 
ATOM   6934 C  CD2   . LEU   B  2 288 ? 18.81800 -121.83400 -33.08000 1.000 102.65080 ? 280 LEU   B CD2   1 
ATOM   6935 N  N     . ALA   B  2 289 ? 15.01100 -119.30500 -33.91300 1.000 95.95293  ? 281 ALA   B N     1 
ATOM   6936 C  CA    . ALA   B  2 289 ? 14.02100 -119.86200 -34.86300 1.000 96.46588  ? 281 ALA   B CA    1 
ATOM   6937 C  C     . ALA   B  2 289 ? 14.71800 -120.13900 -36.19700 1.000 94.47258  ? 281 ALA   B C     1 
ATOM   6938 O  O     . ALA   B  2 289 ? 15.58400 -119.33400 -36.58700 1.000 94.71834  ? 281 ALA   B O     1 
ATOM   6939 C  CB    . ALA   B  2 289 ? 12.85900 -118.91300 -35.02400 1.000 90.55549  ? 281 ALA   B CB    1 
ATOM   6940 N  N     . VAL   B  2 290 ? 14.36800 -121.25300 -36.84300 1.000 97.08724  ? 282 VAL   B N     1 
ATOM   6941 C  CA    . VAL   B  2 290 ? 14.87000 -121.64500 -38.19400 1.000 96.12051  ? 282 VAL   B CA    1 
ATOM   6942 C  C     . VAL   B  2 290 ? 13.65400 -121.79400 -39.11500 1.000 97.43210  ? 282 VAL   B C     1 
ATOM   6943 O  O     . VAL   B  2 290 ? 12.69900 -122.49700 -38.71800 1.000 100.02005 ? 282 VAL   B O     1 
ATOM   6944 C  CB    . VAL   B  2 290 ? 15.71900 -122.92900 -38.13000 1.000 94.81701  ? 282 VAL   B CB    1 
ATOM   6945 C  CG1   . VAL   B  2 290 ? 16.28100 -123.30500 -39.49000 1.000 95.43827  ? 282 VAL   B CG1   1 
ATOM   6946 C  CG2   . VAL   B  2 290 ? 16.84200 -122.80800 -37.11100 1.000 94.29027  ? 282 VAL   B CG2   1 
ATOM   6947 N  N     . LEU   B  2 291 ? 13.69100 -121.15000 -40.28700 1.000 91.89405  ? 283 LEU   B N     1 
ATOM   6948 C  CA    . LEU   B  2 291 ? 12.52500 -120.98900 -41.19900 1.000 96.18103  ? 283 LEU   B CA    1 
ATOM   6949 C  C     . LEU   B  2 291 ? 12.85600 -121.53200 -42.59500 1.000 96.75894  ? 283 LEU   B C     1 
ATOM   6950 O  O     . LEU   B  2 291 ? 14.05600 -121.65000 -42.92400 1.000 95.84479  ? 283 LEU   B O     1 
ATOM   6951 C  CB    . LEU   B  2 291 ? 12.15200 -119.50400 -41.26600 1.000 96.59849  ? 283 LEU   B CB    1 
ATOM   6952 C  CG    . LEU   B  2 291 ? 12.11300 -118.76600 -39.92800 1.000 93.77794  ? 283 LEU   B CG    1 
ATOM   6953 C  CD1   . LEU   B  2 291 ? 11.95200 -117.27000 -40.14400 1.000 87.51063  ? 283 LEU   B CD1   1 
ATOM   6954 C  CD2   . LEU   B  2 291 ? 11.00200 -119.30200 -39.03900 1.000 96.20354  ? 283 LEU   B CD2   1 
ATOM   6955 N  N     . ASP   B  2 292 ? 11.81600 -121.83100 -43.38200 1.000 99.45634  ? 284 ASP   B N     1 
ATOM   6956 C  CA    . ASP   B  2 292 ? 11.91200 -122.30000 -44.79200 1.000 103.10562 ? 284 ASP   B CA    1 
ATOM   6957 C  C     . ASP   B  2 292 ? 11.98200 -121.07700 -45.72100 1.000 101.87199 ? 284 ASP   B C     1 
ATOM   6958 O  O     . ASP   B  2 292 ? 12.13700 -119.95000 -45.20700 1.000 98.75429  ? 284 ASP   B O     1 
ATOM   6959 C  CB    . ASP   B  2 292 ? 10.75900 -123.25100 -45.14100 1.000 103.62761 ? 284 ASP   B CB    1 
ATOM   6960 C  CG    . ASP   B  2 292 ? 9.36600  -122.69300 -44.89800 1.000 104.33997 ? 284 ASP   B CG    1 
ATOM   6961 O  OD1   . ASP   B  2 292 ? 9.26200  -121.51200 -44.51800 1.000 99.95773  ? 284 ASP   B OD1   1 
ATOM   6962 O  OD2   . ASP   B  2 292 ? 8.39400  -123.45100 -45.08200 1.000 107.15797 ? 284 ASP   B OD2   1 
ATOM   6963 N  N     . SER   B  2 293 ? 11.88800 -121.29800 -47.03700 1.000 107.19836 ? 285 SER   B N     1 
ATOM   6964 C  CA    . SER   B  2 293 ? 11.93500 -120.25200 -48.09400 1.000 104.56172 ? 285 SER   B CA    1 
ATOM   6965 C  C     . SER   B  2 293 ? 10.79300 -119.24300 -47.91100 1.000 107.14369 ? 285 SER   B C     1 
ATOM   6966 O  O     . SER   B  2 293 ? 10.99800 -118.06400 -48.26300 1.000 104.88232 ? 285 SER   B O     1 
ATOM   6967 C  CB    . SER   B  2 293 ? 11.89500 -120.87500 -49.46500 1.000 108.93280 ? 285 SER   B CB    1 
ATOM   6968 O  OG    . SER   B  2 293 ? 10.74800 -121.69800 -49.61600 1.000 110.92595 ? 285 SER   B OG    1 
ATOM   6969 N  N     . SER   B  2 294 ? 9.64600  -119.69000 -47.38100 1.000 105.30605 ? 286 SER   B N     1 
ATOM   6970 C  CA    . SER   B  2 294 ? 8.41200  -118.88100 -47.17900 1.000 102.11934 ? 286 SER   B CA    1 
ATOM   6971 C  C     . SER   B  2 294 ? 8.24300  -118.48400 -45.70100 1.000 98.66014  ? 286 SER   B C     1 
ATOM   6972 O  O     . SER   B  2 294 ? 7.10500  -118.15400 -45.30900 1.000 98.93655  ? 286 SER   B O     1 
ATOM   6973 C  CB    . SER   B  2 294 ? 7.20600  -119.62600 -47.70000 1.000 98.29008  ? 286 SER   B CB    1 
ATOM   6974 O  OG    . SER   B  2 294 ? 7.07800  -120.89000 -47.06800 1.000 101.06647 ? 286 SER   B OG    1 
ATOM   6975 N  N     . LEU   B  2 295 ? 9.33200  -118.51100 -44.92000 1.000 98.92111  ? 287 LEU   B N     1 
ATOM   6976 C  CA    . LEU   B  2 295 ? 9.43100  -117.96900 -43.53200 1.000 100.43440 ? 287 LEU   B CA    1 
ATOM   6977 C  C     . LEU   B  2 295 ? 8.42500  -118.65000 -42.59000 1.000 100.87285 ? 287 LEU   B C     1 
ATOM   6978 O  O     . LEU   B  2 295 ? 7.91400  -117.96200 -41.67900 1.000 98.54602  ? 287 LEU   B O     1 
ATOM   6979 C  CB    . LEU   B  2 295 ? 9.21600  -116.45100 -43.57000 1.000 89.02077  ? 287 LEU   B CB    1 
ATOM   6980 C  CG    . LEU   B  2 295 ? 10.21100 -115.66500 -44.42400 1.000 84.26633  ? 287 LEU   B CG    1 
ATOM   6981 C  CD1   . LEU   B  2 295 ? 9.71100  -114.25200 -44.68200 1.000 82.32838  ? 287 LEU   B CD1   1 
ATOM   6982 C  CD2   . LEU   B  2 295 ? 11.58500 -115.63400 -43.77300 1.000 83.34626  ? 287 LEU   B CD2   1 
ATOM   6983 N  N     . SER   B  2 296 ? 8.17400  -119.95100 -42.78000 1.000 97.54743  ? 288 SER   B N     1 
ATOM   6984 C  CA    . SER   B  2 296 ? 7.34300  -120.80600 -41.89000 1.000 100.00611 ? 288 SER   B CA    1 
ATOM   6985 C  C     . SER   B  2 296 ? 8.24600  -121.45900 -40.83700 1.000 103.03314 ? 288 SER   B C     1 
ATOM   6986 O  O     . SER   B  2 296 ? 9.36900  -121.86000 -41.19700 1.000 101.57324 ? 288 SER   B O     1 
ATOM   6987 C  CB    . SER   B  2 296 ? 6.58100  -121.84400 -42.67300 1.000 98.32470  ? 288 SER   B CB    1 
ATOM   6988 O  OG    . SER   B  2 296 ? 5.91800  -121.25900 -43.78300 1.000 100.74310 ? 288 SER   B OG    1 
ATOM   6989 N  N     . GLU   B  2 297 ? 7.76500  -121.56500 -39.59400 1.000 103.54130 ? 289 GLU   B N     1 
ATOM   6990 C  CA    . GLU   B  2 297 ? 8.54200  -122.06600 -38.42600 1.000 102.75217 ? 289 GLU   B CA    1 
ATOM   6991 C  C     . GLU   B  2 297 ? 8.71800  -123.58700 -38.54100 1.000 103.34936 ? 289 GLU   B C     1 
ATOM   6992 O  O     . GLU   B  2 297 ? 7.69300  -124.29900 -38.54100 1.000 106.39152 ? 289 GLU   B O     1 
ATOM   6993 C  CB    . GLU   B  2 297 ? 7.84000  -121.68000 -37.12200 1.000 108.48765 ? 289 GLU   B CB    1 
ATOM   6994 C  CG    . GLU   B  2 297 ? 8.64900  -121.99600 -35.87400 1.000 108.84304 ? 289 GLU   B CG    1 
ATOM   6995 C  CD    . GLU   B  2 297 ? 7.99900  -121.59200 -34.56000 1.000 110.49019 ? 289 GLU   B CD    1 
ATOM   6996 O  OE1   . GLU   B  2 297 ? 7.18200  -120.64800 -34.56600 1.000 106.52874 ? 289 GLU   B OE1   1 
ATOM   6997 O  OE2   . GLU   B  2 297 ? 8.31500  -122.22000 -33.53000 1.000 113.51725 ? 289 GLU   B OE2   1 
ATOM   6998 N  N     . LEU   B  2 298 ? 9.97000  -124.05200 -38.63700 1.000 104.21568 ? 290 LEU   B N     1 
ATOM   6999 C  CA    . LEU   B  2 298 ? 10.34900 -125.49300 -38.69000 1.000 104.66495 ? 290 LEU   B CA    1 
ATOM   7000 C  C     . LEU   B  2 298 ? 10.99100 -125.92300 -37.36500 1.000 107.35919 ? 290 LEU   B C     1 
ATOM   7001 O  O     . LEU   B  2 298 ? 10.84900 -127.11100 -37.00900 1.000 109.58581 ? 290 LEU   B O     1 
ATOM   7002 C  CB    . LEU   B  2 298 ? 11.32200 -125.72700 -39.85100 1.000 104.27224 ? 290 LEU   B CB    1 
ATOM   7003 C  CG    . LEU   B  2 298 ? 10.84000 -125.29400 -41.23500 1.000 106.78267 ? 290 LEU   B CG    1 
ATOM   7004 C  CD1   . LEU   B  2 298 ? 11.93700 -125.50400 -42.26600 1.000 102.88215 ? 290 LEU   B CD1   1 
ATOM   7005 C  CD2   . LEU   B  2 298 ? 9.57600  -126.03800 -41.64500 1.000 105.51151 ? 290 LEU   B CD2   1 
ATOM   7006 N  N     . PHE   B  2 299 ? 11.69600 -125.00900 -36.68600 1.000 106.13898 ? 291 PHE   B N     1 
ATOM   7007 C  CA    . PHE   B  2 299 ? 12.40900 -125.25900 -35.40500 1.000 105.95706 ? 291 PHE   B CA    1 
ATOM   7008 C  C     . PHE   B  2 299 ? 12.35000 -124.00800 -34.51900 1.000 105.76321 ? 291 PHE   B C     1 
ATOM   7009 O  O     . PHE   B  2 299 ? 12.19100 -122.88700 -35.04900 1.000 101.39328 ? 291 PHE   B O     1 
ATOM   7010 C  CB    . PHE   B  2 299 ? 13.85700 -125.68200 -35.67500 1.000 109.10248 ? 291 PHE   B CB    1 
ATOM   7011 C  CG    . PHE   B  2 299 ? 14.60700 -126.18500 -34.46600 1.000 115.51499 ? 291 PHE   B CG    1 
ATOM   7012 C  CD1   . PHE   B  2 299 ? 14.19300 -127.33000 -33.80000 1.000 116.46030 ? 291 PHE   B CD1   1 
ATOM   7013 C  CD2   . PHE   B  2 299 ? 15.73000 -125.51900 -33.99500 1.000 112.40505 ? 291 PHE   B CD2   1 
ATOM   7014 C  CE1   . PHE   B  2 299 ? 14.88100 -127.79400 -32.68800 1.000 115.98102 ? 291 PHE   B CE1   1 
ATOM   7015 C  CE2   . PHE   B  2 299 ? 16.41700 -125.98500 -32.88300 1.000 108.13517 ? 291 PHE   B CE2   1 
ATOM   7016 C  CZ    . PHE   B  2 299 ? 15.99200 -127.12100 -32.23200 1.000 113.33912 ? 291 PHE   B CZ    1 
ATOM   7017 N  N     . ARG   B  2 300 ? 12.46900 -124.21200 -33.20300 1.000 111.02329 ? 292 ARG   B N     1 
ATOM   7018 C  CA    . ARG   B  2 300 ? 12.50700 -123.14000 -32.17100 1.000 105.69298 ? 292 ARG   B CA    1 
ATOM   7019 C  C     . ARG   B  2 300 ? 13.19200 -123.68700 -30.91100 1.000 100.47276 ? 292 ARG   B C     1 
ATOM   7020 O  O     . ARG   B  2 300 ? 12.92000 -124.84900 -30.55200 1.000 103.49999 ? 292 ARG   B O     1 
ATOM   7021 C  CB    . ARG   B  2 300 ? 11.08900 -122.63000 -31.89400 1.000 103.94309 ? 292 ARG   B CB    1 
ATOM   7022 C  CG    . ARG   B  2 300 ? 10.94300 -121.81300 -30.61800 1.000 106.13500 ? 292 ARG   B CG    1 
ATOM   7023 C  CD    . ARG   B  2 300 ? 9.94800  -120.68400 -30.79200 1.000 107.10533 ? 292 ARG   B CD    1 
ATOM   7024 N  NE    . ARG   B  2 300 ? 10.56000 -119.53800 -31.45400 1.000 103.12820 ? 292 ARG   B NE    1 
ATOM   7025 C  CZ    . ARG   B  2 300 ? 9.90300  -118.59800 -32.13200 1.000 103.64144 ? 292 ARG   B CZ    1 
ATOM   7026 N  NH1   . ARG   B  2 300 ? 8.58900  -118.65400 -32.26900 1.000 106.41863 ? 292 ARG   B NH1   1 
ATOM   7027 N  NH2   . ARG   B  2 300 ? 10.57400 -117.60000 -32.68100 1.000 97.93008  ? 292 ARG   B NH2   1 
ATOM   7028 N  N     . SER   B  2 301 ? 14.05100 -122.87700 -30.28100 1.000 99.48802  ? 293 SER   B N     1 
ATOM   7029 C  CA    . SER   B  2 301 ? 14.83400 -123.22700 -29.06600 1.000 99.96473  ? 293 SER   B CA    1 
ATOM   7030 C  C     . SER   B  2 301 ? 14.69800 -122.13100 -28.00000 1.000 103.19373 ? 293 SER   B C     1 
ATOM   7031 O  O     . SER   B  2 301 ? 15.04800 -120.97000 -28.29000 1.000 99.04190  ? 293 SER   B O     1 
ATOM   7032 C  CB    . SER   B  2 301 ? 16.28100 -123.46600 -29.40900 1.000 99.49815  ? 293 SER   B CB    1 
ATOM   7033 O  OG    . SER   B  2 301 ? 17.02800 -123.77100 -28.24200 1.000 100.81319 ? 293 SER   B OG    1 
ATOM   7034 N  N     . GLN   B  2 302 ? 14.23700 -122.51000 -26.80400 1.000 100.91771 ? 294 GLN   B N     1 
ATOM   7035 C  CA    . GLN   B  2 302 ? 14.13000 -121.63700 -25.60300 1.000 100.52103 ? 294 GLN   B CA    1 
ATOM   7036 C  C     . GLN   B  2 302 ? 15.32700 -121.89900 -24.67700 1.000 101.45438 ? 294 GLN   B C     1 
ATOM   7037 O  O     . GLN   B  2 302 ? 15.22400 -121.57200 -23.47800 1.000 102.37601 ? 294 GLN   B O     1 
ATOM   7038 C  CB    . GLN   B  2 302 ? 12.82100 -121.92400 -24.86000 1.000 102.82835 ? 294 GLN   B CB    1 
ATOM   7039 C  CG    . GLN   B  2 302 ? 11.58300 -121.90000 -25.74500 1.000 102.61881 ? 294 GLN   B CG    1 
ATOM   7040 C  CD    . GLN   B  2 302 ? 11.07700 -120.50200 -25.99200 1.000 100.92305 ? 294 GLN   B CD    1 
ATOM   7041 O  OE1   . GLN   B  2 302 ? 11.08200 -120.01100 -27.11800 1.000 110.55826 ? 294 GLN   B OE1   1 
ATOM   7042 N  NE2   . GLN   B  2 302 ? 10.63500 -119.84700 -24.93000 1.000 104.91567 ? 294 GLN   B NE2   1 
ATOM   7043 N  N     . ALA   B  2 303 ? 16.41400 -122.46500 -25.21400 1.000 101.41427 ? 295 ALA   B N     1 
ATOM   7044 C  CA    . ALA   B  2 303 ? 17.59300 -122.95700 -24.45900 1.000 102.78780 ? 295 ALA   B CA    1 
ATOM   7045 C  C     . ALA   B  2 303 ? 18.29700 -121.79200 -23.75700 1.000 101.02346 ? 295 ALA   B C     1 
ATOM   7046 O  O     . ALA   B  2 303 ? 18.75300 -121.97800 -22.61200 1.000 102.71027 ? 295 ALA   B O     1 
ATOM   7047 C  CB    . ALA   B  2 303 ? 18.53600 -123.67900 -25.38900 1.000 102.87083 ? 295 ALA   B CB    1 
ATOM   7048 N  N     . HIS   B  2 304 ? 18.38600 -120.64000 -24.42500 1.000 97.95400  ? 296 HIS   B N     1 
ATOM   7049 C  CA    . HIS   B  2 304 ? 19.07000 -119.42000 -23.91800 1.000 96.11754  ? 296 HIS   B CA    1 
ATOM   7050 C  C     . HIS   B  2 304 ? 18.21300 -118.74500 -22.84200 1.000 96.61304  ? 296 HIS   B C     1 
ATOM   7051 O  O     . HIS   B  2 304 ? 16.97700 -118.69600 -23.01600 1.000 96.78642  ? 296 HIS   B O     1 
ATOM   7052 C  CB    . HIS   B  2 304 ? 19.40500 -118.47400 -25.07600 1.000 93.49921  ? 296 HIS   B CB    1 
ATOM   7053 C  CG    . HIS   B  2 304 ? 20.62700 -118.87700 -25.82500 1.000 92.58121  ? 296 HIS   B CG    1 
ATOM   7054 N  ND1   . HIS   B  2 304 ? 21.88600 -118.81100 -25.26200 1.000 92.89735  ? 296 HIS   B ND1   1 
ATOM   7055 C  CD2   . HIS   B  2 304 ? 20.79300 -119.35100 -27.07800 1.000 94.45556  ? 296 HIS   B CD2   1 
ATOM   7056 C  CE1   . HIS   B  2 304 ? 22.77700 -119.22500 -26.13700 1.000 92.62274  ? 296 HIS   B CE1   1 
ATOM   7057 N  NE2   . HIS   B  2 304 ? 22.13300 -119.56200 -27.26100 1.000 97.09784  ? 296 HIS   B NE2   1 
ATOM   7058 N  N     . ARG   B  2 305 ? 18.86400 -118.25300 -21.78000 1.000 97.02657  ? 297 ARG   B N     1 
ATOM   7059 C  CA    . ARG   B  2 305 ? 18.23800 -117.54600 -20.62700 1.000 97.79705  ? 297 ARG   B CA    1 
ATOM   7060 C  C     . ARG   B  2 305 ? 18.49300 -116.03500 -20.72100 1.000 95.19142  ? 297 ARG   B C     1 
ATOM   7061 O  O     . ARG   B  2 305 ? 17.84900 -115.29500 -19.95800 1.000 95.54095  ? 297 ARG   B O     1 
ATOM   7062 C  CB    . ARG   B  2 305 ? 18.78900 -118.09200 -19.30600 1.000 101.55517 ? 297 ARG   B CB    1 
ATOM   7063 C  CG    . ARG   B  2 305 ? 18.56400 -119.58300 -19.10000 1.000 103.56952 ? 297 ARG   B CG    1 
ATOM   7064 C  CD    . ARG   B  2 305 ? 19.21400 -120.08000 -17.82300 1.000 110.68594 ? 297 ARG   B CD    1 
ATOM   7065 N  NE    . ARG   B  2 305 ? 20.64700 -119.80300 -17.79700 1.000 107.62316 ? 297 ARG   B NE    1 
ATOM   7066 C  CZ    . ARG   B  2 305 ? 21.59900 -120.59300 -18.29600 1.000 106.17299 ? 297 ARG   B CZ    1 
ATOM   7067 N  NH1   . ARG   B  2 305 ? 21.29500 -121.74500 -18.87300 1.000 107.04787 ? 297 ARG   B NH1   1 
ATOM   7068 N  NH2   . ARG   B  2 305 ? 22.86600 -120.22300 -18.21100 1.000 105.02838 ? 297 ARG   B NH2   1 
ATOM   7069 N  N     . ASP   B  2 306 ? 19.41100 -115.60300 -21.59700 1.000 92.94293  ? 298 ASP   B N     1 
ATOM   7070 C  CA    . ASP   B  2 306 ? 19.64700 -114.17500 -21.95700 1.000 90.33097  ? 298 ASP   B CA    1 
ATOM   7071 C  C     . ASP   B  2 306 ? 19.58000 -114.04600 -23.48600 1.000 88.07348  ? 298 ASP   B C     1 
ATOM   7072 O  O     . ASP   B  2 306 ? 19.20600 -115.03800 -24.13200 1.000 88.73480  ? 298 ASP   B O     1 
ATOM   7073 C  CB    . ASP   B  2 306 ? 20.96900 -113.66800 -21.37300 1.000 90.22084  ? 298 ASP   B CB    1 
ATOM   7074 C  CG    . ASP   B  2 306 ? 20.92200 -112.22100 -20.90800 1.000 89.10438  ? 298 ASP   B CG    1 
ATOM   7075 O  OD1   . ASP   B  2 306 ? 20.21100 -111.41600 -21.54700 1.000 87.33084  ? 298 ASP   B OD1   1 
ATOM   7076 O  OD2   . ASP   B  2 306 ? 21.58800 -111.91000 -19.89900 1.000 90.20679  ? 298 ASP   B OD2   1 
ATOM   7077 N  N     . PHE   B  2 307 ? 19.91200 -112.87200 -24.03700 1.000 85.97190  ? 299 PHE   B N     1 
ATOM   7078 C  CA    . PHE   B  2 307 ? 19.74700 -112.52600 -25.47800 1.000 83.59403  ? 299 PHE   B CA    1 
ATOM   7079 C  C     . PHE   B  2 307 ? 20.60000 -113.44200 -26.36100 1.000 84.83046  ? 299 PHE   B C     1 
ATOM   7080 O  O     . PHE   B  2 307 ? 21.74300 -113.75400 -25.97900 1.000 90.10947  ? 299 PHE   B O     1 
ATOM   7081 C  CB    . PHE   B  2 307 ? 20.14500 -111.07300 -25.75900 1.000 82.39546  ? 299 PHE   B CB    1 
ATOM   7082 C  CG    . PHE   B  2 307 ? 19.27200 -110.01000 -25.13900 1.000 82.60750  ? 299 PHE   B CG    1 
ATOM   7083 C  CD1   . PHE   B  2 307 ? 18.02400 -110.30700 -24.60700 1.000 82.87815  ? 299 PHE   B CD1   1 
ATOM   7084 C  CD2   . PHE   B  2 307 ? 19.69300 -108.69000 -25.12200 1.000 81.20042  ? 299 PHE   B CD2   1 
ATOM   7085 C  CE1   . PHE   B  2 307 ? 17.23600 -109.31400 -24.04800 1.000 82.33851  ? 299 PHE   B CE1   1 
ATOM   7086 C  CE2   . PHE   B  2 307 ? 18.90100 -107.69700 -24.56600 1.000 79.65534  ? 299 PHE   B CE2   1 
ATOM   7087 C  CZ    . PHE   B  2 307 ? 17.67400 -108.01100 -24.03000 1.000 80.95037  ? 299 PHE   B CZ    1 
ATOM   7088 N  N     . VAL   B  2 308 ? 20.05900 -113.82500 -27.52400 1.000 83.09007  ? 300 VAL   B N     1 
ATOM   7089 C  CA    . VAL   B  2 308 ? 20.75900 -114.62200 -28.57700 1.000 83.15536  ? 300 VAL   B CA    1 
ATOM   7090 C  C     . VAL   B  2 308 ? 21.46900 -113.63500 -29.51300 1.000 83.67345  ? 300 VAL   B C     1 
ATOM   7091 O  O     . VAL   B  2 308 ? 20.76900 -112.83800 -30.17200 1.000 83.03315  ? 300 VAL   B O     1 
ATOM   7092 C  CB    . VAL   B  2 308 ? 19.79300 -115.53800 -29.35600 1.000 83.98557  ? 300 VAL   B CB    1 
ATOM   7093 C  CG1   . VAL   B  2 308 ? 20.54800 -116.57600 -30.16900 1.000 84.87643  ? 300 VAL   B CG1   1 
ATOM   7094 C  CG2   . VAL   B  2 308 ? 18.77700 -116.22000 -28.45100 1.000 88.74877  ? 300 VAL   B CG2   1 
ATOM   7095 N  N     . ARG   B  2 309 ? 22.80300 -113.69700 -29.57500 1.000 84.57642  ? 301 ARG   B N     1 
ATOM   7096 C  CA    . ARG   B  2 309 ? 23.66200 -112.64700 -30.18900 1.000 84.98997  ? 301 ARG   B CA    1 
ATOM   7097 C  C     . ARG   B  2 309 ? 24.05400 -113.03000 -31.62000 1.000 88.96817  ? 301 ARG   B C     1 
ATOM   7098 O  O     . ARG   B  2 309 ? 23.90200 -112.17200 -32.51300 1.000 86.45611  ? 301 ARG   B O     1 
ATOM   7099 C  CB    . ARG   B  2 309 ? 24.91000 -112.42100 -29.33200 1.000 87.05742  ? 301 ARG   B CB    1 
ATOM   7100 C  CG    . ARG   B  2 309 ? 24.70200 -111.45800 -28.17300 1.000 86.26188  ? 301 ARG   B CG    1 
ATOM   7101 C  CD    . ARG   B  2 309 ? 24.44200 -110.04100 -28.64500 1.000 85.06748  ? 301 ARG   B CD    1 
ATOM   7102 N  NE    . ARG   B  2 309 ? 23.03200 -109.68700 -28.61100 1.000 76.98693  ? 301 ARG   B NE    1 
ATOM   7103 C  CZ    . ARG   B  2 309 ? 22.55000 -108.49100 -28.92500 1.000 75.49375  ? 301 ARG   B CZ    1 
ATOM   7104 N  NH1   . ARG   B  2 309 ? 23.36700 -107.52300 -29.30800 1.000 74.35978  ? 301 ARG   B NH1   1 
ATOM   7105 N  NH2   . ARG   B  2 309 ? 21.25000 -108.26700 -28.85300 1.000 80.85593  ? 301 ARG   B NH2   1 
ATOM   7106 N  N     . ASP   B  2 310 ? 24.56100 -114.25000 -31.82700 1.000 87.44771  ? 302 ASP   B N     1 
ATOM   7107 C  CA    . ASP   B  2 310 ? 25.06200 -114.71800 -33.14900 1.000 88.43010  ? 302 ASP   B CA    1 
ATOM   7108 C  C     . ASP   B  2 310 ? 24.74000 -116.20400 -33.34000 1.000 87.82202  ? 302 ASP   B C     1 
ATOM   7109 O  O     . ASP   B  2 310 ? 24.66300 -116.93200 -32.33000 1.000 89.03241  ? 302 ASP   B O     1 
ATOM   7110 C  CB    . ASP   B  2 310 ? 26.56400 -114.46400 -33.29500 1.000 90.04682  ? 302 ASP   B CB    1 
ATOM   7111 C  CG    . ASP   B  2 310 ? 27.00300 -114.21800 -34.72700 1.000 88.10291  ? 302 ASP   B CG    1 
ATOM   7112 O  OD1   . ASP   B  2 310 ? 26.25500 -114.60000 -35.64700 1.000 87.94566  ? 302 ASP   B OD1   1 
ATOM   7113 O  OD2   . ASP   B  2 310 ? 28.08900 -113.63700 -34.91100 1.000 91.52432  ? 302 ASP   B OD2   1 
ATOM   7114 N  N     . ALA   B  2 311 ? 24.55700 -116.61400 -34.60000 1.000 85.80991  ? 303 ALA   B N     1 
ATOM   7115 C  CA    . ALA   B  2 311 ? 24.32000 -118.01000 -35.03700 1.000 89.52413  ? 303 ALA   B CA    1 
ATOM   7116 C  C     . ALA   B  2 311 ? 25.21600 -118.32400 -36.24000 1.000 90.57806  ? 303 ALA   B C     1 
ATOM   7117 O  O     . ALA   B  2 311 ? 25.36800 -117.44500 -37.11400 1.000 92.06235  ? 303 ALA   B O     1 
ATOM   7118 C  CB    . ALA   B  2 311 ? 22.86300 -118.20700 -35.37500 1.000 86.89571  ? 303 ALA   B CB    1 
ATOM   7119 N  N     . THR   B  2 312 ? 25.78400 -119.53200 -36.28000 1.000 88.47210  ? 304 THR   B N     1 
ATOM   7120 C  CA    . THR   B  2 312 ? 26.70000 -120.00000 -37.35300 1.000 88.78353  ? 304 THR   B CA    1 
ATOM   7121 C  C     . THR   B  2 312 ? 26.45300 -121.49000 -37.60800 1.000 95.34614  ? 304 THR   B C     1 
ATOM   7122 O  O     . THR   B  2 312 ? 26.50000 -122.27200 -36.63900 1.000 94.21897  ? 304 THR   B O     1 
ATOM   7123 C  CB    . THR   B  2 312 ? 28.16100 -119.69000 -37.00400 1.000 88.76476  ? 304 THR   B CB    1 
ATOM   7124 O  OG1   . THR   B  2 312 ? 28.99900 -120.32400 -37.96800 1.000 101.24402 ? 304 THR   B OG1   1 
ATOM   7125 C  CG2   . THR   B  2 312 ? 28.56200 -120.14700 -35.61800 1.000 95.28857  ? 304 THR   B CG2   1 
ATOM   7126 N  N     . TRP   B  2 313 ? 26.18900 -121.85200 -38.86600 1.000 100.27526 ? 305 TRP   B N     1 
ATOM   7127 C  CA    . TRP   B  2 313 ? 25.92500 -123.24800 -39.30700 1.000 102.29513 ? 305 TRP   B CA    1 
ATOM   7128 C  C     . TRP   B  2 313 ? 27.25000 -123.99800 -39.46500 1.000 107.24134 ? 305 TRP   B C     1 
ATOM   7129 O  O     . TRP   B  2 313 ? 28.21100 -123.40300 -39.99300 1.000 106.26543 ? 305 TRP   B O     1 
ATOM   7130 C  CB    . TRP   B  2 313 ? 25.12400 -123.25900 -40.61100 1.000 97.95505  ? 305 TRP   B CB    1 
ATOM   7131 C  CG    . TRP   B  2 313 ? 23.75900 -122.65900 -40.48800 1.000 93.63650  ? 305 TRP   B CG    1 
ATOM   7132 C  CD1   . TRP   B  2 313 ? 23.43800 -121.33500 -40.53500 1.000 90.88743  ? 305 TRP   B CD1   1 
ATOM   7133 C  CD2   . TRP   B  2 313 ? 22.52100 -123.36800 -40.30500 1.000 94.95374  ? 305 TRP   B CD2   1 
ATOM   7134 N  NE1   . TRP   B  2 313 ? 22.08600 -121.17100 -40.39400 1.000 94.93867  ? 305 TRP   B NE1   1 
ATOM   7135 C  CE2   . TRP   B  2 313 ? 21.49700 -122.39900 -40.25000 1.000 92.83233  ? 305 TRP   B CE2   1 
ATOM   7136 C  CE3   . TRP   B  2 313 ? 22.17800 -124.71900 -40.17900 1.000 97.89155  ? 305 TRP   B CE3   1 
ATOM   7137 C  CZ2   . TRP   B  2 313 ? 20.15600 -122.74300 -40.07800 1.000 93.55597  ? 305 TRP   B CZ2   1 
ATOM   7138 C  CZ3   . TRP   B  2 313 ? 20.85300 -125.05800 -40.00800 1.000 98.62788  ? 305 TRP   B CZ3   1 
ATOM   7139 C  CH2   . TRP   B  2 313 ? 19.85800 -124.08100 -39.95900 1.000 96.47544  ? 305 TRP   B CH2   1 
ATOM   7140 N  N     . SER   B  2 314 ? 27.28800 -125.25700 -39.02200 1.000 115.09873 ? 306 SER   B N     1 
ATOM   7141 C  CA    . SER   B  2 314 ? 28.46100 -126.16100 -39.13500 1.000 119.23010 ? 306 SER   B CA    1 
ATOM   7142 C  C     . SER   B  2 314 ? 28.72200 -126.44900 -40.61200 1.000 123.87714 ? 306 SER   B C     1 
ATOM   7143 O  O     . SER   B  2 314 ? 27.83700 -126.94400 -41.30800 1.000 125.38942 ? 306 SER   B O     1 
ATOM   7144 C  CB    . SER   B  2 314 ? 28.24600 -127.42700 -38.34300 1.000 116.22898 ? 306 SER   B CB    1 
ATOM   7145 O  OG    . SER   B  2 314 ? 29.41000 -128.24000 -38.34900 1.000 117.96023 ? 306 SER   B OG    1 
ATOM   7146 N  N     . PRO   B  2 315 ? 29.92600 -126.12600 -41.14300 1.000 118.71948 ? 307 PRO   B N     1 
ATOM   7147 C  CA    . PRO   B  2 315 ? 30.26000 -126.43100 -42.53400 1.000 115.58105 ? 307 PRO   B CA    1 
ATOM   7148 C  C     . PRO   B  2 315 ? 30.42600 -127.94000 -42.77000 1.000 113.01158 ? 307 PRO   B C     1 
ATOM   7149 O  O     . PRO   B  2 315 ? 30.32500 -128.35800 -43.90700 1.000 110.58302 ? 307 PRO   B O     1 
ATOM   7150 C  CB    . PRO   B  2 315 ? 31.58600 -125.70000 -42.80800 1.000 114.16681 ? 307 PRO   B CB    1 
ATOM   7151 C  CG    . PRO   B  2 315 ? 32.14300 -125.31600 -41.44300 1.000 113.64489 ? 307 PRO   B CG    1 
ATOM   7152 C  CD    . PRO   B  2 315 ? 31.02000 -125.44900 -40.43400 1.000 113.08691 ? 307 PRO   B CD    1 
ATOM   7153 N  N     . LEU   B  2 316 ? 30.66700 -128.69900 -41.69500 1.000 113.54376 ? 308 LEU   B N     1 
ATOM   7154 C  CA    . LEU   B  2 316 ? 30.94600 -130.16200 -41.71400 1.000 114.34894 ? 308 LEU   B CA    1 
ATOM   7155 C  C     . LEU   B  2 316 ? 29.63400 -130.95000 -41.59800 1.000 115.70581 ? 308 LEU   B C     1 
ATOM   7156 O  O     . LEU   B  2 316 ? 29.54600 -132.03000 -42.21900 1.000 118.90624 ? 308 LEU   B O     1 
ATOM   7157 C  CB    . LEU   B  2 316 ? 31.90000 -130.49800 -40.56100 1.000 115.30014 ? 308 LEU   B CB    1 
ATOM   7158 C  CG    . LEU   B  2 316 ? 33.37400 -130.14500 -40.77700 1.000 115.42647 ? 308 LEU   B CG    1 
ATOM   7159 C  CD1   . LEU   B  2 316 ? 33.54500 -128.75500 -41.37400 1.000 112.27795 ? 308 LEU   B CD1   1 
ATOM   7160 C  CD2   . LEU   B  2 316 ? 34.14900 -130.25400 -39.47200 1.000 115.78731 ? 308 LEU   B CD2   1 
ATOM   7161 N  N     . ASN   B  2 317 ? 28.66400 -130.43700 -40.83000 1.000 113.59791 ? 309 ASN   B N     1 
ATOM   7162 C  CA    . ASN   B  2 317 ? 27.34900 -131.08800 -40.57300 1.000 114.77281 ? 309 ASN   B CA    1 
ATOM   7163 C  C     . ASN   B  2 317 ? 26.23900 -130.03500 -40.68500 1.000 114.75446 ? 309 ASN   B C     1 
ATOM   7164 O  O     . ASN   B  2 317 ? 25.92700 -129.39700 -39.66500 1.000 119.40699 ? 309 ASN   B O     1 
ATOM   7165 C  CB    . ASN   B  2 317 ? 27.34000 -131.79200 -39.21200 1.000 117.99923 ? 309 ASN   B CB    1 
ATOM   7166 C  CG    . ASN   B  2 317 ? 26.07200 -132.57400 -38.93600 1.000 121.42247 ? 309 ASN   B CG    1 
ATOM   7167 O  OD1   . ASN   B  2 317 ? 25.20800 -132.70500 -39.80000 1.000 124.24825 ? 309 ASN   B OD1   1 
ATOM   7168 N  ND2   . ASN   B  2 317 ? 25.95300 -133.10300 -37.73000 1.000 124.13582 ? 309 ASN   B ND2   1 
ATOM   7169 N  N     . HIS   B  2 318 ? 25.63900 -129.90200 -41.87400 1.000 124.40064 ? 310 HIS   B N     1 
ATOM   7170 C  CA    . HIS   B  2 318 ? 24.69900 -128.80900 -42.25500 1.000 125.09391 ? 310 HIS   B CA    1 
ATOM   7171 C  C     . HIS   B  2 318 ? 23.44100 -128.80500 -41.37000 1.000 120.97194 ? 310 HIS   B C     1 
ATOM   7172 O  O     . HIS   B  2 318 ? 22.76500 -127.75700 -41.33500 1.000 120.97239 ? 310 HIS   B O     1 
ATOM   7173 C  CB    . HIS   B  2 318 ? 24.33300 -128.90000 -43.74500 1.000 123.63040 ? 310 HIS   B CB    1 
ATOM   7174 C  CG    . HIS   B  2 318 ? 25.46400 -128.59900 -44.67300 1.000 123.57605 ? 310 HIS   B CG    1 
ATOM   7175 N  ND1   . HIS   B  2 318 ? 25.58900 -129.20800 -45.91000 1.000 129.29967 ? 310 HIS   B ND1   1 
ATOM   7176 C  CD2   . HIS   B  2 318 ? 26.52000 -127.76500 -44.55300 1.000 120.99592 ? 310 HIS   B CD2   1 
ATOM   7177 C  CE1   . HIS   B  2 318 ? 26.66900 -128.75600 -46.51300 1.000 131.08829 ? 310 HIS   B CE1   1 
ATOM   7178 N  NE2   . HIS   B  2 318 ? 27.26000 -127.86800 -45.70000 1.000 121.90213 ? 310 HIS   B NE2   1 
ATOM   7179 N  N     . SER   B  2 319 ? 23.13100 -129.91600 -40.69200 1.000 115.64638 ? 311 SER   B N     1 
ATOM   7180 C  CA    . SER   B  2 319 ? 21.98700 -130.03900 -39.74700 1.000 119.39425 ? 311 SER   B CA    1 
ATOM   7181 C  C     . SER   B  2 319 ? 22.33100 -129.41400 -38.38600 1.000 119.93332 ? 311 SER   B C     1 
ATOM   7182 O  O     . SER   B  2 319 ? 21.39400 -129.19100 -37.58900 1.000 108.50522 ? 311 SER   B O     1 
ATOM   7183 C  CB    . SER   B  2 319 ? 21.55900 -131.47700 -39.59700 1.000 114.80532 ? 311 SER   B CB    1 
ATOM   7184 O  OG    . SER   B  2 319 ? 20.90100 -131.93000 -40.77000 1.000 120.06220 ? 311 SER   B OG    1 
ATOM   7185 N  N     . LEU   B  2 320 ? 23.61600 -129.13600 -38.13300 1.000 116.51492 ? 312 LEU   B N     1 
ATOM   7186 C  CA    . LEU   B  2 320 ? 24.13200 -128.62300 -36.83500 1.000 110.85551 ? 312 LEU   B CA    1 
ATOM   7187 C  C     . LEU   B  2 320 ? 24.30200 -127.10100 -36.91300 1.000 109.31558 ? 312 LEU   B C     1 
ATOM   7188 O  O     . LEU   B  2 320 ? 25.11600 -126.63800 -37.73400 1.000 109.47026 ? 312 LEU   B O     1 
ATOM   7189 C  CB    . LEU   B  2 320 ? 25.45800 -129.32500 -36.51700 1.000 116.78752 ? 312 LEU   B CB    1 
ATOM   7190 C  CG    . LEU   B  2 320 ? 25.79600 -129.45700 -35.03200 1.000 119.98839 ? 312 LEU   B CG    1 
ATOM   7191 C  CD1   . LEU   B  2 320 ? 26.67100 -130.67700 -34.78300 1.000 121.88216 ? 312 LEU   B CD1   1 
ATOM   7192 C  CD2   . LEU   B  2 320 ? 26.47000 -128.19800 -34.50500 1.000 110.45060 ? 312 LEU   B CD2   1 
ATOM   7193 N  N     . LEU   B  2 321 ? 23.55600 -126.36400 -36.08200 1.000 110.60147 ? 313 LEU   B N     1 
ATOM   7194 C  CA    . LEU   B  2 321 ? 23.59100 -124.87900 -35.97000 1.000 103.81696 ? 313 LEU   B CA    1 
ATOM   7195 C  C     . LEU   B  2 321 ? 24.02600 -124.49300 -34.54800 1.000 101.93577 ? 313 LEU   B C     1 
ATOM   7196 O  O     . LEU   B  2 321 ? 23.45000 -125.04400 -33.58700 1.000 101.28527 ? 313 LEU   B O     1 
ATOM   7197 C  CB    . LEU   B  2 321 ? 22.19900 -124.33200 -36.30500 1.000 98.97102  ? 313 LEU   B CB    1 
ATOM   7198 C  CG    . LEU   B  2 321 ? 21.98300 -122.83800 -36.06400 1.000 93.73236  ? 313 LEU   B CG    1 
ATOM   7199 C  CD1   . LEU   B  2 321 ? 22.98000 -122.00200 -36.85000 1.000 91.94511  ? 313 LEU   B CD1   1 
ATOM   7200 C  CD2   . LEU   B  2 321 ? 20.55900 -122.44000 -36.41800 1.000 92.90334  ? 313 LEU   B CD2   1 
ATOM   7201 N  N     . THR   B  2 322 ? 25.00300 -123.58500 -34.43000 1.000 97.06843  ? 314 THR   B N     1 
ATOM   7202 C  CA    . THR   B  2 322 ? 25.65200 -123.17000 -33.15500 1.000 95.53592  ? 314 THR   B CA    1 
ATOM   7203 C  C     . THR   B  2 322 ? 25.29100 -121.71300 -32.84100 1.000 92.65064  ? 314 THR   B C     1 
ATOM   7204 O  O     . THR   B  2 322 ? 25.60900 -120.84200 -33.67400 1.000 93.50435  ? 314 THR   B O     1 
ATOM   7205 C  CB    . THR   B  2 322 ? 27.17200 -123.36500 -33.23700 1.000 98.45269  ? 314 THR   B CB    1 
ATOM   7206 O  OG1   . THR   B  2 322 ? 27.42600 -124.77000 -33.25200 1.000 101.78820 ? 314 THR   B OG1   1 
ATOM   7207 C  CG2   . THR   B  2 322 ? 27.93300 -122.73500 -32.09100 1.000 97.45382  ? 314 THR   B CG2   1 
ATOM   7208 N  N     . THR   B  2 323 ? 24.67800 -121.46600 -31.67700 1.000 92.61071  ? 315 THR   B N     1 
ATOM   7209 C  CA    . THR   B  2 323 ? 24.31100 -120.11500 -31.16900 1.000 90.28852  ? 315 THR   B CA    1 
ATOM   7210 C  C     . THR   B  2 323 ? 25.17100 -119.75200 -29.95400 1.000 90.47999  ? 315 THR   B C     1 
ATOM   7211 O  O     . THR   B  2 323 ? 25.60700 -120.67300 -29.24100 1.000 94.44293  ? 315 THR   B O     1 
ATOM   7212 C  CB    . THR   B  2 323 ? 22.83300 -120.03600 -30.77000 1.000 90.29720  ? 315 THR   B CB    1 
ATOM   7213 O  OG1   . THR   B  2 323 ? 22.56800 -121.07200 -29.82300 1.000 92.86898  ? 315 THR   B OG1   1 
ATOM   7214 C  CG2   . THR   B  2 323 ? 21.90000 -120.15600 -31.95400 1.000 93.99203  ? 315 THR   B CG2   1 
ATOM   7215 N  N     . VAL   B  2 324 ? 25.38300 -118.45200 -29.73600 1.000 88.38841  ? 316 VAL   B N     1 
ATOM   7216 C  CA    . VAL   B  2 324 ? 26.00100 -117.87900 -28.50300 1.000 89.41569  ? 316 VAL   B CA    1 
ATOM   7217 C  C     . VAL   B  2 324 ? 25.09900 -116.74700 -27.99400 1.000 91.22786  ? 316 VAL   B C     1 
ATOM   7218 O  O     . VAL   B  2 324 ? 24.43500 -116.09500 -28.82900 1.000 85.13620  ? 316 VAL   B O     1 
ATOM   7219 C  CB    . VAL   B  2 324 ? 27.44300 -117.39700 -28.75600 1.000 87.81939  ? 316 VAL   B CB    1 
ATOM   7220 C  CG1   . VAL   B  2 324 ? 28.35800 -118.55900 -29.10400 1.000 90.32436  ? 316 VAL   B CG1   1 
ATOM   7221 C  CG2   . VAL   B  2 324 ? 27.51600 -116.31900 -29.82600 1.000 94.02357  ? 316 VAL   B CG2   1 
ATOM   7222 N  N     . GLY   B  2 325 ? 25.06700 -116.53800 -26.67500 1.000 90.25374  ? 317 GLY   B N     1 
ATOM   7223 C  CA    . GLY   B  2 325 ? 24.22900 -115.51400 -26.02100 1.000 89.45286  ? 317 GLY   B CA    1 
ATOM   7224 C  C     . GLY   B  2 325 ? 24.95900 -114.81500 -24.88700 1.000 89.97519  ? 317 GLY   B C     1 
ATOM   7225 O  O     . GLY   B  2 325 ? 26.10600 -115.20300 -24.58700 1.000 90.40822  ? 317 GLY   B O     1 
ATOM   7226 N  N     . TRP   B  2 326 ? 24.30600 -113.82700 -24.26700 1.000 89.10943  ? 318 TRP   B N     1 
ATOM   7227 C  CA    . TRP   B  2 326 ? 24.85300 -113.04200 -23.12600 1.000 89.08285  ? 318 TRP   B CA    1 
ATOM   7228 C  C     . TRP   B  2 326 ? 24.77200 -113.85400 -21.82800 1.000 90.38636  ? 318 TRP   B C     1 
ATOM   7229 O  O     . TRP   B  2 326 ? 25.32100 -113.38200 -20.81600 1.000 99.36678  ? 318 TRP   B O     1 
ATOM   7230 C  CB    . TRP   B  2 326 ? 24.14000 -111.68800 -22.99800 1.000 89.83747  ? 318 TRP   B CB    1 
ATOM   7231 C  CG    . TRP   B  2 326 ? 24.58000 -110.66200 -23.99800 1.000 86.67890  ? 318 TRP   B CG    1 
ATOM   7232 C  CD1   . TRP   B  2 326 ? 25.62700 -110.74800 -24.87100 1.000 87.88070  ? 318 TRP   B CD1   1 
ATOM   7233 C  CD2   . TRP   B  2 326 ? 24.00000 -109.36200 -24.20300 1.000 83.85447  ? 318 TRP   B CD2   1 
ATOM   7234 N  NE1   . TRP   B  2 326 ? 25.72800 -109.60300 -25.61300 1.000 82.97336  ? 318 TRP   B NE1   1 
ATOM   7235 C  CE2   . TRP   B  2 326 ? 24.74400 -108.73400 -25.22600 1.000 79.60579  ? 318 TRP   B CE2   1 
ATOM   7236 C  CE3   . TRP   B  2 326 ? 22.92400 -108.67200 -23.63100 1.000 83.51371  ? 318 TRP   B CE3   1 
ATOM   7237 C  CZ2   . TRP   B  2 326 ? 24.44400 -107.45200 -25.68300 1.000 77.91365  ? 318 TRP   B CZ2   1 
ATOM   7238 C  CZ3   . TRP   B  2 326 ? 22.63000 -107.40500 -24.08400 1.000 81.80014  ? 318 TRP   B CZ3   1 
ATOM   7239 C  CH2   . TRP   B  2 326 ? 23.37900 -106.80700 -25.09800 1.000 78.33707  ? 318 TRP   B CH2   1 
ATOM   7240 N  N     . ASP   B  2 327 ? 24.13500 -115.03000 -21.86200 1.000 91.12364  ? 319 ASP   B N     1 
ATOM   7241 C  CA    . ASP   B  2 327 ? 24.09000 -116.00700 -20.73900 1.000 94.58007  ? 319 ASP   B CA    1 
ATOM   7242 C  C     . ASP   B  2 327 ? 25.36800 -116.86100 -20.73100 1.000 95.44770  ? 319 ASP   B C     1 
ATOM   7243 O  O     . ASP   B  2 327 ? 25.42900 -117.81400 -19.93400 1.000 99.22471  ? 319 ASP   B O     1 
ATOM   7244 C  CB    . ASP   B  2 327 ? 22.83600 -116.88500 -20.82300 1.000 95.37947  ? 319 ASP   B CB    1 
ATOM   7245 C  CG    . ASP   B  2 327 ? 22.68500 -117.64600 -22.13100 1.000 94.73554  ? 319 ASP   B CG    1 
ATOM   7246 O  OD1   . ASP   B  2 327 ? 23.38700 -117.29800 -23.10200 1.000 92.85894  ? 319 ASP   B OD1   1 
ATOM   7247 O  OD2   . ASP   B  2 327 ? 21.86000 -118.57800 -22.16900 1.000 96.31486  ? 319 ASP   B OD2   1 
ATOM   7248 N  N     . HIS   B  2 328 ? 26.33800 -116.54400 -21.59600 1.000 93.84869  ? 320 HIS   B N     1 
ATOM   7249 C  CA    . HIS   B  2 328 ? 27.64600 -117.24100 -21.74000 1.000 96.33277  ? 320 HIS   B CA    1 
ATOM   7250 C  C     . HIS   B  2 328 ? 27.44000 -118.70300 -22.16500 1.000 99.43211  ? 320 HIS   B C     1 
ATOM   7251 O  O     . HIS   B  2 328 ? 28.36100 -119.50900 -21.94500 1.000 104.04117 ? 320 HIS   B O     1 
ATOM   7252 C  CB    . HIS   B  2 328 ? 28.47100 -117.13100 -20.44900 1.000 96.75498  ? 320 HIS   B CB    1 
ATOM   7253 C  CG    . HIS   B  2 328 ? 29.92300 -117.41600 -20.64800 1.000 101.12075 ? 320 HIS   B CG    1 
ATOM   7254 N  ND1   . HIS   B  2 328 ? 30.77700 -116.51400 -21.25700 1.000 100.39019 ? 320 HIS   B ND1   1 
ATOM   7255 C  CD2   . HIS   B  2 328 ? 30.67400 -118.49600 -20.33500 1.000 104.59159 ? 320 HIS   B CD2   1 
ATOM   7256 C  CE1   . HIS   B  2 328 ? 31.99100 -117.02500 -21.30500 1.000 107.18071 ? 320 HIS   B CE1   1 
ATOM   7257 N  NE2   . HIS   B  2 328 ? 31.95500 -118.24200 -20.74800 1.000 109.01469 ? 320 HIS   B NE2   1 
ATOM   7258 N  N     . GLN   B  2 329 ? 26.29400 -119.03000 -22.77100 1.000 96.25693  ? 321 GLN   B N     1 
ATOM   7259 C  CA    . GLN   B  2 329 ? 25.99400 -120.38900 -23.29700 1.000 97.94381  ? 321 GLN   B CA    1 
ATOM   7260 C  C     . GLN   B  2 329 ? 26.43200 -120.46000 -24.76300 1.000 97.85321  ? 321 GLN   B C     1 
ATOM   7261 O  O     . GLN   B  2 329 ? 26.21700 -119.47400 -25.49500 1.000 95.23292  ? 321 GLN   B O     1 
ATOM   7262 C  CB    . GLN   B  2 329 ? 24.50700 -120.72900 -23.16300 1.000 98.63485  ? 321 GLN   B CB    1 
ATOM   7263 C  CG    . GLN   B  2 329 ? 24.16600 -121.52500 -21.91100 1.000 101.81373 ? 321 GLN   B CG    1 
ATOM   7264 C  CD    . GLN   B  2 329 ? 22.82800 -122.21400 -22.02100 1.000 103.00445 ? 321 GLN   B CD    1 
ATOM   7265 O  OE1   . GLN   B  2 329 ? 22.72700 -123.43500 -21.91000 1.000 105.60802 ? 321 GLN   B OE1   1 
ATOM   7266 N  NE2   . GLN   B  2 329 ? 21.78600 -121.43100 -22.25100 1.000 101.33523 ? 321 GLN   B NE2   1 
ATOM   7267 N  N     . VAL   B  2 330 ? 27.04300 -121.58200 -25.15400 1.000 106.01144 ? 322 VAL   B N     1 
ATOM   7268 C  CA    . VAL   B  2 330 ? 27.34400 -121.94800 -26.56900 1.000 97.61428  ? 322 VAL   B CA    1 
ATOM   7269 C  C     . VAL   B  2 330 ? 26.55500 -123.22300 -26.87700 1.000 99.71148  ? 322 VAL   B C     1 
ATOM   7270 O  O     . VAL   B  2 330 ? 27.12100 -124.31700 -26.72500 1.000 113.66009 ? 322 VAL   B O     1 
ATOM   7271 C  CB    . VAL   B  2 330 ? 28.85800 -122.12600 -26.80700 1.000 98.15054  ? 322 VAL   B CB    1 
ATOM   7272 C  CG1   . VAL   B  2 330 ? 29.17500 -122.43400 -28.26200 1.000 104.00056 ? 322 VAL   B CG1   1 
ATOM   7273 C  CG2   . VAL   B  2 330 ? 29.64300 -120.91000 -26.34400 1.000 100.06812 ? 322 VAL   B CG2   1 
ATOM   7274 N  N     . VAL   B  2 331 ? 25.28300 -123.07300 -27.25600 1.000 98.91187  ? 323 VAL   B N     1 
ATOM   7275 C  CA    . VAL   B  2 331 ? 24.33700 -124.20000 -27.51100 1.000 100.97969 ? 323 VAL   B CA    1 
ATOM   7276 C  C     . VAL   B  2 331 ? 24.55600 -124.70700 -28.94100 1.000 105.48006 ? 323 VAL   B C     1 
ATOM   7277 O  O     . VAL   B  2 331 ? 24.65600 -123.86400 -29.85400 1.000 101.05770 ? 323 VAL   B O     1 
ATOM   7278 C  CB    . VAL   B  2 331 ? 22.87300 -123.77300 -27.28300 1.000 100.29726 ? 323 VAL   B CB    1 
ATOM   7279 C  CG1   . VAL   B  2 331 ? 21.90000 -124.91700 -27.52900 1.000 102.63345 ? 323 VAL   B CG1   1 
ATOM   7280 C  CG2   . VAL   B  2 331 ? 22.66500 -123.19100 -25.89200 1.000 100.42403 ? 323 VAL   B CG2   1 
ATOM   7281 N  N     . HIS   B  2 332 ? 24.62800 -126.03400 -29.11100 1.000 109.91393 ? 324 HIS   B N     1 
ATOM   7282 C  CA    . HIS   B  2 332 ? 24.72700 -126.74400 -30.41600 1.000 104.59459 ? 324 HIS   B CA    1 
ATOM   7283 C  C     . HIS   B  2 332 ? 23.38700 -127.42400 -30.71800 1.000 105.99369 ? 324 HIS   B C     1 
ATOM   7284 O  O     . HIS   B  2 332 ? 22.98800 -128.30900 -29.93600 1.000 108.63149 ? 324 HIS   B O     1 
ATOM   7285 C  CB    . HIS   B  2 332 ? 25.88300 -127.75400 -30.39400 1.000 107.11651 ? 324 HIS   B CB    1 
ATOM   7286 C  CG    . HIS   B  2 332 ? 27.19600 -127.15900 -30.00800 1.000 106.24822 ? 324 HIS   B CG    1 
ATOM   7287 N  ND1   . HIS   B  2 332 ? 27.85600 -126.24400 -30.80700 1.000 104.45046 ? 324 HIS   B ND1   1 
ATOM   7288 C  CD2   . HIS   B  2 332 ? 27.97600 -127.34600 -28.92200 1.000 108.07601 ? 324 HIS   B CD2   1 
ATOM   7289 C  CE1   . HIS   B  2 332 ? 28.98400 -125.89100 -30.22600 1.000 109.64652 ? 324 HIS   B CE1   1 
ATOM   7290 N  NE2   . HIS   B  2 332 ? 29.08100 -126.55300 -29.06800 1.000 112.12763 ? 324 HIS   B NE2   1 
ATOM   7291 N  N     . HIS   B  2 333 ? 22.73100 -127.02700 -31.81300 1.000 105.42984 ? 325 HIS   B N     1 
ATOM   7292 C  CA    . HIS   B  2 333 ? 21.35800 -127.45600 -32.19800 1.000 108.49281 ? 325 HIS   B CA    1 
ATOM   7293 C  C     . HIS   B  2 333 ? 21.42300 -128.48200 -33.33400 1.000 110.70600 ? 325 HIS   B C     1 
ATOM   7294 O  O     . HIS   B  2 333 ? 22.27100 -128.30800 -34.23000 1.000 110.43475 ? 325 HIS   B O     1 
ATOM   7295 C  CB    . HIS   B  2 333 ? 20.51500 -126.24300 -32.61600 1.000 107.02825 ? 325 HIS   B CB    1 
ATOM   7296 C  CG    . HIS   B  2 333 ? 20.47800 -125.14600 -31.60500 1.000 109.34377 ? 325 HIS   B CG    1 
ATOM   7297 N  ND1   . HIS   B  2 333 ? 19.51200 -125.08200 -30.62000 1.000 106.31896 ? 325 HIS   B ND1   1 
ATOM   7298 C  CD2   . HIS   B  2 333 ? 21.27400 -124.06900 -31.42700 1.000 103.55621 ? 325 HIS   B CD2   1 
ATOM   7299 C  CE1   . HIS   B  2 333 ? 19.71900 -124.01300 -29.87800 1.000 102.26455 ? 325 HIS   B CE1   1 
ATOM   7300 N  NE2   . HIS   B  2 333 ? 20.79300 -123.37600 -30.35100 1.000 99.06865  ? 325 HIS   B NE2   1 
ATOM   7301 N  N     . VAL   B  2 334 ? 20.55800 -129.50200 -33.28700 1.000 114.50259 ? 326 VAL   B N     1 
ATOM   7302 C  CA    . VAL   B  2 334 ? 20.25200 -130.41300 -34.43300 1.000 114.25445 ? 326 VAL   B CA    1 
ATOM   7303 C  C     . VAL   B  2 334 ? 18.93900 -129.93000 -35.06200 1.000 116.14516 ? 326 VAL   B C     1 
ATOM   7304 O  O     . VAL   B  2 334 ? 17.94500 -129.79100 -34.31900 1.000 120.92878 ? 326 VAL   B O     1 
ATOM   7305 C  CB    . VAL   B  2 334 ? 20.19300 -131.90000 -34.01900 1.000 116.50152 ? 326 VAL   B CB    1 
ATOM   7306 C  CG1   . VAL   B  2 334 ? 21.53100 -132.38500 -33.48300 1.000 117.80157 ? 326 VAL   B CG1   1 
ATOM   7307 C  CG2   . VAL   B  2 334 ? 19.08300 -132.20400 -33.02200 1.000 124.08734 ? 326 VAL   B CG2   1 
ATOM   7308 N  N     . VAL   B  2 335 ? 18.95200 -129.64700 -36.36900 1.000 111.51266 ? 327 VAL   B N     1 
ATOM   7309 C  CA    . VAL   B  2 335 ? 17.81000 -129.04000 -37.11900 1.000 113.25085 ? 327 VAL   B CA    1 
ATOM   7310 C  C     . VAL   B  2 335 ? 17.17200 -130.12100 -37.99000 1.000 124.32313 ? 327 VAL   B C     1 
ATOM   7311 O  O     . VAL   B  2 335 ? 17.83900 -130.69400 -38.85000 1.000 124.88107 ? 327 VAL   B O     1 
ATOM   7312 C  CB    . VAL   B  2 335 ? 18.27100 -127.82900 -37.95400 1.000 112.21777 ? 327 VAL   B CB    1 
ATOM   7313 C  CG1   . VAL   B  2 335 ? 17.09800 -127.10400 -38.59700 1.000 106.03458 ? 327 VAL   B CG1   1 
ATOM   7314 C  CG2   . VAL   B  2 335 ? 19.10300 -126.85500 -37.13100 1.000 110.20991 ? 327 VAL   B CG2   1 
ATOM   7315 N  N     . PRO   B  2 336 ? 15.86600 -130.43200 -37.80100 1.000 134.01809 ? 328 PRO   B N     1 
ATOM   7316 C  CA    . PRO   B  2 336 ? 15.20600 -131.49000 -38.56800 1.000 133.81497 ? 328 PRO   B CA    1 
ATOM   7317 C  C     . PRO   B  2 336 ? 14.81500 -131.03500 -39.98300 1.000 129.37227 ? 328 PRO   B C     1 
ATOM   7318 O  O     . PRO   B  2 336 ? 15.65800 -130.97200 -40.88200 1.000 128.77451 ? 328 PRO   B O     1 
ATOM   7319 C  CB    . PRO   B  2 336 ? 13.96800 -131.80200 -37.71500 1.000 134.48533 ? 328 PRO   B CB    1 
ATOM   7320 C  CG    . PRO   B  2 336 ? 13.62200 -130.47500 -37.07300 1.000 133.39426 ? 328 PRO   B CG    1 
ATOM   7321 C  CD    . PRO   B  2 336 ? 14.95400 -129.78700 -36.84300 1.000 126.74139 ? 328 PRO   B CD    1 
HETATM 7322 C  CS    . MTA   C  3 .   ? 21.41800 -38.85100  -6.56600  1.000 58.72724  ? 701 MTA   A CS    1 
HETATM 7323 S  "S5'" . MTA   C  3 .   ? 19.90700 -39.73900  -6.57000  1.000 61.74759  ? 701 MTA   A "S5'" 1 
HETATM 7324 C  "C5'" . MTA   C  3 .   ? 18.92700 -38.33200  -6.20000  1.000 60.35041  ? 701 MTA   A "C5'" 1 
HETATM 7325 C  "C4'" . MTA   C  3 .   ? 19.19600 -37.77300  -4.80700  1.000 60.42598  ? 701 MTA   A "C4'" 1 
HETATM 7326 O  "O4'" . MTA   C  3 .   ? 18.19500 -36.78000  -4.62900  1.000 58.50799  ? 701 MTA   A "O4'" 1 
HETATM 7327 C  "C2'" . MTA   C  3 .   ? 17.69900 -38.47800  -3.05900  1.000 57.99432  ? 701 MTA   A "C2'" 1 
HETATM 7328 O  "O2'" . MTA   C  3 .   ? 17.66400 -38.62300  -1.63600  1.000 60.62282  ? 701 MTA   A "O2'" 1 
HETATM 7329 C  "C3'" . MTA   C  3 .   ? 19.06900 -38.74700  -3.63800  1.000 60.09617  ? 701 MTA   A "C3'" 1 
HETATM 7330 O  "O3'" . MTA   C  3 .   ? 20.06700 -38.44100  -2.66000  1.000 51.89111  ? 701 MTA   A "O3'" 1 
HETATM 7331 C  "C1'" . MTA   C  3 .   ? 17.43900 -37.03400  -3.45700  1.000 56.84582  ? 701 MTA   A "C1'" 1 
HETATM 7332 N  N9    . MTA   C  3 .   ? 16.00800 -36.76700  -3.70800  1.000 54.74024  ? 701 MTA   A N9    1 
HETATM 7333 C  C8    . MTA   C  3 .   ? 15.12400 -37.55900  -4.34300  1.000 56.64080  ? 701 MTA   A C8    1 
HETATM 7334 N  N7    . MTA   C  3 .   ? 13.89900 -36.97800  -4.37000  1.000 50.24066  ? 701 MTA   A N7    1 
HETATM 7335 C  C5    . MTA   C  3 .   ? 13.99900 -35.79700  -3.74500  1.000 52.21299  ? 701 MTA   A C5    1 
HETATM 7336 C  C6    . MTA   C  3 .   ? 13.08900 -34.68200  -3.41500  1.000 53.91459  ? 701 MTA   A C6    1 
HETATM 7337 N  N6    . MTA   C  3 .   ? 11.78900 -34.72000  -3.77900  1.000 61.69512  ? 701 MTA   A N6    1 
HETATM 7338 N  N1    . MTA   C  3 .   ? 13.60000 -33.62200  -2.74900  1.000 53.31967  ? 701 MTA   A N1    1 
HETATM 7339 C  C2    . MTA   C  3 .   ? 14.89600 -33.56200  -2.37800  1.000 63.58086  ? 701 MTA   A C2    1 
HETATM 7340 N  N3    . MTA   C  3 .   ? 15.77500 -34.54700  -2.64400  1.000 61.72539  ? 701 MTA   A N3    1 
HETATM 7341 C  C4    . MTA   C  3 .   ? 15.39300 -35.66100  -3.31400  1.000 57.20185  ? 701 MTA   A C4    1 
HETATM 7342 N  N3    . A1BLI D  4 .   ? 25.70200 -38.34300  -4.02600  1.000 67.28904  ? 702 A1BLI A N3    1 
HETATM 7343 C  C4    . A1BLI D  4 .   ? 24.72800 -37.62300  -4.49500  1.000 63.26673  ? 702 A1BLI A C4    1 
HETATM 7344 C  C5    . A1BLI D  4 .   ? 24.33900 -38.13800  -5.72500  1.000 60.54229  ? 702 A1BLI A C5    1 
HETATM 7345 C  C6    . A1BLI D  4 .   ? 25.09700 -39.22300  -5.98500  1.000 64.28223  ? 702 A1BLI A C6    1 
HETATM 7346 C  C7    . A1BLI D  4 .   ? 25.06200 -40.09200  -7.21700  1.000 70.43924  ? 702 A1BLI A C7    1 
HETATM 7347 C  C8    . A1BLI D  4 .   ? 23.91300 -41.04300  -7.44600  1.000 67.66225  ? 702 A1BLI A C8    1 
HETATM 7348 C  C10   . A1BLI D  4 .   ? 21.82200 -42.12600  -6.97400  1.000 67.40138  ? 702 A1BLI A C10   1 
HETATM 7349 C  C15   . A1BLI D  4 .   ? 23.20600 -43.41300  -10.26800 1.000 65.58002  ? 702 A1BLI A C15   1 
HETATM 7350 C  C17   . A1BLI D  4 .   ? 23.99000 -41.76000  -8.61800  1.000 70.64443  ? 702 A1BLI A C17   1 
HETATM 7351 C  C20   . A1BLI D  4 .   ? 21.02600 -48.60300  -9.26300  1.000 58.56945  ? 702 A1BLI A C20   1 
HETATM 7352 C  C22   . A1BLI D  4 .   ? 19.38500 -47.72000  -10.86800 1.000 58.59200  ? 702 A1BLI A C22   1 
HETATM 7353 C  C28   . A1BLI D  4 .   ? 22.09600 -51.33400  -10.54500 1.000 49.98245  ? 702 A1BLI A C28   1 
HETATM 7354 C  C1    . A1BLI D  4 .   ? 26.98000 -40.35600  -4.79600  1.000 66.17911  ? 702 A1BLI A C1    1 
HETATM 7355 C  C11   . A1BLI D  4 .   ? 21.91800 -42.84400  -8.15500  1.000 75.56184  ? 702 A1BLI A C11   1 
HETATM 7356 C  C12   . A1BLI D  4 .   ? 20.83000 -43.81200  -8.52200  1.000 67.80337  ? 702 A1BLI A C12   1 
HETATM 7357 C  C14   . A1BLI D  4 .   ? 22.06700 -44.39200  -10.55200 1.000 62.19820  ? 702 A1BLI A C14   1 
HETATM 7358 C  C16   . A1BLI D  4 .   ? 23.01000 -42.66300  -8.97600  1.000 72.95114  ? 702 A1BLI A C16   1 
HETATM 7359 C  C18   . A1BLI D  4 .   ? 20.64500 -46.11000  -9.39800  1.000 60.95700  ? 702 A1BLI A C18   1 
HETATM 7360 C  C19   . A1BLI D  4 .   ? 21.64000 -47.21800  -9.04700  1.000 58.57851  ? 702 A1BLI A C19   1 
HETATM 7361 C  C23   . A1BLI D  4 .   ? 19.99800 -46.32100  -10.78700 1.000 60.95072  ? 702 A1BLI A C23   1 
HETATM 7362 C  C25   . A1BLI D  4 .   ? 21.10100 -49.33300  -11.63800 1.000 57.76413  ? 702 A1BLI A C25   1 
HETATM 7363 C  C27   . A1BLI D  4 .   ? 22.26500 -50.19300  -11.33900 1.000 53.44846  ? 702 A1BLI A C27   1 
HETATM 7364 C  C29   . A1BLI D  4 .   ? 23.19300 -52.11400  -10.25900 1.000 57.40216  ? 702 A1BLI A C29   1 
HETATM 7365 C  C31   . A1BLI D  4 .   ? 24.60000 -50.73000  -11.47900 1.000 53.95649  ? 702 A1BLI A C31   1 
HETATM 7366 C  C33   . A1BLI D  4 .   ? 26.99000 -51.32800  -11.43000 1.000 57.68511  ? 702 A1BLI A C33   1 
HETATM 7367 C  C34   . A1BLI D  4 .   ? 28.19100 -51.47500  -12.37600 1.000 67.40617  ? 702 A1BLI A C34   1 
HETATM 7368 C  C35   . A1BLI D  4 .   ? 29.03800 -51.52700  -11.09300 1.000 65.72912  ? 702 A1BLI A C35   1 
HETATM 7369 C  C36   . A1BLI D  4 .   ? 27.96800 -50.59800  -10.49600 1.000 56.67780  ? 702 A1BLI A C36   1 
HETATM 7370 C  C37   . A1BLI D  4 .   ? 23.54500 -49.88300  -11.81200 1.000 54.06681  ? 702 A1BLI A C37   1 
HETATM 7371 C  C9    . A1BLI D  4 .   ? 22.81900 -41.22900  -6.61500  1.000 63.81303  ? 702 A1BLI A C9    1 
HETATM 7372 N  N13   . A1BLI D  4 .   ? 21.44700 -44.87800  -9.30300  1.000 62.18832  ? 702 A1BLI A N13   1 
HETATM 7373 N  N2    . A1BLI D  4 .   ? 25.95900 -39.34300  -4.96200  1.000 64.16545  ? 702 A1BLI A N2    1 
HETATM 7374 N  N21   . A1BLI D  4 .   ? 20.52500 -48.61300  -10.64400 1.000 58.85958  ? 702 A1BLI A N21   1 
HETATM 7375 N  N30   . A1BLI D  4 .   ? 24.38300 -51.79600  -10.72400 1.000 56.55619  ? 702 A1BLI A N30   1 
HETATM 7376 N  N32   . A1BLI D  4 .   ? 25.89500 -50.48200  -11.92500 1.000 54.87252  ? 702 A1BLI A N32   1 
HETATM 7377 O  O24   . A1BLI D  4 .   ? 18.98500 -45.34400  -11.02100 1.000 61.37958  ? 702 A1BLI A O24   1 
HETATM 7378 O  O26   . A1BLI D  4 .   ? 20.66600 -49.30200  -12.77000 1.000 58.99681  ? 702 A1BLI A O26   1 
HETATM 7379 C  C1    . EDO   E  5 .   ? 7.63500  -83.50700  -28.13800 1.000 56.02094  ? 703 EDO   A C1    1 
HETATM 7380 O  O1    . EDO   E  5 .   ? 8.92600  -83.01100  -28.43000 1.000 58.49633  ? 703 EDO   A O1    1 
HETATM 7381 C  C2    . EDO   E  5 .   ? 6.56100  -82.85700  -28.92900 1.000 61.64075  ? 703 EDO   A C2    1 
HETATM 7382 O  O2    . EDO   E  5 .   ? 6.79300  -82.88200  -30.32600 1.000 69.83021  ? 703 EDO   A O2    1 
HETATM 7383 C  C1    . EDO   F  5 .   ? -0.16800 -43.26200  -28.72300 1.000 73.42094  ? 704 EDO   A C1    1 
HETATM 7384 O  O1    . EDO   F  5 .   ? 1.12600  -43.78200  -28.95300 1.000 71.64094  ? 704 EDO   A O1    1 
HETATM 7385 C  C2    . EDO   F  5 .   ? -1.09500 -44.25700  -28.12800 1.000 73.94094  ? 704 EDO   A C2    1 
HETATM 7386 O  O2    . EDO   F  5 .   ? -2.38000 -43.73800  -27.85000 1.000 74.71094  ? 704 EDO   A O2    1 
HETATM 7387 C  C1    . EDO   G  5 .   ? 4.03000  -102.59100 -31.11700 1.000 77.63094  ? 705 EDO   A C1    1 
HETATM 7388 O  O1    . EDO   G  5 .   ? 3.37800  -103.79700 -31.46000 1.000 83.40743  ? 705 EDO   A O1    1 
HETATM 7389 C  C2    . EDO   G  5 .   ? 3.13500  -101.40700 -31.17100 1.000 81.87027  ? 705 EDO   A C2    1 
HETATM 7390 O  O2    . EDO   G  5 .   ? 2.70000  -100.96600 -29.89900 1.000 85.14168  ? 705 EDO   A O2    1 
HETATM 7391 C  C1    . EDO   H  5 .   ? -3.53400 -42.86000  -18.78600 1.000 82.89094  ? 706 EDO   A C1    1 
HETATM 7392 O  O1    . EDO   H  5 .   ? -4.61800 -43.74000  -19.01300 1.000 82.08094  ? 706 EDO   A O1    1 
HETATM 7393 C  C2    . EDO   H  5 .   ? -2.87400 -43.07900  -17.47300 1.000 82.74094  ? 706 EDO   A C2    1 
HETATM 7394 O  O2    . EDO   H  5 .   ? -3.47800 -42.38800  -16.39300 1.000 82.55094  ? 706 EDO   A O2    1 
HETATM 7395 C  C1    . EDO   I  5 .   ? 8.43500  -39.10900  0.61900   1.000 70.92094  ? 707 EDO   A C1    1 
HETATM 7396 O  O1    . EDO   I  5 .   ? 7.18300  -38.45900  0.68200   1.000 74.55368  ? 707 EDO   A O1    1 
HETATM 7397 C  C2    . EDO   I  5 .   ? 9.58200  -38.18000  0.77900   1.000 71.38094  ? 707 EDO   A C2    1 
HETATM 7398 O  O2    . EDO   I  5 .   ? 10.73000 -38.79000  1.33800   1.000 76.18375  ? 707 EDO   A O2    1 
HETATM 7399 C  C1    . EDO   J  5 .   ? 15.63600 -65.94500  -29.80000 1.000 55.47094  ? 708 EDO   A C1    1 
HETATM 7400 O  O1    . EDO   J  5 .   ? 15.03100 -65.40700  -30.95700 1.000 56.37512  ? 708 EDO   A O1    1 
HETATM 7401 C  C2    . EDO   J  5 .   ? 15.03600 -67.23700  -29.39000 1.000 55.32094  ? 708 EDO   A C2    1 
HETATM 7402 O  O2    . EDO   J  5 .   ? 14.70900 -68.06700  -30.48700 1.000 54.96094  ? 708 EDO   A O2    1 
HETATM 7403 C  C1    . EDO   K  5 .   ? 21.93200 -51.23800  12.33800  1.000 84.22094  ? 709 EDO   A C1    1 
HETATM 7404 O  O1    . EDO   K  5 .   ? 22.95600 -51.90200  11.62600  1.000 82.59094  ? 709 EDO   A O1    1 
HETATM 7405 C  C2    . EDO   K  5 .   ? 20.87800 -50.68400  11.45400  1.000 83.74094  ? 709 EDO   A C2    1 
HETATM 7406 O  O2    . EDO   K  5 .   ? 19.79500 -50.09500  12.15100  1.000 82.99094  ? 709 EDO   A O2    1 
HETATM 7407 C  C1    . EDO   L  5 .   ? 15.83900 -33.49000  -28.77400 1.000 79.83094  ? 710 EDO   A C1    1 
HETATM 7408 O  O1    . EDO   L  5 .   ? 16.41400 -34.78100  -28.75600 1.000 79.06094  ? 710 EDO   A O1    1 
HETATM 7409 C  C2    . EDO   L  5 .   ? 14.36300 -33.51400  -28.91800 1.000 81.55176  ? 710 EDO   A C2    1 
HETATM 7410 O  O2    . EDO   L  5 .   ? 13.75200 -32.27700  -28.60800 1.000 80.51094  ? 710 EDO   A O2    1 
HETATM 7411 C  C1    . EDO   M  5 .   ? 20.01600 -100.05400 -10.59800 1.000 68.13656  ? 711 EDO   A C1    1 
HETATM 7412 O  O1    . EDO   M  5 .   ? 21.41500 -99.96200  -10.76100 1.000 71.69978  ? 711 EDO   A O1    1 
HETATM 7413 C  C2    . EDO   M  5 .   ? 19.47500 -101.38500 -10.97400 1.000 66.12187  ? 711 EDO   A C2    1 
HETATM 7414 O  O2    . EDO   M  5 .   ? 18.07300 -101.39500 -11.17100 1.000 70.71293  ? 711 EDO   A O2    1 
HETATM 7415 C  C1    . EDO   N  5 .   ? 23.69900 -69.34100  -19.66800 1.000 83.97094  ? 712 EDO   A C1    1 
HETATM 7416 O  O1    . EDO   N  5 .   ? 22.51400 -69.90500  -19.13900 1.000 83.55094  ? 712 EDO   A O1    1 
HETATM 7417 C  C2    . EDO   N  5 .   ? 23.59000 -67.87900  -19.92300 1.000 83.76094  ? 712 EDO   A C2    1 
HETATM 7418 O  O2    . EDO   N  5 .   ? 24.51800 -67.07700  -19.21300 1.000 86.24124  ? 712 EDO   A O2    1 
HETATM 7419 C  C1    . EDO   O  5 .   ? 30.73800 -45.68800  3.36900   1.000 68.99902  ? 713 EDO   A C1    1 
HETATM 7420 O  O1    . EDO   O  5 .   ? 29.49700 -45.90700  4.00400   1.000 66.54034  ? 713 EDO   A O1    1 
HETATM 7421 C  C2    . EDO   O  5 .   ? 30.95700 -44.28900  2.93700   1.000 73.23338  ? 713 EDO   A C2    1 
HETATM 7422 O  O2    . EDO   O  5 .   ? 32.32300 -43.98600  2.73000   1.000 79.11314  ? 713 EDO   A O2    1 
HETATM 7423 C  C1    . EDO   P  5 .   ? 13.90100 -58.98100  -6.46200  1.000 75.24094  ? 714 EDO   A C1    1 
HETATM 7424 O  O1    . EDO   P  5 .   ? 14.84200 -58.19600  -7.16700  1.000 73.98094  ? 714 EDO   A O1    1 
HETATM 7425 C  C2    . EDO   P  5 .   ? 13.93900 -60.42000  -6.82600  1.000 75.17094  ? 714 EDO   A C2    1 
HETATM 7426 O  O2    . EDO   P  5 .   ? 15.22800 -60.88800  -7.18100  1.000 75.46094  ? 714 EDO   A O2    1 
HETATM 7427 C  C1    . EDO   Q  5 .   ? -3.15700 -49.38000  -33.32000 1.000 89.77094  ? 715 EDO   A C1    1 
HETATM 7428 O  O1    . EDO   Q  5 .   ? -1.78300 -49.05400  -33.35900 1.000 89.02094  ? 715 EDO   A O1    1 
HETATM 7429 C  C2    . EDO   Q  5 .   ? -3.41200 -50.83600  -33.44200 1.000 89.90094  ? 715 EDO   A C2    1 
HETATM 7430 O  O2    . EDO   Q  5 .   ? -4.76700 -51.18700  -33.23600 1.000 89.22094  ? 715 EDO   A O2    1 
HETATM 7431 C  C1    . EDO   R  5 .   ? 1.60800  -97.50900  -24.21600 1.000 71.19055  ? 716 EDO   A C1    1 
HETATM 7432 O  O1    . EDO   R  5 .   ? 0.60000  -97.57800  -23.22800 1.000 72.59914  ? 716 EDO   A O1    1 
HETATM 7433 C  C2    . EDO   R  5 .   ? 2.92900  -98.00700  -23.75300 1.000 76.35380  ? 716 EDO   A C2    1 
HETATM 7434 O  O2    . EDO   R  5 .   ? 3.67900  -97.06500  -23.00700 1.000 70.68094  ? 716 EDO   A O2    1 
HETATM 7435 NA NA    . NA    S  6 .   ? 4.76900  -70.89600  -19.31300 1.000 50.71015  ? 717 NA    A NA    1 
HETATM 7436 NA NA    . NA    T  6 .   ? 30.33900 -80.14600  -14.73500 1.000 63.63545  ? 718 NA    A NA    1 
HETATM 7437 NA NA    . NA    U  6 .   ? -2.87200 -47.78500  -5.77100  1.000 66.44919  ? 719 NA    A NA    1 
HETATM 7438 NA NA    . NA    V  6 .   ? 2.95000  -52.21500  -4.00400  1.000 70.72020  ? 720 NA    A NA    1 
HETATM 7439 C  C1    . GOL   W  7 .   ? 11.88100 -78.28700  -10.34000 1.000 85.03551  ? 721 GOL   A C1    1 
HETATM 7440 O  O1    . GOL   W  7 .   ? 12.84400 -77.36900  -10.85100 1.000 80.97094  ? 721 GOL   A O1    1 
HETATM 7441 C  C2    . GOL   W  7 .   ? 11.91200 -78.34400  -8.82700  1.000 93.84383  ? 721 GOL   A C2    1 
HETATM 7442 O  O2    . GOL   W  7 .   ? 10.77400 -79.06100  -8.35000  1.000 88.45048  ? 721 GOL   A O2    1 
HETATM 7443 C  C3    . GOL   W  7 .   ? 13.17600 -78.97700  -8.28300  1.000 93.71328  ? 721 GOL   A C3    1 
HETATM 7444 O  O3    . GOL   W  7 .   ? 13.65400 -78.30600  -7.11800  1.000 95.61791  ? 721 GOL   A O3    1 
HETATM 7445 CL CL    . CL    X  8 .   ? 26.89000 -50.75800  -23.77400 1.000 90.44349  ? 722 CL    A CL    1 
HETATM 7446 C  C1    . EDO   Y  5 .   ? 20.51600 -92.23500  -32.85600 1.000 73.13384  ? 401 EDO   B C1    1 
HETATM 7447 O  O1    . EDO   Y  5 .   ? 19.16000 -91.90600  -33.08200 1.000 69.13094  ? 401 EDO   B O1    1 
HETATM 7448 C  C2    . EDO   Y  5 .   ? 21.45500 -91.21300  -33.38900 1.000 75.37764  ? 401 EDO   B C2    1 
HETATM 7449 O  O2    . EDO   Y  5 .   ? 22.81700 -91.44700  -33.07700 1.000 80.16983  ? 401 EDO   B O2    1 
HETATM 7450 C  C1    . EDO   Z  5 .   ? 47.58800 -99.14200  -35.57500 1.000 107.58199 ? 402 EDO   B C1    1 
HETATM 7451 O  O1    . EDO   Z  5 .   ? 47.62200 -100.11900 -36.59500 1.000 104.94721 ? 402 EDO   B O1    1 
HETATM 7452 C  C2    . EDO   Z  5 .   ? 47.26500 -97.78800  -36.09100 1.000 103.59297 ? 402 EDO   B C2    1 
HETATM 7453 O  O2    . EDO   Z  5 .   ? 47.85100 -96.73000  -35.35400 1.000 102.64038 ? 402 EDO   B O2    1 
HETATM 7454 O  O     . HOH   AA 9 .   ? 11.14700 -50.41700  -7.09400  1.000 52.85701  ? 801 HOH   A O     1 
HETATM 7455 O  O     . HOH   AA 9 .   ? 5.79700  -90.55900  -28.09700 1.000 60.47420  ? 802 HOH   A O     1 
HETATM 7456 O  O     . HOH   AA 9 .   ? 2.05900  -38.02000  -11.49800 1.000 58.91122  ? 803 HOH   A O     1 
HETATM 7457 O  O     . HOH   AA 9 .   ? 0.82700  -37.64100  -8.66300  1.000 63.17839  ? 804 HOH   A O     1 
HETATM 7458 O  O     . HOH   AA 9 .   ? 15.76000 -87.82000  -28.14100 1.000 47.16934  ? 805 HOH   A O     1 
HETATM 7459 O  O     . HOH   AA 9 .   ? 18.88100 -106.51400 -16.23900 1.000 56.90989  ? 806 HOH   A O     1 
HETATM 7460 O  O     . HOH   AA 9 .   ? 13.54100 -56.23600  -36.84300 1.000 60.42095  ? 807 HOH   A O     1 
HETATM 7461 O  O     . HOH   AA 9 .   ? 26.17300 -89.81900  -3.45200  1.000 66.96849  ? 808 HOH   A O     1 
HETATM 7462 O  O     . HOH   AA 9 .   ? 24.64600 -82.02300  -35.98100 1.000 57.89715  ? 809 HOH   A O     1 
HETATM 7463 O  O     . HOH   AA 9 .   ? 12.57100 -89.71700  -27.18000 1.000 50.60024  ? 810 HOH   A O     1 
HETATM 7464 O  O     . HOH   AA 9 .   ? 11.05000 -71.88500  -36.56300 1.000 62.07629  ? 811 HOH   A O     1 
HETATM 7465 O  O     . HOH   AA 9 .   ? 15.14100 -36.67500  -24.60400 1.000 50.57185  ? 812 HOH   A O     1 
HETATM 7466 O  O     . HOH   AA 9 .   ? 29.787   -28.397    -28.731   1.000 68.68762  ? 813 HOH   A O     1 
HETATM 7467 O  O     . HOH   AA 9 .   ? 13.52800 -78.75600  -43.54100 1.000 69.02261  ? 814 HOH   A O     1 
HETATM 7468 O  O     . HOH   AA 9 .   ? 5.93000  -47.66200  -33.18900 1.000 53.88200  ? 815 HOH   A O     1 
HETATM 7469 O  O     . HOH   AA 9 .   ? 15.44100 -65.77900  -33.61500 1.000 53.03912  ? 816 HOH   A O     1 
HETATM 7470 O  O     . HOH   AA 9 .   ? 20.94400 -30.61200  10.23100  1.000 59.24001  ? 817 HOH   A O     1 
HETATM 7471 O  O     . HOH   AA 9 .   ? 11.99300 -30.32400  -24.61400 1.000 66.99072  ? 818 HOH   A O     1 
HETATM 7472 O  O     . HOH   AA 9 .   ? 23.40900 -68.35300  -30.44900 1.000 61.15463  ? 819 HOH   A O     1 
HETATM 7473 O  O     . HOH   AA 9 .   ? 5.86200  -38.70700  -23.41900 1.000 48.96702  ? 820 HOH   A O     1 
HETATM 7474 O  O     . HOH   AA 9 .   ? 20.82000 -87.81000  -51.33500 1.000 67.88576  ? 821 HOH   A O     1 
HETATM 7475 O  O     . HOH   AA 9 .   ? 15.28500 -83.36500  -8.61600  1.000 91.15701  ? 822 HOH   A O     1 
HETATM 7476 O  O     . HOH   AA 9 .   ? 20.29600 -59.13500  -28.96700 1.000 56.11828  ? 823 HOH   A O     1 
HETATM 7477 O  O     . HOH   AA 9 .   ? 20.75400 -72.90900  -42.49300 1.000 61.66549  ? 824 HOH   A O     1 
HETATM 7478 O  O     . HOH   AA 9 .   ? 14.07600 -58.89600  -35.91200 1.000 59.03037  ? 825 HOH   A O     1 
HETATM 7479 O  O     . HOH   AA 9 .   ? 12.77800 -98.41900  -13.19200 1.000 47.17733  ? 826 HOH   A O     1 
HETATM 7480 O  O     . HOH   AA 9 .   ? 13.86400 -75.93600  -18.93600 1.000 47.49903  ? 827 HOH   A O     1 
HETATM 7481 O  O     . HOH   AA 9 .   ? 9.95900  -49.21600  1.22100   1.000 64.15468  ? 828 HOH   A O     1 
HETATM 7482 O  O     . HOH   AA 9 .   ? 18.67400 -63.30200  -37.66000 1.000 70.79186  ? 829 HOH   A O     1 
HETATM 7483 O  O     . HOH   AA 9 .   ? 1.65400  -67.70500  0.22800   1.000 61.31273  ? 830 HOH   A O     1 
HETATM 7484 O  O     . HOH   AA 9 .   ? 9.73900  -87.83700  -33.97700 1.000 48.11063  ? 831 HOH   A O     1 
HETATM 7485 O  O     . HOH   AA 9 .   ? 32.17100 -37.96600  -1.52400  1.000 68.10991  ? 832 HOH   A O     1 
HETATM 7486 O  O     . HOH   AA 9 .   ? 12.75100 -92.27000  -28.11000 1.000 45.82116  ? 833 HOH   A O     1 
HETATM 7487 O  O     . HOH   AA 9 .   ? 7.26300  -80.50900  -3.77800  1.000 89.02964  ? 834 HOH   A O     1 
HETATM 7488 O  O     . HOH   AA 9 .   ? 20.16900 -92.22900  -29.18100 1.000 56.08006  ? 835 HOH   A O     1 
HETATM 7489 O  O     . HOH   AA 9 .   ? 20.91500 -84.96900  -30.34800 1.000 52.29325  ? 836 HOH   A O     1 
HETATM 7490 O  O     . HOH   AA 9 .   ? 23.63400 -13.44700  -22.28100 1.000 91.69157  ? 837 HOH   A O     1 
HETATM 7491 O  O     . HOH   AA 9 .   ? 25.09600 -79.33900  -35.79400 1.000 52.80564  ? 838 HOH   A O     1 
HETATM 7492 O  O     . HOH   AA 9 .   ? -0.38400 -62.32500  -20.41200 1.000 43.64460  ? 839 HOH   A O     1 
HETATM 7493 O  O     . HOH   AA 9 .   ? 21.37100 -33.98900  9.00300   1.000 61.79623  ? 840 HOH   A O     1 
HETATM 7494 O  O     . HOH   AA 9 .   ? -7.29900 -51.00400  -34.86600 1.000 59.30856  ? 841 HOH   A O     1 
HETATM 7495 O  O     . HOH   AA 9 .   ? 20.18300 -47.64600  -1.42000  1.000 62.90350  ? 842 HOH   A O     1 
HETATM 7496 O  O     . HOH   AA 9 .   ? 18.81100 -51.41200  -8.32700  1.000 57.28528  ? 843 HOH   A O     1 
HETATM 7497 O  O     . HOH   AA 9 .   ? 19.60700 -92.19400  -25.56400 1.000 54.21105  ? 844 HOH   A O     1 
HETATM 7498 O  O     . HOH   AA 9 .   ? 4.64000  -34.97800  -6.01900  1.000 54.91821  ? 845 HOH   A O     1 
HETATM 7499 O  O     . HOH   AA 9 .   ? 17.00400 -85.83000  -9.49800  1.000 69.00778  ? 846 HOH   A O     1 
HETATM 7500 O  O     . HOH   AA 9 .   ? 13.81400 -65.25800  -45.08300 1.000 66.93754  ? 847 HOH   A O     1 
HETATM 7501 O  O     . HOH   AA 9 .   ? 36.70200 -33.45900  -9.70700  1.000 70.75052  ? 848 HOH   A O     1 
HETATM 7502 O  O     . HOH   AA 9 .   ? 4.90300  -77.85300  -32.35200 1.000 50.09390  ? 849 HOH   A O     1 
HETATM 7503 O  O     . HOH   AA 9 .   ? 36.58800 -23.35400  4.87900   1.000 67.45271  ? 850 HOH   A O     1 
HETATM 7504 O  O     . HOH   AA 9 .   ? 6.63400  -19.36400  -4.97000  1.000 61.67860  ? 851 HOH   A O     1 
HETATM 7505 O  O     . HOH   AA 9 .   ? 18.02700 -104.17000 -15.08500 1.000 53.11025  ? 852 HOH   A O     1 
HETATM 7506 O  O     . HOH   AA 9 .   ? 8.51900  -39.99300  -27.64100 1.000 51.34584  ? 853 HOH   A O     1 
HETATM 7507 O  O     . HOH   AA 9 .   ? 13.51700 -46.20500  3.72400   1.000 61.39078  ? 854 HOH   A O     1 
HETATM 7508 O  O     . HOH   AA 9 .   ? 24.03500 -10.56300  -9.35000  1.000 82.72375  ? 855 HOH   A O     1 
HETATM 7509 O  O     . HOH   AA 9 .   ? 34.79700 -79.58900  -12.67000 1.000 70.13523  ? 856 HOH   A O     1 
HETATM 7510 O  O     . HOH   AA 9 .   ? 14.01900 -33.61200  5.27100   1.000 53.14919  ? 857 HOH   A O     1 
HETATM 7511 O  O     . HOH   AA 9 .   ? 5.92000  -52.06300  -5.01000  1.000 50.50735  ? 858 HOH   A O     1 
HETATM 7512 O  O     . HOH   AA 9 .   ? 17.29200 -85.84000  -38.02700 1.000 61.26556  ? 859 HOH   A O     1 
HETATM 7513 O  O     . HOH   AA 9 .   ? 15.60400 -91.75800  -29.36600 1.000 55.87145  ? 860 HOH   A O     1 
HETATM 7514 O  O     . HOH   AA 9 .   ? 23.21500 -84.78500  -7.67800  1.000 68.78385  ? 861 HOH   A O     1 
HETATM 7515 O  O     . HOH   AA 9 .   ? 0.948    -47.589    -38.496   1.000 63.03146  ? 862 HOH   A O     1 
HETATM 7516 O  O     . HOH   AA 9 .   ? 2.330    -36.269    -23.639   1.000 60.47758  ? 863 HOH   A O     1 
HETATM 7517 O  O     . HOH   AA 9 .   ? 5.403    -44.384    -30.881   1.000 55.09653  ? 864 HOH   A O     1 
HETATM 7518 O  O     . HOH   AA 9 .   ? 9.20500  -19.04500  -5.60100  1.000 72.11792  ? 865 HOH   A O     1 
HETATM 7519 O  O     . HOH   AA 9 .   ? 30.01500 -73.18200  -16.43700 1.000 67.42499  ? 866 HOH   A O     1 
HETATM 7520 O  O     . HOH   AA 9 .   ? 19.283   -45.583    5.251     1.000 63.58187  ? 867 HOH   A O     1 
HETATM 7521 O  O     . HOH   AA 9 .   ? 6.25400  -48.02500  -36.25400 1.000 59.91831  ? 868 HOH   A O     1 
HETATM 7522 O  O     . HOH   AA 9 .   ? 17.21600 -27.28400  7.15700   1.000 64.57263  ? 869 HOH   A O     1 
HETATM 7523 O  O     . HOH   AA 9 .   ? 17.41300 -37.55700  -25.59000 1.000 57.46416  ? 870 HOH   A O     1 
HETATM 7524 O  O     . HOH   AA 9 .   ? 4.23600  -27.23400  -12.98000 1.000 70.55748  ? 871 HOH   A O     1 
HETATM 7525 O  O     . HOH   AA 9 .   ? 38.912   -95.296    -4.567    1.000 70.43750  ? 872 HOH   A O     1 
HETATM 7526 O  O     . HOH   AA 9 .   ? 0.74000  -30.22800  -15.55600 1.000 66.57424  ? 873 HOH   A O     1 
HETATM 7527 O  O     . HOH   AA 9 .   ? 18.71900 -29.52400  9.32600   1.000 60.41567  ? 874 HOH   A O     1 
HETATM 7528 O  O     . HOH   AA 9 .   ? 4.532    -75.137    -11.255   1.000 63.79248  ? 875 HOH   A O     1 
HETATM 7529 O  O     . HOH   AA 9 .   ? 30.85500 -80.64100  -47.45100 1.000 74.13268  ? 876 HOH   A O     1 
HETATM 7530 O  O     . HOH   AA 9 .   ? 42.70300 -69.15400  -39.32500 1.000 63.77375  ? 877 HOH   A O     1 
HETATM 7531 O  O     . HOH   AA 9 .   ? 20.94700 -10.01000  -10.38000 1.000 68.82891  ? 878 HOH   A O     1 
HETATM 7532 O  O     . HOH   BA 9 .   ? 53.27200 -119.93800 -35.04000 1.000 119.79144 ? 501 HOH   B O     1 
HETATM 7533 O  O     . HOH   BA 9 .   ? 37.95000 -104.18300 -29.22400 1.000 84.91534  ? 502 HOH   B O     1 
HETATM 7534 O  O     . HOH   BA 9 .   ? 24.04500 -113.48100 -41.84400 1.000 69.26335  ? 503 HOH   B O     1 
HETATM 7535 O  O     . HOH   BA 9 .   ? 15.66900 -100.67300 -32.96700 1.000 55.85835  ? 504 HOH   B O     1 
HETATM 7536 O  O     . HOH   BA 9 .   ? 7.297    -101.296   -51.913   1.000 130.87723 ? 505 HOH   B O     1 
HETATM 7537 O  O     . HOH   BA 9 .   ? 6.45500  -105.64600 -37.92700 1.000 63.39477  ? 506 HOH   B O     1 
HETATM 7538 O  O     . HOH   BA 9 .   ? 25.62200 -93.22400  -29.60600 1.000 63.93599  ? 507 HOH   B O     1 
HETATM 7539 O  O     . HOH   BA 9 .   ? 10.32800 -99.77600  -41.91400 1.000 80.41146  ? 508 HOH   B O     1 
HETATM 7540 O  O     . HOH   BA 9 .   ? 23.164   -117.578   -16.371   1.000 89.03237  ? 509 HOH   B O     1 
HETATM 7541 O  O     . HOH   BA 9 .   ? 19.80100 -89.16300  -35.14400 1.000 61.19559  ? 510 HOH   B O     1 
HETATM 7542 O  O     . HOH   BA 9 .   ? 24.48800 -110.72500 -42.67800 1.000 58.66527  ? 511 HOH   B O     1 
HETATM 7543 O  O     . HOH   BA 9 .   ? 32.69100 -114.40000 -40.52300 1.000 89.70737  ? 512 HOH   B O     1 
HETATM 7544 O  O     . HOH   BA 9 .   ? 43.50000 -126.84100 -29.35500 1.000 103.81695 ? 513 HOH   B O     1 
HETATM 7545 O  O     . HOH   BA 9 .   ? 27.43000 -90.21000  -31.88600 1.000 53.94759  ? 514 HOH   B O     1 
HETATM 7546 O  O     . HOH   BA 9 .   ? 48.35100 -98.77100  -41.18700 1.000 90.56320  ? 515 HOH   B O     1 
HETATM 7547 O  O     . HOH   BA 9 .   ? 19.46100 -99.14600  -30.26700 1.000 48.59171  ? 516 HOH   B O     1 
HETATM 7548 O  O     . HOH   BA 9 .   ? 14.57400 -133.04400 -42.55900 1.000 81.50135  ? 517 HOH   B O     1 
HETATM 7549 O  O     . HOH   BA 9 .   ? 20.31900 -84.29100  -57.16300 1.000 77.94488  ? 518 HOH   B O     1 
HETATM 7550 O  O     . HOH   BA 9 .   ? 18.92300 -129.82700 -41.39900 1.000 106.06713 ? 519 HOH   B O     1 
HETATM 7551 O  O     . HOH   BA 9 .   ? 23.849   -130.412   -47.923   1.000 96.43237  ? 520 HOH   B O     1 
HETATM 7552 O  O     . HOH   BA 9 .   ? 29.046   -119.313   -17.632   1.000 90.41048  ? 521 HOH   B O     1 
HETATM 7553 O  O     . HOH   BA 9 .   ? 5.50500  -123.55400 -45.65500 1.000 82.47676  ? 522 HOH   B O     1 
HETATM 7554 O  O     . HOH   BA 9 .   ? 16.92800 -89.71300  -37.85500 1.000 58.36795  ? 523 HOH   B O     1 
HETATM 7555 O  O     . HOH   BA 9 .   ? 26.51800 -108.74100 -37.59800 1.000 84.28653  ? 524 HOH   B O     1 
HETATM 7556 O  O     . HOH   BA 9 .   ? 22.29900 -109.37700 -39.70600 1.000 72.90065  ? 525 HOH   B O     1 
HETATM 7557 O  O     . HOH   BA 9 .   ? 3.065    -102.026   -46.177   1.000 118.66117 ? 526 HOH   B O     1 
HETATM 7558 O  O     . HOH   BA 9 .   ? 12.71900 -93.09200  -44.77400 1.000 69.63449  ? 527 HOH   B O     1 
HETATM 7559 O  O     . HOH   BA 9 .   ? 50.12200 -113.89200 -36.54300 1.000 108.33939 ? 528 HOH   B O     1 
HETATM 7560 O  O     . HOH   BA 9 .   ? 38.23200 -131.58700 -32.72300 1.000 101.00276 ? 529 HOH   B O     1 
HETATM 7561 O  O     . HOH   BA 9 .   ? 23.54600 -92.86600  -59.12400 1.000 76.21463  ? 530 HOH   B O     1 
HETATM 7562 O  O     . HOH   BA 9 .   ? 47.21000 -114.94500 -24.48600 1.000 62.47260  ? 531 HOH   B O     1 
HETATM 7563 O  O     . HOH   BA 9 .   ? 36.196   -110.872   -17.727   1.000 82.12522  ? 532 HOH   B O     1 
HETATM 7564 O  O     . HOH   BA 9 .   ? 12.24800 -100.21500 -43.82700 1.000 70.33540  ? 533 HOH   B O     1 
HETATM 7565 O  O     . HOH   BA 9 .   ? 22.03200 -104.00800 -57.08100 1.000 56.13416  ? 534 HOH   B O     1 
HETATM 7566 O  O     . HOH   BA 9 .   ? 38.66900 -110.28800 -16.96500 1.000 64.05865  ? 535 HOH   B O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ARG A 21  ? 1.33130 1.60327 1.35827 -0.00573 -0.23668 -0.04511 13  ARG A N   
2    C CA  . ARG A 21  ? 1.20562 1.49622 1.21982 0.00191  -0.21246 -0.02128 13  ARG A CA  
3    C C   . ARG A 21  ? 1.12880 1.38647 1.08871 0.02281  -0.19597 -0.02678 13  ARG A C   
4    O O   . ARG A 21  ? 1.17745 1.39975 1.11577 0.02825  -0.20275 -0.04634 13  ARG A O   
5    C CB  . ARG A 21  ? 1.23222 1.57673 1.26252 0.00908  -0.20919 -0.01277 13  ARG A CB  
6    C CG  . ARG A 21  ? 1.21997 1.57372 1.22505 0.03155  -0.21591 -0.02952 13  ARG A CG  
7    C CD  . ARG A 21  ? 1.23764 1.64805 1.27434 0.03527  -0.21844 -0.02063 13  ARG A CD  
8    N NE  . ARG A 21  ? 1.31473 1.73769 1.34543 0.04682  -0.23806 -0.03682 13  ARG A NE  
9    C CZ  . ARG A 21  ? 1.30614 1.77746 1.37297 0.04653  -0.25073 -0.03380 13  ARG A CZ  
10   N NH1 . ARG A 21  ? 1.25132 1.76559 1.36644 0.03507  -0.24355 -0.01578 13  ARG A NH1 
11   N NH2 . ARG A 21  ? 1.24171 1.72018 1.29648 0.05714  -0.27091 -0.04831 13  ARG A NH2 
12   N N   . VAL A 22  ? 1.17831 1.44775 1.11831 0.03334  -0.17451 -0.01124 14  VAL A N   
13   C CA  . VAL A 22  ? 1.13664 1.37295 1.03121 0.04742  -0.15760 -0.01153 14  VAL A CA  
14   C C   . VAL A 22  ? 1.11777 1.35015 0.97416 0.07308  -0.15305 -0.02528 14  VAL A C   
15   O O   . VAL A 22  ? 1.11074 1.37659 0.96929 0.08505  -0.14859 -0.02085 14  VAL A O   
16   C CB  . VAL A 22  ? 1.12669 1.37588 1.01613 0.04481  -0.13737 0.01030  14  VAL A CB  
17   C CG1 . VAL A 22  ? 1.08868 1.30044 0.93644 0.05413  -0.12421 0.00959  14  VAL A CG1 
18   C CG2 . VAL A 22  ? 1.12175 1.38459 1.05022 0.01814  -0.14170 0.02904  14  VAL A CG2 
19   N N   . SER A 23  ? 1.12318 1.31664 0.94824 0.08094  -0.15386 -0.04024 15  SER A N   
20   C CA  . SER A 23  ? 1.10305 1.28277 0.88366 0.10407  -0.14490 -0.04883 15  SER A CA  
21   C C   . SER A 23  ? 1.07748 1.24599 0.83390 0.11268  -0.12340 -0.03676 15  SER A C   
22   O O   . SER A 23  ? 1.03747 1.17932 0.78962 0.10370  -0.11869 -0.03403 15  SER A O   
23   C CB  . SER A 23  ? 1.08754 1.23268 0.84627 0.10622  -0.15184 -0.06867 15  SER A CB  
24   O OG  . SER A 23  ? 1.07132 1.20177 0.78661 0.12611  -0.14130 -0.07310 15  SER A OG  
25   N N   . SER A 24  ? 1.01807 1.20597 0.76135 0.12946  -0.11211 -0.03051 16  SER A N   
26   C CA  . SER A 24  ? 0.97899 1.16208 0.70249 0.13762  -0.09129 -0.02039 16  SER A CA  
27   C C   . SER A 24  ? 0.95265 1.12734 0.64344 0.16241  -0.08226 -0.02482 16  SER A C   
28   O O   . SER A 24  ? 1.02230 1.21273 0.71562 0.17348  -0.09162 -0.02911 16  SER A O   
29   C CB  . SER A 24  ? 1.00023 1.22172 0.75147 0.13013  -0.08368 -0.00589 16  SER A CB  
30   O OG  . SER A 24  ? 1.09717 1.35781 0.87061 0.13917  -0.08853 -0.00556 16  SER A OG  
31   N N   . GLY A 25  ? 1.00385 1.15432 0.66615 0.16990  -0.06611 -0.02286 17  GLY A N   
32   C CA  . GLY A 25  ? 1.05032 1.18619 0.68188 0.19238  -0.05600 -0.02562 17  GLY A CA  
33   C C   . GLY A 25  ? 1.00966 1.15097 0.63400 0.20003  -0.03697 -0.01933 17  GLY A C   
34   O O   . GLY A 25  ? 0.96628 1.11806 0.60165 0.18572  -0.03081 -0.01284 17  GLY A O   
35   N N   . ARG A 26  ? 0.99487 1.12914 0.60102 0.22171  -0.02840 -0.02118 18  ARG A N   
36   C CA  . ARG A 26  ? 0.98674 1.12008 0.58181 0.23291  -0.00911 -0.01987 18  ARG A CA  
37   C C   . ARG A 26  ? 0.99889 1.08455 0.55618 0.23872  -0.00187 -0.02520 18  ARG A C   
38   O O   . ARG A 26  ? 0.97828 1.04170 0.51993 0.24785  -0.00848 -0.02812 18  ARG A O   
39   C CB  . ARG A 26  ? 0.95702 1.11837 0.56770 0.25477  -0.00569 -0.01870 18  ARG A CB  
40   C CG  . ARG A 26  ? 1.06403 1.22541 0.66673 0.26880  0.01516  -0.02094 18  ARG A CG  
41   C CD  . ARG A 26  ? 1.08557 1.28575 0.71066 0.25891  0.02759  -0.01758 18  ARG A CD  
42   N NE  . ARG A 26  ? 1.15649 1.35613 0.77045 0.27269  0.04922  -0.02346 18  ARG A NE  
43   C CZ  . ARG A 26  ? 1.11129 1.28450 0.69430 0.26625  0.06198  -0.02829 18  ARG A CZ  
44   N NH1 . ARG A 26  ? 1.07427 1.22008 0.63678 0.24639  0.05478  -0.02585 18  ARG A NH1 
45   N NH2 . ARG A 26  ? 1.13549 1.31040 0.70961 0.28012  0.08142  -0.03664 18  ARG A NH2 
46   N N   . ASP A 27  ? 1.05095 1.12277 0.59361 0.23228  0.01076  -0.02586 19  ASP A N   
47   C CA  . ASP A 27  ? 1.02042 1.04939 0.53006 0.23747  0.01894  -0.03142 19  ASP A CA  
48   C C   . ASP A 27  ? 1.00372 1.03333 0.50474 0.25660  0.03445  -0.03534 19  ASP A C   
49   O O   . ASP A 27  ? 1.10338 1.15644 0.61122 0.25392  0.04546  -0.03542 19  ASP A O   
50   C CB  . ASP A 27  ? 1.01098 1.02244 0.50988 0.21729  0.01978  -0.03080 19  ASP A CB  
51   C CG  . ASP A 27  ? 0.99616 0.96670 0.46472 0.22071  0.02715  -0.03690 19  ASP A CG  
52   O OD1 . ASP A 27  ? 1.02722 0.97471 0.48341 0.23433  0.02774  -0.04066 19  ASP A OD1 
53   O OD2 . ASP A 27  ? 1.01099 0.97324 0.46834 0.20877  0.03137  -0.03689 19  ASP A OD2 
54   N N   . LEU A 28  ? 0.99050 0.99508 0.47753 0.27492  0.03557  -0.03838 20  LEU A N   
55   C CA  . LEU A 28  ? 1.03863 1.03241 0.51695 0.29519  0.04938  -0.04400 20  LEU A CA  
56   C C   . LEU A 28  ? 1.05918 1.00172 0.50681 0.29692  0.05236  -0.04856 20  LEU A C   
57   O O   . LEU A 28  ? 1.09462 1.01611 0.53262 0.29018  0.04266  -0.04512 20  LEU A O   
58   C CB  . LEU A 28  ? 1.03286 1.04620 0.53110 0.31739  0.04514  -0.04027 20  LEU A CB  
59   C CG  . LEU A 28  ? 1.08992 1.15736 0.62446 0.31658  0.04146  -0.03576 20  LEU A CG  
60   C CD1 . LEU A 28  ? 1.06841 1.15235 0.62268 0.33689  0.03093  -0.03035 20  LEU A CD1 
61   C CD2 . LEU A 28  ? 1.10054 1.19479 0.64679 0.31756  0.05960  -0.04093 20  LEU A CD2 
62   N N   . ASN A 29  ? 1.03827 0.96253 0.47201 0.30454  0.06596  -0.05718 21  ASN A N   
63   C CA  . ASN A 29  ? 1.07160 0.94625 0.47948 0.30750  0.06952  -0.06247 21  ASN A CA  
64   C C   . ASN A 29  ? 1.10333 0.96394 0.51348 0.33377  0.07586  -0.06533 21  ASN A C   
65   O O   . ASN A 29  ? 1.14007 0.95869 0.53200 0.33846  0.08012  -0.07023 21  ASN A O   
66   C CB  . ASN A 29  ? 1.04959 0.90927 0.43850 0.29224  0.07702  -0.07141 21  ASN A CB  
67   C CG  . ASN A 29  ? 1.12796 0.94738 0.49793 0.27923  0.07155  -0.07166 21  ASN A CG  
68   O OD1 . ASN A 29  ? 1.09502 0.90754 0.46832 0.27374  0.06190  -0.06412 21  ASN A OD1 
69   N ND2 . ASN A 29  ? 1.18966 0.98430 0.54040 0.27340  0.07786  -0.08139 21  ASN A ND2 
70   N N   . CYS A 30  ? 1.07087 0.96527 0.50619 0.35000  0.07513  -0.06167 22  CYS A N   
71   C CA  . CYS A 30  ? 1.07432 0.96244 0.52144 0.37788  0.07934  -0.06287 22  CYS A CA  
72   C C   . CYS A 30  ? 1.15332 1.06964 0.62411 0.38928  0.06528  -0.04957 22  CYS A C   
73   O O   . CYS A 30  ? 1.17429 1.13767 0.66939 0.38516  0.06266  -0.04745 22  CYS A O   
74   C CB  . CYS A 30  ? 1.09612 1.00482 0.55585 0.38866  0.09658  -0.07653 22  CYS A CB  
75   S SG  . CYS A 30  ? 1.14065 1.05493 0.63002 0.42530  0.10085  -0.07823 22  CYS A SG  
76   N N   . VAL A 31  ? 1.16759 1.05628 0.63083 0.40167  0.05576  -0.03999 23  VAL A N   
77   C CA  . VAL A 31  ? 1.20363 1.11359 0.68226 0.41233  0.03881  -0.02562 23  VAL A CA  
78   C C   . VAL A 31  ? 1.25335 1.13601 0.73421 0.43824  0.03649  -0.01868 23  VAL A C   
79   O O   . VAL A 31  ? 1.30472 1.14681 0.76060 0.43769  0.03127  -0.01003 23  VAL A O   
80   C CB  . VAL A 31  ? 1.18224 1.08584 0.64049 0.39342  0.02503  -0.01717 23  VAL A CB  
81   C CG1 . VAL A 31  ? 1.22238 1.14721 0.69006 0.40266  0.00631  -0.00383 23  VAL A CG1 
82   C CG2 . VAL A 31  ? 1.10318 1.02825 0.56274 0.36846  0.02630  -0.02393 23  VAL A CG2 
83   N N   . PRO A 32  ? 1.22517 1.12884 0.73813 0.46173  0.04071  -0.02152 24  PRO A N   
84   C CA  . PRO A 32  ? 1.25823 1.13469 0.77910 0.48836  0.03702  -0.01411 24  PRO A CA  
85   C C   . PRO A 32  ? 1.33824 1.21800 0.85698 0.49386  0.01380  0.00791  24  PRO A C   
86   O O   . PRO A 32  ? 1.38967 1.22627 0.88174 0.49445  0.00783  0.01932  24  PRO A O   
87   C CB  . PRO A 32  ? 1.26670 1.17602 0.82986 0.51096  0.04745  -0.02460 24  PRO A CB  
88   C CG  . PRO A 32  ? 1.25456 1.20290 0.82366 0.49282  0.06126  -0.03920 24  PRO A CG  
89   C CD  . PRO A 32  ? 1.22258 1.17761 0.76884 0.46425  0.04983  -0.03137 24  PRO A CD  
90   N N   . GLU A 33  ? 1.32177 1.25307 0.86706 0.49586  0.00114  0.01354  25  GLU A N   
91   C CA  . GLU A 33  ? 1.31480 1.25856 0.85783 0.49909  -0.02375 0.03298  25  GLU A CA  
92   C C   . GLU A 33  ? 1.28925 1.26194 0.82091 0.47261  -0.03214 0.03118  25  GLU A C   
93   O O   . GLU A 33  ? 1.27427 1.29648 0.83769 0.46884  -0.03429 0.02565  25  GLU A O   
94   C CB  . GLU A 33  ? 1.31812 1.29770 0.90730 0.52584  -0.03475 0.04044  25  GLU A CB  
95   C CG  . GLU A 33  ? 1.36082 1.32948 0.94230 0.53900  -0.05971 0.06383  25  GLU A CG  
96   C CD  . GLU A 33  ? 1.51032 1.42443 1.08013 0.55830  -0.05821 0.07437  25  GLU A CD  
97   O OE1 . GLU A 33  ? 1.53343 1.40792 1.08839 0.55535  -0.03814 0.06260  25  GLU A OE1 
98   O OE2 . GLU A 33  ? 1.64543 1.55599 1.22169 0.57574  -0.07856 0.09509  25  GLU A OE2 
99   N N   . ILE A 34  ? 1.27989 1.22205 0.77005 0.45470  -0.03554 0.03495  26  ILE A N   
100  C CA  . ILE A 34  ? 1.25643 1.21676 0.73155 0.42973  -0.04384 0.03190  26  ILE A CA  
101  C C   . ILE A 34  ? 1.22586 1.23595 0.72660 0.43290  -0.06467 0.03764  26  ILE A C   
102  O O   . ILE A 34  ? 1.18533 1.22635 0.69727 0.41508  -0.06776 0.02909  26  ILE A O   
103  C CB  . ILE A 34  ? 1.25784 1.17756 0.68639 0.41765  -0.04641 0.03838  26  ILE A CB  
104  C CG1 . ILE A 34  ? 1.22238 1.15811 0.63732 0.39321  -0.05251 0.03128  26  ILE A CG1 
105  C CG2 . ILE A 34  ? 1.27665 1.17983 0.68931 0.43381  -0.06115 0.05818  26  ILE A CG2 
106  C CD1 . ILE A 34  ? 1.28877 1.18571 0.66351 0.37795  -0.04558 0.03067  26  ILE A CD1 
107  N N   . ALA A 35  ? 1.23821 1.25486 0.74973 0.45427  -0.07994 0.05221  27  ALA A N   
108  C CA  . ALA A 35  ? 1.20252 1.26788 0.74313 0.46061  -0.10281 0.05932  27  ALA A CA  
109  C C   . ALA A 35  ? 1.22228 1.33637 0.81524 0.46203  -0.09520 0.04830  27  ALA A C   
110  O O   . ALA A 35  ? 1.18442 1.33465 0.79101 0.44459  -0.10324 0.04246  27  ALA A O   
111  C CB  . ALA A 35  ? 1.22077 1.27823 0.76536 0.48604  -0.11901 0.07858  27  ALA A CB  
112  N N   . ASP A 36  ? 1.22505 1.33931 0.84616 0.48130  -0.07923 0.04487  28  ASP A N   
113  C CA  . ASP A 36  ? 1.18611 1.34851 0.85839 0.48565  -0.06770 0.03486  28  ASP A CA  
114  C C   . ASP A 36  ? 1.17281 1.34323 0.83745 0.45833  -0.05192 0.02076  28  ASP A C   
115  O O   . ASP A 36  ? 1.16396 1.38264 0.86082 0.44726  -0.05550 0.01784  28  ASP A O   
116  C CB  . ASP A 36  ? 1.19556 1.34765 0.89091 0.51170  -0.04954 0.03043  28  ASP A CB  
117  C CG  . ASP A 36  ? 1.29812 1.44825 1.01499 0.54188  -0.06556 0.04510  28  ASP A CG  
118  O OD1 . ASP A 36  ? 1.36721 1.55423 1.10721 0.54590  -0.08952 0.05668  28  ASP A OD1 
119  O OD2 . ASP A 36  ? 1.36064 1.47160 1.07230 0.56089  -0.05535 0.04500  28  ASP A OD2 
120  N N   . THR A 37  ? 1.19436 1.31941 0.82045 0.44764  -0.03622 0.01368  29  THR A N   
121  C CA  . THR A 37  ? 1.17235 1.29681 0.78714 0.42246  -0.02153 0.00198  29  THR A CA  
122  C C   . THR A 37  ? 1.17995 1.32938 0.79674 0.39919  -0.03752 0.00336  29  THR A C   
123  O O   . THR A 37  ? 1.11913 1.30537 0.76290 0.38601  -0.03313 -0.00126 29  THR A O   
124  C CB  . THR A 37  ? 1.13884 1.20648 0.70969 0.41551  -0.00899 -0.00295 29  THR A CB  
125  O OG1 . THR A 37  ? 1.15191 1.19917 0.72627 0.43604  0.00625  -0.00725 29  THR A OG1 
126  C CG2 . THR A 37  ? 1.11708 1.18196 0.67527 0.38952  0.00164  -0.01245 29  THR A CG2 
127  N N   . LEU A 38  ? 1.16166 1.29135 0.75063 0.39390  -0.05478 0.00915  30  LEU A N   
128  C CA  . LEU A 38  ? 1.14217 1.28786 0.72759 0.37186  -0.07061 0.00707  30  LEU A CA  
129  C C   . LEU A 38  ? 1.11830 1.31968 0.74786 0.37368  -0.08687 0.01029  30  LEU A C   
130  O O   . LEU A 38  ? 1.11151 1.33779 0.75771 0.35324  -0.09207 0.00488  30  LEU A O   
131  C CB  . LEU A 38  ? 1.11944 1.23183 0.66229 0.36985  -0.08330 0.01149  30  LEU A CB  
132  C CG  . LEU A 38  ? 1.12316 1.24574 0.65657 0.34849  -0.09858 0.00561  30  LEU A CG  
133  C CD1 . LEU A 38  ? 1.06841 1.18477 0.60381 0.32579  -0.08667 -0.00613 30  LEU A CD1 
134  C CD2 . LEU A 38  ? 1.10449 1.19609 0.59228 0.34853  -0.10791 0.00951  30  LEU A CD2 
135  N N   . GLY A 39  ? 1.09441 1.31420 0.74536 0.39704  -0.09574 0.01936  31  GLY A N   
136  C CA  . GLY A 39  ? 1.09364 1.37028 0.79401 0.40188  -0.11146 0.02344  31  GLY A CA  
137  C C   . GLY A 39  ? 1.09465 1.41061 0.83919 0.39540  -0.09453 0.01714  31  GLY A C   
138  O O   . GLY A 39  ? 1.10419 1.46757 0.88744 0.38562  -0.10652 0.01778  31  GLY A O   
139  N N   . ALA A 40  ? 1.09061 1.38812 0.82855 0.39937  -0.06771 0.01128  32  ALA A N   
140  C CA  . ALA A 40  ? 1.06391 1.39561 0.83556 0.39368  -0.04672 0.00540  32  ALA A CA  
141  C C   . ALA A 40  ? 1.11625 1.45005 0.87957 0.36159  -0.04410 0.00121  32  ALA A C   
142  O O   . ALA A 40  ? 1.16919 1.54903 0.97158 0.34968  -0.04224 0.00211  32  ALA A O   
143  C CB  . ALA A 40  ? 1.07693 1.38390 0.83685 0.40966  -0.02075 -0.00090 32  ALA A CB  
144  N N   . VAL A 41  ? 1.10306 1.38988 0.82104 0.34799  -0.04418 -0.00225 33  VAL A N   
145  C CA  . VAL A 41  ? 1.11346 1.39521 0.82340 0.31886  -0.04156 -0.00593 33  VAL A CA  
146  C C   . VAL A 41  ? 1.13951 1.44817 0.87131 0.30269  -0.06503 -0.00421 33  VAL A C   
147  O O   . VAL A 41  ? 1.16557 1.49491 0.91856 0.28111  -0.06408 -0.00427 33  VAL A O   
148  C CB  . VAL A 41  ? 1.11267 1.33817 0.77381 0.31077  -0.03568 -0.01070 33  VAL A CB  
149  C CG1 . VAL A 41  ? 1.14937 1.34467 0.78796 0.32708  -0.01590 -0.01351 33  VAL A CG1 
150  C CG2 . VAL A 41  ? 1.10104 1.29981 0.73537 0.30925  -0.05425 -0.01103 33  VAL A CG2 
151  N N   . ALA A 42  ? 1.12297 1.43015 0.84852 0.31185  -0.08616 -0.00246 34  ALA A N   
152  C CA  . ALA A 42  ? 1.11397 1.44800 0.85931 0.29886  -0.11150 -0.00305 34  ALA A CA  
153  C C   . ALA A 42  ? 1.14460 1.53880 0.94876 0.29926  -0.11477 0.00199  34  ALA A C   
154  O O   . ALA A 42  ? 1.15325 1.57327 0.98484 0.27787  -0.12545 0.00050  34  ALA A O   
155  C CB  . ALA A 42  ? 1.11247 1.43089 0.83103 0.31083  -0.13186 -0.00168 34  ALA A CB  
156  N N   . LYS A 43  ? 1.11508 1.53024 0.94066 0.32277  -0.10523 0.00733  35  LYS A N   
157  C CA  . LYS A 43  ? 1.13155 1.60758 1.01793 0.32703  -0.10221 0.01192  35  LYS A CA  
158  C C   . LYS A 43  ? 1.15539 1.64741 1.05842 0.30728  -0.07966 0.01065  35  LYS A C   
159  O O   . LYS A 43  ? 1.14503 1.68622 1.09596 0.29401  -0.08332 0.01437  35  LYS A O   
160  C CB  . LYS A 43  ? 1.15020 1.63588 1.05118 0.35974  -0.09361 0.01564  35  LYS A CB  
161  C CG  . LYS A 43  ? 1.14636 1.69419 1.11136 0.36814  -0.08351 0.01844  35  LYS A CG  
162  C CD  . LYS A 43  ? 1.20915 1.80893 1.22387 0.36622  -0.11072 0.02450  35  LYS A CD  
163  C CE  . LYS A 43  ? 1.21474 1.87608 1.29648 0.38178  -0.10034 0.02782  35  LYS A CE  
164  N NZ  . LYS A 43  ? 1.19057 1.90052 1.32147 0.38402  -0.13089 0.03462  35  LYS A NZ  
165  N N   . GLN A 44  ? 1.11555 1.56846 0.98062 0.30451  -0.05816 0.00674  36  GLN A N   
166  C CA  . GLN A 44  ? 1.13586 1.59552 1.00419 0.28375  -0.03779 0.00710  36  GLN A CA  
167  C C   . GLN A 44  ? 1.12738 1.58877 1.00318 0.25311  -0.05401 0.00913  36  GLN A C   
168  O O   . GLN A 44  ? 1.20011 1.69145 1.10396 0.23392  -0.04560 0.01472  36  GLN A O   
169  C CB  . GLN A 44  ? 1.18516 1.59641 1.00497 0.28753  -0.01731 0.00189  36  GLN A CB  
170  C CG  . GLN A 44  ? 1.25727 1.67491 1.07917 0.31213  0.00571  -0.00185 36  GLN A CG  
171  C CD  . GLN A 44  ? 1.24469 1.60792 1.01595 0.31863  0.02020  -0.00894 36  GLN A CD  
172  O OE1 . GLN A 44  ? 1.21312 1.53975 0.95029 0.30130  0.01789  -0.00993 36  GLN A OE1 
173  N NE2 . GLN A 44  ? 1.24175 1.59938 1.01121 0.34404  0.03482  -0.01460 36  GLN A NE2 
174  N N   . GLY A 45  ? 1.14665 1.57703 0.99868 0.24858  -0.07571 0.00462  37  GLY A N   
175  C CA  . GLY A 45  ? 1.09892 1.52951 0.96170 0.22262  -0.09510 0.00298  37  GLY A CA  
176  C C   . GLY A 45  ? 1.07141 1.44714 0.89009 0.21176  -0.09793 -0.00414 37  GLY A C   
177  O O   . GLY A 45  ? 1.04818 1.41980 0.87683 0.19034  -0.11226 -0.00737 37  GLY A O   
178  N N   . PHE A 46  ? 1.11392 1.44914 0.88924 0.22569  -0.08522 -0.00720 38  PHE A N   
179  C CA  . PHE A 46  ? 1.05935 1.34338 0.79462 0.21710  -0.08483 -0.01388 38  PHE A CA  
180  C C   . PHE A 46  ? 1.11519 1.38197 0.83244 0.21894  -0.10545 -0.02239 38  PHE A C   
181  O O   . PHE A 46  ? 1.18933 1.47326 0.90957 0.23397  -0.11665 -0.02140 38  PHE A O   
182  C CB  . PHE A 46  ? 1.01121 1.26212 0.71059 0.23101  -0.06440 -0.01397 38  PHE A CB  
183  C CG  . PHE A 46  ? 1.06441 1.32604 0.77161 0.22544  -0.04386 -0.00865 38  PHE A CG  
184  C CD1 . PHE A 46  ? 1.00065 1.24714 0.70259 0.20393  -0.03989 -0.00675 38  PHE A CD1 
185  C CD2 . PHE A 46  ? 1.07546 1.36333 0.79550 0.24170  -0.02881 -0.00567 38  PHE A CD2 
186  C CE1 . PHE A 46  ? 0.98236 1.23962 0.68586 0.19733  -0.02192 -0.00067 38  PHE A CE1 
187  C CE2 . PHE A 46  ? 1.05612 1.35546 0.77862 0.23565  -0.00839 -0.00257 38  PHE A CE2 
188  C CZ  . PHE A 46  ? 1.05200 1.33618 0.76350 0.21268  -0.00533 0.00060  38  PHE A CZ  
189  N N   . ASP A 47  ? 1.13843 1.37322 0.83774 0.20420  -0.11025 -0.03061 39  ASP A N   
190  C CA  . ASP A 47  ? 1.13294 1.34920 0.81112 0.20267  -0.12709 -0.04218 39  ASP A CA  
191  C C   . ASP A 47  ? 1.07595 1.25291 0.70603 0.21742  -0.11769 -0.04467 39  ASP A C   
192  O O   . ASP A 47  ? 1.18544 1.35351 0.79186 0.22277  -0.12928 -0.05084 39  ASP A O   
193  C CB  . ASP A 47  ? 1.08229 1.28582 0.77178 0.17956  -0.13576 -0.05195 39  ASP A CB  
194  C CG  . ASP A 47  ? 1.13306 1.37268 0.87012 0.16297  -0.15020 -0.05050 39  ASP A CG  
195  O OD1 . ASP A 47  ? 1.12731 1.40602 0.89059 0.16876  -0.15197 -0.04127 39  ASP A OD1 
196  O OD2 . ASP A 47  ? 1.22081 1.44925 0.97159 0.14436  -0.15959 -0.05878 39  ASP A OD2 
197  N N   . PHE A 48  ? 1.04939 1.20390 0.66442 0.22226  -0.09794 -0.04001 40  PHE A N   
198  C CA  . PHE A 48  ? 1.05122 1.16648 0.62427 0.23407  -0.08724 -0.04118 40  PHE A CA  
199  C C   . PHE A 48  ? 1.04733 1.15301 0.61522 0.24379  -0.06755 -0.03394 40  PHE A C   
200  O O   . PHE A 48  ? 1.01951 1.14958 0.61339 0.24022  -0.06115 -0.02916 40  PHE A O   
201  C CB  . PHE A 48  ? 1.06179 1.14501 0.61704 0.22024  -0.08720 -0.05184 40  PHE A CB  
202  C CG  . PHE A 48  ? 1.02342 1.09731 0.59455 0.20394  -0.07975 -0.05250 40  PHE A CG  
203  C CD1 . PHE A 48  ? 1.01877 1.11175 0.62372 0.18664  -0.08993 -0.05412 40  PHE A CD1 
204  C CD2 . PHE A 48  ? 1.01129 1.05608 0.56400 0.20497  -0.06444 -0.05056 40  PHE A CD2 
205  C CE1 . PHE A 48  ? 1.05209 1.13489 0.67111 0.17142  -0.08512 -0.05158 40  PHE A CE1 
206  C CE2 . PHE A 48  ? 0.96906 1.00576 0.53524 0.18969  -0.06051 -0.04943 40  PHE A CE2 
207  C CZ  . PHE A 48  ? 0.98112 1.03650 0.57983 0.17326  -0.07100 -0.04891 40  PHE A CZ  
208  N N   . LEU A 49  ? 1.02396 1.09515 0.55838 0.25485  -0.05792 -0.03371 41  LEU A N   
209  C CA  . LEU A 49  ? 1.00345 1.05873 0.52728 0.26653  -0.04033 -0.02953 41  LEU A CA  
210  C C   . LEU A 49  ? 1.03480 1.04664 0.52960 0.26039  -0.03059 -0.03368 41  LEU A C   
211  O O   . LEU A 49  ? 1.04785 1.03751 0.51956 0.26186  -0.03430 -0.03576 41  LEU A O   
212  C CB  . LEU A 49  ? 1.00505 1.06290 0.52252 0.29028  -0.04131 -0.02317 41  LEU A CB  
213  C CG  . LEU A 49  ? 1.02388 1.05502 0.52545 0.30480  -0.02468 -0.02129 41  LEU A CG  
214  C CD1 . LEU A 49  ? 1.03893 1.09093 0.56249 0.30570  -0.01152 -0.02280 41  LEU A CD1 
215  C CD2 . LEU A 49  ? 1.01849 1.04231 0.51110 0.32765  -0.02919 -0.01373 41  LEU A CD2 
216  N N   . CYS A 50  ? 0.98990 0.99217 0.48565 0.25321  -0.01865 -0.03448 42  CYS A N   
217  C CA  . CYS A 50  ? 0.99467 0.95753 0.46643 0.24895  -0.00871 -0.03762 42  CYS A CA  
218  C C   . CYS A 50  ? 1.03807 0.98415 0.49433 0.26594  0.00378  -0.03579 42  CYS A C   
219  O O   . CYS A 50  ? 1.08541 1.04630 0.55145 0.26928  0.01203  -0.03575 42  CYS A O   
220  C CB  . CYS A 50  ? 0.97754 0.93963 0.45919 0.22994  -0.00657 -0.03923 42  CYS A CB  
221  S SG  . CYS A 50  ? 0.99722 0.98130 0.50721 0.21070  -0.02210 -0.04062 42  CYS A SG  
222  N N   . MET A 51  ? 1.08844 1.00500 0.52183 0.27604  0.00558  -0.03450 43  MET A N   
223  C CA  . MET A 51  ? 1.07094 0.96559 0.49103 0.29355  0.01549  -0.03246 43  MET A CA  
224  C C   . MET A 51  ? 1.05937 0.91004 0.45395 0.28948  0.02163  -0.03355 43  MET A C   
225  O O   . MET A 51  ? 1.03097 0.87195 0.41841 0.27635  0.01820  -0.03499 43  MET A O   
226  C CB  . MET A 51  ? 1.06416 0.96983 0.48743 0.31370  0.00868  -0.02479 43  MET A CB  
227  C CG  . MET A 51  ? 1.02451 0.92196 0.43130 0.31282  -0.00247 -0.01932 43  MET A CG  
228  S SD  . MET A 51  ? 1.18637 1.09573 0.59444 0.33672  -0.01398 -0.00681 43  MET A SD  
229  C CE  . MET A 51  ? 1.21945 1.08396 0.61079 0.35327  -0.00141 -0.00149 43  MET A CE  
230  N N   . PRO A 52  ? 1.09355 0.91683 0.47663 0.30021  0.03147  -0.03400 44  PRO A N   
231  C CA  . PRO A 52  ? 1.13554 0.91666 0.49674 0.29830  0.03643  -0.03251 44  PRO A CA  
232  C C   . PRO A 52  ? 1.08723 0.85822 0.43548 0.30917  0.03091  -0.02140 44  PRO A C   
233  O O   . PRO A 52  ? 1.06830 0.85544 0.42379 0.32534  0.02518  -0.01517 44  PRO A O   
234  C CB  . PRO A 52  ? 1.15845 0.91611 0.51530 0.30739  0.04707  -0.03757 44  PRO A CB  
235  C CG  . PRO A 52  ? 1.11173 0.90256 0.48625 0.31126  0.04978  -0.04385 44  PRO A CG  
236  C CD  . PRO A 52  ? 1.10123 0.93226 0.49359 0.31378  0.03942  -0.03756 44  PRO A CD  
237  N N   . VAL A 53  ? 1.04738 0.79380 0.37752 0.29971  0.03271  -0.01840 45  VAL A N   
238  C CA  . VAL A 53  ? 1.13503 0.86870 0.44531 0.30668  0.02892  -0.00590 45  VAL A CA  
239  C C   . VAL A 53  ? 1.17669 0.86833 0.47329 0.31482  0.03693  0.00172  45  VAL A C   
240  O O   . VAL A 53  ? 1.17779 0.85601 0.45847 0.32405  0.03344  0.01602  45  VAL A O   
241  C CB  . VAL A 53  ? 1.12986 0.86681 0.42820 0.29059  0.02774  -0.00765 45  VAL A CB  
242  C CG1 . VAL A 53  ? 1.07163 0.84762 0.38383 0.28534  0.01697  -0.01449 45  VAL A CG1 
243  C CG2 . VAL A 53  ? 1.12247 0.83875 0.42116 0.27359  0.03813  -0.01552 45  VAL A CG2 
244  N N   . PHE A 54  ? 1.15473 0.82559 0.45654 0.31025  0.04608  -0.00706 46  PHE A N   
245  C CA  . PHE A 54  ? 1.15709 0.78931 0.45385 0.32005  0.05294  -0.00459 46  PHE A CA  
246  C C   . PHE A 54  ? 1.21428 0.85405 0.52663 0.32717  0.05683  -0.01805 46  PHE A C   
247  O O   . PHE A 54  ? 1.24809 0.91110 0.56909 0.31515  0.05738  -0.02886 46  PHE A O   
248  C CB  . PHE A 54  ? 1.14254 0.73951 0.42794 0.30399  0.06100  -0.00519 46  PHE A CB  
249  C CG  . PHE A 54  ? 1.18492 0.77069 0.45269 0.29727  0.06152  0.00859  46  PHE A CG  
250  C CD1 . PHE A 54  ? 1.13824 0.74992 0.40288 0.28530  0.05919  0.00713  46  PHE A CD1 
251  C CD2 . PHE A 54  ? 1.22969 0.77825 0.48367 0.30216  0.06516  0.02265  46  PHE A CD2 
252  C CE1 . PHE A 54  ? 1.19061 0.79422 0.43574 0.27869  0.06214  0.01793  46  PHE A CE1 
253  C CE2 . PHE A 54  ? 1.28504 0.82540 0.51946 0.29435  0.06742  0.03685  46  PHE A CE2 
254  C CZ  . PHE A 54  ? 1.25709 0.82635 0.48563 0.28267  0.06679  0.03365  46  PHE A CZ  
255  N N   . HIS A 55  ? 1.27647 0.89741 0.59241 0.34592  0.05974  -0.01750 47  HIS A N   
256  C CA  . HIS A 55  ? 1.31880 0.94616 0.64749 0.35469  0.06638  -0.03282 47  HIS A CA  
257  C C   . HIS A 55  ? 1.27073 0.88731 0.59234 0.33477  0.07276  -0.04719 47  HIS A C   
258  O O   . HIS A 55  ? 1.27223 0.85253 0.58227 0.32466  0.07535  -0.04730 47  HIS A O   
259  C CB  . HIS A 55  ? 1.35939 0.95699 0.69255 0.37729  0.06987  -0.03203 47  HIS A CB  
260  C CG  . HIS A 55  ? 1.37351 0.98824 0.72306 0.39135  0.07716  -0.04786 47  HIS A CG  
261  N ND1 . HIS A 55  ? 1.28650 0.90187 0.63141 0.38042  0.08643  -0.06692 47  HIS A ND1 
262  C CD2 . HIS A 55  ? 1.44279 1.07678 0.81357 0.41521  0.07721  -0.04782 47  HIS A CD2 
263  C CE1 . HIS A 55  ? 1.36407 0.99851 0.72362 0.39645  0.09395  -0.07887 47  HIS A CE1 
264  N NE2 . HIS A 55  ? 1.34985 0.99664 0.72854 0.41858  0.08898  -0.06791 47  HIS A NE2 
265  N N   . PRO A 56  ? 1.22433 0.87322 0.55324 0.32713  0.07428  -0.05790 48  PRO A N   
266  C CA  . PRO A 56  ? 1.21553 0.85829 0.53671 0.30653  0.07672  -0.06865 48  PRO A CA  
267  C C   . PRO A 56  ? 1.22302 0.82235 0.53164 0.30447  0.08289  -0.07921 48  PRO A C   
268  O O   . PRO A 56  ? 1.17815 0.76318 0.47980 0.28558  0.08106  -0.08240 48  PRO A O   
269  C CB  . PRO A 56  ? 1.17325 0.85517 0.50301 0.30609  0.07924  -0.07697 48  PRO A CB  
270  C CG  . PRO A 56  ? 1.10785 0.82591 0.45468 0.31754  0.07415  -0.06690 48  PRO A CG  
271  C CD  . PRO A 56  ? 1.16723 0.86183 0.51330 0.33636  0.07261  -0.05808 48  PRO A CD  
272  N N   . ARG A 57  ? 1.19750 0.77721 0.50651 0.32376  0.08907  -0.08511 49  ARG A N   
273  C CA  . ARG A 57  ? 1.31561 0.85327 0.61407 0.32349  0.09504  -0.09943 49  ARG A CA  
274  C C   . ARG A 57  ? 1.30141 0.79286 0.59688 0.32548  0.09323  -0.08902 49  ARG A C   
275  O O   . ARG A 57  ? 1.37561 0.82791 0.66373 0.32026  0.09603  -0.09934 49  ARG A O   
276  C CB  . ARG A 57  ? 1.28473 0.82669 0.58777 0.34373  0.10420  -0.11492 49  ARG A CB  
277  C CG  . ARG A 57  ? 1.24426 0.82944 0.54637 0.33819  0.10896  -0.12626 49  ARG A CG  
278  C CD  . ARG A 57  ? 1.33190 0.92101 0.63669 0.35678  0.12166  -0.14520 49  ARG A CD  
279  N NE  . ARG A 57  ? 1.32886 0.92650 0.65700 0.38410  0.12381  -0.13867 49  ARG A NE  
280  C CZ  . ARG A 57  ? 1.35055 0.91223 0.68646 0.40488  0.12700  -0.14301 49  ARG A CZ  
281  N NH1 . ARG A 57  ? 1.35271 0.86477 0.67421 0.40093  0.12937  -0.15547 49  ARG A NH1 
282  N NH2 . ARG A 57  ? 1.37478 0.94990 0.73559 0.42965  0.12639  -0.13444 49  ARG A NH2 
283  N N   . PHE A 58  ? 1.28599 0.78171 0.58557 0.33113  0.08831  -0.06910 50  PHE A N   
284  C CA  . PHE A 58  ? 1.36441 0.81953 0.65917 0.33232  0.08697  -0.05410 50  PHE A CA  
285  C C   . PHE A 58  ? 1.29621 0.73572 0.58322 0.30644  0.08681  -0.05220 50  PHE A C   
286  O O   . PHE A 58  ? 1.33398 0.78541 0.61842 0.29748  0.08427  -0.03781 50  PHE A O   
287  C CB  . PHE A 58  ? 1.37668 0.84787 0.67365 0.34488  0.08099  -0.03286 50  PHE A CB  
288  C CG  . PHE A 58  ? 1.40227 0.83271 0.69345 0.35198  0.07953  -0.01465 50  PHE A CG  
289  C CD1 . PHE A 58  ? 1.43900 0.82890 0.73586 0.36678  0.08208  -0.01783 50  PHE A CD1 
290  C CD2 . PHE A 58  ? 1.37246 0.80496 0.65215 0.34414  0.07573  0.00594  50  PHE A CD2 
291  C CE1 . PHE A 58  ? 1.48270 0.83306 0.77572 0.37283  0.07949  0.00207  50  PHE A CE1 
292  C CE2 . PHE A 58  ? 1.45329 0.84897 0.72489 0.34937  0.07448  0.02591  50  PHE A CE2 
293  C CZ  . PHE A 58  ? 1.48717 0.84105 0.76642 0.36350  0.07562  0.02549  50  PHE A CZ  
294  N N   . LYS A 59  ? 1.29148 0.70659 0.57581 0.29477  0.08941  -0.06756 51  LYS A N   
295  C CA  . LYS A 59  ? 1.30822 0.70716 0.59101 0.27009  0.08855  -0.06707 51  LYS A CA  
296  C C   . LYS A 59  ? 1.38415 0.74645 0.66575 0.26938  0.09080  -0.04974 51  LYS A C   
297  O O   . LYS A 59  ? 1.37463 0.70687 0.65551 0.28590  0.09223  -0.04582 51  LYS A O   
298  C CB  . LYS A 59  ? 1.39058 0.77261 0.67045 0.25891  0.08824  -0.08823 51  LYS A CB  
299  C CG  . LYS A 59  ? 1.37229 0.74492 0.65594 0.23281  0.08479  -0.08917 51  LYS A CG  
300  C CD  . LYS A 59  ? 1.45524 0.82539 0.73401 0.21998  0.08031  -0.10980 51  LYS A CD  
301  C CE  . LYS A 59  ? 1.53298 0.90139 0.82118 0.19431  0.07403  -0.10907 51  LYS A CE  
302  N NZ  . LYS A 59  ? 1.53608 0.89680 0.81678 0.18150  0.06691  -0.12840 51  LYS A NZ  
303  N N   . ARG A 60  ? 1.31264 0.67867 0.59556 0.25128  0.09161  -0.03906 52  ARG A N   
304  C CA  . ARG A 60  ? 1.29294 0.63335 0.57221 0.24774  0.09569  -0.01846 52  ARG A CA  
305  C C   . ARG A 60  ? 1.31191 0.63386 0.59928 0.22297  0.09905  -0.02003 52  ARG A C   
306  O O   . ARG A 60  ? 1.34747 0.69529 0.64364 0.20780  0.09735  -0.02946 52  ARG A O   
307  C CB  . ARG A 60  ? 1.26387 0.63646 0.53577 0.25182  0.09558  -0.00219 52  ARG A CB  
308  C CG  . ARG A 60  ? 1.27634 0.67125 0.54459 0.27507  0.09008  -0.00019 52  ARG A CG  
309  C CD  . ARG A 60  ? 1.27334 0.69328 0.53106 0.27924  0.08777  0.01713  52  ARG A CD  
310  N NE  . ARG A 60  ? 1.30395 0.76163 0.56439 0.26506  0.08772  0.01069  52  ARG A NE  
311  C CZ  . ARG A 60  ? 1.25421 0.74830 0.52358 0.26717  0.08250  -0.00163 52  ARG A CZ  
312  N NH1 . ARG A 60  ? 1.20535 0.70749 0.48080 0.28244  0.07855  -0.00920 52  ARG A NH1 
313  N NH2 . ARG A 60  ? 1.20362 0.72618 0.47785 0.25369  0.08197  -0.00635 52  ARG A NH2 
314  N N   . GLU A 61  ? 1.33653 0.61516 0.62420 0.21912  0.10283  -0.01012 53  GLU A N   
315  C CA  . GLU A 61  ? 1.35785 0.61458 0.65728 0.19512  0.10660  -0.00924 53  GLU A CA  
316  C C   . GLU A 61  ? 1.45994 0.72089 0.75610 0.18623  0.11542  0.01452  53  GLU A C   
317  O O   . GLU A 61  ? 1.52007 0.77079 0.80127 0.19968  0.11732  0.03338  53  GLU A O   
318  C CB  . GLU A 61  ? 1.37774 0.58196 0.68107 0.19537  0.10504  -0.01503 53  GLU A CB  
319  C CG  . GLU A 61  ? 1.43540 0.61497 0.75435 0.16983  0.10745  -0.01435 53  GLU A CG  
320  C CD  . GLU A 61  ? 1.43052 0.63688 0.76393 0.15015  0.10319  -0.03100 53  GLU A CD  
321  O OE1 . GLU A 61  ? 1.42184 0.65390 0.75083 0.15605  0.09626  -0.04800 53  GLU A OE1 
322  O OE2 . GLU A 61  ? 1.45844 0.66062 0.80923 0.12856  0.10655  -0.02563 53  GLU A OE2 
323  N N   . PHE A 62  ? 1.39013 0.66703 0.70014 0.16454  0.12054  0.01361  54  PHE A N   
324  C CA  . PHE A 62  ? 1.30202 0.59220 0.60991 0.15343  0.13219  0.03207  54  PHE A CA  
325  C C   . PHE A 62  ? 1.41558 0.67907 0.74058 0.13104  0.14042  0.03928  54  PHE A C   
326  O O   . PHE A 62  ? 1.45280 0.71969 0.77327 0.12188  0.15292  0.05785  54  PHE A O   
327  C CB  . PHE A 62  ? 1.25845 0.59854 0.57343 0.14838  0.13323  0.02290  54  PHE A CB  
328  C CG  . PHE A 62  ? 1.25693 0.62601 0.55750 0.16744  0.12569  0.01789  54  PHE A CG  
329  C CD1 . PHE A 62  ? 1.26154 0.63899 0.56679 0.17595  0.11469  0.00062  54  PHE A CD1 
330  C CD2 . PHE A 62  ? 1.25325 0.64256 0.53490 0.17560  0.12957  0.03059  54  PHE A CD2 
331  C CE1 . PHE A 62  ? 1.24833 0.65439 0.54406 0.19188  0.10858  -0.00276 54  PHE A CE1 
332  C CE2 . PHE A 62  ? 1.20659 0.62348 0.47854 0.19169  0.12123  0.02578  54  PHE A CE2 
333  C CZ  . PHE A 62  ? 1.24387 0.66941 0.52508 0.19966  0.11116  0.00966  54  PHE A CZ  
334  N N   . ILE A 63  ? 1.40689 0.64618 0.75014 0.12144  0.13392  0.02507  55  ILE A N   
335  C CA  . ILE A 63  ? 1.43257 0.65174 0.80033 0.09671  0.13923  0.02793  55  ILE A CA  
336  C C   . ILE A 63  ? 1.51086 0.67302 0.87717 0.09714  0.13635  0.03323  55  ILE A C   
337  O O   . ILE A 63  ? 1.53633 0.67439 0.90282 0.08842  0.14624  0.05552  55  ILE A O   
338  C CB  . ILE A 63  ? 1.35839 0.59916 0.75307 0.08174  0.13114  0.00597  55  ILE A CB  
339  C CG1 . ILE A 63  ? 1.36133 0.65390 0.76675 0.07733  0.13615  0.00424  55  ILE A CG1 
340  C CG2 . ILE A 63  ? 1.42392 0.63690 0.84570 0.05843  0.13120  0.00507  55  ILE A CG2 
341  C CD1 . ILE A 63  ? 1.36443 0.68128 0.79503 0.06732  0.12433  -0.01582 55  ILE A CD1 
342  N N   . GLN A 64  ? 1.56631 0.70773 0.93144 0.10598  0.12384  0.01301  56  GLN A N   
343  C CA  . GLN A 64  ? 1.55251 0.63823 0.92418 0.10247  0.11874  0.00830  56  GLN A CA  
344  C C   . GLN A 64  ? 1.59820 0.65039 0.95041 0.12633  0.11878  0.02043  56  GLN A C   
345  O O   . GLN A 64  ? 1.60926 0.67942 0.94509 0.14944  0.11475  0.01331  56  GLN A O   
346  C CB  . GLN A 64  ? 1.51431 0.59687 0.89250 0.09926  0.10550  -0.02308 56  GLN A CB  
347  C CG  . GLN A 64  ? 1.70650 0.74093 1.10180 0.08224  0.10002  -0.03195 56  GLN A CG  
348  C CD  . GLN A 64  ? 1.81223 0.84428 1.20798 0.07822  0.08584  -0.06420 56  GLN A CD  
349  O OE1 . GLN A 64  ? 1.71466 0.78207 1.09798 0.08713  0.08053  -0.07871 56  GLN A OE1 
350  N NE2 . GLN A 64  ? 1.83621 0.82552 1.24512 0.06340  0.07904  -0.07541 56  GLN A NE2 
351  N N   . GLU A 65  ? 1.63967 0.64540 0.99690 0.12038  0.12267  0.03926  57  GLU A N   
352  C CA  . GLU A 65  ? 1.70820 0.67014 1.05432 0.14164  0.12003  0.05157  57  GLU A CA  
353  C C   . GLU A 65  ? 1.80118 0.73364 1.15155 0.15403  0.10943  0.02141  57  GLU A C   
354  O O   . GLU A 65  ? 1.82375 0.75424 1.18593 0.13868  0.10449  -0.00295 57  GLU A O   
355  C CB  . GLU A 65  ? 1.75512 0.67288 1.10961 0.12679  0.12625  0.08012  57  GLU A CB  
356  C CG  . GLU A 65  ? 1.86555 0.81117 1.20908 0.11686  0.13908  0.11191  57  GLU A CG  
357  C CD  . GLU A 65  ? 2.03010 0.94759 1.38844 0.08962  0.14896  0.13534  57  GLU A CD  
358  O OE1 . GLU A 65  ? 2.09155 0.99971 1.47668 0.06730  0.14857  0.12077  57  GLU A OE1 
359  O OE2 . GLU A 65  ? 2.00294 0.90955 1.34597 0.08968  0.15663  0.16910  57  GLU A OE2 
360  N N   . PRO A 66  ? 1.73869 0.64845 1.08023 0.18196  0.10541  0.02065  58  PRO A N   
361  C CA  . PRO A 66  ? 1.71155 0.62206 1.04027 0.20153  0.10764  0.05016  58  PRO A CA  
362  C C   . PRO A 66  ? 1.71663 0.68291 1.02866 0.22112  0.10711  0.04922  58  PRO A C   
363  O O   . PRO A 66  ? 1.74055 0.71228 1.04098 0.23489  0.10729  0.07445  58  PRO A O   
364  C CB  . PRO A 66  ? 1.71962 0.57398 1.05616 0.22202  0.10120  0.04511  58  PRO A CB  
365  C CG  . PRO A 66  ? 1.72010 0.57683 1.06128 0.22674  0.09676  0.00301  58  PRO A CG  
366  C CD  . PRO A 66  ? 1.73721 0.61901 1.08208 0.19648  0.09811  -0.01013 58  PRO A CD  
367  N N   . ALA A 67  ? 1.70702 0.71231 1.01817 0.22110  0.10523  0.02179  59  ALA A N   
368  C CA  . ALA A 67  ? 1.63170 0.69060 0.93099 0.23764  0.10398  0.01739  59  ALA A CA  
369  C C   . ALA A 67  ? 1.62931 0.72658 0.91832 0.22831  0.10909  0.04038  59  ALA A C   
370  O O   . ALA A 67  ? 1.57860 0.70930 0.85608 0.24481  0.10707  0.04743  59  ALA A O   
371  C CB  . ALA A 67  ? 1.61254 0.69956 0.91409 0.23364  0.10118  -0.01456 59  ALA A CB  
372  N N   . LYS A 68  ? 1.70661 0.80065 1.00115 0.20249  0.11573  0.04978  60  LYS A N   
373  C CA  . LYS A 68  ? 1.65771 0.78341 0.94311 0.19044  0.12410  0.07051  60  LYS A CA  
374  C C   . LYS A 68  ? 1.69116 0.81319 0.95560 0.20738  0.12383  0.09850  60  LYS A C   
375  O O   . LYS A 68  ? 1.62189 0.78584 0.87119 0.21160  0.12512  0.10501  60  LYS A O   
376  C CB  . LYS A 68  ? 1.65671 0.76416 0.95574 0.16207  0.13309  0.07952  60  LYS A CB  
377  C CG  . LYS A 68  ? 1.60818 0.74693 0.89975 0.14745  0.14547  0.09841  60  LYS A CG  
378  C CD  . LYS A 68  ? 1.65789 0.77259 0.96378 0.12152  0.15648  0.11312  60  LYS A CD  
379  C CE  . LYS A 68  ? 1.71626 0.87066 1.02130 0.10419  0.17160  0.12287  60  LYS A CE  
380  N NZ  . LYS A 68  ? 1.76101 0.92090 1.03405 0.11097  0.17922  0.15129  60  LYS A NZ  
381  N N   . ASN A 69  ? 1.60418 0.67695 0.86854 0.21659  0.12063  0.11411  61  ASN A N   
382  C CA  . ASN A 69  ? 1.61446 0.67498 0.85990 0.23047  0.11821  0.14661  61  ASN A CA  
383  C C   . ASN A 69  ? 1.59855 0.65806 0.84422 0.26276  0.10594  0.14114  61  ASN A C   
384  O O   . ASN A 69  ? 1.64815 0.67172 0.89193 0.27734  0.09983  0.16272  61  ASN A O   
385  C CB  . ASN A 69  ? 1.70311 0.70874 0.95141 0.21854  0.12194  0.17246  61  ASN A CB  
386  C CG  . ASN A 69  ? 1.73829 0.74680 0.99188 0.18581  0.13564  0.17784  61  ASN A CG  
387  O OD1 . ASN A 69  ? 1.83246 0.79754 1.10191 0.17056  0.13868  0.18382  61  ASN A OD1 
388  N ND2 . ASN A 69  ? 1.69060 0.75019 0.93434 0.17475  0.14409  0.17505  61  ASN A ND2 
389  N N   . ARG A 70  ? 1.55020 0.64935 0.80007 0.27339  0.10246  0.11510  62  ARG A N   
390  C CA  . ARG A 70  ? 1.54698 0.65711 0.80079 0.30359  0.09282  0.10751  62  ARG A CA  
391  C C   . ARG A 70  ? 1.55844 0.68988 0.79430 0.31670  0.08648  0.13530  62  ARG A C   
392  O O   . ARG A 70  ? 1.54723 0.72121 0.76720 0.30749  0.08862  0.13946  62  ARG A O   
393  C CB  . ARG A 70  ? 1.50006 0.65405 0.76076 0.30607  0.09278  0.07586  62  ARG A CB  
394  C CG  . ARG A 70  ? 1.48277 0.65870 0.74976 0.33490  0.08533  0.06793  62  ARG A CG  
395  C CD  . ARG A 70  ? 1.52183 0.74394 0.79367 0.33394  0.08656  0.04041  62  ARG A CD  
396  N NE  . ARG A 70  ? 1.52228 0.72867 0.80172 0.32081  0.09139  0.01446  62  ARG A NE  
397  C CZ  . ARG A 70  ? 1.49531 0.73493 0.77663 0.31421  0.09265  -0.00871 62  ARG A CZ  
398  N NH1 . ARG A 70  ? 1.38860 0.67865 0.66794 0.31921  0.09039  -0.00969 62  ARG A NH1 
399  N NH2 . ARG A 70  ? 1.60053 0.82195 0.88538 0.30156  0.09498  -0.03017 62  ARG A NH2 
400  N N   . PRO A 71  ? 1.60118 0.70395 0.83969 0.33866  0.07725  0.15441  63  PRO A N   
401  C CA  . PRO A 71  ? 1.61268 0.73710 0.83415 0.35260  0.06742  0.18110  63  PRO A CA  
402  C C   . PRO A 71  ? 1.55904 0.74536 0.77894 0.36238  0.06266  0.16561  63  PRO A C   
403  O O   . PRO A 71  ? 1.57387 0.77549 0.81371 0.37224  0.06302  0.13797  63  PRO A O   
404  C CB  . PRO A 71  ? 1.66490 0.74862 0.90268 0.37936  0.05613  0.19453  63  PRO A CB  
405  C CG  . PRO A 71  ? 1.69779 0.72383 0.95258 0.37078  0.06289  0.18562  63  PRO A CG  
406  C CD  . PRO A 71  ? 1.64818 0.69515 0.90763 0.35151  0.07425  0.15115  63  PRO A CD  
407  N N   . GLY A 72  ? 1.57067 0.79054 0.76605 0.35815  0.05863  0.18340  64  GLY A N   
408  C CA  . GLY A 72  ? 1.50700 0.78469 0.69999 0.36585  0.05193  0.17236  64  GLY A CA  
409  C C   . GLY A 72  ? 1.52257 0.80884 0.72888 0.39612  0.03583  0.18043  64  GLY A C   
410  O O   . GLY A 72  ? 1.56515 0.81182 0.78590 0.41273  0.03074  0.19099  64  GLY A O   
411  N N   . PRO A 73  ? 1.49052 0.82837 0.69664 0.40456  0.02665  0.17536  65  PRO A N   
412  C CA  . PRO A 73  ? 1.44172 0.82480 0.63495 0.38619  0.03152  0.16074  65  PRO A CA  
413  C C   . PRO A 73  ? 1.46719 0.86214 0.67998 0.37602  0.04330  0.12792  65  PRO A C   
414  O O   . PRO A 73  ? 1.58876 0.97210 0.82574 0.38876  0.04475  0.11316  65  PRO A O   
415  C CB  . PRO A 73  ? 1.42784 0.85700 0.62392 0.40202  0.01544  0.16371  65  PRO A CB  
416  C CG  . PRO A 73  ? 1.44934 0.86535 0.67527 0.43066  0.00627  0.16641  65  PRO A CG  
417  C CD  . PRO A 73  ? 1.50240 0.85740 0.72491 0.43256  0.00991  0.18373  65  PRO A CD  
418  N N   . GLN A 74  ? 1.38977 0.80804 0.59155 0.35389  0.05100  0.11727  66  GLN A N   
419  C CA  . GLN A 74  ? 1.33015 0.75877 0.54745 0.34015  0.06077  0.08982  66  GLN A CA  
420  C C   . GLN A 74  ? 1.33136 0.80770 0.56402 0.34739  0.05473  0.07238  66  GLN A C   
421  O O   . GLN A 74  ? 1.36906 0.85184 0.61814 0.34311  0.05999  0.05114  66  GLN A O   
422  C CB  . GLN A 74  ? 1.30463 0.73444 0.50830 0.31384  0.07116  0.08868  66  GLN A CB  
423  C CG  . GLN A 74  ? 1.34650 0.73081 0.53957 0.30313  0.07969  0.10481  66  GLN A CG  
424  C CD  . GLN A 74  ? 1.41666 0.76086 0.62849 0.30558  0.08319  0.09562  66  GLN A CD  
425  O OE1 . GLN A 74  ? 1.33210 0.68377 0.56096 0.30234  0.08537  0.07187  66  GLN A OE1 
426  N NE2 . GLN A 74  ? 1.47597 0.77584 0.68358 0.31074  0.08295  0.11464  66  GLN A NE2 
427  N N   . THR A 75  ? 1.31800 0.82692 0.54488 0.35635  0.04346  0.08158  67  THR A N   
428  C CA  . THR A 75  ? 1.25779 0.81243 0.50345 0.36546  0.03561  0.06879  67  THR A CA  
429  C C   . THR A 75  ? 1.30020 0.87439 0.54302 0.38311  0.01972  0.08605  67  THR A C   
430  O O   . THR A 75  ? 1.33999 0.88904 0.56427 0.38848  0.01488  0.10828  67  THR A O   
431  C CB  . THR A 75  ? 1.27130 0.85897 0.51673 0.34580  0.03839  0.05347  67  THR A CB  
432  O OG1 . THR A 75  ? 1.28996 0.91772 0.55681 0.35410  0.03124  0.04272  67  THR A OG1 
433  C CG2 . THR A 75  ? 1.23631 0.83454 0.45671 0.33335  0.03587  0.06295  67  THR A CG2 
434  N N   . ARG A 76  ? 1.29677 0.91472 0.55833 0.39074  0.01104  0.07736  68  ARG A N   
435  C CA  . ARG A 76  ? 1.34176 0.98596 0.60778 0.40785  -0.00691 0.09149  68  ARG A CA  
436  C C   . ARG A 76  ? 1.30762 0.96908 0.54319 0.39448  -0.01584 0.10091  68  ARG A C   
437  O O   . ARG A 76  ? 1.24879 0.91504 0.47134 0.37338  -0.00705 0.08929  68  ARG A O   
438  C CB  . ARG A 76  ? 1.37136 1.05749 0.67347 0.41902  -0.01118 0.07722  68  ARG A CB  
439  C CG  . ARG A 76  ? 1.34378 1.07068 0.65062 0.40155  -0.01163 0.06149  68  ARG A CG  
440  C CD  . ARG A 76  ? 1.30636 1.07984 0.64782 0.41256  -0.01979 0.05450  68  ARG A CD  
441  N NE  . ARG A 76  ? 1.37479 1.16055 0.73854 0.40712  -0.00659 0.03515  68  ARG A NE  
442  C CZ  . ARG A 76  ? 1.38536 1.17122 0.77341 0.42223  0.00177  0.02798  68  ARG A CZ  
443  N NH1 . ARG A 76  ? 1.35950 1.13225 0.75905 0.44607  -0.00180 0.03756  68  ARG A NH1 
444  N NH2 . ARG A 76  ? 1.37062 1.16995 0.77145 0.41342  0.01383  0.01091  68  ARG A NH2 
445  N N   . SER A 77  ? 1.35181 1.02314 0.57743 0.40692  -0.03337 0.12038  69  SER A N   
446  C CA  . SER A 77  ? 1.29962 0.98056 0.48700 0.39641  -0.04330 0.13327  69  SER A CA  
447  C C   . SER A 77  ? 1.27838 1.00503 0.46834 0.38383  -0.04912 0.11511  69  SER A C   
448  O O   . SER A 77  ? 1.24226 1.00030 0.46744 0.39024  -0.05419 0.10186  69  SER A O   
449  C CB  . SER A 77  ? 1.34698 1.02561 0.52462 0.41450  -0.06331 0.16014  69  SER A CB  
450  O OG  . SER A 77  ? 1.42677 1.10696 0.55832 0.40270  -0.07066 0.17462  69  SER A OG  
451  N N   . ASP A 78  ? 1.27338 1.00316 0.42758 0.36632  -0.04783 0.11465  70  ASP A N   
452  C CA  . ASP A 78  ? 1.24772 1.01859 0.40718 0.35052  -0.05483 0.09701  70  ASP A CA  
453  C C   . ASP A 78  ? 1.26757 1.06965 0.42932 0.36033  -0.08003 0.10726  70  ASP A C   
454  O O   . ASP A 78  ? 1.24696 1.08528 0.42032 0.35061  -0.08979 0.09232  70  ASP A O   
455  C CB  . ASP A 78  ? 1.25230 1.01802 0.39287 0.32395  -0.04214 0.08964  70  ASP A CB  
456  C CG  . ASP A 78  ? 1.30541 1.05558 0.41189 0.31997  -0.04452 0.11154  70  ASP A CG  
457  O OD1 . ASP A 78  ? 1.33891 1.06344 0.43588 0.33642  -0.04898 0.13477  70  ASP A OD1 
458  O OD2 . ASP A 78  ? 1.31625 1.07970 0.40575 0.30044  -0.04196 0.10561  70  ASP A OD2 
459  N N   . LEU A 79  ? 1.30863 1.09602 0.46188 0.37851  -0.09147 0.13234  71  LEU A N   
460  C CA  . LEU A 79  ? 1.33434 1.14944 0.49246 0.38924  -0.11809 0.14633  71  LEU A CA  
461  C C   . LEU A 79  ? 1.30522 1.15305 0.50270 0.40974  -0.13117 0.13945  71  LEU A C   
462  O O   . LEU A 79  ? 1.32111 1.20366 0.53089 0.41439  -0.15414 0.14408  71  LEU A O   
463  C CB  . LEU A 79  ? 1.38843 1.17245 0.53101 0.40233  -0.12490 0.17712  71  LEU A CB  
464  C CG  . LEU A 79  ? 1.45202 1.20965 0.55412 0.38155  -0.11479 0.18889  71  LEU A CG  
465  C CD1 . LEU A 79  ? 1.50375 1.22092 0.59597 0.39550  -0.11713 0.21980  71  LEU A CD1 
466  C CD2 . LEU A 79  ? 1.44662 1.23534 0.52701 0.36261  -0.12862 0.18828  71  LEU A CD2 
467  N N   . LEU A 80  ? 1.29525 1.13730 0.52693 0.41388  -0.11439 0.12555  72  LEU A N   
468  C CA  . LEU A 80  ? 1.28195 1.15617 0.56809 0.42811  -0.11894 0.11693  72  LEU A CA  
469  C C   . LEU A 80  ? 1.25420 1.17567 0.55747 0.41481  -0.12767 0.09882  72  LEU A C   
470  O O   . LEU A 80  ? 1.24792 1.20528 0.59483 0.42537  -0.13643 0.09541  72  LEU A O   
471  C CB  . LEU A 80  ? 1.22585 1.07711 0.53599 0.43154  -0.09522 0.10557  72  LEU A CB  
472  C CG  . LEU A 80  ? 1.25887 1.06237 0.56096 0.44606  -0.08742 0.12103  72  LEU A CG  
473  C CD1 . LEU A 80  ? 1.30963 1.08918 0.62772 0.44390  -0.06364 0.10487  72  LEU A CD1 
474  C CD2 . LEU A 80  ? 1.28700 1.09822 0.61482 0.47368  -0.10447 0.13866  72  LEU A CD2 
475  N N   . LEU A 81  ? 1.27317 1.19503 0.54657 0.39260  -0.12494 0.08723  73  LEU A N   
476  C CA  . LEU A 81  ? 1.28116 1.24294 0.56725 0.37800  -0.13548 0.06977  73  LEU A CA  
477  C C   . LEU A 81  ? 1.24875 1.21078 0.49284 0.36201  -0.14537 0.06854  73  LEU A C   
478  O O   . LEU A 81  ? 1.29588 1.22554 0.50949 0.35368  -0.13403 0.07611  73  LEU A O   
479  C CB  . LEU A 81  ? 1.21095 1.17180 0.51742 0.36277  -0.11588 0.04840  73  LEU A CB  
480  C CG  . LEU A 81  ? 1.16480 1.13636 0.51756 0.37227  -0.10590 0.04444  73  LEU A CG  
481  C CD1 . LEU A 81  ? 1.16407 1.12718 0.52537 0.35507  -0.08696 0.02699  73  LEU A CD1 
482  C CD2 . LEU A 81  ? 1.16403 1.18430 0.55806 0.37968  -0.12314 0.04423  73  LEU A CD2 
483  N N   . SER A 82  ? 1.24331 1.24217 0.49866 0.35233  -0.16281 0.05700  74  SER A N   
484  C CA  . SER A 82  ? 1.26994 1.27438 0.50126 0.32925  -0.16891 0.04669  74  SER A CA  
485  C C   . SER A 82  ? 1.23151 1.21868 0.45720 0.30872  -0.14654 0.02553  74  SER A C   
486  O O   . SER A 82  ? 1.24079 1.22686 0.49059 0.31024  -0.13514 0.01555  74  SER A O   
487  C CB  . SER A 82  ? 1.28685 1.33436 0.53577 0.32648  -0.19524 0.03871  74  SER A CB  
488  O OG  . SER A 82  ? 1.23375 1.30353 0.51718 0.32530  -0.19447 0.02187  74  SER A OG  
489  N N   . GLY A 83  ? 1.22915 1.20525 0.42503 0.29039  -0.14086 0.01940  75  GLY A N   
490  C CA  . GLY A 83  ? 1.26294 1.22696 0.45661 0.27096  -0.12169 -0.00191 75  GLY A CA  
491  C C   . GLY A 83  ? 1.23592 1.22297 0.45922 0.26429  -0.12825 -0.02450 75  GLY A C   
492  O O   . GLY A 83  ? 1.22963 1.20469 0.46689 0.25605  -0.11189 -0.03830 75  GLY A O   
493  N N   . ARG A 84  ? 1.29033 1.30962 0.52409 0.26728  -0.15295 -0.02723 76  ARG A N   
494  C CA  . ARG A 84  ? 1.27080 1.31645 0.53497 0.26187  -0.16448 -0.04655 76  ARG A CA  
495  C C   . ARG A 84  ? 1.20762 1.25482 0.50370 0.27269  -0.15612 -0.04327 76  ARG A C   
496  O O   . ARG A 84  ? 1.18715 1.23428 0.50711 0.26073  -0.14853 -0.05924 76  ARG A O   
497  C CB  . ARG A 84  ? 1.28815 1.37014 0.55887 0.26448  -0.19503 -0.04565 76  ARG A CB  
498  C CG  . ARG A 84  ? 1.31761 1.43251 0.62849 0.26420  -0.21022 -0.05796 76  ARG A CG  
499  C CD  . ARG A 84  ? 1.46157 1.61271 0.78018 0.26072  -0.24155 -0.06232 76  ARG A CD  
500  N NE  . ARG A 84  ? 1.61844 1.76783 0.92224 0.23989  -0.24740 -0.08728 76  ARG A NE  
501  C CZ  . ARG A 84  ? 1.63036 1.78298 0.95773 0.22649  -0.24666 -0.11049 76  ARG A CZ  
502  N NH1 . ARG A 84  ? 1.50722 1.66284 0.88529 0.22463  -0.23548 -0.10765 76  ARG A NH1 
503  N NH2 . ARG A 84  ? 1.65750 1.80685 0.96699 0.21059  -0.25340 -0.13493 76  ARG A NH2 
504  N N   . ASP A 85  ? 1.20719 1.25520 0.51232 0.29129  -0.15596 -0.02295 77  ASP A N   
505  C CA  . ASP A 85  ? 1.13976 1.18995 0.48771 0.29732  -0.14324 -0.01858 77  ASP A CA  
506  C C   . ASP A 85  ? 1.12384 1.13931 0.46349 0.28966  -0.11793 -0.02479 77  ASP A C   
507  O O   . ASP A 85  ? 1.12269 1.14341 0.49437 0.28071  -0.10997 -0.03382 77  ASP A O   
508  C CB  . ASP A 85  ? 1.13951 1.19439 0.49795 0.31978  -0.14663 0.00220  77  ASP A CB  
509  C CG  . ASP A 85  ? 1.20066 1.29934 0.59131 0.32759  -0.17024 0.00738  77  ASP A CG  
510  O OD1 . ASP A 85  ? 1.18674 1.31214 0.59077 0.31389  -0.18487 -0.00523 77  ASP A OD1 
511  O OD2 . ASP A 85  ? 1.27396 1.37979 0.67942 0.34745  -0.17430 0.02349  77  ASP A OD2 
512  N N   . TRP A 86  ? 1.13608 1.11863 0.43527 0.29188  -0.10668 -0.01896 78  TRP A N   
513  C CA  . TRP A 86  ? 1.12502 1.07512 0.41890 0.28211  -0.08344 -0.02495 78  TRP A CA  
514  C C   . TRP A 86  ? 1.15847 1.11389 0.46348 0.26278  -0.08146 -0.04661 78  TRP A C   
515  O O   . TRP A 86  ? 1.21643 1.16113 0.53882 0.25662  -0.06932 -0.05351 78  TRP A O   
516  C CB  . TRP A 86  ? 1.07927 0.99942 0.34365 0.28040  -0.07218 -0.01433 78  TRP A CB  
517  C CG  . TRP A 86  ? 1.16762 1.07259 0.42005 0.30000  -0.07217 0.00732  78  TRP A CG  
518  C CD1 . TRP A 86  ? 1.20123 1.10440 0.43088 0.30868  -0.08290 0.02424  78  TRP A CD1 
519  C CD2 . TRP A 86  ? 1.18354 1.07026 0.44425 0.31386  -0.06151 0.01438  78  TRP A CD2 
520  N NE1 . TRP A 86  ? 1.16856 1.05208 0.39415 0.32855  -0.08035 0.04220  78  TRP A NE1 
521  C CE2 . TRP A 86  ? 1.22146 1.09436 0.46606 0.33209  -0.06652 0.03509  78  TRP A CE2 
522  C CE3 . TRP A 86  ? 1.10323 0.98413 0.38992 0.30987  -0.04830 0.00504  78  TRP A CE3 
523  C CZ2 . TRP A 86  ? 1.19689 1.04981 0.45731 0.34570  -0.05737 0.04357  78  TRP A CZ2 
524  C CZ3 . TRP A 86  ? 1.13504 0.99819 0.43245 0.32225  -0.03919 0.01312  78  TRP A CZ3 
525  C CH2 . TRP A 86  ? 1.14869 0.99736 0.43429 0.34027  -0.04310 0.03073  78  TRP A CH2 
526  N N   . ASN A 87  ? 1.12096 1.09153 0.41676 0.25372  -0.09399 -0.05714 79  ASN A N   
527  C CA  . ASN A 87  ? 1.14955 1.12206 0.45126 0.23684  -0.09324 -0.08040 79  ASN A CA  
528  C C   . ASN A 87  ? 1.13610 1.12815 0.47923 0.23184  -0.10196 -0.08996 79  ASN A C   
529  O O   . ASN A 87  ? 1.18934 1.17301 0.54943 0.21905  -0.09542 -0.10516 79  ASN A O   
530  C CB  . ASN A 87  ? 1.16967 1.15393 0.45027 0.22851  -0.10526 -0.09037 79  ASN A CB  
531  C CG  . ASN A 87  ? 1.20546 1.16875 0.45609 0.22037  -0.08926 -0.08983 79  ASN A CG  
532  O OD1 . ASN A 87  ? 1.15337 1.09355 0.39970 0.22186  -0.07059 -0.07980 79  ASN A OD1 
533  N ND2 . ASN A 87  ? 1.36447 1.33709 0.59352 0.21074  -0.09660 -0.10133 79  ASN A ND2 
534  N N   . THR A 88  ? 1.05612 1.07438 0.42467 0.23865  -0.11520 -0.07994 80  THR A N   
535  C CA  . THR A 88  ? 1.09284 1.13673 0.50866 0.22899  -0.12540 -0.08650 80  THR A CA  
536  C C   . THR A 88  ? 1.12473 1.17343 0.57168 0.23398  -0.11547 -0.07343 80  THR A C   
537  O O   . THR A 88  ? 1.20015 1.25201 0.67804 0.22162  -0.11239 -0.07876 80  THR A O   
538  C CB  . THR A 88  ? 1.11675 1.19430 0.54108 0.22919  -0.15002 -0.08845 80  THR A CB  
539  O OG1 . THR A 88  ? 1.11770 1.20686 0.53349 0.24706  -0.15541 -0.06967 80  THR A OG1 
540  C CG2 . THR A 88  ? 1.12831 1.20276 0.52173 0.22102  -0.16086 -0.10586 80  THR A CG2 
541  N N   . LEU A 89  ? 1.13159 1.18019 0.57057 0.25110  -0.11076 -0.05732 81  LEU A N   
542  C CA  . LEU A 89  ? 1.11698 1.18073 0.58743 0.25842  -0.10426 -0.04670 81  LEU A CA  
543  C C   . LEU A 89  ? 1.04989 1.08324 0.51099 0.26117  -0.08258 -0.04286 81  LEU A C   
544  O O   . LEU A 89  ? 1.05163 1.09551 0.53806 0.26037  -0.07489 -0.03964 81  LEU A O   
545  C CB  . LEU A 89  ? 1.07731 1.16233 0.55114 0.27743  -0.11395 -0.03367 81  LEU A CB  
546  C CG  . LEU A 89  ? 1.06465 1.17913 0.54246 0.27655  -0.13854 -0.03560 81  LEU A CG  
547  C CD1 . LEU A 89  ? 1.04154 1.17940 0.53159 0.29676  -0.14849 -0.02049 81  LEU A CD1 
548  C CD2 . LEU A 89  ? 1.05781 1.20040 0.57273 0.25849  -0.14909 -0.04674 81  LEU A CD2 
549  N N   . ILE A 90  ? 1.06541 1.06420 0.49155 0.26353  -0.07299 -0.04297 82  ILE A N   
550  C CA  . ILE A 90  ? 1.01293 0.98155 0.42796 0.26871  -0.05444 -0.03776 82  ILE A CA  
551  C C   . ILE A 90  ? 1.02669 0.97304 0.43946 0.25243  -0.04462 -0.04773 82  ILE A C   
552  O O   . ILE A 90  ? 1.08794 1.02157 0.48241 0.24560  -0.04509 -0.05512 82  ILE A O   
553  C CB  . ILE A 90  ? 1.06344 1.00873 0.44543 0.28385  -0.05102 -0.02721 82  ILE A CB  
554  C CG1 . ILE A 90  ? 1.11050 1.07836 0.49801 0.30112  -0.06413 -0.01602 82  ILE A CG1 
555  C CG2 . ILE A 90  ? 0.95960 0.87270 0.33324 0.28820  -0.03342 -0.02323 82  ILE A CG2 
556  C CD1 . ILE A 90  ? 1.08304 1.07388 0.50589 0.31070  -0.06198 -0.01252 82  ILE A CD1 
557  N N   . VAL A 91  ? 1.03479 0.97814 0.46565 0.24681  -0.03606 -0.04781 83  VAL A N   
558  C CA  . VAL A 91  ? 1.02593 0.94482 0.45589 0.23404  -0.02637 -0.05364 83  VAL A CA  
559  C C   . VAL A 91  ? 1.00366 0.89499 0.41552 0.24251  -0.01252 -0.04757 83  VAL A C   
560  O O   . VAL A 91  ? 0.95447 0.85236 0.37204 0.25167  -0.00874 -0.04200 83  VAL A O   
561  C CB  . VAL A 91  ? 1.00817 0.94223 0.46907 0.21996  -0.02949 -0.05620 83  VAL A CB  
562  C CG1 . VAL A 91  ? 0.97964 0.88937 0.44151 0.20844  -0.02187 -0.05946 83  VAL A CG1 
563  C CG2 . VAL A 91  ? 0.98270 0.93991 0.46490 0.21013  -0.04404 -0.06288 83  VAL A CG2 
564  N N   . GLY A 92  ? 1.00491 0.86722 0.39744 0.23922  -0.00466 -0.04973 84  GLY A N   
565  C CA  . GLY A 92  ? 1.02806 0.86013 0.40471 0.24439  0.00766  -0.04499 84  GLY A CA  
566  C C   . GLY A 92  ? 1.00639 0.83208 0.39679 0.23533  0.01271  -0.04807 84  GLY A C   
567  O O   . GLY A 92  ? 1.04465 0.88503 0.45539 0.22260  0.00709  -0.05276 84  GLY A O   
568  N N   . LYS A 93  ? 1.04424 0.84758 0.42343 0.24115  0.02178  -0.04532 85  LYS A N   
569  C CA  . LYS A 93  ? 0.99709 0.79069 0.38195 0.23232  0.02634  -0.04876 85  LYS A CA  
570  C C   . LYS A 93  ? 0.98833 0.74502 0.35657 0.23239  0.03531  -0.04902 85  LYS A C   
571  O O   . LYS A 93  ? 1.02817 0.76897 0.38172 0.24614  0.04036  -0.04473 85  LYS A O   
572  C CB  . LYS A 93  ? 1.00031 0.81116 0.39051 0.24017  0.02799  -0.04779 85  LYS A CB  
573  C CG  . LYS A 93  ? 1.00264 0.85196 0.41432 0.23614  0.02009  -0.04657 85  LYS A CG  
574  C CD  . LYS A 93  ? 0.98734 0.85654 0.40497 0.24328  0.02528  -0.04571 85  LYS A CD  
575  C CE  . LYS A 93  ? 1.06074 0.92177 0.47291 0.23242  0.03118  -0.04890 85  LYS A CE  
576  N NZ  . LYS A 93  ? 1.11987 0.98335 0.52397 0.24504  0.04242  -0.05228 85  LYS A NZ  
577  N N   . LEU A 94  ? 0.95029 0.69385 0.32411 0.21740  0.03607  -0.05318 86  LEU A N   
578  C CA  . LEU A 94  ? 1.00962 0.71966 0.37295 0.21387  0.04343  -0.05416 86  LEU A CA  
579  C C   . LEU A 94  ? 1.04047 0.73863 0.39356 0.22133  0.04739  -0.05591 86  LEU A C   
580  O O   . LEU A 94  ? 1.06485 0.77856 0.42360 0.21709  0.04436  -0.05938 86  LEU A O   
581  C CB  . LEU A 94  ? 0.91976 0.62591 0.29876 0.19580  0.04046  -0.05870 86  LEU A CB  
582  C CG  . LEU A 94  ? 1.00342 0.67849 0.37758 0.18927  0.04651  -0.05998 86  LEU A CG  
583  C CD1 . LEU A 94  ? 1.05309 0.71430 0.41953 0.19184  0.05484  -0.05615 86  LEU A CD1 
584  C CD2 . LEU A 94  ? 1.00073 0.67684 0.39518 0.17218  0.04021  -0.06413 86  LEU A CD2 
585  N N   . SER A 95  ? 1.01318 0.68428 0.35136 0.23178  0.05426  -0.05368 87  SER A N   
586  C CA  . SER A 95  ? 1.06851 0.72191 0.39702 0.24053  0.05936  -0.05850 87  SER A CA  
587  C C   . SER A 95  ? 1.13891 0.78673 0.46840 0.22523  0.05780  -0.06739 87  SER A C   
588  O O   . SER A 95  ? 1.10380 0.73999 0.43841 0.21017  0.05522  -0.06796 87  SER A O   
589  C CB  . SER A 95  ? 1.02427 0.64182 0.34053 0.24974  0.06543  -0.05423 87  SER A CB  
590  O OG  . SER A 95  ? 1.08671 0.71118 0.39968 0.26578  0.06475  -0.04426 87  SER A OG  
591  N N   . PRO A 96  ? 1.05803 0.71655 0.38298 0.22813  0.05907  -0.07439 88  PRO A N   
592  C CA  . PRO A 96  ? 1.02605 0.68512 0.34798 0.21200  0.05516  -0.08118 88  PRO A CA  
593  C C   . PRO A 96  ? 1.06989 0.69166 0.38203 0.20358  0.05572  -0.08808 88  PRO A C   
594  O O   . PRO A 96  ? 1.15015 0.77185 0.46355 0.18683  0.04850  -0.09085 88  PRO A O   
595  C CB  . PRO A 96  ? 1.02095 0.70189 0.33970 0.21853  0.05948  -0.08642 88  PRO A CB  
596  C CG  . PRO A 96  ? 1.06840 0.74472 0.38531 0.24181  0.06792  -0.08678 88  PRO A CG  
597  C CD  . PRO A 96  ? 1.05698 0.73011 0.37986 0.24677  0.06448  -0.07593 88  PRO A CD  
598  N N   . TRP A 97  ? 1.09043 0.68133 0.39516 0.21431  0.06255  -0.08953 89  TRP A N   
599  C CA  . TRP A 97  ? 1.10937 0.66156 0.40760 0.20594  0.06305  -0.09594 89  TRP A CA  
600  C C   . TRP A 97  ? 1.13005 0.67670 0.44311 0.18940  0.05823  -0.08897 89  TRP A C   
601  O O   . TRP A 97  ? 1.11037 0.63497 0.42433 0.17609  0.05497  -0.09447 89  TRP A O   
602  C CB  . TRP A 97  ? 1.09814 0.61755 0.38802 0.22240  0.07137  -0.09731 89  TRP A CB  
603  C CG  . TRP A 97  ? 1.15048 0.66499 0.44592 0.23211  0.07454  -0.08244 89  TRP A CG  
604  C CD1 . TRP A 97  ? 1.16237 0.69421 0.45868 0.25011  0.07648  -0.07458 89  TRP A CD1 
605  C CD2 . TRP A 97  ? 1.21352 0.70468 0.51270 0.22383  0.07606  -0.07292 89  TRP A CD2 
606  N NE1 . TRP A 97  ? 1.22849 0.74868 0.52478 0.25334  0.07771  -0.06046 89  TRP A NE1 
607  C CE2 . TRP A 97  ? 1.22183 0.71733 0.51904 0.23722  0.07895  -0.05898 89  TRP A CE2 
608  C CE3 . TRP A 97  ? 1.18496 0.65439 0.48991 0.20564  0.07525  -0.07423 89  TRP A CE3 
609  C CZ2 . TRP A 97  ? 1.19634 0.67465 0.49251 0.23245  0.08261  -0.04602 89  TRP A CZ2 
610  C CZ3 . TRP A 97  ? 1.22053 0.67447 0.52960 0.20115  0.08008  -0.06188 89  TRP A CZ3 
611  C CH2 . TRP A 97  ? 1.18222 0.64026 0.48470 0.21415  0.08449  -0.04775 89  TRP A CH2 
612  N N   . ILE A 98  ? 1.09719 0.66428 0.42277 0.19001  0.05789  -0.07882 90  ILE A N   
613  C CA  . ILE A 98  ? 1.06435 0.62961 0.40658 0.17674  0.05679  -0.07345 90  ILE A CA  
614  C C   . ILE A 98  ? 1.09423 0.67413 0.45230 0.15924  0.04611  -0.07754 90  ILE A C   
615  O O   . ILE A 98  ? 1.10320 0.71197 0.46863 0.15821  0.03984  -0.07606 90  ILE A O   
616  C CB  . ILE A 98  ? 1.09878 0.68255 0.44579 0.18386  0.06030  -0.06455 90  ILE A CB  
617  C CG1 . ILE A 98  ? 1.09253 0.66170 0.42251 0.20118  0.06781  -0.05764 90  ILE A CG1 
618  C CG2 . ILE A 98  ? 1.03778 0.62263 0.40231 0.17061  0.06194  -0.06212 90  ILE A CG2 
619  C CD1 . ILE A 98  ? 1.04877 0.63810 0.37729 0.20881  0.06890  -0.04922 90  ILE A CD1 
620  N N   . ARG A 99  ? 1.05537 0.61543 0.42020 0.14558  0.04280  -0.08145 91  ARG A N   
621  C CA  . ARG A 99  ? 1.07066 0.64034 0.45144 0.12815  0.02964  -0.08439 91  ARG A CA  
622  C C   . ARG A 99  ? 0.98736 0.54868 0.39456 0.11550  0.02966  -0.08237 91  ARG A C   
623  O O   . ARG A 99  ? 1.00867 0.54636 0.41703 0.10677  0.02867  -0.08622 91  ARG A O   
624  C CB  . ARG A 99  ? 1.03488 0.59030 0.39573 0.12333  0.02320  -0.09360 91  ARG A CB  
625  C CG  . ARG A 99  ? 1.02216 0.59194 0.35962 0.13383  0.02450  -0.09690 91  ARG A CG  
626  C CD  . ARG A 99  ? 1.38623 0.93530 0.69752 0.13299  0.02420  -0.10982 91  ARG A CD  
627  N NE  . ARG A 99  ? 1.42485 0.96579 0.73827 0.11332  0.01034  -0.11446 91  ARG A NE  
628  C CZ  . ARG A 99  ? 1.36872 0.92837 0.67588 0.10144  -0.00247 -0.11407 91  ARG A CZ  
629  N NH1 . ARG A 99  ? 1.34189 0.92974 0.64046 0.10628  -0.00155 -0.10916 91  ARG A NH1 
630  N NH2 . ARG A 99  ? 1.34203 0.89263 0.65226 0.08365  -0.01720 -0.11721 91  ARG A NH2 
631  N N   . PRO A 100 ? 0.98410 0.56513 0.41517 0.11393  0.03160  -0.07755 92  PRO A N   
632  C CA  . PRO A 100 ? 1.02136 0.59932 0.48143 0.10285  0.03480  -0.07664 92  PRO A CA  
633  C C   . PRO A 100 ? 0.98099 0.56138 0.46758 0.08594  0.01983  -0.07960 92  PRO A C   
634  O O   . PRO A 100 ? 0.95849 0.53437 0.47119 0.07616  0.02265  -0.07968 92  PRO A O   
635  C CB  . PRO A 100 ? 1.00620 0.60897 0.48318 0.10735  0.04008  -0.07427 92  PRO A CB  
636  C CG  . PRO A 100 ? 1.02075 0.63260 0.47120 0.12247  0.04200  -0.07228 92  PRO A CG  
637  C CD  . PRO A 100 ? 0.97698 0.58438 0.40974 0.12285  0.03205  -0.07434 92  PRO A CD  
638  N N   . ASP A 101 ? 1.01027 0.59939 0.49029 0.08230  0.00422  -0.08083 93  ASP A N   
639  C CA  . ASP A 101 ? 0.97599 0.56940 0.47799 0.06609  -0.01456 -0.08140 93  ASP A CA  
640  C C   . ASP A 101 ? 0.98333 0.55638 0.45652 0.05999  -0.02290 -0.08736 93  ASP A C   
641  O O   . ASP A 101 ? 1.06435 0.64280 0.54395 0.04723  -0.04160 -0.08721 93  ASP A O   
642  C CB  . ASP A 101 ? 0.96143 0.58162 0.47965 0.06430  -0.02807 -0.07592 93  ASP A CB  
643  C CG  . ASP A 101 ? 0.96860 0.60613 0.52463 0.06690  -0.02269 -0.07396 93  ASP A CG  
644  O OD1 . ASP A 101 ? 0.95080 0.59064 0.54449 0.05796  -0.02593 -0.07484 93  ASP A OD1 
645  O OD2 . ASP A 101 ? 0.98217 0.63122 0.53064 0.07791  -0.01476 -0.07298 93  ASP A OD2 
646  N N   . SER A 102 ? 1.01594 0.56532 0.45941 0.06851  -0.01047 -0.09277 94  SER A N   
647  C CA  . SER A 102 ? 1.10195 0.62568 0.51964 0.06313  -0.01567 -0.10272 94  SER A CA  
648  C C   . SER A 102 ? 1.10728 0.62124 0.55110 0.04398  -0.02823 -0.10511 94  SER A C   
649  O O   . SER A 102 ? 1.10874 0.62958 0.58986 0.03882  -0.02484 -0.09932 94  SER A O   
650  C CB  . SER A 102 ? 1.14748 0.64398 0.54100 0.07625  0.00083  -0.10749 94  SER A CB  
651  O OG  . SER A 102 ? 1.17657 0.64560 0.54844 0.07090  -0.00418 -0.12004 94  SER A OG  
652  N N   . LYS A 103 ? 1.12222 0.62269 0.54742 0.03352  -0.04212 -0.11428 95  LYS A N   
653  C CA  . LYS A 103 ? 1.15132 0.64190 0.59906 0.01372  -0.05797 -0.11807 95  LYS A CA  
654  C C   . LYS A 103 ? 1.15736 0.61503 0.60951 0.01193  -0.04608 -0.12388 95  LYS A C   
655  O O   . LYS A 103 ? 1.16658 0.61780 0.64867 -0.00451 -0.05517 -0.12487 95  LYS A O   
656  C CB  . LYS A 103 ? 1.23902 0.72746 0.65804 0.00283  -0.07849 -0.12655 95  LYS A CB  
657  C CG  . LYS A 103 ? 1.20116 0.72087 0.61574 0.00105  -0.09255 -0.11738 95  LYS A CG  
658  C CD  . LYS A 103 ? 1.18368 0.72609 0.64789 -0.01040 -0.10907 -0.10502 95  LYS A CD  
659  C CE  . LYS A 103 ? 1.24746 0.81373 0.70525 -0.01700 -0.12989 -0.09533 95  LYS A CE  
660  N NZ  . LYS A 103 ? 1.26711 0.82492 0.69442 -0.03250 -0.15126 -0.10179 95  LYS A NZ  
661  N N   . VAL A 104 ? 1.19334 0.63151 0.61983 0.02787  -0.02744 -0.12624 96  VAL A N   
662  C CA  . VAL A 104 ? 1.28183 0.68394 0.70903 0.02810  -0.01514 -0.12918 96  VAL A CA  
663  C C   . VAL A 104 ? 1.19949 0.61005 0.65526 0.03177  0.00140  -0.11456 96  VAL A C   
664  O O   . VAL A 104 ? 1.19165 0.61878 0.63845 0.04746  0.01258  -0.10706 96  VAL A O   
665  C CB  . VAL A 104 ? 1.30030 0.67554 0.68670 0.04467  -0.00502 -0.13842 96  VAL A CB  
666  C CG1 . VAL A 104 ? 1.29742 0.62921 0.68529 0.04158  0.00182  -0.14304 96  VAL A CG1 
667  C CG2 . VAL A 104 ? 1.25445 0.63231 0.60686 0.04515  -0.01661 -0.15315 96  VAL A CG2 
668  N N   . GLU A 105 ? 1.22955 0.63045 0.71776 0.01687  0.00297  -0.11121 97  GLU A N   
669  C CA  . GLU A 105 ? 1.24374 0.65213 0.75879 0.01696  0.02103  -0.09792 97  GLU A CA  
670  C C   . GLU A 105 ? 1.17814 0.56951 0.66313 0.03549  0.03986  -0.09098 97  GLU A C   
671  O O   . GLU A 105 ? 1.24190 0.65487 0.72897 0.04512  0.05186  -0.08138 97  GLU A O   
672  C CB  . GLU A 105 ? 1.27132 0.66509 0.82101 -0.00332 0.02082  -0.09680 97  GLU A CB  
673  C CG  . GLU A 105 ? 1.19729 0.59537 0.76947 -0.00486 0.04285  -0.08297 97  GLU A CG  
674  C CD  . GLU A 105 ? 1.25423 0.65929 0.87661 -0.02685 0.04281  -0.08033 97  GLU A CD  
675  O OE1 . GLU A 105 ? 1.27613 0.67149 0.91411 -0.04227 0.02460  -0.08911 97  GLU A OE1 
676  O OE2 . GLU A 105 ? 1.23266 0.65463 0.87876 -0.02899 0.06122  -0.07004 97  GLU A OE2 
677  N N   . LYS A 106 ? 1.18403 0.53807 0.64261 0.04070  0.04090  -0.09650 98  LYS A N   
678  C CA  . LYS A 106 ? 1.26464 0.59668 0.69791 0.05850  0.05620  -0.08862 98  LYS A CA  
679  C C   . LYS A 106 ? 1.25447 0.61250 0.66556 0.07895  0.05903  -0.08662 98  LYS A C   
680  O O   . LYS A 106 ? 1.26133 0.62499 0.66650 0.09024  0.07194  -0.07370 98  LYS A O   
681  C CB  . LYS A 106 ? 1.42806 0.71458 0.84178 0.06099  0.05320  -0.09881 98  LYS A CB  
682  C CG  . LYS A 106 ? 1.47535 0.73110 0.91111 0.04009  0.04975  -0.10108 98  LYS A CG  
683  C CD  . LYS A 106 ? 1.53094 0.73520 0.94982 0.04519  0.05145  -0.10731 98  LYS A CD  
684  C CE  . LYS A 106 ? 1.57809 0.75080 1.02215 0.02239  0.04751  -0.10876 98  LYS A CE  
685  N NZ  . LYS A 106 ? 1.58825 0.70664 1.01909 0.02843  0.05062  -0.11242 98  LYS A NZ  
686  N N   . ILE A 107 ? 1.23341 0.60737 0.63200 0.08231  0.04705  -0.09816 99  ILE A N   
687  C CA  . ILE A 107 ? 1.19754 0.59733 0.57700 0.10011  0.04851  -0.09724 99  ILE A CA  
688  C C   . ILE A 107 ? 1.18436 0.62121 0.58395 0.09866  0.05085  -0.08717 99  ILE A C   
689  O O   . ILE A 107 ? 1.21092 0.66442 0.59920 0.11364  0.05721  -0.08132 99  ILE A O   
690  C CB  . ILE A 107 ? 1.21502 0.62255 0.57637 0.10044  0.03612  -0.11135 99  ILE A CB  
691  C CG1 . ILE A 107 ? 1.23869 0.60944 0.57626 0.10586  0.03692  -0.12491 99  ILE A CG1 
692  C CG2 . ILE A 107 ? 1.18144 0.62283 0.53218 0.11394  0.03709  -0.10801 99  ILE A CG2 
693  C CD1 . ILE A 107 ? 1.21994 0.59852 0.53333 0.10680  0.02811  -0.14067 99  ILE A CD1 
694  N N   . ARG A 108 ? 1.19012 0.63973 0.62071 0.08160  0.04522  -0.08649 100 ARG A N   
695  C CA  . ARG A 108 ? 1.11631 0.59855 0.57249 0.07950  0.04874  -0.07963 100 ARG A CA  
696  C C   . ARG A 108 ? 1.18330 0.66095 0.63586 0.08668  0.06763  -0.06915 100 ARG A C   
697  O O   . ARG A 108 ? 1.20268 0.70091 0.64707 0.09826  0.07306  -0.06510 100 ARG A O   
698  C CB  . ARG A 108 ? 1.16230 0.65581 0.65818 0.06038  0.03967  -0.08177 100 ARG A CB  
699  C CG  . ARG A 108 ? 1.15483 0.67039 0.66008 0.05530  0.02006  -0.08665 100 ARG A CG  
700  C CD  . ARG A 108 ? 1.16433 0.69397 0.71462 0.03818  0.00890  -0.08700 100 ARG A CD  
701  N NE  . ARG A 108 ? 1.22278 0.73577 0.77266 0.02414  -0.00769 -0.09329 100 ARG A NE  
702  C CZ  . ARG A 108 ? 1.27773 0.78346 0.85904 0.00797  -0.01219 -0.09455 100 ARG A CZ  
703  N NH1 . ARG A 108 ? 1.21142 0.72692 0.82997 0.00350  0.00090  -0.08936 100 ARG A NH1 
704  N NH2 . ARG A 108 ? 1.37646 0.86680 0.95209 -0.00464 -0.02989 -0.10182 100 ARG A NH2 
705  N N   . ARG A 109 ? 1.20876 0.65978 0.66559 0.07898  0.07631  -0.06444 101 ARG A N   
706  C CA  . ARG A 109 ? 1.15228 0.59677 0.60506 0.08156  0.09484  -0.05141 101 ARG A CA  
707  C C   . ARG A 109 ? 1.13444 0.57148 0.55077 0.10209  0.09977  -0.04486 101 ARG A C   
708  O O   . ARG A 109 ? 1.17886 0.63355 0.58799 0.10889  0.10935  -0.03683 101 ARG A O   
709  C CB  . ARG A 109 ? 1.15535 0.56893 0.62004 0.06718  0.10094  -0.04644 101 ARG A CB  
710  C CG  . ARG A 109 ? 1.17711 0.60578 0.68507 0.04656  0.09892  -0.05016 101 ARG A CG  
711  C CD  . ARG A 109 ? 1.16129 0.56316 0.68640 0.02997  0.10598  -0.04407 101 ARG A CD  
712  N NE  . ARG A 109 ? 1.23542 0.65929 0.80783 0.01122  0.10356  -0.04801 101 ARG A NE  
713  C CZ  . ARG A 109 ? 1.27991 0.73446 0.87980 0.00622  0.11752  -0.04355 101 ARG A CZ  
714  N NH1 . ARG A 109 ? 1.24195 0.70812 0.82173 0.01722  0.13505  -0.03526 101 ARG A NH1 
715  N NH2 . ARG A 109 ? 1.27923 0.75403 0.92775 -0.00973 0.11357  -0.04842 101 ARG A NH2 
716  N N   . ASN A 110 ? 1.14167 0.55536 0.53702 0.11186  0.09301  -0.04942 102 ASN A N   
717  C CA  . ASN A 110 ? 1.16659 0.57516 0.53288 0.13331  0.09555  -0.04419 102 ASN A CA  
718  C C   . ASN A 110 ? 1.16576 0.61427 0.52913 0.14264  0.09207  -0.04618 102 ASN A C   
719  O O   . ASN A 110 ? 1.19699 0.65554 0.54731 0.15365  0.09838  -0.03638 102 ASN A O   
720  C CB  . ASN A 110 ? 1.16530 0.54558 0.51631 0.14226  0.08917  -0.05328 102 ASN A CB  
721  C CG  . ASN A 110 ? 1.35562 0.69029 0.70484 0.13875  0.09407  -0.04818 102 ASN A CG  
722  O OD1 . ASN A 110 ? 1.35658 0.67936 0.70406 0.13862  0.10397  -0.03160 102 ASN A OD1 
723  N ND2 . ASN A 110 ? 1.42984 0.73791 0.77815 0.13509  0.08699  -0.06220 102 ASN A ND2 
724  N N   . SER A 111 ? 1.16523 0.63496 0.54048 0.13700  0.08128  -0.05742 103 SER A N   
725  C CA  . SER A 111 ? 1.13971 0.64602 0.51682 0.14312  0.07565  -0.05993 103 SER A CA  
726  C C   . SER A 111 ? 1.12102 0.65013 0.51168 0.13979  0.08245  -0.05453 103 SER A C   
727  O O   . SER A 111 ? 1.08858 0.63903 0.47076 0.15030  0.08246  -0.05261 103 SER A O   
728  C CB  . SER A 111 ? 1.10877 0.62827 0.49768 0.13391  0.06225  -0.06991 103 SER A CB  
729  O OG  . SER A 111 ? 1.13060 0.63329 0.50046 0.13860  0.05747  -0.07717 103 SER A OG  
730  N N   . GLU A 112 ? 1.11809 0.64415 0.53036 0.12540  0.08827  -0.05360 104 GLU A N   
731  C CA  . GLU A 112 ? 1.09574 0.64210 0.52166 0.12136  0.09870  -0.05094 104 GLU A CA  
732  C C   . GLU A 112 ? 1.12473 0.66604 0.52090 0.13291  0.11019  -0.04019 104 GLU A C   
733  O O   . GLU A 112 ? 1.14230 0.70696 0.53076 0.14080  0.11045  -0.04118 104 GLU A O   
734  C CB  . GLU A 112 ? 1.16176 0.70270 0.61645 0.10421  0.10602  -0.05097 104 GLU A CB  
735  C CG  . GLU A 112 ? 1.21193 0.76773 0.70355 0.09233  0.09355  -0.06068 104 GLU A CG  
736  C CD  . GLU A 112 ? 1.26573 0.81716 0.79121 0.07523  0.09891  -0.06076 104 GLU A CD  
737  O OE1 . GLU A 112 ? 1.34173 0.89275 0.87012 0.07160  0.11697  -0.05481 104 GLU A OE1 
738  O OE2 . GLU A 112 ? 1.22297 0.77291 0.77175 0.06474  0.08484  -0.06615 104 GLU A OE2 
739  N N   . ALA A 113 ? 1.13022 0.64096 0.51077 0.13314  0.11766  -0.02981 105 ALA A N   
740  C CA  . ALA A 113 ? 1.11800 0.61790 0.46844 0.14315  0.12685  -0.01513 105 ALA A CA  
741  C C   . ALA A 113 ? 1.14335 0.65243 0.47185 0.16243  0.11751  -0.01460 105 ALA A C   
742  O O   . ALA A 113 ? 1.19108 0.71292 0.50049 0.17034  0.12094  -0.00702 105 ALA A O   
743  C CB  . ALA A 113 ? 1.13925 0.59942 0.48217 0.13956  0.13239  -0.00384 105 ALA A CB  
744  N N   . ALA A 114 ? 1.14333 0.64808 0.47447 0.16896  0.10630  -0.02274 106 ALA A N   
745  C CA  . ALA A 114 ? 1.16225 0.67741 0.47874 0.18704  0.09808  -0.02335 106 ALA A CA  
746  C C   . ALA A 114 ? 1.12389 0.67840 0.44648 0.18855  0.09299  -0.02907 106 ALA A C   
747  O O   . ALA A 114 ? 1.04825 0.61624 0.35618 0.20174  0.09008  -0.02404 106 ALA A O   
748  C CB  . ALA A 114 ? 1.08299 0.58612 0.40284 0.19032  0.09067  -0.03303 106 ALA A CB  
749  N N   . MET A 115 ? 1.10483 0.67631 0.45092 0.17548  0.09037  -0.03907 107 MET A N   
750  C CA  . MET A 115 ? 1.06128 0.66696 0.41945 0.17506  0.08401  -0.04614 107 MET A CA  
751  C C   . MET A 115 ? 1.09159 0.70979 0.43972 0.17676  0.09169  -0.04266 107 MET A C   
752  O O   . MET A 115 ? 1.07053 0.70833 0.40906 0.18598  0.08606  -0.04297 107 MET A O   
753  C CB  . MET A 115 ? 1.00622 0.62201 0.39547 0.16040  0.07899  -0.05572 107 MET A CB  
754  C CG  . MET A 115 ? 0.99733 0.64337 0.40242 0.16014  0.06988  -0.06243 107 MET A CG  
755  S SD  . MET A 115 ? 0.91103 0.56633 0.35594 0.14408  0.06063  -0.07039 107 MET A SD  
756  C CE  . MET A 115 ? 0.90414 0.58865 0.36825 0.14462  0.05811  -0.07755 107 MET A CE  
757  N N   . LEU A 116 ? 1.05634 0.66470 0.40580 0.16745  0.10432  -0.03970 108 LEU A N   
758  C CA  . LEU A 116 ? 1.07068 0.68937 0.40422 0.16734  0.11502  -0.03638 108 LEU A CA  
759  C C   . LEU A 116 ? 1.09952 0.71315 0.39739 0.18193  0.11229  -0.02368 108 LEU A C   
760  O O   . LEU A 116 ? 1.11813 0.75258 0.40227 0.18665  0.11025  -0.02558 108 LEU A O   
761  C CB  . LEU A 116 ? 1.04819 0.65278 0.38622 0.15469  0.13153  -0.03163 108 LEU A CB  
762  C CG  . LEU A 116 ? 1.08809 0.70272 0.46631 0.14030  0.13506  -0.04393 108 LEU A CG  
763  C CD1 . LEU A 116 ? 1.12276 0.72337 0.50750 0.12769  0.15204  -0.03715 108 LEU A CD1 
764  C CD2 . LEU A 116 ? 1.06384 0.70971 0.45775 0.13949  0.13512  -0.05837 108 LEU A CD2 
765  N N   . GLN A 117 ? 1.07327 0.65992 0.35891 0.18902  0.11082  -0.01212 109 GLN A N   
766  C CA  . GLN A 117 ? 1.10036 0.67849 0.35753 0.20487  0.10622  0.00220  109 GLN A CA  
767  C C   . GLN A 117 ? 1.07868 0.68432 0.33686 0.21704  0.09239  -0.00399 109 GLN A C   
768  O O   . GLN A 117 ? 1.16685 0.78498 0.40449 0.22525  0.08833  0.00307  109 GLN A O   
769  C CB  . GLN A 117 ? 1.15024 0.69285 0.40510 0.21079  0.10587  0.01116  109 GLN A CB  
770  C CG  . GLN A 117 ? 1.15622 0.68586 0.38703 0.22794  0.10108  0.02795  109 GLN A CG  
771  C CD  . GLN A 117 ? 1.26332 0.76004 0.49896 0.23706  0.09860  0.03125  109 GLN A CD  
772  O OE1 . GLN A 117 ? 1.30994 0.81195 0.55012 0.25229  0.08981  0.02714  109 GLN A OE1 
773  N NE2 . GLN A 117 ? 1.26097 0.72375 0.49779 0.22743  0.10704  0.03741  109 GLN A NE2 
774  N N   . GLU A 118 ? 1.10340 0.71895 0.38401 0.21711  0.08488  -0.01565 110 GLU A N   
775  C CA  . GLU A 118 ? 1.10173 0.74417 0.38806 0.22718  0.07253  -0.02057 110 GLU A CA  
776  C C   . GLU A 118 ? 1.12371 0.79646 0.41559 0.22098  0.06892  -0.02915 110 GLU A C   
777  O O   . GLU A 118 ? 1.17159 0.86501 0.45685 0.22963  0.05998  -0.02750 110 GLU A O   
778  C CB  . GLU A 118 ? 1.00601 0.64954 0.31197 0.22634  0.06784  -0.02915 110 GLU A CB  
779  C CG  . GLU A 118 ? 1.06551 0.68010 0.36465 0.23466  0.07067  -0.02468 110 GLU A CG  
780  C CD  . GLU A 118 ? 1.11529 0.73921 0.42289 0.24291  0.06524  -0.03131 110 GLU A CD  
781  O OE1 . GLU A 118 ? 1.08226 0.73464 0.40342 0.23846  0.05921  -0.03834 110 GLU A OE1 
782  O OE2 . GLU A 118 ? 1.06169 0.66395 0.36292 0.25347  0.06780  -0.02964 110 GLU A OE2 
783  N N   . LEU A 119 ? 1.03375 0.70948 0.34119 0.20656  0.07481  -0.03877 111 LEU A N   
784  C CA  . LEU A 119 ? 1.10401 0.80475 0.42035 0.20021  0.07296  -0.05033 111 LEU A CA  
785  C C   . LEU A 119 ? 1.09201 0.79715 0.38046 0.20262  0.07807  -0.04540 111 LEU A C   
786  O O   . LEU A 119 ? 1.06622 0.79710 0.35928 0.20290  0.06903  -0.05097 111 LEU A O   
787  C CB  . LEU A 119 ? 1.06862 0.76831 0.41285 0.18571  0.07940  -0.06118 111 LEU A CB  
788  C CG  . LEU A 119 ? 1.01984 0.72251 0.39467 0.18036  0.07010  -0.06672 111 LEU A CG  
789  C CD1 . LEU A 119 ? 0.98383 0.68705 0.38899 0.16697  0.07445  -0.07606 111 LEU A CD1 
790  C CD2 . LEU A 119 ? 0.98979 0.71591 0.37431 0.18435  0.05605  -0.07102 111 LEU A CD2 
791  N N   . ASN A 120 ? 1.06762 0.75025 0.33291 0.20154  0.09090  -0.03440 112 ASN A N   
792  C CA  . ASN A 120 ? 1.10740 0.79381 0.34508 0.20043  0.09704  -0.02631 112 ASN A CA  
793  C C   . ASN A 120 ? 1.16032 0.85475 0.38350 0.21280  0.08243  -0.01371 112 ASN A C   
794  O O   . ASN A 120 ? 1.16615 0.87962 0.37659 0.21082  0.07855  -0.01313 112 ASN A O   
795  C CB  . ASN A 120 ? 1.10930 0.76757 0.32590 0.19493  0.11506  -0.01412 112 ASN A CB  
796  C CG  . ASN A 120 ? 1.09799 0.75926 0.33838 0.17941  0.13017  -0.02658 112 ASN A CG  
797  O OD1 . ASN A 120 ? 1.07872 0.76267 0.33596 0.17459  0.13057  -0.04459 112 ASN A OD1 
798  N ND2 . ASN A 120 ? 1.11156 0.74994 0.35720 0.17153  0.14223  -0.01744 112 ASN A ND2 
799  N N   . PHE A 121 ? 1.14101 0.82163 0.36459 0.22557  0.07492  -0.00513 113 PHE A N   
800  C CA  . PHE A 121 ? 1.17516 0.86372 0.38866 0.24101  0.06057  0.00608  113 PHE A CA  
801  C C   . PHE A 121 ? 1.18045 0.90612 0.41780 0.24078  0.04630  -0.00683 113 PHE A C   
802  O O   . PHE A 121 ? 1.21867 0.96198 0.44629 0.24733  0.03456  -0.00148 113 PHE A O   
803  C CB  . PHE A 121 ? 1.17684 0.83858 0.38397 0.25664  0.05946  0.01615  113 PHE A CB  
804  C CG  . PHE A 121 ? 1.16262 0.82606 0.35572 0.27484  0.04731  0.03163  113 PHE A CG  
805  C CD1 . PHE A 121 ? 1.18122 0.82687 0.34332 0.27910  0.04797  0.05152  113 PHE A CD1 
806  C CD2 . PHE A 121 ? 1.11707 0.80190 0.32960 0.28730  0.03481  0.02764  113 PHE A CD2 
807  C CE1 . PHE A 121 ? 1.20676 0.85429 0.35894 0.29666  0.03411  0.06751  113 PHE A CE1 
808  C CE2 . PHE A 121 ? 1.14817 0.83749 0.35377 0.30506  0.02272  0.04186  113 PHE A CE2 
809  C CZ  . PHE A 121 ? 1.18531 0.85537 0.36137 0.31031  0.02119  0.06194  113 PHE A CZ  
810  N N   . GLY A 122 ? 1.07251 0.80835 0.33838 0.23318  0.04630  -0.02208 114 GLY A N   
811  C CA  . GLY A 122 ? 1.07426 0.84169 0.36182 0.23018  0.03431  -0.03467 114 GLY A CA  
812  C C   . GLY A 122 ? 1.13165 0.91658 0.41073 0.22199  0.03236  -0.04228 114 GLY A C   
813  O O   . GLY A 122 ? 1.09194 0.89932 0.36995 0.22581  0.01869  -0.04399 114 GLY A O   
814  N N   . ALA A 123 ? 1.12384 0.89922 0.39544 0.21128  0.04618  -0.04755 115 ALA A N   
815  C CA  . ALA A 123 ? 1.09718 0.88751 0.35797 0.20194  0.04922  -0.05829 115 ALA A CA  
816  C C   . ALA A 123 ? 1.09366 0.88813 0.32192 0.20625  0.04411  -0.04441 115 ALA A C   
817  O O   . ALA A 123 ? 1.16753 0.98253 0.38655 0.20147  0.03739  -0.05345 115 ALA A O   
818  C CB  . ALA A 123 ? 1.12673 0.90505 0.38738 0.19156  0.06862  -0.06597 115 ALA A CB  
819  N N   . TYR A 124 ? 1.10622 0.87984 0.31593 0.21506  0.04642  -0.02352 116 TYR A N   
820  C CA  . TYR A 124 ? 1.16243 0.93486 0.33928 0.22149  0.03974  -0.00515 116 TYR A CA  
821  C C   . TYR A 124 ? 1.14198 0.93820 0.32377 0.23107  0.01782  -0.00516 116 TYR A C   
822  O O   . TYR A 124 ? 1.17228 0.98447 0.33330 0.22833  0.00884  -0.00329 116 TYR A O   
823  C CB  . TYR A 124 ? 1.16901 0.90807 0.32919 0.23135  0.04605  0.01707  116 TYR A CB  
824  C CG  . TYR A 124 ? 1.22150 0.95536 0.35145 0.24165  0.03580  0.03968  116 TYR A CG  
825  C CD1 . TYR A 124 ? 1.25438 0.99046 0.35257 0.23236  0.03963  0.04902  116 TYR A CD1 
826  C CD2 . TYR A 124 ? 1.22624 0.95327 0.35889 0.26111  0.02230  0.05252  116 TYR A CD2 
827  C CE1 . TYR A 124 ? 1.29824 1.02915 0.36862 0.24091  0.02803  0.07240  116 TYR A CE1 
828  C CE2 . TYR A 124 ? 1.25859 0.97991 0.36646 0.27221  0.01081  0.07500  116 TYR A CE2 
829  C CZ  . TYR A 124 ? 1.29987 1.02260 0.37679 0.26142  0.01260  0.08597  116 TYR A CZ  
830  O OH  . TYR A 124 ? 1.34473 1.06194 0.39819 0.27126  -0.00095 0.11042  116 TYR A OH  
831  N N   . LEU A 125 ? 1.11634 0.91646 0.32376 0.24106  0.00972  -0.00764 117 LEU A N   
832  C CA  . LEU A 125 ? 1.11587 0.94070 0.33248 0.25173  -0.01035 -0.00741 117 LEU A CA  
833  C C   . LEU A 125 ? 1.08769 0.94018 0.31792 0.24022  -0.01828 -0.02814 117 LEU A C   
834  O O   . LEU A 125 ? 1.13104 1.00696 0.36366 0.24591  -0.03624 -0.02885 117 LEU A O   
835  C CB  . LEU A 125 ? 1.11436 0.93511 0.35307 0.26498  -0.01210 -0.00463 117 LEU A CB  
836  C CG  . LEU A 125 ? 1.09914 0.88954 0.32418 0.27946  -0.00541 0.01306  117 LEU A CG  
837  C CD1 . LEU A 125 ? 1.12197 0.91019 0.36814 0.28988  -0.00401 0.00965  117 LEU A CD1 
838  C CD2 . LEU A 125 ? 1.13884 0.92853 0.34016 0.29445  -0.01763 0.03276  117 LEU A CD2 
839  N N   . GLY A 126 ? 1.07269 0.92191 0.31255 0.22592  -0.00626 -0.04472 118 GLY A N   
840  C CA  . GLY A 126 ? 1.09741 0.96657 0.35045 0.21574  -0.01222 -0.06701 118 GLY A CA  
841  C C   . GLY A 126 ? 1.11734 0.99958 0.40026 0.22019  -0.02357 -0.07370 118 GLY A C   
842  O O   . GLY A 126 ? 1.13668 1.04122 0.42416 0.21924  -0.03923 -0.08367 118 GLY A O   
843  N N   . LEU A 127 ? 1.10068 0.97001 0.40152 0.22385  -0.01632 -0.06874 119 LEU A N   
844  C CA  . LEU A 127 ? 1.11094 0.99250 0.43709 0.22767  -0.02484 -0.07193 119 LEU A CA  
845  C C   . LEU A 127 ? 1.07549 0.96433 0.41862 0.21650  -0.02801 -0.09223 119 LEU A C   
846  O O   . LEU A 127 ? 1.10893 0.98357 0.45376 0.20771  -0.01677 -0.10232 119 LEU A O   
847  C CB  . LEU A 127 ? 1.05400 0.91693 0.38885 0.23234  -0.01409 -0.06219 119 LEU A CB  
848  C CG  . LEU A 127 ? 1.11016 0.96022 0.42862 0.24621  -0.01084 -0.04429 119 LEU A CG  
849  C CD1 . LEU A 127 ? 1.00522 0.83501 0.33163 0.24924  -0.00005 -0.03986 119 LEU A CD1 
850  C CD2 . LEU A 127 ? 1.06510 0.93813 0.38088 0.26070  -0.02616 -0.03668 119 LEU A CD2 
851  N N   . PRO A 128 ? 1.03070 0.94327 0.39915 0.21393  -0.04328 -0.09744 120 PRO A N   
852  C CA  . PRO A 128 ? 1.02179 0.94024 0.42094 0.20024  -0.04811 -0.11417 120 PRO A CA  
853  C C   . PRO A 128 ? 1.03012 0.93168 0.45372 0.19295  -0.03759 -0.11408 120 PRO A C   
854  O O   . PRO A 128 ? 1.07966 0.97423 0.51845 0.18351  -0.03540 -0.12839 120 PRO A O   
855  C CB  . PRO A 128 ? 1.04224 0.98900 0.46830 0.19871  -0.06605 -0.11255 120 PRO A CB  
856  C CG  . PRO A 128 ? 1.05527 1.01089 0.47310 0.21252  -0.06661 -0.09343 120 PRO A CG  
857  C CD  . PRO A 128 ? 1.02795 0.96370 0.40392 0.22293  -0.05668 -0.08651 120 PRO A CD  
858  N N   . ALA A 129 ? 1.01569 0.91118 0.44263 0.19782  -0.03198 -0.09908 121 ALA A N   
859  C CA  . ALA A 129 ? 0.99660 0.87622 0.44161 0.19109  -0.02383 -0.09656 121 ALA A CA  
860  C C   . ALA A 129 ? 1.00011 0.86452 0.42696 0.20001  -0.01322 -0.08292 121 ALA A C   
861  O O   . ALA A 129 ? 1.01025 0.88052 0.41999 0.21214  -0.01424 -0.07391 121 ALA A O   
862  C CB  . ALA A 129 ? 1.01490 0.90959 0.49569 0.18188  -0.03425 -0.09559 121 ALA A CB  
863  N N   . PHE A 130 ? 0.99609 0.84133 0.42947 0.19411  -0.00475 -0.08216 122 PHE A N   
864  C CA  . PHE A 130 ? 0.99034 0.81661 0.40959 0.19960  0.00505  -0.07250 122 PHE A CA  
865  C C   . PHE A 130 ? 0.97089 0.79305 0.41180 0.18932  0.00397  -0.07155 122 PHE A C   
866  O O   . PHE A 130 ? 0.96388 0.78191 0.42433 0.17811  0.00199  -0.07822 122 PHE A O   
867  C CB  . PHE A 130 ? 1.02619 0.82892 0.42290 0.20153  0.01706  -0.07291 122 PHE A CB  
868  C CG  . PHE A 130 ? 1.06174 0.84229 0.44041 0.20880  0.02604  -0.06302 122 PHE A CG  
869  C CD1 . PHE A 130 ? 1.03623 0.80037 0.42414 0.20204  0.03059  -0.06281 122 PHE A CD1 
870  C CD2 . PHE A 130 ? 1.00934 0.78426 0.36386 0.22179  0.02830  -0.05388 122 PHE A CD2 
871  C CE1 . PHE A 130 ? 1.02652 0.76784 0.39855 0.20799  0.03808  -0.05627 122 PHE A CE1 
872  C CE2 . PHE A 130 ? 1.04406 0.79508 0.38591 0.22859  0.03587  -0.04561 122 PHE A CE2 
873  C CZ  . PHE A 130 ? 1.03280 0.76614 0.38209 0.22174  0.04129  -0.04818 122 PHE A CZ  
874  N N   . LEU A 131 ? 0.98245 0.80660 0.42020 0.19321  0.00489  -0.06391 123 LEU A N   
875  C CA  . LEU A 131 ? 0.94070 0.76465 0.39269 0.18295  0.00245  -0.06121 123 LEU A CA  
876  C C   . LEU A 131 ? 0.95122 0.74735 0.39221 0.18021  0.01020  -0.06133 123 LEU A C   
877  O O   . LEU A 131 ? 1.01141 0.79178 0.43042 0.19038  0.01892  -0.05963 123 LEU A O   
878  C CB  . LEU A 131 ? 0.84347 0.68650 0.29417 0.18821  0.00174  -0.05481 123 LEU A CB  
879  C CG  . LEU A 131 ? 0.87930 0.75318 0.35286 0.18276  -0.00841 -0.05266 123 LEU A CG  
880  C CD1 . LEU A 131 ? 0.82461 0.72115 0.29579 0.19244  -0.00551 -0.04709 123 LEU A CD1 
881  C CD2 . LEU A 131 ? 0.86509 0.74164 0.36031 0.16532  -0.01607 -0.05007 123 LEU A CD2 
882  N N   . LEU A 132 ? 0.95097 0.74109 0.40941 0.16664  0.00548  -0.06264 124 LEU A N   
883  C CA  . LEU A 132 ? 0.95957 0.72681 0.41330 0.16060  0.00895  -0.06263 124 LEU A CA  
884  C C   . LEU A 132 ? 0.92692 0.70059 0.39208 0.14858  -0.00073 -0.05805 124 LEU A C   
885  O O   . LEU A 132 ? 0.92328 0.71093 0.41238 0.13986  -0.01103 -0.05592 124 LEU A O   
886  C CB  . LEU A 132 ? 0.93424 0.68863 0.40134 0.15502  0.01166  -0.06837 124 LEU A CB  
887  C CG  . LEU A 132 ? 0.96228 0.70810 0.41240 0.16435  0.02307  -0.07122 124 LEU A CG  
888  C CD1 . LEU A 132 ? 0.94814 0.71179 0.40579 0.16671  0.02057  -0.07664 124 LEU A CD1 
889  C CD2 . LEU A 132 ? 0.98189 0.70760 0.43599 0.15839  0.03128  -0.07395 124 LEU A CD2 
890  N N   . PRO A 133 ? 0.97621 0.73890 0.42359 0.14712  0.00155  -0.05628 125 PRO A N   
891  C CA  . PRO A 133 ? 0.94117 0.71042 0.39231 0.13449  -0.00802 -0.05075 125 PRO A CA  
892  C C   . PRO A 133 ? 0.91865 0.67576 0.38883 0.12039  -0.01822 -0.04987 125 PRO A C   
893  O O   . PRO A 133 ? 0.96031 0.69891 0.43239 0.12092  -0.01392 -0.05532 125 PRO A O   
894  C CB  . PRO A 133 ? 0.94453 0.70484 0.36445 0.14002  0.00017  -0.05302 125 PRO A CB  
895  C CG  . PRO A 133 ? 1.00727 0.74236 0.41594 0.14959  0.01014  -0.05978 125 PRO A CG  
896  C CD  . PRO A 133 ? 0.93349 0.67586 0.35480 0.15708  0.01275  -0.05969 125 PRO A CD  
897  N N   . LEU A 134 ? 0.86394 0.63281 0.35018 0.10787  -0.03198 -0.04156 126 LEU A N   
898  C CA  . LEU A 134 ? 0.91147 0.67107 0.41175 0.09350  -0.04554 -0.03709 126 LEU A CA  
899  C C   . LEU A 134 ? 0.97692 0.73906 0.44894 0.08585  -0.04992 -0.03058 126 LEU A C   
900  O O   . LEU A 134 ? 0.95920 0.73890 0.43350 0.07816  -0.05803 -0.01953 126 LEU A O   
901  C CB  . LEU A 134 ? 0.92847 0.69796 0.46943 0.08537  -0.05960 -0.03110 126 LEU A CB  
902  C CG  . LEU A 134 ? 0.92302 0.69024 0.49156 0.09214  -0.05446 -0.04115 126 LEU A CG  
903  C CD1 . LEU A 134 ? 0.92570 0.70041 0.53732 0.08449  -0.06917 -0.03735 126 LEU A CD1 
904  C CD2 . LEU A 134 ? 0.89268 0.64206 0.46358 0.09397  -0.04693 -0.04985 126 LEU A CD2 
905  N N   . ASN A 135 ? 1.01839 0.76330 0.46323 0.08773  -0.04360 -0.03792 127 ASN A N   
906  C CA  . ASN A 135 ? 0.93060 0.67495 0.33953 0.08293  -0.04343 -0.03776 127 ASN A CA  
907  C C   . ASN A 135 ? 0.97683 0.71343 0.38698 0.06546  -0.06150 -0.03221 127 ASN A C   
908  O O   . ASN A 135 ? 1.01946 0.76457 0.40468 0.05620  -0.06727 -0.02634 127 ASN A O   
909  C CB  . ASN A 135 ? 0.93938 0.66480 0.31909 0.09447  -0.02818 -0.05158 127 ASN A CB  
910  C CG  . ASN A 135 ? 0.99839 0.73120 0.37093 0.11279  -0.01157 -0.05602 127 ASN A CG  
911  O OD1 . ASN A 135 ? 1.07224 0.78669 0.43734 0.12444  -0.00090 -0.06447 127 ASN A OD1 
912  N ND2 . ASN A 135 ? 1.07949 0.83917 0.45581 0.11483  -0.01039 -0.04905 127 ASN A ND2 
913  N N   . GLN A 136 ? 0.92649 0.64878 0.36335 0.06114  -0.06942 -0.03433 128 GLN A N   
914  C CA  . GLN A 136 ? 0.96981 0.68204 0.41137 0.04579  -0.08755 -0.03120 128 GLN A CA  
915  C C   . GLN A 136 ? 0.96373 0.68088 0.45639 0.03941  -0.10257 -0.02282 128 GLN A C   
916  O O   . GLN A 136 ? 0.93969 0.66543 0.45858 0.04745  -0.09630 -0.02264 128 GLN A O   
917  C CB  . GLN A 136 ? 0.95075 0.63872 0.37682 0.04742  -0.08090 -0.04525 128 GLN A CB  
918  C CG  . GLN A 136 ? 0.99533 0.67203 0.43213 0.06173  -0.06220 -0.05494 128 GLN A CG  
919  C CD  . GLN A 136 ? 1.07361 0.72425 0.50027 0.06092  -0.05702 -0.06613 128 GLN A CD  
920  O OE1 . GLN A 136 ? 1.09408 0.73065 0.49553 0.07174  -0.04161 -0.07493 128 GLN A OE1 
921  N NE2 . GLN A 136 ? 1.08570 0.72939 0.53573 0.04788  -0.07087 -0.06536 128 GLN A NE2 
922  N N   . GLU A 137 ? 1.00165 0.71404 0.50861 0.02568  -0.12256 -0.01700 129 GLU A N   
923  C CA  . GLU A 137 ? 0.92159 0.63857 0.48289 0.01953  -0.13962 -0.00890 129 GLU A CA  
924  C C   . GLU A 137 ? 0.93092 0.64008 0.52559 0.02809  -0.12680 -0.02188 129 GLU A C   
925  O O   . GLU A 137 ? 0.98220 0.69954 0.61648 0.03328  -0.12521 -0.02182 129 GLU A O   
926  C CB  . GLU A 137 ? 0.92960 0.64411 0.49442 0.00287  -0.16568 0.00117  129 GLU A CB  
927  C CG  . GLU A 137 ? 0.91687 0.63789 0.54098 -0.00294 -0.18651 0.01226  129 GLU A CG  
928  C CD  . GLU A 137 ? 0.95117 0.67279 0.57904 -0.01981 -0.21695 0.02707  129 GLU A CD  
929  O OE1 . GLU A 137 ? 1.18503 0.90272 0.76311 -0.02866 -0.22205 0.02841  129 GLU A OE1 
930  O OE2 . GLU A 137 ? 1.03153 0.75775 0.71246 -0.02379 -0.23608 0.03672  129 GLU A OE2 
931  N N   . ASP A 138 ? 0.92805 0.62168 0.50709 0.02868  -0.11760 -0.03292 130 ASP A N   
932  C CA  . ASP A 138 ? 0.95137 0.63741 0.56002 0.03350  -0.10486 -0.04333 130 ASP A CA  
933  C C   . ASP A 138 ? 0.95945 0.64088 0.54518 0.04856  -0.07886 -0.05219 130 ASP A C   
934  O O   . ASP A 138 ? 1.00432 0.67072 0.55304 0.05194  -0.06829 -0.05814 130 ASP A O   
935  C CB  . ASP A 138 ? 0.97535 0.64643 0.58369 0.02347  -0.11090 -0.04818 130 ASP A CB  
936  C CG  . ASP A 138 ? 0.93968 0.60567 0.58254 0.02558  -0.09766 -0.05645 130 ASP A CG  
937  O OD1 . ASP A 138 ? 0.93408 0.61149 0.60912 0.03286  -0.08831 -0.05778 130 ASP A OD1 
938  O OD2 . ASP A 138 ? 1.03705 0.68791 0.67401 0.01913  -0.09625 -0.06209 130 ASP A OD2 
939  N N   . ASN A 139 ? 0.92754 0.62078 0.53495 0.05719  -0.07053 -0.05319 131 ASN A N   
940  C CA  . ASN A 139 ? 0.94093 0.63227 0.53313 0.07095  -0.04793 -0.06080 131 ASN A CA  
941  C C   . ASN A 139 ? 0.95437 0.64833 0.58474 0.07259  -0.03833 -0.06766 131 ASN A C   
942  O O   . ASN A 139 ? 0.92755 0.62932 0.55964 0.08201  -0.02615 -0.07240 131 ASN A O   
943  C CB  . ASN A 139 ? 0.90533 0.61069 0.48316 0.07909  -0.04621 -0.05760 131 ASN A CB  
944  C CG  . ASN A 139 ? 0.90994 0.61557 0.44863 0.07860  -0.04998 -0.05222 131 ASN A CG  
945  O OD1 . ASN A 139 ? 0.95252 0.64435 0.45911 0.08197  -0.04151 -0.05653 131 ASN A OD1 
946  N ND2 . ASN A 139 ? 0.95672 0.67788 0.49886 0.07429  -0.06167 -0.04317 131 ASN A ND2 
947  N N   . THR A 140 ? 0.91675 0.60605 0.57630 0.06328  -0.04335 -0.06891 132 THR A N   
948  C CA  . THR A 140 ? 0.84580 0.54147 0.54936 0.06284  -0.03397 -0.07580 132 THR A CA  
949  C C   . THR A 140 ? 0.89372 0.58157 0.57512 0.07057  -0.00810 -0.08222 132 THR A C   
950  O O   . THR A 140 ? 0.86074 0.55934 0.55538 0.07728  0.00509  -0.08869 132 THR A O   
951  C CB  . THR A 140 ? 0.88524 0.57909 0.62473 0.05007  -0.04624 -0.07432 132 THR A CB  
952  O OG1 . THR A 140 ? 0.93487 0.63706 0.69540 0.04331  -0.07221 -0.06597 132 THR A OG1 
953  C CG2 . THR A 140 ? 0.83858 0.54187 0.62619 0.04944  -0.03372 -0.08203 132 THR A CG2 
954  N N   . ASN A 141 ? 0.89914 0.56784 0.54759 0.06918  -0.00176 -0.08054 133 ASN A N   
955  C CA  . ASN A 141 ? 0.95197 0.60877 0.57764 0.07504  0.02101  -0.08265 133 ASN A CA  
956  C C   . ASN A 141 ? 0.91805 0.57947 0.51094 0.08915  0.03004  -0.08252 133 ASN A C   
957  O O   . ASN A 141 ? 0.98633 0.65099 0.57574 0.09459  0.04698  -0.08516 133 ASN A O   
958  C CB  . ASN A 141 ? 0.97524 0.60658 0.57614 0.07013  0.02248  -0.08031 133 ASN A CB  
959  C CG  . ASN A 141 ? 1.03198 0.65036 0.62656 0.07073  0.04376  -0.07973 133 ASN A CG  
960  O OD1 . ASN A 141 ? 1.04674 0.67815 0.66185 0.07123  0.05741  -0.08165 133 ASN A OD1 
961  N ND2 . ASN A 141 ? 1.06637 0.65854 0.63257 0.07021  0.04719  -0.07716 133 ASN A ND2 
962  N N   . LEU A 142 ? 0.91802 0.58181 0.48821 0.09397  0.01905  -0.07933 134 LEU A N   
963  C CA  . LEU A 142 ? 0.92724 0.60038 0.47300 0.10657  0.02369  -0.07883 134 LEU A CA  
964  C C   . LEU A 142 ? 0.94891 0.64104 0.52080 0.10879  0.02713  -0.08468 134 LEU A C   
965  O O   . LEU A 142 ? 0.93079 0.62644 0.48458 0.11764  0.03923  -0.08717 134 LEU A O   
966  C CB  . LEU A 142 ? 0.87831 0.55746 0.40980 0.10729  0.00933  -0.07443 134 LEU A CB  
967  C CG  . LEU A 142 ? 0.89043 0.58183 0.40074 0.11904  0.01215  -0.07310 134 LEU A CG  
968  C CD1 . LEU A 142 ? 0.97081 0.64845 0.44311 0.12979  0.02262  -0.07146 134 LEU A CD1 
969  C CD2 . LEU A 142 ? 0.93342 0.64015 0.44852 0.11527  -0.00292 -0.06841 134 LEU A CD2 
970  N N   . ALA A 143 ? 0.91130 0.61449 0.52443 0.10119  0.01584  -0.08724 135 ALA A N   
971  C CA  . ALA A 143 ? 0.91792 0.63753 0.56354 0.10303  0.01772  -0.09597 135 ALA A CA  
972  C C   . ALA A 143 ? 0.93027 0.64990 0.58260 0.10426  0.03868  -0.10437 135 ALA A C   
973  O O   . ALA A 143 ? 0.89232 0.62195 0.54094 0.11071  0.04883  -0.11300 135 ALA A O   
974  C CB  . ALA A 143 ? 0.85656 0.58390 0.54879 0.09484  -0.00040 -0.09513 135 ALA A CB  
975  N N   . ARG A 144 ? 0.90120 0.61066 0.56183 0.09713  0.04496  -0.10201 136 ARG A N   
976  C CA  . ARG A 144 ? 0.88337 0.59400 0.55371 0.09516  0.06656  -0.10763 136 ARG A CA  
977  C C   . ARG A 144 ? 0.93101 0.63453 0.55226 0.10327  0.08360  -0.10518 136 ARG A C   
978  O O   . ARG A 144 ? 0.99267 0.70694 0.61315 0.10619  0.09983  -0.11297 136 ARG A O   
979  C CB  . ARG A 144 ? 0.86471 0.56465 0.55386 0.08388  0.06657  -0.10284 136 ARG A CB  
980  C CG  . ARG A 144 ? 0.86856 0.58013 0.59803 0.07776  0.08284  -0.11007 136 ARG A CG  
981  C CD  . ARG A 144 ? 0.92016 0.62890 0.62226 0.07962  0.10988  -0.11019 136 ARG A CD  
982  N NE  . ARG A 144 ? 1.02900 0.71320 0.69204 0.07721  0.11426  -0.09791 136 ARG A NE  
983  C CZ  . ARG A 144 ? 1.13692 0.81271 0.76983 0.07787  0.13494  -0.09245 136 ARG A CZ  
984  N NH1 . ARG A 144 ? 1.01313 0.70548 0.64520 0.08022  0.15450  -0.09882 136 ARG A NH1 
985  N NH2 . ARG A 144 ? 1.28175 0.93150 0.88423 0.07599  0.13567  -0.08059 136 ARG A NH2 
986  N N   . VAL A 145 ? 0.92476 0.61138 0.50660 0.10715  0.07959  -0.09515 137 VAL A N   
987  C CA  . VAL A 145 ? 1.00377 0.68058 0.53936 0.11583  0.09232  -0.08922 137 VAL A CA  
988  C C   . VAL A 145 ? 0.98012 0.67395 0.50128 0.12565  0.09135  -0.09470 137 VAL A C   
989  O O   . VAL A 145 ? 1.10559 0.80211 0.60421 0.12976  0.10549  -0.09536 137 VAL A O   
990  C CB  . VAL A 145 ? 0.98652 0.64094 0.49136 0.11923  0.08615  -0.07893 137 VAL A CB  
991  C CG1 . VAL A 145 ? 0.97961 0.62499 0.44160 0.13060  0.09509  -0.07140 137 VAL A CG1 
992  C CG2 . VAL A 145 ? 0.98850 0.62335 0.50510 0.10839  0.08779  -0.07542 137 VAL A CG2 
993  N N   . LEU A 146 ? 0.94826 0.65340 0.48136 0.12793  0.07480  -0.09792 138 LEU A N   
994  C CA  . LEU A 146 ? 0.92285 0.64481 0.44825 0.13538  0.07093  -0.10429 138 LEU A CA  
995  C C   . LEU A 146 ? 0.96587 0.70178 0.51477 0.13296  0.08076  -0.11897 138 LEU A C   
996  O O   . LEU A 146 ? 1.00148 0.74585 0.52825 0.13872  0.08772  -0.12504 138 LEU A O   
997  C CB  . LEU A 146 ? 0.93522 0.66546 0.47568 0.13498  0.05109  -0.10299 138 LEU A CB  
998  C CG  . LEU A 146 ? 0.95687 0.70442 0.49688 0.14023  0.04447  -0.10966 138 LEU A CG  
999  C CD1 . LEU A 146 ? 0.94880 0.69743 0.44636 0.15048  0.04960  -0.10549 138 LEU A CD1 
1000 C CD2 . LEU A 146 ? 0.85948 0.61475 0.41905 0.13683  0.02558  -0.10567 138 LEU A CD2 
1001 N N   . THR A 147 ? 0.95425 0.69344 0.54722 0.12507  0.08058  -0.12534 139 THR A N   
1002 C CA  . THR A 147 ? 0.91954 0.67280 0.54387 0.12325  0.09193  -0.14200 139 THR A CA  
1003 C C   . THR A 147 ? 1.01760 0.77018 0.61380 0.12363  0.11667  -0.14362 139 THR A C   
1004 O O   . THR A 147 ? 1.05756 0.82291 0.64685 0.12690  0.12755  -0.15739 139 THR A O   
1005 C CB  . THR A 147 ? 0.92817 0.68466 0.60962 0.11545  0.08601  -0.14562 139 THR A CB  
1006 O OG1 . THR A 147 ? 0.93599 0.69189 0.63614 0.11433  0.06172  -0.14032 139 THR A OG1 
1007 C CG2 . THR A 147 ? 0.89871 0.67113 0.61961 0.11548  0.09797  -0.16483 139 THR A CG2 
1008 N N   . ASN A 148 ? 1.03420 0.77166 0.61354 0.11955  0.12479  -0.13005 140 ASN A N   
1009 C CA  . ASN A 148 ? 1.06277 0.79585 0.61116 0.11806  0.14780  -0.12547 140 ASN A CA  
1010 C C   . ASN A 148 ? 1.06952 0.80484 0.56726 0.12734  0.14969  -0.12404 140 ASN A C   
1011 O O   . ASN A 148 ? 1.08504 0.83152 0.56717 0.12723  0.16650  -0.13225 140 ASN A O   
1012 C CB  . ASN A 148 ? 1.17652 0.88749 0.71479 0.11221  0.15079  -0.10847 140 ASN A CB  
1013 C CG  . ASN A 148 ? 1.32576 1.02880 0.82955 0.10994  0.17259  -0.09906 140 ASN A CG  
1014 O OD1 . ASN A 148 ? 1.26663 0.98432 0.77570 0.10579  0.19216  -0.10696 140 ASN A OD1 
1015 N ND2 . ASN A 148 ? 1.24998 0.92965 0.71879 0.11251  0.16992  -0.08194 140 ASN A ND2 
1016 N N   . HIS A 149 ? 1.06497 0.79225 0.53920 0.13482  0.13284  -0.11469 141 HIS A N   
1017 C CA  . HIS A 149 ? 1.05562 0.78549 0.48480 0.14454  0.12952  -0.11055 141 HIS A CA  
1018 C C   . HIS A 149 ? 1.09985 0.85151 0.53364 0.14695  0.12753  -0.12918 141 HIS A C   
1019 O O   . HIS A 149 ? 1.22785 0.98561 0.62446 0.15072  0.13422  -0.13060 141 HIS A O   
1020 C CB  . HIS A 149 ? 0.97886 0.69948 0.39603 0.15184  0.11136  -0.09875 141 HIS A CB  
1021 C CG  . HIS A 149 ? 1.03466 0.76279 0.41749 0.16225  0.10392  -0.09545 141 HIS A CG  
1022 N ND1 . HIS A 149 ? 1.06349 0.78371 0.40424 0.16775  0.11126  -0.08353 141 HIS A ND1 
1023 C CD2 . HIS A 149 ? 1.04646 0.78978 0.43289 0.16753  0.08841  -0.10098 141 HIS A CD2 
1024 C CE1 . HIS A 149 ? 1.07238 0.80391 0.39286 0.17679  0.09950  -0.08253 141 HIS A CE1 
1025 N NE2 . HIS A 149 ? 1.07526 0.82169 0.42404 0.17642  0.08598  -0.09376 141 HIS A NE2 
1026 N N   . ILE A 150 ? 1.04593 0.80761 0.52290 0.14451  0.11724  -0.14261 142 ILE A N   
1027 C CA  . ILE A 150 ? 1.08017 0.85938 0.56865 0.14652  0.11240  -0.16256 142 ILE A CA  
1028 C C   . ILE A 150 ? 1.16727 0.95633 0.65339 0.14364  0.13458  -0.17919 142 ILE A C   
1029 O O   . ILE A 150 ? 1.28343 1.08380 0.74712 0.14683  0.13617  -0.19274 142 ILE A O   
1030 C CB  . ILE A 150 ? 1.04437 0.82748 0.58411 0.14386  0.09512  -0.16956 142 ILE A CB  
1031 C CG1 . ILE A 150 ? 1.06313 0.84361 0.59450 0.14711  0.07417  -0.15635 142 ILE A CG1 
1032 C CG2 . ILE A 150 ? 1.07608 0.87305 0.64245 0.14375  0.09530  -0.19384 142 ILE A CG2 
1033 C CD1 . ILE A 150 ? 0.98598 0.76711 0.56217 0.14230  0.05697  -0.15567 142 ILE A CD1 
1034 N N   . HIS A 151 ? 1.07302 0.85937 0.58007 0.13725  0.15149  -0.17861 143 HIS A N   
1035 C CA  . HIS A 151 ? 1.06730 0.86602 0.57762 0.13333  0.17703  -0.19435 143 HIS A CA  
1036 C C   . HIS A 151 ? 1.18122 0.97440 0.63739 0.13127  0.19575  -0.17983 143 HIS A C   
1037 O O   . HIS A 151 ? 1.18246 0.98140 0.64507 0.12442  0.21975  -0.18295 143 HIS A O   
1038 C CB  . HIS A 151 ? 0.99744 0.80029 0.56910 0.12703  0.18447  -0.20149 143 HIS A CB  
1039 C CG  . HIS A 151 ? 1.04247 0.85074 0.66804 0.12911  0.16620  -0.21516 143 HIS A CG  
1040 N ND1 . HIS A 151 ? 1.05499 0.85266 0.69814 0.12928  0.14103  -0.20207 143 HIS A ND1 
1041 C CD2 . HIS A 151 ? 1.09693 0.91896 0.76282 0.13096  0.16919  -0.24003 143 HIS A CD2 
1042 C CE1 . HIS A 151 ? 1.08089 0.88499 0.77226 0.13023  0.12822  -0.21537 143 HIS A CE1 
1043 N NE2 . HIS A 151 ? 1.10709 0.92496 0.81564 0.13199  0.14455  -0.23936 143 HIS A NE2 
1044 N N   . THR A 152 ? 1.24241 1.02590 0.64976 0.13686  0.18507  -0.16370 144 THR A N   
1045 C CA  . THR A 152 ? 1.30565 1.08162 0.65591 0.13648  0.19768  -0.14641 144 THR A CA  
1046 C C   . THR A 152 ? 1.52487 1.31352 0.83112 0.14219  0.19311  -0.15527 144 THR A C   
1047 O O   . THR A 152 ? 1.60568 1.39139 0.88783 0.14716  0.17467  -0.13969 144 THR A O   
1048 C CB  . THR A 152 ? 1.25968 1.01159 0.59701 0.13881  0.18739  -0.11930 144 THR A CB  
1049 O OG1 . THR A 152 ? 1.28102 1.02351 0.65548 0.13031  0.19616  -0.11499 144 THR A OG1 
1050 C CG2 . THR A 152 ? 1.35750 1.09763 0.63784 0.14103  0.19332  -0.09801 144 THR A CG2 
1051 N N   . GLY A 153 ? 1.62440 1.43250 0.93398 0.13888  0.20639  -0.17982 145 GLY A N   
1052 C CA  . GLY A 153 ? 1.65875 1.49017 0.95265 0.13712  0.19605  -0.19274 145 GLY A CA  
1053 C C   . GLY A 153 ? 1.79236 1.62633 1.11329 0.14351  0.17285  -0.20857 145 GLY A C   
1054 O O   . GLY A 153 ? 1.78489 1.60414 1.11837 0.14996  0.15611  -0.19578 145 GLY A O   
1055 N N   . HIS A 154 ? 1.84843 1.69971 1.17749 0.14124  0.17243  -0.23606 146 HIS A N   
1056 C CA  . HIS A 154 ? 1.85590 1.70918 1.20878 0.14606  0.15020  -0.25311 146 HIS A CA  
1057 C C   . HIS A 154 ? 1.81099 1.66703 1.13735 0.14724  0.12618  -0.23472 146 HIS A C   
1058 O O   . HIS A 154 ? 1.90366 1.77363 1.20214 0.14188  0.12274  -0.24010 146 HIS A O   
1059 C CB  . HIS A 154 ? 1.83217 1.69979 1.19806 0.14222  0.15828  -0.28863 146 HIS A CB  
1060 C CG  . HIS A 154 ? 1.89921 1.76757 1.29843 0.14312  0.18256  -0.30949 146 HIS A CG  
1061 N ND1 . HIS A 154 ? 1.91228 1.79650 1.30383 0.13580  0.20663  -0.33113 146 HIS A ND1 
1062 C CD2 . HIS A 154 ? 1.85317 1.71290 1.30478 0.14607  0.18534  -0.30946 146 HIS A CD2 
1063 C CE1 . HIS A 154 ? 1.83464 1.71883 1.26689 0.14000  0.22580  -0.34726 146 HIS A CE1 
1064 N NE2 . HIS A 154 ? 1.77912 1.64969 1.25500 0.14377  0.21095  -0.33190 146 HIS A NE2 
1065 N N   . HIS A 155 ? 1.78844 1.63213 1.12283 0.15396  0.11084  -0.21446 147 HIS A N   
1066 C CA  . HIS A 155 ? 1.71026 1.55713 1.02567 0.15753  0.08955  -0.19484 147 HIS A CA  
1067 C C   . HIS A 155 ? 1.60735 1.45210 0.95116 0.16378  0.06889  -0.19917 147 HIS A C   
1068 O O   . HIS A 155 ? 1.63879 1.46978 1.00424 0.16733  0.06883  -0.19219 147 HIS A O   
1069 C CB  . HIS A 155 ? 1.67276 1.50805 0.96606 0.15976  0.09391  -0.16423 147 HIS A CB  
1070 C CG  . HIS A 155 ? 1.78625 1.62491 1.04610 0.15327  0.11070  -0.15788 147 HIS A CG  
1071 N ND1 . HIS A 155 ? 1.81134 1.63621 1.06449 0.15100  0.13046  -0.14619 147 HIS A ND1 
1072 C CD2 . HIS A 155 ? 1.78342 1.63756 1.01246 0.14746  0.11106  -0.16181 147 HIS A CD2 
1073 C CE1 . HIS A 155 ? 1.78413 1.61684 1.00406 0.14429  0.14269  -0.14167 147 HIS A CE1 
1074 N NE2 . HIS A 155 ? 1.77965 1.63080 0.98317 0.14179  0.13082  -0.15122 147 HIS A NE2 
1075 N N   . SER A 156 ? 1.52961 1.38784 0.87219 0.16381  0.05168  -0.21027 148 SER A N   
1076 C CA  . SER A 156 ? 1.44305 1.30318 0.81257 0.16787  0.03072  -0.21694 148 SER A CA  
1077 C C   . SER A 156 ? 1.42571 1.28525 0.79135 0.17365  0.01871  -0.18967 148 SER A C   
1078 O O   . SER A 156 ? 1.41643 1.28775 0.75970 0.17676  0.00761  -0.17977 148 SER A O   
1079 C CB  . SER A 156 ? 1.44232 1.31688 0.81004 0.16532  0.01664  -0.23907 148 SER A CB  
1080 O OG  . SER A 156 ? 1.49399 1.38204 0.82928 0.16451  0.00791  -0.22673 148 SER A OG  
1081 N N   . SER A 157 ? 1.33419 1.18269 0.72807 0.17279  0.02139  -0.17699 149 SER A N   
1082 C CA  . SER A 157 ? 1.22799 1.07540 0.62647 0.17746  0.01222  -0.15484 149 SER A CA  
1083 C C   . SER A 157 ? 1.12431 0.96782 0.56941 0.17088  0.00713  -0.15416 149 SER A C   
1084 O O   . SER A 157 ? 1.12449 0.95757 0.59033 0.16549  0.01666  -0.16168 149 SER A O   
1085 C CB  . SER A 157 ? 1.25795 1.09080 0.62587 0.18388  0.02440  -0.13639 149 SER A CB  
1086 O OG  . SER A 157 ? 1.28539 1.10410 0.65271 0.17915  0.04286  -0.14098 149 SER A OG  
1087 N N   . MET A 158 ? 1.12344 0.77941 0.49535 0.16765  0.05725  0.05241  150 MET A N   
1088 C CA  . MET A 158 ? 1.07219 0.76897 0.48887 0.15721  0.05780  0.04993  150 MET A CA  
1089 C C   . MET A 158 ? 1.06958 0.76156 0.49076 0.16442  0.06236  0.04811  150 MET A C   
1090 O O   . MET A 158 ? 1.07271 0.74934 0.47015 0.18182  0.05852  0.04919  150 MET A O   
1091 C CB  . MET A 158 ? 1.03032 0.77813 0.47115 0.15982  0.04299  0.04978  150 MET A CB  
1092 C CG  . MET A 158 ? 1.09464 0.85504 0.54340 0.14673  0.03970  0.04985  150 MET A CG  
1093 S SD  . MET A 158 ? 1.07251 0.82147 0.53896 0.12341  0.05387  0.04883  150 MET A SD  
1094 C CE  . MET A 158 ? 0.98604 0.76038 0.48410 0.12123  0.05564  0.04723  150 MET A CE  
1095 N N   . PHE A 159 ? 1.05118 0.75409 0.50027 0.15252  0.06893  0.04470  151 PHE A N   
1096 C CA  . PHE A 159 ? 1.01006 0.71289 0.46812 0.15734  0.07176  0.04127  151 PHE A CA  
1097 C C   . PHE A 159 ? 0.92775 0.67332 0.41655 0.15419  0.06454  0.04039  151 PHE A C   
1098 O O   . PHE A 159 ? 0.96276 0.71556 0.47191 0.14046  0.06696  0.03806  151 PHE A O   
1099 C CB  . PHE A 159 ? 0.97336 0.64152 0.43164 0.14646  0.08663  0.03567  151 PHE A CB  
1100 C CG  . PHE A 159 ? 1.05634 0.67638 0.47896 0.14774  0.09779  0.03686  151 PHE A CG  
1101 C CD1 . PHE A 159 ? 1.04191 0.63388 0.43243 0.16321  0.09843  0.03893  151 PHE A CD1 
1102 C CD2 . PHE A 159 ? 1.05889 0.65824 0.47576 0.13429  0.10818  0.03608  151 PHE A CD2 
1103 C CE1 . PHE A 159 ? 1.14428 0.68427 0.49385 0.16484  0.10959  0.04096  151 PHE A CE1 
1104 C CE2 . PHE A 159 ? 1.05151 0.60090 0.42889 0.13505  0.12073  0.03758  151 PHE A CE2 
1105 C CZ  . PHE A 159 ? 1.16657 0.68448 0.50832 0.15025  0.12144  0.04047  151 PHE A CZ  
1106 N N   . TRP A 160 ? 0.91479 0.68601 0.40477 0.16723  0.05627  0.04179  152 TRP A N   
1107 C CA  . TRP A 160 ? 0.93453 0.74232 0.44692 0.16576  0.05217  0.04110  152 TRP A CA  
1108 C C   . TRP A 160 ? 0.90962 0.70711 0.42479 0.16809  0.05584  0.03693  152 TRP A C   
1109 O O   . TRP A 160 ? 0.93479 0.72369 0.43753 0.18210  0.05579  0.03547  152 TRP A O   
1110 C CB  . TRP A 160 ? 0.88699 0.72621 0.40124 0.17858  0.04456  0.04194  152 TRP A CB  
1111 C CG  . TRP A 160 ? 0.92119 0.77792 0.43880 0.17532  0.03837  0.04354  152 TRP A CG  
1112 C CD1 . TRP A 160 ? 0.90523 0.75401 0.42361 0.16112  0.03941  0.04537  152 TRP A CD1 
1113 C CD2 . TRP A 160 ? 0.91234 0.80009 0.43580 0.18668  0.02934  0.04147  152 TRP A CD2 
1114 N NE1 . TRP A 160 ? 0.91747 0.78780 0.43899 0.16245  0.03118  0.04503  152 TRP A NE1 
1115 C CE2 . TRP A 160 ? 0.89899 0.79526 0.42584 0.17792  0.02431  0.04196  152 TRP A CE2 
1116 C CE3 . TRP A 160 ? 0.86610 0.77643 0.39445 0.20384  0.02472  0.03765  152 TRP A CE3 
1117 C CZ2 . TRP A 160 ? 0.92802 0.85596 0.46475 0.18533  0.01356  0.03783  152 TRP A CZ2 
1118 C CZ3 . TRP A 160 ? 0.86787 0.81127 0.40831 0.21183  0.01479  0.03326  152 TRP A CZ3 
1119 C CH2 . TRP A 160 ? 0.90953 0.86236 0.45500 0.20243  0.00865  0.03292  152 TRP A CH2 
1120 N N   . MET A 161 ? 0.86461 0.66140 0.39443 0.15608  0.05750  0.03416  153 MET A N   
1121 C CA  . MET A 161 ? 0.90351 0.69309 0.43766 0.15809  0.05776  0.02837  153 MET A CA  
1122 C C   . MET A 161 ? 0.88307 0.69936 0.41893 0.16465  0.05344  0.02998  153 MET A C   
1123 O O   . MET A 161 ? 0.85537 0.69086 0.39957 0.15685  0.05141  0.03302  153 MET A O   
1124 C CB  . MET A 161 ? 0.93901 0.71937 0.48893 0.14502  0.05800  0.02301  153 MET A CB  
1125 C CG  . MET A 161 ? 0.93677 0.69282 0.48894 0.13608  0.06566  0.01974  153 MET A CG  
1126 S SD  . MET A 161 ? 0.89313 0.61475 0.42468 0.14358  0.07533  0.01702  153 MET A SD  
1127 C CE  . MET A 161 ? 0.93179 0.64888 0.47138 0.14846  0.07292  0.00725  153 MET A CE  
1128 N N   . ARG A 162 ? 0.90839 0.72315 0.43441 0.17823  0.05370  0.02781  154 ARG A N   
1129 C CA  . ARG A 162 ? 0.90104 0.73841 0.42607 0.18576  0.05264  0.02796  154 ARG A CA  
1130 C C   . ARG A 162 ? 0.87586 0.70531 0.40132 0.18096  0.05048  0.02403  154 ARG A C   
1131 O O   . ARG A 162 ? 0.89621 0.70418 0.41710 0.18509  0.04932  0.01749  154 ARG A O   
1132 C CB  . ARG A 162 ? 0.89770 0.73286 0.41107 0.20344  0.05367  0.02580  154 ARG A CB  
1133 C CG  . ARG A 162 ? 0.89381 0.75868 0.40908 0.21212  0.05502  0.02565  154 ARG A CG  
1134 C CD  . ARG A 162 ? 0.95493 0.82325 0.46303 0.23115  0.05460  0.02349  154 ARG A CD  
1135 N NE  . ARG A 162 ? 0.95734 0.85753 0.47210 0.23942  0.05775  0.02111  154 ARG A NE  
1136 C CZ  . ARG A 162 ? 0.99516 0.91116 0.51144 0.25673  0.05677  0.01779  154 ARG A CZ  
1137 N NH1 . ARG A 162 ? 1.03498 0.93343 0.54098 0.26924  0.05090  0.01776  154 ARG A NH1 
1138 N NH2 . ARG A 162 ? 0.90913 0.85681 0.43594 0.26204  0.06218  0.01385  154 ARG A NH2 
1139 N N   . VAL A 163 ? 0.86826 0.71163 0.39728 0.17252  0.04937  0.02723  155 VAL A N   
1140 C CA  . VAL A 163 ? 0.86995 0.70313 0.39332 0.16951  0.04480  0.02429  155 VAL A CA  
1141 C C   . VAL A 163 ? 0.91540 0.76430 0.42656 0.17233  0.04898  0.02776  155 VAL A C   
1142 O O   . VAL A 163 ? 0.85771 0.72846 0.37384 0.16726  0.05487  0.03307  155 VAL A O   
1143 C CB  . VAL A 163 ? 0.87683 0.70284 0.40948 0.15679  0.04012  0.02492  155 VAL A CB  
1144 C CG1 . VAL A 163 ? 0.95652 0.76476 0.48388 0.15796  0.03103  0.01843  155 VAL A CG1 
1145 C CG2 . VAL A 163 ? 0.92565 0.74358 0.47268 0.15087  0.04134  0.02327  155 VAL A CG2 
1146 N N   . PRO A 164 ? 0.94666 0.78407 0.44109 0.17975  0.04711  0.02376  156 PRO A N   
1147 C CA  . PRO A 164 ? 0.89734 0.74390 0.37508 0.18118  0.05395  0.02672  156 PRO A CA  
1148 C C   . PRO A 164 ? 0.92939 0.76421 0.39443 0.17119  0.05131  0.03060  156 PRO A C   
1149 O O   . PRO A 164 ? 0.95710 0.77091 0.42018 0.17009  0.03985  0.02727  156 PRO A O   
1150 C CB  . PRO A 164 ? 0.94603 0.77838 0.40685 0.19469  0.05214  0.01995  156 PRO A CB  
1151 C CG  . PRO A 164 ? 0.94633 0.75470 0.41222 0.19543  0.03977  0.01279  156 PRO A CG  
1152 C CD  . PRO A 164 ? 0.89955 0.71337 0.38923 0.18659  0.03933  0.01501  156 PRO A CD  
1153 N N   . LEU A 165 ? 0.94775 0.79547 0.40495 0.16432  0.06226  0.03648  157 LEU A N   
1154 C CA  . LEU A 165 ? 0.94572 0.77648 0.38201 0.15506  0.06277  0.04146  157 LEU A CA  
1155 C C   . LEU A 165 ? 1.02903 0.82825 0.43255 0.16467  0.05484  0.03782  157 LEU A C   
1156 O O   . LEU A 165 ? 1.07755 0.85123 0.46430 0.16231  0.04486  0.03892  157 LEU A O   
1157 C CB  . LEU A 165 ? 0.94466 0.79563 0.37839 0.14562  0.08076  0.04664  157 LEU A CB  
1158 C CG  . LEU A 165 ? 0.95112 0.78790 0.36911 0.13116  0.08527  0.05340  157 LEU A CG  
1159 C CD1 . LEU A 165 ? 1.03630 0.85964 0.46453 0.12584  0.07108  0.05489  157 LEU A CD1 
1160 C CD2 . LEU A 165 ? 1.00231 0.86915 0.43497 0.11820  0.10367  0.05592  157 LEU A CD2 
1161 N N   . VAL A 166 ? 0.98912 0.78905 0.38308 0.17647  0.05777  0.03281  158 VAL A N   
1162 C CA  . VAL A 166 ? 1.02048 0.79107 0.38391 0.18830  0.04837  0.02676  158 VAL A CA  
1163 C C   . VAL A 166 ? 1.02395 0.79914 0.40235 0.19969  0.04319  0.01791  158 VAL A C   
1164 O O   . VAL A 166 ? 1.01187 0.81003 0.40371 0.20284  0.05461  0.01823  158 VAL A O   
1165 C CB  . VAL A 166 ? 1.05571 0.81614 0.38077 0.19007  0.06213  0.03002  158 VAL A CB  
1166 C CG1 . VAL A 166 ? 1.07800 0.80457 0.36584 0.20323  0.05115  0.02357  158 VAL A CG1 
1167 C CG2 . VAL A 166 ? 1.05632 0.80902 0.36448 0.17661  0.07129  0.03921  158 VAL A CG2 
1168 N N   . ALA A 167 ? 1.02236 0.77590 0.39900 0.20589  0.02632  0.00914  159 ALA A N   
1169 C CA  . ALA A 167 ? 1.01337 0.76417 0.40239 0.21487  0.02088  -0.00096 159 ALA A CA  
1170 C C   . ALA A 167 ? 1.06919 0.81715 0.43396 0.22650  0.02892  -0.00348 159 ALA A C   
1171 O O   . ALA A 167 ? 1.10012 0.83527 0.43155 0.22958  0.03163  -0.00160 159 ALA A O   
1172 C CB  . ALA A 167 ? 0.99889 0.72768 0.39148 0.21709  0.00135  -0.01203 159 ALA A CB  
1173 N N   . PRO A 168 ? 1.10151 0.85715 0.47849 0.23393  0.03349  -0.00809 160 PRO A N   
1174 C CA  . PRO A 168 ? 1.09801 0.85273 0.45410 0.24607  0.04235  -0.01107 160 PRO A CA  
1175 C C   . PRO A 168 ? 1.07419 0.79880 0.39602 0.25430  0.03246  -0.01914 160 PRO A C   
1176 O O   . PRO A 168 ? 1.11242 0.83306 0.40636 0.26165  0.04193  -0.01904 160 PRO A O   
1177 C CB  . PRO A 168 ? 1.02254 0.78192 0.39805 0.25306  0.04381  -0.01602 160 PRO A CB  
1178 C CG  . PRO A 168 ? 0.98733 0.75760 0.39328 0.24260  0.04187  -0.01163 160 PRO A CG  
1179 C CD  . PRO A 168 ? 1.05216 0.81311 0.45948 0.23170  0.03134  -0.01090 160 PRO A CD  
1180 N N   . GLU A 169 ? 1.07111 0.77602 0.39685 0.25314  0.01377  -0.02724 161 GLU A N   
1181 C CA  . GLU A 169 ? 1.10768 0.78247 0.40343 0.26163  -0.00194 -0.03761 161 GLU A CA  
1182 C C   . GLU A 169 ? 1.13934 0.79942 0.39478 0.26194  -0.00120 -0.03050 161 GLU A C   
1183 O O   . GLU A 169 ? 1.21388 0.84923 0.42973 0.27217  -0.00577 -0.03581 161 GLU A O   
1184 C CB  . GLU A 169 ? 1.09801 0.76264 0.41775 0.25839  -0.02273 -0.04917 161 GLU A CB  
1185 C CG  . GLU A 169 ? 1.17824 0.81433 0.47271 0.26820  -0.04338 -0.06304 161 GLU A CG  
1186 C CD  . GLU A 169 ? 1.24035 0.86341 0.51598 0.27947  -0.04208 -0.07268 161 GLU A CD  
1187 O OE1 . GLU A 169 ? 1.22993 0.86143 0.53056 0.27839  -0.03499 -0.07719 161 GLU A OE1 
1188 O OE2 . GLU A 169 ? 1.22599 0.82686 0.45823 0.28968  -0.04767 -0.07557 161 GLU A OE2 
1189 N N   . ASP A 170 ? 1.15208 0.82294 0.41382 0.25099  0.00482  -0.01917 162 ASP A N   
1190 C CA  . ASP A 170 ? 1.15848 0.80864 0.38084 0.24879  0.00501  -0.01165 162 ASP A CA  
1191 C C   . ASP A 170 ? 1.17012 0.83193 0.37391 0.24428  0.03195  -0.00101 162 ASP A C   
1192 O O   . ASP A 170 ? 1.20907 0.85327 0.38011 0.23906  0.03779  0.00690  162 ASP A O   
1193 C CB  . ASP A 170 ? 1.14024 0.79118 0.38044 0.23876  -0.00499 -0.00705 162 ASP A CB  
1194 C CG  . ASP A 170 ? 1.13817 0.78437 0.40673 0.24132  -0.02903 -0.01938 162 ASP A CG  
1195 O OD1 . ASP A 170 ? 1.16431 0.79117 0.41965 0.25246  -0.04523 -0.03208 162 ASP A OD1 
1196 O OD2 . ASP A 170 ? 1.23379 0.89623 0.53872 0.23166  -0.03082 -0.01748 162 ASP A OD2 
1197 N N   . LEU A 171 ? 1.15167 0.84094 0.37573 0.24614  0.04816  -0.00163 163 LEU A N   
1198 C CA  . LEU A 171 ? 1.16474 0.86981 0.37672 0.24362  0.07465  0.00412  163 LEU A CA  
1199 C C   . LEU A 171 ? 1.18088 0.88744 0.38285 0.25747  0.08245  -0.00398 163 LEU A C   
1200 O O   . LEU A 171 ? 1.18783 0.91394 0.38884 0.25706  0.10523  -0.00219 163 LEU A O   
1201 C CB  . LEU A 171 ? 1.12279 0.86875 0.37815 0.23169  0.08760  0.01082  163 LEU A CB  
1202 C CG  . LEU A 171 ? 1.08118 0.85449 0.38111 0.23578  0.08296  0.00680  163 LEU A CG  
1203 C CD1 . LEU A 171 ? 1.09975 0.89461 0.40642 0.24605  0.09794  0.00235  163 LEU A CD1 
1204 C CD2 . LEU A 171 ? 1.08574 0.88454 0.42175 0.22286  0.08380  0.01345  163 LEU A CD2 
1205 N N   . ARG A 172 ? 1.18890 0.87579 0.38476 0.26895  0.06493  -0.01393 164 ARG A N   
1206 C CA  . ARG A 172 ? 1.20903 0.89078 0.39140 0.28329  0.06990  -0.02293 164 ARG A CA  
1207 C C   . ARG A 172 ? 1.26244 0.92073 0.39146 0.28789  0.08282  -0.02252 164 ARG A C   
1208 O O   . ARG A 172 ? 1.33708 0.96684 0.43061 0.28376  0.07674  -0.01841 164 ARG A O   
1209 C CB  . ARG A 172 ? 1.21036 0.87131 0.39607 0.29177  0.04705  -0.03473 164 ARG A CB  
1210 C CG  . ARG A 172 ? 1.24563 0.86848 0.39609 0.29489  0.02607  -0.04046 164 ARG A CG  
1211 C CD  . ARG A 172 ? 1.24828 0.85794 0.41448 0.30044  0.00332  -0.05481 164 ARG A CD  
1212 N NE  . ARG A 172 ? 1.32223 0.89872 0.45851 0.30528  -0.02018 -0.06297 164 ARG A NE  
1213 C CZ  . ARG A 172 ? 1.40899 0.95356 0.49430 0.31707  -0.02578 -0.06925 164 ARG A CZ  
1214 N NH1 . ARG A 172 ? 1.39601 0.93791 0.45505 0.32426  -0.00691 -0.06829 164 ARG A NH1 
1215 N NH2 . ARG A 172 ? 1.36087 0.87536 0.42051 0.32279  -0.05107 -0.07744 164 ARG A NH2 
1216 N N   . ASP A 173 ? 1.31012 0.97763 0.43161 0.29676  0.10059  -0.02682 165 ASP A N   
1217 C CA  . ASP A 173 ? 1.33361 0.97697 0.40206 0.30236  0.11658  -0.02840 165 ASP A CA  
1218 C C   . ASP A 173 ? 1.37274 0.96998 0.40341 0.30979  0.09309  -0.03501 165 ASP A C   
1219 O O   . ASP A 173 ? 1.36265 0.95155 0.40028 0.31970  0.07279  -0.04476 165 ASP A O   
1220 C CB  . ASP A 173 ? 1.33715 1.00298 0.41537 0.31207  0.13752  -0.03466 165 ASP A CB  
1221 C CG  . ASP A 173 ? 1.33670 1.05181 0.45777 0.30421  0.16037  -0.03012 165 ASP A CG  
1222 O OD1 . ASP A 173 ? 1.37617 1.10412 0.51087 0.28865  0.16463  -0.02109 165 ASP A OD1 
1223 O OD2 . ASP A 173 ? 1.31566 1.05610 0.45741 0.31431  0.17263  -0.03678 165 ASP A OD2 
1224 N N   . ASP A 174 ? 1.41853 0.98599 0.41107 0.30488  0.09569  -0.03077 166 ASP A N   
1225 C CA  . ASP A 174 ? 1.46399 0.98532 0.41700 0.31288  0.07213  -0.03691 166 ASP A CA  
1226 C C   . ASP A 174 ? 1.49484 1.00506 0.43017 0.32502  0.07727  -0.04669 166 ASP A C   
1227 O O   . ASP A 174 ? 1.57638 1.05904 0.47234 0.32538  0.08531  -0.04543 166 ASP A O   
1228 C CB  . ASP A 174 ? 1.50573 0.99630 0.42207 0.30399  0.07350  -0.02752 166 ASP A CB  
1229 C CG  . ASP A 174 ? 1.57814 1.02101 0.45539 0.31403  0.04450  -0.03369 166 ASP A CG  
1230 O OD1 . ASP A 174 ? 1.55730 0.99523 0.44316 0.32566  0.01939  -0.04605 166 ASP A OD1 
1231 O OD2 . ASP A 174 ? 1.60062 1.01056 0.43873 0.31036  0.04710  -0.02705 166 ASP A OD2 
1232 N N   . ILE A 175 ? 1.46745 0.99534 0.42876 0.33462  0.07324  -0.05612 167 ILE A N   
1233 C CA  . ILE A 175 ? 1.48910 1.01396 0.44205 0.34633  0.08223  -0.06539 167 ILE A CA  
1234 C C   . ILE A 175 ? 1.49182 0.99726 0.44413 0.35847  0.05573  -0.07981 167 ILE A C   
1235 O O   . ILE A 175 ? 1.50753 1.00909 0.45533 0.36869  0.06088  -0.08841 167 ILE A O   
1236 C CB  . ILE A 175 ? 1.45781 1.02563 0.44487 0.34667  0.10926  -0.06345 167 ILE A CB  
1237 C CG1 . ILE A 175 ? 1.40211 0.99900 0.43223 0.34716  0.10246  -0.06349 167 ILE A CG1 
1238 C CG2 . ILE A 175 ? 1.46680 1.05134 0.45078 0.33438  0.13744  -0.05339 167 ILE A CG2 
1239 C CD1 . ILE A 175 ? 1.37606 1.01206 0.43887 0.35271  0.12360  -0.06415 167 ILE A CD1 
1240 N N   . ILE A 176 ? 1.47988 0.97325 0.43700 0.35720  0.02894  -0.08392 168 ILE A N   
1241 C CA  . ILE A 176 ? 1.49014 0.96121 0.44462 0.36663  0.00129  -0.10105 168 ILE A CA  
1242 C C   . ILE A 176 ? 1.63427 1.06585 0.54739 0.37092  -0.01929 -0.10566 168 ILE A C   
1243 O O   . ILE A 176 ? 1.62866 1.05051 0.53506 0.36623  -0.03401 -0.10137 168 ILE A O   
1244 C CB  . ILE A 176 ? 1.44525 0.93066 0.43740 0.36189  -0.01481 -0.10601 168 ILE A CB  
1245 C CG1 . ILE A 176 ? 1.48136 1.00661 0.52476 0.35537  0.00500  -0.09844 168 ILE A CG1 
1246 C CG2 . ILE A 176 ? 1.45617 0.92153 0.45566 0.36712  -0.04249 -0.12549 168 ILE A CG2 
1247 C CD1 . ILE A 176 ? 1.37327 0.92034 0.47032 0.34263  -0.00505 -0.09584 168 ILE A CD1 
1248 N N   . GLU A 177 ? 1.59848 1.00705 0.48462 0.38067  -0.02102 -0.11438 169 GLU A N   
1249 C CA  . GLU A 177 ? 1.64706 1.01515 0.48605 0.38690  -0.03555 -0.11747 169 GLU A CA  
1250 C C   . GLU A 177 ? 1.67339 1.02173 0.51124 0.39063  -0.07384 -0.12887 169 GLU A C   
1251 O O   . GLU A 177 ? 1.74322 1.06611 0.55050 0.39171  -0.08529 -0.12384 169 GLU A O   
1252 C CB  . GLU A 177 ? 1.68427 1.03588 0.50152 0.39718  -0.03021 -0.12689 169 GLU A CB  
1253 C CG  . GLU A 177 ? 1.78258 1.09033 0.55548 0.40668  -0.05364 -0.13582 169 GLU A CG  
1254 C CD  . GLU A 177 ? 1.86230 1.15809 0.64703 0.41408  -0.08950 -0.15633 169 GLU A CD  
1255 O OE1 . GLU A 177 ? 1.71692 1.03023 0.53449 0.41430  -0.08955 -0.16708 169 GLU A OE1 
1256 O OE2 . GLU A 177 ? 1.93016 1.19824 0.69200 0.41966  -0.11738 -0.16263 169 GLU A OE2 
1257 N N   . ASN A 178 ? 1.66331 1.02182 0.53375 0.39265  -0.09246 -0.14494 170 ASN A N   
1258 C CA  . ASN A 178 ? 1.63622 0.97980 0.51363 0.39711  -0.13101 -0.16267 170 ASN A CA  
1259 C C   . ASN A 178 ? 1.65520 1.02056 0.56772 0.38861  -0.13996 -0.16114 170 ASN A C   
1260 O O   . ASN A 178 ? 1.66861 1.03161 0.60231 0.39065  -0.16986 -0.17972 170 ASN A O   
1261 C CB  . ASN A 178 ? 1.67419 1.01289 0.56722 0.40277  -0.14575 -0.18576 170 ASN A CB  
1262 C CG  . ASN A 178 ? 1.70069 1.06565 0.63265 0.39677  -0.12756 -0.18882 170 ASN A CG  
1263 O OD1 . ASN A 178 ? 1.68232 1.07181 0.63005 0.38974  -0.10451 -0.17339 170 ASN A OD1 
1264 N ND2 . ASN A 178 ? 1.66692 1.02501 0.61458 0.39941  -0.13736 -0.20885 170 ASN A ND2 
1265 N N   . ALA A 179 ? 1.58848 0.97553 0.50975 0.37899  -0.11532 -0.14152 171 ALA A N   
1266 C CA  . ALA A 179 ? 1.57003 0.97700 0.52007 0.37017  -0.12013 -0.13655 171 ALA A CA  
1267 C C   . ALA A 179 ? 1.55871 0.97657 0.49893 0.36088  -0.09339 -0.11193 171 ALA A C   
1268 O O   . ALA A 179 ? 1.53854 0.98529 0.50085 0.35329  -0.06777 -0.10192 171 ALA A O   
1269 C CB  . ALA A 179 ? 1.57654 1.02002 0.59789 0.35909  -0.11430 -0.14111 171 ALA A CB  
1270 N N   . PRO A 180 ? 1.64590 1.03946 0.55303 0.36113  -0.09829 -0.10253 172 PRO A N   
1271 C CA  . PRO A 180 ? 1.61100 1.01005 0.50610 0.35037  -0.07075 -0.08137 172 PRO A CA  
1272 C C   . PRO A 180 ? 1.57445 0.99227 0.49576 0.33998  -0.07243 -0.07260 172 PRO A C   
1273 O O   . PRO A 180 ? 1.57403 0.98807 0.50914 0.34374  -0.10040 -0.08259 172 PRO A O   
1274 C CB  . PRO A 180 ? 1.61435 0.96997 0.45730 0.35614  -0.07705 -0.07803 172 PRO A CB  
1275 C CG  . PRO A 180 ? 1.63982 0.97042 0.47552 0.37002  -0.11786 -0.09603 172 PRO A CG  
1276 C CD  . PRO A 180 ? 1.65366 1.01129 0.53326 0.37195  -0.13050 -0.11297 172 PRO A CD  
1277 N N   . THR A 181 ? 1.58210 1.02094 0.51163 0.32719  -0.04284 -0.05593 173 THR A N   
1278 C CA  . THR A 181 ? 1.65021 1.10542 0.60038 0.31534  -0.03946 -0.04478 173 THR A CA  
1279 C C   . THR A 181 ? 1.83156 1.25024 0.74790 0.31567  -0.05356 -0.03945 173 THR A C   
1280 O O   . THR A 181 ? 1.96851 1.36302 0.84718 0.31385  -0.03879 -0.03155 173 THR A O   
1281 C CB  . THR A 181 ? 1.60047 1.08829 0.56849 0.30188  -0.00363 -0.03069 173 THR A CB  
1282 O OG1 . THR A 181 ? 1.57480 1.04624 0.50914 0.29763  0.01787  -0.02247 173 THR A OG1 
1283 C CG2 . THR A 181 ? 1.47706 0.99859 0.47699 0.30460  0.00913  -0.03607 173 THR A CG2 
1284 N N   . THR A 182 ? 1.87347 1.28643 0.80167 0.31886  -0.08107 -0.04488 174 THR A N   
1285 C CA  . THR A 182 ? 2.02614 1.40169 0.92436 0.32353  -0.10124 -0.04285 174 THR A CA  
1286 C C   . THR A 182 ? 2.13938 1.50398 1.01410 0.30995  -0.07403 -0.02316 174 THR A C   
1287 O O   . THR A 182 ? 2.07785 1.47296 0.98009 0.29547  -0.05370 -0.01290 174 THR A O   
1288 C CB  . THR A 182 ? 2.05712 1.43968 0.98413 0.32764  -0.13166 -0.05231 174 THR A CB  
1289 O OG1 . THR A 182 ? 1.83765 1.25865 0.80449 0.31475  -0.11638 -0.04571 174 THR A OG1 
1290 C CG2 . THR A 182 ? 2.05939 1.44146 1.00127 0.34220  -0.16403 -0.07608 174 THR A CG2 
1291 N N   . HIS A 183 ? 2.28171 1.60257 1.10639 0.31436  -0.07380 -0.01916 175 HIS A N   
1292 C CA  . HIS A 183 ? 2.27841 1.57872 1.07166 0.30139  -0.04780 -0.00247 175 HIS A CA  
1293 C C   . HIS A 183 ? 2.40476 1.67942 1.18727 0.30190  -0.06579 0.00204  175 HIS A C   
1294 O O   . HIS A 183 ? 2.47478 1.71213 1.21527 0.29703  -0.05396 0.01240  175 HIS A O   
1295 C CB  . HIS A 183 ? 2.40245 1.66303 1.14163 0.30606  -0.03627 -0.00097 175 HIS A CB  
1296 C CG  . HIS A 183 ? 2.49514 1.77048 1.23794 0.31182  -0.02808 -0.00937 175 HIS A CG  
1297 N ND1 . HIS A 183 ? 2.39686 1.72190 1.18311 0.30447  -0.00929 -0.01038 175 HIS A ND1 
1298 C CD2 . HIS A 183 ? 2.49087 1.73551 1.19717 0.32492  -0.03568 -0.01720 175 HIS A CD2 
1299 C CE1 . HIS A 183 ? 2.40008 1.72449 1.17744 0.31304  -0.00584 -0.01878 175 HIS A CE1 
1300 N NE2 . HIS A 183 ? 2.50212 1.77805 1.23073 0.32497  -0.02154 -0.02298 175 HIS A NE2 
1301 N N   . THR A 184 ? 2.18070 1.47224 0.99817 0.30803  -0.09301 -0.00641 176 THR A N   
1302 C CA  . THR A 184 ? 2.11159 1.38413 0.92704 0.31062  -0.11339 -0.00464 176 THR A CA  
1303 C C   . THR A 184 ? 2.05639 1.37020 0.91790 0.29559  -0.10216 0.00216  176 THR A C   
1304 O O   . THR A 184 ? 2.04147 1.39806 0.94036 0.28932  -0.09007 0.00001  176 THR A O   
1305 C CB  . THR A 184 ? 2.07103 1.32760 0.88949 0.33245  -0.15773 -0.02333 176 THR A CB  
1306 O OG1 . THR A 184 ? 2.05543 1.35316 0.92058 0.33527  -0.16854 -0.03734 176 THR A OG1 
1307 C CG2 . THR A 184 ? 2.00347 1.21297 0.77173 0.34866  -0.17173 -0.02975 176 THR A CG2 
1308 N N   . GLU A 185 ? 2.01177 1.31019 0.86804 0.29092  -0.10603 0.00988  177 GLU A N   
1309 C CA  . GLU A 185 ? 1.90462 1.23624 0.80032 0.27707  -0.09737 0.01674  177 GLU A CA  
1310 C C   . GLU A 185 ? 1.89049 1.23319 0.81849 0.28983  -0.13302 0.00257  177 GLU A C   
1311 O O   . GLU A 185 ? 1.92405 1.23366 0.83331 0.30497  -0.16195 -0.00522 177 GLU A O   
1312 C CB  . GLU A 185 ? 1.87396 1.18103 0.74512 0.26388  -0.08035 0.03231  177 GLU A CB  
1313 C CG  . GLU A 185 ? 1.83743 1.18202 0.74521 0.24430  -0.05895 0.04223  177 GLU A CG  
1314 C CD  . GLU A 185 ? 1.91071 1.23118 0.80350 0.23452  -0.05431 0.05313  177 GLU A CD  
1315 O OE1 . GLU A 185 ? 1.97717 1.24826 0.82334 0.23940  -0.05822 0.05636  177 GLU A OE1 
1316 O OE2 . GLU A 185 ? 1.87035 1.21871 0.79576 0.22236  -0.04650 0.05818  177 GLU A OE2 
1317 N N   . GLU A 186 ? 1.77423 1.16234 0.75157 0.28410  -0.13047 -0.00206 178 GLU A N   
1318 C CA  . GLU A 186 ? 1.64914 1.06609 0.69232 0.28597  -0.15374 -0.01606 178 GLU A CA  
1319 C C   . GLU A 186 ? 1.55827 1.00564 0.64427 0.26636  -0.13436 -0.00487 178 GLU A C   
1320 O O   . GLU A 186 ? 1.52951 1.01957 0.66138 0.25231  -0.11327 -0.00245 178 GLU A O   
1321 C CB  . GLU A 186 ? 1.61624 1.06759 0.70912 0.28878  -0.16069 -0.03309 178 GLU A CB  
1322 C CG  . GLU A 186 ? 1.79401 1.21671 0.85592 0.30993  -0.18974 -0.04994 178 GLU A CG  
1323 C CD  . GLU A 186 ? 1.84276 1.28344 0.91917 0.31123  -0.18380 -0.05976 178 GLU A CD  
1324 O OE1 . GLU A 186 ? 1.69901 1.18106 0.82778 0.29729  -0.16401 -0.05865 178 GLU A OE1 
1325 O OE2 . GLU A 186 ? 1.88377 1.29366 0.91547 0.32709  -0.19961 -0.06869 178 GLU A OE2 
1326 N N   . TYR A 187 ? 1.60965 1.03200 0.67659 0.26670  -0.14214 0.00152  179 TYR A N   
1327 C CA  . TYR A 187 ? 1.55073 0.99121 0.64454 0.24849  -0.12415 0.01349  179 TYR A CA  
1328 C C   . TYR A 187 ? 1.42207 0.91784 0.59703 0.23812  -0.12041 0.00524  179 TYR A C   
1329 O O   . TYR A 187 ? 1.36465 0.89099 0.56445 0.22078  -0.09404 0.01492  179 TYR A O   
1330 C CB  . TYR A 187 ? 1.52773 0.93013 0.59452 0.25611  -0.14296 0.01544  179 TYR A CB  
1331 C CG  . TYR A 187 ? 1.56280 0.97052 0.63819 0.23761  -0.12257 0.02985  179 TYR A CG  
1332 C CD1 . TYR A 187 ? 1.54924 0.92998 0.57308 0.22599  -0.09729 0.04748  179 TYR A CD1 
1333 C CD2 . TYR A 187 ? 1.49950 0.93862 0.63479 0.23057  -0.12701 0.02476  179 TYR A CD2 
1334 C CE1 . TYR A 187 ? 1.60157 0.98728 0.63479 0.20774  -0.07874 0.05908  179 TYR A CE1 
1335 C CE2 . TYR A 187 ? 1.40024 0.84303 0.54220 0.21370  -0.10925 0.03700  179 TYR A CE2 
1336 C CZ  . TYR A 187 ? 1.45257 0.86919 0.54428 0.20213  -0.08585 0.05396  179 TYR A CZ  
1337 O OH  . TYR A 187 ? 1.46147 0.88168 0.56099 0.18433  -0.06852 0.06449  179 TYR A OH  
1338 N N   . SER A 188 ? 1.43146 0.93815 0.64505 0.24864  -0.14583 -0.01325 180 SER A N   
1339 C CA  . SER A 188 ? 1.30290 0.85502 0.59086 0.23964  -0.14338 -0.02378 180 SER A CA  
1340 C C   . SER A 188 ? 1.26652 0.84462 0.57339 0.23522  -0.12871 -0.02665 180 SER A C   
1341 O O   . SER A 188 ? 1.22030 0.83156 0.56852 0.22133  -0.11035 -0.02353 180 SER A O   
1342 C CB  . SER A 188 ? 1.24429 0.79720 0.56581 0.25177  -0.17345 -0.04465 180 SER A CB  
1343 O OG  . SER A 188 ? 1.27430 0.80381 0.58035 0.25715  -0.18702 -0.04211 180 SER A OG  
1344 N N   . GLY A 189 ? 1.31315 0.87323 0.58696 0.24771  -0.13711 -0.03244 181 GLY A N   
1345 C CA  . GLY A 189 ? 1.22894 0.80667 0.51195 0.24642  -0.12460 -0.03568 181 GLY A CA  
1346 C C   . GLY A 189 ? 1.23183 0.83002 0.51496 0.23209  -0.09232 -0.01884 181 GLY A C   
1347 O O   . GLY A 189 ? 1.22725 0.85401 0.54623 0.22612  -0.08046 -0.02162 181 GLY A O   
1348 N N   . GLU A 190 ? 1.24726 0.83035 0.49202 0.22679  -0.07869 -0.00297 182 GLU A N   
1349 C CA  . GLU A 190 ? 1.23090 0.83440 0.47492 0.21324  -0.04821 0.01139  182 GLU A CA  
1350 C C   . GLU A 190 ? 1.23095 0.86700 0.52412 0.19833  -0.03845 0.01580  182 GLU A C   
1351 O O   . GLU A 190 ? 1.19305 0.85196 0.49489 0.18751  -0.01606 0.02506  182 GLU A O   
1352 C CB  . GLU A 190 ? 1.31510 0.88826 0.50175 0.21087  -0.03632 0.02439  182 GLU A CB  
1353 C CG  . GLU A 190 ? 1.40065 0.94002 0.53138 0.22446  -0.03982 0.02186  182 GLU A CG  
1354 C CD  . GLU A 190 ? 1.56462 1.05897 0.62804 0.22429  -0.03247 0.03302  182 GLU A CD  
1355 O OE1 . GLU A 190 ? 1.54303 1.03484 0.60475 0.21133  -0.02106 0.04378  182 GLU A OE1 
1356 O OE2 . GLU A 190 ? 1.57508 1.03347 0.58466 0.23686  -0.03757 0.03071  182 GLU A OE2 
1357 N N   . GLU A 191 ? 1.20856 0.84670 0.53259 0.19835  -0.05479 0.00817  183 GLU A N   
1358 C CA  . GLU A 191 ? 1.09287 0.75757 0.46211 0.18524  -0.04740 0.01038  183 GLU A CA  
1359 C C   . GLU A 191 ? 1.10796 0.79421 0.52397 0.18591  -0.05170 -0.00256 183 GLU A C   
1360 O O   . GLU A 191 ? 1.09812 0.80222 0.54951 0.17606  -0.04613 -0.00245 183 GLU A O   
1361 C CB  . GLU A 191 ? 1.11060 0.75876 0.47909 0.18388  -0.05984 0.01081  183 GLU A CB  
1362 C CG  . GLU A 191 ? 1.18354 0.80302 0.50237 0.18185  -0.05471 0.02390  183 GLU A CG  
1363 C CD  . GLU A 191 ? 1.18600 0.78281 0.49890 0.18322  -0.06907 0.02388  183 GLU A CD  
1364 O OE1 . GLU A 191 ? 1.12384 0.72271 0.46568 0.19124  -0.08907 0.01039  183 GLU A OE1 
1365 O OE2 . GLU A 191 ? 1.25293 0.82995 0.53367 0.17600  -0.05947 0.03632  183 GLU A OE2 
1366 N N   . LYS A 192 ? 1.08630 0.76812 0.50021 0.19624  -0.05988 -0.01359 184 LYS A N   
1367 C CA  . LYS A 192 ? 1.01907 0.71473 0.47425 0.19637  -0.06384 -0.02814 184 LYS A CA  
1368 C C   . LYS A 192 ? 0.97608 0.69606 0.45733 0.18495  -0.04304 -0.02122 184 LYS A C   
1369 O O   . LYS A 192 ? 0.95629 0.68522 0.47399 0.17950  -0.04246 -0.02981 184 LYS A O   
1370 C CB  . LYS A 192 ? 1.03336 0.71877 0.47463 0.20809  -0.07195 -0.03899 184 LYS A CB  
1371 C CG  . LYS A 192 ? 1.01743 0.70665 0.43402 0.21013  -0.05499 -0.03006 184 LYS A CG  
1372 C CD  . LYS A 192 ? 1.02270 0.70444 0.43511 0.21998  -0.06096 -0.04275 184 LYS A CD  
1373 C CE  . LYS A 192 ? 1.06119 0.71732 0.44877 0.23279  -0.08450 -0.05473 184 LYS A CE  
1374 N NZ  . LYS A 192 ? 1.09996 0.73463 0.43276 0.23935  -0.08371 -0.04362 184 LYS A NZ  
1375 N N   . THR A 193 ? 0.95920 0.68823 0.42155 0.18196  -0.02660 -0.00744 185 THR A N   
1376 C CA  . THR A 193 ? 0.91668 0.66803 0.39712 0.17446  -0.00902 -0.00046 185 THR A CA  
1377 C C   . THR A 193 ? 0.99173 0.75208 0.49771 0.16272  -0.00632 0.00261  185 THR A C   
1378 O O   . THR A 193 ? 0.90783 0.67970 0.43471 0.15786  0.00260  0.00268  185 THR A O   
1379 C CB  . THR A 193 ? 0.94430 0.70581 0.40123 0.17478  0.00522  0.01109  185 THR A CB  
1380 O OG1 . THR A 193 ? 0.92336 0.70518 0.39799 0.17299  0.01727  0.01367  185 THR A OG1 
1381 C CG2 . THR A 193 ? 1.02052 0.78237 0.46365 0.16614  0.01018  0.02173  185 THR A CG2 
1382 N N   . TRP A 194 ? 1.00994 0.76151 0.51022 0.15913  -0.01360 0.00513  186 TRP A N   
1383 C CA  . TRP A 194 ? 0.92106 0.67807 0.44329 0.14854  -0.01207 0.00712  186 TRP A CA  
1384 C C   . TRP A 194 ? 0.90160 0.65584 0.45651 0.14857  -0.02044 -0.00753 186 TRP A C   
1385 O O   . TRP A 194 ? 0.89910 0.66198 0.47753 0.13955  -0.01210 -0.00769 186 TRP A O   
1386 C CB  . TRP A 194 ? 0.95067 0.69500 0.45249 0.14580  -0.01691 0.01418  186 TRP A CB  
1387 C CG  . TRP A 194 ? 0.99275 0.74084 0.51528 0.13571  -0.01559 0.01555  186 TRP A CG  
1388 C CD1 . TRP A 194 ? 0.94825 0.70900 0.47414 0.12406  -0.00273 0.02547  186 TRP A CD1 
1389 C CD2 . TRP A 194 ? 0.93097 0.67122 0.47612 0.13675  -0.02769 0.00474  186 TRP A CD2 
1390 N NE1 . TRP A 194 ? 0.87509 0.63329 0.41989 0.11770  -0.00554 0.02270  186 TRP A NE1 
1391 C CE2 . TRP A 194 ? 0.86348 0.60990 0.42152 0.12537  -0.01994 0.00999  186 TRP A CE2 
1392 C CE3 . TRP A 194 ? 0.90718 0.63750 0.46530 0.14652  -0.04478 -0.01059 186 TRP A CE3 
1393 C CZ2 . TRP A 194 ? 0.87713 0.61903 0.45920 0.12371  -0.02700 0.00109  186 TRP A CZ2 
1394 C CZ3 . TRP A 194 ? 0.87978 0.60901 0.46607 0.14498  -0.05254 -0.02062 186 TRP A CZ3 
1395 C CH2 . TRP A 194 ? 0.86479 0.59928 0.46230 0.13377  -0.04283 -0.01446 186 TRP A CH2 
1396 N N   . MET A 195 ? 0.90231 0.64460 0.45867 0.15802  -0.03601 -0.02057 187 MET A N   
1397 C CA  . MET A 195 ? 0.88500 0.62747 0.47828 0.15784  -0.04428 -0.03876 187 MET A CA  
1398 C C   . MET A 195 ? 0.90284 0.65307 0.51539 0.15261  -0.02998 -0.04308 187 MET A C   
1399 O O   . MET A 195 ? 0.84959 0.60258 0.49540 0.14540  -0.02608 -0.05397 187 MET A O   
1400 C CB  . MET A 195 ? 0.90115 0.63093 0.49042 0.17066  -0.06605 -0.05347 187 MET A CB  
1401 C CG  . MET A 195 ? 0.92417 0.65726 0.55618 0.17047  -0.07810 -0.07434 187 MET A CG  
1402 S SD  . MET A 195 ? 1.27087 1.00249 0.91475 0.16844  -0.08635 -0.07365 187 MET A SD  
1403 C CE  . MET A 195 ? 1.05343 0.79493 0.75566 0.16978  -0.09933 -0.10346 187 MET A CE  
1404 N N   . TRP A 196 ? 0.87049 0.62167 0.46144 0.15647  -0.02165 -0.03555 188 TRP A N   
1405 C CA  . TRP A 196 ? 0.87318 0.62657 0.47194 0.15336  -0.00695 -0.03594 188 TRP A CA  
1406 C C   . TRP A 196 ? 0.90738 0.66719 0.51827 0.14227  0.00665  -0.02847 188 TRP A C   
1407 O O   . TRP A 196 ? 0.92957 0.68390 0.56116 0.13562  0.01481  -0.03648 188 TRP A O   
1408 C CB  . TRP A 196 ? 0.88110 0.63613 0.45095 0.16157  -0.00129 -0.02679 188 TRP A CB  
1409 C CG  . TRP A 196 ? 0.90603 0.65111 0.46047 0.17267  -0.01183 -0.03493 188 TRP A CG  
1410 C CD1 . TRP A 196 ? 0.93011 0.66518 0.49081 0.17715  -0.02869 -0.04902 188 TRP A CD1 
1411 C CD2 . TRP A 196 ? 0.90475 0.64871 0.43339 0.18199  -0.00718 -0.03041 188 TRP A CD2 
1412 N NE1 . TRP A 196 ? 0.92567 0.65116 0.46322 0.18818  -0.03509 -0.05316 188 TRP A NE1 
1413 C CE2 . TRP A 196 ? 0.92627 0.65666 0.44369 0.19101  -0.02093 -0.04167 188 TRP A CE2 
1414 C CE3 . TRP A 196 ? 0.93239 0.68616 0.44756 0.18472  0.00632  -0.01949 188 TRP A CE3 
1415 C CZ2 . TRP A 196 ? 0.94649 0.67074 0.43719 0.20158  -0.01950 -0.04136 188 TRP A CZ2 
1416 C CZ3 . TRP A 196 ? 0.96486 0.71534 0.45763 0.19571  0.00783  -0.01988 188 TRP A CZ3 
1417 C CH2 . TRP A 196 ? 0.94189 0.67674 0.42132 0.20353  -0.00393 -0.03021 188 TRP A CH2 
1418 N N   . TRP A 197 ? 0.87912 0.64814 0.47570 0.13977  0.00970  -0.01438 189 TRP A N   
1419 C CA  . TRP A 197 ? 0.84748 0.62297 0.45001 0.13018  0.02045  -0.00619 189 TRP A CA  
1420 C C   . TRP A 197 ? 0.85195 0.62285 0.47944 0.12174  0.01854  -0.01442 189 TRP A C   
1421 O O   . TRP A 197 ? 0.87460 0.64180 0.51438 0.11421  0.02964  -0.01639 189 TRP A O   
1422 C CB  . TRP A 197 ? 0.82231 0.61024 0.40629 0.12898  0.02212  0.00792  189 TRP A CB  
1423 C CG  . TRP A 197 ? 0.82522 0.61815 0.41698 0.11850  0.02758  0.01356  189 TRP A CG  
1424 C CD1 . TRP A 197 ? 0.82360 0.61606 0.41702 0.11217  0.02330  0.01620  189 TRP A CD1 
1425 C CD2 . TRP A 197 ? 0.80986 0.60461 0.40539 0.11389  0.03772  0.01652  189 TRP A CD2 
1426 N NE1 . TRP A 197 ? 0.88857 0.68493 0.48875 0.10312  0.03053  0.02021  189 TRP A NE1 
1427 C CE2 . TRP A 197 ? 0.88928 0.68675 0.48979 0.10424  0.03899  0.02047  189 TRP A CE2 
1428 C CE3 . TRP A 197 ? 0.86186 0.65217 0.45261 0.11799  0.04527  0.01634  189 TRP A CE3 
1429 C CZ2 . TRP A 197 ? 0.84470 0.64166 0.44533 0.09855  0.04699  0.02372  189 TRP A CZ2 
1430 C CZ3 . TRP A 197 ? 0.90971 0.69698 0.49794 0.11327  0.05283  0.02025  189 TRP A CZ3 
1431 C CH2 . TRP A 197 ? 0.85425 0.64538 0.44732 0.10364  0.05342  0.02366  189 TRP A CH2 
1432 N N   . HIS A 198 ? 0.81743 0.58631 0.44939 0.12390  0.00523  -0.01924 190 HIS A N   
1433 C CA  . HIS A 198 ? 0.83374 0.60020 0.49126 0.11834  0.00097  -0.02849 190 HIS A CA  
1434 C C   . HIS A 198 ? 0.85116 0.61455 0.54059 0.11477  0.00578  -0.04566 190 HIS A C   
1435 O O   . HIS A 198 ? 0.87102 0.63376 0.57970 0.10504  0.01663  -0.04935 190 HIS A O   
1436 C CB  . HIS A 198 ? 0.82499 0.58594 0.47687 0.12593  -0.01775 -0.03193 190 HIS A CB  
1437 C CG  . HIS A 198 ? 0.82149 0.58099 0.50132 0.12312  -0.02400 -0.04308 190 HIS A CG  
1438 N ND1 . HIS A 198 ? 0.81479 0.57453 0.49508 0.11539  -0.01841 -0.03568 190 HIS A ND1 
1439 C CD2 . HIS A 198 ? 0.82442 0.58382 0.53551 0.12725  -0.03523 -0.06275 190 HIS A CD2 
1440 C CE1 . HIS A 198 ? 0.81416 0.57280 0.52313 0.11567  -0.02537 -0.04957 190 HIS A CE1 
1441 N NE2 . HIS A 198 ? 0.81940 0.57954 0.54980 0.12305  -0.03601 -0.06695 190 HIS A NE2 
1442 N N   . ASN A 199 ? 0.83585 0.59608 0.52994 0.12140  -0.00065 -0.05657 191 ASN A N   
1443 C CA  . ASN A 199 ? 0.86221 0.61919 0.58910 0.11663  0.00451  -0.07573 191 ASN A CA  
1444 C C   . ASN A 199 ? 0.87745 0.62649 0.60087 0.10690  0.02766  -0.07047 191 ASN A C   
1445 O O   . ASN A 199 ? 0.87543 0.61980 0.62592 0.09657  0.03960  -0.08239 191 ASN A O   
1446 C CB  . ASN A 199 ? 0.88825 0.64228 0.61632 0.12585  -0.00800 -0.08800 191 ASN A CB  
1447 C CG  . ASN A 199 ? 0.84077 0.59826 0.58091 0.13517  -0.03224 -0.10070 191 ASN A CG  
1448 O OD1 . ASN A 199 ? 0.83714 0.59800 0.58302 0.13565  -0.03979 -0.09933 191 ASN A OD1 
1449 N ND2 . ASN A 199 ? 0.86413 0.61841 0.60625 0.14371  -0.04574 -0.11387 191 ASN A ND2 
1450 N N   . PHE A 200 ? 0.82015 0.56640 0.51061 0.11062  0.03399  -0.05409 192 PHE A N   
1451 C CA  . PHE A 200 ? 0.85642 0.59023 0.53368 0.10548  0.05291  -0.04738 192 PHE A CA  
1452 C C   . PHE A 200 ? 0.86976 0.60185 0.55108 0.09527  0.06349  -0.04243 192 PHE A C   
1453 O O   . PHE A 200 ? 0.89035 0.60770 0.58308 0.08576  0.07889  -0.05015 192 PHE A O   
1454 C CB  . PHE A 200 ? 0.83309 0.56857 0.47623 0.11518  0.05281  -0.03218 192 PHE A CB  
1455 C CG  . PHE A 200 ? 0.88292 0.60181 0.50803 0.11418  0.06824  -0.02626 192 PHE A CG  
1456 C CD1 . PHE A 200 ? 0.90637 0.60544 0.52732 0.11590  0.07595  -0.03361 192 PHE A CD1 
1457 C CD2 . PHE A 200 ? 0.92476 0.64433 0.53428 0.11210  0.07423  -0.01402 192 PHE A CD2 
1458 C CE1 . PHE A 200 ? 0.90041 0.57704 0.49789 0.11666  0.08965  -0.02757 192 PHE A CE1 
1459 C CE2 . PHE A 200 ? 0.95730 0.65678 0.54450 0.11384  0.08589  -0.00888 192 PHE A CE2 
1460 C CZ  . PHE A 200 ? 0.95004 0.62624 0.52927 0.11663  0.09375  -0.01505 192 PHE A CZ  
1461 N N   . ARG A 201 ? 0.82733 0.57172 0.49779 0.09637  0.05688  -0.03052 193 ARG A N   
1462 C CA  . ARG A 201 ? 0.85610 0.59893 0.52493 0.08764  0.06533  -0.02425 193 ARG A CA  
1463 C C   . ARG A 201 ? 0.89050 0.63018 0.59193 0.07866  0.06895  -0.03890 193 ARG A C   
1464 O O   . ARG A 201 ? 0.91494 0.64417 0.61730 0.06946  0.08332  -0.03898 193 ARG A O   
1465 C CB  . ARG A 201 ? 0.81263 0.57016 0.46509 0.09015  0.05641  -0.01038 193 ARG A CB  
1466 C CG  . ARG A 201 ? 0.86963 0.63627 0.53066 0.09328  0.04121  -0.01296 193 ARG A CG  
1467 C CD  . ARG A 201 ? 0.85790 0.62366 0.53557 0.08623  0.03967  -0.01709 193 ARG A CD  
1468 N NE  . ARG A 201 ? 0.80344 0.57281 0.47735 0.09130  0.02427  -0.01556 193 ARG A NE  
1469 C CZ  . ARG A 201 ? 0.85730 0.63051 0.50859 0.09104  0.02108  -0.00234 193 ARG A CZ  
1470 N NH1 . ARG A 201 ? 0.82937 0.60930 0.46551 0.08628  0.03035  0.00906  193 ARG A NH1 
1471 N NH2 . ARG A 201 ? 0.91646 0.68513 0.55952 0.09570  0.00842  -0.00155 193 ARG A NH2 
1472 N N   . THR A 202 ? 0.82323 0.57083 0.54991 0.08211  0.05623  -0.05207 194 THR A N   
1473 C CA  . THR A 202 ? 0.81752 0.56709 0.58329 0.07593  0.05703  -0.07023 194 THR A CA  
1474 C C   . THR A 202 ? 0.80440 0.54183 0.58971 0.06633  0.07627  -0.08423 194 THR A C   
1475 O O   . THR A 202 ? 0.80568 0.53882 0.61180 0.05584  0.09013  -0.09304 194 THR A O   
1476 C CB  . THR A 202 ? 0.79305 0.55382 0.57818 0.08562  0.03442  -0.08183 194 THR A CB  
1477 O OG1 . THR A 202 ? 0.89094 0.65543 0.65208 0.09211  0.02117  -0.06756 194 THR A OG1 
1478 C CG2 . THR A 202 ? 0.79110 0.55799 0.62238 0.08191  0.03256  -0.10400 194 THR A CG2 
1479 N N   . LEU A 203 ? 0.85264 0.58257 0.63016 0.06922  0.07859  -0.08667 195 LEU A N   
1480 C CA  . LEU A 203 ? 0.87136 0.58361 0.66108 0.05915  0.09911  -0.09916 195 LEU A CA  
1481 C C   . LEU A 203 ? 0.87849 0.56773 0.64047 0.05052  0.12219  -0.08752 195 LEU A C   
1482 O O   . LEU A 203 ? 0.85892 0.53175 0.63600 0.03755  0.14361  -0.09931 195 LEU A O   
1483 C CB  . LEU A 203 ? 0.84077 0.54665 0.61799 0.06627  0.09447  -0.10051 195 LEU A CB  
1484 C CG  . LEU A 203 ? 0.83761 0.55785 0.64780 0.07111  0.07716  -0.12004 195 LEU A CG  
1485 C CD1 . LEU A 203 ? 0.84800 0.56197 0.63477 0.08109  0.06937  -0.11653 195 LEU A CD1 
1486 C CD2 . LEU A 203 ? 0.84409 0.56288 0.70125 0.05771  0.08995  -0.14566 195 LEU A CD2 
1487 N N   . CYS A 204 ? 0.84307 0.53050 0.56581 0.05749  0.11806  -0.06653 196 CYS A N   
1488 C CA  . CYS A 204 ? 0.86022 0.52506 0.54835 0.05349  0.13432  -0.05375 196 CYS A CA  
1489 C C   . CYS A 204 ? 0.86558 0.53392 0.55995 0.04589  0.13849  -0.05216 196 CYS A C   
1490 O O   . CYS A 204 ? 0.97576 0.62424 0.64023 0.04262  0.15063  -0.04267 196 CYS A O   
1491 C CB  . CYS A 204 ? 0.86231 0.52854 0.51101 0.06608  0.12479  -0.03511 196 CYS A CB  
1492 S SG  . CYS A 204 ? 0.87756 0.53289 0.51102 0.07617  0.12329  -0.03583 196 CYS A SG  
1493 N N   . ASP A 205 ? 0.85270 0.54288 0.58115 0.04472  0.12749  -0.06123 197 ASP A N   
1494 C CA  . ASP A 205 ? 0.84063 0.53333 0.58366 0.03685  0.13261  -0.06479 197 ASP A CA  
1495 C C   . ASP A 205 ? 0.84407 0.54011 0.55516 0.04046  0.12493  -0.04593 197 ASP A C   
1496 O O   . ASP A 205 ? 0.83525 0.51847 0.53505 0.03310  0.13693  -0.04313 197 ASP A O   
1497 C CB  . ASP A 205 ? 0.88793 0.55660 0.63775 0.02303  0.16015  -0.07552 197 ASP A CB  
1498 C CG  . ASP A 205 ? 0.87757 0.55278 0.65936 0.01459  0.16672  -0.08798 197 ASP A CG  
1499 O OD1 . ASP A 205 ? 0.82503 0.52055 0.61837 0.02043  0.14855  -0.08597 197 ASP A OD1 
1500 O OD2 . ASP A 205 ? 0.94485 0.60295 0.73953 0.00215  0.19116  -0.10052 197 ASP A OD2 
1501 N N   . TYR A 206 ? 0.89319 0.60558 0.59099 0.05061  0.10644  -0.03487 198 TYR A N   
1502 C CA  . TYR A 206 ? 0.87875 0.60031 0.55315 0.05322  0.09728  -0.01928 198 TYR A CA  
1503 C C   . TYR A 206 ? 0.89157 0.59631 0.53450 0.05013  0.10919  -0.00984 198 TYR A C   
1504 O O   . TYR A 206 ? 0.98089 0.68328 0.61665 0.04462  0.11125  -0.00608 198 TYR A O   
1505 C CB  . TYR A 206 ? 0.82861 0.55899 0.52064 0.04940  0.09039  -0.02256 198 TYR A CB  
1506 C CG  . TYR A 206 ? 0.85098 0.59551 0.56234 0.05633  0.07302  -0.02822 198 TYR A CG  
1507 C CD1 . TYR A 206 ? 0.84177 0.58783 0.58595 0.05774  0.07085  -0.04566 198 TYR A CD1 
1508 C CD2 . TYR A 206 ? 0.87838 0.63283 0.57390 0.06151  0.05875  -0.01722 198 TYR A CD2 
1509 C CE1 . TYR A 206 ? 0.88256 0.63831 0.64008 0.06670  0.05172  -0.05163 198 TYR A CE1 
1510 C CE2 . TYR A 206 ? 0.92580 0.68565 0.63005 0.06910  0.04272  -0.02154 198 TYR A CE2 
1511 C CZ  . TYR A 206 ? 0.91270 0.67247 0.64641 0.07301  0.03753  -0.03862 198 TYR A CZ  
1512 O OH  . TYR A 206 ? 0.95945 0.72146 0.69755 0.08299  0.01869  -0.04359 198 TYR A OH  
1513 N N   . SER A 207 ? 0.90154 0.59219 0.52359 0.05474  0.11565  -0.00661 199 SER A N   
1514 C CA  . SER A 207 ? 0.87610 0.54660 0.46060 0.05635  0.12329  0.00278  199 SER A CA  
1515 C C   . SER A 207 ? 0.89802 0.58925 0.46605 0.06339  0.10802  0.01530  199 SER A C   
1516 O O   . SER A 207 ? 0.99111 0.70292 0.56285 0.07157  0.09644  0.01893  199 SER A O   
1517 C CB  . SER A 207 ? 0.90057 0.54810 0.46592 0.06176  0.13208  0.00236  199 SER A CB  
1518 O OG  . SER A 207 ? 0.98723 0.61618 0.51157 0.06822  0.13353  0.01261  199 SER A OG  
1519 N N   . LYS A 208 ? 0.93966 0.62517 0.49039 0.05978  0.10897  0.02033  200 LYS A N   
1520 C CA  . LYS A 208 ? 0.96128 0.66691 0.49881 0.06444  0.09551  0.02967  200 LYS A CA  
1521 C C   . LYS A 208 ? 0.95036 0.65594 0.46479 0.07812  0.09012  0.03539  200 LYS A C   
1522 O O   . LYS A 208 ? 0.89862 0.62745 0.40903 0.08348  0.07806  0.04069  200 LYS A O   
1523 C CB  . LYS A 208 ? 0.92258 0.61596 0.44446 0.05748  0.09858  0.03113  200 LYS A CB  
1524 C CG  . LYS A 208 ? 1.08265 0.73993 0.56818 0.06063  0.10861  0.03222  200 LYS A CG  
1525 C CD  . LYS A 208 ? 1.24739 0.88305 0.71841 0.05129  0.11711  0.03035  200 LYS A CD  
1526 C CE  . LYS A 208 ? 1.26787 0.85774 0.69816 0.05342  0.13145  0.03051  200 LYS A CE  
1527 N NZ  . LYS A 208 ? 1.28446 0.85229 0.69360 0.04580  0.13827  0.02944  200 LYS A NZ  
1528 N N   . ARG A 209 ? 0.94552 0.62515 0.44607 0.08335  0.09929  0.03319  201 ARG A N   
1529 C CA  . ARG A 209 ? 1.00040 0.67292 0.47585 0.09860  0.09481  0.03774  201 ARG A CA  
1530 C C   . ARG A 209 ? 0.97204 0.66695 0.46612 0.10575  0.08843  0.03658  201 ARG A C   
1531 O O   . ARG A 209 ? 0.97235 0.66495 0.44951 0.11964  0.08404  0.03944  201 ARG A O   
1532 C CB  . ARG A 209 ? 1.06908 0.69375 0.51374 0.09998  0.10999  0.03619  201 ARG A CB  
1533 C CG  . ARG A 209 ? 1.18600 0.78059 0.60433 0.09334  0.11893  0.03716  201 ARG A CG  
1534 C CD  . ARG A 209 ? 1.36157 0.91104 0.72894 0.10410  0.12439  0.04130  201 ARG A CD  
1535 N NE  . ARG A 209 ? 1.59175 1.09893 0.92842 0.09569  0.13979  0.04061  201 ARG A NE  
1536 C CZ  . ARG A 209 ? 1.66537 1.17244 0.98733 0.09368  0.13406  0.04307  201 ARG A CZ  
1537 N NH1 . ARG A 209 ? 1.59897 1.14830 0.93799 0.09799  0.11332  0.04573  201 ARG A NH1 
1538 N NH2 . ARG A 209 ? 1.72393 1.18694 1.01343 0.08625  0.15058  0.04195  201 ARG A NH2 
1539 N N   . ILE A 210 ? 0.91492 0.62808 0.43958 0.09812  0.08716  0.03209  202 ILE A N   
1540 C CA  . ILE A 210 ? 0.93467 0.66434 0.47449 0.10409  0.08154  0.02970  202 ILE A CA  
1541 C C   . ILE A 210 ? 0.86873 0.63245 0.42367 0.10274  0.07043  0.03315  202 ILE A C   
1542 O O   . ILE A 210 ? 0.81223 0.58078 0.38394 0.09306  0.06947  0.03055  202 ILE A O   
1543 C CB  . ILE A 210 ? 0.88675 0.60140 0.44498 0.09767  0.08924  0.01932  202 ILE A CB  
1544 C CG1 . ILE A 210 ? 0.87712 0.55467 0.41919 0.09616  0.10442  0.01525  202 ILE A CG1 
1545 C CG2 . ILE A 210 ? 0.89819 0.62806 0.46865 0.10447  0.08110  0.01614  202 ILE A CG2 
1546 C CD1 . ILE A 210 ? 0.87836 0.54313 0.44370 0.08792  0.11393  0.00204  202 ILE A CD1 
1547 N N   . ALA A 211 ? 0.82954 0.61404 0.37810 0.11242  0.06340  0.03796  203 ALA A N   
1548 C CA  . ALA A 211 ? 0.80739 0.62292 0.36617 0.11067  0.05631  0.04141  203 ALA A CA  
1549 C C   . ALA A 211 ? 0.86618 0.69328 0.42634 0.12001  0.05380  0.04058  203 ALA A C   
1550 O O   . ALA A 211 ? 0.86277 0.67544 0.41542 0.12916  0.05596  0.03760  203 ALA A O   
1551 C CB  . ALA A 211 ? 0.81245 0.64556 0.36536 0.11212  0.05229  0.04556  203 ALA A CB  
1552 N N   . VAL A 212 ? 0.86925 0.71833 0.43577 0.11719  0.05080  0.04294  204 VAL A N   
1553 C CA  . VAL A 212 ? 0.81326 0.67232 0.37783 0.12461  0.04986  0.04227  204 VAL A CA  
1554 C C   . VAL A 212 ? 0.83926 0.72467 0.40261 0.13226  0.05038  0.04434  204 VAL A C   
1555 O O   . VAL A 212 ? 0.81072 0.71644 0.38107 0.12532  0.05035  0.04663  204 VAL A O   
1556 C CB  . VAL A 212 ? 0.83010 0.69034 0.39690 0.11662  0.04815  0.04318  204 VAL A CB  
1557 C CG1 . VAL A 212 ? 0.83463 0.70072 0.39268 0.12418  0.04840  0.04279  204 VAL A CG1 
1558 C CG2 . VAL A 212 ? 0.81004 0.64782 0.38260 0.11140  0.04499  0.03871  204 VAL A CG2 
1559 N N   . ALA A 213 ? 0.87887 0.76441 0.43572 0.14608  0.05077  0.04200  205 ALA A N   
1560 C CA  . ALA A 213 ? 0.81244 0.72535 0.37144 0.15571  0.05189  0.04135  205 ALA A CA  
1561 C C   . ALA A 213 ? 0.84321 0.75900 0.39847 0.15616  0.05571  0.04045  205 ALA A C   
1562 O O   . ALA A 213 ? 0.85930 0.76265 0.40524 0.16713  0.05566  0.03732  205 ALA A O   
1563 C CB  . ALA A 213 ? 0.82494 0.73187 0.37564 0.17260  0.04951  0.03898  205 ALA A CB  
1564 N N   . LEU A 214 ? 0.83529 0.76209 0.39367 0.14425  0.05924  0.04303  206 LEU A N   
1565 C CA  . LEU A 214 ? 0.86756 0.78920 0.41411 0.14305  0.06343  0.04329  206 LEU A CA  
1566 C C   . LEU A 214 ? 0.93964 0.88262 0.48552 0.15327  0.07052  0.04037  206 LEU A C   
1567 O O   . LEU A 214 ? 0.86432 0.83785 0.42525 0.15142  0.07548  0.03927  206 LEU A O   
1568 C CB  . LEU A 214 ? 0.86574 0.78823 0.41093 0.12703  0.06690  0.04764  206 LEU A CB  
1569 C CG  . LEU A 214 ? 0.91597 0.82082 0.43948 0.12533  0.06980  0.04914  206 LEU A CG  
1570 C CD1 . LEU A 214 ? 0.92497 0.79836 0.43773 0.13072  0.05879  0.04677  206 LEU A CD1 
1571 C CD2 . LEU A 214 ? 0.88301 0.78757 0.40125 0.10955  0.07613  0.05411  206 LEU A CD2 
1572 N N   . GLU A 215 ? 0.92095 0.84926 0.45184 0.16386  0.07066  0.03756  207 GLU A N   
1573 C CA  . GLU A 215 ? 0.92485 0.86912 0.45225 0.17538  0.07829  0.03365  207 GLU A CA  
1574 C C   . GLU A 215 ? 0.96575 0.90548 0.47570 0.16900  0.08761  0.03503  207 GLU A C   
1575 O O   . GLU A 215 ? 0.89416 0.80385 0.38364 0.16717  0.08242  0.03647  207 GLU A O   
1576 C CB  . GLU A 215 ? 0.94390 0.87025 0.46194 0.19168  0.07298  0.02915  207 GLU A CB  
1577 C CG  . GLU A 215 ? 0.94071 0.88647 0.46029 0.20662  0.07923  0.02418  207 GLU A CG  
1578 C CD  . GLU A 215 ? 1.02104 0.94813 0.53226 0.22331  0.07358  0.01993  207 GLU A CD  
1579 O OE1 . GLU A 215 ? 1.03618 0.93284 0.53860 0.22153  0.06674  0.01991  207 GLU A OE1 
1580 O OE2 . GLU A 215 ? 1.03112 0.97394 0.54584 0.23791  0.07655  0.01559  207 GLU A OE2 
1581 N N   . ILE A 216 ? 0.92158 0.88920 0.43895 0.16618  0.10102  0.03348  208 ILE A N   
1582 C CA  . ILE A 216 ? 0.96747 0.93071 0.46654 0.15606  0.11518  0.03551  208 ILE A CA  
1583 C C   . ILE A 216 ? 1.01285 0.98022 0.49951 0.16829  0.12572  0.03003  208 ILE A C   
1584 O O   . ILE A 216 ? 1.08183 1.08335 0.59154 0.17518  0.13282  0.02377  208 ILE A O   
1585 C CB  . ILE A 216 ? 1.01646 1.00784 0.53600 0.13915  0.12628  0.03648  208 ILE A CB  
1586 C CG1 . ILE A 216 ? 1.01182 0.99330 0.53825 0.12716  0.11581  0.04193  208 ILE A CG1 
1587 C CG2 . ILE A 216 ? 1.02082 1.00728 0.52061 0.12787  0.14595  0.03765  208 ILE A CG2 
1588 C CD1 . ILE A 216 ? 1.00246 1.01649 0.55701 0.11335  0.12193  0.04044  208 ILE A CD1 
1589 N N   . GLY A 217 ? 1.04802 0.98134 0.49915 0.17200  0.12557  0.03125  209 GLY A N   
1590 C CA  . GLY A 217 ? 1.09445 1.02316 0.52577 0.18414  0.13500  0.02600  209 GLY A CA  
1591 C C   . GLY A 217 ? 1.15161 1.09278 0.57416 0.17462  0.15900  0.02539  209 GLY A C   
1592 O O   . GLY A 217 ? 1.10875 1.06181 0.54194 0.15734  0.16786  0.02905  209 GLY A O   
1593 N N   . ALA A 218 ? 1.14632 1.08293 0.54914 0.18465  0.17070  0.02018  210 ALA A N   
1594 C CA  . ALA A 218 ? 1.16154 1.10949 0.55478 0.17694  0.19823  0.01726  210 ALA A CA  
1595 C C   . ALA A 218 ? 1.17714 1.08831 0.53014 0.16017  0.20708  0.02579  210 ALA A C   
1596 O O   . ALA A 218 ? 1.15176 1.07857 0.51215 0.14313  0.22885  0.02611  210 ALA A O   
1597 C CB  . ALA A 218 ? 1.22258 1.16452 0.59666 0.19356  0.20620  0.00991  210 ALA A CB  
1598 N N   . ASP A 219 ? 1.12535 0.98837 0.43726 0.16524  0.19055  0.03129  211 ASP A N   
1599 C CA  . ASP A 219 ? 1.19964 1.01694 0.46334 0.15422  0.19373  0.03967  211 ASP A CA  
1600 C C   . ASP A 219 ? 1.19861 1.00158 0.46985 0.14952  0.17043  0.04591  211 ASP A C   
1601 O O   . ASP A 219 ? 1.23273 1.02339 0.50604 0.16230  0.14649  0.04378  211 ASP A O   
1602 C CB  . ASP A 219 ? 1.25857 1.02874 0.46406 0.16690  0.19135  0.03894  211 ASP A CB  
1603 C CG  . ASP A 219 ? 1.33959 1.12072 0.53475 0.17320  0.21464  0.03182  211 ASP A CG  
1604 O OD1 . ASP A 219 ? 1.27375 1.06365 0.46342 0.15957  0.24375  0.03216  211 ASP A OD1 
1605 O OD2 . ASP A 219 ? 1.40825 1.18899 0.60218 0.19105  0.20475  0.02500  211 ASP A OD2 
1606 N N   . LEU A 220 ? 1.20256 1.00675 0.47868 0.13125  0.17843  0.05212  212 LEU A N   
1607 C CA  . LEU A 220 ? 1.12132 0.91057 0.40311 0.12546  0.15905  0.05792  212 LEU A CA  
1608 C C   . LEU A 220 ? 1.27057 1.00433 0.50164 0.13462  0.14186  0.06120  212 LEU A C   
1609 O O   . LEU A 220 ? 1.39381 1.09458 0.57618 0.13914  0.15017  0.06208  212 LEU A O   
1610 C CB  . LEU A 220 ? 1.12066 0.91759 0.41044 0.10336  0.17505  0.06331  212 LEU A CB  
1611 C CG  . LEU A 220 ? 1.17582 1.02961 0.51846 0.09294  0.19039  0.05798  212 LEU A CG  
1612 C CD1 . LEU A 220 ? 1.16213 1.01910 0.51377 0.07039  0.20087  0.06237  212 LEU A CD1 
1613 C CD2 . LEU A 220 ? 1.12371 1.01280 0.51248 0.10476  0.17195  0.05262  212 LEU A CD2 
1614 N N   . PRO A 221 ? 1.23643 0.95795 0.47715 0.13847  0.11701  0.06182  213 PRO A N   
1615 C CA  . PRO A 221 ? 1.25457 0.92545 0.45155 0.14661  0.09833  0.06356  213 PRO A CA  
1616 C C   . PRO A 221 ? 1.25568 0.89671 0.42322 0.13303  0.10503  0.07290  213 PRO A C   
1617 O O   . PRO A 221 ? 1.19699 0.85799 0.37853 0.11591  0.12667  0.07719  213 PRO A O   
1618 C CB  . PRO A 221 ? 1.27872 0.96001 0.51224 0.15474  0.07216  0.05756  213 PRO A CB  
1619 C CG  . PRO A 221 ? 1.16755 0.89259 0.45324 0.14231  0.08025  0.05900  213 PRO A CG  
1620 C CD  . PRO A 221 ? 1.18086 0.93551 0.47430 0.13609  0.10558  0.05962  213 PRO A CD  
1621 N N   . SER A 222 ? 1.29606 0.88999 0.42477 0.14141  0.08549  0.07461  214 SER A N   
1622 C CA  . SER A 222 ? 1.36155 0.91810 0.45794 0.13207  0.08616  0.08331  214 SER A CA  
1623 C C   . SER A 222 ? 1.30942 0.89814 0.45687 0.11799  0.08600  0.08503  214 SER A C   
1624 O O   . SER A 222 ? 1.27979 0.90746 0.47940 0.12132  0.07564  0.07858  214 SER A O   
1625 C CB  . SER A 222 ? 1.39806 0.90281 0.45096 0.14921  0.05841  0.08183  214 SER A CB  
1626 O OG  . SER A 222 ? 1.53335 1.00462 0.53493 0.16122  0.05889  0.08025  214 SER A OG  
1627 N N   . ASN A 223 ? 1.34513 0.91454 0.47448 0.10251  0.09815  0.09326  215 ASN A N   
1628 C CA  . ASN A 223 ? 1.27926 0.87570 0.45145 0.08682  0.10097  0.09513  215 ASN A CA  
1629 C C   . ASN A 223 ? 1.29549 0.89446 0.49577 0.09769  0.07204  0.09013  215 ASN A C   
1630 O O   . ASN A 223 ? 1.24878 0.88737 0.50045 0.09105  0.07108  0.08709  215 ASN A O   
1631 C CB  . ASN A 223 ? 1.38594 0.94930 0.52381 0.06938  0.11749  0.10432  215 ASN A CB  
1632 C CG  . ASN A 223 ? 1.52882 1.09733 0.65015 0.05346  0.15141  0.10725  215 ASN A CG  
1633 O OD1 . ASN A 223 ? 1.47767 1.08534 0.62478 0.05439  0.16291  0.10166  215 ASN A OD1 
1634 N ND2 . ASN A 223 ? 1.62137 1.14948 0.70007 0.03859  0.16872  0.11510  215 ASN A ND2 
1635 N N   . HIS A 224 ? 1.30932 0.86753 0.47717 0.11429  0.04940  0.08801  216 HIS A N   
1636 C CA  . HIS A 224 ? 1.36131 0.91937 0.55585 0.12557  0.02160  0.08053  216 HIS A CA  
1637 C C   . HIS A 224 ? 1.27140 0.87606 0.52132 0.13024  0.01580  0.07079  216 HIS A C   
1638 O O   . HIS A 224 ? 1.27902 0.90113 0.56901 0.12918  0.00531  0.06576  216 HIS A O   
1639 C CB  . HIS A 224 ? 1.31226 0.81920 0.46052 0.14484  -0.00256 0.07747  216 HIS A CB  
1640 C CG  . HIS A 224 ? 1.43046 0.92817 0.55669 0.16122  -0.01128 0.07101  216 HIS A CG  
1641 N ND1 . HIS A 224 ? 1.38860 0.91122 0.55279 0.17334  -0.02895 0.05795  216 HIS A ND1 
1642 C CD2 . HIS A 224 ? 1.46189 0.92464 0.52952 0.16731  -0.00465 0.07501  216 HIS A CD2 
1643 C CE1 . HIS A 224 ? 1.39554 0.90098 0.52742 0.18634  -0.03405 0.05387  216 HIS A CE1 
1644 N NE2 . HIS A 224 ? 1.48041 0.94873 0.55166 0.18358  -0.01962 0.06435  216 HIS A NE2 
1645 N N   . VAL A 225 ? 1.22285 0.84410 0.47263 0.13476  0.02415  0.06824  217 VAL A N   
1646 C CA  . VAL A 225 ? 1.23175 0.89287 0.52758 0.13902  0.02203  0.06000  217 VAL A CA  
1647 C C   . VAL A 225 ? 1.19558 0.89664 0.53156 0.12368  0.03793  0.06352  217 VAL A C   
1648 O O   . VAL A 225 ? 1.18379 0.90808 0.55963 0.12441  0.03124  0.05809  217 VAL A O   
1649 C CB  . VAL A 225 ? 1.24391 0.90653 0.52207 0.14901  0.02728  0.05664  217 VAL A CB  
1650 C CG1 . VAL A 225 ? 1.17837 0.87687 0.49897 0.15326  0.02676  0.04906  217 VAL A CG1 
1651 C CG2 . VAL A 225 ? 1.25963 0.88071 0.49507 0.16519  0.00920  0.05194  217 VAL A CG2 
1652 N N   . ILE A 226 ? 1.21654 0.92362 0.54120 0.11013  0.05846  0.07122  218 ILE A N   
1653 C CA  . ILE A 226 ? 1.17500 0.92110 0.53609 0.09534  0.07302  0.07316  218 ILE A CA  
1654 C C   . ILE A 226 ? 1.12685 0.86804 0.50297 0.08601  0.06578  0.07526  218 ILE A C   
1655 O O   . ILE A 226 ? 1.15132 0.92136 0.56541 0.08213  0.06435  0.07250  218 ILE A O   
1656 C CB  . ILE A 226 ? 1.17058 0.92521 0.51701 0.08320  0.09773  0.07764  218 ILE A CB  
1657 C CG1 . ILE A 226 ? 1.14381 0.91627 0.48949 0.09253  0.10673  0.07327  218 ILE A CG1 
1658 C CG2 . ILE A 226 ? 1.14161 0.92863 0.52119 0.06570  0.10956  0.07874  218 ILE A CG2 
1659 C CD1 . ILE A 226 ? 1.10359 0.87537 0.42638 0.08278  0.13207  0.07588  218 ILE A CD1 
1660 N N   . ASP A 227 ? 1.17366 0.87615 0.51727 0.08373  0.06125  0.07983  219 ASP A N   
1661 C CA  . ASP A 227 ? 1.21902 0.90908 0.57063 0.07675  0.05331  0.08146  219 ASP A CA  
1662 C C   . ASP A 227 ? 1.16324 0.86389 0.54872 0.08673  0.03472  0.07307  219 ASP A C   
1663 O O   . ASP A 227 ? 1.09504 0.80444 0.50486 0.07906  0.03284  0.07236  219 ASP A O   
1664 C CB  . ASP A 227 ? 1.22102 0.85952 0.52404 0.07858  0.04814  0.08679  219 ASP A CB  
1665 C CG  . ASP A 227 ? 1.24934 0.87048 0.51619 0.06419  0.07067  0.09561  219 ASP A CG  
1666 O OD1 . ASP A 227 ? 1.26073 0.91660 0.54907 0.05084  0.09035  0.09611  219 ASP A OD1 
1667 O OD2 . ASP A 227 ? 1.33063 0.90237 0.54758 0.06676  0.06849  0.10099  219 ASP A OD2 
1668 N N   . ARG A 228 ? 1.12645 0.82547 0.51306 0.10220  0.02311  0.06604  220 ARG A N   
1669 C CA  . ARG A 228 ? 1.08434 0.79190 0.50336 0.11140  0.00754  0.05556  220 ARG A CA  
1670 C C   . ARG A 228 ? 1.06002 0.80196 0.51927 0.10284  0.01597  0.05422  220 ARG A C   
1671 O O   . ARG A 228 ? 0.95883 0.70381 0.44447 0.10472  0.00766  0.04699  220 ARG A O   
1672 C CB  . ARG A 228 ? 1.10431 0.80813 0.51672 0.12655  -0.00138 0.04804  220 ARG A CB  
1673 C CG  . ARG A 228 ? 1.04453 0.74044 0.47648 0.13767  -0.02163 0.03511  220 ARG A CG  
1674 C CD  . ARG A 228 ? 0.99683 0.65803 0.40366 0.14596  -0.03915 0.03292  220 ARG A CD  
1675 N NE  . ARG A 228 ? 1.05747 0.71463 0.48493 0.15906  -0.06033 0.01706  220 ARG A NE  
1676 C CZ  . ARG A 228 ? 1.08452 0.75568 0.55511 0.15720  -0.06620 0.00668  220 ARG A CZ  
1677 N NH1 . ARG A 228 ? 0.98205 0.66908 0.47545 0.14365  -0.05326 0.01163  220 ARG A NH1 
1678 N NH2 . ARG A 228 ? 1.05760 0.72678 0.54899 0.16871  -0.08471 -0.01013 220 ARG A NH2 
1679 N N   . TRP A 229 ? 1.09354 0.85930 0.55661 0.09446  0.03173  0.05975  221 TRP A N   
1680 C CA  . TRP A 229 ? 1.00695 0.80377 0.50146 0.08945  0.03831  0.05845  221 TRP A CA  
1681 C C   . TRP A 229 ? 1.00974 0.81433 0.51364 0.07450  0.04447  0.06285  221 TRP A C   
1682 O O   . TRP A 229 ? 0.96011 0.78864 0.48509 0.07040  0.04909  0.06204  221 TRP A O   
1683 C CB  . TRP A 229 ? 0.94935 0.76950 0.44465 0.09316  0.04828  0.05900  221 TRP A CB  
1684 C CG  . TRP A 229 ? 0.98181 0.79618 0.47279 0.10788  0.04209  0.05323  221 TRP A CG  
1685 C CD1 . TRP A 229 ? 0.97683 0.77882 0.44243 0.11591  0.04231  0.05295  221 TRP A CD1 
1686 C CD2 . TRP A 229 ? 0.93229 0.74946 0.44276 0.11551  0.03558  0.04614  221 TRP A CD2 
1687 N NE1 . TRP A 229 ? 1.03205 0.83121 0.50217 0.12836  0.03487  0.04561  221 TRP A NE1 
1688 C CE2 . TRP A 229 ? 0.97729 0.78534 0.47549 0.12767  0.03134  0.04128  221 TRP A CE2 
1689 C CE3 . TRP A 229 ? 0.86962 0.69285 0.40359 0.11252  0.03449  0.04318  221 TRP A CE3 
1690 C CZ2 . TRP A 229 ? 0.94271 0.74864 0.45432 0.13576  0.02620  0.03312  221 TRP A CZ2 
1691 C CZ3 . TRP A 229 ? 0.86419 0.68307 0.40879 0.12030  0.03116  0.03583  221 TRP A CZ3 
1692 C CH2 . TRP A 229 ? 0.95119 0.76212 0.48615 0.13125  0.02712  0.03066  221 TRP A CH2 
1693 N N   . LEU A 230 ? 1.06511 0.84742 0.55125 0.06745  0.04369  0.06694  222 LEU A N   
1694 C CA  . LEU A 230 ? 1.13055 0.91442 0.62458 0.05305  0.04784  0.06988  222 LEU A CA  
1695 C C   . LEU A 230 ? 1.09938 0.87937 0.61474 0.05563  0.03805  0.06418  222 LEU A C   
1696 O O   . LEU A 230 ? 1.09758 0.86168 0.61382 0.06667  0.02677  0.05853  222 LEU A O   
1697 C CB  . LEU A 230 ? 1.10170 0.85565 0.56470 0.04585  0.05057  0.07594  222 LEU A CB  
1698 C CG  . LEU A 230 ? 1.13146 0.88684 0.57197 0.03881  0.06587  0.08139  222 LEU A CG  
1699 C CD1 . LEU A 230 ? 1.15275 0.86683 0.55377 0.03284  0.06882  0.08777  222 LEU A CD1 
1700 C CD2 . LEU A 230 ? 1.05155 0.84441 0.51610 0.02481  0.08005  0.08106  222 LEU A CD2 
1701 N N   . GLY A 231 ? 0.98335 0.77822 0.51626 0.04592  0.04255  0.06410  223 GLY A N   
1702 C CA  . GLY A 231 ? 0.96628 0.75700 0.51775 0.04620  0.03744  0.05860  223 GLY A CA  
1703 C C   . GLY A 231 ? 0.91976 0.72266 0.48798 0.05471  0.03681  0.05294  223 GLY A C   
1704 O O   . GLY A 231 ? 0.97872 0.77775 0.56125 0.05358  0.03637  0.04797  223 GLY A O   
1705 N N   . GLU A 232 ? 0.86245 0.67664 0.42694 0.06262  0.03828  0.05334  224 GLU A N   
1706 C CA  . GLU A 232 ? 0.91688 0.73829 0.49231 0.07132  0.03864  0.04845  224 GLU A CA  
1707 C C   . GLU A 232 ? 0.87019 0.71173 0.44966 0.06840  0.04488  0.05116  224 GLU A C   
1708 O O   . GLU A 232 ? 0.91074 0.76857 0.48690 0.06259  0.04854  0.05550  224 GLU A O   
1709 C CB  . GLU A 232 ? 0.87463 0.69471 0.44153 0.08263  0.03580  0.04671  224 GLU A CB  
1710 C CG  . GLU A 232 ? 0.87051 0.66935 0.43158 0.08812  0.02590  0.04218  224 GLU A CG  
1711 C CD  . GLU A 232 ? 0.90634 0.69402 0.48757 0.08998  0.01983  0.03219  224 GLU A CD  
1712 O OE1 . GLU A 232 ? 0.86339 0.65654 0.45996 0.08731  0.02595  0.02899  224 GLU A OE1 
1713 O OE2 . GLU A 232 ? 0.91540 0.68774 0.49627 0.09446  0.00924  0.02674  224 GLU A OE2 
1714 N N   . PRO A 233 ? 0.78136 0.62074 0.36727 0.07241  0.04621  0.04768  225 PRO A N   
1715 C CA  . PRO A 233 ? 0.83050 0.68385 0.41541 0.07258  0.04891  0.04957  225 PRO A CA  
1716 C C   . PRO A 233 ? 0.81301 0.68478 0.39445 0.08290  0.04931  0.05056  225 PRO A C   
1717 O O   . PRO A 233 ? 0.79870 0.66463 0.37649 0.09278  0.04951  0.04845  225 PRO A O   
1718 C CB  . PRO A 233 ? 0.78079 0.61469 0.36628 0.07423  0.05124  0.04548  225 PRO A CB  
1719 C CG  . PRO A 233 ? 0.78123 0.60046 0.37210 0.07946  0.05090  0.03999  225 PRO A CG  
1720 C CD  . PRO A 233 ? 0.78062 0.60162 0.37376 0.07677  0.04553  0.04069  225 PRO A CD  
1721 N N   . ILE A 234 ? 0.81716 0.70892 0.39917 0.08009  0.05084  0.05310  226 ILE A N   
1722 C CA  . ILE A 234 ? 0.89807 0.81277 0.48087 0.08932  0.05269  0.05251  226 ILE A CA  
1723 C C   . ILE A 234 ? 0.87458 0.81011 0.46483 0.09062  0.05043  0.05095  226 ILE A C   
1724 O O   . ILE A 234 ? 0.93524 0.88539 0.53348 0.07906  0.05106  0.05108  226 ILE A O   
1725 C CB  . ILE A 234 ? 0.89378 0.82036 0.47442 0.08422  0.05834  0.05436  226 ILE A CB  
1726 C CG1 . ILE A 234 ? 0.83292 0.73417 0.39983 0.08569  0.05734  0.05549  226 ILE A CG1 
1727 C CG2 . ILE A 234 ? 0.89874 0.85258 0.48461 0.09306  0.06231  0.05182  226 ILE A CG2 
1728 C CD1 . ILE A 234 ? 0.88062 0.78092 0.43586 0.07772  0.06356  0.05890  226 ILE A CD1 
1729 N N   . LYS A 235 ? 0.83116 0.76550 0.41708 0.10475  0.04701  0.04885  227 LYS A N   
1730 C CA  . LYS A 235 ? 0.86357 0.81527 0.45235 0.11145  0.04115  0.04618  227 LYS A CA  
1731 C C   . LYS A 235 ? 0.90221 0.88598 0.50157 0.12221  0.04089  0.04230  227 LYS A C   
1732 O O   . LYS A 235 ? 0.94457 0.95721 0.55746 0.12292  0.03624  0.03776  227 LYS A O   
1733 C CB  . LYS A 235 ? 0.85934 0.78241 0.43022 0.12174  0.03744  0.04635  227 LYS A CB  
1734 C CG  . LYS A 235 ? 0.91707 0.81427 0.47997 0.11076  0.03864  0.04797  227 LYS A CG  
1735 C CD  . LYS A 235 ? 1.04340 0.95567 0.61126 0.10218  0.03355  0.04695  227 LYS A CD  
1736 C CE  . LYS A 235 ? 1.13803 1.03164 0.70485 0.08648  0.03734  0.04841  227 LYS A CE  
1737 N NZ  . LYS A 235 ? 1.11773 1.03408 0.69789 0.07325  0.03519  0.04744  227 LYS A NZ  
1738 N N   . ALA A 236 ? 0.87053 0.85048 0.46559 0.13043  0.04541  0.04246  228 ALA A N   
1739 C CA  . ALA A 236 ? 0.87043 0.87805 0.47440 0.14245  0.04715  0.03790  228 ALA A CA  
1740 C C   . ALA A 236 ? 0.86123 0.87084 0.46433 0.13710  0.05730  0.03906  228 ALA A C   
1741 O O   . ALA A 236 ? 0.90979 0.89078 0.49924 0.13231  0.05885  0.04303  228 ALA A O   
1742 C CB  . ALA A 236 ? 0.86414 0.85772 0.45521 0.16305  0.04163  0.03622  228 ALA A CB  
1743 N N   . ALA A 237 ? 0.89040 0.93249 0.50749 0.13839  0.06388  0.03448  229 ALA A N   
1744 C CA  . ALA A 237 ? 0.90913 0.95311 0.52055 0.13657  0.07555  0.03451  229 ALA A CA  
1745 C C   . ALA A 237 ? 0.92660 0.99136 0.54456 0.15484  0.07739  0.02778  229 ALA A C   
1746 O O   . ALA A 237 ? 0.88202 0.98370 0.52371 0.15857  0.07713  0.02050  229 ALA A O   
1747 C CB  . ALA A 237 ? 0.92708 0.98815 0.54804 0.11738  0.08673  0.03461  229 ALA A CB  
1748 N N   . ILE A 238 ? 0.91361 0.95584 0.51274 0.16655  0.07803  0.02867  230 ILE A N   
1749 C CA  . ILE A 238 ? 0.88306 0.93707 0.48350 0.18663  0.07885  0.02238  230 ILE A CA  
1750 C C   . ILE A 238 ? 0.90514 0.97546 0.50647 0.18352  0.09428  0.01906  230 ILE A C   
1751 O O   . ILE A 238 ? 0.98170 1.02659 0.56133 0.17562  0.10005  0.02377  230 ILE A O   
1752 C CB  . ILE A 238 ? 0.89945 0.91603 0.47725 0.20011  0.07161  0.02429  230 ILE A CB  
1753 C CG1 . ILE A 238 ? 0.91521 0.91370 0.48974 0.20273  0.06021  0.02685  230 ILE A CG1 
1754 C CG2 . ILE A 238 ? 0.90181 0.92496 0.47640 0.22015  0.07376  0.01810  230 ILE A CG2 
1755 C CD1 . ILE A 238 ? 0.87070 0.82665 0.42399 0.20704  0.05683  0.02908  230 ILE A CD1 
1756 N N   . LEU A 239 ? 0.87586 0.98617 0.50084 0.19017  0.10051  0.01019  231 LEU A N   
1757 C CA  . LEU A 239 ? 0.89263 1.02347 0.52232 0.18682  0.11926  0.00472  231 LEU A CA  
1758 C C   . LEU A 239 ? 0.93225 1.07445 0.56459 0.21009  0.11999  -0.00351 231 LEU A C   
1759 O O   . LEU A 239 ? 0.89671 1.07495 0.55757 0.22197  0.11627  -0.01305 231 LEU A O   
1760 C CB  . LEU A 239 ? 0.90592 1.08002 0.56933 0.17166  0.12914  -0.00183 231 LEU A CB  
1761 C CG  . LEU A 239 ? 0.88329 1.04877 0.54714 0.14909  0.12771  0.00492  231 LEU A CG  
1762 C CD1 . LEU A 239 ? 0.88797 1.09786 0.58745 0.13348  0.13944  -0.00411 231 LEU A CD1 
1763 C CD2 . LEU A 239 ? 0.85602 0.97806 0.48345 0.13617  0.13470  0.01572  231 LEU A CD2 
1764 N N   . PRO A 240 ? 0.99938 1.11116 0.60227 0.21851  0.12359  -0.00133 232 PRO A N   
1765 C CA  . PRO A 240 ? 0.97127 1.09229 0.57464 0.23989  0.12675  -0.00977 232 PRO A CA  
1766 C C   . PRO A 240 ? 0.97636 1.14080 0.60447 0.23692  0.14633  -0.02016 232 PRO A C   
1767 O O   . PRO A 240 ? 1.01548 1.18217 0.64036 0.21699  0.16196  -0.01789 232 PRO A O   
1768 C CB  . PRO A 240 ? 0.95586 1.03194 0.51981 0.24379  0.12781  -0.00511 232 PRO A CB  
1769 C CG  . PRO A 240 ? 0.96347 1.00606 0.51002 0.22832  0.11903  0.00531  232 PRO A CG  
1770 C CD  . PRO A 240 ? 0.95672 1.02389 0.52486 0.20933  0.12324  0.00773  232 PRO A CD  
1771 N N   . THR A 241 ? 0.93182 1.12759 0.58322 0.25680  0.14576  -0.03192 233 THR A N   
1772 C CA  . THR A 241 ? 1.02811 1.27276 0.71237 0.25697  0.16464  -0.04596 233 THR A CA  
1773 C C   . THR A 241 ? 1.10248 1.33030 0.76026 0.24857  0.18875  -0.04529 233 THR A C   
1774 O O   . THR A 241 ? 1.09983 1.36093 0.77931 0.23751  0.21132  -0.05424 233 THR A O   
1775 C CB  . THR A 241 ? 1.02694 1.30078 0.73633 0.28563  0.15516  -0.05910 233 THR A CB  
1776 O OG1 . THR A 241 ? 1.07272 1.30354 0.74632 0.30502  0.14437  -0.05384 233 THR A OG1 
1777 C CG2 . THR A 241 ? 1.00134 1.30397 0.74334 0.29234  0.13516  -0.06389 233 THR A CG2 
1778 N N   . SER A 242 ? 1.07565 1.25274 0.68774 0.25312  0.18455  -0.03616 234 SER A N   
1779 C CA  . SER A 242 ? 1.08380 1.23385 0.65923 0.24937  0.20295  -0.03495 234 SER A CA  
1780 C C   . SER A 242 ? 1.12886 1.26800 0.68901 0.22212  0.21952  -0.02809 234 SER A C   
1781 O O   . SER A 242 ? 1.19555 1.32895 0.73648 0.21635  0.24286  -0.03112 234 SER A O   
1782 C CB  . SER A 242 ? 1.07010 1.16912 0.60369 0.26156  0.18866  -0.02837 234 SER A CB  
1783 O OG  . SER A 242 ? 1.06636 1.13512 0.58595 0.25137  0.17161  -0.01693 234 SER A OG  
1784 N N   . ILE A 243 ? 1.16034 1.29329 0.72528 0.20628  0.20918  -0.01937 235 ILE A N   
1785 C CA  . ILE A 243 ? 1.19919 1.31016 0.74159 0.18132  0.22128  -0.01071 235 ILE A CA  
1786 C C   . ILE A 243 ? 1.19134 1.34486 0.76682 0.16366  0.24548  -0.01884 235 ILE A C   
1787 O O   . ILE A 243 ? 1.24120 1.37559 0.79567 0.14210  0.26131  -0.01296 235 ILE A O   
1788 C CB  . ILE A 243 ? 1.08636 1.17251 0.62134 0.17246  0.20051  0.00073  235 ILE A CB  
1789 C CG1 . ILE A 243 ? 1.10373 1.22889 0.68380 0.16402  0.19412  -0.00204 235 ILE A CG1 
1790 C CG2 . ILE A 243 ? 1.10350 1.15649 0.61802 0.18950  0.17754  0.00503  235 ILE A CG2 
1791 C CD1 . ILE A 243 ? 1.09624 1.19753 0.66878 0.15321  0.17761  0.00843  235 ILE A CD1 
1792 N N   . PHE A 244 ? 1.12642 1.33413 0.75172 0.17251  0.24781  -0.03279 236 PHE A N   
1793 C CA  . PHE A 244 ? 1.14672 1.40531 0.81629 0.15652  0.26992  -0.04530 236 PHE A CA  
1794 C C   . PHE A 244 ? 1.16837 1.43278 0.82885 0.15421  0.30232  -0.05414 236 PHE A C   
1795 O O   . PHE A 244 ? 1.17069 1.45059 0.83954 0.17597  0.30328  -0.06380 236 PHE A O   
1796 C CB  . PHE A 244 ? 1.10307 1.41842 0.83195 0.16992  0.25454  -0.05882 236 PHE A CB  
1797 C CG  . PHE A 244 ? 1.08693 1.40193 0.82822 0.16567  0.22927  -0.05220 236 PHE A CG  
1798 C CD1 . PHE A 244 ? 1.06568 1.34824 0.78414 0.18200  0.20205  -0.04214 236 PHE A CD1 
1799 C CD2 . PHE A 244 ? 1.06767 1.41286 0.84240 0.14415  0.23440  -0.05688 236 PHE A CD2 
1800 C CE1 . PHE A 244 ? 0.96021 1.23971 0.68695 0.17764  0.18139  -0.03643 236 PHE A CE1 
1801 C CE2 . PHE A 244 ? 1.02960 1.37204 0.81248 0.14066  0.21145  -0.05123 236 PHE A CE2 
1802 C CZ  . PHE A 244 ? 0.96089 1.26997 0.71862 0.15772  0.18548  -0.04076 236 PHE A CZ  
1803 N N   . LEU A 245 ? 1.15806 1.40649 0.79854 0.12849  0.32915  -0.05087 237 LEU A N   
1804 C CA  . LEU A 245 ? 1.21317 1.46916 0.84749 0.11911  0.36745  -0.06051 237 LEU A CA  
1805 C C   . LEU A 245 ? 1.19003 1.52263 0.89880 0.11980  0.38051  -0.08309 237 LEU A C   
1806 O O   . LEU A 245 ? 1.17933 1.55112 0.93657 0.11188  0.36895  -0.08863 237 LEU A O   
1807 C CB  . LEU A 245 ? 1.23098 1.44951 0.82760 0.08852  0.39165  -0.05100 237 LEU A CB  
1808 C CG  . LEU A 245 ? 1.21649 1.35731 0.73033 0.08932  0.39197  -0.03406 237 LEU A CG  
1809 C CD1 . LEU A 245 ? 1.21621 1.32631 0.70695 0.11165  0.35292  -0.02316 237 LEU A CD1 
1810 C CD2 . LEU A 245 ? 1.19580 1.29717 0.67440 0.06110  0.40652  -0.02276 237 LEU A CD2 
1811 N N   . THR A 246 ? 1.25467 1.60810 0.97281 0.12998  0.40264  -0.09693 238 THR A N   
1812 C CA  . THR A 246 ? 1.27389 1.70205 1.06428 0.12951  0.42163  -0.12205 238 THR A CA  
1813 C C   . THR A 246 ? 1.30911 1.74436 1.10470 0.09456  0.46457  -0.12827 238 THR A C   
1814 O O   . THR A 246 ? 1.35949 1.73574 1.08951 0.08087  0.48612  -0.11530 238 THR A O   
1815 C CB  . THR A 246 ? 1.27163 1.71711 1.06932 0.15746  0.42681  -0.13504 238 THR A CB  
1816 O OG1 . THR A 246 ? 1.28206 1.69608 1.05072 0.18586  0.39109  -0.12392 238 THR A OG1 
1817 C CG2 . THR A 246 ? 1.24979 1.77801 1.13100 0.16610  0.43305  -0.16234 238 THR A CG2 
1818 N N   . ASN A 247 ? 1.29187 1.79401 1.16060 0.08074  0.47601  -0.14800 239 ASN A N   
1819 C CA  . ASN A 247 ? 1.41835 1.93589 1.30409 0.04480  0.52030  -0.15829 239 ASN A CA  
1820 C C   . ASN A 247 ? 1.48766 2.06751 1.42997 0.04919  0.55079  -0.18652 239 ASN A C   
1821 O O   . ASN A 247 ? 1.45314 2.06018 1.41730 0.08186  0.53361  -0.19608 239 ASN A O   
1822 C CB  . ASN A 247 ? 1.44805 1.99181 1.37464 0.02043  0.51265  -0.16061 239 ASN A CB  
1823 C CG  . ASN A 247 ? 1.43293 2.06688 1.45644 0.02740  0.50143  -0.18773 239 ASN A CG  
1824 O OD1 . ASN A 247 ? 1.37243 2.03695 1.42388 0.06033  0.47137  -0.19495 239 ASN A OD1 
1825 N ND2 . ASN A 247 ? 1.48829 2.16335 1.56242 -0.00308 0.52464  -0.20372 239 ASN A ND2 
1826 N N   . LYS A 248 ? 1.74465 2.34347 1.70832 0.01686  0.59582  -0.19971 240 LYS A N   
1827 C CA  . LYS A 248 ? 1.80161 2.45976 1.82132 0.01359  0.63475  -0.22900 240 LYS A CA  
1828 C C   . LYS A 248 ? 1.73753 2.48309 1.84914 0.04138  0.60771  -0.25451 240 LYS A C   
1829 O O   . LYS A 248 ? 1.71758 2.48955 1.84750 0.06533  0.61525  -0.26939 240 LYS A O   
1830 C CB  . LYS A 248 ? 1.77183 2.44425 1.81448 -0.03094 0.68235  -0.24065 240 LYS A CB  
1831 C CG  . LYS A 248 ? 1.77040 2.46835 1.85553 -0.05415 0.66759  -0.24234 240 LYS A CG  
1832 C CD  . LYS A 248 ? 1.85157 2.53126 1.92749 -0.10132 0.71523  -0.24453 240 LYS A CD  
1833 C CE  . LYS A 248 ? 1.95942 2.53352 1.92418 -0.11629 0.72657  -0.21203 240 LYS A CE  
1834 N NZ  . LYS A 248 ? 1.90426 2.44353 1.85354 -0.15359 0.76060  -0.20727 240 LYS A NZ  
1835 N N   . LYS A 249 ? 1.42542 2.21128 1.58938 0.03966  0.57677  -0.25977 241 LYS A N   
1836 C CA  . LYS A 249 ? 1.30883 2.17992 1.56328 0.06428  0.54904  -0.28632 241 LYS A CA  
1837 C C   . LYS A 249 ? 1.23794 2.09410 1.46942 0.11054  0.50842  -0.27801 241 LYS A C   
1838 O O   . LYS A 249 ? 1.25549 2.16660 1.53954 0.13725  0.50385  -0.30118 241 LYS A O   
1839 C CB  . LYS A 249 ? 1.27173 2.17456 1.57139 0.04989  0.52384  -0.29022 241 LYS A CB  
1840 C CG  . LYS A 249 ? 1.26222 2.19454 1.60287 0.00504  0.56264  -0.30539 241 LYS A CG  
1841 C CD  . LYS A 249 ? 1.24410 2.17990 1.60081 -0.01339 0.53849  -0.30023 241 LYS A CD  
1842 C CE  . LYS A 249 ? 1.20402 2.15416 1.58799 -0.06134 0.58005  -0.31179 241 LYS A CE  
1843 N NZ  . LYS A 249 ? 1.04117 2.08786 1.53012 -0.06897 0.60037  -0.35304 241 LYS A NZ  
1844 N N   . GLY A 250 ? 1.30657 2.09067 1.46345 0.11924  0.48117  -0.24741 242 GLY A N   
1845 C CA  . GLY A 250 ? 1.25318 2.01241 1.38065 0.15939  0.44200  -0.23660 242 GLY A CA  
1846 C C   . GLY A 250 ? 1.28847 2.01338 1.38869 0.16407  0.39971  -0.21561 242 GLY A C   
1847 O O   . GLY A 250 ? 1.27701 1.95911 1.33217 0.18992  0.37254  -0.20007 242 GLY A O   
1848 N N   . PHE A 251 ? 1.22436 1.96703 1.35163 0.13934  0.39567  -0.21635 243 PHE A N   
1849 C CA  . PHE A 251 ? 1.19776 1.91108 1.30354 0.13877  0.35931  -0.19824 243 PHE A CA  
1850 C C   . PHE A 251 ? 1.25302 1.88010 1.27124 0.13598  0.35489  -0.16733 243 PHE A C   
1851 O O   . PHE A 251 ? 1.31011 1.89872 1.28468 0.12000  0.38493  -0.15873 243 PHE A O   
1852 C CB  . PHE A 251 ? 1.23595 1.97615 1.37838 0.10519  0.36727  -0.20458 243 PHE A CB  
1853 C CG  . PHE A 251 ? 1.26133 2.08129 1.48866 0.11244  0.35004  -0.23172 243 PHE A CG  
1854 C CD1 . PHE A 251 ? 1.21577 2.10596 1.51385 0.10461  0.37651  -0.26207 243 PHE A CD1 
1855 C CD2 . PHE A 251 ? 1.32574 2.15008 1.56211 0.12704  0.30736  -0.22827 243 PHE A CD2 
1856 C CE1 . PHE A 251 ? 1.16949 2.13589 1.54925 0.11268  0.35753  -0.28960 243 PHE A CE1 
1857 C CE2 . PHE A 251 ? 1.30573 2.20108 1.61667 0.13568  0.28831  -0.25420 243 PHE A CE2 
1858 C CZ  . PHE A 251 ? 1.22538 2.19328 1.60974 0.12910  0.31190  -0.28543 243 PHE A CZ  
1859 N N   . PRO A 252 ? 1.21836 1.81185 1.20809 0.15161  0.31738  -0.15094 244 PRO A N   
1860 C CA  . PRO A 252 ? 1.20868 1.72649 1.12549 0.14486  0.31097  -0.12400 244 PRO A CA  
1861 C C   . PRO A 252 ? 1.14730 1.64683 1.05402 0.11106  0.31888  -0.11414 244 PRO A C   
1862 O O   . PRO A 252 ? 1.16647 1.70417 1.11811 0.10194  0.30895  -0.12310 244 PRO A O   
1863 C CB  . PRO A 252 ? 1.14480 1.64521 1.04934 0.17283  0.27014  -0.11540 244 PRO A CB  
1864 C CG  . PRO A 252 ? 1.12320 1.68616 1.09289 0.18199  0.25198  -0.13374 244 PRO A CG  
1865 C CD  . PRO A 252 ? 1.17750 1.80197 1.20203 0.17735  0.27962  -0.15850 244 PRO A CD  
1866 N N   . VAL A 253 ? 1.10377 1.54439 0.95079 0.09458  0.33553  -0.09701 245 VAL A N   
1867 C CA  . VAL A 253 ? 1.10469 1.51196 0.92709 0.06492  0.34161  -0.08397 245 VAL A CA  
1868 C C   . VAL A 253 ? 1.12000 1.45186 0.86882 0.06999  0.32923  -0.06039 245 VAL A C   
1869 O O   . VAL A 253 ? 1.14911 1.46091 0.87254 0.09414  0.31812  -0.05653 245 VAL A O   
1870 C CB  . VAL A 253 ? 1.10768 1.52493 0.93792 0.03368  0.38400  -0.09232 245 VAL A CB  
1871 C CG1 . VAL A 253 ? 1.17037 1.66820 1.08212 0.02757  0.39604  -0.11916 245 VAL A CG1 
1872 C CG2 . VAL A 253 ? 1.14703 1.52572 0.92676 0.03363  0.41304  -0.08787 245 VAL A CG2 
1873 N N   . LEU A 254 ? 1.10487 1.39738 0.82279 0.04861  0.33031  -0.04674 246 LEU A N   
1874 C CA  . LEU A 254 ? 1.10974 1.33159 0.76103 0.05157  0.31763  -0.02606 246 LEU A CA  
1875 C C   . LEU A 254 ? 1.15606 1.33378 0.76170 0.02636  0.34555  -0.01777 246 LEU A C   
1876 O O   . LEU A 254 ? 1.17773 1.37858 0.80850 0.00176  0.36922  -0.02550 246 LEU A O   
1877 C CB  . LEU A 254 ? 1.10761 1.32109 0.76509 0.05390  0.28571  -0.01742 246 LEU A CB  
1878 C CG  . LEU A 254 ? 1.07270 1.30976 0.75624 0.08058  0.25612  -0.02135 246 LEU A CG  
1879 C CD1 . LEU A 254 ? 0.99802 1.23285 0.69319 0.07733  0.23124  -0.01560 246 LEU A CD1 
1880 C CD2 . LEU A 254 ? 1.12098 1.32026 0.76423 0.10321  0.24515  -0.01393 246 LEU A CD2 
1881 N N   . SER A 255 ? 1.17684 1.29126 0.71662 0.03261  0.34203  -0.00339 247 SER A N   
1882 C CA  . SER A 255 ? 1.14946 1.20627 0.62971 0.01345  0.36350  0.00732  247 SER A CA  
1883 C C   . SER A 255 ? 1.21498 1.25857 0.69730 -0.00788 0.35848  0.01466  247 SER A C   
1884 O O   . SER A 255 ? 1.24541 1.30966 0.76006 -0.00206 0.33113  0.01535  247 SER A O   
1885 C CB  . SER A 255 ? 1.17841 1.17269 0.59110 0.03031  0.35114  0.01960  247 SER A CB  
1886 O OG  . SER A 255 ? 1.15055 1.12228 0.55454 0.04071  0.31608  0.02960  247 SER A OG  
1887 N N   . LYS A 256 ? 1.23283 1.23895 0.67779 -0.03150 0.38501  0.01998  248 LYS A N   
1888 C CA  . LYS A 256 ? 1.32008 1.30523 0.75913 -0.05424 0.38516  0.02707  248 LYS A CA  
1889 C C   . LYS A 256 ? 1.33188 1.28107 0.74694 -0.04003 0.34756  0.04060  248 LYS A C   
1890 O O   . LYS A 256 ? 1.30809 1.26745 0.74785 -0.05020 0.33509  0.04195  248 LYS A O   
1891 C CB  . LYS A 256 ? 1.37200 1.30371 0.75446 -0.07731 0.42005  0.03323  248 LYS A CB  
1892 C CG  . LYS A 256 ? 1.45773 1.42540 0.86914 -0.09884 0.46303  0.01824  248 LYS A CG  
1893 C CD  . LYS A 256 ? 1.49963 1.48402 0.94190 -0.13195 0.48310  0.01236  248 LYS A CD  
1894 C CE  . LYS A 256 ? 1.63146 1.53836 1.00088 -0.15439 0.50717  0.02562  248 LYS A CE  
1895 N NZ  . LYS A 256 ? 1.61485 1.54167 1.01648 -0.19068 0.53907  0.01557  248 LYS A NZ  
1896 N N   . MET A 257 ? 1.30224 1.21213 0.67294 -0.01782 0.33067  0.04861  249 MET A N   
1897 C CA  . MET A 257 ? 1.36008 1.23467 0.70800 -0.00306 0.29596  0.05925  249 MET A CA  
1898 C C   . MET A 257 ? 1.33718 1.25921 0.74038 0.01211  0.26897  0.05338  249 MET A C   
1899 O O   . MET A 257 ? 1.31565 1.22622 0.72292 0.01435  0.24568  0.05894  249 MET A O   
1900 C CB  . MET A 257 ? 1.42887 1.24984 0.71537 0.01574  0.28711  0.06622  249 MET A CB  
1901 C CG  . MET A 257 ? 1.64425 1.40193 0.86060 0.00432  0.30773  0.07476  249 MET A CG  
1902 S SD  . MET A 257 ? 1.89652 1.61534 1.09212 -0.01719 0.30730  0.08504  249 MET A SD  
1903 C CE  . MET A 257 ? 1.68232 1.42475 0.89571 -0.05024 0.35409  0.07841  249 MET A CE  
1904 N N   . HIS A 258 ? 1.28155 1.25131 0.72254 0.02304  0.27240  0.04238  250 HIS A N   
1905 C CA  . HIS A 258 ? 1.19605 1.21089 0.68793 0.03746  0.24983  0.03577  250 HIS A CA  
1906 C C   . HIS A 258 ? 1.17969 1.23160 0.71729 0.02060  0.24972  0.03089  250 HIS A C   
1907 O O   . HIS A 258 ? 1.25829 1.31588 0.81334 0.02671  0.22585  0.03296  250 HIS A O   
1908 C CB  . HIS A 258 ? 1.11458 1.16575 0.62942 0.05466  0.25473  0.02484  250 HIS A CB  
1909 C CG  . HIS A 258 ? 1.14493 1.16475 0.62553 0.07709  0.24148  0.02874  250 HIS A CG  
1910 N ND1 . HIS A 258 ? 1.22568 1.20021 0.65220 0.07837  0.25250  0.03392  250 HIS A ND1 
1911 C CD2 . HIS A 258 ? 1.16043 1.18479 0.65094 0.09850  0.21848  0.02747  250 HIS A CD2 
1912 C CE1 . HIS A 258 ? 1.15671 1.11277 0.56487 0.09969  0.23547  0.03459  250 HIS A CE1 
1913 N NE2 . HIS A 258 ? 1.19473 1.18057 0.64232 0.11144  0.21559  0.03072  250 HIS A NE2 
1914 N N   . GLN A 259 ? 1.19261 1.26673 0.74755 -0.00072 0.27639  0.02380  251 GLN A N   
1915 C CA  . GLN A 259 ? 1.17002 1.28025 0.76940 -0.02003 0.27884  0.01666  251 GLN A CA  
1916 C C   . GLN A 259 ? 1.16041 1.23056 0.73592 -0.02964 0.26432  0.02876  251 GLN A C   
1917 O O   . GLN A 259 ? 1.12200 1.21492 0.72944 -0.02876 0.24522  0.02613  251 GLN A O   
1918 C CB  . GLN A 259 ? 1.20824 1.33912 0.82262 -0.04450 0.31459  0.00683  251 GLN A CB  
1919 C CG  . GLN A 259 ? 1.16847 1.35451 0.82464 -0.03618 0.32844  -0.00998 251 GLN A CG  
1920 C CD  . GLN A 259 ? 1.23120 1.43507 0.90148 -0.06222 0.36797  -0.02093 251 GLN A CD  
1921 O OE1 . GLN A 259 ? 1.27391 1.47521 0.95161 -0.08883 0.38121  -0.02215 251 GLN A OE1 
1922 N NE2 . GLN A 259 ? 1.21026 1.43139 0.88448 -0.05555 0.38890  -0.02995 251 GLN A NE2 
1923 N N   . ARG A 260 ? 1.19878 1.20953 0.71795 -0.03689 0.27239  0.04096  252 ARG A N   
1924 C CA  . ARG A 260 ? 1.18683 1.15161 0.67621 -0.04262 0.25790  0.05280  252 ARG A CA  
1925 C C   . ARG A 260 ? 1.15304 1.12416 0.65840 -0.02309 0.22481  0.05480  252 ARG A C   
1926 O O   . ARG A 260 ? 1.15202 1.12874 0.67587 -0.03057 0.21311  0.05526  252 ARG A O   
1927 C CB  . ARG A 260 ? 1.30917 1.20581 0.72945 -0.04104 0.26358  0.06502  252 ARG A CB  
1928 C CG  . ARG A 260 ? 1.41119 1.27773 0.79971 -0.06608 0.29472  0.06777  252 ARG A CG  
1929 C CD  . ARG A 260 ? 1.56466 1.35424 0.87704 -0.06113 0.29346  0.08132  252 ARG A CD  
1930 N NE  . ARG A 260 ? 1.71346 1.47060 1.01095 -0.05421 0.26582  0.08966  252 ARG A NE  
1931 C CZ  . ARG A 260 ? 1.67243 1.36804 0.91259 -0.04197 0.25203  0.09964  252 ARG A CZ  
1932 N NH1 . ARG A 260 ? 1.68205 1.33666 0.86755 -0.03481 0.26216  0.10380  252 ARG A NH1 
1933 N NH2 . ARG A 260 ? 1.58099 1.25602 0.81852 -0.03592 0.22739  0.10428  252 ARG A NH2 
1934 N N   . LEU A 261 ? 1.16809 1.13602 0.66486 0.00007  0.21209  0.05534  253 LEU A N   
1935 C CA  . LEU A 261 ? 1.09565 1.06409 0.60312 0.01889  0.18389  0.05675  253 LEU A CA  
1936 C C   . LEU A 261 ? 1.06196 1.08041 0.62079 0.01929  0.17561  0.04821  253 LEU A C   
1937 O O   . LEU A 261 ? 1.09168 1.10454 0.65833 0.02157  0.15766  0.05071  253 LEU A O   
1938 C CB  . LEU A 261 ? 1.08701 1.04594 0.57756 0.04094  0.17753  0.05633  253 LEU A CB  
1939 C CG  . LEU A 261 ? 1.05530 1.00680 0.55098 0.05908  0.15205  0.05735  253 LEU A CG  
1940 C CD1 . LEU A 261 ? 0.99724 0.90536 0.46733 0.05707  0.13834  0.06503  253 LEU A CD1 
1941 C CD2 . LEU A 261 ? 0.98337 0.93134 0.46764 0.07894  0.14875  0.05440  253 LEU A CD2 
1942 N N   . ILE A 262 ? 1.00045 1.06485 0.59197 0.01790  0.18799  0.03753  254 ILE A N   
1943 C CA  . ILE A 262 ? 1.01317 1.12784 0.65364 0.02098  0.17838  0.02699  254 ILE A CA  
1944 C C   . ILE A 262 ? 1.06163 1.18038 0.71641 0.00013  0.17766  0.02657  254 ILE A C   
1945 O O   . ILE A 262 ? 1.04877 1.17900 0.72162 0.00538  0.15884  0.02480  254 ILE A O   
1946 C CB  . ILE A 262 ? 0.98549 1.14976 0.65980 0.02425  0.19249  0.01320  254 ILE A CB  
1947 C CG1 . ILE A 262 ? 0.97119 1.13009 0.63023 0.04596  0.19315  0.01298  254 ILE A CG1 
1948 C CG2 . ILE A 262 ? 0.96195 1.17665 0.68549 0.02833  0.17962  0.00090  254 ILE A CG2 
1949 C CD1 . ILE A 262 ? 0.92447 1.07577 0.58080 0.07013  0.16814  0.01551  254 ILE A CD1 
1950 N N   . PHE A 263 ? 1.07312 1.17874 0.71634 -0.02275 0.19819  0.02809  255 PHE A N   
1951 C CA  . PHE A 263 ? 1.02116 1.12604 0.67466 -0.04566 0.20100  0.02727  255 PHE A CA  
1952 C C   . PHE A 263 ? 1.05291 1.11837 0.68286 -0.04171 0.18063  0.03807  255 PHE A C   
1953 O O   . PHE A 263 ? 1.07737 1.15644 0.72873 -0.04828 0.16991  0.03452  255 PHE A O   
1954 C CB  . PHE A 263 ? 1.07435 1.16050 0.70924 -0.07040 0.22992  0.02846  255 PHE A CB  
1955 C CG  . PHE A 263 ? 1.11789 1.25260 0.79043 -0.08241 0.25333  0.01339  255 PHE A CG  
1956 C CD1 . PHE A 263 ? 1.13090 1.32212 0.86011 -0.08925 0.24924  -0.00229 255 PHE A CD1 
1957 C CD2 . PHE A 263 ? 1.13604 1.26016 0.78797 -0.08677 0.27955  0.01329  255 PHE A CD2 
1958 C CE1 . PHE A 263 ? 1.11755 1.35844 0.88848 -0.10009 0.27038  -0.01922 255 PHE A CE1 
1959 C CE2 . PHE A 263 ? 1.15253 1.32390 0.84348 -0.09877 0.30368  -0.00263 255 PHE A CE2 
1960 C CZ  . PHE A 263 ? 1.14390 1.37597 0.89757 -0.10554 0.29893  -0.01964 255 PHE A CZ  
1961 N N   . ARG A 264 ? 1.06340 1.08284 0.65220 -0.03083 0.17509  0.04921  256 ARG A N   
1962 C CA  . ARG A 264 ? 1.06715 1.04941 0.63579 -0.02510 0.15625  0.05769  256 ARG A CA  
1963 C C   . ARG A 264 ? 1.02088 1.02504 0.61440 -0.00891 0.13569  0.05385  256 ARG A C   
1964 O O   . ARG A 264 ? 1.06357 1.05685 0.65965 -0.01173 0.12384  0.05563  256 ARG A O   
1965 C CB  . ARG A 264 ? 1.15866 1.09199 0.68228 -0.01513 0.15399  0.06705  256 ARG A CB  
1966 C CG  . ARG A 264 ? 1.30449 1.19254 0.79124 -0.03016 0.16321  0.07473  256 ARG A CG  
1967 C CD  . ARG A 264 ? 1.32357 1.16352 0.76135 -0.01953 0.16237  0.08230  256 ARG A CD  
1968 N NE  . ARG A 264 ? 1.41862 1.24260 0.85087 0.00112  0.13894  0.08378  256 ARG A NE  
1969 C CZ  . ARG A 264 ? 1.35021 1.12864 0.74393 0.01159  0.12904  0.08891  256 ARG A CZ  
1970 N NH1 . ARG A 264 ? 1.44401 1.18142 0.79311 0.00494  0.13959  0.09510  256 ARG A NH1 
1971 N NH2 . ARG A 264 ? 1.15859 0.93096 0.55775 0.02888  0.10836  0.08686  256 ARG A NH2 
1972 N N   . LEU A 265 ? 1.04279 1.07349 0.65105 0.00740  0.13282  0.04861  257 LEU A N   
1973 C CA  . LEU A 265 ? 1.02550 1.07086 0.65023 0.02475  0.11486  0.04538  257 LEU A CA  
1974 C C   . LEU A 265 ? 1.06214 1.14369 0.71973 0.01848  0.10972  0.03697  257 LEU A C   
1975 O O   . LEU A 265 ? 1.00401 1.08153 0.66451 0.02638  0.09418  0.03703  257 LEU A O   
1976 C CB  . LEU A 265 ? 0.97255 1.03109 0.59870 0.04402  0.11494  0.04212  257 LEU A CB  
1977 C CG  . LEU A 265 ? 0.97534 0.99650 0.56935 0.05489  0.11319  0.04883  257 LEU A CG  
1978 C CD1 . LEU A 265 ? 0.94283 0.97818 0.53615 0.06857  0.12000  0.04461  257 LEU A CD1 
1979 C CD2 . LEU A 265 ? 0.90984 0.90754 0.49711 0.06571  0.09606  0.05192  257 LEU A CD2 
1980 N N   . LEU A 266 ? 1.02135 1.13573 0.70209 0.00456  0.12262  0.02892  258 LEU A N   
1981 C CA  . LEU A 266 ? 0.99139 1.14535 0.70794 -0.00237 0.11692  0.01761  258 LEU A CA  
1982 C C   . LEU A 266 ? 1.05137 1.18378 0.76064 -0.01772 0.11109  0.02131  258 LEU A C   
1983 O O   . LEU A 266 ? 1.05592 1.20752 0.78394 -0.01638 0.09760  0.01441  258 LEU A O   
1984 C CB  . LEU A 266 ? 0.99342 1.18780 0.73954 -0.01601 0.13543  0.00607  258 LEU A CB  
1985 C CG  . LEU A 266 ? 1.00646 1.23766 0.77402 0.00127  0.13781  -0.00323 258 LEU A CG  
1986 C CD1 . LEU A 266 ? 1.01431 1.27201 0.80082 -0.01490 0.16407  -0.01203 258 LEU A CD1 
1987 C CD2 . LEU A 266 ? 0.98054 1.25078 0.78062 0.01706  0.11743  -0.01511 258 LEU A CD2 
1988 N N   . LYS A 267 ? 1.07911 1.17090 0.75969 -0.03017 0.11978  0.03126  259 LYS A N   
1989 C CA  . LYS A 267 ? 1.03489 1.09824 0.70321 -0.04266 0.11436  0.03590  259 LYS A CA  
1990 C C   . LYS A 267 ? 1.09000 1.13321 0.74721 -0.02604 0.09565  0.04034  259 LYS A C   
1991 O O   . LYS A 267 ? 1.14240 1.18267 0.80411 -0.03111 0.08658  0.03831  259 LYS A O   
1992 C CB  . LYS A 267 ? 1.06503 1.08614 0.70159 -0.05609 0.12748  0.04527  259 LYS A CB  
1993 C CG  . LYS A 267 ? 1.09046 1.12058 0.73273 -0.07970 0.14882  0.04123  259 LYS A CG  
1994 C CD  . LYS A 267 ? 1.18813 1.16655 0.79166 -0.09328 0.15941  0.05129  259 LYS A CD  
1995 C CE  . LYS A 267 ? 1.24572 1.18472 0.81040 -0.07815 0.15833  0.06186  259 LYS A CE  
1996 N NZ  . LYS A 267 ? 1.36514 1.25263 0.88805 -0.09020 0.16941  0.07065  259 LYS A NZ  
1997 N N   . LEU A 268 ? 1.04756 1.07647 0.69045 -0.00789 0.09146  0.04518  260 LEU A N   
1998 C CA  . LEU A 268 ? 1.08750 1.09744 0.72122 0.00775  0.07718  0.04797  260 LEU A CA  
1999 C C   . LEU A 268 ? 1.05817 1.09619 0.70938 0.01971  0.06660  0.04079  260 LEU A C   
2000 O O   . LEU A 268 ? 1.02852 1.04885 0.67003 0.03031  0.05660  0.04244  260 LEU A O   
2001 C CB  . LEU A 268 ? 1.03929 1.02692 0.65465 0.02152  0.07756  0.05323  260 LEU A CB  
2002 C CG  . LEU A 268 ? 1.08723 1.03398 0.68006 0.01792  0.07713  0.05990  260 LEU A CG  
2003 C CD1 . LEU A 268 ? 1.15712 1.09302 0.73927 0.00065  0.08783  0.06303  260 LEU A CD1 
2004 C CD2 . LEU A 268 ? 1.10346 1.03286 0.68197 0.03292  0.07472  0.06208  260 LEU A CD2 
2005 N N   . GLU A 269 ? 0.94108 1.01954 0.61611 0.01877  0.06907  0.03227  261 GLU A N   
2006 C CA  . GLU A 269 ? 0.99376 1.10239 0.68694 0.03135  0.05633  0.02313  261 GLU A CA  
2007 C C   . GLU A 269 ? 0.98919 1.08605 0.66875 0.05531  0.04872  0.02580  261 GLU A C   
2008 O O   . GLU A 269 ? 1.07481 1.16228 0.74600 0.06691  0.03574  0.02488  261 GLU A O   
2009 C CB  . GLU A 269 ? 1.08096 1.18351 0.77361 0.02502  0.04510  0.02064  261 GLU A CB  
2010 C CG  . GLU A 269 ? 1.10461 1.21124 0.80695 0.00026  0.05266  0.01840  261 GLU A CG  
2011 C CD  . GLU A 269 ? 1.17731 1.27970 0.87946 -0.00569 0.04088  0.01416  261 GLU A CD  
2012 O OE1 . GLU A 269 ? 1.16463 1.28916 0.87736 0.00554  0.02673  0.00546  261 GLU A OE1 
2013 O OE2 . GLU A 269 ? 1.21045 1.28549 0.89968 -0.02029 0.04497  0.01906  261 GLU A OE2 
2014 N N   . VAL A 270 ? 0.97467 1.06854 0.64871 0.06218  0.05725  0.02875  262 VAL A N   
2015 C CA  . VAL A 270 ? 0.98029 1.06071 0.64069 0.08385  0.05217  0.03080  262 VAL A CA  
2016 C C   . VAL A 270 ? 0.94357 1.06006 0.62265 0.09994  0.04554  0.02119  262 VAL A C   
2017 O O   . VAL A 270 ? 0.92707 1.08286 0.63379 0.09266  0.04849  0.01229  262 VAL A O   
2018 C CB  . VAL A 270 ? 0.95703 1.01909 0.60310 0.08512  0.06250  0.03631  262 VAL A CB  
2019 C CG1 . VAL A 270 ? 0.96437 0.99317 0.59383 0.07105  0.06659  0.04387  262 VAL A CG1 
2020 C CG2 . VAL A 270 ? 0.96062 1.05236 0.62054 0.08312  0.07464  0.03153  262 VAL A CG2 
2021 N N   . GLN A 271 ? 0.91990 1.02240 0.58495 0.12100  0.03704  0.02187  263 GLN A N   
2022 C CA  . GLN A 271 ? 0.96981 1.09982 0.64716 0.14182  0.02979  0.01322  263 GLN A CA  
2023 C C   . GLN A 271 ? 0.99143 1.12606 0.66912 0.14847  0.04137  0.01335  263 GLN A C   
2024 O O   . GLN A 271 ? 0.96037 1.05961 0.61401 0.15080  0.04538  0.02121  263 GLN A O   
2025 C CB  . GLN A 271 ? 0.97768 1.08120 0.63180 0.16137  0.01494  0.01468  263 GLN A CB  
2026 C CG  . GLN A 271 ? 0.94557 1.04766 0.59741 0.15829  0.00206  0.01224  263 GLN A CG  
2027 C CD  . GLN A 271 ? 0.97518 1.03776 0.59267 0.17565  -0.00900 0.01599  263 GLN A CD  
2028 O OE1 . GLN A 271 ? 1.00951 1.02916 0.60077 0.17240  -0.00278 0.02473  263 GLN A OE1 
2029 N NE2 . GLN A 271 ? 0.97927 1.05467 0.59599 0.19457  -0.02533 0.00836  263 GLN A NE2 
2030 N N   . PHE A 272 ? 0.91464 1.09186 0.61992 0.15055  0.04722  0.00360  264 PHE A N   
2031 C CA  . PHE A 272 ? 0.86327 1.04801 0.56947 0.15628  0.06051  0.00208  264 PHE A CA  
2032 C C   . PHE A 272 ? 0.91184 1.09830 0.61405 0.18442  0.05093  -0.00263 264 PHE A C   
2033 O O   . PHE A 272 ? 0.94595 1.16318 0.66914 0.19767  0.03969  -0.01294 264 PHE A O   
2034 C CB  . PHE A 272 ? 0.92719 1.15510 0.66502 0.14204  0.07573  -0.00702 264 PHE A CB  
2035 C CG  . PHE A 272 ? 0.95479 1.17011 0.68698 0.11455  0.08889  -0.00064 264 PHE A CG  
2036 C CD1 . PHE A 272 ? 0.94863 1.16872 0.69111 0.09894  0.08346  -0.00118 264 PHE A CD1 
2037 C CD2 . PHE A 272 ? 0.93764 1.13151 0.64954 0.10553  0.10568  0.00592  264 PHE A CD2 
2038 C CE1 . PHE A 272 ? 0.94818 1.15212 0.68233 0.07462  0.09544  0.00484  264 PHE A CE1 
2039 C CE2 . PHE A 272 ? 0.93264 1.10846 0.63330 0.08233  0.11658  0.01228  264 PHE A CE2 
2040 C CZ  . PHE A 272 ? 0.96346 1.14420 0.67582 0.06684  0.11183  0.01187  264 PHE A CZ  
2041 N N   . ILE A 273 ? 0.92472 1.07745 0.60006 0.19387  0.05409  0.00381  265 ILE A N   
2042 C CA  . ILE A 273 ? 0.90270 1.04758 0.56757 0.22041  0.04716  0.00049  265 ILE A CA  
2043 C C   . ILE A 273 ? 0.89485 1.06006 0.56918 0.22545  0.06108  -0.00530 265 ILE A C   
2044 O O   . ILE A 273 ? 0.91282 1.06539 0.57680 0.21110  0.07491  -0.00024 265 ILE A O   
2045 C CB  . ILE A 273 ? 0.93600 1.02640 0.56429 0.22593  0.04213  0.01013  265 ILE A CB  
2046 C CG1 . ILE A 273 ? 0.89360 0.96291 0.51101 0.22139  0.03100  0.01477  265 ILE A CG1 
2047 C CG2 . ILE A 273 ? 0.93807 1.01438 0.55164 0.25103  0.03807  0.00716  265 ILE A CG2 
2048 C CD1 . ILE A 273 ? 0.84331 0.86063 0.42997 0.21919  0.03141  0.02330  265 ILE A CD1 
2049 N N   . ILE A 274 ? 0.88832 1.08268 0.58012 0.24607  0.05710  -0.01624 266 ILE A N   
2050 C CA  . ILE A 274 ? 0.85053 1.06275 0.54990 0.25573  0.07018  -0.02348 266 ILE A CA  
2051 C C   . ILE A 274 ? 0.95095 1.12787 0.62119 0.27954  0.06280  -0.02111 266 ILE A C   
2052 O O   . ILE A 274 ? 0.96448 1.14057 0.63388 0.30071  0.04705  -0.02513 266 ILE A O   
2053 C CB  . ILE A 274 ? 0.84959 1.12248 0.59409 0.26264  0.07217  -0.04016 266 ILE A CB  
2054 C CG1 . ILE A 274 ? 0.83479 1.14175 0.61047 0.23887  0.07654  -0.04427 266 ILE A CG1 
2055 C CG2 . ILE A 274 ? 0.90048 1.19151 0.65317 0.26841  0.09054  -0.04788 266 ILE A CG2 
2056 C CD1 . ILE A 274 ? 0.92354 1.22468 0.69414 0.21091  0.09955  -0.03843 266 ILE A CD1 
2057 N N   . THR A 275 ? 0.98598 1.13178 0.63068 0.27623  0.07306  -0.01523 267 THR A N   
2058 C CA  . THR A 275 ? 0.98053 1.09103 0.59722 0.29578  0.06961  -0.01419 267 THR A CA  
2059 C C   . THR A 275 ? 0.95694 1.08837 0.58093 0.30606  0.08272  -0.02315 267 THR A C   
2060 O O   . THR A 275 ? 0.93169 1.10036 0.57972 0.29455  0.09639  -0.02868 267 THR A O   
2061 C CB  . THR A 275 ? 0.91447 0.97393 0.49873 0.28459  0.06948  -0.00340 267 THR A CB  
2062 O OG1 . THR A 275 ? 0.98708 1.01311 0.54713 0.30270  0.06564  -0.00415 267 THR A OG1 
2063 C CG2 . THR A 275 ? 0.95759 1.01296 0.53578 0.26563  0.08275  0.00003  267 THR A CG2 
2064 N N   . GLY A 276 ? 1.01160 1.11836 0.61488 0.32635  0.08013  -0.02518 268 GLY A N   
2065 C CA  . GLY A 276 ? 1.08907 1.20989 0.69458 0.33927  0.09217  -0.03429 268 GLY A CA  
2066 C C   . GLY A 276 ? 1.07939 1.24886 0.71990 0.35817  0.09020  -0.04822 268 GLY A C   
2067 O O   . GLY A 276 ? 1.11631 1.31259 0.78168 0.35796  0.07940  -0.05100 268 GLY A O   
2068 N N   . THR A 277 ? 1.07466 1.25585 0.71800 0.37466  0.09961  -0.05810 269 THR A N   
2069 C CA  . THR A 277 ? 1.19283 1.42152 0.87188 0.39715  0.09811  -0.07463 269 THR A CA  
2070 C C   . THR A 277 ? 1.14114 1.42558 0.86078 0.38111  0.11869  -0.08514 269 THR A C   
2071 O O   . THR A 277 ? 1.14332 1.41829 0.85153 0.35531  0.13559  -0.07790 269 THR A O   
2072 C CB  . THR A 277 ? 1.21664 1.42606 0.87680 0.42439  0.09864  -0.08088 269 THR A CB  
2073 O OG1 . THR A 277 ? 1.17568 1.37300 0.81855 0.41319  0.11980  -0.07993 269 THR A OG1 
2074 C CG2 . THR A 277 ? 1.24372 1.39567 0.86348 0.43954  0.08069  -0.07186 269 THR A CG2 
2075 N N   . ASN A 278 ? 1.14451 1.48326 0.90919 0.39648  0.11743  -0.10264 270 ASN A N   
2076 C CA  . ASN A 278 ? 1.19190 1.59160 1.00537 0.38141  0.13793  -0.11685 270 ASN A CA  
2077 C C   . ASN A 278 ? 1.28314 1.68312 1.08789 0.37959  0.16603  -0.12229 270 ASN A C   
2078 O O   . ASN A 278 ? 1.30577 1.70395 1.10652 0.40632  0.16463  -0.13087 270 ASN A O   
2079 C CB  . ASN A 278 ? 1.17381 1.63357 1.04264 0.40081  0.12470  -0.13687 270 ASN A CB  
2080 C CG  . ASN A 278 ? 1.29467 1.81752 1.21937 0.37857  0.14175  -0.15101 270 ASN A CG  
2081 O OD1 . ASN A 278 ? 1.31406 1.83799 1.23598 0.35170  0.16983  -0.14824 270 ASN A OD1 
2082 N ND2 . ASN A 278 ? 1.37188 1.94526 1.34588 0.38952  0.12480  -0.16702 270 ASN A ND2 
2083 N N   . HIS A 279 ? 1.26686 1.66480 1.06458 0.34992  0.19060  -0.11738 271 HIS A N   
2084 C CA  . HIS A 279 ? 1.30305 1.69852 1.08751 0.34348  0.22133  -0.12213 271 HIS A CA  
2085 C C   . HIS A 279 ? 1.40450 1.86479 1.24391 0.33185  0.24645  -0.14111 271 HIS A C   
2086 O O   . HIS A 279 ? 1.49255 1.96264 1.33197 0.33379  0.27255  -0.15113 271 HIS A O   
2087 C CB  . HIS A 279 ? 1.20519 1.54509 0.93536 0.32015  0.23137  -0.10364 271 HIS A CB  
2088 C CG  . HIS A 279 ? 1.21729 1.49795 0.89930 0.33163  0.20988  -0.08926 271 HIS A CG  
2089 N ND1 . HIS A 279 ? 1.22271 1.46178 0.87308 0.31426  0.20008  -0.07233 271 HIS A ND1 
2090 C CD2 . HIS A 279 ? 1.24709 1.50364 0.90978 0.35806  0.19683  -0.09070 271 HIS A CD2 
2091 C CE1 . HIS A 279 ? 1.20307 1.39753 0.81968 0.32828  0.18298  -0.06498 271 HIS A CE1 
2092 N NE2 . HIS A 279 ? 1.22323 1.42550 0.84492 0.35452  0.18099  -0.07547 271 HIS A NE2 
2093 N N   . HIS A 280 ? 1.37244 1.87433 1.25670 0.31926  0.23997  -0.14690 272 HIS A N   
2094 C CA  . HIS A 280 ? 1.43712 2.01059 1.38757 0.30941  0.25926  -0.16935 272 HIS A CA  
2095 C C   . HIS A 280 ? 1.50194 2.12549 1.50335 0.34212  0.23669  -0.18930 272 HIS A C   
2096 O O   . HIS A 280 ? 1.46911 2.12882 1.51109 0.34155  0.21754  -0.19673 272 HIS A O   
2097 C CB  . HIS A 280 ? 1.35507 1.93993 1.32128 0.27505  0.26524  -0.16459 272 HIS A CB  
2098 C CG  . HIS A 280 ? 1.38818 1.91807 1.29895 0.24721  0.28462  -0.14487 272 HIS A CG  
2099 N ND1 . HIS A 280 ? 1.42723 1.89915 1.28764 0.24247  0.26530  -0.12214 272 HIS A ND1 
2100 C CD2 . HIS A 280 ? 1.43664 1.95748 1.33141 0.22440  0.32093  -0.14503 272 HIS A CD2 
2101 C CE1 . HIS A 280 ? 1.44833 1.87993 1.26614 0.21954  0.28613  -0.10969 272 HIS A CE1 
2102 N NE2 . HIS A 280 ? 1.47353 1.93092 1.30758 0.20805  0.32045  -0.12243 272 HIS A NE2 
2103 N N   . SER A 281 ? 1.67625 2.29876 1.67242 0.37076  0.23803  -0.19801 273 SER A N   
2104 C CA  . SER A 281 ? 1.74817 2.39787 1.77317 0.41050  0.21186  -0.21330 273 SER A CA  
2105 C C   . SER A 281 ? 1.73017 2.46557 1.83883 0.41413  0.21351  -0.24214 273 SER A C   
2106 O O   . SER A 281 ? 1.74512 2.50515 1.88141 0.44314  0.18199  -0.25325 273 SER A O   
2107 C CB  . SER A 281 ? 1.67861 2.30389 1.67555 0.43613  0.21910  -0.21609 273 SER A CB  
2108 O OG  . SER A 281 ? 1.64502 2.19365 1.56857 0.43190  0.21657  -0.19196 273 SER A OG  
2109 N N   . GLU A 282 ? 1.55285 2.33017 1.69929 0.38601  0.24864  -0.25473 274 GLU A N   
2110 C CA  . GLU A 282 ? 1.46535 2.33048 1.69975 0.38393  0.25641  -0.28594 274 GLU A CA  
2111 C C   . GLU A 282 ? 1.41397 2.30239 1.67793 0.36331  0.23958  -0.28557 274 GLU A C   
2112 O O   . GLU A 282 ? 1.34460 2.30255 1.67992 0.34923  0.25231  -0.30989 274 GLU A O   
2113 C CB  . GLU A 282 ? 1.40073 2.29461 1.65865 0.35928  0.30623  -0.29953 274 GLU A CB  
2114 C CG  . GLU A 282 ? 1.35966 2.23657 1.59341 0.38034  0.32455  -0.30373 274 GLU A CG  
2115 C CD  . GLU A 282 ? 1.43429 2.33712 1.68797 0.35635  0.37644  -0.31816 274 GLU A CD  
2116 O OE1 . GLU A 282 ? 1.43799 2.31626 1.66588 0.31813  0.40327  -0.30564 274 GLU A OE1 
2117 O OE2 . GLU A 282 ? 1.41227 2.35698 1.70481 0.37637  0.39075  -0.34210 274 GLU A OE2 
2118 N N   . LYS A 283 ? 1.43467 2.26839 1.64809 0.36122  0.21295  -0.26076 275 LYS A N   
2119 C CA  . LYS A 283 ? 1.43347 2.27785 1.66342 0.34245  0.19477  -0.25719 275 LYS A CA  
2120 C C   . LYS A 283 ? 1.50951 2.31727 1.70625 0.36958  0.14990  -0.24443 275 LYS A C   
2121 O O   . LYS A 283 ? 1.54787 2.29786 1.68707 0.38889  0.14064  -0.22763 275 LYS A O   
2122 C CB  . LYS A 283 ? 1.41839 2.22057 1.60866 0.30063  0.21799  -0.23562 275 LYS A CB  
2123 C CG  . LYS A 283 ? 1.32002 2.14757 1.53306 0.26860  0.26442  -0.24542 275 LYS A CG  
2124 C CD  . LYS A 283 ? 1.27420 2.17913 1.56874 0.25069  0.27413  -0.27231 275 LYS A CD  
2125 C CE  . LYS A 283 ? 1.17209 2.08144 1.47251 0.20755  0.32034  -0.27394 275 LYS A CE  
2126 N NZ  . LYS A 283 ? 1.16295 2.07463 1.45837 0.20797  0.35836  -0.28188 275 LYS A NZ  
2127 N N   . GLU A 284 ? 1.50391 2.34171 1.73374 0.36962  0.12437  -0.25271 276 GLU A N   
2128 C CA  . GLU A 284 ? 1.57992 2.37682 1.77223 0.38672  0.08466  -0.23829 276 GLU A CA  
2129 C C   . GLU A 284 ? 1.63639 2.36264 1.76335 0.35994  0.09195  -0.20711 276 GLU A C   
2130 O O   . GLU A 284 ? 1.67039 2.39380 1.79522 0.32627  0.12303  -0.20115 276 GLU A O   
2131 C CB  . GLU A 284 ? 1.58326 2.43511 1.83097 0.38868  0.06013  -0.25783 276 GLU A CB  
2132 C CG  . GLU A 284 ? 1.63465 2.44654 1.84416 0.40693  0.01960  -0.24565 276 GLU A CG  
2133 C CD  . GLU A 284 ? 1.69758 2.47735 1.87296 0.45263  -0.00844 -0.24365 276 GLU A CD  
2134 O OE1 . GLU A 284 ? 1.71892 2.54579 1.93718 0.48235  -0.01873 -0.26762 276 GLU A OE1 
2135 O OE2 . GLU A 284 ? 1.54594 2.25276 1.65234 0.45846  -0.01973 -0.21906 276 GLU A OE2 
2136 N N   . PHE A 285 ? 1.46670 2.13633 1.54139 0.37467  0.06527  -0.18878 277 PHE A N   
2137 C CA  . PHE A 285 ? 1.39905 1.99928 1.41159 0.35411  0.06922  -0.16043 277 PHE A CA  
2138 C C   . PHE A 285 ? 1.34722 1.95698 1.37305 0.32076  0.07179  -0.15642 277 PHE A C   
2139 O O   . PHE A 285 ? 1.22976 1.79442 1.21641 0.29653  0.08391  -0.13658 277 PHE A O   
2140 C CB  . PHE A 285 ? 1.34759 1.88907 1.30690 0.37962  0.04149  -0.14572 277 PHE A CB  
2141 C CG  . PHE A 285 ? 1.23552 1.70837 1.13369 0.37165  0.05254  -0.12281 277 PHE A CG  
2142 C CD1 . PHE A 285 ? 1.21591 1.65189 1.08498 0.34346  0.05812  -0.10474 277 PHE A CD1 
2143 C CD2 . PHE A 285 ? 1.23978 1.68631 1.11183 0.39281  0.05677  -0.12116 277 PHE A CD2 
2144 C CE1 . PHE A 285 ? 1.25732 1.63444 1.07562 0.33721  0.06634  -0.08668 277 PHE A CE1 
2145 C CE2 . PHE A 285 ? 1.24720 1.63315 1.06666 0.38507  0.06550  -0.10268 277 PHE A CE2 
2146 C CZ  . PHE A 285 ? 1.24548 1.59852 1.03994 0.35746  0.06974  -0.08612 277 PHE A CZ  
2147 N N   . CYS A 286 ? 1.36161 2.02735 1.44091 0.32063  0.05922  -0.17568 278 CYS A N   
2148 C CA  . CYS A 286 ? 1.35333 2.03753 1.45493 0.28869  0.06210  -0.17686 278 CYS A CA  
2149 C C   . CYS A 286 ? 1.41054 2.10600 1.52487 0.25231  0.10171  -0.17612 278 CYS A C   
2150 O O   . CYS A 286 ? 1.38682 2.06832 1.49316 0.22218  0.10918  -0.16703 278 CYS A O   
2151 C CB  . CYS A 286 ? 1.28643 2.03534 1.44949 0.29852  0.04067  -0.20271 278 CYS A CB  
2152 S SG  . CYS A 286 ? 1.33537 2.16940 1.57716 0.31262  0.05336  -0.23723 278 CYS A SG  
2153 N N   . SER A 287 ? 1.31729 2.03269 1.44644 0.25552  0.12663  -0.18513 279 SER A N   
2154 C CA  . SER A 287 ? 1.20226 1.91751 1.33104 0.22390  0.16771  -0.18312 279 SER A CA  
2155 C C   . SER A 287 ? 1.13250 1.77846 1.19789 0.20102  0.17496  -0.15498 279 SER A C   
2156 O O   . SER A 287 ? 1.12631 1.77170 1.19453 0.16778  0.19840  -0.15254 279 SER A O   
2157 C CB  . SER A 287 ? 1.19586 1.91859 1.32483 0.23841  0.18854  -0.19033 279 SER A CB  
2158 O OG  . SER A 287 ? 1.24283 1.90715 1.31246 0.26072  0.17671  -0.17214 279 SER A OG  
2159 N N   . TYR A 288 ? 1.07395 1.66320 1.08518 0.21840  0.15568  -0.13576 280 TYR A N   
2160 C CA  . TYR A 288 ? 1.09559 1.61892 1.04852 0.20187  0.15672  -0.11053 280 TYR A CA  
2161 C C   . TYR A 288 ? 1.13008 1.65231 1.08981 0.18441  0.14243  -0.10629 280 TYR A C   
2162 O O   . TYR A 288 ? 1.14557 1.64455 1.08764 0.15597  0.15743  -0.09577 280 TYR A O   
2163 C CB  . TYR A 288 ? 1.08883 1.55958 0.99193 0.22653  0.13982  -0.09597 280 TYR A CB  
2164 C CG  . TYR A 288 ? 1.08641 1.54715 0.97301 0.24075  0.15498  -0.09757 280 TYR A CG  
2165 C CD1 . TYR A 288 ? 1.04565 1.47212 0.89684 0.22445  0.17838  -0.08701 280 TYR A CD1 
2166 C CD2 . TYR A 288 ? 1.10197 1.58455 1.00516 0.27200  0.14487  -0.11012 280 TYR A CD2 
2167 C CE1 . TYR A 288 ? 1.09260 1.50739 0.92519 0.23767  0.19192  -0.08909 280 TYR A CE1 
2168 C CE2 . TYR A 288 ? 1.12526 1.59732 1.01229 0.28545  0.15905  -0.11232 280 TYR A CE2 
2169 C CZ  . TYR A 288 ? 1.15329 1.59169 1.00487 0.26767  0.18299  -0.10189 280 TYR A CZ  
2170 O OH  . TYR A 288 ? 1.19484 1.62062 1.02733 0.28114  0.19653  -0.10466 280 TYR A OH  
2171 N N   . LEU A 289 ? 1.10172 1.64494 1.08262 0.20198  0.11388  -0.11443 281 LEU A N   
2172 C CA  . LEU A 289 ? 1.05430 1.59940 1.04317 0.18841  0.09752  -0.11314 281 LEU A CA  
2173 C C   . LEU A 289 ? 1.08248 1.67688 1.12094 0.15958  0.11605  -0.12843 281 LEU A C   
2174 O O   . LEU A 289 ? 1.09326 1.66903 1.12082 0.13312  0.12111  -0.11985 281 LEU A O   
2175 C CB  . LEU A 289 ? 1.03267 1.59097 1.03184 0.21768  0.06290  -0.12154 281 LEU A CB  
2176 C CG  . LEU A 289 ? 1.00908 1.50997 0.95394 0.24249  0.04383  -0.10528 281 LEU A CG  
2177 C CD1 . LEU A 289 ? 0.91795 1.42676 0.86747 0.26877  0.01041  -0.11344 281 LEU A CD1 
2178 C CD2 . LEU A 289 ? 0.96434 1.40470 0.85986 0.22353  0.04856  -0.08228 281 LEU A CD2 
2179 N N   . GLN A 290 ? 1.08964 1.74418 1.18162 0.16440  0.12663  -0.15134 282 GLN A N   
2180 C CA  . GLN A 290 ? 1.06967 1.77814 1.21749 0.13624  0.14871  -0.17051 282 GLN A CA  
2181 C C   . GLN A 290 ? 1.05603 1.72642 1.17186 0.10053  0.18124  -0.15513 282 GLN A C   
2182 O O   . GLN A 290 ? 1.06162 1.74540 1.19814 0.07154  0.19063  -0.15997 282 GLN A O   
2183 C CB  . GLN A 290 ? 1.07977 1.85053 1.28291 0.14793  0.16247  -0.19588 282 GLN A CB  
2184 C CG  . GLN A 290 ? 1.11525 1.94533 1.37423 0.17411  0.13190  -0.22065 282 GLN A CG  
2185 C CD  . GLN A 290 ? 1.23770 2.13177 1.55542 0.18719  0.14554  -0.24764 282 GLN A CD  
2186 O OE1 . GLN A 290 ? 1.20414 2.10089 1.52332 0.17365  0.18146  -0.24888 282 GLN A OE1 
2187 N NE2 . GLN A 290 ? 1.22818 2.17353 1.59394 0.21500  0.11641  -0.27055 282 GLN A NE2 
2188 N N   . TYR A 291 ? 0.98362 1.60547 1.04840 0.10340  0.19633  -0.13777 283 TYR A N   
2189 C CA  . TYR A 291 ? 1.02902 1.60548 1.05264 0.07439  0.22516  -0.12188 283 TYR A CA  
2190 C C   . TYR A 291 ? 1.02731 1.55536 1.01287 0.06182  0.21002  -0.10277 283 TYR A C   
2191 O O   . TYR A 291 ? 1.06321 1.58054 1.04519 0.03145  0.22754  -0.09972 283 TYR A O   
2192 C CB  . TYR A 291 ? 1.05489 1.59193 1.03234 0.08558  0.23989  -0.11021 283 TYR A CB  
2193 C CG  . TYR A 291 ? 1.07666 1.57150 1.01362 0.05801  0.27097  -0.09789 283 TYR A CG  
2194 C CD1 . TYR A 291 ? 1.03489 1.55677 0.99785 0.03239  0.30568  -0.11054 283 TYR A CD1 
2195 C CD2 . TYR A 291 ? 1.09850 1.52484 0.97064 0.05738  0.26568  -0.07465 283 TYR A CD2 
2196 C CE1 . TYR A 291 ? 1.10415 1.57968 1.02204 0.00755  0.33478  -0.09847 283 TYR A CE1 
2197 C CE2 . TYR A 291 ? 1.10943 1.49264 0.93939 0.03491  0.29116  -0.06353 283 TYR A CE2 
2198 C CZ  . TYR A 291 ? 1.14318 1.54774 0.99215 0.01021  0.32599  -0.07447 283 TYR A CZ  
2199 O OH  . TYR A 291 ? 1.22230 1.57675 1.02169 -0.01114 0.35169  -0.06269 283 TYR A OH  
2200 N N   . LEU A 292 ? 1.04881 1.54666 1.00610 0.08387  0.18037  -0.09094 284 LEU A N   
2201 C CA  . LEU A 292 ? 1.07965 1.53410 1.00428 0.07511  0.16410  -0.07469 284 LEU A CA  
2202 C C   . LEU A 292 ? 1.09761 1.58646 1.06159 0.05722  0.15800  -0.08646 284 LEU A C   
2203 O O   . LEU A 292 ? 1.08678 1.54845 1.03317 0.03286  0.16481  -0.07726 284 LEU A O   
2204 C CB  . LEU A 292 ? 1.02768 1.45401 0.92528 0.10366  0.13499  -0.06536 284 LEU A CB  
2205 C CG  . LEU A 292 ? 1.04599 1.42430 0.89599 0.11705  0.13813  -0.05052 284 LEU A CG  
2206 C CD1 . LEU A 292 ? 0.97622 1.33177 0.80640 0.14388  0.11139  -0.04486 284 LEU A CD1 
2207 C CD2 . LEU A 292 ? 1.06714 1.39476 0.87539 0.09630  0.15035  -0.03356 284 LEU A CD2 
2208 N N   . GLU A 293 ? 1.05065 1.59623 1.06544 0.07030  0.14409  -0.10707 285 GLU A N   
2209 C CA  . GLU A 293 ? 1.01571 1.60400 1.07672 0.05609  0.13526  -0.12370 285 GLU A CA  
2210 C C   . GLU A 293 ? 1.02302 1.62777 1.10658 0.01930  0.16878  -0.13081 285 GLU A C   
2211 O O   . GLU A 293 ? 1.06539 1.65715 1.14576 -0.00457 0.16958  -0.12769 285 GLU A O   
2212 C CB  . GLU A 293 ? 1.00329 1.65292 1.11682 0.08085  0.11514  -0.14757 285 GLU A CB  
2213 C CG  . GLU A 293 ? 1.04867 1.67728 1.13695 0.11433  0.07858  -0.14145 285 GLU A CG  
2214 C CD  . GLU A 293 ? 1.11298 1.72465 1.18952 0.10900  0.05493  -0.13764 285 GLU A CD  
2215 O OE1 . GLU A 293 ? 1.11030 1.76227 1.22935 0.09241  0.05265  -0.15436 285 GLU A OE1 
2216 O OE2 . GLU A 293 ? 1.13261 1.69070 1.15815 0.12075  0.03986  -0.11910 285 GLU A OE2 
2217 N N   . TYR A 294 ? 1.01682 1.64521 1.11901 0.01486  0.19678  -0.13994 286 TYR A N   
2218 C CA  . TYR A 294 ? 1.04137 1.68007 1.15933 -0.02034 0.23573  -0.14674 286 TYR A CA  
2219 C C   . TYR A 294 ? 1.06021 1.62801 1.11608 -0.04283 0.24897  -0.12215 286 TYR A C   
2220 O O   . TYR A 294 ? 1.06668 1.63328 1.13171 -0.07412 0.26485  -0.12531 286 TYR A O   
2221 C CB  . TYR A 294 ? 0.99812 1.66122 1.13174 -0.01511 0.26305  -0.15696 286 TYR A CB  
2222 C CG  . TYR A 294 ? 1.03093 1.67337 1.14754 -0.04742 0.30734  -0.15391 286 TYR A CG  
2223 C CD1 . TYR A 294 ? 1.04889 1.72162 1.20562 -0.08153 0.33146  -0.16962 286 TYR A CD1 
2224 C CD2 . TYR A 294 ? 1.08427 1.67414 1.14216 -0.04389 0.32567  -0.13618 286 TYR A CD2 
2225 C CE1 . TYR A 294 ? 1.11728 1.76384 1.25183 -0.11194 0.37469  -0.16623 286 TYR A CE1 
2226 C CE2 . TYR A 294 ? 1.11472 1.67808 1.14801 -0.07197 0.36629  -0.13263 286 TYR A CE2 
2227 C CZ  . TYR A 294 ? 1.14022 1.73001 1.21008 -0.10639 0.39205  -0.14707 286 TYR A CZ  
2228 O OH  . TYR A 294 ? 1.23415 1.79123 1.27385 -0.13487 0.43451  -0.14306 286 TYR A OH  
2229 N N   . LEU A 295 ? 1.11663 1.62723 1.11253 -0.02679 0.24152  -0.09980 287 LEU A N   
2230 C CA  . LEU A 295 ? 1.15050 1.59041 1.08382 -0.04182 0.24962  -0.07640 287 LEU A CA  
2231 C C   . LEU A 295 ? 1.20902 1.63452 1.14024 -0.05450 0.23196  -0.07160 287 LEU A C   
2232 O O   . LEU A 295 ? 1.25010 1.65484 1.17034 -0.08334 0.25034  -0.06829 287 LEU A O   
2233 C CB  . LEU A 295 ? 1.12042 1.51275 1.00155 -0.01676 0.23737  -0.05825 287 LEU A CB  
2234 C CG  . LEU A 295 ? 1.11453 1.46936 0.95292 -0.02108 0.26377  -0.04881 287 LEU A CG  
2235 C CD1 . LEU A 295 ? 1.12556 1.52449 0.99811 -0.02582 0.29181  -0.06630 287 LEU A CD1 
2236 C CD2 . LEU A 295 ? 1.07711 1.39216 0.87210 0.00562  0.24702  -0.03469 287 LEU A CD2 
2237 N N   . SER A 296 ? 1.32073 1.75413 1.25951 -0.03380 0.19886  -0.07169 288 SER A N   
2238 C CA  . SER A 296 ? 1.26086 1.67600 1.19182 -0.04098 0.17880  -0.06632 288 SER A CA  
2239 C C   . SER A 296 ? 1.23020 1.68742 1.20874 -0.06579 0.18491  -0.08453 288 SER A C   
2240 O O   . SER A 296 ? 1.21137 1.64622 1.17838 -0.08098 0.17802  -0.07952 288 SER A O   
2241 C CB  . SER A 296 ? 1.21813 1.63207 1.14427 -0.01183 0.14516  -0.06402 288 SER A CB  
2242 O OG  . SER A 296 ? 1.24070 1.71372 1.21713 0.00150  0.13097  -0.08481 288 SER A OG  
2243 N N   . GLN A 297 ? 1.19368 1.71058 1.22590 -0.06968 0.19728  -0.10641 289 GLN A N   
2244 C CA  . GLN A 297 ? 1.20151 1.76717 1.28909 -0.09478 0.20532  -0.12859 289 GLN A CA  
2245 C C   . GLN A 297 ? 1.20313 1.75079 1.28226 -0.13089 0.24592  -0.12697 289 GLN A C   
2246 O O   . GLN A 297 ? 1.22534 1.80119 1.34256 -0.15816 0.25714  -0.14289 289 GLN A O   
2247 C CB  . GLN A 297 ? 1.21640 1.85882 1.37134 -0.07983 0.19785  -0.15601 289 GLN A CB  
2248 C CG  . GLN A 297 ? 1.32122 2.01170 1.52751 -0.08300 0.17431  -0.17757 289 GLN A CG  
2249 C CD  . GLN A 297 ? 1.39306 2.05785 1.57018 -0.05895 0.13447  -0.16729 289 GLN A CD  
2250 O OE1 . GLN A 297 ? 1.32970 1.96162 1.46651 -0.03155 0.12006  -0.15121 289 GLN A OE1 
2251 N NE2 . GLN A 297 ? 1.37167 2.04925 1.56766 -0.07011 0.11759  -0.17729 289 GLN A NE2 
2252 N N   . ASN A 298 ? 1.21919 1.71903 1.24801 -0.13104 0.26683  -0.10915 290 ASN A N   
2253 C CA  . ASN A 298 ? 1.24816 1.71882 1.25473 -0.16220 0.30747  -0.10501 290 ASN A CA  
2254 C C   . ASN A 298 ? 1.27062 1.65788 1.20072 -0.16659 0.30819  -0.07727 290 ASN A C   
2255 O O   . ASN A 298 ? 1.32612 1.67330 1.21861 -0.18424 0.33890  -0.06873 290 ASN A O   
2256 C CB  . ASN A 298 ? 1.25563 1.74655 1.27152 -0.15834 0.33500  -0.11257 290 ASN A CB  
2257 C CG  . ASN A 298 ? 1.24403 1.81654 1.34070 -0.16683 0.34694  -0.14381 290 ASN A CG  
2258 O OD1 . ASN A 298 ? 1.31344 1.90236 1.43715 -0.19997 0.37548  -0.15700 290 ASN A OD1 
2259 N ND2 . ASN A 298 ? 1.19467 1.81801 1.33103 -0.13707 0.32541  -0.15700 290 ASN A ND2 
2260 N N   . ARG A 299 ? 1.26806 1.62861 1.17497 -0.15103 0.27630  -0.06469 291 ARG A N   
2261 C CA  . ARG A 299 ? 1.27080 1.55874 1.11597 -0.15707 0.27330  -0.04239 291 ARG A CA  
2262 C C   . ARG A 299 ? 1.34289 1.62036 1.19308 -0.19157 0.28960  -0.04663 291 ARG A C   
2263 O O   . ARG A 299 ? 1.29664 1.62577 1.20158 -0.20599 0.29160  -0.06655 291 ARG A O   
2264 C CB  . ARG A 299 ? 1.26684 1.53843 1.09696 -0.13261 0.23677  -0.03234 291 ARG A CB  
2265 C CG  . ARG A 299 ? 1.27589 1.58039 1.14405 -0.13554 0.21521  -0.04405 291 ARG A CG  
2266 C CD  . ARG A 299 ? 1.14979 1.45801 1.01629 -0.10539 0.18146  -0.04071 291 ARG A CD  
2267 N NE  . ARG A 299 ? 1.16788 1.41886 0.98707 -0.09940 0.16834  -0.02213 291 ARG A NE  
2268 C CZ  . ARG A 299 ? 1.15016 1.39078 0.95805 -0.07652 0.14308  -0.01659 291 ARG A CZ  
2269 N NH1 . ARG A 299 ? 1.07797 1.35672 0.91250 -0.05598 0.12661  -0.02661 291 ARG A NH1 
2270 N NH2 . ARG A 299 ? 1.09686 1.28726 0.86603 -0.07397 0.13504  -0.00176 291 ARG A NH2 
2271 N N   . PRO A 300 ? 1.43704 1.64733 1.23112 -0.20558 0.30122  -0.02955 292 PRO A N   
2272 C CA  . PRO A 300 ? 1.45696 1.64980 1.25064 -0.23692 0.31377  -0.03229 292 PRO A CA  
2273 C C   . PRO A 300 ? 1.44241 1.66005 1.26718 -0.23288 0.28340  -0.03927 292 PRO A C   
2274 O O   . PRO A 300 ? 1.46735 1.67506 1.27855 -0.20732 0.25443  -0.03033 292 PRO A O   
2275 C CB  . PRO A 300 ? 1.50460 1.61319 1.22280 -0.24110 0.32258  -0.00961 292 PRO A CB  
2276 C CG  . PRO A 300 ? 1.44515 1.53179 1.13062 -0.20722 0.30189  0.00464  292 PRO A CG  
2277 C CD  . PRO A 300 ? 1.40844 1.55521 1.13666 -0.19117 0.30115  -0.00815 292 PRO A CD  
2278 N N   . PRO A 301 ? 1.45158 1.70241 1.31903 -0.25766 0.28921  -0.05669 293 PRO A N   
2279 C CA  . PRO A 301 ? 1.52340 1.79527 1.41661 -0.25385 0.25979  -0.06439 293 PRO A CA  
2280 C C   . PRO A 301 ? 1.62336 1.84441 1.48442 -0.27178 0.25775  -0.05544 293 PRO A C   
2281 O O   . PRO A 301 ? 1.60038 1.84385 1.49340 -0.29145 0.25587  -0.07015 293 PRO A O   
2282 C CB  . PRO A 301 ? 1.43454 1.78104 1.40038 -0.26911 0.26763  -0.09301 293 PRO A CB  
2283 C CG  . PRO A 301 ? 1.34441 1.67773 1.30637 -0.30182 0.31067  -0.09630 293 PRO A CG  
2284 C CD  . PRO A 301 ? 1.39924 1.67294 1.29608 -0.29050 0.32437  -0.07248 293 PRO A CD  
2285 N N   . PRO A 302 ? 1.80396 1.95546 1.60219 -0.26518 0.25724  -0.03265 294 PRO A N   
2286 C CA  . PRO A 302 ? 1.69849 1.80412 1.46717 -0.27153 0.24546  -0.02380 294 PRO A CA  
2287 C C   . PRO A 302 ? 1.60975 1.74438 1.40525 -0.25760 0.21304  -0.03158 294 PRO A C   
2288 O O   . PRO A 302 ? 1.53807 1.71442 1.35999 -0.23514 0.19529  -0.03778 294 PRO A O   
2289 C CB  . PRO A 302 ? 1.71763 1.75946 1.42422 -0.25329 0.24213  -0.00051 294 PRO A CB  
2290 C CG  . PRO A 302 ? 1.76766 1.80433 1.45959 -0.25478 0.26700  0.00300  294 PRO A CG  
2291 C CD  . PRO A 302 ? 1.74816 1.86033 1.50048 -0.25215 0.26867  -0.01594 294 PRO A CD  
2292 N N   . ASN A 303 ? 1.58031 1.68851 1.36451 -0.26982 0.20533  -0.03102 295 ASN A N   
2293 C CA  . ASN A 303 ? 1.53150 1.58348 1.27910 -0.29384 0.22433  -0.02270 295 ASN A CA  
2294 C C   . ASN A 303 ? 1.52394 1.57350 1.28293 -0.30904 0.21324  -0.03173 295 ASN A C   
2295 O O   . ASN A 303 ? 1.47753 1.56934 1.27061 -0.29893 0.19021  -0.04393 295 ASN A O   
2296 C CB  . ASN A 303 ? 1.50608 1.49050 1.19240 -0.27781 0.22105  0.00032  295 ASN A CB  
2297 C CG  . ASN A 303 ? 1.56110 1.48710 1.20247 -0.29731 0.24777  0.01076  295 ASN A CG  
2298 O OD1 . ASN A 303 ? 1.52925 1.39520 1.12384 -0.29279 0.24319  0.02480  295 ASN A OD1 
2299 N ND2 . ASN A 303 ? 1.67406 1.61494 1.32766 -0.31843 0.27617  0.00338  295 ASN A ND2 
2300 N N   . ALA A 304 ? 1.53526 1.53248 1.26192 -0.33108 0.22834  -0.02565 296 ALA A N   
2301 C CA  . ALA A 304 ? 1.57227 1.54553 1.29116 -0.34114 0.21658  -0.02835 296 ALA A CA  
2302 C C   . ALA A 304 ? 1.57496 1.52466 1.26810 -0.31103 0.18916  -0.01602 296 ALA A C   
2303 O O   . ALA A 304 ? 1.59035 1.56701 1.30562 -0.30256 0.16703  -0.02528 296 ALA A O   
2304 C CB  . ALA A 304 ? 1.58649 1.49913 1.26701 -0.36733 0.24044  -0.02137 296 ALA A CB  
2305 N N   . TYR A 305 ? 1.39958 1.30155 1.04802 -0.29500 0.19097  0.00288  297 TYR A N   
2306 C CA  . TYR A 305 ? 1.35637 1.22871 0.97803 -0.26832 0.16955  0.01481  297 TYR A CA  
2307 C C   . TYR A 305 ? 1.36500 1.28194 1.01160 -0.24225 0.15067  0.01193  297 TYR A C   
2308 O O   . TYR A 305 ? 1.40764 1.32815 1.05777 -0.22929 0.13078  0.00986  297 TYR A O   
2309 C CB  . TYR A 305 ? 1.30630 1.11952 0.87805 -0.25971 0.17768  0.03264  297 TYR A CB  
2310 C CG  . TYR A 305 ? 1.23397 1.01357 0.78059 -0.23567 0.15847  0.04264  297 TYR A CG  
2311 C CD1 . TYR A 305 ? 1.19485 0.99231 0.74775 -0.20898 0.14405  0.04630  297 TYR A CD1 
2312 C CD2 . TYR A 305 ? 1.24121 0.97039 0.75888 -0.23996 0.15594  0.04726  297 TYR A CD2 
2313 C CE1 . TYR A 305 ? 1.14165 0.91083 0.67650 -0.18888 0.12884  0.05310  297 TYR A CE1 
2314 C CE2 . TYR A 305 ? 1.19947 0.90123 0.69946 -0.21803 0.13959  0.05395  297 TYR A CE2 
2315 C CZ  . TYR A 305 ? 1.15574 0.87889 0.66608 -0.19323 0.12665  0.05634  297 TYR A CZ  
2316 O OH  . TYR A 305 ? 1.10210 0.80078 0.59989 -0.17360 0.11282  0.06062  297 TYR A OH  
2317 N N   . GLU A 306 ? 1.35992 1.30572 1.01973 -0.23493 0.15809  0.01184  298 GLU A N   
2318 C CA  . GLU A 306 ? 1.35143 1.32996 1.02620 -0.20781 0.14296  0.01196  298 GLU A CA  
2319 C C   . GLU A 306 ? 1.31201 1.34086 1.02596 -0.20379 0.12566  -0.00355 298 GLU A C   
2320 O O   . GLU A 306 ? 1.32422 1.35468 1.03411 -0.18157 0.10633  -0.00115 298 GLU A O   
2321 C CB  . GLU A 306 ? 1.44780 1.44518 1.12824 -0.20453 0.15796  0.01333  298 GLU A CB  
2322 C CG  . GLU A 306 ? 1.50347 1.44832 1.13876 -0.20378 0.17205  0.02888  298 GLU A CG  
2323 C CD  . GLU A 306 ? 1.58044 1.53963 1.21570 -0.19932 0.18715  0.03040  298 GLU A CD  
2324 O OE1 . GLU A 306 ? 1.53777 1.53981 1.20008 -0.18309 0.17869  0.02465  298 GLU A OE1 
2325 O OE2 . GLU A 306 ? 1.62852 1.55270 1.23335 -0.21158 0.20774  0.03726  298 GLU A OE2 
2326 N N   . LEU A 307 ? 1.29800 1.36499 1.04752 -0.22406 0.13223  -0.01979 299 LEU A N   
2327 C CA  . LEU A 307 ? 1.26384 1.38283 1.05333 -0.21946 0.11351  -0.03769 299 LEU A CA  
2328 C C   . LEU A 307 ? 1.30961 1.40567 1.08402 -0.21765 0.09492  -0.03844 299 LEU A C   
2329 O O   . LEU A 307 ? 1.28145 1.39915 1.06528 -0.19952 0.07288  -0.04486 299 LEU A O   
2330 C CB  . LEU A 307 ? 1.27101 1.43571 1.10542 -0.24438 0.12666  -0.05719 299 LEU A CB  
2331 C CG  . LEU A 307 ? 1.27814 1.50872 1.16169 -0.23416 0.10803  -0.07787 299 LEU A CG  
2332 C CD1 . LEU A 307 ? 1.20755 1.47537 1.11251 -0.21866 0.11345  -0.07991 299 LEU A CD1 
2333 C CD2 . LEU A 307 ? 1.24349 1.50988 1.16966 -0.26193 0.11213  -0.10067 299 LEU A CD2 
2334 N N   . PHE A 308 ? 1.29964 1.35025 1.04807 -0.23479 0.10378  -0.03225 300 PHE A N   
2335 C CA  . PHE A 308 ? 1.27572 1.29553 1.00367 -0.23370 0.08952  -0.03149 300 PHE A CA  
2336 C C   . PHE A 308 ? 1.26785 1.25615 0.96417 -0.20690 0.07849  -0.01684 300 PHE A C   
2337 O O   . PHE A 308 ? 1.22280 1.20198 0.90980 -0.19731 0.06244  -0.01920 300 PHE A O   
2338 C CB  . PHE A 308 ? 1.29139 1.26856 0.99944 -0.25892 0.10417  -0.02886 300 PHE A CB  
2339 C CG  . PHE A 308 ? 1.37830 1.37933 1.11539 -0.28725 0.10934  -0.04702 300 PHE A CG  
2340 C CD1 . PHE A 308 ? 1.37586 1.41886 1.14402 -0.28612 0.09014  -0.06514 300 PHE A CD1 
2341 C CD2 . PHE A 308 ? 1.38367 1.36115 1.11429 -0.31535 0.13306  -0.04677 300 PHE A CD2 
2342 C CE1 . PHE A 308 ? 1.34927 1.41640 1.14792 -0.31281 0.09362  -0.08434 300 PHE A CE1 
2343 C CE2 . PHE A 308 ? 1.41144 1.41037 1.17112 -0.34383 0.13955  -0.06509 300 PHE A CE2 
2344 C CZ  . PHE A 308 ? 1.38921 1.43555 1.18583 -0.34282 0.11927  -0.08472 300 PHE A CZ  
2345 N N   . ALA A 309 ? 1.26984 1.24107 0.94978 -0.19595 0.08758  -0.00339 301 ALA A N   
2346 C CA  . ALA A 309 ? 1.21420 1.15495 0.86740 -0.17275 0.08025  0.00951  301 ALA A CA  
2347 C C   . ALA A 309 ? 1.21185 1.18401 0.87769 -0.14960 0.06888  0.00824  301 ALA A C   
2348 O O   . ALA A 309 ? 1.17235 1.12286 0.81975 -0.13090 0.06315  0.01684  301 ALA A O   
2349 C CB  . ALA A 309 ? 1.21516 1.11920 0.84333 -0.17319 0.09395  0.02272  301 ALA A CB  
2350 N N   . LYS A 310 ? 1.15047 1.17110 0.84748 -0.15051 0.06585  -0.00322 302 LYS A N   
2351 C CA  . LYS A 310 ? 1.10569 1.15633 0.81435 -0.12742 0.05470  -0.00539 302 LYS A CA  
2352 C C   . LYS A 310 ? 1.07063 1.11208 0.76667 -0.11199 0.03543  -0.00750 302 LYS A C   
2353 O O   . LYS A 310 ? 1.09100 1.14749 0.79768 -0.11867 0.02468  -0.01936 302 LYS A O   
2354 C CB  . LYS A 310 ? 1.12387 1.22978 0.87208 -0.13246 0.05589  -0.01965 302 LYS A CB  
2355 C CG  . LYS A 310 ? 1.12840 1.26401 0.88839 -0.10817 0.04702  -0.02154 302 LYS A CG  
2356 C CD  . LYS A 310 ? 1.11650 1.22805 0.85435 -0.09451 0.05574  -0.00663 302 LYS A CD  
2357 C CE  . LYS A 310 ? 1.07837 1.21592 0.82589 -0.07069 0.04771  -0.00871 302 LYS A CE  
2358 N NZ  . LYS A 310 ? 1.06395 1.24800 0.84629 -0.07567 0.05690  -0.01933 302 LYS A NZ  
2359 N N   . GLY A 311 ? 1.06172 1.07728 0.73447 -0.09285 0.03213  0.00282  303 GLY A N   
2360 C CA  . GLY A 311 ? 1.04114 1.03846 0.69408 -0.07757 0.01841  0.00286  303 GLY A CA  
2361 C C   . GLY A 311 ? 1.06152 1.01137 0.68686 -0.07516 0.02444  0.01347  303 GLY A C   
2362 O O   . GLY A 311 ? 1.10142 1.03288 0.70880 -0.05977 0.01887  0.01607  303 GLY A O   
2363 N N   . TYR A 312 ? 0.98589 0.91511 0.60747 -0.08941 0.03593  0.01855  304 TYR A N   
2364 C CA  . TYR A 312 ? 1.07245 0.95813 0.67266 -0.08862 0.04066  0.02572  304 TYR A CA  
2365 C C   . TYR A 312 ? 1.01980 0.89319 0.61540 -0.07800 0.04722  0.03485  304 TYR A C   
2366 O O   . TYR A 312 ? 1.01023 0.85109 0.59309 -0.07578 0.05029  0.03924  304 TYR A O   
2367 C CB  . TYR A 312 ? 1.07579 0.94247 0.67180 -0.10856 0.04653  0.02456  304 TYR A CB  
2368 C CG  . TYR A 312 ? 1.07207 0.94253 0.66890 -0.11921 0.03940  0.01476  304 TYR A CG  
2369 C CD1 . TYR A 312 ? 1.07232 0.91415 0.65071 -0.11593 0.03529  0.01341  304 TYR A CD1 
2370 C CD2 . TYR A 312 ? 1.04746 0.95017 0.66440 -0.13314 0.03727  0.00524  304 TYR A CD2 
2371 C CE1 . TYR A 312 ? 1.08709 0.92924 0.66218 -0.12513 0.02792  0.00390  304 TYR A CE1 
2372 C CE2 . TYR A 312 ? 1.06962 0.97626 0.68800 -0.14281 0.02863  -0.00560 304 TYR A CE2 
2373 C CZ  . TYR A 312 ? 1.09587 0.97054 0.69080 -0.13833 0.02327  -0.00576 304 TYR A CZ  
2374 O OH  . TYR A 312 ? 1.19956 1.07541 0.79217 -0.14727 0.01395  -0.01694 304 TYR A OH  
2375 N N   . GLU A 313 ? 1.02747 0.92639 0.63401 -0.07073 0.04839  0.03615  305 GLU A N   
2376 C CA  . GLU A 313 ? 0.94872 0.83845 0.55063 -0.06184 0.05419  0.04367  305 GLU A CA  
2377 C C   . GLU A 313 ? 0.92603 0.79433 0.51805 -0.04575 0.05054  0.04632  305 GLU A C   
2378 O O   . GLU A 313 ? 1.00670 0.88440 0.59930 -0.03498 0.04502  0.04362  305 GLU A O   
2379 C CB  . GLU A 313 ? 0.98136 0.90485 0.59714 -0.05677 0.05623  0.04266  305 GLU A CB  
2380 C CG  . GLU A 313 ? 0.95659 0.90460 0.58715 -0.07409 0.06350  0.03802  305 GLU A CG  
2381 C CD  . GLU A 313 ? 1.10134 1.09222 0.75593 -0.07355 0.05656  0.02724  305 GLU A CD  
2382 O OE1 . GLU A 313 ? 1.06955 1.06155 0.72410 -0.07170 0.04537  0.02177  305 GLU A OE1 
2383 O OE2 . GLU A 313 ? 1.16618 1.18868 0.83881 -0.07376 0.06182  0.02341  305 GLU A OE2 
2384 N N   . ASP A 314 ? 0.90848 0.74775 0.49150 -0.04424 0.05353  0.05032  306 ASP A N   
2385 C CA  . ASP A 314 ? 0.95565 0.77519 0.53516 -0.03098 0.05214  0.05055  306 ASP A CA  
2386 C C   . ASP A 314 ? 0.95422 0.76456 0.53003 -0.02969 0.05056  0.04592  306 ASP A C   
2387 O O   . ASP A 314 ? 0.94606 0.74590 0.52049 -0.01920 0.05176  0.04455  306 ASP A O   
2388 C CB  . ASP A 314 ? 0.92432 0.75642 0.50772 -0.01725 0.05156  0.05233  306 ASP A CB  
2389 C CG  . ASP A 314 ? 1.00590 0.84000 0.58725 -0.01732 0.05400  0.05671  306 ASP A CG  
2390 O OD1 . ASP A 314 ? 0.92732 0.73969 0.50029 -0.02265 0.05505  0.05892  306 ASP A OD1 
2391 O OD2 . ASP A 314 ? 1.09252 0.94708 0.67762 -0.01123 0.05488  0.05770  306 ASP A OD2 
2392 N N   . TYR A 315 ? 0.90204 0.71338 0.47453 -0.04089 0.04904  0.04293  307 TYR A N   
2393 C CA  . TYR A 315 ? 0.95358 0.75122 0.51609 -0.04128 0.04773  0.03822  307 TYR A CA  
2394 C C   . TYR A 315 ? 0.90784 0.67568 0.46615 -0.04708 0.05235  0.03672  307 TYR A C   
2395 O O   . TYR A 315 ? 0.94600 0.70873 0.50395 -0.05880 0.05251  0.03699  307 TYR A O   
2396 C CB  . TYR A 315 ? 1.01158 0.82827 0.57305 -0.04891 0.04111  0.03395  307 TYR A CB  
2397 C CG  . TYR A 315 ? 1.07844 0.87732 0.62372 -0.05035 0.03849  0.02878  307 TYR A CG  
2398 C CD1 . TYR A 315 ? 1.12866 0.91978 0.65855 -0.03810 0.03609  0.02744  307 TYR A CD1 
2399 C CD2 . TYR A 315 ? 1.10597 0.89136 0.64682 -0.06387 0.03905  0.02522  307 TYR A CD2 
2400 C CE1 . TYR A 315 ? 1.14971 0.91914 0.65788 -0.03901 0.03461  0.02285  307 TYR A CE1 
2401 C CE2 . TYR A 315 ? 1.19054 0.95730 0.71321 -0.06500 0.03691  0.01990  307 TYR A CE2 
2402 C CZ  . TYR A 315 ? 1.17921 0.93749 0.68434 -0.05243 0.03484  0.01880  307 TYR A CZ  
2403 O OH  . TYR A 315 ? 1.38003 1.11487 0.86085 -0.05319 0.03365  0.01375  307 TYR A OH  
2404 N N   . LEU A 316 ? 0.87698 0.62522 0.43319 -0.03915 0.05702  0.03434  308 LEU A N   
2405 C CA  . LEU A 316 ? 0.94027 0.66189 0.49715 -0.04174 0.06193  0.03041  308 LEU A CA  
2406 C C   . LEU A 316 ? 1.02662 0.73512 0.56995 -0.05102 0.06293  0.02606  308 LEU A C   
2407 O O   . LEU A 316 ? 1.09207 0.80436 0.62290 -0.04998 0.06153  0.02451  308 LEU A O   
2408 C CB  . LEU A 316 ? 0.92657 0.63673 0.49080 -0.03128 0.06850  0.02641  308 LEU A CB  
2409 C CG  . LEU A 316 ? 0.86597 0.58691 0.44386 -0.02164 0.06642  0.02868  308 LEU A CG  
2410 C CD1 . LEU A 316 ? 0.84708 0.55791 0.43501 -0.01374 0.07407  0.02210  308 LEU A CD1 
2411 C CD2 . LEU A 316 ? 0.87145 0.58880 0.45591 -0.02216 0.06101  0.03061  308 LEU A CD2 
2412 N N   . GLN A 317 ? 0.99575 0.68691 0.53858 -0.05864 0.06411  0.02394  309 GLN A N   
2413 C CA  . GLN A 317 ? 0.99163 0.66558 0.52105 -0.06805 0.06556  0.01875  309 GLN A CA  
2414 C C   . GLN A 317 ? 0.98040 0.62736 0.51366 -0.06705 0.07138  0.01399  309 GLN A C   
2415 O O   . GLN A 317 ? 1.00040 0.64387 0.54430 -0.06356 0.06933  0.01615  309 GLN A O   
2416 C CB  . GLN A 317 ? 0.97471 0.65856 0.50000 -0.08174 0.05936  0.02016  309 GLN A CB  
2417 C CG  . GLN A 317 ? 1.04839 0.76543 0.57995 -0.08223 0.05331  0.02363  309 GLN A CG  
2418 C CD  . GLN A 317 ? 1.08148 0.81179 0.61359 -0.09771 0.04880  0.02124  309 GLN A CD  
2419 O OE1 . GLN A 317 ? 1.05438 0.80528 0.59734 -0.10327 0.04831  0.02417  309 GLN A OE1 
2420 N NE2 . GLN A 317 ? 1.08840 0.80668 0.60912 -0.10565 0.04653  0.01466  309 GLN A NE2 
2421 N N   . SER A 318 ? 1.01504 0.64223 0.53842 -0.06876 0.07796  0.00700  310 SER A N   
2422 C CA  . SER A 318 ? 1.03909 0.64078 0.56633 -0.06882 0.08371  0.00016  310 SER A CA  
2423 C C   . SER A 318 ? 1.09265 0.68521 0.61372 -0.07849 0.07732  0.00244  310 SER A C   
2424 O O   . SER A 318 ? 1.10722 0.70628 0.61579 -0.08966 0.07282  0.00464  310 SER A O   
2425 C CB  . SER A 318 ? 1.08169 0.66408 0.59552 -0.07025 0.09391  -0.00790 310 SER A CB  
2426 O OG  . SER A 318 ? 1.23487 0.82025 0.74976 -0.06277 0.10242  -0.00955 310 SER A OG  
2427 N N   . PRO A 319 ? 1.07034 0.64708 0.59955 -0.07433 0.07601  0.00143  311 PRO A N   
2428 C CA  . PRO A 319 ? 1.12229 0.68077 0.63930 -0.08369 0.07193  0.00350  311 PRO A CA  
2429 C C   . PRO A 319 ? 1.21628 0.75490 0.71876 -0.09304 0.07629  -0.00368 311 PRO A C   
2430 O O   . PRO A 319 ? 1.19292 0.71773 0.69904 -0.08670 0.08318  -0.01199 311 PRO A O   
2431 C CB  . PRO A 319 ? 1.07918 0.61962 0.60505 -0.07184 0.06871  0.00240  311 PRO A CB  
2432 C CG  . PRO A 319 ? 1.02268 0.58245 0.56979 -0.05769 0.06852  0.00123  311 PRO A CG  
2433 C CD  . PRO A 319 ? 1.07933 0.65360 0.62899 -0.05984 0.07706  -0.00257 311 PRO A CD  
2434 N N   . LEU A 320 ? 1.21318 0.75165 0.70086 -0.10833 0.07307  -0.00174 312 LEU A N   
2435 C CA  . LEU A 320 ? 1.21493 0.73293 0.68584 -0.11898 0.07522  -0.00904 312 LEU A CA  
2436 C C   . LEU A 320 ? 1.21669 0.69986 0.68489 -0.11503 0.07842  -0.01357 312 LEU A C   
2437 O O   . LEU A 320 ? 1.21010 0.68399 0.68275 -0.10984 0.07507  -0.00874 312 LEU A O   
2438 C CB  . LEU A 320 ? 1.13136 0.65794 0.59273 -0.13709 0.06978  -0.00724 312 LEU A CB  
2439 C CG  . LEU A 320 ? 1.19008 0.75203 0.65508 -0.14058 0.06442  -0.00641 312 LEU A CG  
2440 C CD1 . LEU A 320 ? 1.10036 0.67235 0.56246 -0.15970 0.05930  -0.00874 312 LEU A CD1 
2441 C CD2 . LEU A 320 ? 1.23661 0.79800 0.69138 -0.13360 0.06531  -0.01251 312 LEU A CD2 
2442 N N   . GLN A 321 ? 1.20073 0.66355 0.65959 -0.11591 0.08431  -0.02295 313 GLN A N   
2443 C CA  . GLN A 321 ? 1.18768 0.61565 0.64241 -0.11254 0.08764  -0.02977 313 GLN A CA  
2444 C C   . GLN A 321 ? 1.22984 0.63739 0.66088 -0.12822 0.08805  -0.03463 313 GLN A C   
2445 O O   . GLN A 321 ? 1.20757 0.60456 0.62870 -0.12877 0.09439  -0.04335 313 GLN A O   
2446 C CB  . GLN A 321 ? 1.11726 0.54065 0.58721 -0.09772 0.09698  -0.03926 313 GLN A CB  
2447 C CG  . GLN A 321 ? 1.08073 0.52897 0.57619 -0.08435 0.09676  -0.03654 313 GLN A CG  
2448 C CD  . GLN A 321 ? 1.14085 0.58244 0.65964 -0.06973 0.10490  -0.04821 313 GLN A CD  
2449 O OE1 . GLN A 321 ? 1.17516 0.59315 0.69227 -0.06788 0.11068  -0.05820 313 GLN A OE1 
2450 N NE2 . GLN A 321 ? 1.11272 0.57628 0.65602 -0.05929 0.10565  -0.04851 313 GLN A NE2 
2451 N N   . PRO A 322 ? 1.22433 0.62452 0.64421 -0.14242 0.08233  -0.02984 314 PRO A N   
2452 C CA  . PRO A 322 ? 1.20725 0.58885 0.60659 -0.15942 0.08193  -0.03582 314 PRO A CA  
2453 C C   . PRO A 322 ? 1.22628 0.56808 0.61307 -0.15575 0.08757  -0.04535 314 PRO A C   
2454 O O   . PRO A 322 ? 1.26087 0.58798 0.62966 -0.16788 0.08803  -0.05250 314 PRO A O   
2455 C CB  . PRO A 322 ? 1.20794 0.58523 0.60234 -0.17407 0.07803  -0.02876 314 PRO A CB  
2456 C CG  . PRO A 322 ? 1.17660 0.58366 0.58797 -0.16681 0.07555  -0.01847 314 PRO A CG  
2457 C CD  . PRO A 322 ? 1.15736 0.56533 0.58228 -0.14425 0.07744  -0.01924 314 PRO A CD  
2458 N N   . LEU A 323 ? 1.22591 0.55224 0.62350 -0.13867 0.09074  -0.04666 315 LEU A N   
2459 C CA  . LEU A 323 ? 1.25422 0.54488 0.64564 -0.13112 0.09656  -0.05730 315 LEU A CA  
2460 C C   . LEU A 323 ? 1.28574 0.58275 0.68134 -0.12472 0.10707  -0.06765 315 LEU A C   
2461 O O   . LEU A 323 ? 1.33143 0.60822 0.70658 -0.13263 0.11200  -0.07608 315 LEU A O   
2462 C CB  . LEU A 323 ? 1.25616 0.53252 0.66164 -0.11306 0.09335  -0.05599 315 LEU A CB  
2463 C CG  . LEU A 323 ? 1.28804 0.52718 0.69025 -0.10252 0.09698  -0.06745 315 LEU A CG  
2464 C CD1 . LEU A 323 ? 1.33096 0.53183 0.70174 -0.11749 0.09543  -0.06764 315 LEU A CD1 
2465 C CD2 . LEU A 323 ? 1.28726 0.51882 0.70797 -0.08037 0.09040  -0.06801 315 LEU A CD2 
2466 N N   . MET A 324 ? 1.21782 0.53907 0.63668 -0.11160 0.11144  -0.06752 316 MET A N   
2467 C CA  . MET A 324 ? 1.25804 0.58269 0.68190 -0.10501 0.12551  -0.07735 316 MET A CA  
2468 C C   . MET A 324 ? 1.22151 0.55124 0.61857 -0.11748 0.12709  -0.07668 316 MET A C   
2469 O O   . MET A 324 ? 1.24411 0.55523 0.62454 -0.11801 0.13865  -0.08644 316 MET A O   
2470 C CB  . MET A 324 ? 1.23708 0.58904 0.69234 -0.09139 0.12890  -0.07601 316 MET A CB  
2471 C CG  . MET A 324 ? 1.24308 0.59732 0.70443 -0.08642 0.14676  -0.08606 316 MET A CG  
2472 S SD  . MET A 324 ? 1.42839 0.81608 0.92761 -0.07383 0.15051  -0.08476 316 MET A SD  
2473 C CE  . MET A 324 ? 1.11813 0.53121 0.60054 -0.08248 0.13847  -0.06793 316 MET A CE  
2474 N N   . ASP A 325 ? 1.23697 0.59036 0.62956 -0.12590 0.11564  -0.06651 317 ASP A N   
2475 C CA  . ASP A 325 ? 1.21148 0.57498 0.58102 -0.13510 0.11173  -0.06590 317 ASP A CA  
2476 C C   . ASP A 325 ? 1.22991 0.58951 0.58411 -0.15186 0.09948  -0.06539 317 ASP A C   
2477 O O   . ASP A 325 ? 1.25104 0.61217 0.61664 -0.15695 0.09375  -0.05992 317 ASP A O   
2478 C CB  . ASP A 325 ? 1.17888 0.57739 0.56031 -0.13041 0.10720  -0.05700 317 ASP A CB  
2479 C CG  . ASP A 325 ? 1.21235 0.61698 0.61067 -0.11605 0.11949  -0.05773 317 ASP A CG  
2480 O OD1 . ASP A 325 ? 1.19318 0.57867 0.57896 -0.11248 0.13348  -0.06610 317 ASP A OD1 
2481 O OD2 . ASP A 325 ? 1.26235 0.68980 0.68554 -0.10940 0.11599  -0.05070 317 ASP A OD2 
2482 N N   . ASN A 326 ? 1.25354 0.60641 0.58129 -0.16029 0.09582  -0.07171 318 ASN A N   
2483 C CA  . ASN A 326 ? 1.26957 0.62690 0.58665 -0.17767 0.08245  -0.07384 318 ASN A CA  
2484 C C   . ASN A 326 ? 1.24240 0.64169 0.57265 -0.17987 0.07079  -0.06704 318 ASN A C   
2485 O O   . ASN A 326 ? 1.23989 0.65185 0.56178 -0.17105 0.06917  -0.06677 318 ASN A O   
2486 C CB  . ASN A 326 ? 1.30925 0.64224 0.59273 -0.18410 0.08077  -0.08577 318 ASN A CB  
2487 C CG  . ASN A 326 ? 1.34110 0.63213 0.61132 -0.18545 0.09090  -0.09392 318 ASN A CG  
2488 O OD1 . ASN A 326 ? 1.33995 0.61929 0.62451 -0.18659 0.09407  -0.09140 318 ASN A OD1 
2489 N ND2 . ASN A 326 ? 1.38214 0.64711 0.62149 -0.18437 0.09577  -0.10404 318 ASN A ND2 
2490 N N   . LEU A 327 ? 1.23087 0.64829 0.57929 -0.19083 0.06430  -0.06206 319 LEU A N   
2491 C CA  . LEU A 327 ? 1.20548 0.66569 0.57131 -0.19403 0.05429  -0.05704 319 LEU A CA  
2492 C C   . LEU A 327 ? 1.22258 0.69608 0.57499 -0.20148 0.04108  -0.06697 319 LEU A C   
2493 O O   . LEU A 327 ? 1.25545 0.70661 0.59020 -0.21251 0.03829  -0.07711 319 LEU A O   
2494 C CB  . LEU A 327 ? 1.19892 0.66830 0.58357 -0.20687 0.05422  -0.05146 319 LEU A CB  
2495 C CG  . LEU A 327 ? 1.18426 0.64246 0.57980 -0.19700 0.06306  -0.04101 319 LEU A CG  
2496 C CD1 . LEU A 327 ? 1.18980 0.64851 0.59332 -0.21118 0.06387  -0.03560 319 LEU A CD1 
2497 C CD2 . LEU A 327 ? 1.14913 0.63244 0.55897 -0.17939 0.06390  -0.03366 319 LEU A CD2 
2498 N N   . GLU A 328 ? 1.20349 0.71099 0.56332 -0.19431 0.03196  -0.06496 320 GLU A N   
2499 C CA  . GLU A 328 ? 1.21991 0.74387 0.56763 -0.19624 0.01524  -0.07501 320 GLU A CA  
2500 C C   . GLU A 328 ? 1.22193 0.77301 0.59241 -0.21632 0.00490  -0.08231 320 GLU A C   
2501 O O   . GLU A 328 ? 1.20658 0.76574 0.60054 -0.22650 0.01291  -0.07624 320 GLU A O   
2502 C CB  . GLU A 328 ? 1.20110 0.74900 0.54865 -0.17879 0.00927  -0.06992 320 GLU A CB  
2503 C CG  . GLU A 328 ? 1.22898 0.74956 0.55640 -0.16165 0.02300  -0.06336 320 GLU A CG  
2504 C CD  . GLU A 328 ? 1.32373 0.86003 0.64485 -0.14482 0.01868  -0.05826 320 GLU A CD  
2505 O OE1 . GLU A 328 ? 1.33945 0.91337 0.67894 -0.14406 0.00520  -0.05766 320 GLU A OE1 
2506 O OE2 . GLU A 328 ? 1.48849 0.99811 0.78640 -0.13274 0.03006  -0.05561 320 GLU A OE2 
2507 N N   . SER A 329 ? 1.24421 0.80696 0.60675 -0.22188 -0.01199 -0.09594 321 SER A N   
2508 C CA  . SER A 329 ? 1.25197 0.84183 0.63864 -0.24330 -0.02244 -0.10798 321 SER A CA  
2509 C C   . SER A 329 ? 1.21887 0.85793 0.64577 -0.24568 -0.02366 -0.10341 321 SER A C   
2510 O O   . SER A 329 ? 1.21362 0.86291 0.66518 -0.26527 -0.01594 -0.10416 321 SER A O   
2511 C CB  . SER A 329 ? 1.28325 0.87776 0.65353 -0.24423 -0.04335 -0.12526 321 SER A CB  
2512 O OG  . SER A 329 ? 1.29068 0.91428 0.69006 -0.26625 -0.05296 -0.13956 321 SER A OG  
2513 N N   . GLN A 330 ? 1.23558 0.90032 0.66602 -0.22657 -0.03142 -0.09891 322 GLN A N   
2514 C CA  . GLN A 330 ? 1.18239 0.89588 0.64999 -0.22541 -0.03352 -0.09560 322 GLN A CA  
2515 C C   . GLN A 330 ? 1.20433 0.91102 0.68530 -0.22804 -0.01302 -0.07972 322 GLN A C   
2516 O O   . GLN A 330 ? 1.26008 0.99915 0.77245 -0.23802 -0.00939 -0.07911 322 GLN A O   
2517 C CB  . GLN A 330 ? 1.16795 0.90135 0.62878 -0.20121 -0.04646 -0.09377 322 GLN A CB  
2518 C CG  . GLN A 330 ? 1.19537 0.96601 0.66812 -0.20021 -0.07117 -0.11112 322 GLN A CG  
2519 C CD  . GLN A 330 ? 1.30661 1.09902 0.77613 -0.17538 -0.08370 -0.10813 322 GLN A CD  
2520 O OE1 . GLN A 330 ? 1.37496 1.17091 0.84962 -0.16408 -0.07255 -0.09384 322 GLN A OE1 
2521 N NE2 . GLN A 330 ? 1.30151 1.10676 0.76054 -0.16572 -0.10849 -0.12244 322 GLN A NE2 
2522 N N   . THR A 331 ? 1.17573 0.84231 0.63399 -0.21876 -0.00039 -0.06863 323 THR A N   
2523 C CA  . THR A 331 ? 1.16358 0.81645 0.62939 -0.21875 0.01641  -0.05478 323 THR A CA  
2524 C C   . THR A 331 ? 1.14732 0.79258 0.62351 -0.24277 0.02406  -0.05736 323 THR A C   
2525 O O   . THR A 331 ? 1.19406 0.85671 0.68969 -0.24920 0.03142  -0.05119 323 THR A O   
2526 C CB  . THR A 331 ? 1.15513 0.76600 0.59706 -0.20509 0.02603  -0.04762 323 THR A CB  
2527 O OG1 . THR A 331 ? 1.13823 0.75598 0.57158 -0.18497 0.02259  -0.04469 323 THR A OG1 
2528 C CG2 . THR A 331 ? 1.11569 0.70988 0.56423 -0.20387 0.03929  -0.03619 323 THR A CG2 
2529 N N   . TYR A 332 ? 1.17242 0.78906 0.63285 -0.25581 0.02356  -0.06630 324 TYR A N   
2530 C CA  . TYR A 332 ? 1.19446 0.79842 0.66044 -0.28142 0.03083  -0.07114 324 TYR A CA  
2531 C C   . TYR A 332 ? 1.22666 0.87920 0.72649 -0.29729 0.02732  -0.07893 324 TYR A C   
2532 O O   . TYR A 332 ? 1.32172 0.97711 0.83455 -0.30960 0.04036  -0.07295 324 TYR A O   
2533 C CB  . TYR A 332 ? 1.23146 0.80357 0.67616 -0.29212 0.02678  -0.08334 324 TYR A CB  
2534 C CG  . TYR A 332 ? 1.24834 0.76757 0.66315 -0.28261 0.03529  -0.07747 324 TYR A CG  
2535 C CD1 . TYR A 332 ? 1.25517 0.74238 0.66410 -0.28405 0.04902  -0.06685 324 TYR A CD1 
2536 C CD2 . TYR A 332 ? 1.26255 0.76161 0.65338 -0.27176 0.02957  -0.08385 324 TYR A CD2 
2537 C CE1 . TYR A 332 ? 1.27166 0.71316 0.65745 -0.27350 0.05529  -0.06378 324 TYR A CE1 
2538 C CE2 . TYR A 332 ? 1.27872 0.73211 0.64638 -0.26316 0.03892  -0.08073 324 TYR A CE2 
2539 C CZ  . TYR A 332 ? 1.28166 0.70838 0.64964 -0.26353 0.05106  -0.07132 324 TYR A CZ  
2540 O OH  . TYR A 332 ? 1.29810 0.68277 0.64740 -0.25307 0.05876  -0.07035 324 TYR A OH  
2541 N N   . GLU A 333 ? 1.18293 0.87199 0.69576 -0.29548 0.01021  -0.09245 325 GLU A N   
2542 C CA  . GLU A 333 ? 1.17736 0.91807 0.72841 -0.31111 0.00363  -0.10615 325 GLU A CA  
2543 C C   . GLU A 333 ? 1.20657 0.97373 0.78304 -0.31260 0.01676  -0.09610 325 GLU A C   
2544 O O   . GLU A 333 ? 1.27440 1.05931 0.87611 -0.33643 0.02626  -0.10331 325 GLU A O   
2545 C CB  . GLU A 333 ? 1.17128 0.94830 0.72953 -0.29667 -0.02030 -0.11881 325 GLU A CB  
2546 C CG  . GLU A 333 ? 1.17174 1.00334 0.77294 -0.31249 -0.03078 -0.13832 325 GLU A CG  
2547 C CD  . GLU A 333 ? 1.16967 1.03776 0.77781 -0.29483 -0.05821 -0.15208 325 GLU A CD  
2548 O OE1 . GLU A 333 ? 1.15415 1.02041 0.74417 -0.26788 -0.06481 -0.14160 325 GLU A OE1 
2549 O OE2 . GLU A 333 ? 1.18692 1.08370 0.81779 -0.30779 -0.07347 -0.17410 325 GLU A OE2 
2550 N N   . VAL A 334 ? 1.13459 0.90289 0.70405 -0.28932 0.01864  -0.08108 326 VAL A N   
2551 C CA  . VAL A 334 ? 1.20124 0.99958 0.79380 -0.28632 0.02780  -0.07270 326 VAL A CA  
2552 C C   . VAL A 334 ? 1.24129 1.00492 0.82266 -0.29799 0.04940  -0.05985 326 VAL A C   
2553 O O   . VAL A 334 ? 1.31218 1.09534 0.90919 -0.30007 0.05972  -0.05396 326 VAL A O   
2554 C CB  . VAL A 334 ? 1.18054 0.99140 0.76827 -0.25689 0.02072  -0.06258 326 VAL A CB  
2555 C CG1 . VAL A 334 ? 1.12804 0.96168 0.71557 -0.24238 -0.00084 -0.07348 326 VAL A CG1 
2556 C CG2 . VAL A 334 ? 1.16189 0.92697 0.71898 -0.24182 0.02891  -0.04652 326 VAL A CG2 
2557 N N   . PHE A 335 ? 1.21986 0.93152 0.77228 -0.30344 0.05565  -0.05566 327 PHE A N   
2558 C CA  . PHE A 335 ? 1.20112 0.86940 0.73337 -0.30874 0.07318  -0.04213 327 PHE A CA  
2559 C C   . PHE A 335 ? 1.29961 0.93858 0.82403 -0.33761 0.08387  -0.04910 327 PHE A C   
2560 O O   . PHE A 335 ? 1.34649 0.93877 0.84573 -0.34176 0.09720  -0.03843 327 PHE A O   
2561 C CB  . PHE A 335 ? 1.15172 0.78128 0.65608 -0.28505 0.07121  -0.03017 327 PHE A CB  
2562 C CG  . PHE A 335 ? 1.19964 0.85175 0.71093 -0.25998 0.06645  -0.02129 327 PHE A CG  
2563 C CD1 . PHE A 335 ? 1.09715 0.76593 0.61866 -0.25731 0.07395  -0.01253 327 PHE A CD1 
2564 C CD2 . PHE A 335 ? 1.14656 0.79984 0.65158 -0.23987 0.05612  -0.02203 327 PHE A CD2 
2565 C CE1 . PHE A 335 ? 1.06516 0.75310 0.59262 -0.23486 0.06947  -0.00524 327 PHE A CE1 
2566 C CE2 . PHE A 335 ? 1.06476 0.73591 0.57557 -0.21865 0.05335  -0.01453 327 PHE A CE2 
2567 C CZ  . PHE A 335 ? 1.04875 0.73799 0.57178 -0.21604 0.05918  -0.00637 327 PHE A CZ  
2568 N N   . GLU A 336 ? 1.26691 0.93112 0.81151 -0.35675 0.07787  -0.06704 328 GLU A N   
2569 C CA  . GLU A 336 ? 1.24771 0.89258 0.79288 -0.38921 0.08978  -0.07691 328 GLU A CA  
2570 C C   . GLU A 336 ? 1.30845 1.00021 0.89228 -0.41035 0.09963  -0.08614 328 GLU A C   
2571 O O   . GLU A 336 ? 1.34516 1.02936 0.93719 -0.44073 0.11166  -0.09710 328 GLU A O   
2572 C CB  . GLU A 336 ? 1.28150 0.91960 0.82360 -0.39833 0.07675  -0.09356 328 GLU A CB  
2573 C CG  . GLU A 336 ? 1.24209 0.93004 0.80633 -0.38582 0.05371  -0.10703 328 GLU A CG  
2574 C CD  . GLU A 336 ? 1.28275 0.96205 0.83995 -0.39444 0.03934  -0.12468 328 GLU A CD  
2575 O OE1 . GLU A 336 ? 1.29591 0.92210 0.82037 -0.39743 0.04401  -0.12167 328 GLU A OE1 
2576 O OE2 . GLU A 336 ? 1.26079 0.98582 0.84430 -0.39652 0.02221  -0.14219 328 GLU A OE2 
2577 N N   . LYS A 337 ? 1.61002 1.34699 1.21698 -0.39529 0.09633  -0.08249 329 LYS A N   
2578 C CA  . LYS A 337 ? 1.64073 1.43215 1.29096 -0.41094 0.10443  -0.09317 329 LYS A CA  
2579 C C   . LYS A 337 ? 1.60385 1.38292 1.24423 -0.40913 0.12544  -0.07632 329 LYS A C   
2580 O O   . LYS A 337 ? 1.61454 1.44148 1.28882 -0.41302 0.13150  -0.08185 329 LYS A O   
2581 C CB  . LYS A 337 ? 1.61473 1.46966 1.29948 -0.39306 0.08167  -0.10489 329 LYS A CB  
2582 C CG  . LYS A 337 ? 1.56209 1.41600 1.22899 -0.35706 0.06893  -0.08985 329 LYS A CG  
2583 C CD  . LYS A 337 ? 1.57910 1.49455 1.28025 -0.34107 0.05628  -0.09653 329 LYS A CD  
2584 C CE  . LYS A 337 ? 1.55327 1.46174 1.23414 -0.30800 0.04821  -0.08033 329 LYS A CE  
2585 N NZ  . LYS A 337 ? 1.50372 1.46760 1.21515 -0.29242 0.03756  -0.08605 329 LYS A NZ  
2586 N N   . ASP A 338 ? 1.33314 1.05019 0.92840 -0.40223 0.13521  -0.05769 330 ASP A N   
2587 C CA  . ASP A 338 ? 1.27450 0.96727 0.84917 -0.39905 0.15385  -0.04071 330 ASP A CA  
2588 C C   . ASP A 338 ? 1.28040 0.93240 0.83770 -0.43112 0.17916  -0.04134 330 ASP A C   
2589 O O   . ASP A 338 ? 1.31761 0.90475 0.83187 -0.43263 0.18461  -0.03161 330 ASP A O   
2590 C CB  . ASP A 338 ? 1.24239 0.89298 0.77866 -0.36906 0.14604  -0.02176 330 ASP A CB  
2591 C CG  . ASP A 338 ? 1.21028 0.85741 0.73527 -0.35553 0.15534  -0.00688 330 ASP A CG  
2592 O OD1 . ASP A 338 ? 1.24534 0.89306 0.77199 -0.37421 0.17542  -0.00653 330 ASP A OD1 
2593 O OD2 . ASP A 338 ? 1.18405 0.82773 0.69878 -0.32712 0.14328  0.00317  330 ASP A OD2 
2594 N N   . PRO A 339 ? 1.18944 1.06761 0.65158 -0.38972 0.10642  -0.00797 331 PRO A N   
2595 C CA  . PRO A 339 ? 1.22103 1.08130 0.65366 -0.41995 0.11839  -0.00813 331 PRO A CA  
2596 C C   . PRO A 339 ? 1.28476 1.10988 0.67344 -0.42406 0.13415  -0.00275 331 PRO A C   
2597 O O   . PRO A 339 ? 1.36479 1.15087 0.71068 -0.44341 0.13902  0.00301  331 PRO A O   
2598 C CB  . PRO A 339 ? 1.14319 1.06256 0.62658 -0.43761 0.12518  -0.02176 331 PRO A CB  
2599 C CG  . PRO A 339 ? 1.10217 1.06504 0.63429 -0.41418 0.12430  -0.02918 331 PRO A CG  
2600 C CD  . PRO A 339 ? 1.12397 1.06394 0.64858 -0.38568 0.10648  -0.01989 331 PRO A CD  
2601 N N   . ILE A 340 ? 1.20078 1.03825 0.59969 -0.40597 0.14029  -0.00434 332 ILE A N   
2602 C CA  . ILE A 340 ? 1.23608 1.04266 0.59426 -0.40762 0.15348  0.00091  332 ILE A CA  
2603 C C   . ILE A 340 ? 1.22362 0.96598 0.52929 -0.39838 0.14434  0.01469  332 ILE A C   
2604 O O   . ILE A 340 ? 1.33058 1.03197 0.59027 -0.41503 0.15082  0.02161  332 ILE A O   
2605 C CB  . ILE A 340 ? 1.22010 1.05488 0.60335 -0.38728 0.15913  -0.00470 332 ILE A CB  
2606 C CG1 . ILE A 340 ? 1.19354 1.09521 0.64163 -0.38677 0.16267  -0.02014 332 ILE A CG1 
2607 C CG2 . ILE A 340 ? 1.19214 1.00317 0.53539 -0.39645 0.17437  -0.00140 332 ILE A CG2 
2608 C CD1 . ILE A 340 ? 1.21928 1.15216 0.68009 -0.41692 0.18038  -0.03093 332 ILE A CD1 
2609 N N   . LYS A 341 ? 1.17599 0.91010 0.48937 -0.37325 0.12968  0.01806  333 LYS A N   
2610 C CA  . LYS A 341 ? 1.23421 0.91289 0.50602 -0.35948 0.12082  0.02849  333 LYS A CA  
2611 C C   . LYS A 341 ? 1.31096 0.94953 0.54648 -0.38043 0.11875  0.03302  333 LYS A C   
2612 O O   . LYS A 341 ? 1.36487 0.95229 0.55594 -0.38050 0.11913  0.04111  333 LYS A O   
2613 C CB  . LYS A 341 ? 1.25296 0.93962 0.54660 -0.33363 0.10667  0.02865  333 LYS A CB  
2614 C CG  . LYS A 341 ? 1.18123 0.82346 0.44372 -0.31278 0.10074  0.03632  333 LYS A CG  
2615 C CD  . LYS A 341 ? 1.22575 0.87258 0.50444 -0.29324 0.08795  0.03629  333 LYS A CD  
2616 C CE  . LYS A 341 ? 1.32751 0.94005 0.58009 -0.29971 0.08026  0.03863  333 LYS A CE  
2617 N NZ  . LYS A 341 ? 1.22242 0.84280 0.48985 -0.28300 0.06901  0.03807  333 LYS A NZ  
2618 N N   . TYR A 342 ? 1.27718 0.93742 0.53203 -0.39707 0.11540  0.02771  334 TYR A N   
2619 C CA  . TYR A 342 ? 1.28569 0.91138 0.51095 -0.41730 0.11166  0.03020  334 TYR A CA  
2620 C C   . TYR A 342 ? 1.35131 0.96982 0.55742 -0.44856 0.12509  0.03019  334 TYR A C   
2621 O O   . TYR A 342 ? 1.46312 1.03495 0.62929 -0.46394 0.12429  0.03546  334 TYR A O   
2622 C CB  . TYR A 342 ? 1.28384 0.93630 0.53819 -0.41998 0.09984  0.02452  334 TYR A CB  
2623 C CG  . TYR A 342 ? 1.28165 0.93045 0.54333 -0.39298 0.08646  0.02632  334 TYR A CG  
2624 C CD1 . TYR A 342 ? 1.30764 0.90583 0.53147 -0.38263 0.08111  0.03175  334 TYR A CD1 
2625 C CD2 . TYR A 342 ? 1.27403 0.96926 0.58074 -0.37795 0.07950  0.02223  334 TYR A CD2 
2626 C CE1 . TYR A 342 ? 1.29603 0.89193 0.52554 -0.35980 0.07090  0.03253  334 TYR A CE1 
2627 C CE2 . TYR A 342 ? 1.29086 0.98115 0.60134 -0.35536 0.06776  0.02480  334 TYR A CE2 
2628 C CZ  . TYR A 342 ? 1.29583 0.93734 0.56701 -0.34706 0.06439  0.02973  334 TYR A CZ  
2629 O OH  . TYR A 342 ? 1.30985 0.94804 0.58415 -0.32688 0.05471  0.03134  334 TYR A OH  
2630 N N   . SER A 343 ? 1.30074 0.96304 0.53405 -0.45843 0.13747  0.02382  335 SER A N   
2631 C CA  . SER A 343 ? 1.33526 0.99087 0.54637 -0.48736 0.15381  0.02426  335 SER A CA  
2632 C C   . SER A 343 ? 1.37054 0.96531 0.52541 -0.48329 0.15564  0.03666  335 SER A C   
2633 O O   . SER A 343 ? 1.41931 0.97208 0.53308 -0.50598 0.15890  0.04310  335 SER A O   
2634 C CB  . SER A 343 ? 1.31307 1.02648 0.56334 -0.49275 0.16781  0.01390  335 SER A CB  
2635 O OG  . SER A 343 ? 1.29031 1.05759 0.59187 -0.50190 0.16618  0.00208  335 SER A OG  
2636 N N   . GLN A 344 ? 1.34757 0.93691 0.50206 -0.45477 0.15181  0.03998  336 GLN A N   
2637 C CA  . GLN A 344 ? 1.41753 0.95559 0.52913 -0.44387 0.14993  0.05052  336 GLN A CA  
2638 C C   . GLN A 344 ? 1.44005 0.92239 0.52417 -0.43573 0.13538  0.05702  336 GLN A C   
2639 O O   . GLN A 344 ? 1.54460 0.98321 0.60052 -0.43936 0.13197  0.06246  336 GLN A O   
2640 C CB  . GLN A 344 ? 1.33693 0.89224 0.46493 -0.41450 0.14836  0.04992  336 GLN A CB  
2641 C CG  . GLN A 344 ? 1.34259 0.94556 0.49317 -0.42188 0.16359  0.04239  336 GLN A CG  
2642 C CD  . GLN A 344 ? 1.37024 0.95573 0.49971 -0.43605 0.17070  0.04445  336 GLN A CD  
2643 O OE1 . GLN A 344 ? 1.38361 0.98052 0.51066 -0.46488 0.18166  0.04069  336 GLN A OE1 
2644 N NE2 . GLN A 344 ? 1.36492 0.92213 0.47878 -0.41644 0.16359  0.05047  336 GLN A NE2 
2645 N N   . TYR A 345 ? 1.40527 0.88939 0.49806 -0.42526 0.12671  0.05548  337 TYR A N   
2646 C CA  . TYR A 345 ? 1.45297 0.88634 0.51878 -0.41907 0.11503  0.05938  337 TYR A CA  
2647 C C   . TYR A 345 ? 1.53187 0.94011 0.57522 -0.44978 0.11689  0.05977  337 TYR A C   
2648 O O   . TYR A 345 ? 1.54876 0.90387 0.56242 -0.44844 0.10998  0.06377  337 TYR A O   
2649 C CB  . TYR A 345 ? 1.38544 0.83751 0.47813 -0.39871 0.10463  0.05389  337 TYR A CB  
2650 C CG  . TYR A 345 ? 1.42178 0.85726 0.51150 -0.36671 0.09793  0.05678  337 TYR A CG  
2651 C CD1 . TYR A 345 ? 1.41163 0.79252 0.46875 -0.35680 0.09118  0.06092  337 TYR A CD1 
2652 C CD2 . TYR A 345 ? 1.39303 0.86777 0.51536 -0.34611 0.09817  0.05426  337 TYR A CD2 
2653 C CE1 . TYR A 345 ? 1.40192 0.77168 0.46294 -0.32710 0.08506  0.06162  337 TYR A CE1 
2654 C CE2 . TYR A 345 ? 1.38806 0.84869 0.50868 -0.31820 0.09243  0.05646  337 TYR A CE2 
2655 C CZ  . TYR A 345 ? 1.39665 0.80541 0.48601 -0.30917 0.08630  0.06018  337 TYR A CZ  
2656 O OH  . TYR A 345 ? 1.29270 0.69156 0.38666 -0.28148 0.08074  0.06055  337 TYR A OH  
2657 N N   . GLN A 346 ? 1.49359 0.94144 0.55780 -0.47455 0.12448  0.05378  338 GLN A N   
2658 C CA  . GLN A 346 ? 1.54875 0.97867 0.59349 -0.50850 0.12833  0.05360  338 GLN A CA  
2659 C C   . GLN A 346 ? 1.57257 0.96879 0.58994 -0.51846 0.13291  0.05872  338 GLN A C   
2660 O O   . GLN A 346 ? 1.64618 0.99000 0.63203 -0.52434 0.12600  0.06248  338 GLN A O   
2661 C CB  . GLN A 346 ? 1.51828 1.00989 0.60597 -0.52836 0.13459  0.04309  338 GLN A CB  
2662 C CG  . GLN A 346 ? 1.52442 1.00216 0.59728 -0.56337 0.13736  0.04136  338 GLN A CG  
2663 C CD  . GLN A 346 ? 1.58616 1.12814 0.70713 -0.58102 0.14141  0.02964  338 GLN A CD  
2664 O OE1 . GLN A 346 ? 1.59860 1.19091 0.76564 -0.56386 0.13647  0.02245  338 GLN A OE1 
2665 N NE2 . GLN A 346 ? 1.56152 1.10173 0.67324 -0.61595 0.14965  0.02755  338 GLN A NE2 
2666 N N   . GLN A 347 ? 1.54234 0.96797 0.57305 -0.51860 0.14281  0.05772  339 GLN A N   
2667 C CA  . GLN A 347 ? 1.55474 0.95599 0.56300 -0.52779 0.14668  0.06165  339 GLN A CA  
2668 C C   . GLN A 347 ? 1.57891 0.92078 0.55701 -0.50493 0.13276  0.07029  339 GLN A C   
2669 O O   . GLN A 347 ? 1.68674 0.98579 0.63342 -0.51748 0.12966  0.07525  339 GLN A O   
2670 C CB  . GLN A 347 ? 1.53233 0.97919 0.56224 -0.52724 0.15939  0.05778  339 GLN A CB  
2671 C CG  . GLN A 347 ? 1.58081 1.01254 0.58872 -0.54549 0.16634  0.05998  339 GLN A CG  
2672 C CD  . GLN A 347 ? 1.67635 1.12814 0.68648 -0.58297 0.17886  0.05380  339 GLN A CD  
2673 O OE1 . GLN A 347 ? 1.66733 1.16624 0.70817 -0.59614 0.18768  0.04518  339 GLN A OE1 
2674 N NE2 . GLN A 347 ? 1.68170 1.09876 0.65971 -0.60121 0.17951  0.05806  339 GLN A NE2 
2675 N N   . ALA A 348 ? 1.54635 0.88639 0.53410 -0.47326 0.12457  0.07171  340 ALA A N   
2676 C CA  . ALA A 348 ? 1.57074 0.85963 0.53567 -0.44892 0.11138  0.07851  340 ALA A CA  
2677 C C   . ALA A 348 ? 1.66631 0.90107 0.60083 -0.45781 0.10278  0.08071  340 ALA A C   
2678 O O   . ALA A 348 ? 1.72539 0.91086 0.62980 -0.45617 0.09546  0.08711  340 ALA A O   
2679 C CB  . ALA A 348 ? 1.54925 0.85408 0.53541 -0.41690 0.10595  0.07701  340 ALA A CB  
2680 N N   . ILE A 349 ? 1.59978 0.84264 0.54081 -0.46718 0.10303  0.07552  341 ILE A N   
2681 C CA  . ILE A 349 ? 1.66403 0.85847 0.57705 -0.47893 0.09627  0.07550  341 ILE A CA  
2682 C C   . ILE A 349 ? 1.70843 0.88730 0.60155 -0.51114 0.10105  0.07709  341 ILE A C   
2683 O O   . ILE A 349 ? 1.74355 0.86660 0.60352 -0.51436 0.09352  0.08153  341 ILE A O   
2684 C CB  . ILE A 349 ? 1.72072 0.93495 0.64738 -0.48223 0.09586  0.06893  341 ILE A CB  
2685 C CG1 . ILE A 349 ? 1.66918 0.89142 0.60964 -0.44982 0.08998  0.06746  341 ILE A CG1 
2686 C CG2 . ILE A 349 ? 1.66090 0.83058 0.55944 -0.50104 0.09129  0.06737  341 ILE A CG2 
2687 C CD1 . ILE A 349 ? 1.53916 0.80185 0.50164 -0.45185 0.09100  0.06141  341 ILE A CD1 
2688 N N   . TYR A 350 ? 1.67615 0.90327 0.58935 -0.53383 0.11321  0.07311  342 TYR A N   
2689 C CA  . TYR A 350 ? 1.71523 0.94046 0.61539 -0.56715 0.12098  0.07289  342 TYR A CA  
2690 C C   . TYR A 350 ? 1.76590 0.94114 0.63136 -0.56518 0.11539  0.08125  342 TYR A C   
2691 O O   . TYR A 350 ? 1.81621 0.94957 0.65205 -0.58330 0.11159  0.08362  342 TYR A O   
2692 C CB  . TYR A 350 ? 1.70885 0.99949 0.64079 -0.58189 0.13637  0.06736  342 TYR A CB  
2693 C CG  . TYR A 350 ? 1.79889 1.09849 0.72360 -0.61764 0.14708  0.06470  342 TYR A CG  
2694 C CD1 . TYR A 350 ? 1.81135 1.08701 0.71085 -0.62580 0.14935  0.06983  342 TYR A CD1 
2695 C CD2 . TYR A 350 ? 1.81538 1.15018 0.75953 -0.64426 0.15503  0.05676  342 TYR A CD2 
2696 C CE1 . TYR A 350 ? 1.82555 1.11022 0.71720 -0.65925 0.15998  0.06691  342 TYR A CE1 
2697 C CE2 . TYR A 350 ? 1.77670 1.12311 0.71690 -0.67737 0.16573  0.05303  342 TYR A CE2 
2698 C CZ  . TYR A 350 ? 1.83403 1.15510 0.74708 -0.68486 0.16879  0.05796  342 TYR A CZ  
2699 O OH  . TYR A 350 ? 1.83107 1.16346 0.73841 -0.71803 0.17998  0.05399  342 TYR A OH  
2700 N N   . LYS A 351 ? 1.74772 0.92715 0.61635 -0.54412 0.11407  0.08573  343 LYS A N   
2701 C CA  . LYS A 351 ? 1.79142 0.93116 0.62938 -0.54275 0.10871  0.09449  343 LYS A CA  
2702 C C   . LYS A 351 ? 1.82249 0.89725 0.63164 -0.52407 0.09183  0.10088  343 LYS A C   
2703 O O   . LYS A 351 ? 1.87902 0.90713 0.65406 -0.53373 0.08525  0.10780  343 LYS A O   
2704 C CB  . LYS A 351 ? 1.77801 0.94886 0.63161 -0.52724 0.11300  0.09610  343 LYS A CB  
2705 C CG  . LYS A 351 ? 1.76896 1.00274 0.65024 -0.54505 0.13065  0.08872  343 LYS A CG  
2706 C CD  . LYS A 351 ? 1.73666 0.98525 0.61640 -0.54212 0.13603  0.09121  343 LYS A CD  
2707 C CE  . LYS A 351 ? 1.69801 1.01455 0.61296 -0.55166 0.15372  0.08134  343 LYS A CE  
2708 N NZ  . LYS A 351 ? 1.77196 1.09981 0.67982 -0.55525 0.16087  0.08250  343 LYS A NZ  
2709 N N   . CYS A 352 ? 1.78968 0.86126 0.61147 -0.49862 0.08518  0.09843  344 CYS A N   
2710 C CA  . CYS A 352 ? 1.81580 0.82842 0.61411 -0.47833 0.07023  0.10233  344 CYS A CA  
2711 C C   . CYS A 352 ? 1.88819 0.85662 0.65940 -0.49827 0.06623  0.10140  344 CYS A C   
2712 O O   . CYS A 352 ? 1.94677 0.85794 0.68721 -0.49338 0.05473  0.10746  344 CYS A O   
2713 C CB  . CYS A 352 ? 1.77505 0.80013 0.59465 -0.45004 0.06701  0.09777  344 CYS A CB  
2714 S SG  . CYS A 352 ? 1.80333 0.76041 0.59748 -0.42160 0.05020  0.10182  344 CYS A SG  
2715 N N   . LEU A 353 ? 1.85744 0.85160 0.64021 -0.51983 0.07454  0.09405  345 LEU A N   
2716 C CA  . LEU A 353 ? 1.90856 0.86679 0.66837 -0.54208 0.07203  0.09159  345 LEU A CA  
2717 C C   . LEU A 353 ? 1.96384 0.89137 0.69406 -0.56315 0.07084  0.09845  345 LEU A C   
2718 O O   . LEU A 353 ? 2.01633 0.88699 0.71612 -0.56574 0.06106  0.10145  345 LEU A O   
2719 C CB  . LEU A 353 ? 1.88854 0.89185 0.67113 -0.56371 0.08202  0.08261  345 LEU A CB  
2720 C CG  . LEU A 353 ? 1.83222 0.85734 0.63692 -0.54732 0.08115  0.07611  345 LEU A CG  
2721 C CD1 . LEU A 353 ? 1.81024 0.88163 0.63692 -0.57179 0.08950  0.06858  345 LEU A CD1 
2722 C CD2 . LEU A 353 ? 1.85727 0.82568 0.63891 -0.53279 0.07027  0.07465  345 LEU A CD2 
2723 N N   . LEU A 354 ? 1.95818 0.92133 0.69651 -0.57742 0.08053  0.10058  346 LEU A N   
2724 C CA  . LEU A 354 ? 2.01537 0.95515 0.72502 -0.60042 0.08137  0.10719  346 LEU A CA  
2725 C C   . LEU A 354 ? 2.05407 0.93833 0.73363 -0.58141 0.06651  0.11811  346 LEU A C   
2726 O O   . LEU A 354 ? 2.19242 1.02584 0.83795 -0.59359 0.05855  0.12390  346 LEU A O   
2727 C CB  . LEU A 354 ? 1.99434 0.99000 0.72288 -0.61677 0.09662  0.10531  346 LEU A CB  
2728 C CG  . LEU A 354 ? 1.96495 1.01674 0.72310 -0.64002 0.11153  0.09470  346 LEU A CG  
2729 C CD1 . LEU A 354 ? 1.94696 1.05206 0.72405 -0.65346 0.12692  0.09201  346 LEU A CD1 
2730 C CD2 . LEU A 354 ? 2.01198 1.04061 0.75123 -0.66940 0.11196  0.09232  346 LEU A CD2 
2731 N N   . ASP A 355 ? 2.01977 0.91394 0.71207 -0.55293 0.06225  0.12093  347 ASP A N   
2732 C CA  . ASP A 355 ? 2.05120 0.89994 0.71969 -0.53298 0.04741  0.13140  347 ASP A CA  
2733 C C   . ASP A 355 ? 2.09667 0.88394 0.74437 -0.51847 0.03177  0.13325  347 ASP A C   
2734 O O   . ASP A 355 ? 2.16243 0.89879 0.77991 -0.51534 0.01846  0.14270  347 ASP A O   
2735 C CB  . ASP A 355 ? 1.99993 0.87972 0.69219 -0.50547 0.04716  0.13202  347 ASP A CB  
2736 C CG  . ASP A 355 ? 1.97723 0.90836 0.68442 -0.51766 0.06050  0.13159  347 ASP A CG  
2737 O OD1 . ASP A 355 ? 2.02712 0.97760 0.73142 -0.54804 0.07229  0.12897  347 ASP A OD1 
2738 O OD2 . ASP A 355 ? 1.94473 0.89624 0.66645 -0.49696 0.05935  0.13320  347 ASP A OD2 
2739 N N   . ARG A 356 ? 2.10897 0.90005 0.77181 -0.51041 0.03303  0.12439  348 ARG A N   
2740 C CA  . ARG A 356 ? 2.09534 0.83225 0.74390 -0.49254 0.01979  0.12337  348 ARG A CA  
2741 C C   . ARG A 356 ? 2.17697 0.87084 0.79747 -0.51604 0.01628  0.12389  348 ARG A C   
2742 O O   . ARG A 356 ? 2.33236 0.96994 0.92683 -0.50840 0.00202  0.13095  348 ARG A O   
2743 C CB  . ARG A 356 ? 2.03371 0.79268 0.70809 -0.47575 0.02379  0.11292  348 ARG A CB  
2744 C CG  . ARG A 356 ? 1.98993 0.76365 0.68325 -0.44245 0.02010  0.11377  348 ARG A CG  
2745 C CD  . ARG A 356 ? 1.95352 0.73368 0.66416 -0.42445 0.02156  0.10428  348 ARG A CD  
2746 N NE  . ARG A 356 ? 1.99313 0.71382 0.68553 -0.41117 0.01031  0.10180  348 ARG A NE  
2747 C CZ  . ARG A 356 ? 2.00864 0.69310 0.69544 -0.38356 -0.00232 0.10524  348 ARG A CZ  
2748 N NH1 . ARG A 356 ? 1.98891 0.68897 0.68384 -0.36688 -0.00620 0.11238  348 ARG A NH1 
2749 N NH2 . ARG A 356 ? 2.04459 0.67849 0.72019 -0.37241 -0.01139 0.10042  348 ARG A NH2 
2750 N N   . VAL A 357 ? 2.14258 0.86200 0.76947 -0.54301 0.02784  0.11674  349 VAL A N   
2751 C CA  . VAL A 357 ? 2.23032 0.91267 0.83331 -0.56667 0.02558  0.11549  349 VAL A CA  
2752 C C   . VAL A 357 ? 2.25287 0.95171 0.84455 -0.60039 0.03411  0.11991  349 VAL A C   
2753 O O   . VAL A 357 ? 2.19017 0.94528 0.80405 -0.61666 0.04838  0.11495  349 VAL A O   
2754 C CB  . VAL A 357 ? 2.23005 0.92227 0.84654 -0.57173 0.03036  0.10292  349 VAL A CB  
2755 C CG1 . VAL A 357 ? 2.22262 0.91332 0.85551 -0.53956 0.02612  0.09717  349 VAL A CG1 
2756 C CG2 . VAL A 357 ? 2.19481 0.94770 0.83402 -0.59758 0.04572  0.09597  349 VAL A CG2 
2757 N N   . PRO A 358 ? 2.38899 1.03928 0.94632 -0.61168 0.02554  0.12936  350 PRO A N   
2758 C CA  . PRO A 358 ? 2.39842 1.05852 0.94028 -0.64585 0.03380  0.13352  350 PRO A CA  
2759 C C   . PRO A 358 ? 2.41084 1.09870 0.96152 -0.67730 0.04660  0.12411  350 PRO A C   
2760 O O   . PRO A 358 ? 2.47635 1.16790 1.04072 -0.67342 0.04689  0.11495  350 PRO A O   
2761 C CB  . PRO A 358 ? 2.46828 1.05851 0.96921 -0.64856 0.01855  0.14498  350 PRO A CB  
2762 C CG  . PRO A 358 ? 2.46358 1.01904 0.96365 -0.61064 0.00230  0.14929  350 PRO A CG  
2763 C CD  . PRO A 358 ? 2.41433 0.99799 0.94668 -0.59154 0.00697  0.13686  350 PRO A CD  
2764 N N   . GLU A 359 ? 2.35683 1.06259 0.89847 -0.70838 0.05660  0.12638  351 GLU A N   
2765 C CA  . GLU A 359 ? 2.35833 1.09814 0.91037 -0.74211 0.07037  0.11773  351 GLU A CA  
2766 C C   . GLU A 359 ? 2.40840 1.10103 0.93937 -0.75355 0.06277  0.11615  351 GLU A C   
2767 O O   . GLU A 359 ? 2.40295 1.11879 0.95322 -0.76223 0.06799  0.10533  351 GLU A O   
2768 C CB  . GLU A 359 ? 2.44951 1.21090 0.99165 -0.77096 0.08183  0.12162  351 GLU A CB  
2769 C CG  . GLU A 359 ? 2.41214 1.20579 0.96310 -0.80747 0.09578  0.11318  351 GLU A CG  
2770 C CD  . GLU A 359 ? 2.33960 1.20003 0.93652 -0.80930 0.10758  0.09962  351 GLU A CD  
2771 O OE1 . GLU A 359 ? 2.31683 1.21266 0.94115 -0.78710 0.10993  0.09723  351 GLU A OE1 
2772 O OE2 . GLU A 359 ? 2.34305 1.22005 0.94870 -0.83323 0.11372  0.09172  351 GLU A OE2 
2773 N N   . GLU A 360 ? 2.47628 1.10539 0.96959 -0.75398 0.05034  0.12661  352 GLU A N   
2774 C CA  . GLU A 360 ? 2.53419 1.11158 1.00427 -0.76510 0.04214  0.12640  352 GLU A CA  
2775 C C   . GLU A 360 ? 2.51085 1.06923 0.99328 -0.73915 0.03351  0.11852  352 GLU A C   
2776 O O   . GLU A 360 ? 2.54487 1.07400 1.01779 -0.74915 0.02994  0.11373  352 GLU A O   
2777 C CB  . GLU A 360 ? 2.61206 1.12517 1.04043 -0.76814 0.02922  0.14082  352 GLU A CB  
2778 C CG  . GLU A 360 ? 2.61333 1.09211 1.03305 -0.73349 0.01377  0.15016  352 GLU A CG  
2779 C CD  . GLU A 360 ? 2.61058 1.11074 1.02685 -0.73142 0.01633  0.15889  352 GLU A CD  
2780 O OE1 . GLU A 360 ? 2.70806 1.22518 1.11192 -0.76098 0.02631  0.16223  352 GLU A OE1 
2781 O OE2 . GLU A 360 ? 2.57245 1.07190 0.99821 -0.70070 0.00852  0.16184  352 GLU A OE2 
2782 N N   . GLU A 361 ? 2.45877 1.03343 0.96156 -0.70786 0.03089  0.11658  353 GLU A N   
2783 C CA  . GLU A 361 ? 2.43156 0.99064 0.94697 -0.68081 0.02378  0.10840  353 GLU A CA  
2784 C C   . GLU A 361 ? 2.36499 0.98333 0.91494 -0.68352 0.03555  0.09538  353 GLU A C   
2785 O O   . GLU A 361 ? 2.37548 0.98807 0.93742 -0.66146 0.03145  0.08792  353 GLU A O   
2786 C CB  . GLU A 361 ? 2.41678 0.95517 0.93273 -0.64401 0.01287  0.11463  353 GLU A CB  
2787 C CG  . GLU A 361 ? 2.48386 0.95458 0.96874 -0.63408 -0.00369 0.12584  353 GLU A CG  
2788 C CD  . GLU A 361 ? 2.46967 0.91678 0.96009 -0.59472 -0.01647 0.12875  353 GLU A CD  
2789 O OE1 . GLU A 361 ? 2.49704 0.94717 1.00645 -0.57399 -0.01695 0.11839  353 GLU A OE1 
2790 O OE2 . GLU A 361 ? 2.50631 0.93322 0.98245 -0.58542 -0.02589 0.14093  353 GLU A OE2 
2791 N N   . LYS A 362 ? 2.34199 1.01470 0.90806 -0.70964 0.04924  0.09225  354 LYS A N   
2792 C CA  . LYS A 362 ? 2.29783 1.03519 0.90144 -0.71042 0.05970  0.08206  354 LYS A CA  
2793 C C   . LYS A 362 ? 2.31321 1.04531 0.92384 -0.71261 0.05736  0.07035  354 LYS A C   
2794 O O   . LYS A 362 ? 2.34416 1.10203 0.97755 -0.69575 0.05805  0.06360  354 LYS A O   
2795 C CB  . LYS A 362 ? 2.25777 1.05247 0.87843 -0.73956 0.07426  0.08069  354 LYS A CB  
2796 C CG  . LYS A 362 ? 2.29295 1.09267 0.90893 -0.77514 0.07970  0.07531  354 LYS A CG  
2797 C CD  . LYS A 362 ? 2.27108 1.13478 0.91106 -0.80171 0.09523  0.07178  354 LYS A CD  
2798 C CE  . LYS A 362 ? 2.35323 1.24389 1.00781 -0.83052 0.10085  0.06143  354 LYS A CE  
2799 N NZ  . LYS A 362 ? 2.25056 1.20840 0.93449 -0.85431 0.11632  0.05664  354 LYS A NZ  
2800 N N   . ASP A 363 ? 2.32079 1.02101 0.91224 -0.73308 0.05462  0.06787  355 ASP A N   
2801 C CA  . ASP A 363 ? 2.32704 1.02355 0.92391 -0.74027 0.05282  0.05552  355 ASP A CA  
2802 C C   . ASP A 363 ? 2.34466 0.98364 0.92594 -0.71309 0.04092  0.05298  355 ASP A C   
2803 O O   . ASP A 363 ? 2.40461 1.04932 0.99736 -0.70671 0.03980  0.04121  355 ASP A O   
2804 C CB  . ASP A 363 ? 2.36909 1.06242 0.95566 -0.77578 0.05621  0.05302  355 ASP A CB  
2805 C CG  . ASP A 363 ? 2.34353 1.10134 0.95309 -0.80379 0.06919  0.05123  355 ASP A CG  
2806 O OD1 . ASP A 363 ? 2.31456 1.12653 0.95515 -0.79720 0.07514  0.04752  355 ASP A OD1 
2807 O OD2 . ASP A 363 ? 2.47300 1.22680 1.07058 -0.83203 0.07339  0.05327  355 ASP A OD2 
2808 N N   . THR A 364 ? 2.38533 0.97241 0.94297 -0.69772 0.03206  0.06287  356 THR A N   
2809 C CA  . THR A 364 ? 2.41098 0.94119 0.95656 -0.66992 0.02009  0.06052  356 THR A CA  
2810 C C   . THR A 364 ? 2.41167 0.95688 0.97585 -0.63646 0.01890  0.05812  356 THR A C   
2811 O O   . THR A 364 ? 2.39007 0.91916 0.96020 -0.61898 0.01543  0.04714  356 THR A O   
2812 C CB  . THR A 364 ? 2.47730 0.94839 0.99358 -0.66712 0.00948  0.07262  356 THR A CB  
2813 O OG1 . THR A 364 ? 2.60443 1.02258 1.11237 -0.65071 -0.00072 0.06600  356 THR A OG1 
2814 C CG2 . THR A 364 ? 2.46799 0.93470 0.98069 -0.64686 0.00460  0.08553  356 THR A CG2 
2815 N N   . ASN A 365 ? 2.33822 0.91415 0.91185 -0.62845 0.02228  0.06702  357 ASN A N   
2816 C CA  . ASN A 365 ? 2.27532 0.86262 0.86480 -0.59556 0.02035  0.06747  357 ASN A CA  
2817 C C   . ASN A 365 ? 2.28656 0.93476 0.90533 -0.59804 0.03075  0.05911  357 ASN A C   
2818 O O   . ASN A 365 ? 2.22474 0.92241 0.85729 -0.61616 0.03988  0.06221  357 ASN A O   
2819 C CB  . ASN A 365 ? 2.32805 0.91453 0.91197 -0.58471 0.01716  0.08164  357 ASN A CB  
2820 C CG  . ASN A 365 ? 2.25800 0.83994 0.85312 -0.54791 0.01137  0.08294  357 ASN A CG  
2821 O OD1 . ASN A 365 ? 2.19033 0.80286 0.80745 -0.53518 0.01651  0.07504  357 ASN A OD1 
2822 N ND2 . ASN A 365 ? 2.28443 0.82883 0.86469 -0.53121 0.00007  0.09321  357 ASN A ND2 
2823 N N   . VAL A 366 ? 2.26050 0.90501 0.88938 -0.58008 0.02918  0.04845  358 VAL A N   
2824 C CA  . VAL A 366 ? 2.20086 0.89682 0.85645 -0.57624 0.03639  0.04137  358 VAL A CA  
2825 C C   . VAL A 366 ? 2.08828 0.78145 0.75291 -0.54125 0.03363  0.04434  358 VAL A C   
2826 O O   . VAL A 366 ? 2.11366 0.75988 0.76756 -0.51860 0.02556  0.04170  358 VAL A O   
2827 C CB  . VAL A 366 ? 2.17067 0.86789 0.82968 -0.58622 0.03697  0.02584  358 VAL A CB  
2828 C CG1 . VAL A 366 ? 2.16376 0.80342 0.80635 -0.57024 0.02911  0.01693  358 VAL A CG1 
2829 C CG2 . VAL A 366 ? 2.06211 0.80590 0.74581 -0.58037 0.04177  0.01923  358 VAL A CG2 
2830 N N   . GLN A 367 ? 2.03477 0.77846 0.72101 -0.53657 0.04007  0.04927  359 GLN A N   
2831 C CA  . GLN A 367 ? 1.99991 0.74965 0.69715 -0.50471 0.03840  0.05410  359 GLN A CA  
2832 C C   . GLN A 367 ? 1.96814 0.73750 0.68207 -0.49183 0.04156  0.04458  359 GLN A C   
2833 O O   . GLN A 367 ? 1.91808 0.74151 0.65284 -0.50431 0.04845  0.04186  359 GLN A O   
2834 C CB  . GLN A 367 ? 1.96775 0.76372 0.68000 -0.50706 0.04389  0.06442  359 GLN A CB  
2835 C CG  . GLN A 367 ? 2.08825 0.85962 0.78120 -0.51538 0.03985  0.07434  359 GLN A CG  
2836 C CD  . GLN A 367 ? 2.11203 0.84591 0.79431 -0.48635 0.02945  0.08155  359 GLN A CD  
2837 O OE1 . GLN A 367 ? 2.07207 0.83039 0.77004 -0.46614 0.02997  0.08543  359 GLN A OE1 
2838 N NE2 . GLN A 367 ? 2.10368 0.77853 0.76077 -0.48372 0.01898  0.08326  359 GLN A NE2 
2839 N N   . VAL A 368 ? 1.96841 0.70058 0.67771 -0.46598 0.03593  0.03804  360 VAL A N   
2840 C CA  . VAL A 368 ? 1.91800 0.68828 0.65569 -0.44198 0.03722  0.02359  360 VAL A CA  
2841 C C   . VAL A 368 ? 1.87057 0.69548 0.63559 -0.42310 0.04070  0.03094  360 VAL A C   
2842 O O   . VAL A 368 ? 1.85741 0.66460 0.62043 -0.40143 0.03706  0.03860  360 VAL A O   
2843 C CB  . VAL A 368 ? 1.97015 0.69320 0.70104 -0.41793 0.03142  0.01103  360 VAL A CB  
2844 C CG1 . VAL A 368 ? 2.08445 0.75062 0.79809 -0.40155 0.02332  0.02039  360 VAL A CG1 
2845 C CG2 . VAL A 368 ? 1.90656 0.67044 0.66572 -0.39172 0.03431  -0.00141 360 VAL A CG2 
2846 N N   . LEU A 369 ? 1.84291 0.73108 0.63298 -0.43184 0.04640  0.02845  361 LEU A N   
2847 C CA  . LEU A 369 ? 1.75255 0.69946 0.57120 -0.42044 0.05063  0.03501  361 LEU A CA  
2848 C C   . LEU A 369 ? 1.72901 0.71717 0.57542 -0.40087 0.05073  0.02389  361 LEU A C   
2849 O O   . LEU A 369 ? 1.76952 0.77276 0.61987 -0.41365 0.05052  0.01407  361 LEU A O   
2850 C CB  . LEU A 369 ? 1.74481 0.72909 0.57039 -0.45023 0.05659  0.04099  361 LEU A CB  
2851 C CG  . LEU A 369 ? 1.71870 0.73906 0.55872 -0.44678 0.06191  0.05208  361 LEU A CG  
2852 C CD1 . LEU A 369 ? 1.73003 0.76601 0.56561 -0.48071 0.06887  0.05790  361 LEU A CD1 
2853 C CD2 . LEU A 369 ? 1.68510 0.76698 0.56382 -0.42704 0.06339  0.04761  361 LEU A CD2 
2854 N N   . MET A 370 ? 1.66910 0.67364 0.53236 -0.37228 0.05052  0.02556  362 MET A N   
2855 C CA  . MET A 370 ? 1.63354 0.66910 0.51931 -0.35166 0.05064  0.01548  362 MET A CA  
2856 C C   . MET A 370 ? 1.58863 0.68245 0.50533 -0.34084 0.05328  0.02166  362 MET A C   
2857 O O   . MET A 370 ? 1.60329 0.69568 0.52375 -0.32585 0.05360  0.02988  362 MET A O   
2858 C CB  . MET A 370 ? 1.66688 0.66405 0.54604 -0.32502 0.04801  0.00884  362 MET A CB  
2859 C CG  . MET A 370 ? 1.73102 0.66982 0.58305 -0.33262 0.04513  0.00014  362 MET A CG  
2860 S SD  . MET A 370 ? 1.73438 0.63743 0.58763 -0.29998 0.04316  -0.01302 362 MET A SD  
2861 C CE  . MET A 370 ? 1.80773 0.65194 0.63179 -0.31649 0.04111  -0.02614 362 MET A CE  
2862 N N   . VAL A 371 ? 1.53912 0.68060 0.47665 -0.34836 0.05391  0.01766  363 VAL A N   
2863 C CA  . VAL A 371 ? 1.48383 0.68230 0.45442 -0.33703 0.05507  0.02132  363 VAL A CA  
2864 C C   . VAL A 371 ? 1.50763 0.71275 0.48851 -0.31213 0.05382  0.01443  363 VAL A C   
2865 O O   . VAL A 371 ? 1.53470 0.74484 0.51377 -0.31672 0.05193  0.00558  363 VAL A O   
2866 C CB  . VAL A 371 ? 1.46503 0.70958 0.45434 -0.35795 0.05417  0.02078  363 VAL A CB  
2867 C CG1 . VAL A 371 ? 1.46306 0.76305 0.48797 -0.34522 0.05400  0.02404  363 VAL A CG1 
2868 C CG2 . VAL A 371 ? 1.49081 0.73047 0.47115 -0.38502 0.05704  0.02562  363 VAL A CG2 
2869 N N   . LEU A 372 ? 1.44312 0.64845 0.43329 -0.28817 0.05495  0.01804  364 LEU A N   
2870 C CA  . LEU A 372 ? 1.43716 0.64707 0.43775 -0.26386 0.05511  0.01129  364 LEU A CA  
2871 C C   . LEU A 372 ? 1.38517 0.64967 0.41650 -0.25591 0.05515  0.01469  364 LEU A C   
2872 O O   . LEU A 372 ? 1.42411 0.70530 0.47074 -0.24386 0.05617  0.02185  364 LEU A O   
2873 C CB  . LEU A 372 ? 1.43302 0.60857 0.42680 -0.24263 0.05497  0.01249  364 LEU A CB  
2874 C CG  . LEU A 372 ? 1.49140 0.61011 0.45603 -0.24975 0.05267  0.01246  364 LEU A CG  
2875 C CD1 . LEU A 372 ? 1.49893 0.58489 0.46134 -0.22455 0.05005  0.01079  364 LEU A CD1 
2876 C CD2 . LEU A 372 ? 1.52033 0.61537 0.46685 -0.26558 0.05275  0.00170  364 LEU A CD2 
2877 N N   . GLY A 373 ? 1.39672 0.68586 0.43528 -0.26278 0.05318  0.00968  365 GLY A N   
2878 C CA  . GLY A 373 ? 1.31349 0.65351 0.38042 -0.26025 0.05060  0.01368  365 GLY A CA  
2879 C C   . GLY A 373 ? 1.34939 0.71652 0.42632 -0.28229 0.04736  0.01794  365 GLY A C   
2880 O O   . GLY A 373 ? 1.38182 0.77461 0.47859 -0.28147 0.04869  0.02468  365 GLY A O   
2881 N N   . ALA A 374 ? 1.33264 0.69487 0.39698 -0.30173 0.04352  0.01292  366 ALA A N   
2882 C CA  . ALA A 374 ? 1.33936 0.72092 0.41002 -0.32634 0.04009  0.01474  366 ALA A CA  
2883 C C   . ALA A 374 ? 1.30705 0.73870 0.40698 -0.32871 0.03212  0.01652  366 ALA A C   
2884 O O   . ALA A 374 ? 1.32394 0.78193 0.43997 -0.34561 0.02890  0.01821  366 ALA A O   
2885 C CB  . ALA A 374 ? 1.38391 0.73151 0.42528 -0.34607 0.03883  0.00781  366 ALA A CB  
2886 N N   . GLY A 375 ? 1.28670 0.73030 0.39362 -0.31312 0.02863  0.01599  367 GLY A N   
2887 C CA  . GLY A 375 ? 1.26076 0.74616 0.39223 -0.31374 0.01850  0.01875  367 GLY A CA  
2888 C C   . GLY A 375 ? 1.33100 0.82935 0.46215 -0.33820 0.00922  0.01661  367 GLY A C   
2889 O O   . GLY A 375 ? 1.35257 0.82643 0.45556 -0.34919 0.00677  0.01051  367 GLY A O   
2890 N N   . ARG A 376 ? 1.25996 0.79619 0.42243 -0.34662 0.00437  0.02017  368 ARG A N   
2891 C CA  . ARG A 376 ? 1.27327 0.82930 0.44376 -0.37021 -0.00580 0.01800  368 ARG A CA  
2892 C C   . ARG A 376 ? 1.31729 0.86250 0.48225 -0.38898 0.00210  0.01549  368 ARG A C   
2893 O O   . ARG A 376 ? 1.31347 0.87962 0.49093 -0.40951 -0.00466 0.01320  368 ARG A O   
2894 C CB  . ARG A 376 ? 1.33371 0.94147 0.54746 -0.36656 -0.01753 0.02237  368 ARG A CB  
2895 C CG  . ARG A 376 ? 1.25828 0.87400 0.47401 -0.35194 -0.02764 0.02619  368 ARG A CG  
2896 C CD  . ARG A 376 ? 1.21071 0.87231 0.47154 -0.34173 -0.03797 0.03180  368 ARG A CD  
2897 N NE  . ARG A 376 ? 1.21653 0.90474 0.49320 -0.35434 -0.05722 0.03303  368 ARG A NE  
2898 C CZ  . ARG A 376 ? 1.22014 0.95031 0.54010 -0.35890 -0.06668 0.03347  368 ARG A CZ  
2899 N NH1 . ARG A 376 ? 1.21225 0.96456 0.56408 -0.35313 -0.05668 0.03181  368 ARG A NH1 
2900 N NH2 . ARG A 376 ? 1.27863 1.02928 0.61045 -0.36955 -0.08669 0.03491  368 ARG A NH2 
2901 N N   . GLY A 377 ? 1.35197 0.86571 0.49911 -0.38271 0.01506  0.01627  369 GLY A N   
2902 C CA  . GLY A 377 ? 1.37696 0.86377 0.50475 -0.40100 0.02323  0.01469  369 GLY A CA  
2903 C C   . GLY A 377 ? 1.42722 0.94600 0.58206 -0.41236 0.02846  0.01715  369 GLY A C   
2904 O O   . GLY A 377 ? 1.43860 0.95647 0.58954 -0.43682 0.02962  0.01447  369 GLY A O   
2905 N N   . PRO A 378 ? 1.34821 0.89576 0.53062 -0.39662 0.03291  0.02115  370 PRO A N   
2906 C CA  . PRO A 378 ? 1.33831 0.91118 0.54135 -0.40762 0.04160  0.02180  370 PRO A CA  
2907 C C   . PRO A 378 ? 1.40488 0.93678 0.57573 -0.41233 0.05430  0.02523  370 PRO A C   
2908 O O   . PRO A 378 ? 1.38637 0.92968 0.56277 -0.42952 0.06261  0.02523  370 PRO A O   
2909 C CB  . PRO A 378 ? 1.32060 0.93467 0.56162 -0.38639 0.04100  0.02361  370 PRO A CB  
2910 C CG  . PRO A 378 ? 1.28521 0.87404 0.50959 -0.36149 0.03808  0.02681  370 PRO A CG  
2911 C CD  . PRO A 378 ? 1.30157 0.86000 0.49707 -0.36906 0.03051  0.02419  370 PRO A CD  
2912 N N   . LEU A 379 ? 1.39162 0.87758 0.53050 -0.39736 0.05514  0.02787  371 LEU A N   
2913 C CA  . LEU A 379 ? 1.38268 0.82119 0.48697 -0.39920 0.06349  0.03230  371 LEU A CA  
2914 C C   . LEU A 379 ? 1.49882 0.89539 0.56998 -0.42115 0.06233  0.02984  371 LEU A C   
2915 O O   . LEU A 379 ? 1.52673 0.89499 0.57529 -0.43605 0.06895  0.03364  371 LEU A O   
2916 C CB  . LEU A 379 ? 1.38230 0.79455 0.47431 -0.37054 0.06281  0.03504  371 LEU A CB  
2917 C CG  . LEU A 379 ? 1.40842 0.80711 0.49192 -0.36107 0.07015  0.04173  371 LEU A CG  
2918 C CD1 . LEU A 379 ? 1.41533 0.86577 0.53363 -0.35845 0.07496  0.04278  371 LEU A CD1 
2919 C CD2 . LEU A 379 ? 1.37925 0.74846 0.45023 -0.33382 0.06752  0.04316  371 LEU A CD2 
2920 N N   . VAL A 380 ? 1.51124 0.90266 0.57788 -0.42391 0.05399  0.02373  372 VAL A N   
2921 C CA  . VAL A 380 ? 1.50954 0.86711 0.54879 -0.44704 0.05162  0.01897  372 VAL A CA  
2922 C C   . VAL A 380 ? 1.55328 0.93625 0.60536 -0.47645 0.05479  0.01882  372 VAL A C   
2923 O O   . VAL A 380 ? 1.60237 0.94990 0.62778 -0.49677 0.05929  0.01972  372 VAL A O   
2924 C CB  . VAL A 380 ? 1.46629 0.82437 0.50265 -0.44535 0.04183  0.01129  372 VAL A CB  
2925 C CG1 . VAL A 380 ? 1.50731 0.83728 0.51933 -0.47169 0.03902  0.00504  372 VAL A CG1 
2926 C CG2 . VAL A 380 ? 1.45777 0.78903 0.47964 -0.41900 0.04109  0.00954  372 VAL A CG2 
2927 N N   . ASN A 381 ? 1.47818 0.92008 0.57103 -0.47857 0.05225  0.01730  373 ASN A N   
2928 C CA  . ASN A 381 ? 1.48175 0.95980 0.59750 -0.50506 0.05567  0.01500  373 ASN A CA  
2929 C C   . ASN A 381 ? 1.53982 1.00971 0.64771 -0.51243 0.06994  0.02041  373 ASN A C   
2930 O O   . ASN A 381 ? 1.56281 1.02428 0.65991 -0.54053 0.07610  0.01968  373 ASN A O   
2931 C CB  . ASN A 381 ? 1.44937 0.99312 0.61552 -0.50019 0.04862  0.01150  373 ASN A CB  
2932 C CG  . ASN A 381 ? 1.45535 1.00858 0.62691 -0.50044 0.03288  0.00692  373 ASN A CG  
2933 O OD1 . ASN A 381 ? 1.42370 0.95448 0.57387 -0.51988 0.02836  0.00279  373 ASN A OD1 
2934 N ND2 . ASN A 381 ? 1.48469 1.07004 0.68324 -0.48004 0.02391  0.00775  373 ASN A ND2 
2935 N N   . ALA A 382 ? 1.51669 0.98844 0.62816 -0.48939 0.07488  0.02564  374 ALA A N   
2936 C CA  . ALA A 382 ? 1.48989 0.95150 0.58936 -0.49355 0.08772  0.03164  374 ALA A CA  
2937 C C   . ALA A 382 ? 1.55816 0.95404 0.60715 -0.50775 0.09062  0.03698  374 ALA A C   
2938 O O   . ALA A 382 ? 1.62991 1.01853 0.66570 -0.53058 0.10046  0.04029  374 ALA A O   
2939 C CB  . ALA A 382 ? 1.44627 0.91534 0.55462 -0.46340 0.08903  0.03571  374 ALA A CB  
2940 N N   . SER A 383 ? 1.54185 0.89165 0.56419 -0.49545 0.08248  0.03717  375 SER A N   
2941 C CA  . SER A 383 ? 1.56757 0.84895 0.54304 -0.50468 0.08231  0.04124  375 SER A CA  
2942 C C   . SER A 383 ? 1.70729 0.97931 0.67150 -0.53993 0.08356  0.03779  375 SER A C   
2943 O O   . SER A 383 ? 1.79896 1.02691 0.72966 -0.55752 0.08805  0.04366  375 SER A O   
2944 C CB  . SER A 383 ? 1.57277 0.81608 0.53154 -0.48162 0.07365  0.03860  375 SER A CB  
2945 O OG  . SER A 383 ? 1.53834 0.79111 0.50859 -0.45046 0.07299  0.04155  375 SER A OG  
2946 N N   . LEU A 384 ? 1.66973 0.98067 0.66031 -0.55051 0.07874  0.02912  376 LEU A N   
2947 C CA  . LEU A 384 ? 1.73228 1.04213 0.71812 -0.58496 0.07871  0.02410  376 LEU A CA  
2948 C C   . LEU A 384 ? 1.77471 1.11464 0.77397 -0.60997 0.09077  0.02654  376 LEU A C   
2949 O O   . LEU A 384 ? 1.88964 1.19784 0.86235 -0.63797 0.09598  0.02862  376 LEU A O   
2950 C CB  . LEU A 384 ? 1.62881 0.97758 0.64274 -0.58667 0.06814  0.01432  376 LEU A CB  
2951 C CG  . LEU A 384 ? 1.64060 0.95477 0.63342 -0.57386 0.05749  0.00930  376 LEU A CG  
2952 C CD1 . LEU A 384 ? 1.62825 0.98515 0.64793 -0.57784 0.04634  0.00106  376 LEU A CD1 
2953 C CD2 . LEU A 384 ? 1.73677 0.98595 0.68576 -0.59115 0.05788  0.00802  376 LEU A CD2 
2954 N N   . ARG A 385 ? 1.66303 1.06209 0.70259 -0.60120 0.09541  0.02530  377 ARG A N   
2955 C CA  . ARG A 385 ? 1.66084 1.09829 0.72003 -0.62327 0.10903  0.02479  377 ARG A CA  
2956 C C   . ARG A 385 ? 1.75039 1.14076 0.76716 -0.63260 0.12027  0.03515  377 ARG A C   
2957 O O   . ARG A 385 ? 1.75254 1.13853 0.75753 -0.66518 0.13014  0.03577  377 ARG A O   
2958 C CB  . ARG A 385 ? 1.59029 1.09360 0.69930 -0.60480 0.11125  0.02081  377 ARG A CB  
2959 C CG  . ARG A 385 ? 1.52640 1.08288 0.68189 -0.60182 0.09995  0.01116  377 ARG A CG  
2960 C CD  . ARG A 385 ? 1.48612 1.10972 0.69481 -0.59002 0.10356  0.00615  377 ARG A CD  
2961 N NE  . ARG A 385 ? 1.51026 1.12923 0.71738 -0.55891 0.10527  0.01169  377 ARG A NE  
2962 C CZ  . ARG A 385 ? 1.45171 1.06970 0.66586 -0.52950 0.09330  0.01332  377 ARG A CZ  
2963 N NH1 . ARG A 385 ? 1.40805 1.02807 0.62854 -0.52678 0.07846  0.01029  377 ARG A NH1 
2964 N NH2 . ARG A 385 ? 1.47104 1.08553 0.68418 -0.50402 0.09635  0.01793  377 ARG A NH2 
2965 N N   . ALA A 386 ? 1.74952 1.10555 0.74382 -0.60580 0.11797  0.04315  378 ALA A N   
2966 C CA  . ALA A 386 ? 1.77340 1.08375 0.73120 -0.60519 0.12272  0.05256  378 ALA A CA  
2967 C C   . ALA A 386 ? 1.81995 1.07337 0.74170 -0.62301 0.11771  0.05351  378 ALA A C   
2968 O O   . ALA A 386 ? 1.85069 1.08838 0.75693 -0.63579 0.12215  0.05609  378 ALA A O   
2969 C CB  . ALA A 386 ? 1.68492 0.97418 0.63636 -0.56733 0.11546  0.05736  378 ALA A CB  
2970 N N   . ALA A 387 ? 1.85299 1.07636 0.76058 -0.62430 0.10878  0.05114  379 ALA A N   
2971 C CA  . ALA A 387 ? 1.82652 0.99096 0.69887 -0.63790 0.10244  0.05071  379 ALA A CA  
2972 C C   . ALA A 387 ? 1.92708 1.10724 0.80189 -0.67532 0.10925  0.04670  379 ALA A C   
2973 O O   . ALA A 387 ? 2.00361 1.14693 0.85143 -0.68560 0.10938  0.04995  379 ALA A O   
2974 C CB  . ALA A 387 ? 1.86061 0.99806 0.72255 -0.63122 0.09307  0.04657  379 ALA A CB  
2975 N N   . LYS A 388 ? 1.92645 1.15981 0.83305 -0.69514 0.11411  0.04003  380 LYS A N   
2976 C CA  . LYS A 388 ? 2.03935 1.29463 0.95464 -0.73180 0.12055  0.03405  380 LYS A CA  
2977 C C   . LYS A 388 ? 1.97449 1.28444 0.91742 -0.74224 0.13521  0.03320  380 LYS A C   
2978 O O   . LYS A 388 ? 1.98942 1.33444 0.95152 -0.77194 0.14273  0.02625  380 LYS A O   
2979 C CB  . LYS A 388 ? 2.07977 1.35700 1.01429 -0.74950 0.11471  0.02533  380 LYS A CB  
2980 C CG  . LYS A 388 ? 2.00158 1.35659 0.99236 -0.74040 0.11347  0.01722  380 LYS A CG  
2981 C CD  . LYS A 388 ? 2.11311 1.49983 1.13008 -0.75903 0.10471  0.00542  380 LYS A CD  
2982 C CE  . LYS A 388 ? 2.12347 1.46668 1.11553 -0.75156 0.08963  0.00220  380 LYS A CE  
2983 N NZ  . LYS A 388 ? 2.10957 1.45916 1.11101 -0.71285 0.07952  0.00208  380 LYS A NZ  
2984 N N   . GLN A 389 ? 1.87406 1.19124 0.81965 -0.71892 0.13928  0.03871  381 GLN A N   
2985 C CA  . GLN A 389 ? 1.83972 1.19172 0.79862 -0.72671 0.15342  0.03828  381 GLN A CA  
2986 C C   . GLN A 389 ? 1.88033 1.17711 0.79696 -0.72503 0.15172  0.04589  381 GLN A C   
2987 O O   . GLN A 389 ? 1.84640 1.15333 0.75854 -0.74807 0.16195  0.04441  381 GLN A O   
2988 C CB  . GLN A 389 ? 1.80675 1.20210 0.79540 -0.70291 0.15820  0.03862  381 GLN A CB  
2989 C CG  . GLN A 389 ? 1.76169 1.22031 0.78442 -0.71905 0.17541  0.03164  381 GLN A CG  
2990 C CD  . GLN A 389 ? 1.82810 1.31851 0.87167 -0.69340 0.18035  0.03249  381 GLN A CD  
2991 O OE1 . GLN A 389 ? 1.79663 1.27625 0.83981 -0.66448 0.17086  0.03708  381 GLN A OE1 
2992 N NE2 . GLN A 389 ? 1.74250 1.27319 0.80445 -0.70394 0.19581  0.02695  381 GLN A NE2 
2993 N N   . ALA A 390 ? 1.94198 1.18335 0.82970 -0.69936 0.13903  0.05343  382 ALA A N   
2994 C CA  . ALA A 390 ? 1.91971 1.09985 0.76538 -0.69521 0.13279  0.06188  382 ALA A CA  
2995 C C   . ALA A 390 ? 1.93816 1.07305 0.75444 -0.71663 0.12702  0.06138  382 ALA A C   
2996 O O   . ALA A 390 ? 2.03977 1.12912 0.82174 -0.72240 0.12369  0.06799  382 ALA A O   
2997 C CB  . ALA A 390 ? 1.86867 1.01347 0.70230 -0.65858 0.12121  0.06847  382 ALA A CB  
2998 N N   . ASP A 391 ? 1.96702 1.11308 0.79563 -0.72778 0.12492  0.05406  383 ASP A N   
2999 C CA  . ASP A 391 ? 2.02923 1.13686 0.83400 -0.74840 0.11929  0.05149  383 ASP A CA  
3000 C C   . ASP A 391 ? 2.02400 1.05763 0.79028 -0.72769 0.10557  0.05780  383 ASP A C   
3001 O O   . ASP A 391 ? 2.08485 1.07342 0.81851 -0.73755 0.10255  0.06312  383 ASP A O   
3002 C CB  . ASP A 391 ? 2.02149 1.13754 0.81856 -0.78185 0.12880  0.05070  383 ASP A CB  
3003 C CG  . ASP A 391 ? 2.11163 1.20048 0.89155 -0.80614 0.12476  0.04658  383 ASP A CG  
3004 O OD1 . ASP A 391 ? 2.17839 1.25468 0.96023 -0.80063 0.11607  0.04174  383 ASP A OD1 
3005 O OD2 . ASP A 391 ? 2.14260 1.22266 0.90645 -0.83088 0.13046  0.04796  383 ASP A OD2 
3006 N N   . ARG A 392 ? 1.98576 1.00852 0.75677 -0.70005 0.09778  0.05706  384 ARG A N   
3007 C CA  . ARG A 392 ? 2.04516 1.00211 0.78618 -0.67755 0.08508  0.06026  384 ARG A CA  
3008 C C   . ARG A 392 ? 2.09348 1.05007 0.84387 -0.66822 0.07992  0.05196  384 ARG A C   
3009 O O   . ARG A 392 ? 1.99864 1.00641 0.78003 -0.66563 0.08433  0.04807  384 ARG A O   
3010 C CB  . ARG A 392 ? 2.02802 0.97026 0.76395 -0.64731 0.08143  0.06883  384 ARG A CB  
3011 C CG  . ARG A 392 ? 2.10602 1.04257 0.82798 -0.65570 0.08466  0.07735  384 ARG A CG  
3012 C CD  . ARG A 392 ? 2.17648 1.05133 0.85885 -0.66754 0.07711  0.08264  384 ARG A CD  
3013 N NE  . ARG A 392 ? 2.13153 0.98750 0.79468 -0.66507 0.07534  0.09322  384 ARG A NE  
3014 C CZ  . ARG A 392 ? 2.15701 1.02769 0.81290 -0.69049 0.08364  0.09640  384 ARG A CZ  
3015 N NH1 . ARG A 392 ? 2.15682 1.06352 0.82545 -0.72068 0.09507  0.08941  384 ARG A NH1 
3016 N NH2 . ARG A 392 ? 2.18496 1.03422 0.82046 -0.68621 0.08028  0.10634  384 ARG A NH2 
3017 N N   . ARG A 393 ? 2.09453 0.99557 0.81907 -0.66379 0.07086  0.04904  385 ARG A N   
3018 C CA  . ARG A 393 ? 2.01770 0.90973 0.74541 -0.65565 0.06561  0.03940  385 ARG A CA  
3019 C C   . ARG A 393 ? 2.00481 0.88438 0.73483 -0.61978 0.06174  0.04155  385 ARG A C   
3020 O O   . ARG A 393 ? 2.00472 0.85174 0.71996 -0.60081 0.05798  0.04935  385 ARG A O   
3021 C CB  . ARG A 393 ? 2.14787 0.98663 0.84827 -0.66561 0.05879  0.03353  385 ARG A CB  
3022 C CG  . ARG A 393 ? 2.22376 1.07140 0.91977 -0.70065 0.06244  0.03225  385 ARG A CG  
3023 C CD  . ARG A 393 ? 2.32680 1.15128 1.01221 -0.71492 0.05745  0.02137  385 ARG A CD  
3024 N NE  . ARG A 393 ? 2.36801 1.12480 1.02431 -0.69882 0.04911  0.02064  385 ARG A NE  
3025 C CZ  . ARG A 393 ? 2.42815 1.15966 1.07961 -0.68602 0.04340  0.00974  385 ARG A CZ  
3026 N NH1 . ARG A 393 ? 2.47536 1.24174 1.14556 -0.68836 0.04401  -0.00112 385 ARG A NH1 
3027 N NH2 . ARG A 393 ? 2.47490 1.14656 1.10355 -0.67090 0.03660  0.00897  385 ARG A NH2 
3028 N N   . ILE A 394 ? 1.98419 0.88971 0.73233 -0.61172 0.06207  0.03513  386 ILE A N   
3029 C CA  . ILE A 394 ? 1.91516 0.81527 0.66819 -0.57869 0.05981  0.03610  386 ILE A CA  
3030 C C   . ILE A 394 ? 1.97444 0.87774 0.73576 -0.56813 0.05399  0.02013  386 ILE A C   
3031 O O   . ILE A 394 ? 2.01156 0.94390 0.78394 -0.58880 0.05371  0.01182  386 ILE A O   
3032 C CB  . ILE A 394 ? 1.85240 0.81876 0.63967 -0.56511 0.06533  0.04094  386 ILE A CB  
3033 C CG1 . ILE A 394 ? 1.82255 0.85619 0.64313 -0.58359 0.06892  0.03450  386 ILE A CG1 
3034 C CG2 . ILE A 394 ? 1.85891 0.82362 0.64165 -0.56245 0.06880  0.05231  386 ILE A CG2 
3035 C CD1 . ILE A 394 ? 1.76873 0.86707 0.62890 -0.56231 0.07069  0.03414  386 ILE A CD1 
3036 N N   . LYS A 395 ? 1.91072 0.78632 0.66703 -0.53770 0.04954  0.01558  387 LYS A N   
3037 C CA  . LYS A 395 ? 1.88687 0.77044 0.65210 -0.52259 0.04597  -0.00006 387 LYS A CA  
3038 C C   . LYS A 395 ? 1.85618 0.78655 0.65054 -0.49254 0.04718  0.00089  387 LYS A C   
3039 O O   . LYS A 395 ? 1.89219 0.80544 0.68510 -0.46915 0.04720  0.00761  387 LYS A O   
3040 C CB  . LYS A 395 ? 1.93767 0.75176 0.67539 -0.51286 0.04155  -0.00853 387 LYS A CB  
3041 C CG  . LYS A 395 ? 1.93349 0.74938 0.67416 -0.50296 0.03979  -0.02708 387 LYS A CG  
3042 C CD  . LYS A 395 ? 1.99251 0.73881 0.70589 -0.50053 0.03654  -0.03831 387 LYS A CD  
3043 C CE  . LYS A 395 ? 1.98499 0.73202 0.70259 -0.48193 0.03709  -0.05726 387 LYS A CE  
3044 N NZ  . LYS A 395 ? 2.07760 0.75577 0.77276 -0.47486 0.03471  -0.06930 387 LYS A NZ  
3045 N N   . LEU A 396 ? 1.86415 0.85056 0.68377 -0.49403 0.04704  -0.00488 388 LEU A N   
3046 C CA  . LEU A 396 ? 1.75882 0.79627 0.60888 -0.46977 0.04793  -0.00274 388 LEU A CA  
3047 C C   . LEU A 396 ? 1.74454 0.77604 0.59468 -0.44792 0.04559  -0.01471 388 LEU A C   
3048 O O   . LEU A 396 ? 1.79082 0.80930 0.62831 -0.45947 0.04300  -0.02660 388 LEU A O   
3049 C CB  . LEU A 396 ? 1.70648 0.80836 0.58541 -0.48529 0.04782  -0.00090 388 LEU A CB  
3050 C CG  . LEU A 396 ? 1.67099 0.79936 0.56395 -0.49500 0.05328  0.01096  388 LEU A CG  
3051 C CD1 . LEU A 396 ? 1.66877 0.85113 0.58759 -0.51812 0.05272  0.00922  388 LEU A CD1 
3052 C CD2 . LEU A 396 ? 1.64793 0.79846 0.55914 -0.46711 0.05602  0.01812  388 LEU A CD2 
3053 N N   . TYR A 397 ? 1.72524 0.76567 0.58825 -0.41865 0.04709  -0.01220 389 TYR A N   
3054 C CA  . TYR A 397 ? 1.66128 0.71621 0.53408 -0.39705 0.04690  -0.02186 389 TYR A CA  
3055 C C   . TYR A 397 ? 1.63364 0.74715 0.53844 -0.38460 0.04735  -0.01424 389 TYR A C   
3056 O O   . TYR A 397 ? 1.64170 0.76452 0.55732 -0.37633 0.04942  -0.00327 389 TYR A O   
3057 C CB  . TYR A 397 ? 1.67841 0.68796 0.53943 -0.37274 0.04838  -0.02747 389 TYR A CB  
3058 C CG  . TYR A 397 ? 1.80365 0.75538 0.63617 -0.38148 0.04734  -0.03861 389 TYR A CG  
3059 C CD1 . TYR A 397 ? 1.79798 0.70526 0.61019 -0.39479 0.04519  -0.03234 389 TYR A CD1 
3060 C CD2 . TYR A 397 ? 1.80008 0.74004 0.62475 -0.37725 0.04875  -0.05588 389 TYR A CD2 
3061 C CE1 . TYR A 397 ? 1.85210 0.70335 0.63892 -0.40251 0.04336  -0.04279 389 TYR A CE1 
3062 C CE2 . TYR A 397 ? 1.82394 0.71024 0.62378 -0.38480 0.04821  -0.06814 389 TYR A CE2 
3063 C CZ  . TYR A 397 ? 1.88760 0.72863 0.66946 -0.39683 0.04495  -0.06151 389 TYR A CZ  
3064 O OH  . TYR A 397 ? 1.96959 0.75492 0.72774 -0.40399 0.04357  -0.07370 389 TYR A OH  
3065 N N   . ALA A 398 ? 1.60531 0.75534 0.52301 -0.38484 0.04481  -0.01970 390 ALA A N   
3066 C CA  . ALA A 398 ? 1.52072 0.72498 0.46920 -0.37272 0.04352  -0.01364 390 ALA A CA  
3067 C C   . ALA A 398 ? 1.54731 0.75202 0.49743 -0.34986 0.04493  -0.02058 390 ALA A C   
3068 O O   . ALA A 398 ? 1.57371 0.79501 0.52244 -0.35507 0.04168  -0.02712 390 ALA A O   
3069 C CB  . ALA A 398 ? 1.50750 0.75341 0.47018 -0.39342 0.03737  -0.01275 390 ALA A CB  
3070 N N   . VAL A 399 ? 1.49988 0.68628 0.45181 -0.32654 0.04936  -0.01933 391 VAL A N   
3071 C CA  . VAL A 399 ? 1.51894 0.70724 0.47631 -0.30308 0.05250  -0.02615 391 VAL A CA  
3072 C C   . VAL A 399 ? 1.46888 0.70996 0.45431 -0.29481 0.05053  -0.01874 391 VAL A C   
3073 O O   . VAL A 399 ? 1.48094 0.74355 0.48512 -0.29073 0.04989  -0.00787 391 VAL A O   
3074 C CB  . VAL A 399 ? 1.49424 0.64808 0.44877 -0.28112 0.05623  -0.02690 391 VAL A CB  
3075 C CG1 . VAL A 399 ? 1.47510 0.63640 0.44038 -0.25743 0.06035  -0.03450 391 VAL A CG1 
3076 C CG2 . VAL A 399 ? 1.54774 0.64590 0.47559 -0.28833 0.05633  -0.03395 391 VAL A CG2 
3077 N N   . GLU A 400 ? 1.42360 0.68318 0.41018 -0.29363 0.04950  -0.02462 392 GLU A N   
3078 C CA  . GLU A 400 ? 1.38043 0.68644 0.39165 -0.28612 0.04608  -0.01772 392 GLU A CA  
3079 C C   . GLU A 400 ? 1.38889 0.69466 0.39385 -0.27532 0.04954  -0.02627 392 GLU A C   
3080 O O   . GLU A 400 ? 1.42533 0.71566 0.40742 -0.28743 0.04987  -0.03648 392 GLU A O   
3081 C CB  . GLU A 400 ? 1.37295 0.71120 0.39262 -0.30687 0.03689  -0.01233 392 GLU A CB  
3082 C CG  . GLU A 400 ? 1.33306 0.71630 0.37884 -0.29964 0.03092  -0.00481 392 GLU A CG  
3083 C CD  . GLU A 400 ? 1.33756 0.73771 0.40914 -0.27825 0.03458  0.00277  392 GLU A CD  
3084 O OE1 . GLU A 400 ? 1.29857 0.70756 0.38434 -0.27968 0.03522  0.00898  392 GLU A OE1 
3085 O OE2 . GLU A 400 ? 1.34664 0.75080 0.42302 -0.26125 0.03742  0.00177  392 GLU A OE2 
3086 N N   . LYS A 401 ? 1.35844 0.68125 0.38241 -0.25469 0.05258  -0.02275 393 LYS A N   
3087 C CA  . LYS A 401 ? 1.35756 0.68258 0.37855 -0.24334 0.05792  -0.03048 393 LYS A CA  
3088 C C   . LYS A 401 ? 1.34578 0.70800 0.37791 -0.25137 0.05060  -0.02494 393 LYS A C   
3089 O O   . LYS A 401 ? 1.35375 0.71762 0.38132 -0.25128 0.05357  -0.03218 393 LYS A O   
3090 C CB  . LYS A 401 ? 1.32762 0.65588 0.36862 -0.21801 0.06365  -0.02871 393 LYS A CB  
3091 C CG  . LYS A 401 ? 1.31957 0.68437 0.38971 -0.20985 0.05868  -0.01481 393 LYS A CG  
3092 C CD  . LYS A 401 ? 1.34875 0.73589 0.43398 -0.19561 0.06113  -0.01413 393 LYS A CD  
3093 C CE  . LYS A 401 ? 1.32434 0.75133 0.43258 -0.19773 0.05259  -0.00181 393 LYS A CE  
3094 N NZ  . LYS A 401 ? 1.25605 0.70310 0.37803 -0.18856 0.05356  -0.00158 393 LYS A NZ  
3095 N N   . ASN A 402 ? 1.30081 0.69295 0.35099 -0.25722 0.04118  -0.01265 394 ASN A N   
3096 C CA  . ASN A 402 ? 1.30783 0.73563 0.37282 -0.26387 0.03061  -0.00543 394 ASN A CA  
3097 C C   . ASN A 402 ? 1.37739 0.79931 0.42184 -0.28665 0.02379  -0.01018 394 ASN A C   
3098 O O   . ASN A 402 ? 1.41017 0.82984 0.44691 -0.30284 0.01808  -0.00860 394 ASN A O   
3099 C CB  . ASN A 402 ? 1.27841 0.73678 0.36714 -0.26285 0.02267  0.00726  394 ASN A CB  
3100 C CG  . ASN A 402 ? 1.28226 0.77373 0.38550 -0.26639 0.01034  0.01537  394 ASN A CG  
3101 O OD1 . ASN A 402 ? 1.30340 0.79537 0.39762 -0.27205 0.00660  0.01280  394 ASN A OD1 
3102 N ND2 . ASN A 402 ? 1.28647 0.80849 0.42165 -0.26153 0.00346  0.02474  394 ASN A ND2 
3103 N N   . PRO A 403 ? 1.32886 0.74917 0.36333 -0.29006 0.02424  -0.01622 395 PRO A N   
3104 C CA  . PRO A 403 ? 1.39880 0.80979 0.41094 -0.31169 0.01870  -0.02227 395 PRO A CA  
3105 C C   . PRO A 403 ? 1.35911 0.79799 0.37798 -0.32798 0.00096  -0.01189 395 PRO A C   
3106 O O   . PRO A 403 ? 1.38706 0.81808 0.38900 -0.34784 -0.00533 -0.01565 395 PRO A O   
3107 C CB  . PRO A 403 ? 1.37594 0.78291 0.37933 -0.30849 0.02510  -0.03007 395 PRO A CB  
3108 C CG  . PRO A 403 ? 1.33939 0.76957 0.36685 -0.29009 0.02628  -0.02188 395 PRO A CG  
3109 C CD  . PRO A 403 ? 1.32859 0.75752 0.37221 -0.27525 0.03010  -0.01736 395 PRO A CD  
3110 N N   . ASN A 404 ? 1.32629 0.79590 0.36915 -0.31946 -0.00727 0.00027  396 ASN A N   
3111 C CA  . ASN A 404 ? 1.31998 0.81833 0.37228 -0.33230 -0.02611 0.01096  396 ASN A CA  
3112 C C   . ASN A 404 ? 1.34707 0.84759 0.40322 -0.34282 -0.02857 0.01173  396 ASN A C   
3113 O O   . ASN A 404 ? 1.33349 0.84752 0.39190 -0.36103 -0.04203 0.01324  396 ASN A O   
3114 C CB  . ASN A 404 ? 1.28610 0.81265 0.36345 -0.31823 -0.03318 0.02301  396 ASN A CB  
3115 C CG  . ASN A 404 ? 1.32556 0.84994 0.40231 -0.30724 -0.02817 0.02227  396 ASN A CG  
3116 O OD1 . ASN A 404 ? 1.35578 0.87957 0.41863 -0.31811 -0.03488 0.02170  396 ASN A OD1 
3117 N ND2 . ASN A 404 ? 1.29065 0.81420 0.38153 -0.28698 -0.01633 0.02216  396 ASN A ND2 
3118 N N   . ALA A 405 ? 1.35880 0.85112 0.42830 -0.32969 -0.01595 0.01061  397 ALA A N   
3119 C CA  . ALA A 405 ? 1.30113 0.79678 0.38633 -0.33607 -0.01401 0.01104  397 ALA A CA  
3120 C C   . ALA A 405 ? 1.34326 0.80664 0.39727 -0.35509 -0.01076 0.00130  397 ALA A C   
3121 O O   . ALA A 405 ? 1.36664 0.83940 0.42892 -0.37166 -0.01609 0.00183  397 ALA A O   
3122 C CB  . ALA A 405 ? 1.27741 0.76872 0.37827 -0.31671 -0.00174 0.01317  397 ALA A CB  
3123 N N   . VAL A 406 ? 1.37056 0.79802 0.39176 -0.35298 -0.00194 -0.00830 398 VAL A N   
3124 C CA  . VAL A 406 ? 1.41529 0.80588 0.40360 -0.36950 0.00202  -0.01990 398 VAL A CA  
3125 C C   . VAL A 406 ? 1.43645 0.83985 0.41562 -0.39450 -0.01214 -0.02091 398 VAL A C   
3126 O O   . VAL A 406 ? 1.46527 0.85104 0.43111 -0.41239 -0.01250 -0.02681 398 VAL A O   
3127 C CB  . VAL A 406 ? 1.43544 0.79375 0.40199 -0.35910 0.01340  -0.03136 398 VAL A CB  
3128 C CG1 . VAL A 406 ? 1.48265 0.80815 0.41901 -0.37686 0.01525  -0.04437 398 VAL A CG1 
3129 C CG2 . VAL A 406 ? 1.42401 0.76269 0.39454 -0.33729 0.02613  -0.03234 398 VAL A CG2 
3130 N N   . VAL A 407 ? 1.42533 0.85673 0.41060 -0.39621 -0.02442 -0.01506 399 VAL A N   
3131 C CA  . VAL A 407 ? 1.44868 0.89627 0.42755 -0.41910 -0.04185 -0.01428 399 VAL A CA  
3132 C C   . VAL A 407 ? 1.47031 0.94251 0.48001 -0.42978 -0.04949 -0.00936 399 VAL A C   
3133 O O   . VAL A 407 ? 1.50496 0.97251 0.50297 -0.45230 -0.05657 -0.01463 399 VAL A O   
3134 C CB  . VAL A 407 ? 1.42993 0.90547 0.42029 -0.41411 -0.05493 -0.00557 399 VAL A CB  
3135 C CG1 . VAL A 407 ? 1.44598 0.94323 0.43485 -0.43622 -0.07718 -0.00171 399 VAL A CG1 
3136 C CG2 . VAL A 407 ? 1.44063 0.89922 0.41898 -0.40432 -0.04534 -0.01130 399 VAL A CG2 
3137 N N   . THR A 408 ? 1.39256 0.89064 0.44028 -0.41495 -0.04735 -0.00077 400 THR A N   
3138 C CA  . THR A 408 ? 1.42006 0.94709 0.50277 -0.42319 -0.05173 0.00311  400 THR A CA  
3139 C C   . THR A 408 ? 1.40286 0.90076 0.46928 -0.43681 -0.04050 -0.00419 400 THR A C   
3140 O O   . THR A 408 ? 1.44167 0.95290 0.51743 -0.45748 -0.04728 -0.00596 400 THR A O   
3141 C CB  . THR A 408 ? 1.34584 0.90188 0.46831 -0.40257 -0.04809 0.01156  400 THR A CB  
3142 O OG1 . THR A 408 ? 1.31220 0.88266 0.44126 -0.38770 -0.05579 0.01773  400 THR A OG1 
3143 C CG2 . THR A 408 ? 1.31687 0.91278 0.48049 -0.41131 -0.05499 0.01457  400 THR A CG2 
3144 N N   . LEU A 409 ? 1.41323 0.87246 0.45697 -0.42582 -0.02495 -0.00825 401 LEU A N   
3145 C CA  . LEU A 409 ? 1.47886 0.90221 0.50418 -0.43561 -0.01394 -0.01381 401 LEU A CA  
3146 C C   . LEU A 409 ? 1.54013 0.93777 0.53361 -0.45924 -0.01851 -0.02385 401 LEU A C   
3147 O O   . LEU A 409 ? 1.52984 0.92424 0.52392 -0.47942 -0.01927 -0.02572 401 LEU A O   
3148 C CB  . LEU A 409 ? 1.44296 0.83038 0.45234 -0.41473 0.00029  -0.01561 401 LEU A CB  
3149 C CG  . LEU A 409 ? 1.42034 0.82702 0.45753 -0.39254 0.00610  -0.00660 401 LEU A CG  
3150 C CD1 . LEU A 409 ? 1.41563 0.78773 0.43644 -0.37132 0.01718  -0.00946 401 LEU A CD1 
3151 C CD2 . LEU A 409 ? 1.43741 0.85648 0.49348 -0.40130 0.00944  -0.00137 401 LEU A CD2 
3152 N N   . GLU A 410 ? 1.54097 0.92054 0.50675 -0.45774 -0.02039 -0.03083 402 GLU A N   
3153 C CA  . GLU A 410 ? 1.55552 0.90619 0.48569 -0.47895 -0.02347 -0.04283 402 GLU A CA  
3154 C C   . GLU A 410 ? 1.56183 0.94355 0.50310 -0.50317 -0.04025 -0.04106 402 GLU A C   
3155 O O   . GLU A 410 ? 1.61606 0.97816 0.53929 -0.52557 -0.04192 -0.04904 402 GLU A O   
3156 C CB  . GLU A 410 ? 1.57158 0.90280 0.47230 -0.47097 -0.02071 -0.05096 402 GLU A CB  
3157 C CG  . GLU A 410 ? 1.57849 0.87123 0.46491 -0.45158 -0.00368 -0.05777 402 GLU A CG  
3158 C CD  . GLU A 410 ? 1.60767 0.89178 0.48807 -0.43823 0.00290  -0.06502 402 GLU A CD  
3159 O OE1 . GLU A 410 ? 1.60181 0.91691 0.49504 -0.43429 -0.00398 -0.05927 402 GLU A OE1 
3160 O OE2 . GLU A 410 ? 1.65771 0.90381 0.52089 -0.43212 0.01487  -0.07669 402 GLU A OE2 
3161 N N   . ASN A 411 ? 1.52889 0.95661 0.50031 -0.49869 -0.05303 -0.03130 403 ASN A N   
3162 C CA  . ASN A 411 ? 1.55800 1.02313 0.55143 -0.51849 -0.07119 -0.02825 403 ASN A CA  
3163 C C   . ASN A 411 ? 1.59249 1.06649 0.60944 -0.53015 -0.06610 -0.02791 403 ASN A C   
3164 O O   . ASN A 411 ? 1.64532 1.12173 0.65908 -0.55514 -0.07379 -0.03320 403 ASN A O   
3165 C CB  . ASN A 411 ? 1.50479 1.01588 0.53091 -0.50716 -0.08606 -0.01727 403 ASN A CB  
3166 C CG  . ASN A 411 ? 1.54494 1.05802 0.54796 -0.51479 -0.10248 -0.01755 403 ASN A CG  
3167 O OD1 . ASN A 411 ? 1.56238 1.10483 0.58046 -0.52849 -0.12265 -0.01425 403 ASN A OD1 
3168 N ND2 . ASN A 411 ? 1.52931 1.01150 0.49544 -0.50685 -0.09432 -0.02186 403 ASN A ND2 
3169 N N   . TRP A 412 ? 1.59586 1.07381 0.63363 -0.51394 -0.05323 -0.02226 404 TRP A N   
3170 C CA  . TRP A 412 ? 1.55533 1.04216 0.61444 -0.52401 -0.04545 -0.02091 404 TRP A CA  
3171 C C   . TRP A 412 ? 1.60654 1.04258 0.62948 -0.53915 -0.03455 -0.02851 404 TRP A C   
3172 O O   . TRP A 412 ? 1.60881 1.04962 0.63933 -0.56108 -0.03383 -0.03033 404 TRP A O   
3173 C CB  . TRP A 412 ? 1.55721 1.06107 0.64396 -0.50131 -0.03520 -0.01268 404 TRP A CB  
3174 C CG  . TRP A 412 ? 1.64581 1.17598 0.76358 -0.51180 -0.02987 -0.01040 404 TRP A CG  
3175 C CD1 . TRP A 412 ? 1.66619 1.17137 0.77285 -0.51848 -0.01507 -0.01051 404 TRP A CD1 
3176 C CD2 . TRP A 412 ? 1.67660 1.26338 0.84185 -0.51758 -0.03888 -0.00829 404 TRP A CD2 
3177 N NE1 . TRP A 412 ? 1.59011 1.13291 0.73154 -0.52960 -0.01239 -0.00891 404 TRP A NE1 
3178 C CE2 . TRP A 412 ? 1.66872 1.26346 0.84907 -0.52862 -0.02641 -0.00859 404 TRP A CE2 
3179 C CE3 . TRP A 412 ? 1.60832 1.23901 0.80511 -0.51473 -0.05680 -0.00638 404 TRP A CE3 
3180 C CZ2 . TRP A 412 ? 1.60444 1.25240 0.83264 -0.53660 -0.02930 -0.00912 404 TRP A CZ2 
3181 C CZ3 . TRP A 412 ? 1.63957 1.32148 0.88569 -0.52088 -0.06183 -0.00630 404 TRP A CZ3 
3182 C CH2 . TRP A 412 ? 1.64144 1.33330 0.90427 -0.53158 -0.04725 -0.00866 404 TRP A CH2 
3183 N N   . GLN A 413 ? 1.60723 0.99668 0.59385 -0.52834 -0.02655 -0.03343 405 GLN A N   
3184 C CA  . GLN A 413 ? 1.63477 0.96907 0.58512 -0.53950 -0.01729 -0.04164 405 GLN A CA  
3185 C C   . GLN A 413 ? 1.64333 0.97068 0.57600 -0.56860 -0.02712 -0.05099 405 GLN A C   
3186 O O   . GLN A 413 ? 1.67233 0.98088 0.59738 -0.58926 -0.02383 -0.05398 405 GLN A O   
3187 C CB  . GLN A 413 ? 1.69049 0.98274 0.61222 -0.51864 -0.00846 -0.04683 405 GLN A CB  
3188 C CG  . GLN A 413 ? 1.72389 0.95749 0.61427 -0.52413 0.00138  -0.05419 405 GLN A CG  
3189 C CD  . GLN A 413 ? 1.74388 0.94681 0.60172 -0.54453 -0.00264 -0.06809 405 GLN A CD  
3190 O OE1 . GLN A 413 ? 1.80646 1.02817 0.65922 -0.55277 -0.01215 -0.07318 405 GLN A OE1 
3191 N NE2 . GLN A 413 ? 1.82233 0.97537 0.65612 -0.55328 0.00394  -0.07437 405 GLN A NE2 
3192 N N   . PHE A 414 ? 1.64691 0.98757 0.57133 -0.57119 -0.03904 -0.05516 406 PHE A N   
3193 C CA  . PHE A 414 ? 1.70622 1.04286 0.61175 -0.59855 -0.05098 -0.06452 406 PHE A CA  
3194 C C   . PHE A 414 ? 1.67681 1.05419 0.61531 -0.62002 -0.06116 -0.06056 406 PHE A C   
3195 O O   . PHE A 414 ? 1.76384 1.12493 0.68979 -0.64570 -0.06253 -0.06783 406 PHE A O   
3196 C CB  . PHE A 414 ? 1.68717 1.03460 0.57807 -0.59509 -0.06267 -0.06727 406 PHE A CB  
3197 C CG  . PHE A 414 ? 1.72274 1.07439 0.59750 -0.62315 -0.07833 -0.07512 406 PHE A CG  
3198 C CD1 . PHE A 414 ? 1.76901 1.08027 0.61131 -0.63361 -0.07266 -0.08665 406 PHE A CD1 
3199 C CD2 . PHE A 414 ? 1.72380 1.12470 0.62795 -0.63446 -0.09760 -0.06869 406 PHE A CD2 
3200 C CE1 . PHE A 414 ? 1.79794 1.11845 0.63578 -0.65474 -0.08496 -0.09074 406 PHE A CE1 
3201 C CE2 . PHE A 414 ? 1.74004 1.14608 0.63156 -0.65972 -0.11340 -0.07517 406 PHE A CE2 
3202 C CZ  . PHE A 414 ? 1.78351 1.15126 0.64548 -0.66769 -0.10547 -0.08457 406 PHE A CZ  
3203 N N   . GLU A 415 ? 1.63168 1.06075 0.61281 -0.60987 -0.06787 -0.05042 407 GLU A N   
3204 C CA  . GLU A 415 ? 1.61862 1.09699 0.63987 -0.62760 -0.07966 -0.04786 407 GLU A CA  
3205 C C   . GLU A 415 ? 1.64610 1.12158 0.68145 -0.63970 -0.06610 -0.04751 407 GLU A C   
3206 O O   . GLU A 415 ? 1.67448 1.15825 0.71531 -0.66727 -0.07120 -0.05292 407 GLU A O   
3207 C CB  . GLU A 415 ? 1.57020 1.10205 0.63467 -0.60962 -0.09007 -0.03820 407 GLU A CB  
3208 C CG  . GLU A 415 ? 1.57275 1.11867 0.62975 -0.60767 -0.11011 -0.03726 407 GLU A CG  
3209 C CD  . GLU A 415 ? 1.66292 1.25488 0.76007 -0.58767 -0.12116 -0.02669 407 GLU A CD  
3210 O OE1 . GLU A 415 ? 1.69320 1.29016 0.80774 -0.56537 -0.10871 -0.02064 407 GLU A OE1 
3211 O OE2 . GLU A 415 ? 1.71832 1.33997 0.82919 -0.59456 -0.14332 -0.02445 407 GLU A OE2 
3212 N N   . GLU A 416 ? 1.60174 1.06603 0.64159 -0.62139 -0.04991 -0.04136 408 GLU A N   
3213 C CA  . GLU A 416 ? 1.61238 1.08700 0.67350 -0.63008 -0.03751 -0.03791 408 GLU A CA  
3214 C C   . GLU A 416 ? 1.62858 1.04318 0.65171 -0.63198 -0.02113 -0.03852 408 GLU A C   
3215 O O   . GLU A 416 ? 1.66491 1.06015 0.67538 -0.65820 -0.01779 -0.04273 408 GLU A O   
3216 C CB  . GLU A 416 ? 1.57654 1.09437 0.67878 -0.60817 -0.03402 -0.02932 408 GLU A CB  
3217 C CG  . GLU A 416 ? 1.57928 1.15547 0.72315 -0.60439 -0.05149 -0.02804 408 GLU A CG  
3218 C CD  . GLU A 416 ? 1.61891 1.23361 0.79261 -0.63187 -0.06158 -0.03332 408 GLU A CD  
3219 O OE1 . GLU A 416 ? 1.68720 1.31259 0.87721 -0.64689 -0.05019 -0.03481 408 GLU A OE1 
3220 O OE2 . GLU A 416 ? 1.70950 1.34387 0.88981 -0.63898 -0.08106 -0.03601 408 GLU A OE2 
3221 N N   . TRP A 417 ? 1.61803 1.00465 0.62539 -0.60561 -0.01217 -0.03420 409 TRP A N   
3222 C CA  . TRP A 417 ? 1.64378 0.97726 0.62216 -0.60193 0.00227  -0.03209 409 TRP A CA  
3223 C C   . TRP A 417 ? 1.70115 0.98007 0.63871 -0.62114 0.00207  -0.04117 409 TRP A C   
3224 O O   . TRP A 417 ? 1.80964 1.06644 0.73686 -0.64234 0.00808  -0.04067 409 TRP A O   
3225 C CB  . TRP A 417 ? 1.66906 0.98496 0.63987 -0.56828 0.00813  -0.02764 409 TRP A CB  
3226 C CG  . TRP A 417 ? 1.62865 0.98756 0.63510 -0.54953 0.01136  -0.01837 409 TRP A CG  
3227 C CD1 . TRP A 417 ? 1.62278 1.01649 0.65829 -0.55857 0.01610  -0.01309 409 TRP A CD1 
3228 C CD2 . TRP A 417 ? 1.55955 0.93023 0.57605 -0.51893 0.01122  -0.01447 409 TRP A CD2 
3229 N NE1 . TRP A 417 ? 1.59203 1.01813 0.65508 -0.53516 0.01837  -0.00679 409 TRP A NE1 
3230 C CE2 . TRP A 417 ? 1.58792 0.99994 0.63987 -0.51065 0.01500  -0.00687 409 TRP A CE2 
3231 C CE3 . TRP A 417 ? 1.53942 0.89085 0.53903 -0.49889 0.00909  -0.01760 409 TRP A CE3 
3232 C CZ2 . TRP A 417 ? 1.55015 0.98284 0.62061 -0.48297 0.01542  -0.00183 409 TRP A CZ2 
3233 C CZ3 . TRP A 417 ? 1.57588 0.94878 0.59397 -0.47239 0.01006  -0.01208 409 TRP A CZ3 
3234 C CH2 . TRP A 417 ? 1.52690 0.93902 0.57978 -0.46443 0.01257  -0.00399 409 TRP A CH2 
3235 N N   . GLY A 418 ? 1.71629 0.97356 0.63070 -0.61454 -0.00395 -0.04960 410 GLY A N   
3236 C CA  . GLY A 418 ? 1.77346 0.97423 0.64707 -0.62792 -0.00332 -0.06070 410 GLY A CA  
3237 C C   . GLY A 418 ? 1.82251 0.97040 0.66986 -0.60477 0.00619  -0.06221 410 GLY A C   
3238 O O   . GLY A 418 ? 1.75272 0.91376 0.61244 -0.57699 0.00960  -0.05652 410 GLY A O   
3239 N N   . SER A 419 ? 1.84171 0.93166 0.65604 -0.61568 0.00972  -0.07001 411 SER A N   
3240 C CA  . SER A 419 ? 1.86346 0.89676 0.65203 -0.59498 0.01687  -0.07477 411 SER A CA  
3241 C C   . SER A 419 ? 1.85778 0.87266 0.65059 -0.58240 0.02463  -0.06184 411 SER A C   
3242 O O   . SER A 419 ? 1.88254 0.85432 0.65973 -0.56176 0.02905  -0.06393 411 SER A O   
3243 C CB  . SER A 419 ? 1.96050 0.93911 0.71450 -0.61188 0.01612  -0.08907 411 SER A CB  
3244 O OG  . SER A 419 ? 1.95827 0.91805 0.70512 -0.63965 0.01613  -0.08540 411 SER A OG  
3245 N N   . GLN A 420 ? 1.83909 0.88503 0.65207 -0.59464 0.02609  -0.04975 412 GLN A N   
3246 C CA  . GLN A 420 ? 1.83448 0.87141 0.65213 -0.58326 0.03335  -0.03614 412 GLN A CA  
3247 C C   . GLN A 420 ? 1.80399 0.85676 0.63594 -0.54733 0.03518  -0.03278 412 GLN A C   
3248 O O   . GLN A 420 ? 1.88211 0.89658 0.70120 -0.52892 0.03908  -0.02891 412 GLN A O   
3249 C CB  . GLN A 420 ? 1.81121 0.89105 0.65217 -0.60351 0.03583  -0.02641 412 GLN A CB  
3250 C CG  . GLN A 420 ? 1.81802 0.88382 0.65654 -0.59781 0.04401  -0.01303 412 GLN A CG  
3251 C CD  . GLN A 420 ? 1.94378 1.03723 0.79498 -0.62610 0.04907  -0.00637 412 GLN A CD  
3252 O OE1 . GLN A 420 ? 2.01670 1.15550 0.89097 -0.64489 0.04628  -0.01102 412 GLN A OE1 
3253 N NE2 . GLN A 420 ? 1.83856 0.90505 0.67473 -0.62999 0.05640  0.00436  412 GLN A NE2 
3254 N N   . VAL A 421 ? 1.74118 0.84649 0.59832 -0.53829 0.03125  -0.03428 413 VAL A N   
3255 C CA  . VAL A 421 ? 1.74198 0.86691 0.61418 -0.50596 0.03240  -0.03217 413 VAL A CA  
3256 C C   . VAL A 421 ? 1.73084 0.83506 0.58554 -0.49579 0.03019  -0.04560 413 VAL A C   
3257 O O   . VAL A 421 ? 1.75287 0.87547 0.60581 -0.51020 0.02381  -0.05316 413 VAL A O   
3258 C CB  . VAL A 421 ? 1.70165 0.89425 0.61156 -0.50231 0.02910  -0.02530 413 VAL A CB  
3259 C CG1 . VAL A 421 ? 1.60323 0.81282 0.52826 -0.47033 0.03102  -0.02162 413 VAL A CG1 
3260 C CG2 . VAL A 421 ? 1.63979 0.85795 0.56861 -0.51761 0.03235  -0.01581 413 VAL A CG2 
3261 N N   . THR A 422 ? 1.72208 0.78990 0.56446 -0.47253 0.03516  -0.04905 414 THR A N   
3262 C CA  . THR A 422 ? 1.72413 0.78144 0.55720 -0.45583 0.03632  -0.06178 414 THR A CA  
3263 C C   . THR A 422 ? 1.70852 0.80910 0.56755 -0.43207 0.03723  -0.05544 414 THR A C   
3264 O O   . THR A 422 ? 1.71018 0.80614 0.57977 -0.41146 0.04144  -0.04795 414 THR A O   
3265 C CB  . THR A 422 ? 1.78614 0.78258 0.59712 -0.44283 0.04138  -0.07053 414 THR A CB  
3266 O OG1 . THR A 422 ? 1.90975 0.86542 0.69726 -0.46643 0.03959  -0.07524 414 THR A OG1 
3267 C CG2 . THR A 422 ? 1.76865 0.75545 0.57181 -0.42667 0.04496  -0.08622 414 THR A CG2 
3268 N N   . VAL A 423 ? 1.68645 0.82644 0.55465 -0.43568 0.03231  -0.05757 415 VAL A N   
3269 C CA  . VAL A 423 ? 1.60714 0.78678 0.49826 -0.41465 0.03221  -0.05198 415 VAL A CA  
3270 C C   . VAL A 423 ? 1.60830 0.76257 0.48609 -0.39433 0.03919  -0.06310 415 VAL A C   
3271 O O   . VAL A 423 ? 1.69602 0.83487 0.55183 -0.40305 0.03940  -0.07654 415 VAL A O   
3272 C CB  . VAL A 423 ? 1.58703 0.81399 0.49083 -0.42700 0.02238  -0.04933 415 VAL A CB  
3273 C CG1 . VAL A 423 ? 1.53354 0.79602 0.45868 -0.40608 0.02161  -0.04316 415 VAL A CG1 
3274 C CG2 . VAL A 423 ? 1.58778 0.84269 0.50975 -0.44703 0.01567  -0.04077 415 VAL A CG2 
3275 N N   . VAL A 424 ? 1.58663 0.73718 0.47751 -0.36918 0.04497  -0.05873 416 VAL A N   
3276 C CA  . VAL A 424 ? 1.58966 0.72184 0.47566 -0.34685 0.05251  -0.06934 416 VAL A CA  
3277 C C   . VAL A 424 ? 1.57084 0.74699 0.47773 -0.33271 0.05248  -0.06397 416 VAL A C   
3278 O O   . VAL A 424 ? 1.60000 0.80366 0.53140 -0.32333 0.05039  -0.05041 416 VAL A O   
3279 C CB  . VAL A 424 ? 1.60065 0.69635 0.48787 -0.32835 0.05722  -0.06862 416 VAL A CB  
3280 C CG1 . VAL A 424 ? 1.59659 0.68212 0.48792 -0.30310 0.06452  -0.07918 416 VAL A CG1 
3281 C CG2 . VAL A 424 ? 1.65195 0.69815 0.51580 -0.34243 0.05634  -0.07399 416 VAL A CG2 
3282 N N   . SER A 425 ? 1.55306 0.73404 0.44888 -0.33255 0.05507  -0.07466 417 SER A N   
3283 C CA  . SER A 425 ? 1.51565 0.73330 0.42545 -0.32158 0.05531  -0.07087 417 SER A CA  
3284 C C   . SER A 425 ? 1.53897 0.74327 0.45451 -0.29642 0.06626  -0.07874 417 SER A C   
3285 O O   . SER A 425 ? 1.62522 0.82834 0.53668 -0.29360 0.07271  -0.09056 417 SER A O   
3286 C CB  . SER A 425 ? 1.52372 0.76071 0.43056 -0.33650 0.05090  -0.07475 417 SER A CB  
3287 O OG  . SER A 425 ? 1.59458 0.86759 0.52268 -0.32559 0.05012  -0.06885 417 SER A OG  
3288 N N   . SER A 426 ? 1.49767 0.69838 0.43304 -0.27792 0.06791  -0.07124 418 SER A N   
3289 C CA  . SER A 426 ? 1.48688 0.67140 0.43114 -0.25287 0.07662  -0.07881 418 SER A CA  
3290 C C   . SER A 426 ? 1.48441 0.68928 0.45686 -0.23428 0.07465  -0.06462 418 SER A C   
3291 O O   . SER A 426 ? 1.46743 0.69100 0.44985 -0.24153 0.06772  -0.05017 418 SER A O   
3292 C CB  . SER A 426 ? 1.53439 0.66930 0.46326 -0.25064 0.08008  -0.09081 418 SER A CB  
3293 O OG  . SER A 426 ? 1.57913 0.69961 0.51952 -0.22604 0.08720  -0.09983 418 SER A OG  
3294 N N   . ASP A 427 ? 1.46936 0.67177 0.45498 -0.21158 0.08105  -0.07014 419 ASP A N   
3295 C CA  . ASP A 427 ? 1.41059 0.62102 0.42015 -0.19097 0.07968  -0.06023 419 ASP A CA  
3296 C C   . ASP A 427 ? 1.49243 0.66051 0.49443 -0.18549 0.07748  -0.06092 419 ASP A C   
3297 O O   . ASP A 427 ? 1.53521 0.66769 0.52294 -0.18423 0.08107  -0.07536 419 ASP A O   
3298 C CB  . ASP A 427 ? 1.38518 0.61068 0.41209 -0.17054 0.08673  -0.06707 419 ASP A CB  
3299 C CG  . ASP A 427 ? 1.41489 0.66034 0.46833 -0.15214 0.08407  -0.05548 419 ASP A CG  
3300 O OD1 . ASP A 427 ? 1.39332 0.62411 0.44898 -0.14809 0.07871  -0.04702 419 ASP A OD1 
3301 O OD2 . ASP A 427 ? 1.50377 0.77845 0.57373 -0.14319 0.08730  -0.05492 419 ASP A OD2 
3302 N N   . MET A 428 ? 1.43819 0.60870 0.44842 -0.18284 0.07166  -0.04626 420 MET A N   
3303 C CA  . MET A 428 ? 1.45432 0.58325 0.45284 -0.18157 0.06733  -0.04279 420 MET A CA  
3304 C C   . MET A 428 ? 1.49070 0.59253 0.49668 -0.15648 0.06839  -0.05138 420 MET A C   
3305 O O   . MET A 428 ? 1.53050 0.58741 0.52242 -0.15517 0.06464  -0.05413 420 MET A O   
3306 C CB  . MET A 428 ? 1.43670 0.57929 0.44085 -0.18633 0.06198  -0.02485 420 MET A CB  
3307 C CG  . MET A 428 ? 1.40683 0.57590 0.43532 -0.16602 0.06152  -0.01747 420 MET A CG  
3308 S SD  . MET A 428 ? 1.38073 0.56759 0.41336 -0.17465 0.05722  0.00114  420 MET A SD  
3309 C CE  . MET A 428 ? 1.34740 0.58562 0.39289 -0.19274 0.05875  0.00407  420 MET A CE  
3310 N N   . ARG A 429 ? 1.46979 0.59705 0.49800 -0.13768 0.07261  -0.05575 421 ARG A N   
3311 C CA  . ARG A 429 ? 1.46935 0.57770 0.51103 -0.11257 0.07397  -0.06626 421 ARG A CA  
3312 C C   . ARG A 429 ? 1.54763 0.63063 0.57991 -0.11252 0.08096  -0.08760 421 ARG A C   
3313 O O   . ARG A 429 ? 1.63428 0.68890 0.67433 -0.09433 0.08037  -0.09818 421 ARG A O   
3314 C CB  . ARG A 429 ? 1.45964 0.60686 0.52932 -0.09513 0.07756  -0.06563 421 ARG A CB  
3315 C CG  . ARG A 429 ? 1.41675 0.58876 0.49871 -0.09191 0.07128  -0.04719 421 ARG A CG  
3316 C CD  . ARG A 429 ? 1.34161 0.56181 0.43562 -0.09889 0.07485  -0.04144 421 ARG A CD  
3317 N NE  . ARG A 429 ? 1.29590 0.54132 0.41472 -0.08052 0.07899  -0.04570 421 ARG A NE  
3318 C CZ  . ARG A 429 ? 1.40651 0.68671 0.53528 -0.08361 0.08427  -0.04683 421 ARG A CZ  
3319 N NH1 . ARG A 429 ? 1.41452 0.70894 0.53080 -0.10347 0.08479  -0.04396 421 ARG A NH1 
3320 N NH2 . ARG A 429 ? 1.41998 0.71986 0.57110 -0.06726 0.08813  -0.05063 421 ARG A NH2 
3321 N N   . GLU A 430 ? 1.53109 0.62446 0.54817 -0.13181 0.08680  -0.09441 422 GLU A N   
3322 C CA  . GLU A 430 ? 1.58371 0.65860 0.58932 -0.13502 0.09568  -0.11664 422 GLU A CA  
3323 C C   . GLU A 430 ? 1.56965 0.60337 0.54780 -0.15252 0.09197  -0.12052 422 GLU A C   
3324 O O   . GLU A 430 ? 1.60842 0.60519 0.58162 -0.14541 0.09491  -0.13764 422 GLU A O   
3325 C CB  . GLU A 430 ? 1.65039 0.76246 0.65268 -0.14697 0.10393  -0.12158 422 GLU A CB  
3326 C CG  . GLU A 430 ? 1.66650 0.81397 0.69409 -0.13031 0.10995  -0.12228 422 GLU A CG  
3327 C CD  . GLU A 430 ? 1.84875 0.98541 0.88992 -0.11157 0.12028  -0.14362 422 GLU A CD  
3328 O OE1 . GLU A 430 ? 1.93484 1.03542 0.96572 -0.11083 0.12328  -0.15998 422 GLU A OE1 
3329 O OE2 . GLU A 430 ? 1.91864 1.08356 0.98240 -0.09790 0.12554  -0.14478 422 GLU A OE2 
3330 N N   . TRP A 431 ? 1.57923 0.61989 0.54235 -0.17455 0.08590  -0.10632 423 TRP A N   
3331 C CA  . TRP A 431 ? 1.63888 0.64715 0.57462 -0.19693 0.08262  -0.10897 423 TRP A CA  
3332 C C   . TRP A 431 ? 1.65053 0.60314 0.57921 -0.18721 0.07908  -0.11590 423 TRP A C   
3333 O O   . TRP A 431 ? 1.74543 0.68412 0.68098 -0.17670 0.07140  -0.10267 423 TRP A O   
3334 C CB  . TRP A 431 ? 1.61558 0.64128 0.54519 -0.21722 0.07512  -0.08933 423 TRP A CB  
3335 C CG  . TRP A 431 ? 1.63097 0.62926 0.53447 -0.24255 0.07200  -0.09173 423 TRP A CG  
3336 C CD1 . TRP A 431 ? 1.66206 0.64939 0.54671 -0.25760 0.07573  -0.10729 423 TRP A CD1 
3337 C CD2 . TRP A 431 ? 1.66050 0.63921 0.55269 -0.25770 0.06486  -0.07850 423 TRP A CD2 
3338 N NE1 . TRP A 431 ? 1.72439 0.68646 0.58843 -0.28032 0.07064  -0.10483 423 TRP A NE1 
3339 C CE2 . TRP A 431 ? 1.68783 0.64428 0.55628 -0.28130 0.06434  -0.08712 423 TRP A CE2 
3340 C CE3 . TRP A 431 ? 1.75372 0.73133 0.65181 -0.25514 0.05945  -0.06077 423 TRP A CE3 
3341 C CZ2 . TRP A 431 ? 1.76251 0.69625 0.61503 -0.30226 0.05880  -0.07833 423 TRP A CZ2 
3342 C CZ3 . TRP A 431 ? 1.78894 0.74413 0.66934 -0.27645 0.05480  -0.05201 423 TRP A CZ3 
3343 C CH2 . TRP A 431 ? 1.80197 0.73575 0.66079 -0.29979 0.05455  -0.06056 423 TRP A CH2 
3344 N N   . VAL A 432 ? 1.73456 0.65561 0.64907 -0.19108 0.08394  -0.13612 424 VAL A N   
3345 C CA  . VAL A 432 ? 1.80277 0.66446 0.70684 -0.18610 0.07932  -0.14449 424 VAL A CA  
3346 C C   . VAL A 432 ? 1.77566 0.61396 0.65193 -0.21438 0.07301  -0.13602 424 VAL A C   
3347 O O   . VAL A 432 ? 1.79021 0.63239 0.64930 -0.23482 0.07751  -0.14612 424 VAL A O   
3348 C CB  . VAL A 432 ? 1.77667 0.61703 0.68203 -0.17590 0.08877  -0.17307 424 VAL A CB  
3349 C CG1 . VAL A 432 ? 1.82910 0.60849 0.73086 -0.16515 0.08234  -0.18163 424 VAL A CG1 
3350 C CG2 . VAL A 432 ? 1.74294 0.61739 0.67581 -0.15352 0.09810  -0.18305 424 VAL A CG2 
3351 N N   . ALA A 433 ? 1.87977 0.69604 0.75100 -0.21679 0.06299  -0.11790 425 ALA A N   
3352 C CA  . ALA A 433 ? 1.91173 0.71495 0.76003 -0.24538 0.05733  -0.10527 425 ALA A CA  
3353 C C   . ALA A 433 ? 2.02668 0.77052 0.85152 -0.25569 0.05482  -0.11769 425 ALA A C   
3354 O O   . ALA A 433 ? 2.08667 0.79067 0.91473 -0.23674 0.05344  -0.12972 425 ALA A O   
3355 C CB  . ALA A 433 ? 1.88698 0.69156 0.73829 -0.24420 0.04948  -0.08170 425 ALA A CB  
3356 N N   . PRO A 434 ? 1.94621 0.68240 0.74867 -0.28592 0.05360  -0.11590 426 PRO A N   
3357 C CA  . PRO A 434 ? 1.95681 0.63396 0.73531 -0.29853 0.05029  -0.12603 426 PRO A CA  
3358 C C   . PRO A 434 ? 2.00010 0.62746 0.76943 -0.29526 0.03978  -0.11123 426 PRO A C   
3359 O O   . PRO A 434 ? 2.11935 0.70693 0.88976 -0.28401 0.03586  -0.11867 426 PRO A O   
3360 C CB  . PRO A 434 ? 1.99320 0.68711 0.75373 -0.33328 0.05116  -0.12458 426 PRO A CB  
3361 C CG  . PRO A 434 ? 1.98098 0.73297 0.75614 -0.33933 0.05070  -0.10475 426 PRO A CG  
3362 C CD  . PRO A 434 ? 1.88464 0.66879 0.68595 -0.30943 0.05458  -0.10487 426 PRO A CD  
3363 N N   . GLU A 435 ? 2.00316 0.65097 0.77411 -0.30186 0.03555  -0.08777 427 GLU A N   
3364 C CA  . GLU A 435 ? 1.99946 0.60518 0.75661 -0.30406 0.02551  -0.06936 427 GLU A CA  
3365 C C   . GLU A 435 ? 2.02894 0.67058 0.80325 -0.28973 0.02379  -0.05091 427 GLU A C   
3366 O O   . GLU A 435 ? 1.89696 0.59905 0.69038 -0.28820 0.03068  -0.04973 427 GLU A O   
3367 C CB  . GLU A 435 ? 2.03088 0.62075 0.76201 -0.34044 0.02375  -0.06007 427 GLU A CB  
3368 C CG  . GLU A 435 ? 1.98685 0.63895 0.72489 -0.36260 0.03062  -0.05574 427 GLU A CG  
3369 C CD  . GLU A 435 ? 2.01573 0.65812 0.73262 -0.39947 0.02957  -0.04809 427 GLU A CD  
3370 O OE1 . GLU A 435 ? 2.21356 0.80461 0.91046 -0.40810 0.02413  -0.04545 427 GLU A OE1 
3371 O OE2 . GLU A 435 ? 1.98096 0.67510 0.70688 -0.41741 0.03379  -0.04426 427 GLU A OE2 
3372 N N   . LYS A 436 ? 2.01033 0.61433 0.77679 -0.28010 0.01402  -0.03702 428 LYS A N   
3373 C CA  . LYS A 436 ? 1.94347 0.57450 0.72110 -0.26835 0.01103  -0.01861 428 LYS A CA  
3374 C C   . LYS A 436 ? 1.93000 0.58914 0.69595 -0.29801 0.01440  -0.00153 428 LYS A C   
3375 O O   . LYS A 436 ? 1.96310 0.60309 0.70814 -0.32609 0.01545  -0.00154 428 LYS A O   
3376 C CB  . LYS A 436 ? 1.99549 0.57230 0.76545 -0.24901 -0.00234 -0.01048 428 LYS A CB  
3377 C CG  . LYS A 436 ? 1.99589 0.54807 0.78373 -0.21792 -0.00584 -0.02923 428 LYS A CG  
3378 C CD  . LYS A 436 ? 2.01391 0.53577 0.80820 -0.19150 -0.02005 -0.02029 428 LYS A CD  
3379 C CE  . LYS A 436 ? 2.00565 0.52772 0.83132 -0.15746 -0.02060 -0.04044 428 LYS A CE  
3380 N NZ  . LYS A 436 ? 2.09250 0.58435 0.93010 -0.13254 -0.03789 -0.03393 428 LYS A NZ  
3381 N N   . ALA A 437 ? 1.88347 0.58791 0.66437 -0.29219 0.01662  0.01085  429 ALA A N   
3382 C CA  . ALA A 437 ? 1.87209 0.61767 0.65144 -0.31697 0.02238  0.02385  429 ALA A CA  
3383 C C   . ALA A 437 ? 1.95708 0.67401 0.71380 -0.32660 0.01669  0.04374  429 ALA A C   
3384 O O   . ALA A 437 ? 1.99034 0.68107 0.74474 -0.30488 0.00827  0.05013  429 ALA A O   
3385 C CB  . ALA A 437 ? 1.78957 0.60360 0.60086 -0.30432 0.02902  0.02289  429 ALA A CB  
3386 N N   . ASP A 438 ? 1.92943 0.65349 0.67048 -0.35886 0.02120  0.05286  430 ASP A N   
3387 C CA  . ASP A 438 ? 1.93894 0.65715 0.66450 -0.37140 0.01847  0.06937  430 ASP A CA  
3388 C C   . ASP A 438 ? 1.87149 0.64766 0.61903 -0.36387 0.02437  0.07641  430 ASP A C   
3389 O O   . ASP A 438 ? 1.88401 0.65751 0.63127 -0.35134 0.01821  0.08507  430 ASP A O   
3390 C CB  . ASP A 438 ? 1.96835 0.68954 0.68115 -0.40613 0.02212  0.07027  430 ASP A CB  
3391 C CG  . ASP A 438 ? 2.04555 0.70753 0.73404 -0.41277 0.01347  0.06731  430 ASP A CG  
3392 O OD1 . ASP A 438 ? 2.05156 0.67732 0.72701 -0.40131 0.00263  0.07502  430 ASP A OD1 
3393 O OD2 . ASP A 438 ? 2.03927 0.69326 0.72304 -0.42914 0.01680  0.05726  430 ASP A OD2 
3394 N N   . ILE A 439 ? 1.88328 0.71285 0.65169 -0.37086 0.03475  0.07151  431 ILE A N   
3395 C CA  . ILE A 439 ? 1.76021 0.65264 0.55658 -0.36167 0.04105  0.07475  431 ILE A CA  
3396 C C   . ILE A 439 ? 1.70729 0.64264 0.53796 -0.34171 0.04326  0.06085  431 ILE A C   
3397 O O   . ILE A 439 ? 1.72421 0.67230 0.56072 -0.35400 0.04602  0.05081  431 ILE A O   
3398 C CB  . ILE A 439 ? 1.76504 0.70635 0.57549 -0.38811 0.04910  0.07636  431 ILE A CB  
3399 C CG1 . ILE A 439 ? 1.83636 0.74914 0.62549 -0.40853 0.04636  0.08244  431 ILE A CG1 
3400 C CG2 . ILE A 439 ? 1.68591 0.68846 0.52948 -0.37603 0.05426  0.07795  431 ILE A CG2 
3401 C CD1 . ILE A 439 ? 1.78973 0.74300 0.58891 -0.43927 0.05580  0.08173  431 ILE A CD1 
3402 N N   . ILE A 440 ? 1.74936 0.70537 0.60018 -0.31353 0.04172  0.06066  432 ILE A N   
3403 C CA  . ILE A 440 ? 1.65923 0.66697 0.54462 -0.29692 0.04544  0.05068  432 ILE A CA  
3404 C C   . ILE A 440 ? 1.56858 0.63356 0.47554 -0.30214 0.05158  0.05704  432 ILE A C   
3405 O O   . ILE A 440 ? 1.58545 0.65154 0.49062 -0.29437 0.05101  0.06626  432 ILE A O   
3406 C CB  . ILE A 440 ? 1.64780 0.64388 0.54454 -0.26368 0.04076  0.04461  432 ILE A CB  
3407 C CG1 . ILE A 440 ? 1.60908 0.58640 0.49995 -0.24754 0.03491  0.05537  432 ILE A CG1 
3408 C CG2 . ILE A 440 ? 1.63783 0.58979 0.52206 -0.25935 0.03729  0.03267  432 ILE A CG2 
3409 C CD1 . ILE A 440 ? 1.58696 0.56679 0.49768 -0.21464 0.03097  0.04897  432 ILE A CD1 
3410 N N   . VAL A 441 ? 1.54035 0.64961 0.46638 -0.31575 0.05646  0.05190  433 VAL A N   
3411 C CA  . VAL A 441 ? 1.52313 0.69074 0.47547 -0.32154 0.06220  0.05535  433 VAL A CA  
3412 C C   . VAL A 441 ? 1.47614 0.68637 0.46114 -0.30134 0.06155  0.04845  433 VAL A C   
3413 O O   . VAL A 441 ? 1.47073 0.68387 0.45950 -0.30241 0.05952  0.03988  433 VAL A O   
3414 C CB  . VAL A 441 ? 1.50800 0.69423 0.46020 -0.35347 0.06667  0.05505  433 VAL A CB  
3415 C CG1 . VAL A 441 ? 1.46630 0.71298 0.44953 -0.35873 0.07262  0.05656  433 VAL A CG1 
3416 C CG2 . VAL A 441 ? 1.56411 0.70400 0.48084 -0.37564 0.06768  0.06199  433 VAL A CG2 
3417 N N   . SER A 442 ? 1.45243 0.69265 0.45800 -0.28469 0.06304  0.05209  434 SER A N   
3418 C CA  . SER A 442 ? 1.36266 0.63930 0.39806 -0.26357 0.06198  0.04717  434 SER A CA  
3419 C C   . SER A 442 ? 1.32951 0.65843 0.39422 -0.26311 0.06561  0.05044  434 SER A C   
3420 O O   . SER A 442 ? 1.40304 0.73673 0.46299 -0.27588 0.07003  0.05597  434 SER A O   
3421 C CB  . SER A 442 ? 1.36294 0.61455 0.39457 -0.23722 0.05876  0.04595  434 SER A CB  
3422 O OG  . SER A 442 ? 1.50170 0.73717 0.52340 -0.23086 0.05816  0.05420  434 SER A OG  
3423 N N   . GLU A 443 ? 1.33788 0.70272 0.43093 -0.24890 0.06400  0.04663  435 GLU A N   
3424 C CA  . GLU A 443 ? 1.23984 0.65856 0.36721 -0.24862 0.06564  0.04710  435 GLU A CA  
3425 C C   . GLU A 443 ? 1.24460 0.68216 0.39363 -0.22333 0.06309  0.04563  435 GLU A C   
3426 O O   . GLU A 443 ? 1.20434 0.68254 0.38244 -0.22111 0.06119  0.04420  435 GLU A O   
3427 C CB  . GLU A 443 ? 1.33165 0.77506 0.47097 -0.26715 0.06327  0.04329  435 GLU A CB  
3428 C CG  . GLU A 443 ? 1.28226 0.77586 0.45412 -0.27577 0.06519  0.04339  435 GLU A CG  
3429 C CD  . GLU A 443 ? 1.30446 0.82042 0.48836 -0.29507 0.06077  0.03961  435 GLU A CD  
3430 O OE1 . GLU A 443 ? 1.28554 0.77657 0.44902 -0.30302 0.05648  0.03714  435 GLU A OE1 
3431 O OE2 . GLU A 443 ? 1.31209 0.87064 0.52671 -0.30221 0.06130  0.03826  435 GLU A OE2 
3432 N N   . LEU A 444 ? 1.23751 0.64630 0.37413 -0.20517 0.06233  0.04595  436 LEU A N   
3433 C CA  . LEU A 444 ? 1.18460 0.60210 0.33645 -0.18245 0.06013  0.04274  436 LEU A CA  
3434 C C   . LEU A 444 ? 1.15558 0.59560 0.32730 -0.16695 0.06132  0.04605  436 LEU A C   
3435 O O   . LEU A 444 ? 1.20906 0.65041 0.39065 -0.14737 0.05989  0.04397  436 LEU A O   
3436 C CB  . LEU A 444 ? 1.21160 0.58552 0.34158 -0.17184 0.05885  0.03885  436 LEU A CB  
3437 C CG  . LEU A 444 ? 1.27943 0.62117 0.38423 -0.18725 0.05825  0.03468  436 LEU A CG  
3438 C CD1 . LEU A 444 ? 1.30871 0.60718 0.39608 -0.17381 0.05716  0.02942  436 LEU A CD1 
3439 C CD2 . LEU A 444 ? 1.29468 0.65872 0.40732 -0.19746 0.05724  0.02972  436 LEU A CD2 
3440 N N   . LEU A 445 ? 1.19272 0.65008 0.37000 -0.17611 0.06456  0.04992  437 LEU A N   
3441 C CA  . LEU A 445 ? 1.15771 0.63524 0.35109 -0.16343 0.06643  0.05199  437 LEU A CA  
3442 C C   . LEU A 445 ? 1.08635 0.60949 0.31677 -0.15626 0.06552  0.04916  437 LEU A C   
3443 O O   . LEU A 445 ? 1.12474 0.66885 0.36787 -0.16798 0.06412  0.04741  437 LEU A O   
3444 C CB  . LEU A 445 ? 1.20054 0.67897 0.38314 -0.17869 0.07180  0.05573  437 LEU A CB  
3445 C CG  . LEU A 445 ? 1.22951 0.66329 0.37916 -0.18684 0.07092  0.05988  437 LEU A CG  
3446 C CD1 . LEU A 445 ? 1.19834 0.63843 0.34511 -0.19556 0.07541  0.06332  437 LEU A CD1 
3447 C CD2 . LEU A 445 ? 1.21741 0.61461 0.35313 -0.16734 0.06449  0.06046  437 LEU A CD2 
3448 N N   . GLY A 446 ? 1.08162 0.61757 0.32834 -0.13779 0.06503  0.04890  438 GLY A N   
3449 C CA  . GLY A 446 ? 1.08560 0.66271 0.36818 -0.12962 0.06386  0.04686  438 GLY A CA  
3450 C C   . GLY A 446 ? 1.09457 0.69330 0.39083 -0.12806 0.06840  0.04645  438 GLY A C   
3451 O O   . GLY A 446 ? 1.04031 0.62399 0.31564 -0.13776 0.07305  0.04833  438 GLY A O   
3452 N N   . SER A 447 ? 1.03298 0.66431 0.36166 -0.11709 0.06713  0.04388  439 SER A N   
3453 C CA  . SER A 447 ? 1.01798 0.67493 0.36523 -0.11422 0.07186  0.04091  439 SER A CA  
3454 C C   . SER A 447 ? 1.00045 0.63463 0.32689 -0.10475 0.07377  0.04257  439 SER A C   
3455 O O   . SER A 447 ? 0.98110 0.62443 0.30571 -0.10968 0.07958  0.04089  439 SER A O   
3456 C CB  . SER A 447 ? 0.98552 0.67661 0.37170 -0.10270 0.06815  0.03760  439 SER A CB  
3457 O OG  . SER A 447 ? 1.03630 0.74908 0.44212 -0.11244 0.06445  0.03668  439 SER A OG  
3458 N N   . PHE A 448 ? 1.00760 0.61366 0.31899 -0.09229 0.06890  0.04509  440 PHE A N   
3459 C CA  . PHE A 448 ? 1.02556 0.60820 0.31932 -0.08069 0.06733  0.04690  440 PHE A CA  
3460 C C   . PHE A 448 ? 1.05805 0.59692 0.31500 -0.08633 0.06507  0.05145  440 PHE A C   
3461 O O   . PHE A 448 ? 1.06160 0.57553 0.30737 -0.07264 0.05993  0.05258  440 PHE A O   
3462 C CB  . PHE A 448 ? 0.99629 0.58535 0.30959 -0.05985 0.06276  0.04452  440 PHE A CB  
3463 C CG  . PHE A 448 ? 1.02659 0.60850 0.33607 -0.04669 0.06067  0.04434  440 PHE A CG  
3464 C CD1 . PHE A 448 ? 1.00833 0.60751 0.32213 -0.04941 0.06422  0.04281  440 PHE A CD1 
3465 C CD2 . PHE A 448 ? 1.03212 0.59156 0.33504 -0.03177 0.05507  0.04452  440 PHE A CD2 
3466 C CE1 . PHE A 448 ? 1.04379 0.63596 0.35194 -0.03821 0.06114  0.04254  440 PHE A CE1 
3467 C CE2 . PHE A 448 ? 1.04905 0.60302 0.34995 -0.01967 0.05124  0.04429  440 PHE A CE2 
3468 C CZ  . PHE A 448 ? 1.03112 0.60061 0.33303 -0.02322 0.05375  0.04381  440 PHE A CZ  
3469 N N   . ALA A 449 ? 1.11263 0.64262 0.35317 -0.10592 0.06824  0.05347  441 ALA A N   
3470 C CA  . ALA A 449 ? 1.16145 0.64838 0.36663 -0.11502 0.06617  0.05778  441 ALA A CA  
3471 C C   . ALA A 449 ? 1.12134 0.58898 0.32535 -0.10560 0.06136  0.05541  441 ALA A C   
3472 O O   . ALA A 449 ? 1.18860 0.65474 0.38979 -0.11754 0.06239  0.05394  441 ALA A O   
3473 C CB  . ALA A 449 ? 1.15837 0.62040 0.34574 -0.11059 0.06260  0.06195  441 ALA A CB  
3474 N N   . ASP A 450 ? 1.12885 0.58464 0.33637 -0.08552 0.05671  0.05389  442 ASP A N   
3475 C CA  . ASP A 450 ? 1.15995 0.58946 0.36116 -0.07576 0.05310  0.05027  442 ASP A CA  
3476 C C   . ASP A 450 ? 1.13749 0.59284 0.36546 -0.06597 0.05439  0.04429  442 ASP A C   
3477 O O   . ASP A 450 ? 1.14264 0.58075 0.36810 -0.05729 0.05331  0.03930  442 ASP A O   
3478 C CB  . ASP A 450 ? 1.15665 0.55565 0.34588 -0.06020 0.04673  0.05145  442 ASP A CB  
3479 C CG  . ASP A 450 ? 1.15666 0.57716 0.36597 -0.04391 0.04467  0.05089  442 ASP A CG  
3480 O OD1 . ASP A 450 ? 1.22303 0.65436 0.42901 -0.04889 0.04537  0.05520  442 ASP A OD1 
3481 O OD2 . ASP A 450 ? 1.08221 0.50957 0.31041 -0.02754 0.04318  0.04528  442 ASP A OD2 
3482 N N   . ASN A 451 ? 1.09007 0.58386 0.34227 -0.06794 0.05662  0.04431  443 ASN A N   
3483 C CA  . ASN A 451 ? 1.07662 0.59461 0.35378 -0.05844 0.05656  0.04058  443 ASN A CA  
3484 C C   . ASN A 451 ? 1.05140 0.56656 0.32293 -0.06867 0.05714  0.03828  443 ASN A C   
3485 O O   . ASN A 451 ? 1.11563 0.63985 0.39844 -0.06169 0.05720  0.03505  443 ASN A O   
3486 C CB  . ASN A 451 ? 1.00504 0.56134 0.31006 -0.05643 0.05691  0.04174  443 ASN A CB  
3487 C CG  . ASN A 451 ? 1.05578 0.63185 0.36580 -0.07338 0.05842  0.04377  443 ASN A CG  
3488 O OD1 . ASN A 451 ? 1.06761 0.63292 0.36081 -0.08495 0.06082  0.04573  443 ASN A OD1 
3489 N ND2 . ASN A 451 ? 1.04935 0.65468 0.38351 -0.07517 0.05659  0.04329  443 ASN A ND2 
3490 N N   . GLU A 452 ? 1.11042 0.61299 0.36365 -0.08580 0.05762  0.03969  444 GLU A N   
3491 C CA  . GLU A 452 ? 1.10012 0.59452 0.34220 -0.09735 0.05746  0.03679  444 GLU A CA  
3492 C C   . GLU A 452 ? 1.13845 0.59148 0.35473 -0.09565 0.05843  0.03239  444 GLU A C   
3493 O O   . GLU A 452 ? 1.18969 0.62982 0.39115 -0.10738 0.05890  0.02904  444 GLU A O   
3494 C CB  . GLU A 452 ? 1.06005 0.56803 0.30104 -0.11773 0.05664  0.03978  444 GLU A CB  
3495 C CG  . GLU A 452 ? 1.06944 0.61920 0.34034 -0.11867 0.05419  0.04197  444 GLU A CG  
3496 C CD  . GLU A 452 ? 1.10328 0.67127 0.37962 -0.13783 0.05237  0.04344  444 GLU A CD  
3497 O OE1 . GLU A 452 ? 1.09468 0.64279 0.34928 -0.15281 0.05316  0.04276  444 GLU A OE1 
3498 O OE2 . GLU A 452 ? 1.14781 0.75017 0.45213 -0.13758 0.04979  0.04460  444 GLU A OE2 
3499 N N   . LEU A 453 ? 1.14390 0.57679 0.35598 -0.08134 0.05776  0.03186  445 LEU A N   
3500 C CA  . LEU A 453 ? 1.18125 0.57594 0.37677 -0.07321 0.05724  0.02605  445 LEU A CA  
3501 C C   . LEU A 453 ? 1.22582 0.58676 0.39288 -0.08865 0.05617  0.02735  445 LEU A C   
3502 O O   . LEU A 453 ? 1.24495 0.57977 0.39882 -0.08934 0.05701  0.02007  445 LEU A O   
3503 C CB  . LEU A 453 ? 1.17301 0.57237 0.37612 -0.06704 0.06080  0.01678  445 LEU A CB  
3504 C CG  . LEU A 453 ? 1.20187 0.61629 0.42755 -0.04716 0.06189  0.01294  445 LEU A CG  
3505 C CD1 . LEU A 453 ? 1.12063 0.56474 0.36614 -0.04212 0.05958  0.02037  445 LEU A CD1 
3506 C CD2 . LEU A 453 ? 1.14209 0.56982 0.37475 -0.04745 0.06718  0.00539  445 LEU A CD2 
3507 N N   . SER A 454 ? 1.24377 0.60375 0.40129 -0.10070 0.05495  0.03549  446 SER A N   
3508 C CA  . SER A 454 ? 1.26117 0.58591 0.38968 -0.11631 0.05359  0.03864  446 SER A CA  
3509 C C   . SER A 454 ? 1.30170 0.58151 0.41374 -0.10365 0.04867  0.03708  446 SER A C   
3510 O O   . SER A 454 ? 1.36692 0.61235 0.45925 -0.11043 0.04753  0.03362  446 SER A O   
3511 C CB  . SER A 454 ? 1.28649 0.62209 0.40960 -0.13096 0.05463  0.04743  446 SER A CB  
3512 O OG  . SER A 454 ? 1.28334 0.58634 0.37803 -0.14933 0.05417  0.05056  446 SER A OG  
3513 N N   . PRO A 455 ? 1.29123 0.56883 0.41165 -0.08482 0.04446  0.03909  447 PRO A N   
3514 C CA  . PRO A 455 ? 1.34896 0.58445 0.45744 -0.07090 0.03719  0.03763  447 PRO A CA  
3515 C C   . PRO A 455 ? 1.38744 0.60312 0.49816 -0.06259 0.03833  0.02497  447 PRO A C   
3516 O O   . PRO A 455 ? 1.39068 0.56444 0.48123 -0.06535 0.03418  0.02353  447 PRO A O   
3517 C CB  . PRO A 455 ? 1.30949 0.56123 0.43704 -0.05059 0.03312  0.03924  447 PRO A CB  
3518 C CG  . PRO A 455 ? 1.27583 0.56642 0.41214 -0.06028 0.03744  0.04599  447 PRO A CG  
3519 C CD  . PRO A 455 ? 1.25083 0.56514 0.39322 -0.07593 0.04518  0.04256  447 PRO A CD  
3520 N N   . GLU A 456 ? 1.34197 0.58693 0.47606 -0.05357 0.04420  0.01581  448 GLU A N   
3521 C CA  . GLU A 456 ? 1.34618 0.57890 0.48535 -0.04506 0.04794  0.00124  448 GLU A CA  
3522 C C   . GLU A 456 ? 1.34440 0.55741 0.46154 -0.06430 0.05133  -0.00297 448 GLU A C   
3523 O O   . GLU A 456 ? 1.33094 0.50958 0.43881 -0.05991 0.05077  -0.01280 448 GLU A O   
3524 C CB  . GLU A 456 ? 1.25502 0.52735 0.42022 -0.03676 0.05500  -0.00580 448 GLU A CB  
3525 C CG  . GLU A 456 ? 1.27167 0.55614 0.46086 -0.01433 0.05222  -0.00732 448 GLU A CG  
3526 C CD  . GLU A 456 ? 1.26543 0.57394 0.46362 -0.01264 0.04810  0.00477  448 GLU A CD  
3527 O OE1 . GLU A 456 ? 1.28288 0.60527 0.47273 -0.02895 0.04913  0.01354  448 GLU A OE1 
3528 O OE2 . GLU A 456 ? 1.20874 0.52308 0.42363 0.00487  0.04396  0.00424  448 GLU A OE2 
3529 N N   . CYS A 457 ? 1.28973 0.52417 0.40074 -0.08448 0.05418  0.00326  449 CYS A N   
3530 C CA  . CYS A 457 ? 1.31243 0.53487 0.40391 -0.10564 0.05682  -0.00016 449 CYS A CA  
3531 C C   . CYS A 457 ? 1.38045 0.55512 0.44567 -0.11355 0.05176  0.00253  449 CYS A C   
3532 O O   . CYS A 457 ? 1.46643 0.61084 0.51815 -0.11663 0.05276  -0.00753 449 CYS A O   
3533 C CB  . CYS A 457 ? 1.31654 0.57500 0.41180 -0.12413 0.05845  0.00736  449 CYS A CB  
3534 S SG  . CYS A 457 ? 1.34484 0.65198 0.46548 -0.11921 0.06272  0.00372  449 CYS A SG  
3535 N N   . LEU A 458 ? 1.43007 0.59705 0.48713 -0.11736 0.04673  0.01527  450 LEU A N   
3536 C CA  . LEU A 458 ? 1.43122 0.55188 0.45957 -0.12849 0.04114  0.02128  450 LEU A CA  
3537 C C   . LEU A 458 ? 1.52164 0.59780 0.54506 -0.10910 0.03411  0.01596  450 LEU A C   
3538 O O   . LEU A 458 ? 1.55011 0.58182 0.55125 -0.11693 0.03044  0.01411  450 LEU A O   
3539 C CB  . LEU A 458 ? 1.41582 0.54532 0.43690 -0.13829 0.03892  0.03636  450 LEU A CB  
3540 C CG  . LEU A 458 ? 1.38043 0.55175 0.40825 -0.15868 0.04548  0.04051  450 LEU A CG  
3541 C CD1 . LEU A 458 ? 1.37697 0.55930 0.40033 -0.16619 0.04523  0.05276  450 LEU A CD1 
3542 C CD2 . LEU A 458 ? 1.40806 0.56615 0.41890 -0.18242 0.04785  0.03742  450 LEU A CD2 
3543 N N   . ASP A 459 ? 1.49192 0.57941 0.53704 -0.08481 0.03168  0.01301  451 ASP A N   
3544 C CA  . ASP A 459 ? 1.50909 0.56122 0.55874 -0.06253 0.02445  0.00525  451 ASP A CA  
3545 C C   . ASP A 459 ? 1.52123 0.55368 0.56929 -0.06273 0.02958  -0.01186 451 ASP A C   
3546 O O   . ASP A 459 ? 1.59568 0.58030 0.63126 -0.05801 0.02269  -0.01601 451 ASP A O   
3547 C CB  . ASP A 459 ? 1.48507 0.56471 0.56506 -0.03798 0.02338  0.00186  451 ASP A CB  
3548 C CG  . ASP A 459 ? 1.51885 0.59765 0.59739 -0.03062 0.01349  0.01606  451 ASP A CG  
3549 O OD1 . ASP A 459 ? 1.62817 0.69408 0.68215 -0.04741 0.01005  0.02970  451 ASP A OD1 
3550 O OD2 . ASP A 459 ? 1.50938 0.60095 0.61084 -0.00917 0.00965  0.01278  451 ASP A OD2 
3551 N N   . GLY A 460 ? 1.49288 0.55970 0.55207 -0.06845 0.04072  -0.02145 452 GLY A N   
3552 C CA  . GLY A 460 ? 1.53980 0.59447 0.59592 -0.07130 0.04792  -0.03920 452 GLY A CA  
3553 C C   . GLY A 460 ? 1.52944 0.55411 0.55600 -0.09489 0.04744  -0.03848 452 GLY A C   
3554 O O   . GLY A 460 ? 1.59356 0.59449 0.61297 -0.09626 0.05116  -0.05388 452 GLY A O   
3555 N N   . ALA A 461 ? 1.56172 0.58863 0.57248 -0.11361 0.04389  -0.02254 453 ALA A N   
3556 C CA  . ALA A 461 ? 1.58527 0.58745 0.56841 -0.13945 0.04321  -0.01961 453 ALA A CA  
3557 C C   . ALA A 461 ? 1.64879 0.59970 0.61036 -0.14121 0.03305  -0.00998 453 ALA A C   
3558 O O   . ALA A 461 ? 1.69104 0.61505 0.62799 -0.16303 0.03186  -0.00705 453 ALA A O   
3559 C CB  . ALA A 461 ? 1.51613 0.55916 0.49934 -0.16036 0.04688  -0.00942 453 ALA A CB  
3560 N N   . GLN A 462 ? 1.63962 0.57665 0.60914 -0.12007 0.02512  -0.00481 454 GLN A N   
3561 C CA  . GLN A 462 ? 1.71233 0.60317 0.65986 -0.12134 0.01298  0.00866  454 GLN A CA  
3562 C C   . GLN A 462 ? 1.76039 0.59118 0.69113 -0.12039 0.00682  -0.00008 454 GLN A C   
3563 O O   . GLN A 462 ? 1.84252 0.63175 0.74448 -0.13571 -0.00053 0.01093  454 GLN A O   
3564 C CB  . GLN A 462 ? 1.67831 0.57453 0.64098 -0.09754 0.00474  0.01560  454 GLN A CB  
3565 C CG  . GLN A 462 ? 1.73271 0.58812 0.66942 -0.10170 -0.00844 0.03308  454 GLN A CG  
3566 C CD  . GLN A 462 ? 1.75177 0.62513 0.70078 -0.08453 -0.01531 0.04248  454 GLN A CD  
3567 O OE1 . GLN A 462 ? 1.78581 0.70914 0.74991 -0.08590 -0.00787 0.04558  454 GLN A OE1 
3568 N NE2 . GLN A 462 ? 1.74506 0.57636 0.68771 -0.06822 -0.03084 0.04706  454 GLN A NE2 
3569 N N   . HIS A 463 ? 1.71438 0.54058 0.66226 -0.10405 0.01034  -0.01979 455 HIS A N   
3570 C CA  . HIS A 463 ? 1.74095 0.51086 0.68042 -0.09701 0.00455  -0.03238 455 HIS A CA  
3571 C C   . HIS A 463 ? 1.78072 0.51986 0.68913 -0.12550 0.00620  -0.03198 455 HIS A C   
3572 O O   . HIS A 463 ? 1.93235 0.61332 0.82444 -0.12466 -0.00309 -0.03386 455 HIS A O   
3573 C CB  . HIS A 463 ? 1.73529 0.51821 0.70242 -0.07659 0.01246  -0.05670 455 HIS A CB  
3574 C CG  . HIS A 463 ? 1.76835 0.58804 0.73740 -0.09134 0.02808  -0.06913 455 HIS A CG  
3575 N ND1 . HIS A 463 ? 1.76628 0.56164 0.71873 -0.10601 0.03325  -0.08303 455 HIS A ND1 
3576 C CD2 . HIS A 463 ? 1.66740 0.54409 0.65130 -0.09420 0.03833  -0.06940 455 HIS A CD2 
3577 C CE1 . HIS A 463 ? 1.74464 0.58127 0.70025 -0.11770 0.04566  -0.09095 455 HIS A CE1 
3578 N NE2 . HIS A 463 ? 1.69119 0.57730 0.66610 -0.11058 0.04856  -0.08222 455 HIS A NE2 
3579 N N   . PHE A 464 ? 1.77689 0.55198 0.67862 -0.14945 0.01636  -0.02999 456 PHE A N   
3580 C CA  . PHE A 464 ? 1.82125 0.57383 0.69555 -0.17906 0.01844  -0.03022 456 PHE A CA  
3581 C C   . PHE A 464 ? 1.82050 0.57150 0.67374 -0.20202 0.01455  -0.00818 456 PHE A C   
3582 O O   . PHE A 464 ? 1.81236 0.56102 0.64750 -0.22994 0.01820  -0.00657 456 PHE A O   
3583 C CB  . PHE A 464 ? 1.76467 0.55447 0.64495 -0.19152 0.03073  -0.04445 456 PHE A CB  
3584 C CG  . PHE A 464 ? 1.70570 0.56052 0.60123 -0.19833 0.03772  -0.03727 456 PHE A CG  
3585 C CD1 . PHE A 464 ? 1.69578 0.57049 0.58130 -0.22246 0.03787  -0.02249 456 PHE A CD1 
3586 C CD2 . PHE A 464 ? 1.70896 0.60500 0.62979 -0.18167 0.04447  -0.04659 456 PHE A CD2 
3587 C CE1 . PHE A 464 ? 1.66908 0.60283 0.57213 -0.22726 0.04324  -0.01733 456 PHE A CE1 
3588 C CE2 . PHE A 464 ? 1.68368 0.63603 0.61858 -0.18775 0.04938  -0.03980 456 PHE A CE2 
3589 C CZ  . PHE A 464 ? 1.68722 0.65806 0.61435 -0.20958 0.04815  -0.02542 456 PHE A CZ  
3590 N N   . LEU A 465 ? 1.80694 0.55861 0.66170 -0.19183 0.00757  0.00742  457 LEU A N   
3591 C CA  . LEU A 465 ? 1.86398 0.60138 0.69343 -0.21253 0.00293  0.02812  457 LEU A CA  
3592 C C   . LEU A 465 ? 1.89356 0.55712 0.69605 -0.21139 -0.01077 0.03417  457 LEU A C   
3593 O O   . LEU A 465 ? 1.89343 0.53039 0.70604 -0.18413 -0.02032 0.02957  457 LEU A O   
3594 C CB  . LEU A 465 ? 1.85594 0.63301 0.69899 -0.20275 0.00281  0.04080  457 LEU A CB  
3595 C CG  . LEU A 465 ? 1.87801 0.65191 0.69701 -0.22533 0.00151  0.06053  457 LEU A CG  
3596 C CD1 . LEU A 465 ? 1.84414 0.64258 0.65546 -0.25779 0.01213  0.06091  457 LEU A CD1 
3597 C CD2 . LEU A 465 ? 1.75761 0.57052 0.59159 -0.21292 0.00173  0.06987  457 LEU A CD2 
3598 N N   . LYS A 466 ? 1.92296 0.55455 0.69362 -0.24023 -0.01222 0.04385  458 LYS A N   
3599 C CA  . LYS A 466 ? 2.00179 0.56806 0.74654 -0.24280 -0.02615 0.05117  458 LYS A CA  
3600 C C   . LYS A 466 ? 2.06998 0.63267 0.81675 -0.22422 -0.03896 0.06565  458 LYS A C   
3601 O O   . LYS A 466 ? 2.06623 0.66795 0.81845 -0.22488 -0.03418 0.07520  458 LYS A O   
3602 C CB  . LYS A 466 ? 2.02041 0.58289 0.74138 -0.27795 -0.02320 0.05848  458 LYS A CB  
3603 C CG  . LYS A 466 ? 2.09031 0.60418 0.79763 -0.28316 -0.03106 0.05228  458 LYS A CG  
3604 C CD  . LYS A 466 ? 2.16667 0.68096 0.85294 -0.31966 -0.02549 0.05600  458 LYS A CD  
3605 C CE  . LYS A 466 ? 2.07091 0.62606 0.76327 -0.34024 -0.00972 0.04776  458 LYS A CE  
3606 N NZ  . LYS A 466 ? 2.11901 0.66554 0.79506 -0.37139 -0.00627 0.04498  458 LYS A NZ  
3607 N N   . ASP A 467 ? 2.11067 0.63065 0.85506 -0.20816 -0.05524 0.06665  459 ASP A N   
3608 C CA  . ASP A 467 ? 2.04976 0.56046 0.79732 -0.18785 -0.07128 0.07876  459 ASP A CA  
3609 C C   . ASP A 467 ? 2.04547 0.57929 0.77412 -0.20923 -0.07033 0.09723  459 ASP A C   
3610 O O   . ASP A 467 ? 2.07194 0.62303 0.80786 -0.19527 -0.07633 0.10549  459 ASP A O   
3611 C CB  . ASP A 467 ? 2.11045 0.56932 0.85593 -0.17385 -0.08989 0.07800  459 ASP A CB  
3612 C CG  . ASP A 467 ? 2.10784 0.55241 0.88350 -0.14386 -0.09285 0.05802  459 ASP A CG  
3613 O OD1 . ASP A 467 ? 2.06148 0.53476 0.86180 -0.12463 -0.08638 0.04855  459 ASP A OD1 
3614 O OD2 . ASP A 467 ? 2.15383 0.56059 0.93006 -0.14004 -0.10097 0.05096  459 ASP A OD2 
3615 N N   . ASP A 468 ? 2.06236 0.59937 0.77026 -0.24190 -0.06250 0.10147  460 ASP A N   
3616 C CA  . ASP A 468 ? 2.06007 0.62360 0.75313 -0.26625 -0.05844 0.11491  460 ASP A CA  
3617 C C   . ASP A 468 ? 2.00521 0.62539 0.71018 -0.28412 -0.03835 0.11056  460 ASP A C   
3618 O O   . ASP A 468 ? 2.00632 0.64998 0.70246 -0.31101 -0.03084 0.11612  460 ASP A O   
3619 C CB  . ASP A 468 ? 2.12265 0.65001 0.78699 -0.29001 -0.06489 0.12212  460 ASP A CB  
3620 C CG  . ASP A 468 ? 2.19020 0.70537 0.84691 -0.31067 -0.05623 0.11281  460 ASP A CG  
3621 O OD1 . ASP A 468 ? 2.11759 0.66912 0.77415 -0.33600 -0.04120 0.11110  460 ASP A OD1 
3622 O OD2 . ASP A 468 ? 2.22772 0.69924 0.88162 -0.30085 -0.06487 0.10627  460 ASP A OD2 
3623 N N   . GLY A 469 ? 1.98136 0.62424 0.70781 -0.26933 -0.03027 0.10063  461 GLY A N   
3624 C CA  . GLY A 469 ? 1.91644 0.61128 0.65672 -0.28433 -0.01279 0.09545  461 GLY A CA  
3625 C C   . GLY A 469 ? 1.90677 0.65780 0.66404 -0.28328 -0.00665 0.10190  461 GLY A C   
3626 O O   . GLY A 469 ? 1.87564 0.62584 0.63896 -0.26160 -0.01500 0.10709  461 GLY A O   
3627 N N   . VAL A 470 ? 1.83007 0.62982 0.59793 -0.30556 0.00684  0.10027  462 VAL A N   
3628 C CA  . VAL A 470 ? 1.77722 0.64011 0.57020 -0.30565 0.01529  0.10239  462 VAL A CA  
3629 C C   . VAL A 470 ? 1.79680 0.70070 0.61606 -0.29324 0.02382  0.09415  462 VAL A C   
3630 O O   . VAL A 470 ? 1.83387 0.72916 0.64919 -0.29988 0.02784  0.08710  462 VAL A O   
3631 C CB  . VAL A 470 ? 1.78038 0.67285 0.57349 -0.33725 0.02430  0.10439  462 VAL A CB  
3632 C CG1 . VAL A 470 ? 1.72199 0.68366 0.54776 -0.33834 0.03546  0.10252  462 VAL A CG1 
3633 C CG2 . VAL A 470 ? 1.83348 0.69163 0.60043 -0.34872 0.01645  0.11373  462 VAL A CG2 
3634 N N   . SER A 471 ? 1.67437 0.62040 0.51839 -0.27630 0.02594  0.09486  463 SER A N   
3635 C CA  . SER A 471 ? 1.61471 0.61459 0.48931 -0.26732 0.03475  0.08767  463 SER A CA  
3636 C C   . SER A 471 ? 1.57733 0.63752 0.47788 -0.28081 0.04367  0.08816  463 SER A C   
3637 O O   . SER A 471 ? 1.63333 0.69907 0.53425 -0.28073 0.04195  0.09424  463 SER A O   
3638 C CB  . SER A 471 ? 1.59159 0.59126 0.47647 -0.23593 0.03003  0.08666  463 SER A CB  
3639 O OG  . SER A 471 ? 1.53386 0.58909 0.45265 -0.22731 0.03751  0.07823  463 SER A OG  
3640 N N   . ILE A 472 ? 1.54686 0.64800 0.46652 -0.29304 0.05238  0.08186  464 ILE A N   
3641 C CA  . ILE A 472 ? 1.50555 0.66862 0.45581 -0.30270 0.06141  0.08042  464 ILE A CA  
3642 C C   . ILE A 472 ? 1.52500 0.72979 0.50566 -0.28461 0.06350  0.07418  464 ILE A C   
3643 O O   . ILE A 472 ? 1.52326 0.73426 0.50660 -0.28835 0.06449  0.06844  464 ILE A O   
3644 C CB  . ILE A 472 ? 1.52253 0.69615 0.46847 -0.33497 0.06819  0.07899  464 ILE A CB  
3645 C CG1 . ILE A 472 ? 1.57677 0.71083 0.49305 -0.35338 0.06627  0.08535  464 ILE A CG1 
3646 C CG2 . ILE A 472 ? 1.47979 0.71748 0.45859 -0.34357 0.07777  0.07585  464 ILE A CG2 
3647 C CD1 . ILE A 472 ? 1.60177 0.73786 0.50931 -0.38632 0.07234  0.08351  464 ILE A CD1 
3648 N N   . PRO A 473 ? 1.46678 0.69983 0.46961 -0.26486 0.06349  0.07493  465 PRO A N   
3649 C CA  . PRO A 473 ? 1.42394 0.65535 0.42413 -0.26213 0.06260  0.08106  465 PRO A CA  
3650 C C   . PRO A 473 ? 1.45848 0.63724 0.43301 -0.24643 0.05190  0.08651  465 PRO A C   
3651 O O   . PRO A 473 ? 1.46135 0.61570 0.42941 -0.22989 0.04656  0.08409  465 PRO A O   
3652 C CB  . PRO A 473 ? 1.40628 0.68898 0.44083 -0.24642 0.06641  0.07810  465 PRO A CB  
3653 C CG  . PRO A 473 ? 1.34516 0.63199 0.39118 -0.22845 0.06348  0.07263  465 PRO A CG  
3654 C CD  . PRO A 473 ? 1.36920 0.63545 0.39897 -0.24453 0.06375  0.06967  465 PRO A CD  
3655 N N   . GLY A 474 ? 1.48672 0.64899 0.44605 -0.25265 0.04893  0.09351  466 GLY A N   
3656 C CA  . GLY A 474 ? 1.52284 0.63680 0.45807 -0.23846 0.03648  0.10022  466 GLY A CA  
3657 C C   . GLY A 474 ? 1.49113 0.62450 0.44388 -0.21340 0.03269  0.10059  466 GLY A C   
3658 O O   . GLY A 474 ? 1.52777 0.62618 0.46896 -0.19316 0.02174  0.10284  466 GLY A O   
3659 N N   . GLU A 475 ? 1.44914 0.63574 0.42911 -0.21454 0.04130  0.09792  467 GLU A N   
3660 C CA  . GLU A 475 ? 1.42002 0.62873 0.41663 -0.19406 0.03862  0.09817  467 GLU A CA  
3661 C C   . GLU A 475 ? 1.36374 0.63262 0.39681 -0.19201 0.04953  0.09098  467 GLU A C   
3662 O O   . GLU A 475 ? 1.35510 0.65126 0.39739 -0.21164 0.05946  0.08814  467 GLU A O   
3663 C CB  . GLU A 475 ? 1.44810 0.64734 0.42846 -0.20167 0.03522  0.10538  467 GLU A CB  
3664 C CG  . GLU A 475 ? 1.46980 0.65324 0.44582 -0.17891 0.02332  0.10926  467 GLU A CG  
3665 C CD  . GLU A 475 ? 1.54565 0.73330 0.51068 -0.18724 0.02192  0.11498  467 GLU A CD  
3666 O OE1 . GLU A 475 ? 1.54541 0.77866 0.52974 -0.19329 0.03288  0.11104  467 GLU A OE1 
3667 O OE2 . GLU A 475 ? 1.64104 0.78532 0.57699 -0.18836 0.00974  0.12313  467 GLU A OE2 
3668 N N   . TYR A 476 ? 1.32977 0.61678 0.38203 -0.16919 0.04704  0.08809  468 TYR A N   
3669 C CA  . TYR A 476 ? 1.27958 0.62104 0.36524 -0.16425 0.05521  0.08235  468 TYR A CA  
3670 C C   . TYR A 476 ? 1.26331 0.61054 0.35691 -0.14249 0.04959  0.08283  468 TYR A C   
3671 O O   . TYR A 476 ? 1.27991 0.59333 0.36011 -0.12621 0.03922  0.08546  468 TYR A O   
3672 C CB  . TYR A 476 ? 1.26077 0.62462 0.36673 -0.16204 0.05953  0.07578  468 TYR A CB  
3673 C CG  . TYR A 476 ? 1.30174 0.63406 0.39751 -0.15015 0.05330  0.07423  468 TYR A CG  
3674 C CD1 . TYR A 476 ? 1.26014 0.59170 0.36493 -0.12644 0.04886  0.07161  468 TYR A CD1 
3675 C CD2 . TYR A 476 ? 1.30983 0.61418 0.38629 -0.16369 0.05309  0.07418  468 TYR A CD2 
3676 C CE1 . TYR A 476 ? 1.29700 0.60058 0.39064 -0.11631 0.04533  0.06859  468 TYR A CE1 
3677 C CE2 . TYR A 476 ? 1.32117 0.59589 0.38549 -0.15372 0.04904  0.07118  468 TYR A CE2 
3678 C CZ  . TYR A 476 ? 1.38198 0.65747 0.45616 -0.12969 0.04558  0.06784  468 TYR A CZ  
3679 O OH  . TYR A 476 ? 1.41839 0.67405 0.49477 -0.11888 0.04248  0.06076  468 TYR A OH  
3680 N N   . THR A 477 ? 1.23492 0.62272 0.34824 -0.14295 0.05629  0.07988  469 THR A N   
3681 C CA  . THR A 477 ? 1.21902 0.61811 0.34046 -0.12576 0.05240  0.07947  469 THR A CA  
3682 C C   . THR A 477 ? 1.17144 0.61871 0.32516 -0.11990 0.06060  0.07192  469 THR A C   
3683 O O   . THR A 477 ? 1.16123 0.63756 0.32527 -0.13564 0.07095  0.06854  469 THR A O   
3684 C CB  . THR A 477 ? 1.24805 0.63914 0.35061 -0.13597 0.05143  0.08441  469 THR A CB  
3685 O OG1 . THR A 477 ? 1.29571 0.63791 0.36690 -0.14082 0.04188  0.09222  469 THR A OG1 
3686 C CG2 . THR A 477 ? 1.23542 0.63749 0.34362 -0.12035 0.04693  0.08368  469 THR A CG2 
3687 N N   . SER A 478 ? 1.14669 0.60015 0.31439 -0.09839 0.05591  0.06916  470 SER A N   
3688 C CA  . SER A 478 ? 1.10484 0.59878 0.30099 -0.08985 0.06153  0.06249  470 SER A CA  
3689 C C   . SER A 478 ? 1.17250 0.68193 0.36976 -0.08727 0.06291  0.06110  470 SER A C   
3690 O O   . SER A 478 ? 1.12559 0.61061 0.30461 -0.08193 0.05480  0.06564  470 SER A O   
3691 C CB  . SER A 478 ? 1.10448 0.59546 0.31276 -0.06991 0.05637  0.06004  470 SER A CB  
3692 O OG  . SER A 478 ? 1.16419 0.62681 0.35907 -0.05424 0.04654  0.06279  470 SER A OG  
3693 N N   . PHE A 479 ? 1.10195 0.64891 0.31785 -0.09139 0.07244  0.05462  471 PHE A N   
3694 C CA  . PHE A 479 ? 1.09763 0.66433 0.31640 -0.08978 0.07632  0.05027  471 PHE A CA  
3695 C C   . PHE A 479 ? 1.06505 0.66194 0.31911 -0.07252 0.07640  0.04250  471 PHE A C   
3696 O O   . PHE A 479 ? 1.05942 0.67587 0.34218 -0.07033 0.07789  0.03932  471 PHE A O   
3697 C CB  . PHE A 479 ? 1.08248 0.67042 0.29863 -0.11198 0.08907  0.04660  471 PHE A CB  
3698 C CG  . PHE A 479 ? 1.14318 0.70697 0.33219 -0.12834 0.08813  0.05334  471 PHE A CG  
3699 C CD1 . PHE A 479 ? 1.15380 0.69657 0.33114 -0.14051 0.08699  0.05886  471 PHE A CD1 
3700 C CD2 . PHE A 479 ? 1.15099 0.71124 0.32399 -0.13244 0.08801  0.05415  471 PHE A CD2 
3701 C CE1 . PHE A 479 ? 1.20054 0.71777 0.35078 -0.15630 0.08578  0.06533  471 PHE A CE1 
3702 C CE2 . PHE A 479 ? 1.18691 0.72222 0.33215 -0.14853 0.08646  0.06128  471 PHE A CE2 
3703 C CZ  . PHE A 479 ? 1.20710 0.72024 0.34104 -0.16037 0.08534  0.06699  471 PHE A CZ  
3704 N N   . LEU A 480 ? 1.04231 0.64414 0.29919 -0.06089 0.07315  0.03958  472 LEU A N   
3705 C CA  . LEU A 480 ? 1.02006 0.65365 0.31655 -0.04504 0.07278  0.03110  472 LEU A CA  
3706 C C   . LEU A 480 ? 1.02688 0.68407 0.32696 -0.05040 0.08044  0.02314  472 LEU A C   
3707 O O   . LEU A 480 ? 1.09714 0.73770 0.36211 -0.06119 0.08211  0.02598  472 LEU A O   
3708 C CB  . LEU A 480 ? 1.01752 0.63418 0.31619 -0.02476 0.06102  0.03334  472 LEU A CB  
3709 C CG  . LEU A 480 ? 1.01320 0.61814 0.32212 -0.01598 0.05573  0.03643  472 LEU A CG  
3710 C CD1 . LEU A 480 ? 0.97182 0.55742 0.27881 0.00197  0.04507  0.03778  472 LEU A CD1 
3711 C CD2 . LEU A 480 ? 0.97253 0.60915 0.31985 -0.01281 0.05971  0.03117  472 LEU A CD2 
3712 N N   . ALA A 481 ? 0.96606 0.65919 0.30617 -0.04355 0.08462  0.01335  473 ALA A N   
3713 C CA  . ALA A 481 ? 0.96003 0.67970 0.31215 -0.04540 0.09222  0.00236  473 ALA A CA  
3714 C C   . ALA A 481 ? 0.94518 0.68860 0.33981 -0.02728 0.08844  -0.00510 473 ALA A C   
3715 O O   . ALA A 481 ? 0.91151 0.66909 0.33679 -0.02230 0.08699  -0.00549 473 ALA A O   
3716 C CB  . ALA A 481 ? 0.95032 0.69380 0.30914 -0.06396 0.10588  -0.00428 473 ALA A CB  
3717 N N   . PRO A 482 ? 0.93171 0.67851 0.32801 -0.01778 0.08584  -0.01072 474 PRO A N   
3718 C CA  . PRO A 482 ? 0.90355 0.67226 0.34020 -0.00213 0.08274  -0.01841 474 PRO A CA  
3719 C C   . PRO A 482 ? 0.86500 0.66945 0.33672 -0.00712 0.09256  -0.02995 474 PRO A C   
3720 O O   . PRO A 482 ? 0.94762 0.76221 0.40857 -0.02114 0.10310  -0.03608 474 PRO A O   
3721 C CB  . PRO A 482 ? 0.95743 0.71938 0.38074 0.00506  0.07851  -0.02235 474 PRO A CB  
3722 C CG  . PRO A 482 ? 0.95407 0.70169 0.33381 -0.01118 0.08381  -0.02064 474 PRO A CG  
3723 C CD  . PRO A 482 ? 0.93897 0.66757 0.29729 -0.02256 0.08478  -0.00971 474 PRO A CD  
3724 N N   . ILE A 483 ? 0.82478 0.64646 0.33696 0.00360  0.08867  -0.03246 475 ILE A N   
3725 C CA  . ILE A 483 ? 0.83947 0.69486 0.39228 0.00197  0.09472  -0.04330 475 ILE A CA  
3726 C C   . ILE A 483 ? 0.84419 0.71374 0.43328 0.01791  0.08944  -0.05060 475 ILE A C   
3727 O O   . ILE A 483 ? 0.77995 0.63374 0.36605 0.02930  0.08038  -0.04452 475 ILE A O   
3728 C CB  . ILE A 483 ? 0.81485 0.67580 0.38194 -0.00364 0.09310  -0.03721 475 ILE A CB  
3729 C CG1 . ILE A 483 ? 0.79183 0.63999 0.36841 0.00764  0.08117  -0.02703 475 ILE A CG1 
3730 C CG2 . ILE A 483 ? 0.82303 0.67025 0.35533 -0.02090 0.09896  -0.03116 475 ILE A CG2 
3731 C CD1 . ILE A 483 ? 0.76447 0.62977 0.37359 0.00710  0.07722  -0.02591 475 ILE A CD1 
3732 N N   . SER A 484 ? 0.78995 0.68858 0.41381 0.01815  0.09520  -0.06400 476 SER A N   
3733 C CA  . SER A 484 ? 0.83300 0.74741 0.49894 0.03225  0.09002  -0.07198 476 SER A CA  
3734 C C   . SER A 484 ? 0.79231 0.72799 0.49863 0.03252  0.08789  -0.07393 476 SER A C   
3735 O O   . SER A 484 ? 0.87852 0.83608 0.59782 0.02350  0.09713  -0.08386 476 SER A O   
3736 C CB  . SER A 484 ? 0.79852 0.72685 0.47105 0.03389  0.09750  -0.08841 476 SER A CB  
3737 O OG  . SER A 484 ? 0.76905 0.71079 0.48339 0.04720  0.09215  -0.09656 476 SER A OG  
3738 N N   . SER A 485 ? 0.72404 0.65314 0.44809 0.04144  0.07583  -0.06447 477 SER A N   
3739 C CA  . SER A 485 ? 0.77879 0.72519 0.54387 0.04453  0.06898  -0.06481 477 SER A CA  
3740 C C   . SER A 485 ? 0.74570 0.68169 0.52811 0.05721  0.05586  -0.05746 477 SER A C   
3741 O O   . SER A 485 ? 0.80408 0.72099 0.56853 0.05646  0.04882  -0.04303 477 SER A O   
3742 C CB  . SER A 485 ? 0.77923 0.72494 0.53485 0.03332  0.06804  -0.05584 477 SER A CB  
3743 O OG  . SER A 485 ? 0.75413 0.71554 0.54856 0.03655  0.05876  -0.05522 477 SER A OG  
3744 N N   . SER A 486 ? 0.70423 0.65163 0.51919 0.06746  0.05354  -0.06784 478 SER A N   
3745 C CA  . SER A 486 ? 0.72544 0.66588 0.56457 0.07843  0.04066  -0.06229 478 SER A CA  
3746 C C   . SER A 486 ? 0.72087 0.66384 0.57823 0.07659  0.02970  -0.05208 478 SER A C   
3747 O O   . SER A 486 ? 0.80009 0.72717 0.65599 0.07982  0.01886  -0.03951 478 SER A O   
3748 C CB  . SER A 486 ? 0.72570 0.67950 0.59918 0.08828  0.04087  -0.07756 478 SER A CB  
3749 O OG  . SER A 486 ? 0.71711 0.66478 0.57030 0.09001  0.04824  -0.08499 478 SER A OG  
3750 N N   . LYS A 487 ? 0.68757 0.65021 0.56029 0.07038  0.03254  -0.05755 479 LYS A N   
3751 C CA  . LYS A 487 ? 0.75455 0.72223 0.64290 0.06656  0.02168  -0.04858 479 LYS A CA  
3752 C C   . LYS A 487 ? 0.75449 0.69867 0.60256 0.05837  0.01831  -0.03095 479 LYS A C   
3753 O O   . LYS A 487 ? 0.76162 0.69440 0.61311 0.06006  0.00517  -0.01862 479 LYS A O   
3754 C CB  . LYS A 487 ? 0.79456 0.79013 0.70336 0.05960  0.02877  -0.06044 479 LYS A CB  
3755 C CG  . LYS A 487 ? 0.81240 0.81329 0.72643 0.05140  0.02017  -0.05136 479 LYS A CG  
3756 C CD  . LYS A 487 ? 0.86206 0.86281 0.80882 0.05930  0.00016  -0.04347 479 LYS A CD  
3757 C CE  . LYS A 487 ? 0.97452 0.98193 0.92611 0.05040  -0.00967 -0.03518 479 LYS A CE  
3758 N NZ  . LYS A 487 ? 0.90409 0.94499 0.88840 0.04617  -0.00348 -0.05041 479 LYS A NZ  
3759 N N   . LEU A 488 ? 0.74147 0.67750 0.55209 0.04926  0.02951  -0.03008 480 LEU A N   
3760 C CA  . LEU A 488 ? 0.76793 0.68130 0.53958 0.04116  0.02814  -0.01594 480 LEU A CA  
3761 C C   . LEU A 488 ? 0.76788 0.65818 0.52197 0.04803  0.02436  -0.00787 480 LEU A C   
3762 O O   . LEU A 488 ? 0.79162 0.66518 0.52579 0.04388  0.01934  0.00396  480 LEU A O   
3763 C CB  . LEU A 488 ? 0.82206 0.73130 0.56073 0.03054  0.04084  -0.01862 480 LEU A CB  
3764 C CG  . LEU A 488 ? 0.75923 0.68645 0.50552 0.01855  0.04478  -0.02258 480 LEU A CG  
3765 C CD1 . LEU A 488 ? 0.76230 0.68529 0.47689 0.00789  0.05881  -0.02701 480 LEU A CD1 
3766 C CD2 . LEU A 488 ? 0.71882 0.63869 0.45889 0.01141  0.03522  -0.01064 480 LEU A CD2 
3767 N N   . TYR A 489 ? 0.68589 0.57619 0.44678 0.05719  0.02740  -0.01510 481 TYR A N   
3768 C CA  . TYR A 489 ? 0.74076 0.61321 0.49161 0.06410  0.02407  -0.00964 481 TYR A CA  
3769 C C   . TYR A 489 ? 0.81933 0.68871 0.59067 0.06710  0.01166  -0.00114 481 TYR A C   
3770 O O   . TYR A 489 ? 0.78981 0.64177 0.54317 0.06561  0.00855  0.00890  481 TYR A O   
3771 C CB  . TYR A 489 ? 0.72814 0.60446 0.48601 0.07244  0.02893  -0.02075 481 TYR A CB  
3772 C CG  . TYR A 489 ? 0.73169 0.59375 0.48626 0.07941  0.02503  -0.01679 481 TYR A CG  
3773 C CD1 . TYR A 489 ? 0.77685 0.62150 0.50071 0.07821  0.02778  -0.01124 481 TYR A CD1 
3774 C CD2 . TYR A 489 ? 0.77743 0.64346 0.56149 0.08695  0.01841  -0.01919 481 TYR A CD2 
3775 C CE1 . TYR A 489 ? 0.75449 0.58928 0.47868 0.08396  0.02507  -0.00908 481 TYR A CE1 
3776 C CE2 . TYR A 489 ? 0.79456 0.64856 0.57644 0.09154  0.01557  -0.01589 481 TYR A CE2 
3777 C CZ  . TYR A 489 ? 0.80595 0.64590 0.55859 0.08982  0.01943  -0.01125 481 TYR A CZ  
3778 O OH  . TYR A 489 ? 0.84360 0.67491 0.59755 0.09378  0.01747  -0.00948 481 TYR A OH  
3779 N N   . ASN A 490 ? 0.72617 0.61153 0.53394 0.07079  0.00474  -0.00544 482 ASN A N   
3780 C CA  . ASN A 490 ? 0.74824 0.62996 0.57723 0.07288  -0.01003 0.00372  482 ASN A CA  
3781 C C   . ASN A 490 ? 0.75508 0.62694 0.56282 0.06245  -0.01603 0.01752  482 ASN A C   
3782 O O   . ASN A 490 ? 0.75879 0.61441 0.55660 0.06049  -0.02383 0.02925  482 ASN A O   
3783 C CB  . ASN A 490 ? 0.74600 0.64768 0.62036 0.07935  -0.01723 -0.00491 482 ASN A CB  
3784 C CG  . ASN A 490 ? 0.84820 0.74690 0.74924 0.09010  -0.02348 -0.00866 482 ASN A CG  
3785 O OD1 . ASN A 490 ? 0.89142 0.77245 0.77781 0.09124  -0.02469 -0.00195 482 ASN A OD1 
3786 N ND2 . ASN A 490 ? 0.79745 0.71362 0.73951 0.09769  -0.02737 -0.02021 482 ASN A ND2 
3787 N N   . GLU A 491 ? 0.73068 0.61182 0.53052 0.05468  -0.01203 0.01567  483 GLU A N   
3788 C CA  . GLU A 491 ? 0.79671 0.67098 0.57800 0.04356  -0.01801 0.02681  483 GLU A CA  
3789 C C   . GLU A 491 ? 0.80039 0.65018 0.54082 0.03843  -0.01374 0.03580  483 GLU A C   
3790 O O   . GLU A 491 ? 0.79314 0.63109 0.52178 0.03234  -0.02242 0.04718  483 GLU A O   
3791 C CB  . GLU A 491 ? 0.74777 0.63694 0.52721 0.03554  -0.01162 0.02065  483 GLU A CB  
3792 C CG  . GLU A 491 ? 0.72172 0.63876 0.54484 0.03932  -0.01511 0.01021  483 GLU A CG  
3793 C CD  . GLU A 491 ? 0.97905 0.90536 0.82551 0.03616  -0.03149 0.01656  483 GLU A CD  
3794 O OE1 . GLU A 491 ? 1.08070 0.98942 0.91033 0.03200  -0.04277 0.03079  483 GLU A OE1 
3795 O OE2 . GLU A 491 ? 1.02625 0.97810 0.90810 0.03743  -0.03313 0.00668  483 GLU A OE2 
3796 N N   . VAL A 492 ? 0.78955 0.63219 0.50963 0.04066  -0.00131 0.03028  484 VAL A N   
3797 C CA  . VAL A 492 ? 0.77095 0.59204 0.45686 0.03814  0.00404  0.03560  484 VAL A CA  
3798 C C   . VAL A 492 ? 0.80639 0.61865 0.49874 0.04255  -0.00156 0.04112  484 VAL A C   
3799 O O   . VAL A 492 ? 0.85486 0.65295 0.52707 0.03590  -0.00344 0.04969  484 VAL A O   
3800 C CB  . VAL A 492 ? 0.78968 0.60636 0.45862 0.04175  0.01585  0.02770  484 VAL A CB  
3801 C CG1 . VAL A 492 ? 0.77923 0.57602 0.42195 0.04241  0.02004  0.03106  484 VAL A CG1 
3802 C CG2 . VAL A 492 ? 0.73305 0.55401 0.38907 0.03435  0.02187  0.02408  484 VAL A CG2 
3803 N N   . ARG A 493 ? 0.78760 0.60773 0.50623 0.05212  -0.00350 0.03571  485 ARG A N   
3804 C CA  . ARG A 493 ? 0.80272 0.61465 0.53004 0.05606  -0.00817 0.03984  485 ARG A CA  
3805 C C   . ARG A 493 ? 0.83661 0.64181 0.56621 0.04908  -0.02077 0.05249  485 ARG A C   
3806 O O   . ARG A 493 ? 0.84642 0.63822 0.56601 0.04586  -0.02252 0.05974  485 ARG A O   
3807 C CB  . ARG A 493 ? 0.79187 0.61497 0.55068 0.06689  -0.00937 0.03044  485 ARG A CB  
3808 C CG  . ARG A 493 ? 0.87145 0.68582 0.63360 0.07150  -0.00875 0.03037  485 ARG A CG  
3809 C CD  . ARG A 493 ? 0.79233 0.61768 0.58084 0.08184  -0.00760 0.01813  485 ARG A CD  
3810 N NE  . ARG A 493 ? 0.84815 0.68048 0.66935 0.08525  -0.01845 0.01817  485 ARG A NE  
3811 C CZ  . ARG A 493 ? 0.82881 0.65407 0.66876 0.08804  -0.02715 0.02189  485 ARG A CZ  
3812 N NH1 . ARG A 493 ? 0.78875 0.60188 0.61836 0.08676  -0.02482 0.02523  485 ARG A NH1 
3813 N NH2 . ARG A 493 ? 0.76312 0.59354 0.63396 0.09201  -0.03851 0.02174  485 ARG A NH2 
3814 N N   . ALA A 494 ? 0.80285 0.61729 0.54462 0.04593  -0.02943 0.05494  486 ALA A N   
3815 C CA  . ALA A 494 ? 0.77247 0.58145 0.51806 0.03936  -0.04503 0.06745  486 ALA A CA  
3816 C C   . ALA A 494 ? 0.83608 0.63102 0.54353 0.02598  -0.04389 0.07686  486 ALA A C   
3817 O O   . ALA A 494 ? 0.90850 0.69574 0.61125 0.01829  -0.05694 0.08853  486 ALA A O   
3818 C CB  . ALA A 494 ? 0.72747 0.55468 0.50453 0.04227  -0.05494 0.06415  486 ALA A CB  
3819 N N   . CYS A 495 ? 0.86810 0.65854 0.54881 0.02310  -0.02982 0.07187  487 CYS A N   
3820 C CA  . CYS A 495 ? 0.87131 0.64831 0.51542 0.01079  -0.02647 0.07758  487 CYS A CA  
3821 C C   . CYS A 495 ? 0.89716 0.65761 0.51893 0.00749  -0.02003 0.08092  487 CYS A C   
3822 O O   . CYS A 495 ? 0.92989 0.67924 0.52109 -0.00085 -0.01291 0.08154  487 CYS A O   
3823 C CB  . CYS A 495 ? 0.80669 0.58585 0.43518 0.00942  -0.01528 0.06968  487 CYS A CB  
3824 S SG  . CYS A 495 ? 0.82599 0.62506 0.47463 0.00770  -0.02051 0.06576  487 CYS A SG  
3825 N N   . ARG A 496 ? 0.82539 0.58853 0.44459 -0.00975 -0.00088 0.11207  488 ARG A N   
3826 C CA  . ARG A 496 ? 0.89493 0.66458 0.50067 -0.01993 0.00151  0.12019  488 ARG A CA  
3827 C C   . ARG A 496 ? 0.93432 0.71241 0.52791 -0.02561 -0.00548 0.14054  488 ARG A C   
3828 O O   . ARG A 496 ? 0.94197 0.71078 0.54946 -0.02363 -0.01406 0.15514  488 ARG A O   
3829 C CB  . ARG A 496 ? 0.90233 0.65782 0.52536 -0.02567 0.00349  0.12245  488 ARG A CB  
3830 C CG  . ARG A 496 ? 0.89971 0.66701 0.51003 -0.03814 0.00794  0.12755  488 ARG A CG  
3831 C CD  . ARG A 496 ? 1.03920 0.79746 0.66409 -0.04482 0.01268  0.12038  488 ARG A CD  
3832 N NE  . ARG A 496 ? 1.12699 0.85939 0.77095 -0.04935 0.00804  0.13321  488 ARG A NE  
3833 C CZ  . ARG A 496 ? 1.02716 0.75332 0.66845 -0.06105 0.00472  0.15432  488 ARG A CZ  
3834 N NH1 . ARG A 496 ? 0.97957 0.72802 0.59969 -0.07052 0.00648  0.16419  488 ARG A NH1 
3835 N NH2 . ARG A 496 ? 0.96354 0.65987 0.62257 -0.06326 -0.00013 0.16543  488 ARG A NH2 
3836 N N   . GLU A 497 ? 0.94790 0.74389 0.51627 -0.03148 -0.00212 0.14065  489 GLU A N   
3837 C CA  . GLU A 497 ? 0.90459 0.71339 0.45470 -0.03903 -0.00728 0.15760  489 GLU A CA  
3838 C C   . GLU A 497 ? 0.91798 0.73745 0.45665 -0.05137 -0.00171 0.16474  489 GLU A C   
3839 O O   . GLU A 497 ? 0.89993 0.72550 0.43843 -0.05182 0.00719  0.15074  489 GLU A O   
3840 C CB  . GLU A 497 ? 0.90383 0.72647 0.43191 -0.03598 -0.00692 0.14813  489 GLU A CB  
3841 C CG  . GLU A 497 ? 1.01702 0.83486 0.55463 -0.02874 -0.01432 0.14705  489 GLU A CG  
3842 C CD  . GLU A 497 ? 1.07500 0.90265 0.59110 -0.02788 -0.01336 0.13539  489 GLU A CD  
3843 O OE1 . GLU A 497 ? 0.99860 0.83327 0.49198 -0.03029 -0.00637 0.12600  489 GLU A OE1 
3844 O OE2 . GLU A 497 ? 1.17304 1.00143 0.69598 -0.02489 -0.01948 0.13499  489 GLU A OE2 
3845 N N   . LYS A 498 ? 0.97984 0.80346 0.50959 -0.06151 -0.00716 0.18638  490 LYS A N   
3846 C CA  . LYS A 498 ? 0.97543 0.81438 0.48971 -0.07661 -0.00148 0.19571  490 LYS A CA  
3847 C C   . LYS A 498 ? 0.97697 0.84276 0.46735 -0.07639 0.00731  0.17977  490 LYS A C   
3848 O O   . LYS A 498 ? 0.93216 0.80083 0.41235 -0.06742 0.00548  0.16922  490 LYS A O   
3849 C CB  . LYS A 498 ? 1.00565 0.84256 0.51101 -0.08721 -0.01070 0.22394  490 LYS A CB  
3850 C CG  . LYS A 498 ? 1.04315 0.89150 0.53092 -0.08436 -0.01934 0.23042  490 LYS A CG  
3851 C CD  . LYS A 498 ? 1.09268 0.92823 0.58608 -0.08595 -0.03416 0.25757  490 LYS A CD  
3852 C CE  . LYS A 498 ? 1.15852 1.00678 0.64120 -0.08062 -0.04452 0.26045  490 LYS A CE  
3853 N NZ  . LYS A 498 ? 1.19661 1.03195 0.69293 -0.07694 -0.06085 0.28511  490 LYS A NZ  
3854 N N   . ASP A 499 ? 0.98864 0.87314 0.47180 -0.08593 0.01691  0.17700  491 ASP A N   
3855 C CA  . ASP A 499 ? 0.96981 0.88344 0.43049 -0.08639 0.02619  0.16348  491 ASP A CA  
3856 C C   . ASP A 499 ? 0.92427 0.83672 0.38750 -0.06969 0.03064  0.13793  491 ASP A C   
3857 O O   . ASP A 499 ? 0.96547 0.88981 0.40875 -0.06414 0.03404  0.12612  491 ASP A O   
3858 C CB  . ASP A 499 ? 0.94397 0.86898 0.37821 -0.09141 0.02215  0.17255  491 ASP A CB  
3859 C CG  . ASP A 499 ? 0.94292 0.86417 0.37303 -0.10605 0.01409  0.20129  491 ASP A CG  
3860 O OD1 . ASP A 499 ? 0.92526 0.84208 0.36632 -0.11679 0.01603  0.21357  491 ASP A OD1 
3861 O OD2 . ASP A 499 ? 0.98587 0.90765 0.40158 -0.10702 0.00520  0.21157  491 ASP A OD2 
3862 N N   . ARG A 500 ? 0.93164 0.82880 0.41676 -0.06248 0.03049  0.12974  492 ARG A N   
3863 C CA  . ARG A 500 ? 0.96632 0.86283 0.45351 -0.04789 0.03474  0.10732  492 ARG A CA  
3864 C C   . ARG A 500 ? 0.91653 0.80514 0.42761 -0.04708 0.03583  0.10222  492 ARG A C   
3865 O O   . ARG A 500 ? 0.90670 0.78570 0.43268 -0.05746 0.03316  0.11527  492 ARG A O   
3866 C CB  . ARG A 500 ? 0.93048 0.80923 0.41008 -0.03682 0.02954  0.10074  492 ARG A CB  
3867 C CG  . ARG A 500 ? 0.82654 0.68109 0.32620 -0.03174 0.02382  0.10111  492 ARG A CG  
3868 C CD  . ARG A 500 ? 0.85885 0.70146 0.34988 -0.02454 0.01943  0.09614  492 ARG A CD  
3869 N NE  . ARG A 500 ? 0.88839 0.71268 0.39913 -0.01970 0.01548  0.09471  492 ARG A NE  
3870 C CZ  . ARG A 500 ? 0.89703 0.71199 0.40577 -0.01483 0.01227  0.08985  492 ARG A CZ  
3871 N NH1 . ARG A 500 ? 0.94486 0.76374 0.43178 -0.01497 0.01174  0.08618  492 ARG A NH1 
3872 N NH2 . ARG A 500 ? 0.89385 0.69643 0.42248 -0.01088 0.01026  0.08747  492 ARG A NH2 
3873 N N   . ASP A 501 ? 0.84120 0.73267 0.35425 -0.03551 0.03915  0.08403  493 ASP A N   
3874 C CA  . ASP A 501 ? 0.86485 0.75119 0.39772 -0.03393 0.03967  0.07585  493 ASP A CA  
3875 C C   . ASP A 501 ? 0.90538 0.76380 0.45423 -0.03685 0.03365  0.08404  493 ASP A C   
3876 O O   . ASP A 501 ? 0.84828 0.69050 0.39348 -0.03064 0.02901  0.08619  493 ASP A O   
3877 C CB  . ASP A 501 ? 0.89899 0.78649 0.42648 -0.01839 0.04101  0.05737  493 ASP A CB  
3878 C CG  . ASP A 501 ? 1.00287 0.90074 0.54551 -0.01785 0.04278  0.04714  493 ASP A CG  
3879 O OD1 . ASP A 501 ? 0.93596 0.82017 0.49530 -0.02432 0.04055  0.04897  493 ASP A OD1 
3880 O OD2 . ASP A 501 ? 1.06076 0.98120 0.59882 -0.01046 0.04606  0.03658  493 ASP A OD2 
3881 N N   . PRO A 502 ? 0.92749 0.77999 0.49526 -0.04673 0.03372  0.08832  494 PRO A N   
3882 C CA  . PRO A 502 ? 0.88144 0.70555 0.46678 -0.04699 0.02873  0.09284  494 PRO A CA  
3883 C C   . PRO A 502 ? 0.90050 0.71155 0.49021 -0.03388 0.02765  0.07765  494 PRO A C   
3884 O O   . PRO A 502 ? 0.90270 0.69367 0.50381 -0.03078 0.02371  0.08085  494 PRO A O   
3885 C CB  . PRO A 502 ? 0.87341 0.69552 0.47551 -0.05993 0.03113  0.09363  494 PRO A CB  
3886 C CG  . PRO A 502 ? 0.87384 0.72444 0.46607 -0.07132 0.03620  0.09899  494 PRO A CG  
3887 C CD  . PRO A 502 ? 0.84105 0.71402 0.41491 -0.05905 0.03896  0.08838  494 PRO A CD  
3888 N N   . GLU A 503 ? 0.81920 0.64270 0.39987 -0.02637 0.03104  0.06212  495 GLU A N   
3889 C CA  . GLU A 503 ? 0.90071 0.71367 0.48136 -0.01600 0.03078  0.04773  495 GLU A CA  
3890 C C   . GLU A 503 ? 0.85990 0.67382 0.41895 -0.00565 0.03049  0.04379  495 GLU A C   
3891 O O   . GLU A 503 ? 0.86949 0.67576 0.42319 0.00199  0.03080  0.03273  495 GLU A O   
3892 C CB  . GLU A 503 ? 0.93975 0.76354 0.52558 -0.01644 0.03340  0.03422  495 GLU A CB  
3893 C CG  . GLU A 503 ? 0.92324 0.74816 0.52809 -0.02989 0.03439  0.03680  495 GLU A CG  
3894 C CD  . GLU A 503 ? 0.97564 0.80862 0.58835 -0.03180 0.03570  0.02143  495 GLU A CD  
3895 O OE1 . GLU A 503 ? 0.95441 0.81118 0.55866 -0.02740 0.03656  0.01355  495 GLU A OE1 
3896 O OE2 . GLU A 503 ? 1.11831 0.93441 0.74575 -0.03706 0.03546  0.01668  495 GLU A OE2 
3897 N N   . ALA A 504 ? 0.80999 0.63130 0.35544 -0.00673 0.03003  0.05236  496 ALA A N   
3898 C CA  . ALA A 504 ? 0.81404 0.63373 0.33712 0.00099  0.02994  0.04832  496 ALA A CA  
3899 C C   . ALA A 504 ? 0.86691 0.66755 0.39050 0.00471  0.02726  0.04554  496 ALA A C   
3900 O O   . ALA A 504 ? 0.90339 0.69717 0.41032 0.01143  0.02825  0.03672  496 ALA A O   
3901 C CB  . ALA A 504 ? 0.89712 0.72659 0.40831 -0.00420 0.02936  0.05873  496 ALA A CB  
3902 N N   . GLN A 505 ? 0.84232 0.63479 0.38467 0.00048  0.02413  0.05292  497 GLN A N   
3903 C CA  . GLN A 505 ? 0.84056 0.62107 0.38872 0.00312  0.02195  0.05084  497 GLN A CA  
3904 C C   . GLN A 505 ? 0.81820 0.59108 0.36464 0.00813  0.02567  0.03602  497 GLN A C   
3905 O O   . GLN A 505 ? 0.86052 0.62666 0.40151 0.00984  0.02590  0.03157  497 GLN A O   
3906 C CB  . GLN A 505 ? 0.81535 0.59074 0.38879 0.00029  0.01784  0.06079  497 GLN A CB  
3907 C CG  . GLN A 505 ? 0.80048 0.56952 0.39444 -0.00153 0.01969  0.05817  497 GLN A CG  
3908 C CD  . GLN A 505 ? 0.87565 0.65020 0.47132 -0.00937 0.01926  0.06876  497 GLN A CD  
3909 O OE1 . GLN A 505 ? 0.87314 0.66143 0.45151 -0.01210 0.02073  0.07151  497 GLN A OE1 
3910 N NE2 . GLN A 505 ? 0.95861 0.72196 0.57518 -0.01364 0.01790  0.07407  497 GLN A NE2 
3911 N N   . PHE A 506 ? 0.74979 0.52559 0.30008 0.00888  0.02828  0.02895  498 PHE A N   
3912 C CA  . PHE A 506 ? 0.86209 0.63279 0.40903 0.01264  0.03101  0.01551  498 PHE A CA  
3913 C C   . PHE A 506 ? 0.83725 0.60782 0.35713 0.01903  0.03164  0.01019  498 PHE A C   
3914 O O   . PHE A 506 ? 0.75639 0.51846 0.26591 0.02197  0.03290  0.00211  498 PHE A O   
3915 C CB  . PHE A 506 ? 0.81469 0.59038 0.37697 0.00964  0.03224  0.00994  498 PHE A CB  
3916 C CG  . PHE A 506 ? 0.82927 0.59681 0.41748 0.00472  0.03220  0.01155  498 PHE A CG  
3917 C CD1 . PHE A 506 ? 0.81882 0.57653 0.41618 0.00681  0.03380  0.00485  498 PHE A CD1 
3918 C CD2 . PHE A 506 ? 0.81881 0.58777 0.42227 -0.00203 0.03102  0.01937  498 PHE A CD2 
3919 C CE1 . PHE A 506 ? 0.84635 0.59512 0.46932 0.00501  0.03389  0.00475  498 PHE A CE1 
3920 C CE2 . PHE A 506 ? 0.81088 0.56642 0.43769 -0.00525 0.03046  0.02106  498 PHE A CE2 
3921 C CZ  . PHE A 506 ? 0.85401 0.59913 0.49140 -0.00034 0.03173  0.01313  498 PHE A CZ  
3922 N N   . GLU A 507 ? 0.86157 0.64033 0.36965 0.02121  0.03099  0.01454  499 GLU A N   
3923 C CA  . GLU A 507 ? 0.85181 0.62972 0.33608 0.03003  0.03133  0.00903  499 GLU A CA  
3924 C C   . GLU A 507 ? 0.84653 0.61082 0.31069 0.03088  0.03102  0.01093  499 GLU A C   
3925 O O   . GLU A 507 ? 0.84775 0.61235 0.29421 0.03703  0.03145  0.00899  499 GLU A O   
3926 C CB  . GLU A 507 ? 0.84456 0.64319 0.33074 0.03262  0.03205  0.00961  499 GLU A CB  
3927 C CG  . GLU A 507 ? 0.81239 0.62635 0.31665 0.03015  0.03219  0.00607  499 GLU A CG  
3928 C CD  . GLU A 507 ? 0.82863 0.66754 0.33292 0.03457  0.03315  0.00325  499 GLU A CD  
3929 O OE1 . GLU A 507 ? 0.85969 0.70901 0.35912 0.03417  0.03526  0.00760  499 GLU A OE1 
3930 O OE2 . GLU A 507 ? 0.83561 0.68629 0.34456 0.03841  0.03182  -0.00407 499 GLU A OE2 
3931 N N   . MET A 508 ? 0.75144 0.50532 0.21878 0.02493  0.03054  0.01314  500 MET A N   
3932 C CA  . MET A 508 ? 0.84827 0.58983 0.29694 0.02259  0.03005  0.01376  500 MET A CA  
3933 C C   . MET A 508 ? 0.88421 0.61609 0.33677 0.01716  0.03082  0.01154  500 MET A C   
3934 O O   . MET A 508 ? 0.86923 0.60807 0.34498 0.01428  0.03108  0.01241  500 MET A O   
3935 C CB  . MET A 508 ? 0.83619 0.58795 0.28765 0.01703  0.02781  0.02215  500 MET A CB  
3936 C CG  . MET A 508 ? 0.85141 0.61282 0.32916 0.01067  0.02503  0.03091  500 MET A CG  
3937 S SD  . MET A 508 ? 0.84885 0.62241 0.32468 0.00383  0.02036  0.04312  500 MET A SD  
3938 C CE  . MET A 508 ? 0.82907 0.61576 0.29834 0.00581  0.02298  0.04527  500 MET A CE  
3939 N N   . PRO A 509 ? 0.86785 0.58330 0.29794 0.01504  0.03181  0.00792  501 PRO A N   
3940 C CA  . PRO A 509 ? 0.88061 0.59051 0.31323 0.00753  0.03382  0.00531  501 PRO A CA  
3941 C C   . PRO A 509 ? 0.85161 0.57306 0.29870 -0.00072 0.03160  0.01027  501 PRO A C   
3942 O O   . PRO A 509 ? 0.89717 0.62171 0.33717 -0.00238 0.02841  0.01478  501 PRO A O   
3943 C CB  . PRO A 509 ? 0.94573 0.63425 0.35039 0.00689  0.03506  0.00106  501 PRO A CB  
3944 C CG  . PRO A 509 ? 0.93711 0.62709 0.33894 0.01123  0.03207  0.00234  501 PRO A CG  
3945 C CD  . PRO A 509 ? 0.86193 0.56717 0.27237 0.01878  0.03117  0.00532  501 PRO A CD  
3946 N N   . TYR A 510 ? 0.88109 0.61080 0.34786 -0.00527 0.03323  0.00855  502 TYR A N   
3947 C CA  . TYR A 510 ? 0.91909 0.66385 0.40332 -0.01195 0.03040  0.01248  502 TYR A CA  
3948 C C   . TYR A 510 ? 0.87976 0.62196 0.35658 -0.02136 0.03472  0.00572  502 TYR A C   
3949 O O   . TYR A 510 ? 0.89828 0.63466 0.37301 -0.02151 0.04057  -0.00124 502 TYR A O   
3950 C CB  . TYR A 510 ? 0.85389 0.61472 0.37437 -0.00727 0.02845  0.01619  502 TYR A CB  
3951 C CG  . TYR A 510 ? 0.84601 0.60820 0.37378 -0.00117 0.02485  0.02387  502 TYR A CG  
3952 C CD1 . TYR A 510 ? 0.83913 0.59414 0.36413 0.00385  0.02798  0.01978  502 TYR A CD1 
3953 C CD2 . TYR A 510 ? 0.85495 0.62738 0.39109 -0.00199 0.01814  0.03563  502 TYR A CD2 
3954 C CE1 . TYR A 510 ? 0.84277 0.60140 0.37479 0.00674  0.02554  0.02639  502 TYR A CE1 
3955 C CE2 . TYR A 510 ? 0.84837 0.62214 0.38899 0.00090  0.01576  0.04368  502 TYR A CE2 
3956 C CZ  . TYR A 510 ? 0.76755 0.53469 0.30686 0.00469  0.02000  0.03864  502 TYR A CZ  
3957 O OH  . TYR A 510 ? 0.84906 0.61987 0.39334 0.00500  0.01850  0.04608  502 TYR A OH  
3958 N N   . VAL A 511 ? 0.86590 0.61383 0.33746 -0.03067 0.03204  0.00751  503 VAL A N   
3959 C CA  . VAL A 511 ? 0.92137 0.67676 0.39511 -0.04269 0.03573  0.00198  503 VAL A CA  
3960 C C   . VAL A 511 ? 0.90091 0.68495 0.41575 -0.03940 0.03492  0.00228  503 VAL A C   
3961 O O   . VAL A 511 ? 0.92913 0.72772 0.46440 -0.03357 0.02744  0.01051  503 VAL A O   
3962 C CB  . VAL A 511 ? 0.90534 0.65912 0.36031 -0.05529 0.03245  0.00285  503 VAL A CB  
3963 C CG1 . VAL A 511 ? 0.87151 0.64352 0.33769 -0.06921 0.03510  -0.00183 503 VAL A CG1 
3964 C CG2 . VAL A 511 ? 0.93465 0.65450 0.34841 -0.05795 0.03468  -0.00006 503 VAL A CG2 
3965 N N   . VAL A 512 ? 0.88723 0.67845 0.41294 -0.04245 0.04245  -0.00632 504 VAL A N   
3966 C CA  . VAL A 512 ? 0.87379 0.69098 0.44062 -0.03647 0.04363  -0.00958 504 VAL A CA  
3967 C C   . VAL A 512 ? 0.87226 0.70003 0.44121 -0.04605 0.05389  -0.02138 504 VAL A C   
3968 O O   . VAL A 512 ? 0.86433 0.67292 0.40653 -0.05099 0.06102  -0.02672 504 VAL A O   
3969 C CB  . VAL A 512 ? 0.91527 0.72570 0.49812 -0.02231 0.04337  -0.00907 504 VAL A CB  
3970 C CG1 . VAL A 512 ? 0.84673 0.63409 0.40311 -0.02176 0.04920  -0.01451 504 VAL A CG1 
3971 C CG2 . VAL A 512 ? 0.85748 0.68809 0.48062 -0.01502 0.04599  -0.01526 504 VAL A CG2 
3972 N N   . ARG A 513 ? 0.83608 0.69532 0.43561 -0.04856 0.05436  -0.02487 505 ARG A N   
3973 C CA  . ARG A 513 ? 0.88328 0.76155 0.49399 -0.05621 0.06571  -0.03789 505 ARG A CA  
3974 C C   . ARG A 513 ? 0.90229 0.78209 0.53516 -0.04271 0.07129  -0.04616 505 ARG A C   
3975 O O   . ARG A 513 ? 0.89372 0.79766 0.56747 -0.03213 0.07017  -0.04964 505 ARG A O   
3976 C CB  . ARG A 513 ? 0.86007 0.77709 0.49970 -0.06241 0.06408  -0.03991 505 ARG A CB  
3977 C CG  . ARG A 513 ? 0.92876 0.86203 0.56130 -0.08084 0.07606  -0.05116 505 ARG A CG  
3978 C CD  . ARG A 513 ? 0.99401 0.93955 0.64197 -0.07763 0.08914  -0.06531 505 ARG A CD  
3979 N NE  . ARG A 513 ? 0.95368 0.86566 0.57177 -0.07556 0.09470  -0.06742 505 ARG A NE  
3980 C CZ  . ARG A 513 ? 0.99153 0.87718 0.56519 -0.08988 0.09979  -0.06630 505 ARG A CZ  
3981 N NH1 . ARG A 513 ? 1.03897 0.92270 0.59017 -0.10910 0.10105  -0.06341 505 ARG A NH1 
3982 N NH2 . ARG A 513 ? 0.95262 0.81273 0.50377 -0.08513 0.10286  -0.06770 505 ARG A NH2 
3983 N N   . LEU A 514 ? 0.89946 0.75379 0.50578 -0.04278 0.07641  -0.04948 506 LEU A N   
3984 C CA  . LEU A 514 ? 0.85681 0.70854 0.47651 -0.03277 0.08200  -0.05908 506 LEU A CA  
3985 C C   . LEU A 514 ? 0.88909 0.77173 0.53940 -0.03368 0.09192  -0.07380 506 LEU A C   
3986 O O   . LEU A 514 ? 0.93552 0.82938 0.57169 -0.04851 0.10069  -0.08020 506 LEU A O   
3987 C CB  . LEU A 514 ? 0.87853 0.70464 0.45843 -0.03823 0.08657  -0.06136 506 LEU A CB  
3988 C CG  . LEU A 514 ? 0.86045 0.65851 0.41010 -0.03612 0.07791  -0.04891 506 LEU A CG  
3989 C CD1 . LEU A 514 ? 0.89373 0.66987 0.40177 -0.04334 0.08198  -0.05023 506 LEU A CD1 
3990 C CD2 . LEU A 514 ? 0.88008 0.67183 0.44602 -0.02201 0.07120  -0.04479 506 LEU A CD2 
3991 N N   . HIS A 515 ? 0.87668 0.77253 0.56769 -0.01869 0.09069  -0.07882 507 HIS A N   
3992 C CA  . HIS A 515 ? 0.86717 0.79674 0.59620 -0.01496 0.09906  -0.09364 507 HIS A CA  
3993 C C   . HIS A 515 ? 0.92337 0.84792 0.66871 -0.00423 0.10655  -0.10885 507 HIS A C   
3994 O O   . HIS A 515 ? 0.99162 0.92487 0.72666 -0.01255 0.11984  -0.12452 507 HIS A O   
3995 C CB  . HIS A 515 ? 0.84438 0.79767 0.61203 -0.00511 0.08925  -0.08598 507 HIS A CB  
3996 C CG  . HIS A 515 ? 0.83729 0.83096 0.64393 -0.00170 0.09731  -0.10081 507 HIS A CG  
3997 N ND1 . HIS A 515 ? 0.91951 0.94207 0.72059 -0.01847 0.10598  -0.10802 507 HIS A ND1 
3998 C CD2 . HIS A 515 ? 0.85354 0.86418 0.70583 0.01648  0.09859  -0.11061 507 HIS A CD2 
3999 C CE1 . HIS A 515 ? 0.92523 0.98600 0.76866 -0.01070 0.11268  -0.12224 507 HIS A CE1 
4000 N NE2 . HIS A 515 ? 0.91744 0.97071 0.79336 0.01219  0.10808  -0.12442 507 HIS A NE2 
4001 N N   . ASN A 516 ? 0.95862 0.86960 0.72745 0.01207  0.09873  -0.10484 508 ASN A N   
4002 C CA  . ASN A 516 ? 0.95372 0.85284 0.73574 0.02138  0.10463  -0.11933 508 ASN A CA  
4003 C C   . ASN A 516 ? 0.98719 0.85668 0.72920 0.01397  0.10378  -0.11602 508 ASN A C   
4004 O O   . ASN A 516 ? 0.99312 0.84055 0.73315 0.01981  0.09385  -0.10391 508 ASN A O   
4005 C CB  . ASN A 516 ? 0.96010 0.85376 0.78374 0.04057  0.09659  -0.11606 508 ASN A CB  
4006 C CG  . ASN A 516 ? 0.95749 0.83916 0.79780 0.04919  0.10413  -0.13457 508 ASN A CG  
4007 O OD1 . ASN A 516 ? 0.94998 0.83994 0.78055 0.04249  0.11736  -0.15417 508 ASN A OD1 
4008 N ND2 . ASN A 516 ? 0.96643 0.82738 0.83011 0.06278  0.09592  -0.12868 508 ASN A ND2 
4009 N N   . PHE A 517 ? 0.96808 0.83937 0.67892 0.00099  0.11346  -0.12547 509 PHE A N   
4010 C CA  . PHE A 517 ? 0.94872 0.79673 0.61968 -0.00601 0.11253  -0.12316 509 PHE A CA  
4011 C C   . PHE A 517 ? 0.90701 0.76395 0.55760 -0.01665 0.12572  -0.14025 509 PHE A C   
4012 O O   . PHE A 517 ? 0.94713 0.82893 0.61163 -0.02069 0.13632  -0.15253 509 PHE A O   
4013 C CB  . PHE A 517 ? 0.89512 0.72922 0.53355 -0.01268 0.10378  -0.10385 509 PHE A CB  
4014 C CG  . PHE A 517 ? 0.87655 0.71712 0.48603 -0.02759 0.10960  -0.10301 509 PHE A CG  
4015 C CD1 . PHE A 517 ? 0.85948 0.72523 0.48620 -0.03318 0.11508  -0.10687 509 PHE A CD1 
4016 C CD2 . PHE A 517 ? 0.88976 0.71106 0.45496 -0.03636 0.10911  -0.09778 509 PHE A CD2 
4017 C CE1 . PHE A 517 ? 0.86530 0.73540 0.46409 -0.05007 0.12100  -0.10577 509 PHE A CE1 
4018 C CE2 . PHE A 517 ? 0.87163 0.69310 0.40794 -0.05125 0.11422  -0.09551 509 PHE A CE2 
4019 C CZ  . PHE A 517 ? 0.84203 0.68714 0.39437 -0.05952 0.12063  -0.09956 509 PHE A CZ  
4020 N N   . HIS A 518 ? 0.90198 0.74192 0.52032 -0.02136 0.12480  -0.14076 510 HIS A N   
4021 C CA  . HIS A 518 ? 0.90298 0.74844 0.49372 -0.03252 0.13518  -0.15440 510 HIS A CA  
4022 C C   . HIS A 518 ? 0.90659 0.73319 0.44897 -0.04098 0.12912  -0.14045 510 HIS A C   
4023 O O   . HIS A 518 ? 0.90956 0.71901 0.44278 -0.03501 0.11950  -0.13312 510 HIS A O   
4024 C CB  . HIS A 518 ? 0.93393 0.77965 0.53958 -0.02711 0.13955  -0.17322 510 HIS A CB  
4025 C CG  . HIS A 518 ? 0.95385 0.81218 0.53798 -0.03823 0.15188  -0.19116 510 HIS A CG  
4026 N ND1 . HIS A 518 ? 0.92663 0.77949 0.49994 -0.03940 0.15297  -0.20409 510 HIS A ND1 
4027 C CD2 . HIS A 518 ? 0.93426 0.81206 0.50408 -0.05041 0.16381  -0.19844 510 HIS A CD2 
4028 C CE1 . HIS A 518 ? 0.90595 0.77433 0.45817 -0.05103 0.16475  -0.21864 510 HIS A CE1 
4029 N NE2 . HIS A 518 ? 0.95323 0.83689 0.50267 -0.05822 0.17208  -0.21507 510 HIS A NE2 
4030 N N   . GLN A 519 ? 0.89245 0.72211 0.40591 -0.05432 0.13448  -0.13675 511 GLN A N   
4031 C CA  . GLN A 519 ? 0.92614 0.73477 0.39045 -0.06228 0.12946  -0.12389 511 GLN A CA  
4032 C C   . GLN A 519 ? 0.93850 0.74766 0.38031 -0.06593 0.13276  -0.13445 511 GLN A C   
4033 O O   . GLN A 519 ? 0.91744 0.74535 0.35870 -0.07506 0.14529  -0.14981 511 GLN A O   
4034 C CB  . GLN A 519 ? 0.95288 0.76179 0.39446 -0.07724 0.13475  -0.11671 511 GLN A CB  
4035 C CG  . GLN A 519 ? 1.04598 0.82494 0.43991 -0.08251 0.12706  -0.09967 511 GLN A CG  
4036 C CD  . GLN A 519 ? 1.01682 0.78600 0.39955 -0.09181 0.12631  -0.08779 511 GLN A CD  
4037 O OE1 . GLN A 519 ? 1.10271 0.87155 0.47087 -0.10497 0.12857  -0.08192 511 GLN A OE1 
4038 N NE2 . GLN A 519 ? 0.92594 0.69416 0.33295 -0.08309 0.11910  -0.08161 511 GLN A NE2 
4039 N N   . LEU A 520 ? 0.90141 0.69428 0.32651 -0.05925 0.12202  -0.12745 512 LEU A N   
4040 C CA  . LEU A 520 ? 0.95308 0.74955 0.36331 -0.06043 0.12197  -0.13822 512 LEU A CA  
4041 C C   . LEU A 520 ? 1.00016 0.79846 0.38525 -0.06575 0.11472  -0.12469 512 LEU A C   
4042 O O   . LEU A 520 ? 1.03909 0.84806 0.41735 -0.06674 0.11238  -0.13084 512 LEU A O   
4043 C CB  . LEU A 520 ? 0.96686 0.75572 0.39197 -0.04802 0.11045  -0.13539 512 LEU A CB  
4044 C CG  . LEU A 520 ? 0.94022 0.73156 0.41160 -0.03827 0.10962  -0.13819 512 LEU A CG  
4045 C CD1 . LEU A 520 ? 0.84606 0.63067 0.32695 -0.03020 0.09947  -0.13558 512 LEU A CD1 
4046 C CD2 . LEU A 520 ? 0.94002 0.74794 0.44194 -0.03970 0.12178  -0.15871 512 LEU A CD2 
4047 N N   . SER A 521 ? 0.98457 0.77139 0.35610 -0.06917 0.11106  -0.10736 513 SER A N   
4048 C CA  . SER A 521 ? 1.03027 0.81165 0.37640 -0.07430 0.10473  -0.09294 513 SER A CA  
4049 C C   . SER A 521 ? 1.06197 0.82974 0.39845 -0.08269 0.10668  -0.08020 513 SER A C   
4050 O O   . SER A 521 ? 1.04795 0.80969 0.39684 -0.08112 0.10867  -0.07962 513 SER A O   
4051 C CB  . SER A 521 ? 0.98083 0.75116 0.31673 -0.06262 0.08965  -0.08167 513 SER A CB  
4052 O OG  . SER A 521 ? 1.03898 0.80548 0.34961 -0.06643 0.08418  -0.07071 513 SER A OG  
4053 N N   . ALA A 522 ? 1.02032 0.78238 0.33353 -0.09242 0.10615  -0.07053 514 ALA A N   
4054 C CA  . ALA A 522 ? 0.99652 0.74098 0.29565 -0.10341 0.10770  -0.05814 514 ALA A CA  
4055 C C   . ALA A 522 ? 1.07476 0.79048 0.36912 -0.09221 0.09521  -0.04354 514 ALA A C   
4056 O O   . ALA A 522 ? 1.09141 0.79736 0.37827 -0.07977 0.08405  -0.03663 514 ALA A O   
4057 C CB  . ALA A 522 ? 1.01632 0.75739 0.28837 -0.11641 0.10953  -0.05108 514 ALA A CB  
4058 N N   . PRO A 523 ? 1.04165 0.74534 0.34049 -0.09615 0.09687  -0.03969 515 PRO A N   
4059 C CA  . PRO A 523 ? 1.06418 0.74009 0.35748 -0.08616 0.08604  -0.02758 515 PRO A CA  
4060 C C   . PRO A 523 ? 1.10198 0.75041 0.36655 -0.08433 0.07736  -0.01378 515 PRO A C   
4061 O O   . PRO A 523 ? 1.11284 0.75483 0.35708 -0.09850 0.08166  -0.00975 515 PRO A O   
4062 C CB  . PRO A 523 ? 1.08275 0.75263 0.37880 -0.09786 0.09174  -0.02710 515 PRO A CB  
4063 C CG  . PRO A 523 ? 1.09164 0.79414 0.40655 -0.10686 0.10462  -0.04192 515 PRO A CG  
4064 C CD  . PRO A 523 ? 1.06593 0.78475 0.37558 -0.11044 0.10943  -0.04820 515 PRO A CD  
4065 N N   . GLN A 524 ? 1.05882 0.69241 0.32166 -0.06696 0.06585  -0.00728 516 GLN A N   
4066 C CA  . GLN A 524 ? 1.10795 0.71205 0.34320 -0.06026 0.05603  0.00571  516 GLN A CA  
4067 C C   . GLN A 524 ? 1.13655 0.71039 0.36765 -0.05092 0.04984  0.01207  516 GLN A C   
4068 O O   . GLN A 524 ? 1.10691 0.69046 0.36009 -0.04391 0.04989  0.00670  516 GLN A O   
4069 C CB  . GLN A 524 ? 1.04330 0.66219 0.27910 -0.04627 0.04793  0.00536  516 GLN A CB  
4070 C CG  . GLN A 524 ? 1.03058 0.67654 0.26442 -0.05595 0.05338  -0.00134 516 GLN A CG  
4071 C CD  . GLN A 524 ? 1.04855 0.70876 0.27909 -0.04384 0.04417  -0.00144 516 GLN A CD  
4072 O OE1 . GLN A 524 ? 1.08128 0.72361 0.29513 -0.03232 0.03302  0.00949  516 GLN A OE1 
4073 N NE2 . GLN A 524 ? 1.02951 0.72193 0.27492 -0.04637 0.04876  -0.01486 516 GLN A NE2 
4074 N N   . PRO A 525 ? 1.10923 0.64368 0.30958 -0.05039 0.04444  0.02329  517 PRO A N   
4075 C CA  . PRO A 525 ? 1.08605 0.58691 0.27750 -0.04179 0.03955  0.02737  517 PRO A CA  
4076 C C   . PRO A 525 ? 1.19038 0.69490 0.39175 -0.01697 0.03004  0.02703  517 PRO A C   
4077 O O   . PRO A 525 ? 1.10774 0.62120 0.30486 -0.00635 0.02364  0.02981  517 PRO A O   
4078 C CB  . PRO A 525 ? 1.14367 0.59839 0.29434 -0.04866 0.03686  0.03883  517 PRO A CB  
4079 C CG  . PRO A 525 ? 1.22324 0.69054 0.36317 -0.04874 0.03411  0.04374  517 PRO A CG  
4080 C CD  . PRO A 525 ? 1.11772 0.63532 0.28732 -0.05757 0.04261  0.03247  517 PRO A CD  
4081 N N   . CYS A 526 ? 1.17093 0.67083 0.38418 -0.00943 0.02947  0.02343  518 CYS A N   
4082 C CA  . CYS A 526 ? 1.11277 0.62029 0.33817 0.01267  0.02244  0.02141  518 CYS A CA  
4083 C C   . CYS A 526 ? 1.18159 0.64408 0.37853 0.02564  0.01636  0.02693  518 CYS A C   
4084 O O   . CYS A 526 ? 1.17616 0.62441 0.35529 0.04185  0.00799  0.03258  518 CYS A O   
4085 C CB  . CYS A 526 ? 1.07689 0.61414 0.33504 0.01180  0.02678  0.01299  518 CYS A CB  
4086 S SG  . CYS A 526 ? 1.06128 0.61550 0.33608 0.03516  0.02000  0.00996  518 CYS A SG  
4087 N N   . PHE A 527 ? 1.21156 0.65170 0.40210 0.01932  0.02003  0.02483  519 PHE A N   
4088 C CA  . PHE A 527 ? 1.17377 0.56641 0.33412 0.03117  0.01577  0.02714  519 PHE A CA  
4089 C C   . PHE A 527 ? 1.18530 0.53478 0.31547 0.01140  0.02023  0.03024  519 PHE A C   
4090 O O   . PHE A 527 ? 1.18194 0.54867 0.32626 -0.01004 0.02787  0.02643  519 PHE A O   
4091 C CB  . PHE A 527 ? 1.13720 0.54336 0.31546 0.04184  0.01622  0.01931  519 PHE A CB  
4092 C CG  . PHE A 527 ? 1.13829 0.58708 0.34591 0.05845  0.01287  0.01567  519 PHE A CG  
4093 C CD1 . PHE A 527 ? 1.11864 0.56825 0.31806 0.07726  0.00520  0.01932  519 PHE A CD1 
4094 C CD2 . PHE A 527 ? 1.11895 0.60627 0.36021 0.05474  0.01682  0.00910  519 PHE A CD2 
4095 C CE1 . PHE A 527 ? 1.12517 0.61515 0.35017 0.09016  0.00239  0.01519  519 PHE A CE1 
4096 C CE2 . PHE A 527 ? 1.06482 0.58818 0.32979 0.06739  0.01427  0.00604  519 PHE A CE2 
4097 C CZ  . PHE A 527 ? 1.07409 0.59953 0.33120 0.08427  0.00747  0.00842  519 PHE A CZ  
4098 N N   . THR A 528 ? 1.22499 0.51875 0.31304 0.01888  0.01518  0.03697  520 THR A N   
4099 C CA  . THR A 528 ? 1.27864 0.51828 0.32838 0.00068  0.01841  0.04055  520 THR A CA  
4100 C C   . THR A 528 ? 1.31938 0.50817 0.33818 0.01589  0.01491  0.03789  520 THR A C   
4101 O O   . THR A 528 ? 1.32493 0.50892 0.34001 0.04458  0.00761  0.03797  520 THR A O   
4102 C CB  . THR A 528 ? 1.32426 0.53563 0.34483 -0.00657 0.01561  0.05233  520 THR A CB  
4103 O OG1 . THR A 528 ? 1.28505 0.54811 0.33424 -0.01841 0.01948  0.05256  520 THR A OG1 
4104 C CG2 . THR A 528 ? 1.38096 0.53853 0.36287 -0.02974 0.01974  0.05643  520 THR A CG2 
4105 N N   . PHE A 529 ? 1.34929 0.50247 0.34513 -0.00287 0.02019  0.03466  521 PHE A N   
4106 C CA  . PHE A 529 ? 1.40296 0.49531 0.35783 0.00695  0.01823  0.03117  521 PHE A CA  
4107 C C   . PHE A 529 ? 1.46746 0.49845 0.37749 -0.01875 0.02168  0.03582  521 PHE A C   
4108 O O   . PHE A 529 ? 1.48757 0.54085 0.41080 -0.04924 0.02888  0.03530  521 PHE A O   
4109 C CB  . PHE A 529 ? 1.36767 0.48958 0.34652 0.00848  0.02216  0.01768  521 PHE A CB  
4110 C CG  . PHE A 529 ? 1.38470 0.55901 0.40237 0.03393  0.01878  0.01308  521 PHE A CG  
4111 C CD1 . PHE A 529 ? 1.38784 0.53977 0.38715 0.06468  0.01318  0.00990  521 PHE A CD1 
4112 C CD2 . PHE A 529 ? 1.29283 0.53717 0.36283 0.02722  0.02138  0.01161  521 PHE A CD2 
4113 C CE1 . PHE A 529 ? 1.35656 0.56006 0.39191 0.08552  0.01082  0.00532  521 PHE A CE1 
4114 C CE2 . PHE A 529 ? 1.21643 0.50556 0.31915 0.04742  0.01860  0.00800  521 PHE A CE2 
4115 C CZ  . PHE A 529 ? 1.26313 0.53415 0.34978 0.07517  0.01360  0.00496  521 PHE A CZ  
4116 N N   . SER A 530 ? 1.54157 0.49747 0.40034 -0.00612 0.01651  0.04041  522 SER A N   
4117 C CA  . SER A 530 ? 1.61674 0.50064 0.42666 -0.02884 0.01879  0.04532  522 SER A CA  
4118 C C   . SER A 530 ? 1.67004 0.49910 0.44448 -0.02435 0.02023  0.03612  522 SER A C   
4119 O O   . SER A 530 ? 1.67448 0.51427 0.46619 0.00768  0.01562  0.02674  522 SER A O   
4120 C CB  . SER A 530 ? 1.67242 0.51274 0.45611 -0.01836 0.01058  0.05956  522 SER A CB  
4121 O OG  . SER A 530 ? 1.70254 0.59620 0.51640 -0.02218 0.00940  0.06696  522 SER A OG  
4122 N N   . HIS A 531 ? 1.71851 0.50924 0.46917 -0.05611 0.02648  0.03243  523 HIS A N   
4123 C CA  . HIS A 531 ? 1.73887 0.48816 0.47659 -0.05803 0.02821  0.01626  523 HIS A CA  
4124 C C   . HIS A 531 ? 1.82451 0.49267 0.51321 -0.08462 0.03003  0.02294  523 HIS A C   
4125 O O   . HIS A 531 ? 1.82950 0.50186 0.50802 -0.12042 0.03599  0.03101  523 HIS A O   
4126 C CB  . HIS A 531 ? 1.67983 0.48972 0.45193 -0.07461 0.03514  -0.00126 523 HIS A CB  
4127 C CG  . HIS A 531 ? 1.62051 0.50113 0.43681 -0.04853 0.03311  -0.00696 523 HIS A CG  
4128 N ND1 . HIS A 531 ? 1.65823 0.53592 0.48260 -0.01291 0.02843  -0.01556 523 HIS A ND1 
4129 C CD2 . HIS A 531 ? 1.54021 0.49443 0.39442 -0.05279 0.03533  -0.00508 523 HIS A CD2 
4130 C CE1 . HIS A 531 ? 1.59731 0.54461 0.46173 0.00124  0.02807  -0.01799 523 HIS A CE1 
4131 N NE2 . HIS A 531 ? 1.49020 0.48349 0.37485 -0.02234 0.03182  -0.01133 523 HIS A NE2 
4132 N N   . PRO A 532 ? 1.89771 0.48894 0.55449 -0.06876 0.02549  0.01952  524 PRO A N   
4133 C CA  . PRO A 532 ? 1.94528 0.53154 0.61416 -0.02461 0.01917  0.00881  524 PRO A CA  
4134 C C   . PRO A 532 ? 2.01692 0.61983 0.69577 0.01249  0.00946  0.02381  524 PRO A C   
4135 O O   . PRO A 532 ? 2.05123 0.64446 0.71641 0.00660  0.00531  0.04183  524 PRO A O   
4136 C CB  . PRO A 532 ? 1.99145 0.50638 0.63030 -0.02175 0.01720  0.00311  524 PRO A CB  
4137 C CG  . PRO A 532 ? 2.02788 0.51235 0.63911 -0.05366 0.01782  0.01910  524 PRO A CG  
4138 C CD  . PRO A 532 ? 1.97496 0.50643 0.59724 -0.09159 0.02633  0.02196  524 PRO A CD  
4139 N N   . ASN A 533 ? 1.94846 0.59430 0.66013 0.04768  0.00621  0.01274  525 ASN A N   
4140 C CA  . ASN A 533 ? 2.08284 0.75226 0.80938 0.08582  -0.00370 0.02327  525 ASN A CA  
4141 C C   . ASN A 533 ? 2.20603 0.79827 0.90165 0.11773  -0.01337 0.02786  525 ASN A C   
4142 O O   . ASN A 533 ? 2.26299 0.85674 0.97326 0.15021  -0.01533 0.01234  525 ASN A O   
4143 C CB  . ASN A 533 ? 1.98388 0.73430 0.75962 0.10669  -0.00214 0.00884  525 ASN A CB  
4144 C CG  . ASN A 533 ? 2.10711 0.88700 0.90070 0.14380  -0.01212 0.01751  525 ASN A CG  
4145 O OD1 . ASN A 533 ? 2.10801 0.92113 0.92864 0.17285  -0.01354 0.00493  525 ASN A OD1 
4146 N ND2 . ASN A 533 ? 2.17948 0.94984 0.95751 0.14202  -0.01902 0.03858  525 ASN A ND2 
4147 N N   . ARG A 534 ? 2.33832 0.89837 1.01132 0.10650  -0.01846 0.04350  526 ARG A N   
4148 C CA  . ARG A 534 ? 2.46969 0.98109 1.12709 0.13285  -0.02881 0.04862  526 ARG A CA  
4149 C C   . ARG A 534 ? 2.56503 1.10940 1.24287 0.17388  -0.04095 0.05756  526 ARG A C   
4150 O O   . ARG A 534 ? 2.55918 1.10248 1.23010 0.17421  -0.04938 0.07550  526 ARG A O   
4151 C CB  . ARG A 534 ? 2.53997 1.00680 1.16621 0.10327  -0.02977 0.06291  526 ARG A CB  
4152 C CG  . ARG A 534 ? 2.48375 0.91393 1.08869 0.06505  -0.01906 0.05324  526 ARG A CG  
4153 C CD  . ARG A 534 ? 2.58226 0.95474 1.15399 0.04526  -0.02169 0.06541  526 ARG A CD  
4154 N NE  . ARG A 534 ? 2.63528 0.95345 1.19505 0.07586  -0.03019 0.06456  526 ARG A NE  
4155 C CZ  . ARG A 534 ? 2.70413 0.96042 1.23419 0.06459  -0.03312 0.07286  526 ARG A CZ  
4156 N NH1 . ARG A 534 ? 2.64669 0.88813 1.15440 0.02193  -0.02790 0.08252  526 ARG A NH1 
4157 N NH2 . ARG A 534 ? 2.78632 0.99648 1.31050 0.09629  -0.04108 0.07109  526 ARG A NH2 
4158 N N   . ASP A 535 ? 2.44362 1.02294 1.14825 0.20431  -0.04113 0.04460  527 ASP A N   
4159 C CA  . ASP A 535 ? 2.39460 1.01295 1.12265 0.24462  -0.05268 0.05080  527 ASP A CA  
4160 C C   . ASP A 535 ? 2.31933 0.94827 1.06969 0.28235  -0.05229 0.03021  527 ASP A C   
4161 O O   . ASP A 535 ? 2.28525 0.88448 1.02927 0.27556  -0.04411 0.01275  527 ASP A O   
4162 C CB  . ASP A 535 ? 2.35517 1.04105 1.10402 0.23449  -0.05221 0.05998  527 ASP A CB  
4163 C CG  . ASP A 535 ? 2.42816 1.15838 1.20076 0.27080  -0.06486 0.06709  527 ASP A CG  
4164 O OD1 . ASP A 535 ? 2.48472 1.24246 1.28045 0.30268  -0.06636 0.05530  527 ASP A OD1 
4165 O OD2 . ASP A 535 ? 2.29451 1.03512 1.06488 0.26584  -0.07274 0.08293  527 ASP A OD2 
4166 N N   . ASP A 539 ? 1.59293 0.66957 0.56132 0.27993  -0.03437 0.00069  531 ASP A N   
4167 C CA  . ASP A 539 ? 1.52484 0.63649 0.51514 0.26246  -0.02135 -0.01638 531 ASP A CA  
4168 C C   . ASP A 539 ? 1.48419 0.62287 0.48073 0.22447  -0.01512 -0.00969 531 ASP A C   
4169 O O   . ASP A 539 ? 1.51837 0.63747 0.49627 0.21109  -0.01920 0.00581  531 ASP A O   
4170 C CB  . ASP A 539 ? 1.53240 0.70705 0.56188 0.28625  -0.01996 -0.02992 531 ASP A CB  
4171 C CG  . ASP A 539 ? 1.44608 0.68426 0.50551 0.29126  -0.02535 -0.02208 531 ASP A CG  
4172 O OD1 . ASP A 539 ? 1.46419 0.72481 0.52928 0.26476  -0.02299 -0.01395 531 ASP A OD1 
4173 O OD2 . ASP A 539 ? 1.49595 0.76140 0.57348 0.32167  -0.03182 -0.02526 531 ASP A OD2 
4174 N N   . ASN A 540 ? 1.38311 0.56468 0.40401 0.20806  -0.00565 -0.02079 532 ASN A N   
4175 C CA  . ASN A 540 ? 1.36754 0.57592 0.39809 0.17373  0.00063  -0.01654 532 ASN A CA  
4176 C C   . ASN A 540 ? 1.31445 0.59368 0.38593 0.17441  0.00015  -0.01415 532 ASN A C   
4177 O O   . ASN A 540 ? 1.27184 0.58535 0.37495 0.14775  0.00440  -0.01001 532 ASN A O   
4178 C CB  . ASN A 540 ? 1.37881 0.58539 0.40921 0.15316  0.00984  -0.02840 532 ASN A CB  
4179 C CG  . ASN A 540 ? 1.43594 0.57391 0.42744 0.14026  0.01127  -0.02931 532 ASN A CG  
4180 O OD1 . ASN A 540 ? 1.50144 0.60333 0.46895 0.12711  0.00885  -0.01704 532 ASN A OD1 
4181 N ND2 . ASN A 540 ? 1.51218 0.63195 0.49589 0.14189  0.01573  -0.04433 532 ASN A ND2 
4182 N N   . ASN A 541 ? 1.28607 0.59411 0.37347 0.20190  -0.00490 -0.01704 533 ASN A N   
4183 C CA  . ASN A 541 ? 1.22507 0.59517 0.34733 0.20339  -0.00688 -0.01418 533 ASN A CA  
4184 C C   . ASN A 541 ? 1.31089 0.67431 0.42710 0.19851  -0.01404 -0.00009 533 ASN A C   
4185 O O   . ASN A 541 ? 1.35280 0.66598 0.43019 0.21147  -0.02147 0.00780  533 ASN A O   
4186 C CB  . ASN A 541 ? 1.23355 0.64018 0.37784 0.23220  -0.00997 -0.02237 533 ASN A CB  
4187 C CG  . ASN A 541 ? 1.25531 0.68828 0.41775 0.23172  -0.00095 -0.03656 533 ASN A CG  
4188 O OD1 . ASN A 541 ? 1.27970 0.71626 0.44784 0.20751  0.00652  -0.03856 533 ASN A OD1 
4189 N ND2 . ASN A 541 ? 1.31898 0.77648 0.49679 0.25727  -0.00187 -0.04590 533 ASN A ND2 
4190 N N   . ARG A 542 ? 1.26615 0.62553 0.57653 0.06055  0.00142  0.01400  534 ARG A N   
4191 C CA  . ARG A 542 ? 1.22338 0.58306 0.52306 0.05441  -0.00631 0.02528  534 ARG A CA  
4192 C C   . ARG A 542 ? 1.19353 0.59005 0.51606 0.06111  -0.00849 0.02487  534 ARG A C   
4193 O O   . ARG A 542 ? 1.23080 0.65525 0.57560 0.06374  -0.00219 0.01738  534 ARG A O   
4194 C CB  . ARG A 542 ? 1.18777 0.54618 0.46869 0.03227  -0.00136 0.02955  534 ARG A CB  
4195 C CG  . ARG A 542 ? 1.19069 0.51260 0.44800 0.02195  -0.00045 0.03142  534 ARG A CG  
4196 C CD  . ARG A 542 ? 1.23071 0.51399 0.46762 0.02588  -0.01164 0.04106  534 ARG A CD  
4197 N NE  . ARG A 542 ? 1.25666 0.51131 0.46657 0.00718  -0.01195 0.04832  534 ARG A NE  
4198 C CZ  . ARG A 542 ? 1.23530 0.45539 0.43294 0.00463  -0.01299 0.04580  534 ARG A CZ  
4199 N NH1 . ARG A 542 ? 1.29585 0.50551 0.50488 0.02091  -0.01262 0.03448  534 ARG A NH1 
4200 N NH2 . ARG A 542 ? 1.26214 0.45863 0.43604 -0.01488 -0.01419 0.05406  534 ARG A NH2 
4201 N N   . TYR A 543 ? 1.24312 0.63801 0.55821 0.06245  -0.01800 0.03320  535 TYR A N   
4202 C CA  . TYR A 543 ? 1.13310 0.55882 0.46370 0.06568  -0.02228 0.03364  535 TYR A CA  
4203 C C   . TYR A 543 ? 1.19150 0.61036 0.49741 0.05473  -0.02741 0.04228  535 TYR A C   
4204 O O   . TYR A 543 ? 1.28244 0.67316 0.56768 0.05629  -0.03628 0.05129  535 TYR A O   
4205 C CB  . TYR A 543 ? 1.11335 0.54556 0.46582 0.08530  -0.03104 0.03288  535 TYR A CB  
4206 C CG  . TYR A 543 ? 1.15797 0.61435 0.52253 0.08891  -0.03954 0.03505  535 TYR A CG  
4207 C CD1 . TYR A 543 ? 1.12478 0.60837 0.49605 0.07918  -0.03542 0.03151  535 TYR A CD1 
4208 C CD2 . TYR A 543 ? 1.22784 0.67931 0.59883 0.10271  -0.05314 0.04003  535 TYR A CD2 
4209 C CE1 . TYR A 543 ? 1.10134 0.60465 0.48292 0.08251  -0.04422 0.03205  535 TYR A CE1 
4210 C CE2 . TYR A 543 ? 1.18465 0.65722 0.56585 0.10535  -0.06244 0.04168  535 TYR A CE2 
4211 C CZ  . TYR A 543 ? 1.15932 0.65721 0.54491 0.09501  -0.05775 0.03719  535 TYR A CZ  
4212 O OH  . TYR A 543 ? 1.15450 0.67067 0.54907 0.09747  -0.06783 0.03749  535 TYR A OH  
4213 N N   . CYS A 544 ? 1.17096 0.61452 0.47869 0.04367  -0.02195 0.03935  536 CYS A N   
4214 C CA  . CYS A 544 ? 1.15895 0.60269 0.44321 0.03092  -0.02263 0.04461  536 CYS A CA  
4215 C C   . CYS A 544 ? 1.13545 0.61094 0.43403 0.03276  -0.02464 0.03901  536 CYS A C   
4216 O O   . CYS A 544 ? 1.15894 0.65899 0.48116 0.03220  -0.01870 0.03036  536 CYS A O   
4217 C CB  . CYS A 544 ? 1.11107 0.55271 0.38237 0.01306  -0.01134 0.04419  536 CYS A CB  
4218 S SG  . CYS A 544 ? 1.22239 0.67096 0.46713 -0.00365 -0.00855 0.04898  536 CYS A SG  
4219 N N   . THR A 545 ? 1.16595 0.63884 0.44936 0.03431  -0.03393 0.04399  537 THR A N   
4220 C CA  . THR A 545 ? 1.11797 0.61638 0.40738 0.03445  -0.03719 0.03822  537 THR A CA  
4221 C C   . THR A 545 ? 1.11671 0.61849 0.37983 0.01852  -0.02992 0.03825  537 THR A C   
4222 O O   . THR A 545 ? 1.22921 0.70842 0.46119 0.01080  -0.03134 0.04849  537 THR A O   
4223 C CB  . THR A 545 ? 1.07846 0.57273 0.36748 0.04641  -0.05310 0.04284  537 THR A CB  
4224 O OG1 . THR A 545 ? 1.09977 0.59449 0.41664 0.06080  -0.05758 0.04219  537 THR A OG1 
4225 C CG2 . THR A 545 ? 1.04345 0.56127 0.33749 0.04662  -0.05810 0.03590  537 THR A CG2 
4226 N N   . LEU A 546 ? 1.07758 0.60665 0.35381 0.01363  -0.02251 0.02729  538 LEU A N   
4227 C CA  . LEU A 546 ? 1.09015 0.63045 0.34697 -0.00017 -0.01368 0.02378  538 LEU A CA  
4228 C C   . LEU A 546 ? 1.07968 0.64135 0.34074 0.00406  -0.01847 0.01385  538 LEU A C   
4229 O O   . LEU A 546 ? 1.05938 0.63449 0.34955 0.01462  -0.02452 0.00652  538 LEU A O   
4230 C CB  . LEU A 546 ? 1.05410 0.60813 0.32605 -0.00939 0.00001  0.01750  538 LEU A CB  
4231 C CG  . LEU A 546 ? 1.10482 0.63780 0.37263 -0.01483 0.00445  0.02552  538 LEU A CG  
4232 C CD1 . LEU A 546 ? 1.04845 0.59785 0.33211 -0.02484 0.01613  0.01909  538 LEU A CD1 
4233 C CD2 . LEU A 546 ? 1.16771 0.67335 0.39858 -0.02418 0.00341  0.03860  538 LEU A CD2 
4234 N N   . GLU A 547 ? 1.15504 0.71885 0.38627 -0.00483 -0.01613 0.01381  539 GLU A N   
4235 C CA  . GLU A 547 ? 1.11689 0.70070 0.34560 -0.00310 -0.01869 0.00184  539 GLU A CA  
4236 C C   . GLU A 547 ? 1.06785 0.67264 0.29058 -0.01531 -0.00234 -0.00839 539 GLU A C   
4237 O O   . GLU A 547 ? 1.09092 0.68882 0.28288 -0.02874 0.00580  -0.00073 539 GLU A O   
4238 C CB  . GLU A 547 ? 1.09710 0.66581 0.29289 -0.00232 -0.03129 0.01003  539 GLU A CB  
4239 C CG  . GLU A 547 ? 1.09357 0.64727 0.30228 0.01175  -0.04873 0.01790  539 GLU A CG  
4240 C CD  . GLU A 547 ? 1.33529 0.88495 0.52486 0.01581  -0.06467 0.01980  539 GLU A CD  
4241 O OE1 . GLU A 547 ? 1.41206 0.94561 0.56236 0.00762  -0.06833 0.03023  539 GLU A OE1 
4242 O OE2 . GLU A 547 ? 1.39507 0.95743 0.60817 0.02590  -0.07434 0.01145  539 GLU A OE2 
4243 N N   . PHE A 548 ? 1.03674 0.66632 0.29009 -0.01091 0.00179  -0.02457 540 PHE A N   
4244 C CA  . PHE A 548 ? 1.05909 0.71364 0.31886 -0.01924 0.01722  -0.03748 540 PHE A CA  
4245 C C   . PHE A 548 ? 1.13280 0.80545 0.38609 -0.01624 0.01651  -0.05377 540 PHE A C   
4246 O O   . PHE A 548 ? 1.11353 0.79448 0.39241 -0.00491 0.00754  -0.06512 540 PHE A O   
4247 C CB  . PHE A 548 ? 0.98915 0.65673 0.29140 -0.01550 0.02059  -0.04423 540 PHE A CB  
4248 C CG  . PHE A 548 ? 1.05187 0.70581 0.35781 -0.02166 0.02502  -0.03161 540 PHE A CG  
4249 C CD1 . PHE A 548 ? 1.07613 0.73149 0.36670 -0.03624 0.03798  -0.02693 540 PHE A CD1 
4250 C CD2 . PHE A 548 ? 0.97275 0.61331 0.29714 -0.01372 0.01648  -0.02503 540 PHE A CD2 
4251 C CE1 . PHE A 548 ? 1.01283 0.65348 0.30567 -0.04256 0.04068  -0.01617 540 PHE A CE1 
4252 C CE2 . PHE A 548 ? 0.97787 0.60481 0.30306 -0.01935 0.02061  -0.01544 540 PHE A CE2 
4253 C CZ  . PHE A 548 ? 1.02676 0.65225 0.33586 -0.03366 0.03188  -0.01116 540 PHE A CZ  
4254 N N   . PRO A 549 ? 1.08715 0.76606 0.30516 -0.02699 0.02569  -0.05568 541 PRO A N   
4255 C CA  . PRO A 549 ? 1.10972 0.80744 0.31895 -0.02477 0.02724  -0.07404 541 PRO A CA  
4256 C C   . PRO A 549 ? 1.09415 0.82185 0.33881 -0.02171 0.03851  -0.09504 541 PRO A C   
4257 O O   . PRO A 549 ? 1.10036 0.84197 0.35017 -0.03113 0.05402  -0.09529 541 PRO A O   
4258 C CB  . PRO A 549 ? 1.13478 0.83126 0.29500 -0.03993 0.03618  -0.06715 541 PRO A CB  
4259 C CG  . PRO A 549 ? 1.13382 0.82384 0.29315 -0.05223 0.04596  -0.05030 541 PRO A CG  
4260 C CD  . PRO A 549 ? 1.11187 0.77979 0.29510 -0.04288 0.03496  -0.04044 541 PRO A CD  
4261 N N   . VAL A 550 ? 1.05017 0.78618 0.31990 -0.00880 0.02907  -0.11152 542 VAL A N   
4262 C CA  . VAL A 550 ? 1.07304 0.83408 0.38219 -0.00232 0.03479  -0.13280 542 VAL A CA  
4263 C C   . VAL A 550 ? 1.16135 0.94002 0.45497 -0.00051 0.03986  -0.15520 542 VAL A C   
4264 O O   . VAL A 550 ? 1.14799 0.91576 0.42404 0.00496  0.02679  -0.15902 542 VAL A O   
4265 C CB  . VAL A 550 ? 1.05353 0.80767 0.40438 0.01049  0.01848  -0.13410 542 VAL A CB  
4266 C CG1 . VAL A 550 ? 1.07599 0.85159 0.46738 0.01787  0.02039  -0.15508 542 VAL A CG1 
4267 C CG2 . VAL A 550 ? 1.04638 0.78523 0.40990 0.00824  0.01538  -0.11378 542 VAL A CG2 
4268 N N   . GLU A 551 ? 1.07523 0.88134 0.37636 -0.00480 0.05801  -0.17035 543 GLU A N   
4269 C CA  . GLU A 551 ? 1.09196 0.91952 0.37516 -0.00465 0.06815  -0.19381 543 GLU A CA  
4270 C C   . GLU A 551 ? 1.09158 0.94044 0.42168 0.00873  0.06858  -0.22041 543 GLU A C   
4271 O O   . GLU A 551 ? 1.21791 1.09350 0.54543 0.00844  0.08384  -0.24226 543 GLU A O   
4272 C CB  . GLU A 551 ? 1.12001 0.96518 0.37159 -0.02159 0.09083  -0.19014 543 GLU A CB  
4273 C CG  . GLU A 551 ? 1.23270 1.05372 0.43706 -0.03565 0.08870  -0.16297 543 GLU A CG  
4274 C CD  . GLU A 551 ? 1.45018 1.25131 0.61715 -0.03369 0.07341  -0.15862 543 GLU A CD  
4275 O OE1 . GLU A 551 ? 1.44252 1.26050 0.60040 -0.03001 0.07475  -0.17748 543 GLU A OE1 
4276 O OE2 . GLU A 551 ? 1.34209 1.11575 0.49885 -0.03456 0.05882  -0.13567 543 GLU A OE2 
4277 N N   . VAL A 552 ? 1.09208 0.92964 0.46313 0.01994  0.05215  -0.21890 544 VAL A N   
4278 C CA  . VAL A 552 ? 1.02055 0.87187 0.44003 0.03359  0.04706  -0.24149 544 VAL A CA  
4279 C C   . VAL A 552 ? 1.02912 0.85684 0.47101 0.04386  0.02212  -0.23640 544 VAL A C   
4280 O O   . VAL A 552 ? 0.98702 0.79403 0.42007 0.03987  0.01300  -0.21293 544 VAL A O   
4281 C CB  . VAL A 552 ? 1.01270 0.88361 0.47158 0.03189  0.05784  -0.24148 544 VAL A CB  
4282 C CG1 . VAL A 552 ? 1.01810 0.92096 0.46734 0.02427  0.08258  -0.25419 544 VAL A CG1 
4283 C CG2 . VAL A 552 ? 1.02528 0.87998 0.48792 0.02378  0.05427  -0.21320 544 VAL A CG2 
4284 N N   . ASN A 553 ? 1.03785 0.86913 0.50897 0.05638  0.01162  -0.25797 545 ASN A N   
4285 C CA  . ASN A 553 ? 0.98321 0.79702 0.48952 0.06512  -0.01141 -0.25380 545 ASN A CA  
4286 C C   . ASN A 553 ? 0.94094 0.75983 0.48662 0.06380  -0.01019 -0.24257 545 ASN A C   
4287 O O   . ASN A 553 ? 0.94109 0.78198 0.50509 0.06394  0.00348  -0.25388 545 ASN A O   
4288 C CB  . ASN A 553 ? 1.00347 0.81796 0.53020 0.07784  -0.02364 -0.28058 545 ASN A CB  
4289 C CG  . ASN A 553 ? 1.06998 0.87913 0.55658 0.07882  -0.02609 -0.29383 545 ASN A CG  
4290 O OD1 . ASN A 553 ? 1.11020 0.90469 0.56129 0.07226  -0.03094 -0.27763 545 ASN A OD1 
4291 N ND2 . ASN A 553 ? 1.04702 0.86745 0.53960 0.08751  -0.02392 -0.32410 545 ASN A ND2 
4292 N N   . THR A 554 ? 0.91463 0.71579 0.47216 0.06193  -0.02334 -0.22126 546 THR A N   
4293 C CA  . THR A 554 ? 0.93167 0.73495 0.51980 0.05840  -0.02304 -0.20749 546 THR A CA  
4294 C C   . THR A 554 ? 0.93299 0.71626 0.53438 0.05844  -0.04110 -0.18893 546 THR A C   
4295 O O   . THR A 554 ? 0.90155 0.67135 0.49189 0.06169  -0.05375 -0.18755 546 THR A O   
4296 C CB  . THR A 554 ? 0.90306 0.71369 0.46901 0.04670  -0.00392 -0.19432 546 THR A CB  
4297 O OG1 . THR A 554 ? 0.85885 0.67294 0.45555 0.04351  -0.00450 -0.18452 546 THR A OG1 
4298 C CG2 . THR A 554 ? 0.94858 0.74110 0.47403 0.03951  -0.00312 -0.17471 546 THR A CG2 
4299 N N   . VAL A 555 ? 0.87975 0.66297 0.50396 0.05413  -0.04199 -0.17544 547 VAL A N   
4300 C CA  . VAL A 555 ? 0.90667 0.67476 0.54335 0.05178  -0.05570 -0.15624 547 VAL A CA  
4301 C C   . VAL A 555 ? 0.89705 0.66294 0.52081 0.04194  -0.04459 -0.13719 547 VAL A C   
4302 O O   . VAL A 555 ? 0.80929 0.58569 0.44833 0.03793  -0.03740 -0.13753 547 VAL A O   
4303 C CB  . VAL A 555 ? 0.81574 0.58430 0.49650 0.05617  -0.07163 -0.16054 547 VAL A CB  
4304 C CG1 . VAL A 555 ? 0.85555 0.61227 0.54782 0.05094  -0.08319 -0.13971 547 VAL A CG1 
4305 C CG2 . VAL A 555 ? 0.81978 0.58620 0.51322 0.06611  -0.08468 -0.17983 547 VAL A CG2 
4306 N N   . LEU A 556 ? 0.87453 0.62696 0.47247 0.03864  -0.04421 -0.12197 548 LEU A N   
4307 C CA  . LEU A 556 ? 0.92131 0.66686 0.50435 0.03030  -0.03529 -0.10424 548 LEU A CA  
4308 C C   . LEU A 556 ? 0.86314 0.60577 0.47282 0.02770  -0.04388 -0.09343 548 LEU A C   
4309 O O   . LEU A 556 ? 0.83637 0.57333 0.45872 0.03114  -0.05728 -0.08938 548 LEU A O   
4310 C CB  . LEU A 556 ? 0.88091 0.61212 0.43158 0.03043  -0.03487 -0.09385 548 LEU A CB  
4311 C CG  . LEU A 556 ? 0.85056 0.57018 0.38720 0.02444  -0.02892 -0.07640 548 LEU A CG  
4312 C CD1 . LEU A 556 ? 0.87879 0.60145 0.40203 0.01573  -0.01375 -0.07508 548 LEU A CD1 
4313 C CD2 . LEU A 556 ? 0.84084 0.54627 0.35169 0.02742  -0.03175 -0.06765 548 LEU A CD2 
4314 N N   . HIS A 557 ? 0.80004 0.54695 0.41665 0.02057  -0.03677 -0.08836 549 HIS A N   
4315 C CA  . HIS A 557 ? 0.79384 0.53836 0.43129 0.01567  -0.04396 -0.07739 549 HIS A CA  
4316 C C   . HIS A 557 ? 0.84255 0.57698 0.45805 0.00771  -0.03508 -0.06263 549 HIS A C   
4317 O O   . HIS A 557 ? 0.92270 0.65258 0.54717 0.00384  -0.04086 -0.05225 549 HIS A O   
4318 C CB  . HIS A 557 ? 0.81147 0.56898 0.47911 0.01414  -0.04671 -0.08478 549 HIS A CB  
4319 C CG  . HIS A 557 ? 0.87011 0.63432 0.56468 0.02314  -0.05854 -0.09929 549 HIS A CG  
4320 N ND1 . HIS A 557 ? 0.80364 0.58106 0.50393 0.02889  -0.05263 -0.11758 549 HIS A ND1 
4321 C CD2 . HIS A 557 ? 0.82771 0.58657 0.54448 0.02715  -0.07599 -0.09887 549 HIS A CD2 
4322 C CE1 . HIS A 557 ? 0.88008 0.65847 0.60543 0.03744  -0.06638 -0.12928 549 HIS A CE1 
4323 N NE2 . HIS A 557 ? 0.86252 0.62843 0.59849 0.03599  -0.08175 -0.11727 549 HIS A NE2 
4324 N N   . GLY A 558 ? 0.87050 0.60085 0.45762 0.00468  -0.02198 -0.06180 550 GLY A N   
4325 C CA  . GLY A 558 ? 0.85289 0.56994 0.41728 -0.00221 -0.01406 -0.04938 550 GLY A CA  
4326 C C   . GLY A 558 ? 0.86785 0.58077 0.40340 -0.00654 -0.00123 -0.04989 550 GLY A C   
4327 O O   . GLY A 558 ? 0.87190 0.59319 0.40170 -0.00368 0.00194  -0.05941 550 GLY A O   
4328 N N   . PHE A 559 ? 0.89037 0.59010 0.40714 -0.01402 0.00561  -0.04011 551 PHE A N   
4329 C CA  . PHE A 559 ? 0.85666 0.54756 0.34343 -0.02075 0.01663  -0.03694 551 PHE A CA  
4330 C C   . PHE A 559 ? 0.82646 0.51774 0.31429 -0.03305 0.02326  -0.03307 551 PHE A C   
4331 O O   . PHE A 559 ? 0.90567 0.58548 0.39377 -0.03609 0.02080  -0.02587 551 PHE A O   
4332 C CB  . PHE A 559 ? 0.83690 0.50493 0.29683 -0.01692 0.01562  -0.02787 551 PHE A CB  
4333 C CG  . PHE A 559 ? 0.93967 0.60791 0.39606 -0.00626 0.00864  -0.03103 551 PHE A CG  
4334 C CD1 . PHE A 559 ? 0.87929 0.55162 0.35636 0.00246  -0.00179 -0.03210 551 PHE A CD1 
4335 C CD2 . PHE A 559 ? 0.96552 0.63058 0.39733 -0.00647 0.01178  -0.03241 551 PHE A CD2 
4336 C CE1 . PHE A 559 ? 0.85188 0.52477 0.32692 0.01127  -0.00963 -0.03500 551 PHE A CE1 
4337 C CE2 . PHE A 559 ? 0.91723 0.58206 0.34453 0.00256  0.00372  -0.03540 551 PHE A CE2 
4338 C CZ  . PHE A 559 ? 0.94259 0.61133 0.39254 0.01165  -0.00730 -0.03703 551 PHE A CZ  
4339 N N   . ALA A 560 ? 0.83906 0.54489 0.32796 -0.04033 0.03151  -0.03837 552 ALA A N   
4340 C CA  . ALA A 560 ? 0.83873 0.54606 0.32593 -0.05413 0.03861  -0.03417 552 ALA A CA  
4341 C C   . ALA A 560 ? 0.89385 0.57457 0.34516 -0.06108 0.04343  -0.02298 552 ALA A C   
4342 O O   . ALA A 560 ? 0.91114 0.58248 0.33833 -0.05847 0.04600  -0.02116 552 ALA A O   
4343 C CB  . ALA A 560 ? 0.83708 0.57050 0.33601 -0.05936 0.04708  -0.04335 552 ALA A CB  
4344 N N   . GLY A 561 ? 0.91785 0.58500 0.36529 -0.06951 0.04306  -0.01584 553 GLY A N   
4345 C CA  . GLY A 561 ? 0.91059 0.54947 0.32622 -0.07696 0.04642  -0.00606 553 GLY A CA  
4346 C C   . GLY A 561 ? 0.94740 0.58937 0.35984 -0.09419 0.05291  -0.00295 553 GLY A C   
4347 O O   . GLY A 561 ? 1.01975 0.67694 0.45579 -0.09976 0.05114  -0.00568 553 GLY A O   
4348 N N   . TYR A 562 ? 0.94665 0.57530 0.33166 -0.10324 0.05906  0.00341  554 TYR A N   
4349 C CA  . TYR A 562 ? 0.99094 0.61840 0.36778 -0.12228 0.06522  0.00894  554 TYR A CA  
4350 C C   . TYR A 562 ? 1.03705 0.62433 0.37921 -0.12783 0.06329  0.01995  554 TYR A C   
4351 O O   . TYR A 562 ? 1.06138 0.62598 0.39142 -0.11506 0.05738  0.02154  554 TYR A O   
4352 C CB  . TYR A 562 ? 1.02468 0.67889 0.40273 -0.13010 0.07544  0.00596  554 TYR A CB  
4353 C CG  . TYR A 562 ? 0.95390 0.64498 0.36369 -0.12062 0.07727  -0.00743 554 TYR A CG  
4354 C CD1 . TYR A 562 ? 0.92414 0.64381 0.36839 -0.12507 0.07847  -0.01416 554 TYR A CD1 
4355 C CD2 . TYR A 562 ? 0.92171 0.61832 0.32772 -0.10717 0.07664  -0.01379 554 TYR A CD2 
4356 C CE1 . TYR A 562 ? 0.95298 0.70457 0.42833 -0.11517 0.07908  -0.02753 554 TYR A CE1 
4357 C CE2 . TYR A 562 ? 0.92292 0.65059 0.35746 -0.09813 0.07752  -0.02762 554 TYR A CE2 
4358 C CZ  . TYR A 562 ? 0.91933 0.67405 0.38930 -0.10154 0.07882  -0.03487 554 TYR A CZ  
4359 O OH  . TYR A 562 ? 0.86759 0.65082 0.36784 -0.09127 0.07848  -0.04953 554 TYR A OH  
4360 N N   . PHE A 563 ? 1.02207 0.60072 0.35033 -0.14611 0.06744  0.02721  555 PHE A N   
4361 C CA  . PHE A 563 ? 1.04823 0.58553 0.34250 -0.15314 0.06453  0.03818  555 PHE A CA  
4362 C C   . PHE A 563 ? 1.08831 0.62626 0.36848 -0.17567 0.07100  0.04675  555 PHE A C   
4363 O O   . PHE A 563 ? 1.09305 0.66313 0.39419 -0.18720 0.07749  0.04349  555 PHE A O   
4364 C CB  . PHE A 563 ? 1.11718 0.62840 0.41030 -0.15137 0.05727  0.03797  555 PHE A CB  
4365 C CG  . PHE A 563 ? 1.09347 0.60819 0.39454 -0.16931 0.05767  0.03910  555 PHE A CG  
4366 C CD1 . PHE A 563 ? 1.07754 0.62360 0.41010 -0.17052 0.05754  0.03208  555 PHE A CD1 
4367 C CD2 . PHE A 563 ? 1.14994 0.63546 0.42760 -0.18560 0.05643  0.04780  555 PHE A CD2 
4368 C CE1 . PHE A 563 ? 1.08879 0.63880 0.42966 -0.18744 0.05614  0.03372  555 PHE A CE1 
4369 C CE2 . PHE A 563 ? 1.13817 0.62716 0.42359 -0.20324 0.05551  0.04897  555 PHE A CE2 
4370 C CZ  . PHE A 563 ? 1.14658 0.66878 0.46379 -0.20406 0.05536  0.04192  555 PHE A CZ  
4371 N N   . GLU A 564 ? 1.09849 0.60161 0.34517 -0.18175 0.06845  0.05798  556 GLU A N   
4372 C CA  . GLU A 564 ? 1.15304 0.64256 0.37954 -0.20558 0.07121  0.06989  556 GLU A CA  
4373 C C   . GLU A 564 ? 1.19634 0.63468 0.40033 -0.20749 0.06088  0.07697  556 GLU A C   
4374 O O   . GLU A 564 ? 1.20455 0.61901 0.40249 -0.18866 0.05353  0.07400  556 GLU A O   
4375 C CB  . GLU A 564 ? 1.23931 0.73097 0.44161 -0.21276 0.07639  0.07868  556 GLU A CB  
4376 C CG  . GLU A 564 ? 1.13816 0.67754 0.35746 -0.20916 0.08714  0.06979  556 GLU A CG  
4377 C CD  . GLU A 564 ? 1.29902 0.84090 0.48926 -0.22018 0.09332  0.07899  556 GLU A CD  
4378 O OE1 . GLU A 564 ? 1.33306 0.84272 0.50043 -0.21513 0.08406  0.08807  556 GLU A OE1 
4379 O OE2 . GLU A 564 ? 1.34278 0.92318 0.54159 -0.23239 0.10619  0.07592  556 GLU A OE2 
4380 N N   . THR A 565 ? 1.19147 0.61401 0.38455 -0.22928 0.06020  0.08536  557 THR A N   
4381 C CA  . THR A 565 ? 1.22724 0.59738 0.39701 -0.23356 0.04970  0.09161  557 THR A CA  
4382 C C   . THR A 565 ? 1.27050 0.62285 0.41770 -0.26014 0.04963  0.10685  557 THR A C   
4383 O O   . THR A 565 ? 1.26457 0.64988 0.42477 -0.27933 0.05796  0.10912  557 THR A O   
4384 C CB  . THR A 565 ? 1.21208 0.57692 0.39711 -0.23139 0.04531  0.08199  557 THR A CB  
4385 O OG1 . THR A 565 ? 1.25135 0.56350 0.41127 -0.23396 0.03548  0.08610  557 THR A OG1 
4386 C CG2 . THR A 565 ? 1.20339 0.60047 0.41031 -0.25041 0.05002  0.08059  557 THR A CG2 
4387 N N   . VAL A 566 ? 1.31096 0.61670 0.43195 -0.25963 0.03951  0.11574  558 VAL A N   
4388 C CA  . VAL A 566 ? 1.35456 0.63733 0.46187 -0.28184 0.03368  0.12815  558 VAL A CA  
4389 C C   . VAL A 566 ? 1.39838 0.64553 0.49995 -0.28969 0.02546  0.12583  558 VAL A C   
4390 O O   . VAL A 566 ? 1.41763 0.61921 0.50356 -0.27548 0.01529  0.12274  558 VAL A O   
4391 C CB  . VAL A 566 ? 1.39001 0.64094 0.47635 -0.27516 0.02402  0.13760  558 VAL A CB  
4392 C CG1 . VAL A 566 ? 1.44359 0.67023 0.51590 -0.29815 0.01643  0.15096  558 VAL A CG1 
4393 C CG2 . VAL A 566 ? 1.39635 0.68072 0.48618 -0.26647 0.03084  0.13885  558 VAL A CG2 
4394 N N   . LEU A 567 ? 1.39939 0.66704 0.51346 -0.31111 0.02971  0.12643  559 LEU A N   
4395 C CA  . LEU A 567 ? 1.38980 0.62500 0.49788 -0.32362 0.02066  0.12513  559 LEU A CA  
4396 C C   . LEU A 567 ? 1.44265 0.63399 0.52951 -0.33352 0.00848  0.13518  559 LEU A C   
4397 O O   . LEU A 567 ? 1.55555 0.69653 0.62499 -0.32412 -0.00315 0.13135  559 LEU A O   
4398 C CB  . LEU A 567 ? 1.38297 0.65597 0.51207 -0.34663 0.02725  0.12572  559 LEU A CB  
4399 C CG  . LEU A 567 ? 1.39303 0.71953 0.55543 -0.33549 0.03694  0.11356  559 LEU A CG  
4400 C CD1 . LEU A 567 ? 1.36846 0.72966 0.55608 -0.35777 0.03983  0.11381  559 LEU A CD1 
4401 C CD2 . LEU A 567 ? 1.33866 0.65321 0.50683 -0.31009 0.03156  0.09869  559 LEU A CD2 
4402 N N   . TYR A 568 ? 1.54427 0.75487 0.63225 -0.35115 0.01134  0.14736  560 TYR A N   
4403 C CA  . TYR A 568 ? 1.64310 0.81819 0.71171 -0.36252 -0.00026 0.15992  560 TYR A CA  
4404 C C   . TYR A 568 ? 1.58852 0.79974 0.65983 -0.37463 0.00815  0.17198  560 TYR A C   
4405 O O   . TYR A 568 ? 1.55490 0.81488 0.64467 -0.39019 0.02109  0.17295  560 TYR A O   
4406 C CB  . TYR A 568 ? 1.60229 0.75403 0.66819 -0.38412 -0.00957 0.16217  560 TYR A CB  
4407 C CG  . TYR A 568 ? 1.63809 0.74338 0.68273 -0.39295 -0.02497 0.17302  560 TYR A CG  
4408 C CD1 . TYR A 568 ? 1.63984 0.69321 0.66476 -0.37298 -0.03769 0.17067  560 TYR A CD1 
4409 C CD2 . TYR A 568 ? 1.64575 0.75909 0.69119 -0.42128 -0.02741 0.18581  560 TYR A CD2 
4410 C CE1 . TYR A 568 ? 1.68085 0.69024 0.68758 -0.38032 -0.05339 0.18070  560 TYR A CE1 
4411 C CE2 . TYR A 568 ? 1.68367 0.75356 0.70965 -0.43003 -0.04284 0.19667  560 TYR A CE2 
4412 C CZ  . TYR A 568 ? 1.71041 0.72738 0.71702 -0.40926 -0.05639 0.19407  560 TYR A CZ  
4413 O OH  . TYR A 568 ? 1.76743 0.74049 0.75624 -0.41721 -0.07296 0.20490  560 TYR A OH  
4414 N N   . GLN A 569 ? 1.61978 0.80869 0.67338 -0.36673 0.00120  0.18023  561 GLN A N   
4415 C CA  . GLN A 569 ? 1.66858 0.88198 0.71720 -0.37921 0.00612  0.19354  561 GLN A CA  
4416 C C   . GLN A 569 ? 1.61346 0.89132 0.68175 -0.37995 0.02607  0.18839  561 GLN A C   
4417 O O   . GLN A 569 ? 1.54593 0.83638 0.61830 -0.35737 0.03083  0.17933  561 GLN A O   
4418 C CB  . GLN A 569 ? 1.60416 0.80424 0.64497 -0.40795 -0.00076 0.20755  561 GLN A CB  
4419 C CG  . GLN A 569 ? 1.65449 0.78932 0.67281 -0.40486 -0.02188 0.21386  561 GLN A CG  
4420 C CD  . GLN A 569 ? 1.70060 0.81911 0.71245 -0.43308 -0.03050 0.22635  561 GLN A CD  
4421 O OE1 . GLN A 569 ? 1.69816 0.85586 0.72138 -0.45682 -0.02036 0.23258  561 GLN A OE1 
4422 N NE2 . GLN A 569 ? 1.74543 0.80568 0.73965 -0.43034 -0.04974 0.22994  561 GLN A NE2 
4423 N N   . ASP A 570 ? 1.51480 0.83227 0.59537 -0.40441 0.03710  0.19346  562 ASP A N   
4424 C CA  . ASP A 570 ? 1.53939 0.91994 0.63760 -0.40746 0.05699  0.18913  562 ASP A CA  
4425 C C   . ASP A 570 ? 1.50041 0.91198 0.62523 -0.40604 0.06660  0.17599  562 ASP A C   
4426 O O   . ASP A 570 ? 1.53054 0.99196 0.67202 -0.40300 0.08248  0.16865  562 ASP A O   
4427 C CB  . ASP A 570 ? 1.55116 0.96156 0.64823 -0.43477 0.06529  0.20194  562 ASP A CB  
4428 C CG  . ASP A 570 ? 1.57439 0.98388 0.68009 -0.46157 0.06278  0.20868  562 ASP A CG  
4429 O OD1 . ASP A 570 ? 1.60468 0.96879 0.70408 -0.46112 0.04741  0.20889  562 ASP A OD1 
4430 O OD2 . ASP A 570 ? 1.55141 1.00650 0.67047 -0.48252 0.07628  0.21294  562 ASP A OD2 
4431 N N   . ILE A 571 ? 1.50775 0.89063 0.63569 -0.40824 0.05685  0.17273  563 ILE A N   
4432 C CA  . ILE A 571 ? 1.43538 0.84223 0.58704 -0.40775 0.06281  0.16144  563 ILE A CA  
4433 C C   . ILE A 571 ? 1.42683 0.82540 0.57858 -0.37768 0.06208  0.14857  563 ILE A C   
4434 O O   . ILE A 571 ? 1.46311 0.81376 0.59750 -0.36266 0.04922  0.14705  563 ILE A O   
4435 C CB  . ILE A 571 ? 1.46362 0.84254 0.61646 -0.42389 0.05132  0.16348  563 ILE A CB  
4436 C CG1 . ILE A 571 ? 1.51767 0.89051 0.66393 -0.45126 0.04696  0.17800  563 ILE A CG1 
4437 C CG2 . ILE A 571 ? 1.40508 0.81755 0.58480 -0.42965 0.05801  0.15502  563 ILE A CG2 
4438 C CD1 . ILE A 571 ? 1.56476 0.87531 0.68296 -0.44961 0.02867  0.18500  563 ILE A CD1 
4439 N N   . THR A 572 ? 1.38508 0.82931 0.55570 -0.36923 0.07551  0.13948  564 THR A N   
4440 C CA  . THR A 572 ? 1.34092 0.78610 0.51419 -0.34091 0.07618  0.12733  564 THR A CA  
4441 C C   . THR A 572 ? 1.25949 0.74910 0.47255 -0.33486 0.08195  0.11283  564 THR A C   
4442 O O   . THR A 572 ? 1.25246 0.77842 0.48759 -0.35344 0.08930  0.11359  564 THR A O   
4443 C CB  . THR A 572 ? 1.36786 0.83188 0.53558 -0.32759 0.08273  0.12647  564 THR A CB  
4444 O OG1 . THR A 572 ? 1.34175 0.85945 0.52495 -0.34105 0.09899  0.12533  564 THR A OG1 
4445 C CG2 . THR A 572 ? 1.38007 0.80931 0.52289 -0.32842 0.07329  0.13810  564 THR A CG2 
4446 N N   . LEU A 573 ? 1.21422 0.70254 0.43992 -0.30904 0.07738  0.10000  565 LEU A N   
4447 C CA  . LEU A 573 ? 1.20474 0.73766 0.47097 -0.29707 0.08122  0.08529  565 LEU A CA  
4448 C C   . LEU A 573 ? 1.18186 0.72914 0.45224 -0.27217 0.08474  0.07650  565 LEU A C   
4449 O O   . LEU A 573 ? 1.17994 0.69321 0.42391 -0.25996 0.07951  0.07983  565 LEU A O   
4450 C CB  . LEU A 573 ? 1.23692 0.75153 0.51329 -0.29258 0.06994  0.07937  565 LEU A CB  
4451 C CG  . LEU A 573 ? 1.25442 0.75416 0.52773 -0.31724 0.06435  0.08646  565 LEU A CG  
4452 C CD1 . LEU A 573 ? 1.29918 0.77210 0.57224 -0.31087 0.05216  0.08002  565 LEU A CD1 
4453 C CD2 . LEU A 573 ? 1.19347 0.74391 0.49963 -0.33482 0.07217  0.08648  565 LEU A CD2 
4454 N N   . SER A 574 ? 1.14444 0.73994 0.44816 -0.26506 0.09229  0.06551  566 SER A N   
4455 C CA  . SER A 574 ? 1.15172 0.76563 0.46364 -0.24271 0.09545  0.05552  566 SER A CA  
4456 C C   . SER A 574 ? 1.10162 0.75872 0.45815 -0.23352 0.09723  0.04154  566 SER A C   
4457 O O   . SER A 574 ? 1.10352 0.79179 0.48469 -0.24751 0.10238  0.04009  566 SER A O   
4458 C CB  . SER A 574 ? 1.15230 0.77825 0.44497 -0.24777 0.10583  0.05963  566 SER A CB  
4459 O OG  . SER A 574 ? 1.17185 0.82256 0.47687 -0.22858 0.10955  0.04776  566 SER A OG  
4460 N N   . ILE A 575 ? 1.07698 0.73471 0.44464 -0.21127 0.09180  0.03238  567 ILE A N   
4461 C CA  . ILE A 575 ? 1.06201 0.75944 0.47011 -0.19881 0.09262  0.01868  567 ILE A CA  
4462 C C   . ILE A 575 ? 1.05673 0.76676 0.46122 -0.18319 0.09756  0.01116  567 ILE A C   
4463 O O   . ILE A 575 ? 1.03917 0.77594 0.47408 -0.16976 0.09652  -0.00105 567 ILE A O   
4464 C CB  . ILE A 575 ? 1.01759 0.70496 0.44317 -0.18855 0.08005  0.01512  567 ILE A CB  
4465 C CG1 . ILE A 575 ? 0.97849 0.63187 0.38176 -0.17264 0.07286  0.01649  567 ILE A CG1 
4466 C CG2 . ILE A 575 ? 1.04317 0.72039 0.47121 -0.20554 0.07488  0.02139  567 ILE A CG2 
4467 C CD1 . ILE A 575 ? 0.98306 0.63745 0.40707 -0.16007 0.06297  0.01086  567 ILE A CD1 
4468 N N   . ARG A 576 ? 1.04365 0.73288 0.41166 -0.18525 0.10101  0.01857  568 ARG A N   
4469 C CA  . ARG A 576 ? 1.11641 0.81799 0.47385 -0.17538 0.10671  0.01297  568 ARG A CA  
4470 C C   . ARG A 576 ? 1.09185 0.84075 0.47093 -0.18270 0.12037  0.00345  568 ARG A C   
4471 O O   . ARG A 576 ? 1.08488 0.84403 0.45610 -0.20244 0.12978  0.01010  568 ARG A O   
4472 C CB  . ARG A 576 ? 1.13377 0.80155 0.44536 -0.18160 0.10633  0.02638  568 ARG A CB  
4473 C CG  . ARG A 576 ? 1.18200 0.85418 0.47599 -0.17112 0.10848  0.02267  568 ARG A CG  
4474 C CD  . ARG A 576 ? 1.24833 0.88340 0.49721 -0.17826 0.10491  0.03845  568 ARG A CD  
4475 N NE  . ARG A 576 ? 1.24924 0.89415 0.47553 -0.17705 0.10975  0.03751  568 ARG A NE  
4476 C CZ  . ARG A 576 ? 1.27420 0.89959 0.46177 -0.18933 0.11010  0.05155  568 ARG A CZ  
4477 N NH1 . ARG A 576 ? 1.29064 0.88723 0.46664 -0.20196 0.10462  0.06690  568 ARG A NH1 
4478 N NH2 . ARG A 576 ? 1.32025 0.96111 0.49733 -0.18588 0.11251  0.04885  568 ARG A NH2 
4479 N N   . PRO A 577 ? 1.04450 0.82417 0.45324 -0.16744 0.12180  -0.01282 569 PRO A N   
4480 C CA  . PRO A 577 ? 1.01599 0.84354 0.45515 -0.17181 0.13405  -0.02517 569 PRO A CA  
4481 C C   . PRO A 577 ? 1.11570 0.95967 0.53049 -0.18927 0.15058  -0.02128 569 PRO A C   
4482 O O   . PRO A 577 ? 1.14718 1.02357 0.58266 -0.20273 0.16109  -0.02362 569 PRO A O   
4483 C CB  . PRO A 577 ? 0.94557 0.79083 0.40629 -0.14985 0.13133  -0.04274 569 PRO A CB  
4484 C CG  . PRO A 577 ? 0.93144 0.74270 0.38976 -0.13579 0.11444  -0.03853 569 PRO A CG  
4485 C CD  . PRO A 577 ? 0.95431 0.72479 0.37063 -0.14530 0.11142  -0.02073 569 PRO A CD  
4486 N N   . GLU A 578 ? 1.07762 0.89969 0.44978 -0.18960 0.15183  -0.01454 570 GLU A N   
4487 C CA  . GLU A 578 ? 1.16712 1.00015 0.50715 -0.20742 0.16638  -0.00834 570 GLU A CA  
4488 C C   . GLU A 578 ? 1.19043 1.01620 0.52141 -0.23298 0.17017  0.00829  570 GLU A C   
4489 O O   . GLU A 578 ? 1.23899 1.10082 0.57682 -0.24982 0.18586  0.00689  570 GLU A O   
4490 C CB  . GLU A 578 ? 1.21432 1.01393 0.50666 -0.20382 0.16114  0.00053  570 GLU A CB  
4491 C CG  . GLU A 578 ? 1.17048 0.97006 0.46733 -0.17971 0.15421  -0.01336 570 GLU A CG  
4492 C CD  . GLU A 578 ? 1.19041 0.95168 0.48909 -0.16363 0.13550  -0.00849 570 GLU A CD  
4493 O OE1 . GLU A 578 ? 1.15380 0.91714 0.48610 -0.15712 0.12935  -0.01262 570 GLU A OE1 
4494 O OE2 . GLU A 578 ? 1.19031 0.92067 0.45687 -0.15843 0.12701  -0.00006 570 GLU A OE2 
4495 N N   . THR A 579 ? 1.14345 0.92509 0.46051 -0.23571 0.15640  0.02250  571 THR A N   
4496 C CA  . THR A 579 ? 1.18669 0.94671 0.48531 -0.25993 0.15574  0.04074  571 THR A CA  
4497 C C   . THR A 579 ? 1.18767 0.94768 0.51951 -0.26247 0.14838  0.03972  571 THR A C   
4498 O O   . THR A 579 ? 1.19957 0.92850 0.51506 -0.27789 0.14195  0.05400  571 THR A O   
4499 C CB  . THR A 579 ? 1.21973 0.92371 0.47218 -0.26106 0.14421  0.05739  571 THR A CB  
4500 O OG1 . THR A 579 ? 1.23550 0.90677 0.49633 -0.24595 0.12876  0.05662  571 THR A OG1 
4501 C CG2 . THR A 579 ? 1.26704 0.96497 0.48964 -0.25142 0.14521  0.05696  571 THR A CG2 
4502 N N   . HIS A 580 ? 1.14273 0.93470 0.51836 -0.24863 0.14807  0.02372  572 HIS A N   
4503 C CA  . HIS A 580 ? 1.07822 0.86991 0.48651 -0.24753 0.13798  0.02161  572 HIS A CA  
4504 C C   . HIS A 580 ? 1.13893 0.93980 0.55306 -0.27392 0.14203  0.03144  572 HIS A C   
4505 O O   . HIS A 580 ? 1.08182 0.92314 0.50882 -0.28666 0.15663  0.02895  572 HIS A O   
4506 C CB  . HIS A 580 ? 1.10339 0.93351 0.55885 -0.23005 0.13768  0.00336  572 HIS A CB  
4507 C CG  . HIS A 580 ? 1.13835 0.95646 0.61795 -0.22248 0.12247  0.00202  572 HIS A CG  
4508 N ND1 . HIS A 580 ? 1.12386 0.93556 0.61193 -0.23853 0.11670  0.01013  572 HIS A ND1 
4509 C CD2 . HIS A 580 ? 1.06962 0.88081 0.56478 -0.20230 0.11136  -0.00572 572 HIS A CD2 
4510 C CE1 . HIS A 580 ? 1.05293 0.85416 0.55861 -0.22834 0.10292  0.00721  572 HIS A CE1 
4511 N NE2 . HIS A 580 ? 1.06351 0.86456 0.57402 -0.20652 0.09971  -0.00187 572 HIS A NE2 
4512 N N   . SER A 581 ? 1.16596 0.93140 0.57106 -0.28202 0.12971  0.04145  573 SER A N   
4513 C CA  . SER A 581 ? 1.16944 0.93807 0.58195 -0.30725 0.12922  0.05089  573 SER A CA  
4514 C C   . SER A 581 ? 1.12182 0.94473 0.58722 -0.30889 0.13384  0.03988  573 SER A C   
4515 O O   . SER A 581 ? 1.09774 0.93125 0.59287 -0.29133 0.12599  0.02883  573 SER A O   
4516 C CB  . SER A 581 ? 1.13754 0.85764 0.53362 -0.31000 0.11298  0.05877  573 SER A CB  
4517 O OG  . SER A 581 ? 1.16032 0.83150 0.51324 -0.30321 0.10774  0.06611  573 SER A OG  
4518 N N   . PRO A 582 ? 1.18591 1.04589 0.66649 -0.32990 0.14617  0.04280  574 PRO A N   
4519 C CA  . PRO A 582 ? 1.18607 1.10422 0.72125 -0.32887 0.15247  0.03032  574 PRO A CA  
4520 C C   . PRO A 582 ? 1.20625 1.12382 0.77514 -0.32819 0.13610  0.02890  574 PRO A C   
4521 O O   . PRO A 582 ? 1.18395 1.07946 0.74251 -0.34732 0.12799  0.04101  574 PRO A O   
4522 C CB  . PRO A 582 ? 1.19114 1.14256 0.72867 -0.35601 0.16865  0.03756  574 PRO A CB  
4523 C CG  . PRO A 582 ? 1.32054 1.23326 0.80004 -0.36764 0.17302  0.05235  574 PRO A CG  
4524 C CD  . PRO A 582 ? 1.24704 1.09617 0.69527 -0.35626 0.15421  0.05865  574 PRO A CD  
4525 N N   . GLY A 583 ? 1.16176 1.10151 0.76831 -0.30691 0.13044  0.01457  575 GLY A N   
4526 C CA  . GLY A 583 ? 1.16871 1.11527 0.81253 -0.30466 0.11427  0.01209  575 GLY A CA  
4527 C C   . GLY A 583 ? 1.10229 0.99434 0.71630 -0.30612 0.09642  0.02183  575 GLY A C   
4528 O O   . GLY A 583 ? 1.11950 1.01011 0.74936 -0.31831 0.08437  0.02664  575 GLY A O   
4529 N N   . MET A 584 ? 1.04606 0.89627 0.61951 -0.29394 0.09446  0.02382  576 MET A N   
4530 C CA  . MET A 584 ? 1.10579 0.90391 0.64874 -0.29218 0.07952  0.03057  576 MET A CA  
4531 C C   . MET A 584 ? 1.12014 0.91538 0.67782 -0.26878 0.06911  0.02166  576 MET A C   
4532 O O   . MET A 584 ? 1.07399 0.86669 0.62344 -0.25035 0.07365  0.01563  576 MET A O   
4533 C CB  . MET A 584 ? 1.11659 0.87002 0.60727 -0.29362 0.08334  0.03885  576 MET A CB  
4534 C CG  . MET A 584 ? 1.08398 0.78557 0.54439 -0.29516 0.06975  0.04500  576 MET A CG  
4535 S SD  . MET A 584 ? 1.16967 0.81768 0.57402 -0.29251 0.07202  0.05324  576 MET A SD  
4536 C CE  . MET A 584 ? 1.02536 0.68379 0.43255 -0.26323 0.07666  0.04337  576 MET A CE  
4537 N N   . PHE A 585 ? 1.09305 0.88660 0.66921 -0.27118 0.05450  0.02209  577 PHE A N   
4538 C CA  . PHE A 585 ? 1.06381 0.86053 0.66062 -0.25316 0.04253  0.01545  577 PHE A CA  
4539 C C   . PHE A 585 ? 1.02351 0.77328 0.58456 -0.24903 0.03229  0.01999  577 PHE A C   
4540 O O   . PHE A 585 ? 0.99464 0.74333 0.56750 -0.23725 0.02165  0.01682  577 PHE A O   
4541 C CB  . PHE A 585 ? 1.08117 0.91098 0.72446 -0.25939 0.03212  0.01355  577 PHE A CB  
4542 C CG  . PHE A 585 ? 1.18503 1.00211 0.82221 -0.28182 0.02257  0.02277  577 PHE A CG  
4543 C CD1 . PHE A 585 ? 1.15600 0.93613 0.76852 -0.28465 0.00836  0.02770  577 PHE A CD1 
4544 C CD2 . PHE A 585 ? 1.18045 1.02386 0.83649 -0.30096 0.02791  0.02599  577 PHE A CD2 
4545 C CE1 . PHE A 585 ? 1.19287 0.95977 0.79762 -0.30578 -0.00136 0.03496  577 PHE A CE1 
4546 C CE2 . PHE A 585 ? 1.22532 1.05626 0.87613 -0.32270 0.01755  0.03454  577 PHE A CE2 
4547 C CZ  . PHE A 585 ? 1.24116 1.03247 0.86537 -0.32489 0.00237  0.03864  577 PHE A CZ  
4548 N N   . SER A 586 ? 1.04313 0.75568 0.56259 -0.25845 0.03524  0.02695  578 SER A N   
4549 C CA  . SER A 586 ? 1.01016 0.67742 0.49432 -0.25554 0.02711  0.02971  578 SER A CA  
4550 C C   . SER A 586 ? 1.01836 0.67755 0.49586 -0.23230 0.02777  0.02437  578 SER A C   
4551 O O   . SER A 586 ? 1.09370 0.73707 0.56490 -0.22639 0.01856  0.02341  578 SER A O   
4552 C CB  . SER A 586 ? 1.11096 0.74103 0.55557 -0.26828 0.03066  0.03670  578 SER A CB  
4553 O OG  . SER A 586 ? 1.15935 0.78600 0.60559 -0.29066 0.02418  0.04196  578 SER A OG  
4554 N N   . TRP A 587 ? 1.00710 0.67810 0.48575 -0.22072 0.03799  0.02112  579 TRP A N   
4555 C CA  . TRP A 587 ? 1.04529 0.71005 0.51872 -0.19924 0.03841  0.01631  579 TRP A CA  
4556 C C   . TRP A 587 ? 0.94428 0.64749 0.45129 -0.18751 0.04220  0.00832  579 TRP A C   
4557 O O   . TRP A 587 ? 1.03618 0.76122 0.55095 -0.19267 0.05225  0.00660  579 TRP A O   
4558 C CB  . TRP A 587 ? 1.05309 0.68662 0.48853 -0.19475 0.04508  0.01974  579 TRP A CB  
4559 C CG  . TRP A 587 ? 1.06470 0.65629 0.46672 -0.20223 0.04097  0.02530  579 TRP A CG  
4560 C CD1 . TRP A 587 ? 1.10396 0.66887 0.48948 -0.19268 0.03531  0.02375  579 TRP A CD1 
4561 C CD2 . TRP A 587 ? 1.04274 0.61338 0.42322 -0.22063 0.04254  0.03243  579 TRP A CD2 
4562 N NE1 . TRP A 587 ? 1.09865 0.62693 0.45425 -0.20238 0.03334  0.02764  579 TRP A NE1 
4563 C CE2 . TRP A 587 ? 1.09460 0.62357 0.44615 -0.21990 0.03664  0.03356  579 TRP A CE2 
4564 C CE3 . TRP A 587 ? 1.03650 0.62010 0.41980 -0.23831 0.04842  0.03783  579 TRP A CE3 
4565 C CZ2 . TRP A 587 ? 1.14558 0.64208 0.47103 -0.23558 0.03475  0.03949  579 TRP A CZ2 
4566 C CZ3 . TRP A 587 ? 1.09719 0.64999 0.45458 -0.25559 0.04659  0.04567  579 TRP A CZ3 
4567 C CH2 . TRP A 587 ? 1.09429 0.60223 0.42297 -0.25390 0.03901  0.04632  579 TRP A CH2 
4568 N N   . PHE A 588 ? 0.92445 0.63456 0.44916 -0.17289 0.03448  0.00345  580 PHE A N   
4569 C CA  . PHE A 588 ? 0.91847 0.65327 0.46706 -0.15669 0.03631  -0.00536 580 PHE A CA  
4570 C C   . PHE A 588 ? 0.94301 0.65649 0.46497 -0.14315 0.03957  -0.00569 580 PHE A C   
4571 O O   . PHE A 588 ? 0.93737 0.61966 0.43052 -0.14355 0.03771  0.00012  580 PHE A O   
4572 C CB  . PHE A 588 ? 0.93810 0.68807 0.52052 -0.14942 0.02320  -0.00879 580 PHE A CB  
4573 C CG  . PHE A 588 ? 0.91799 0.69599 0.53726 -0.15839 0.01756  -0.01030 580 PHE A CG  
4574 C CD1 . PHE A 588 ? 0.93898 0.74502 0.57620 -0.16471 0.02731  -0.01484 580 PHE A CD1 
4575 C CD2 . PHE A 588 ? 0.87477 0.65336 0.51257 -0.16033 0.00196  -0.00708 580 PHE A CD2 
4576 C CE1 . PHE A 588 ? 0.95353 0.78846 0.62967 -0.17181 0.02157  -0.01677 580 PHE A CE1 
4577 C CE2 . PHE A 588 ? 0.89400 0.69860 0.56857 -0.16775 -0.00558 -0.00792 580 PHE A CE2 
4578 C CZ  . PHE A 588 ? 0.92956 0.76297 0.62518 -0.17281 0.00419  -0.01318 580 PHE A CZ  
4579 N N   . PRO A 589 ? 0.89337 0.62303 0.42497 -0.13034 0.04380  -0.01327 581 PRO A N   
4580 C CA  . PRO A 589 ? 0.90172 0.61298 0.41077 -0.11748 0.04484  -0.01332 581 PRO A CA  
4581 C C   . PRO A 589 ? 0.96455 0.66368 0.47805 -0.10709 0.03395  -0.01235 581 PRO A C   
4582 O O   . PRO A 589 ? 0.90808 0.61916 0.44714 -0.10749 0.02525  -0.01355 581 PRO A O   
4583 C CB  . PRO A 589 ? 0.83905 0.57497 0.36198 -0.10788 0.05025  -0.02331 581 PRO A CB  
4584 C CG  . PRO A 589 ? 0.88287 0.65058 0.43226 -0.11699 0.05578  -0.02877 581 PRO A CG  
4585 C CD  . PRO A 589 ? 0.87831 0.64487 0.44315 -0.12720 0.04748  -0.02328 581 PRO A CD  
4586 N N   . ILE A 590 ? 0.95340 0.63014 0.44269 -0.09867 0.03430  -0.00953 582 ILE A N   
4587 C CA  . ILE A 590 ? 0.91103 0.57829 0.40265 -0.08844 0.02618  -0.00849 582 ILE A CA  
4588 C C   . ILE A 590 ? 0.89388 0.57485 0.39983 -0.07421 0.02374  -0.01482 582 ILE A C   
4589 O O   . ILE A 590 ? 0.84539 0.53352 0.34609 -0.07174 0.02998  -0.01907 582 ILE A O   
4590 C CB  . ILE A 590 ? 0.91928 0.55538 0.37876 -0.08770 0.02824  -0.00256 582 ILE A CB  
4591 C CG1 . ILE A 590 ? 0.91301 0.54203 0.37527 -0.08410 0.02164  -0.00071 582 ILE A CG1 
4592 C CG2 . ILE A 590 ? 0.93617 0.56181 0.37748 -0.07783 0.03228  -0.00256 582 ILE A CG2 
4593 C CD1 . ILE A 590 ? 0.99779 0.59796 0.43112 -0.08506 0.02458  0.00276  582 ILE A CD1 
4594 N N   . LEU A 591 ? 0.90883 0.59332 0.43114 -0.06666 0.01463  -0.01522 583 LEU A N   
4595 C CA  . LEU A 591 ? 0.84304 0.53833 0.38084 -0.05376 0.00947  -0.02093 583 LEU A CA  
4596 C C   . LEU A 591 ? 0.82437 0.50625 0.35370 -0.04644 0.00497  -0.01606 583 LEU A C   
4597 O O   . LEU A 591 ? 0.83655 0.51620 0.37222 -0.05002 -0.00045 -0.01128 583 LEU A O   
4598 C CB  . LEU A 591 ? 0.86433 0.58085 0.43859 -0.05302 0.00041  -0.02614 583 LEU A CB  
4599 C CG  . LEU A 591 ? 0.87256 0.59728 0.46571 -0.04086 -0.00815 -0.03187 583 LEU A CG  
4600 C CD1 . LEU A 591 ? 0.82750 0.55596 0.41068 -0.03302 -0.00171 -0.04028 583 LEU A CD1 
4601 C CD2 . LEU A 591 ? 0.82269 0.56432 0.45296 -0.04045 -0.01914 -0.03642 583 LEU A CD2 
4602 N N   . PHE A 592 ? 0.88785 0.56280 0.40362 -0.03723 0.00702  -0.01708 584 PHE A N   
4603 C CA  . PHE A 592 ? 0.90538 0.57363 0.41959 -0.02810 0.00224  -0.01395 584 PHE A CA  
4604 C C   . PHE A 592 ? 0.92309 0.60710 0.46186 -0.02033 -0.00692 -0.01925 584 PHE A C   
4605 O O   . PHE A 592 ? 0.93341 0.62095 0.46949 -0.01403 -0.00676 -0.02502 584 PHE A O   
4606 C CB  . PHE A 592 ? 0.83968 0.49048 0.32690 -0.02253 0.00750  -0.01142 584 PHE A CB  
4607 C CG  . PHE A 592 ? 0.93770 0.56805 0.40145 -0.02876 0.01420  -0.00616 584 PHE A CG  
4608 C CD1 . PHE A 592 ? 0.94486 0.56761 0.39261 -0.03801 0.02068  -0.00543 584 PHE A CD1 
4609 C CD2 . PHE A 592 ? 0.92811 0.54724 0.38626 -0.02585 0.01413  -0.00261 584 PHE A CD2 
4610 C CE1 . PHE A 592 ? 1.00748 0.60825 0.43359 -0.04439 0.02510  -0.00084 584 PHE A CE1 
4611 C CE2 . PHE A 592 ? 0.90840 0.50641 0.34470 -0.03075 0.01967  0.00008  584 PHE A CE2 
4612 C CZ  . PHE A 592 ? 0.96845 0.55555 0.38855 -0.04010 0.02422  0.00116  584 PHE A CZ  
4613 N N   . PRO A 593 ? 0.87912 0.57178 0.44107 -0.02154 -0.01604 -0.01733 585 PRO A N   
4614 C CA  . PRO A 593 ? 0.81189 0.51649 0.39854 -0.01510 -0.02689 -0.02200 585 PRO A CA  
4615 C C   . PRO A 593 ? 0.83800 0.53899 0.41976 -0.00594 -0.03005 -0.02083 585 PRO A C   
4616 O O   . PRO A 593 ? 0.82212 0.51239 0.38349 -0.00393 -0.02376 -0.01629 585 PRO A O   
4617 C CB  . PRO A 593 ? 0.82838 0.53870 0.43669 -0.02140 -0.03661 -0.01635 585 PRO A CB  
4618 C CG  . PRO A 593 ? 0.84294 0.54667 0.43748 -0.03195 -0.03006 -0.01049 585 PRO A CG  
4619 C CD  . PRO A 593 ? 0.85076 0.54065 0.41455 -0.03026 -0.01753 -0.01014 585 PRO A CD  
4620 N N   . ILE A 594 ? 0.89009 0.59961 0.49223 -0.00045 -0.04083 -0.02531 586 ILE A N   
4621 C CA  . ILE A 594 ? 0.85595 0.56536 0.46153 0.00652  -0.04775 -0.02294 586 ILE A CA  
4622 C C   . ILE A 594 ? 0.83425 0.55246 0.46978 0.00484  -0.06204 -0.02162 586 ILE A C   
4623 O O   . ILE A 594 ? 0.79064 0.51382 0.44371 0.00326  -0.06816 -0.02768 586 ILE A O   
4624 C CB  . ILE A 594 ? 0.89542 0.60239 0.48839 0.01498  -0.04742 -0.03050 586 ILE A CB  
4625 C CG1 . ILE A 594 ? 0.85556 0.56933 0.45523 0.01619  -0.04853 -0.04312 586 ILE A CG1 
4626 C CG2 . ILE A 594 ? 0.84164 0.53641 0.40403 0.01620  -0.03640 -0.02677 586 ILE A CG2 
4627 C CD1 . ILE A 594 ? 0.87853 0.59252 0.47125 0.02411  -0.05295 -0.05179 586 ILE A CD1 
4628 N N   . LYS A 595 ? 0.85959 0.58003 0.50191 0.00487  -0.06732 -0.01364 587 LYS A N   
4629 C CA  . LYS A 595 ? 0.85057 0.57825 0.51939 0.00015  -0.08120 -0.00824 587 LYS A CA  
4630 C C   . LYS A 595 ? 0.86886 0.59807 0.55700 0.00488  -0.09426 -0.01825 587 LYS A C   
4631 O O   . LYS A 595 ? 0.86744 0.59824 0.57588 0.00055  -0.10377 -0.01900 587 LYS A O   
4632 C CB  . LYS A 595 ? 0.83991 0.57271 0.51188 0.00077  -0.08338 0.00019  587 LYS A CB  
4633 C CG  . LYS A 595 ? 0.81624 0.55012 0.47424 -0.00353 -0.07150 0.00902  587 LYS A CG  
4634 C CD  . LYS A 595 ? 0.88843 0.63016 0.54967 0.00087  -0.07086 0.01390  587 LYS A CD  
4635 C CE  . LYS A 595 ? 0.89362 0.63884 0.54376 -0.00235 -0.05836 0.02043  587 LYS A CE  
4636 N NZ  . LYS A 595 ? 0.84544 0.60103 0.50737 -0.01522 -0.06162 0.02966  587 LYS A NZ  
4637 N N   . GLN A 596 ? 0.79386 0.52154 0.47511 0.01368  -0.09540 -0.02607 588 GLN A N   
4638 C CA  . GLN A 596 ? 0.83876 0.56676 0.53547 0.01934  -0.10844 -0.03742 588 GLN A CA  
4639 C C   . GLN A 596 ? 0.86397 0.59004 0.54332 0.02611  -0.10018 -0.05172 588 GLN A C   
4640 O O   . GLN A 596 ? 0.90393 0.62663 0.55776 0.02923  -0.09050 -0.05141 588 GLN A O   
4641 C CB  . GLN A 596 ? 0.85265 0.58178 0.55530 0.02201  -0.11867 -0.03372 588 GLN A CB  
4642 C CG  . GLN A 596 ? 0.86934 0.60359 0.59398 0.01361  -0.12867 -0.02052 588 GLN A CG  
4643 C CD  . GLN A 596 ? 0.90472 0.63687 0.65576 0.00947  -0.14412 -0.02296 588 GLN A CD  
4644 O OE1 . GLN A 596 ? 1.00505 0.73260 0.76448 0.01569  -0.15263 -0.03658 588 GLN A OE1 
4645 N NE2 . GLN A 596 ? 0.99827 0.73309 0.76211 -0.00112 -0.14842 -0.01002 588 GLN A NE2 
4646 N N   . PRO A 597 ? 0.80591 0.53466 0.49889 0.02842  -0.10387 -0.06464 589 PRO A N   
4647 C CA  . PRO A 597 ? 0.84666 0.57749 0.52379 0.03411  -0.09492 -0.07967 589 PRO A CA  
4648 C C   . PRO A 597 ? 0.86072 0.58758 0.52178 0.04058  -0.09885 -0.08564 589 PRO A C   
4649 O O   . PRO A 597 ? 0.92423 0.64856 0.59970 0.04240  -0.11355 -0.08464 589 PRO A O   
4650 C CB  . PRO A 597 ? 0.88284 0.61946 0.58679 0.03696  -0.10187 -0.09357 589 PRO A CB  
4651 C CG  . PRO A 597 ? 0.86947 0.60521 0.59991 0.03040  -0.11228 -0.08193 589 PRO A CG  
4652 C CD  . PRO A 597 ? 0.85853 0.58904 0.58353 0.02580  -0.11711 -0.06571 589 PRO A CD  
4653 N N   . ILE A 598 ? 0.86681 0.59282 0.49781 0.04247  -0.08668 -0.09028 590 ILE A N   
4654 C CA  . ILE A 598 ? 0.92533 0.64664 0.53446 0.04752  -0.09001 -0.09494 590 ILE A CA  
4655 C C   . ILE A 598 ? 0.95490 0.68137 0.55462 0.05138  -0.08609 -0.11465 590 ILE A C   
4656 O O   . ILE A 598 ? 0.92776 0.66008 0.51390 0.04851  -0.07083 -0.11853 590 ILE A O   
4657 C CB  . ILE A 598 ? 0.87906 0.59327 0.45815 0.04570  -0.08065 -0.08207 590 ILE A CB  
4658 C CG1 . ILE A 598 ? 0.80649 0.51795 0.39716 0.04374  -0.08441 -0.06569 590 ILE A CG1 
4659 C CG2 . ILE A 598 ? 0.95143 0.66044 0.50474 0.04999  -0.08426 -0.08652 590 ILE A CG2 
4660 C CD1 . ILE A 598 ? 0.90687 0.61028 0.47281 0.04303  -0.07454 -0.05409 590 ILE A CD1 
4661 N N   . THR A 599 ? 0.90400 0.62918 0.51116 0.05704  -0.09927 -0.12720 591 THR A N   
4662 C CA  . THR A 599 ? 0.91176 0.64180 0.50770 0.06184  -0.09651 -0.14893 591 THR A CA  
4663 C C   . THR A 599 ? 0.97588 0.70411 0.52803 0.05970  -0.08510 -0.14739 591 THR A C   
4664 O O   . THR A 599 ? 0.99598 0.71466 0.53163 0.05969  -0.09268 -0.13723 591 THR A O   
4665 C CB  . THR A 599 ? 0.86040 0.58541 0.47245 0.06795  -0.11578 -0.16174 591 THR A CB  
4666 O OG1 . THR A 599 ? 0.89073 0.61620 0.54303 0.06881  -0.12612 -0.16265 591 THR A OG1 
4667 C CG2 . THR A 599 ? 0.88833 0.61717 0.48414 0.07337  -0.11305 -0.18575 591 THR A CG2 
4668 N N   . VAL A 600 ? 0.91532 0.65316 0.45073 0.05722  -0.06814 -0.15603 592 VAL A N   
4669 C CA  . VAL A 600 ? 0.97976 0.71656 0.47070 0.05298  -0.05654 -0.15506 592 VAL A CA  
4670 C C   . VAL A 600 ? 0.98651 0.73408 0.46600 0.05621  -0.05221 -0.17926 592 VAL A C   
4671 O O   . VAL A 600 ? 0.98974 0.75312 0.48469 0.05681  -0.04107 -0.19271 592 VAL A O   
4672 C CB  . VAL A 600 ? 0.98907 0.72862 0.46640 0.04442  -0.03886 -0.14259 592 VAL A CB  
4673 C CG1 . VAL A 600 ? 1.00986 0.74568 0.44073 0.03819  -0.02884 -0.13865 592 VAL A CG1 
4674 C CG2 . VAL A 600 ? 0.97813 0.70728 0.46837 0.04214  -0.04264 -0.12207 592 VAL A CG2 
4675 N N   . ARG A 601 ? 1.01962 0.75983 0.47413 0.05842  -0.06120 -0.18523 593 ARG A N   
4676 C CA  . ARG A 601 ? 1.07921 0.82817 0.51456 0.06098  -0.05723 -0.20939 593 ARG A CA  
4677 C C   . ARG A 601 ? 1.02361 0.77950 0.41462 0.05181  -0.03809 -0.20679 593 ARG A C   
4678 O O   . ARG A 601 ? 1.06889 0.81355 0.43582 0.04488  -0.03680 -0.18512 593 ARG A O   
4679 C CB  . ARG A 601 ? 1.01288 0.74942 0.43863 0.06587  -0.07717 -0.21643 593 ARG A CB  
4680 C CG  . ARG A 601 ? 1.09757 0.83119 0.56525 0.07459  -0.09437 -0.22922 593 ARG A CG  
4681 C CD  . ARG A 601 ? 1.37557 1.10845 0.83169 0.08026  -0.10229 -0.25550 593 ARG A CD  
4682 N NE  . ARG A 601 ? 1.46450 1.18437 0.88711 0.07772  -0.11529 -0.25021 593 ARG A NE  
4683 C CZ  . ARG A 601 ? 1.58546 1.30268 0.98256 0.07977  -0.12142 -0.27017 593 ARG A CZ  
4684 N NH1 . ARG A 601 ? 1.53000 1.25736 0.93121 0.08542  -0.11409 -0.29887 593 ARG A NH1 
4685 N NH2 . ARG A 601 ? 1.61869 1.32349 0.98635 0.07643  -0.13530 -0.26207 593 ARG A NH2 
4686 N N   . GLU A 602 ? 1.07427 0.84830 0.45609 0.05173  -0.02405 -0.22849 594 GLU A N   
4687 C CA  . GLU A 602 ? 1.14774 0.93344 0.48761 0.04118  -0.00365 -0.22890 594 GLU A CA  
4688 C C   . GLU A 602 ? 1.17353 0.94123 0.46411 0.03429  -0.01088 -0.21384 594 GLU A C   
4689 O O   . GLU A 602 ? 1.14404 0.90096 0.42453 0.03955  -0.02746 -0.22086 594 GLU A O   
4690 C CB  . GLU A 602 ? 1.16990 0.97822 0.50777 0.04483  0.00827  -0.25981 594 GLU A CB  
4691 C CG  . GLU A 602 ? 1.27209 1.09597 0.56462 0.03266  0.02993  -0.26222 594 GLU A CG  
4692 C CD  . GLU A 602 ? 1.33794 1.16990 0.59973 0.03475  0.03197  -0.28748 594 GLU A CD  
4693 O OE1 . GLU A 602 ? 1.36371 1.17573 0.60129 0.03639  0.01427  -0.28538 594 GLU A OE1 
4694 O OE2 . GLU A 602 ? 1.42730 1.28651 0.69078 0.03494  0.05097  -0.31004 594 GLU A OE2 
4695 N N   . GLY A 603 ? 1.13162 0.89514 0.39357 0.02259  -0.00035 -0.19357 595 GLY A N   
4696 C CA  . GLY A 603 ? 1.13870 0.88369 0.35300 0.01489  -0.00722 -0.17613 595 GLY A CA  
4697 C C   . GLY A 603 ? 1.11671 0.83895 0.34109 0.01648  -0.02103 -0.15026 595 GLY A C   
4698 O O   . GLY A 603 ? 1.19617 0.90428 0.38750 0.00797  -0.02057 -0.13060 595 GLY A O   
4699 N N   . GLN A 604 ? 1.08031 0.79919 0.34867 0.02668  -0.03291 -0.15023 596 GLN A N   
4700 C CA  . GLN A 604 ? 1.05820 0.75908 0.34143 0.02994  -0.04602 -0.12861 596 GLN A CA  
4701 C C   . GLN A 604 ? 1.10289 0.79925 0.38378 0.02259  -0.03312 -0.11086 596 GLN A C   
4702 O O   . GLN A 604 ? 1.04824 0.75864 0.33081 0.01628  -0.01554 -0.11678 596 GLN A O   
4703 C CB  . GLN A 604 ? 1.02289 0.72616 0.35465 0.04000  -0.05812 -0.13395 596 GLN A CB  
4704 C CG  . GLN A 604 ? 1.03379 0.73580 0.37039 0.04704  -0.07565 -0.14791 596 GLN A CG  
4705 C CD  . GLN A 604 ? 1.07465 0.77540 0.45729 0.05444  -0.08992 -0.14680 596 GLN A CD  
4706 O OE1 . GLN A 604 ? 1.01918 0.72852 0.43521 0.05628  -0.08488 -0.15181 596 GLN A OE1 
4707 N NE2 . GLN A 604 ? 1.08139 0.77202 0.46652 0.05779  -0.10867 -0.13902 596 GLN A NE2 
4708 N N   . THR A 605 ? 1.04168 0.71953 0.32063 0.02375  -0.04215 -0.09074 597 THR A N   
4709 C CA  . THR A 605 ? 1.08246 0.75010 0.35899 0.01807  -0.03343 -0.07312 597 THR A CA  
4710 C C   . THR A 605 ? 0.99682 0.66420 0.31581 0.02502  -0.03754 -0.06876 597 THR A C   
4711 O O   . THR A 605 ? 0.98867 0.65216 0.32565 0.03367  -0.05261 -0.06700 597 THR A O   
4712 C CB  . THR A 605 ? 1.06250 0.70742 0.30440 0.01510  -0.04105 -0.05443 597 THR A CB  
4713 O OG1 . THR A 605 ? 1.15098 0.79673 0.35180 0.00792  -0.03976 -0.05861 597 THR A OG1 
4714 C CG2 . THR A 605 ? 1.06245 0.69374 0.29703 0.00843  -0.03221 -0.03806 597 THR A CG2 
4715 N N   . ILE A 606 ? 0.99831 0.67091 0.33198 0.02022  -0.02485 -0.06693 598 ILE A N   
4716 C CA  . ILE A 606 ? 1.04341 0.71230 0.40813 0.02370  -0.02684 -0.05887 598 ILE A CA  
4717 C C   . ILE A 606 ? 0.99309 0.64028 0.33851 0.02201  -0.02759 -0.04058 598 ILE A C   
4718 O O   . ILE A 606 ? 0.97337 0.61308 0.29469 0.01265  -0.01710 -0.03424 598 ILE A O   
4719 C CB  . ILE A 606 ? 0.95529 0.63836 0.34240 0.01868  -0.01474 -0.06516 598 ILE A CB  
4720 C CG1 . ILE A 606 ? 0.92035 0.62307 0.33334 0.02315  -0.01696 -0.08373 598 ILE A CG1 
4721 C CG2 . ILE A 606 ? 0.89917 0.57536 0.30748 0.01919  -0.01545 -0.05457 598 ILE A CG2 
4722 C CD1 . ILE A 606 ? 0.93017 0.64915 0.36339 0.01828  -0.00535 -0.09139 598 ILE A CD1 
4723 N N   . CYS A 607 ? 0.94889 0.58675 0.30525 0.03068  -0.04000 -0.03285 599 CYS A N   
4724 C CA  . CYS A 607 ? 0.96511 0.58271 0.31201 0.03263  -0.04215 -0.01734 599 CYS A CA  
4725 C C   . CYS A 607 ? 1.01425 0.63426 0.39095 0.03520  -0.03873 -0.01489 599 CYS A C   
4726 O O   . CYS A 607 ? 0.97008 0.60018 0.37505 0.04232  -0.04665 -0.01749 599 CYS A O   
4727 C CB  . CYS A 607 ? 0.97149 0.57980 0.31287 0.04147  -0.05803 -0.01103 599 CYS A CB  
4728 S SG  . CYS A 607 ? 1.00007 0.58389 0.33486 0.04686  -0.06180 0.00582  599 CYS A SG  
4729 N N   . VAL A 608 ? 0.97618 0.58754 0.34553 0.02825  -0.02768 -0.00996 600 VAL A N   
4730 C CA  . VAL A 608 ? 0.99427 0.60574 0.38551 0.02878  -0.02336 -0.00755 600 VAL A CA  
4731 C C   . VAL A 608 ? 1.00281 0.59120 0.38084 0.03223  -0.02403 0.00343  600 VAL A C   
4732 O O   . VAL A 608 ? 0.96637 0.53656 0.31519 0.02895  -0.02388 0.01001  600 VAL A O   
4733 C CB  . VAL A 608 ? 0.94926 0.56917 0.34543 0.01816  -0.01167 -0.01215 600 VAL A CB  
4734 C CG1 . VAL A 608 ? 0.95309 0.55785 0.32029 0.00795  -0.00246 -0.00615 600 VAL A CG1 
4735 C CG2 . VAL A 608 ? 0.92941 0.55465 0.35132 0.01850  -0.01028 -0.01186 600 VAL A CG2 
4736 N N   . ARG A 609 ? 0.98755 0.57693 0.38652 0.03841  -0.02494 0.00500  601 ARG A N   
4737 C CA  . ARG A 609 ? 0.97641 0.54611 0.36962 0.04431  -0.02496 0.01224  601 ARG A CA  
4738 C C   . ARG A 609 ? 0.98787 0.55591 0.38781 0.03860  -0.01485 0.01090  601 ARG A C   
4739 O O   . ARG A 609 ? 1.05800 0.64511 0.48134 0.03734  -0.01325 0.00625  601 ARG A O   
4740 C CB  . ARG A 609 ? 0.97256 0.54927 0.38671 0.05777  -0.03442 0.01343  601 ARG A CB  
4741 C CG  . ARG A 609 ? 1.06806 0.65304 0.48320 0.06266  -0.04660 0.01298  601 ARG A CG  
4742 C CD  . ARG A 609 ? 1.06124 0.62477 0.45057 0.06662  -0.05444 0.02070  601 ARG A CD  
4743 N NE  . ARG A 609 ? 1.06486 0.63682 0.45451 0.07078  -0.06753 0.02008  601 ARG A NE  
4744 C CZ  . ARG A 609 ? 1.05654 0.61534 0.43315 0.07727  -0.07988 0.02736  601 ARG A CZ  
4745 N NH1 . ARG A 609 ? 1.09666 0.63177 0.46014 0.08141  -0.08130 0.03610  601 ARG A NH1 
4746 N NH2 . ARG A 609 ? 1.09993 0.66792 0.47680 0.07961  -0.09235 0.02578  601 ARG A NH2 
4747 N N   . PHE A 610 ? 0.98476 0.52942 0.36404 0.03448  -0.00967 0.01529  602 PHE A N   
4748 C CA  . PHE A 610 ? 1.01788 0.55656 0.39875 0.02843  -0.00104 0.01384  602 PHE A CA  
4749 C C   . PHE A 610 ? 1.07872 0.59337 0.45161 0.03684  -0.00157 0.01684  602 PHE A C   
4750 O O   . PHE A 610 ? 1.12602 0.61688 0.47834 0.03921  -0.00592 0.02272  602 PHE A O   
4751 C CB  . PHE A 610 ? 1.01184 0.54585 0.37657 0.01291  0.00602  0.01423  602 PHE A CB  
4752 C CG  . PHE A 610 ? 1.00286 0.56218 0.38657 0.00505  0.00977  0.00817  602 PHE A CG  
4753 C CD1 . PHE A 610 ? 1.00383 0.58464 0.39998 0.00626  0.00635  0.00359  602 PHE A CD1 
4754 C CD2 . PHE A 610 ? 1.01995 0.58038 0.40944 -0.00318 0.01527  0.00661  602 PHE A CD2 
4755 C CE1 . PHE A 610 ? 0.96631 0.56852 0.38271 0.00049  0.00809  -0.00241 602 PHE A CE1 
4756 C CE2 . PHE A 610 ? 0.99113 0.57387 0.40000 -0.00992 0.01634  0.00208  602 PHE A CE2 
4757 C CZ  . PHE A 610 ? 0.95531 0.55861 0.37892 -0.00750 0.01259  -0.00244 602 PHE A CZ  
4758 N N   . TRP A 611 ? 1.04213 0.56322 0.43104 0.04122  0.00235  0.01266  603 TRP A N   
4759 C CA  . TRP A 611 ? 1.03222 0.53307 0.41634 0.04920  0.00475  0.01156  603 TRP A CA  
4760 C C   . TRP A 611 ? 1.04223 0.53402 0.41671 0.03785  0.01363  0.00812  603 TRP A C   
4761 O O   . TRP A 611 ? 0.97481 0.48710 0.36016 0.02870  0.01751  0.00550  603 TRP A O   
4762 C CB  . TRP A 611 ? 1.03599 0.55498 0.44585 0.06297  0.00374  0.00791  603 TRP A CB  
4763 C CG  . TRP A 611 ? 1.06714 0.59495 0.48922 0.07485  -0.00650 0.01123  603 TRP A CG  
4764 C CD1 . TRP A 611 ? 1.06737 0.58093 0.48969 0.08908  -0.01323 0.01357  603 TRP A CD1 
4765 C CD2 . TRP A 611 ? 1.02797 0.58095 0.46579 0.07384  -0.01274 0.01213  603 TRP A CD2 
4766 N NE1 . TRP A 611 ? 1.01262 0.54187 0.44910 0.09611  -0.02350 0.01670  603 TRP A NE1 
4767 C CE2 . TRP A 611 ? 1.02765 0.58043 0.47273 0.08669  -0.02322 0.01544  603 TRP A CE2 
4768 C CE3 . TRP A 611 ? 0.99573 0.56981 0.44293 0.06372  -0.01185 0.01007  603 TRP A CE3 
4769 C CZ2 . TRP A 611 ? 1.04576 0.61851 0.50499 0.08850  -0.03249 0.01648  603 TRP A CZ2 
4770 C CZ3 . TRP A 611 ? 0.95402 0.54631 0.41573 0.06649  -0.02075 0.01031  603 TRP A CZ3 
4771 C CH2 . TRP A 611 ? 0.99721 0.58874 0.46382 0.07818  -0.03080 0.01335  603 TRP A CH2 
4772 N N   . ARG A 612 ? 1.11513 0.57578 0.47001 0.03823  0.01507  0.00833  604 ARG A N   
4773 C CA  . ARG A 612 ? 1.08942 0.53821 0.43608 0.03159  0.02245  0.00281  604 ARG A CA  
4774 C C   . ARG A 612 ? 1.08645 0.53134 0.44215 0.04732  0.02469  -0.00411 604 ARG A C   
4775 O O   . ARG A 612 ? 1.09201 0.51553 0.44292 0.05983  0.01965  -0.00313 604 ARG A O   
4776 C CB  . ARG A 612 ? 1.10185 0.51765 0.42089 0.02043  0.02206  0.00652  604 ARG A CB  
4777 C CG  . ARG A 612 ? 1.07676 0.48488 0.38665 0.00781  0.02837  0.00159  604 ARG A CG  
4778 C CD  . ARG A 612 ? 1.10911 0.48653 0.39356 -0.00562 0.02676  0.00657  604 ARG A CD  
4779 N NE  . ARG A 612 ? 1.12200 0.49424 0.39829 -0.02031 0.03114  0.00264  604 ARG A NE  
4780 C CZ  . ARG A 612 ? 1.15090 0.49847 0.41452 -0.01967 0.03280  -0.00427 604 ARG A CZ  
4781 N NH1 . ARG A 612 ? 1.14921 0.47508 0.40909 -0.00337 0.03134  -0.00917 604 ARG A NH1 
4782 N NH2 . ARG A 612 ? 1.16323 0.50799 0.41860 -0.03506 0.03534  -0.00712 604 ARG A NH2 
4783 N N   . CYS A 613 ? 1.08484 0.55187 0.45463 0.04682  0.03152  -0.01049 605 CYS A N   
4784 C CA  . CYS A 613 ? 1.10738 0.58045 0.48922 0.06073  0.03676  -0.01877 605 CYS A CA  
4785 C C   . CYS A 613 ? 1.05750 0.51777 0.42385 0.05369  0.04550  -0.02729 605 CYS A C   
4786 O O   . CYS A 613 ? 1.02773 0.48745 0.38254 0.03652  0.04687  -0.02545 605 CYS A O   
4787 C CB  . CYS A 613 ? 1.03913 0.55197 0.44906 0.06407  0.03800  -0.01853 605 CYS A CB  
4788 S SG  . CYS A 613 ? 0.98550 0.51465 0.41312 0.07031  0.02638  -0.00975 605 CYS A SG  
4789 N N   . SER A 614 ? 1.03474 0.48562 0.40140 0.06675  0.05082  -0.03713 606 SER A N   
4790 C CA  . SER A 614 ? 1.12838 0.56508 0.47766 0.06174  0.05949  -0.04800 606 SER A CA  
4791 C C   . SER A 614 ? 1.17244 0.61426 0.53237 0.07977  0.06752  -0.06083 606 SER A C   
4792 O O   . SER A 614 ? 1.21044 0.65083 0.58628 0.09802  0.06352  -0.06111 606 SER A O   
4793 C CB  . SER A 614 ? 1.12592 0.51991 0.44708 0.05433  0.05525  -0.04786 606 SER A CB  
4794 O OG  . SER A 614 ? 1.13372 0.49775 0.45166 0.07066  0.05037  -0.05059 606 SER A OG  
4795 N N   . ASN A 615 ? 1.08131 0.53039 0.43278 0.07424  0.07832  -0.07121 607 ASN A N   
4796 C CA  . ASN A 615 ? 1.15189 0.59540 0.50235 0.08871  0.08848  -0.08806 607 ASN A CA  
4797 C C   . ASN A 615 ? 1.25126 0.65995 0.56806 0.07816  0.09102  -0.09718 607 ASN A C   
4798 O O   . ASN A 615 ? 1.22304 0.60888 0.52211 0.06347  0.08253  -0.08845 607 ASN A O   
4799 C CB  . ASN A 615 ? 1.17468 0.66344 0.54594 0.09168  0.10014  -0.09289 607 ASN A CB  
4800 C CG  . ASN A 615 ? 1.17321 0.68547 0.53659 0.06940  0.10387  -0.08732 607 ASN A CG  
4801 O OD1 . ASN A 615 ? 1.18777 0.68095 0.52473 0.05381  0.10337  -0.08836 607 ASN A OD1 
4802 N ND2 . ASN A 615 ? 1.11838 0.67150 0.50534 0.06721  0.10619  -0.08073 607 ASN A ND2 
4803 N N   . SER A 616 ? 1.23373 0.63938 0.54208 0.08476  0.10233  -0.11458 608 SER A N   
4804 C CA  . SER A 616 ? 1.25049 0.62157 0.52539 0.07602  0.10489  -0.12652 608 SER A CA  
4805 C C   . SER A 616 ? 1.25797 0.63968 0.51437 0.04944  0.10530  -0.12014 608 SER A C   
4806 O O   . SER A 616 ? 1.27276 0.62216 0.50119 0.03701  0.10156  -0.12360 608 SER A O   
4807 C CB  . SER A 616 ? 1.30562 0.67648 0.57850 0.09139  0.11804  -0.14853 608 SER A CB  
4808 O OG  . SER A 616 ? 1.32468 0.74431 0.61398 0.09146  0.13090  -0.15115 608 SER A OG  
4809 N N   . LYS A 617 ? 1.24715 0.67106 0.51957 0.04081  0.10801  -0.11063 609 LYS A N   
4810 C CA  . LYS A 617 ? 1.23378 0.67378 0.49255 0.01720  0.10869  -0.10529 609 LYS A CA  
4811 C C   . LYS A 617 ? 1.23223 0.67991 0.50008 0.00283  0.09647  -0.08642 609 LYS A C   
4812 O O   . LYS A 617 ? 1.18842 0.62777 0.43877 -0.01653 0.09167  -0.08245 609 LYS A O   
4813 C CB  . LYS A 617 ? 1.20008 0.68202 0.47002 0.01692  0.12027  -0.10840 609 LYS A CB  
4814 C CG  . LYS A 617 ? 1.27060 0.75111 0.52859 0.02758  0.13526  -0.12910 609 LYS A CG  
4815 C CD  . LYS A 617 ? 1.25975 0.78678 0.53504 0.02993  0.14796  -0.13090 609 LYS A CD  
4816 C CE  . LYS A 617 ? 1.30666 0.83646 0.57567 0.04458  0.16487  -0.15340 609 LYS A CE  
4817 N NZ  . LYS A 617 ? 1.29780 0.87773 0.58408 0.04398  0.17840  -0.15365 609 LYS A NZ  
4818 N N   . LYS A 618 ? 1.20959 0.67379 0.50421 0.01186  0.09151  -0.07623 610 LYS A N   
4819 C CA  . LYS A 618 ? 1.10129 0.57993 0.40912 0.00058  0.08152  -0.06032 610 LYS A CA  
4820 C C   . LYS A 618 ? 1.17292 0.63349 0.48684 0.00897  0.07325  -0.05391 610 LYS A C   
4821 O O   . LYS A 618 ? 1.18220 0.63212 0.50187 0.02698  0.07425  -0.05848 610 LYS A O   
4822 C CB  . LYS A 618 ? 1.03785 0.55819 0.37256 0.00151  0.08252  -0.05347 610 LYS A CB  
4823 C CG  . LYS A 618 ? 1.14780 0.69164 0.47836 -0.00976 0.08932  -0.05551 610 LYS A CG  
4824 C CD  . LYS A 618 ? 1.27055 0.80522 0.57982 -0.03126 0.08489  -0.05248 610 LYS A CD  
4825 C CE  . LYS A 618 ? 1.21765 0.77799 0.52360 -0.04471 0.08852  -0.05043 610 LYS A CE  
4826 N NZ  . LYS A 618 ? 1.12875 0.67329 0.40654 -0.06335 0.08557  -0.05178 610 LYS A NZ  
4827 N N   . VAL A 619 ? 1.11719 0.57635 0.43055 -0.00401 0.06521  -0.04355 611 VAL A N   
4828 C CA  . VAL A 619 ? 1.09571 0.54892 0.41692 -0.00005 0.05752  -0.03467 611 VAL A CA  
4829 C C   . VAL A 619 ? 1.07324 0.55891 0.41542 -0.00728 0.05312  -0.02559 611 VAL A C   
4830 O O   . VAL A 619 ? 1.10370 0.60144 0.44558 -0.02209 0.05241  -0.02359 611 VAL A O   
4831 C CB  . VAL A 619 ? 1.12187 0.54128 0.42061 -0.00999 0.05317  -0.03238 611 VAL A CB  
4832 C CG1 . VAL A 619 ? 1.05921 0.47780 0.36335 -0.01068 0.04644  -0.02210 611 VAL A CG1 
4833 C CG2 . VAL A 619 ? 1.14408 0.52676 0.42323 -0.00146 0.05514  -0.04140 611 VAL A CG2 
4834 N N   . TRP A 620 ? 1.00316 0.50125 0.36290 0.00286  0.04899  -0.02065 612 TRP A N   
4835 C CA  . TRP A 620 ? 1.02185 0.54887 0.40284 -0.00183 0.04380  -0.01380 612 TRP A CA  
4836 C C   . TRP A 620 ? 0.97061 0.49616 0.35790 0.00610  0.03782  -0.00902 612 TRP A C   
4837 O O   . TRP A 620 ? 1.01297 0.52015 0.39283 0.01780  0.03724  -0.00993 612 TRP A O   
4838 C CB  . TRP A 620 ? 0.99301 0.54928 0.39399 0.00145  0.04584  -0.01450 612 TRP A CB  
4839 C CG  . TRP A 620 ? 0.96619 0.52989 0.38024 0.01889  0.04776  -0.01703 612 TRP A CG  
4840 C CD1 . TRP A 620 ? 0.91783 0.49903 0.35332 0.02749  0.04191  -0.01278 612 TRP A CD1 
4841 C CD2 . TRP A 620 ? 1.00275 0.55849 0.41169 0.03018  0.05565  -0.02529 612 TRP A CD2 
4842 N NE1 . TRP A 620 ? 0.93781 0.52358 0.38332 0.04278  0.04493  -0.01652 612 TRP A NE1 
4843 C CE2 . TRP A 620 ? 0.95973 0.53108 0.39060 0.04557  0.05395  -0.02470 612 TRP A CE2 
4844 C CE3 . TRP A 620 ? 1.03230 0.56945 0.42104 0.02924  0.06367  -0.03424 612 TRP A CE3 
4845 C CZ2 . TRP A 620 ? 0.94549 0.51668 0.38178 0.06077  0.06051  -0.03264 612 TRP A CZ2 
4846 C CZ3 . TRP A 620 ? 1.03218 0.56740 0.42411 0.04473  0.07076  -0.04345 612 TRP A CZ3 
4847 C CH2 . TRP A 620 ? 0.98525 0.53852 0.40225 0.06071  0.06948  -0.04260 612 TRP A CH2 
4848 N N   . TYR A 621 ? 0.94884 0.49229 0.34870 -0.00023 0.03285  -0.00451 613 TYR A N   
4849 C CA  . TYR A 621 ? 0.94974 0.49805 0.35650 0.00609  0.02705  -0.00101 613 TYR A CA  
4850 C C   . TYR A 621 ? 0.93821 0.51327 0.37073 0.01397  0.02283  -0.00059 613 TYR A C   
4851 O O   . TYR A 621 ? 0.91786 0.51233 0.36520 0.00790  0.02259  -0.00060 613 TYR A O   
4852 C CB  . TYR A 621 ? 0.90514 0.45669 0.30913 -0.00586 0.02515  0.00134  613 TYR A CB  
4853 C CG  . TYR A 621 ? 0.96148 0.49000 0.34254 -0.01657 0.02866  0.00235  613 TYR A CG  
4854 C CD1 . TYR A 621 ? 0.95238 0.45613 0.31319 -0.01392 0.02845  0.00518  613 TYR A CD1 
4855 C CD2 . TYR A 621 ? 0.97858 0.50973 0.35855 -0.03061 0.03061  0.00161  613 TYR A CD2 
4856 C CE1 . TYR A 621 ? 1.00552 0.48729 0.34554 -0.02568 0.03073  0.00731  613 TYR A CE1 
4857 C CE2 . TYR A 621 ? 0.94925 0.46022 0.30973 -0.04196 0.03288  0.00295  613 TYR A CE2 
4858 C CZ  . TYR A 621 ? 0.96872 0.45480 0.30918 -0.03988 0.03326  0.00585  613 TYR A CZ  
4859 O OH  . TYR A 621 ? 1.05002 0.51540 0.37151 -0.05283 0.03465  0.00831  613 TYR A OH  
4860 N N   . GLU A 622 ? 0.95361 0.52835 0.39072 0.02622  0.01827  0.00068  614 GLU A N   
4861 C CA  . GLU A 622 ? 0.96124 0.55958 0.42198 0.03260  0.01136  0.00187  614 GLU A CA  
4862 C C   . GLU A 622 ? 0.87924 0.47519 0.33482 0.03270  0.00490  0.00344  614 GLU A C   
4863 O O   . GLU A 622 ? 0.95664 0.53125 0.39013 0.03231  0.00599  0.00505  614 GLU A O   
4864 C CB  . GLU A 622 ? 0.95330 0.55557 0.42491 0.04690  0.01066  0.00148  614 GLU A CB  
4865 C CG  . GLU A 622 ? 0.93522 0.53653 0.40622 0.04848  0.01978  -0.00226 614 GLU A CG  
4866 C CD  . GLU A 622 ? 0.99129 0.60607 0.48093 0.06242  0.02045  -0.00387 614 GLU A CD  
4867 O OE1 . GLU A 622 ? 1.01244 0.64701 0.52310 0.06683  0.01314  -0.00077 614 GLU A OE1 
4868 O OE2 . GLU A 622 ? 1.02027 0.62636 0.50458 0.06904  0.02811  -0.00900 614 GLU A OE2 
4869 N N   . TRP A 623 ? 0.89309 0.50913 0.36676 0.03237  -0.00177 0.00282  615 TRP A N   
4870 C CA  . TRP A 623 ? 0.90877 0.52529 0.37697 0.03229  -0.00732 0.00192  615 TRP A CA  
4871 C C   . TRP A 623 ? 0.89828 0.53464 0.38908 0.03743  -0.01704 0.00034  615 TRP A C   
4872 O O   . TRP A 623 ? 0.89214 0.54453 0.40503 0.03583  -0.01905 0.00037  615 TRP A O   
4873 C CB  . TRP A 623 ? 0.87964 0.49612 0.34005 0.02021  -0.00290 -0.00056 615 TRP A CB  
4874 C CG  . TRP A 623 ? 0.92989 0.56442 0.41189 0.01319  -0.00390 -0.00308 615 TRP A CG  
4875 C CD1 . TRP A 623 ? 0.87561 0.52730 0.37676 0.01249  -0.01052 -0.00710 615 TRP A CD1 
4876 C CD2 . TRP A 623 ? 0.96251 0.59783 0.44846 0.00561  0.00029  -0.00158 615 TRP A CD2 
4877 N NE1 . TRP A 623 ? 0.88325 0.54552 0.40156 0.00523  -0.01173 -0.00702 615 TRP A NE1 
4878 C CE2 . TRP A 623 ? 0.90633 0.55960 0.41462 0.00021  -0.00519 -0.00312 615 TRP A CE2 
4879 C CE3 . TRP A 623 ? 0.93452 0.55589 0.40629 0.00273  0.00722  0.00042  615 TRP A CE3 
4880 C CZ2 . TRP A 623 ? 0.87299 0.53108 0.38884 -0.00883 -0.00470 -0.00085 615 TRP A CZ2 
4881 C CZ3 . TRP A 623 ? 0.91818 0.54512 0.39568 -0.00636 0.00894  0.00110  615 TRP A CZ3 
4882 C CH2 . TRP A 623 ? 0.89975 0.54510 0.39856 -0.01252 0.00271  0.00139  615 TRP A CH2 
4883 N N   . ALA A 624 ? 0.93705 0.57111 0.42052 0.04219  -0.02358 -0.00049 616 ALA A N   
4884 C CA  . ALA A 624 ? 0.89301 0.54243 0.39391 0.04660  -0.03461 -0.00318 616 ALA A CA  
4885 C C   . ALA A 624 ? 0.93164 0.57682 0.41512 0.04556  -0.03777 -0.00736 616 ALA A C   
4886 O O   . ALA A 624 ? 0.97261 0.60131 0.42936 0.04463  -0.03369 -0.00452 616 ALA A O   
4887 C CB  . ALA A 624 ? 0.86397 0.51635 0.37585 0.05697  -0.04134 0.00104  616 ALA A CB  
4888 N N   . VAL A 625 ? 0.92377 0.58279 0.42119 0.04504  -0.04491 -0.01410 617 VAL A N   
4889 C CA  . VAL A 625 ? 0.87422 0.53295 0.35718 0.04581  -0.04971 -0.02047 617 VAL A CA  
4890 C C   . VAL A 625 ? 0.89581 0.55498 0.38248 0.05440  -0.06292 -0.01803 617 VAL A C   
4891 O O   . VAL A 625 ? 0.83116 0.50119 0.34458 0.05764  -0.07001 -0.01646 617 VAL A O   
4892 C CB  . VAL A 625 ? 0.89131 0.56403 0.38928 0.04169  -0.05064 -0.03155 617 VAL A CB  
4893 C CG1 . VAL A 625 ? 0.93006 0.60412 0.41213 0.04270  -0.05392 -0.04093 617 VAL A CG1 
4894 C CG2 . VAL A 625 ? 0.90180 0.57660 0.40163 0.03349  -0.03921 -0.03295 617 VAL A CG2 
4895 N N   . THR A 626 ? 0.99056 0.63865 0.45118 0.05682  -0.06662 -0.01645 618 THR A N   
4896 C CA  . THR A 626 ? 0.95851 0.60536 0.41937 0.06466  -0.08116 -0.01321 618 THR A CA  
4897 C C   . THR A 626 ? 0.99650 0.64516 0.44164 0.06321  -0.08891 -0.02173 618 THR A C   
4898 O O   . THR A 626 ? 1.09608 0.74482 0.54188 0.06855  -0.10319 -0.02023 618 THR A O   
4899 C CB  . THR A 626 ? 0.99544 0.62484 0.43852 0.06971  -0.08202 -0.00216 618 THR A CB  
4900 O OG1 . THR A 626 ? 1.02141 0.63504 0.43287 0.06291  -0.07187 -0.00012 618 THR A OG1 
4901 C CG2 . THR A 626 ? 0.99733 0.62842 0.46249 0.07533  -0.07889 0.00397  618 THR A CG2 
4902 N N   . ALA A 627 ? 0.99640 0.64764 0.42833 0.05634  -0.08001 -0.03100 619 ALA A N   
4903 C CA  . ALA A 627 ? 1.01293 0.66831 0.42928 0.05468  -0.08455 -0.04274 619 ALA A CA  
4904 C C   . ALA A 627 ? 1.00443 0.67119 0.42714 0.04922  -0.07333 -0.05571 619 ALA A C   
4905 O O   . ALA A 627 ? 0.93240 0.59898 0.35449 0.04398  -0.06005 -0.05290 619 ALA A O   
4906 C CB  . ALA A 627 ? 0.96031 0.60184 0.33564 0.05223  -0.08478 -0.03742 619 ALA A CB  
4907 N N   . PRO A 628 ? 0.99856 0.67540 0.42894 0.05061  -0.07896 -0.07099 620 PRO A N   
4908 C CA  . PRO A 628 ? 1.00955 0.68541 0.43868 0.05562  -0.09583 -0.07561 620 PRO A CA  
4909 C C   . PRO A 628 ? 1.05248 0.73168 0.51703 0.06069  -0.11015 -0.07029 620 PRO A C   
4910 O O   . PRO A 628 ? 1.10204 0.77967 0.56678 0.06422  -0.12550 -0.07071 620 PRO A O   
4911 C CB  . PRO A 628 ? 1.00110 0.68647 0.42990 0.05508  -0.09480 -0.09621 620 PRO A CB  
4912 C CG  . PRO A 628 ? 0.98490 0.68009 0.43896 0.05294  -0.08331 -0.10089 620 PRO A CG  
4913 C CD  . PRO A 628 ? 0.98920 0.67868 0.43171 0.04788  -0.07015 -0.08570 620 PRO A CD  
4914 N N   . VAL A 629 ? 1.01846 0.70311 0.51104 0.05965  -0.10513 -0.06525 621 VAL A N   
4915 C CA  . VAL A 629 ? 0.96879 0.65921 0.49528 0.06191  -0.11532 -0.05754 621 VAL A CA  
4916 C C   . VAL A 629 ? 1.03245 0.72064 0.56188 0.06122  -0.10522 -0.04342 621 VAL A C   
4917 O O   . VAL A 629 ? 1.03601 0.71869 0.54863 0.05767  -0.09097 -0.04225 621 VAL A O   
4918 C CB  . VAL A 629 ? 0.93820 0.63762 0.49563 0.05986  -0.12020 -0.06645 621 VAL A CB  
4919 C CG1 . VAL A 629 ? 0.94272 0.64913 0.53281 0.05829  -0.12589 -0.05571 621 VAL A CG1 
4920 C CG2 . VAL A 629 ? 1.08003 0.77964 0.63853 0.06226  -0.13380 -0.08098 621 VAL A CG2 
4921 N N   . CYS A 630 ? 0.97815 0.67130 0.52831 0.06417  -0.11215 -0.03385 622 CYS A N   
4922 C CA  . CYS A 630 ? 0.89040 0.58421 0.44834 0.06430  -0.10279 -0.02274 622 CYS A CA  
4923 C C   . CYS A 630 ? 0.89926 0.60251 0.48084 0.05801  -0.09805 -0.02300 622 CYS A C   
4924 O O   . CYS A 630 ? 0.86123 0.57453 0.46799 0.05605  -0.10873 -0.02483 622 CYS A O   
4925 C CB  . CYS A 630 ? 0.88177 0.58110 0.45424 0.07049  -0.11107 -0.01374 622 CYS A CB  
4926 S SG  . CYS A 630 ? 1.06046 0.74393 0.60496 0.07836  -0.10981 -0.00652 622 CYS A SG  
4927 N N   . SER A 631 ? 0.93408 0.63269 0.50672 0.05403  -0.08408 -0.02064 623 SER A N   
4928 C CA  . SER A 631 ? 0.84271 0.54867 0.43391 0.04754  -0.07887 -0.01714 623 SER A CA  
4929 C C   . SER A 631 ? 0.81657 0.52692 0.41580 0.04962  -0.07540 -0.00727 623 SER A C   
4930 O O   . SER A 631 ? 0.85258 0.55783 0.44180 0.05713  -0.07547 -0.00412 623 SER A O   
4931 C CB  . SER A 631 ? 0.82939 0.52861 0.40624 0.04184  -0.06663 -0.01975 623 SER A CB  
4932 O OG  . SER A 631 ? 0.83998 0.52757 0.39483 0.04304  -0.05585 -0.01445 623 SER A OG  
4933 N N   . ALA A 632 ? 0.89819 0.61811 0.51478 0.04320  -0.07267 -0.00278 624 ALA A N   
4934 C CA  . ALA A 632 ? 0.83521 0.56073 0.45608 0.04366  -0.06462 0.00464  624 ALA A CA  
4935 C C   . ALA A 632 ? 0.84172 0.55122 0.43626 0.04484  -0.05097 0.00405  624 ALA A C   
4936 O O   . ALA A 632 ? 0.82948 0.52867 0.40895 0.04040  -0.04735 -0.00007 624 ALA A O   
4937 C CB  . ALA A 632 ? 0.75753 0.49669 0.39852 0.03380  -0.06513 0.00945  624 ALA A CB  
4938 N N   . ILE A 633 ? 0.81022 0.51784 0.40071 0.05088  -0.04412 0.00739  625 ILE A N   
4939 C CA  . ILE A 633 ? 0.86311 0.55403 0.43077 0.05091  -0.03147 0.00693  625 ILE A CA  
4940 C C   . ILE A 633 ? 0.86772 0.56334 0.43757 0.03931  -0.02462 0.00757  625 ILE A C   
4941 O O   . ILE A 633 ? 0.78520 0.49772 0.37310 0.03572  -0.02461 0.01091  625 ILE A O   
4942 C CB  . ILE A 633 ? 0.84039 0.52834 0.40729 0.06197  -0.02727 0.00860  625 ILE A CB  
4943 C CG1 . ILE A 633 ? 0.90005 0.58084 0.46325 0.07281  -0.03670 0.00935  625 ILE A CG1 
4944 C CG2 . ILE A 633 ? 0.90416 0.57361 0.44946 0.06132  -0.01507 0.00700  625 ILE A CG2 
4945 C CD1 . ILE A 633 ? 0.95630 0.64151 0.53123 0.08543  -0.03698 0.01129  625 ILE A CD1 
4946 N N   . HIS A 634 ? 0.83499 0.51755 0.38758 0.03245  -0.02003 0.00519  626 HIS A N   
4947 C CA  . HIS A 634 ? 0.86213 0.54708 0.41505 0.02034  -0.01596 0.00599  626 HIS A CA  
4948 C C   . HIS A 634 ? 0.94658 0.62071 0.48235 0.01895  -0.00441 0.00631  626 HIS A C   
4949 O O   . HIS A 634 ? 0.94413 0.59985 0.46034 0.02454  0.00058  0.00427  626 HIS A O   
4950 C CB  . HIS A 634 ? 0.85345 0.53288 0.40073 0.01403  -0.01804 0.00248  626 HIS A CB  
4951 C CG  . HIS A 634 ? 0.86783 0.55959 0.43533 0.01396  -0.02928 0.00011  626 HIS A CG  
4952 N ND1 . HIS A 634 ? 0.89814 0.59235 0.47011 0.02250  -0.03641 -0.00241 626 HIS A ND1 
4953 C CD2 . HIS A 634 ? 0.82881 0.52942 0.41337 0.00680  -0.03596 -0.00074 626 HIS A CD2 
4954 C CE1 . HIS A 634 ? 0.87357 0.57712 0.46372 0.02063  -0.04633 -0.00584 626 HIS A CE1 
4955 N NE2 . HIS A 634 ? 0.79101 0.49828 0.39032 0.01163  -0.04640 -0.00486 626 HIS A NE2 
4956 N N   . ASN A 635 ? 0.85061 0.53484 0.39246 0.01122  -0.00118 0.00885  627 ASN A N   
4957 C CA  . ASN A 635 ? 0.90036 0.57605 0.42518 0.00784  0.00983  0.00756  627 ASN A CA  
4958 C C   . ASN A 635 ? 0.90056 0.57275 0.42199 0.02105  0.01652  0.00459  627 ASN A C   
4959 O O   . ASN A 635 ? 0.86646 0.51945 0.36788 0.02423  0.02408  0.00042  627 ASN A O   
4960 C CB  . ASN A 635 ? 0.90178 0.55680 0.40426 0.00097  0.01330  0.00515  627 ASN A CB  
4961 C CG  . ASN A 635 ? 0.89412 0.54121 0.37984 -0.00675 0.02171  0.00372  627 ASN A CG  
4962 O OD1 . ASN A 635 ? 0.87987 0.54111 0.37181 -0.01332 0.02299  0.00606  627 ASN A OD1 
4963 N ND2 . ASN A 635 ? 0.88368 0.50746 0.34649 -0.00725 0.02692  0.00012  627 ASN A ND2 
4964 N N   . PRO A 636 ? 0.86869 0.55924 0.41132 0.02920  0.01330  0.00634  628 PRO A N   
4965 C CA  . PRO A 636 ? 0.88723 0.57798 0.43206 0.04298  0.01920  0.00300  628 PRO A CA  
4966 C C   . PRO A 636 ? 0.92314 0.61589 0.45919 0.04061  0.03243  -0.00127 628 PRO A C   
4967 O O   . PRO A 636 ? 0.95737 0.66869 0.50036 0.02977  0.03504  0.00160  628 PRO A O   
4968 C CB  . PRO A 636 ? 0.87936 0.59586 0.45365 0.04811  0.01190  0.00691  628 PRO A CB  
4969 C CG  . PRO A 636 ? 0.85244 0.58427 0.43881 0.03361  0.00529  0.01248  628 PRO A CG  
4970 C CD  . PRO A 636 ? 0.82919 0.54141 0.39689 0.02554  0.00304  0.01138  628 PRO A CD  
4971 N N   . THR A 637 ? 0.91175 0.58388 0.43126 0.05007  0.03963  -0.00804 629 THR A N   
4972 C CA  . THR A 637 ? 0.91799 0.58742 0.42569 0.05071  0.05302  -0.01571 629 THR A CA  
4973 C C   . THR A 637 ? 0.91018 0.57137 0.39676 0.03302  0.05639  -0.01549 629 THR A C   
4974 O O   . THR A 637 ? 0.98611 0.65259 0.46365 0.02867  0.06671  -0.02059 629 THR A O   
4975 C CB  . THR A 637 ? 1.02368 0.72585 0.55460 0.05531  0.05983  -0.01700 629 THR A CB  
4976 O OG1 . THR A 637 ? 1.04023 0.75472 0.59617 0.06768  0.05176  -0.01370 629 THR A OG1 
4977 C CG2 . THR A 637 ? 1.08849 0.78805 0.61092 0.06371  0.07434  -0.02845 629 THR A CG2 
4978 N N   . GLY A 638 ? 0.91749 0.56708 0.39648 0.02328  0.04806  -0.01044 630 GLY A N   
4979 C CA  . GLY A 638 ? 0.92191 0.56398 0.38432 0.00631  0.04822  -0.00905 630 GLY A CA  
4980 C C   . GLY A 638 ? 0.95063 0.61757 0.42273 -0.00668 0.04801  -0.00393 630 GLY A C   
4981 O O   . GLY A 638 ? 0.96834 0.62973 0.42386 -0.02000 0.05003  -0.00392 630 GLY A O   
4982 N N   . ARG A 639 ? 0.86148 0.55392 0.35888 -0.00444 0.04405  0.00139  631 ARG A N   
4983 C CA  . ARG A 639 ? 0.85736 0.57483 0.36537 -0.01731 0.04335  0.00822  631 ARG A CA  
4984 C C   . ARG A 639 ? 0.85688 0.57026 0.36059 -0.03414 0.03359  0.01513  631 ARG A C   
4985 O O   . ARG A 639 ? 1.02185 0.74570 0.52045 -0.04816 0.03442  0.02000  631 ARG A O   
4986 C CB  . ARG A 639 ? 0.81181 0.55432 0.35021 -0.01231 0.03768  0.01390  631 ARG A CB  
4987 C CG  . ARG A 639 ? 0.93770 0.67777 0.49239 -0.01090 0.02265  0.01860  631 ARG A CG  
4988 C CD  . ARG A 639 ? 0.91600 0.67968 0.49987 -0.00785 0.01562  0.02412  631 ARG A CD  
4989 N NE  . ARG A 639 ? 0.82731 0.58629 0.42440 -0.00441 0.00160  0.02573  631 ARG A NE  
4990 C CZ  . ARG A 639 ? 0.93431 0.70831 0.55560 -0.00065 -0.00760 0.02926  631 ARG A CZ  
4991 N NH1 . ARG A 639 ? 0.95633 0.75331 0.59398 -0.00049 -0.00418 0.03292  631 ARG A NH1 
4992 N NH2 . ARG A 639 ? 0.89511 0.66222 0.52432 0.00247  -0.01999 0.02849  631 ARG A NH2 
4993 N N   . SER A 640 ? 0.86545 0.56556 0.37161 -0.03302 0.02458  0.01561  632 SER A N   
4994 C CA  . SER A 640 ? 0.88253 0.58051 0.39157 -0.04624 0.01372  0.02113  632 SER A CA  
4995 C C   . SER A 640 ? 0.89766 0.57419 0.38271 -0.05215 0.01698  0.01693  632 SER A C   
4996 O O   . SER A 640 ? 0.94077 0.61755 0.42361 -0.06598 0.01058  0.02150  632 SER A O   
4997 C CB  . SER A 640 ? 0.91356 0.61525 0.44452 -0.04118 0.00217  0.02285  632 SER A CB  
4998 O OG  . SER A 640 ? 0.91215 0.63335 0.46662 -0.04055 -0.00461 0.02851  632 SER A OG  
4999 N N   . TYR A 641 ? 0.92275 0.58071 0.39160 -0.04278 0.02486  0.00944  633 TYR A N   
5000 C CA  . TYR A 641 ? 0.94431 0.57984 0.39207 -0.04841 0.02656  0.00590  633 TYR A CA  
5001 C C   . TYR A 641 ? 0.96314 0.57745 0.38914 -0.03915 0.03697  -0.00209 633 TYR A C   
5002 O O   . TYR A 641 ? 0.96626 0.57657 0.39710 -0.02499 0.03864  -0.00442 633 TYR A O   
5003 C CB  . TYR A 641 ? 0.92977 0.56264 0.38789 -0.04786 0.01914  0.00722  633 TYR A CB  
5004 C CG  . TYR A 641 ? 0.97504 0.58958 0.41601 -0.05583 0.02021  0.00520  633 TYR A CG  
5005 C CD1 . TYR A 641 ? 0.96225 0.57963 0.40379 -0.07062 0.01459  0.00835  633 TYR A CD1 
5006 C CD2 . TYR A 641 ? 0.94381 0.53822 0.36900 -0.04958 0.02547  0.00126  633 TYR A CD2 
5007 C CE1 . TYR A 641 ? 0.97771 0.58068 0.40620 -0.07911 0.01498  0.00695  633 TYR A CE1 
5008 C CE2 . TYR A 641 ? 0.97416 0.55240 0.38435 -0.05888 0.02610  0.00057  633 TYR A CE2 
5009 C CZ  . TYR A 641 ? 1.02011 0.60381 0.43280 -0.07375 0.02125  0.00308  633 TYR A CZ  
5010 O OH  . TYR A 641 ? 1.04830 0.61843 0.44876 -0.08399 0.02137  0.00280  633 TYR A OH  
5011 N N   . THR A 642 ? 1.00841 0.60781 0.41084 -0.04721 0.04218  -0.00622 634 THR A N   
5012 C CA  . THR A 642 ? 1.03432 0.60705 0.41327 -0.04044 0.05029  -0.01498 634 THR A CA  
5013 C C   . THR A 642 ? 1.03822 0.58958 0.39558 -0.05435 0.04824  -0.01602 634 THR A C   
5014 O O   . THR A 642 ? 1.07429 0.63535 0.43317 -0.06927 0.04263  -0.01116 634 THR A O   
5015 C CB  . THR A 642 ? 1.01063 0.58701 0.38156 -0.03424 0.06071  -0.02257 634 THR A CB  
5016 O OG1 . THR A 642 ? 0.99965 0.58807 0.36279 -0.04942 0.06144  -0.02082 634 THR A OG1 
5017 C CG2 . THR A 642 ? 1.07348 0.67086 0.46738 -0.01950 0.06338  -0.02217 634 THR A CG2 
5018 N N   . ILE A 643 ? 1.03412 0.55691 0.37339 -0.04991 0.05114  -0.02133 635 ILE A N   
5019 C CA  . ILE A 643 ? 1.11223 0.61024 0.42892 -0.06303 0.04931  -0.02305 635 ILE A CA  
5020 C C   . ILE A 643 ? 1.18780 0.66262 0.47941 -0.05931 0.05687  -0.03426 635 ILE A C   
5021 O O   . ILE A 643 ? 1.18945 0.65121 0.47926 -0.04319 0.06156  -0.04006 635 ILE A O   
5022 C CB  . ILE A 643 ? 1.09045 0.57341 0.40706 -0.06288 0.04527  -0.01895 635 ILE A CB  
5023 C CG1 . ILE A 643 ? 1.11516 0.62289 0.45783 -0.06018 0.04041  -0.01147 635 ILE A CG1 
5024 C CG2 . ILE A 643 ? 1.13506 0.60038 0.43512 -0.08010 0.04177  -0.01804 635 ILE A CG2 
5025 C CD1 . ILE A 643 ? 1.04946 0.54548 0.39087 -0.05504 0.03919  -0.00861 635 ILE A CD1 
5026 N N   . GLY A 644 ? 1.18530 0.65589 0.45896 -0.07309 0.05736  -0.03779 636 GLY A N   
5027 C CA  . GLY A 644 ? 1.14309 0.59671 0.39220 -0.07042 0.06557  -0.05077 636 GLY A CA  
5028 C C   . GLY A 644 ? 1.16163 0.57460 0.38913 -0.06750 0.06549  -0.05844 636 GLY A C   
5029 O O   . GLY A 644 ? 1.16050 0.55803 0.38147 -0.08005 0.05776  -0.05277 636 GLY A O   
5030 N N   . LEU A 645 ? 1.15791 0.55468 0.37647 -0.05162 0.07335  -0.07090 637 LEU A N   
5031 C CA  . LEU A 645 ? 1.31923 0.67229 0.51452 -0.04772 0.07288  -0.08089 637 LEU A CA  
5032 C C   . LEU A 645 ? 1.26154 0.60121 0.42857 -0.05579 0.07784  -0.09490 637 LEU A C   
5033 O O   . LEU A 645 ? 1.35545 0.71446 0.51687 -0.07133 0.07750  -0.09217 637 LEU A O   
5034 C CB  . LEU A 645 ? 1.32656 0.66889 0.53195 -0.02330 0.07685  -0.08705 637 LEU A CB  
5035 C CG  . LEU A 645 ? 1.22051 0.56272 0.44442 -0.01623 0.06963  -0.07429 637 LEU A CG  
5036 C CD1 . LEU A 645 ? 1.19293 0.53122 0.43027 0.00849  0.07254  -0.07979 637 LEU A CD1 
5037 C CD2 . LEU A 645 ? 1.22425 0.53253 0.43186 -0.02801 0.06049  -0.06794 637 LEU A CD2 
5038 N N   . GLU B 36  ? 2.19890 1.25030 0.78768 0.68268  0.14389  0.06521  28  GLU B N   
5039 C CA  . GLU B 36  ? 2.00012 1.08122 0.63120 0.64537  0.16572  0.05012  28  GLU B CA  
5040 C C   . GLU B 36  ? 2.05463 1.07651 0.65638 0.61939  0.18605  0.04602  28  GLU B C   
5041 O O   . GLU B 36  ? 2.11290 1.10108 0.70586 0.63321  0.18543  0.04855  28  GLU B O   
5042 C CB  . GLU B 36  ? 1.95965 1.10467 0.66534 0.65195  0.16540  0.04041  28  GLU B CB  
5043 C CG  . GLU B 36  ? 1.94202 1.15262 0.68946 0.66305  0.15387  0.03850  28  GLU B CG  
5044 C CD  . GLU B 36  ? 1.97474 1.20342 0.72178 0.70047  0.13531  0.04461  28  GLU B CD  
5045 O OE1 . GLU B 36  ? 2.03121 1.21478 0.73658 0.72187  0.12686  0.05213  28  GLU B OE1 
5046 O OE2 . GLU B 36  ? 1.95396 1.24282 0.74646 0.70769  0.12942  0.03866  28  GLU B OE2 
5047 N N   . ARG B 37  ? 2.14289 1.15827 0.73556 0.58204  0.20444  0.03539  29  ARG B N   
5048 C CA  . ARG B 37  ? 2.14557 1.10563 0.70690 0.54911  0.22869  0.02678  29  ARG B CA  
5049 C C   . ARG B 37  ? 2.13165 1.10837 0.74824 0.54407  0.23769  0.00640  29  ARG B C   
5050 O O   . ARG B 37  ? 2.15974 1.08437 0.75267 0.53909  0.24796  0.00405  29  ARG B O   
5051 C CB  . ARG B 37  ? 2.17047 1.13999 0.72031 0.50945  0.24680  0.01357  29  ARG B CB  
5052 C CG  . ARG B 37  ? 2.20345 1.12727 0.72869 0.46806  0.27720  -0.00211 29  ARG B CG  
5053 C CD  . ARG B 37  ? 2.34153 1.17383 0.77050 0.46012  0.28595  0.02146  29  ARG B CD  
5054 N NE  . ARG B 37  ? 2.41271 1.20992 0.81809 0.41006  0.32142  0.00336  29  ARG B NE  
5055 C CZ  . ARG B 37  ? 2.50993 1.21824 0.83537 0.39040  0.33898  0.01909  29  ARG B CZ  
5056 N NH1 . ARG B 37  ? 2.53931 1.17898 0.79828 0.42083  0.31986  0.05475  29  ARG B NH1 
5057 N NH2 . ARG B 37  ? 2.50580 1.19285 0.81948 0.33930  0.37597  -0.00300 29  ARG B NH2 
5058 N N   . GLN B 38  ? 2.01490 1.05825 0.70047 0.54585  0.23275  -0.00821 30  GLN B N   
5059 C CA  . GLN B 38  ? 1.96397 1.02877 0.70288 0.53950  0.23806  -0.03060 30  GLN B CA  
5060 C C   . GLN B 38  ? 1.95268 1.02714 0.70944 0.57249  0.22204  -0.01877 30  GLN B C   
5061 O O   . GLN B 38  ? 1.97634 1.09194 0.75551 0.59470  0.20805  -0.00788 30  GLN B O   
5062 C CB  . GLN B 38  ? 1.86068 0.98616 0.66227 0.52519  0.23606  -0.04947 30  GLN B CB  
5063 C CG  . GLN B 38  ? 1.87228 0.99858 0.67054 0.48799  0.25369  -0.07170 30  GLN B CG  
5064 C CD  . GLN B 38  ? 1.89649 1.02516 0.65935 0.48350  0.25219  -0.05707 30  GLN B CD  
5065 O OE1 . GLN B 38  ? 1.87843 1.03117 0.64550 0.50806  0.23465  -0.03852 30  GLN B OE1 
5066 N NE2 . GLN B 38  ? 1.94190 1.04838 0.66931 0.45062  0.27165  -0.06817 30  GLN B NE2 
5067 N N   . LEU B 39  ? 1.92377 0.96473 0.67283 0.57295  0.22590  -0.02361 31  LEU B N   
5068 C CA  . LEU B 39  ? 1.90639 0.96161 0.67571 0.59946  0.21162  -0.01743 31  LEU B CA  
5069 C C   . LEU B 39  ? 1.87042 0.97693 0.70395 0.58981  0.20652  -0.03398 31  LEU B C   
5070 O O   . LEU B 39  ? 1.86965 0.97230 0.72419 0.56344  0.21636  -0.05741 31  LEU B O   
5071 C CB  . LEU B 39  ? 1.96733 0.96024 0.69731 0.60353  0.21749  -0.01826 31  LEU B CB  
5072 C CG  . LEU B 39  ? 2.04785 0.96869 0.69724 0.61597  0.22161  -0.00215 31  LEU B CG  
5073 C CD1 . LEU B 39  ? 2.12016 0.96348 0.72944 0.60876  0.23371  -0.00735 31  LEU B CD1 
5074 C CD2 . LEU B 39  ? 2.04612 0.98378 0.68580 0.65615  0.19928  0.01704  31  LEU B CD2 
5075 N N   . GLU B 40  ? 1.80993 0.96037 0.66906 0.61091  0.19227  -0.02398 32  GLU B N   
5076 C CA  . GLU B 40  ? 1.77488 0.96726 0.67983 0.60884  0.18430  -0.03464 32  GLU B CA  
5077 C C   . GLU B 40  ? 1.79832 0.99781 0.70964 0.62205  0.17634  -0.03754 32  GLU B C   
5078 O O   . GLU B 40  ? 1.83503 1.04369 0.77346 0.61084  0.17400  -0.05845 32  GLU B O   
5079 C CB  . GLU B 40  ? 1.75250 0.98010 0.66921 0.62305  0.17787  -0.02052 32  GLU B CB  
5080 C CG  . GLU B 40  ? 1.82865 1.05811 0.74686 0.61077  0.18406  -0.02186 32  GLU B CG  
5081 C CD  . GLU B 40  ? 1.74558 0.98267 0.69690 0.58702  0.18635  -0.04606 32  GLU B CD  
5082 O OE1 . GLU B 40  ? 1.71215 0.95647 0.68893 0.58305  0.18026  -0.06164 32  GLU B OE1 
5083 O OE2 . GLU B 40  ? 1.77822 1.01818 0.73200 0.57374  0.19265  -0.05264 32  GLU B OE2 
5084 N N   . ALA B 41  ? 1.78256 0.98385 0.67359 0.64584  0.17117  -0.02143 33  ALA B N   
5085 C CA  . ALA B 41  ? 1.80025 1.01941 0.69773 0.66180  0.16286  -0.02443 33  ALA B CA  
5086 C C   . ALA B 41  ? 1.84898 1.03354 0.72350 0.66964  0.16363  -0.02621 33  ALA B C   
5087 O O   . ALA B 41  ? 1.91968 1.07048 0.76271 0.67488  0.16685  -0.01534 33  ALA B O   
5088 C CB  . ALA B 41  ? 1.79139 1.04989 0.68937 0.68341  0.15738  -0.00904 33  ALA B CB  
5089 N N   . ALA B 42  ? 1.88947 1.08014 0.77749 0.67263  0.15932  -0.04112 34  ALA B N   
5090 C CA  . ALA B 42  ? 1.87967 1.04219 0.75322 0.68371  0.15741  -0.04685 34  ALA B CA  
5091 C C   . ALA B 42  ? 1.85462 1.05767 0.75359 0.69516  0.14813  -0.06122 34  ALA B C   
5092 O O   . ALA B 42  ? 1.84159 1.05750 0.76661 0.68168  0.14821  -0.08067 34  ALA B O   
5093 C CB  . ALA B 42  ? 1.90648 1.01019 0.76778 0.66274  0.16981  -0.05963 34  ALA B CB  
5094 N N   . ARG B 43  ? 1.85957 1.08625 0.75273 0.71982  0.14003  -0.05536 35  ARG B N   
5095 C CA  . ARG B 43  ? 1.85166 1.12265 0.76360 0.73384  0.13215  -0.06912 35  ARG B CA  
5096 C C   . ARG B 43  ? 1.88300 1.14575 0.79111 0.75268  0.12578  -0.07736 35  ARG B C   
5097 O O   . ARG B 43  ? 1.89437 1.15398 0.78625 0.76805  0.12270  -0.06487 35  ARG B O   
5098 C CB  . ARG B 43  ? 1.82550 1.14746 0.73654 0.74597  0.13088  -0.05607 35  ARG B CB  
5099 C CG  . ARG B 43  ? 1.80715 1.13138 0.71872 0.73214  0.13487  -0.04596 35  ARG B CG  
5100 C CD  . ARG B 43  ? 1.79518 1.12291 0.72402 0.72073  0.13035  -0.06460 35  ARG B CD  
5101 N NE  . ARG B 43  ? 1.77783 1.09922 0.71022 0.70734  0.13182  -0.05950 35  ARG B NE  
5102 C CZ  . ARG B 43  ? 1.76953 1.10897 0.69067 0.71661  0.13050  -0.04527 35  ARG B CZ  
5103 N NH1 . ARG B 43  ? 1.80267 1.16928 0.70538 0.73716  0.13130  -0.03325 35  ARG B NH1 
5104 N NH2 . ARG B 43  ? 1.84951 1.17844 0.77759 0.70500  0.12994  -0.04505 35  ARG B NH2 
5105 N N   . TYR B 44  ? 1.89770 1.15915 0.82449 0.75243  0.12241  -0.10118 36  TYR B N   
5106 C CA  . TYR B 44  ? 1.92735 1.18854 0.86019 0.77196  0.11389  -0.11591 36  TYR B CA  
5107 C C   . TYR B 44  ? 1.90761 1.23893 0.85233 0.79197  0.10773  -0.12078 36  TYR B C   
5108 O O   . TYR B 44  ? 1.89857 1.26979 0.85409 0.78845  0.10870  -0.12747 36  TYR B O   
5109 C CB  . TYR B 44  ? 1.95048 1.18726 0.90535 0.76241  0.11453  -0.14347 36  TYR B CB  
5110 C CG  . TYR B 44  ? 1.99690 1.15287 0.93455 0.75007  0.12176  -0.14294 36  TYR B CG  
5111 C CD1 . TYR B 44  ? 2.04253 1.15054 0.95074 0.76607  0.11588  -0.13096 36  TYR B CD1 
5112 C CD2 . TYR B 44  ? 2.00363 1.12859 0.95266 0.72319  0.13452  -0.15675 36  TYR B CD2 
5113 C CE1 . TYR B 44  ? 2.10164 1.12283 0.98091 0.75632  0.12311  -0.12705 36  TYR B CE1 
5114 C CE2 . TYR B 44  ? 2.05832 1.10192 0.98414 0.71002  0.14599  -0.15637 36  TYR B CE2 
5115 C CZ  . TYR B 44  ? 2.11207 1.09792 0.99713 0.72699  0.14065  -0.13877 36  TYR B CZ  
5116 O OH  . TYR B 44  ? 2.18205 1.07444 1.03077 0.71501  0.15245  -0.13443 36  TYR B OH  
5117 N N   . ARG B 45  ? 1.92069 1.26623 0.86167 0.81314  0.10153  -0.11934 37  ARG B N   
5118 C CA  . ARG B 45  ? 1.91191 1.32565 0.86779 0.83230  0.09827  -0.13151 37  ARG B CA  
5119 C C   . ARG B 45  ? 1.93154 1.35617 0.91259 0.83988  0.09048  -0.16326 37  ARG B C   
5120 O O   . ARG B 45  ? 1.95840 1.32986 0.94456 0.83441  0.08654  -0.17317 37  ARG B O   
5121 C CB  . ARG B 45  ? 1.91922 1.34805 0.87126 0.85084  0.09423  -0.12562 37  ARG B CB  
5122 C CG  . ARG B 45  ? 1.91078 1.41603 0.88095 0.86693  0.09577  -0.14074 37  ARG B CG  
5123 C CD  . ARG B 45  ? 1.91243 1.44132 0.88607 0.88197  0.09392  -0.13812 37  ARG B CD  
5124 N NE  . ARG B 45  ? 1.94675 1.43812 0.92486 0.89889  0.07557  -0.14946 37  ARG B NE  
5125 C CZ  . ARG B 45  ? 1.95755 1.46454 0.94320 0.91725  0.06619  -0.15447 37  ARG B CZ  
5126 N NH1 . ARG B 45  ? 1.93206 1.49652 0.92678 0.91815  0.07731  -0.15118 37  ARG B NH1 
5127 N NH2 . ARG B 45  ? 1.99875 1.46287 0.98395 0.93467  0.04517  -0.16436 37  ARG B NH2 
5128 N N   . SER B 46  ? 1.92324 1.41335 0.91843 0.85101  0.09027  -0.17943 38  SER B N   
5129 C CA  . SER B 46  ? 1.93925 1.45568 0.96222 0.85975  0.08320  -0.21382 38  SER B CA  
5130 C C   . SER B 46  ? 1.97471 1.44846 1.01467 0.86993  0.07191  -0.23086 38  SER B C   
5131 O O   . SER B 46  ? 1.99295 1.44011 1.05218 0.86401  0.06878  -0.25150 38  SER B O   
5132 C CB  . SER B 46  ? 1.93349 1.52861 0.96267 0.87392  0.08594  -0.22634 38  SER B CB  
5133 O OG  . SER B 46  ? 1.94364 1.55981 0.97460 0.88778  0.08593  -0.22336 38  SER B OG  
5134 N N   . ASP B 47  ? 1.98863 1.45436 1.02276 0.88544  0.06530  -0.22391 39  ASP B N   
5135 C CA  . ASP B 47  ? 2.03292 1.45923 1.08023 0.90243  0.04939  -0.24017 39  ASP B CA  
5136 C C   . ASP B 47  ? 2.06595 1.39622 1.09151 0.88950  0.04878  -0.22524 39  ASP B C   
5137 O O   . ASP B 47  ? 2.11374 1.39692 1.14936 0.89923  0.03719  -0.24038 39  ASP B O   
5138 C CB  . ASP B 47  ? 2.03971 1.49265 1.08833 0.92498  0.03948  -0.23972 39  ASP B CB  
5139 C CG  . ASP B 47  ? 2.03629 1.45367 1.05085 0.92169  0.04112  -0.20674 39  ASP B CG  
5140 O OD1 . ASP B 47  ? 2.01224 1.41035 1.00277 0.90021  0.05527  -0.18174 39  ASP B OD1 
5141 O OD2 . ASP B 47  ? 2.05931 1.47110 1.07431 0.94158  0.02655  -0.20902 39  ASP B OD2 
5142 N N   . GLY B 48  ? 2.04733 1.34794 1.04398 0.86825  0.06150  -0.19776 40  GLY B N   
5143 C CA  . GLY B 48  ? 2.09532 1.30891 1.06818 0.85015  0.06737  -0.18480 40  GLY B CA  
5144 C C   . GLY B 48  ? 2.09312 1.26101 1.02287 0.84982  0.06773  -0.15316 40  GLY B C   
5145 O O   . GLY B 48  ? 2.13581 1.22316 1.03682 0.83796  0.07227  -0.14212 40  GLY B O   
5146 N N   . ALA B 49  ? 2.06340 1.27978 0.98789 0.86150  0.06484  -0.14063 41  ALA B N   
5147 C CA  . ALA B 49  ? 2.06827 1.25704 0.95722 0.86199  0.06508  -0.11330 41  ALA B CA  
5148 C C   . ALA B 49  ? 2.03313 1.21606 0.90784 0.83405  0.08389  -0.09427 41  ALA B C   
5149 O O   . ALA B 49  ? 1.99203 1.22087 0.88955 0.82188  0.09267  -0.10108 41  ALA B O   
5150 C CB  . ALA B 49  ? 2.04738 1.29966 0.94885 0.88393  0.05641  -0.11479 41  ALA B CB  
5151 N N   . LEU B 50  ? 2.06475 1.19345 0.90242 0.82565  0.08809  -0.07296 42  LEU B N   
5152 C CA  . LEU B 50  ? 2.02881 1.14232 0.85387 0.79790  0.10550  -0.05853 42  LEU B CA  
5153 C C   . LEU B 50  ? 1.99785 1.14241 0.81390 0.80124  0.10697  -0.03962 42  LEU B C   
5154 O O   . LEU B 50  ? 2.02904 1.14586 0.81761 0.81536  0.09862  -0.02925 42  LEU B O   
5155 C CB  . LEU B 50  ? 2.08619 1.10794 0.87442 0.78309  0.11323  -0.05336 42  LEU B CB  
5156 C CG  . LEU B 50  ? 2.07693 1.07783 0.85447 0.75245  0.13279  -0.04577 42  LEU B CG  
5157 C CD1 . LEU B 50  ? 2.01086 1.07122 0.83486 0.73491  0.13941  -0.06067 42  LEU B CD1 
5158 C CD2 . LEU B 50  ? 2.14812 1.05526 0.88828 0.73609  0.14530  -0.04642 42  LEU B CD2 
5159 N N   . LEU B 51  ? 1.96128 1.15963 0.80016 0.78977  0.11573  -0.03663 43  LEU B N   
5160 C CA  . LEU B 51  ? 1.92480 1.15479 0.76340 0.78845  0.12057  -0.02056 43  LEU B CA  
5161 C C   . LEU B 51  ? 1.94090 1.13601 0.76677 0.76271  0.13210  -0.01052 43  LEU B C   
5162 O O   . LEU B 51  ? 1.93668 1.13319 0.77830 0.74324  0.13877  -0.01830 43  LEU B O   
5163 C CB  . LEU B 51  ? 1.86923 1.16928 0.73651 0.79099  0.12444  -0.02345 43  LEU B CB  
5164 C CG  . LEU B 51  ? 1.83612 1.16543 0.70817 0.78383  0.13364  -0.00834 43  LEU B CG  
5165 C CD1 . LEU B 51  ? 1.84342 1.17679 0.70848 0.79718  0.13037  -0.00162 43  LEU B CD1 
5166 C CD2 . LEU B 51  ? 1.81332 1.19963 0.70235 0.78728  0.13992  -0.00996 43  LEU B CD2 
5167 N N   . LEU B 52  ? 1.95457 1.12442 0.75581 0.76381  0.13311  0.00224  44  LEU B N   
5168 C CA  . LEU B 52  ? 1.93623 1.07508 0.72430 0.73987  0.14501  0.00871  44  LEU B CA  
5169 C C   . LEU B 52  ? 1.94944 1.13081 0.75224 0.73904  0.14738  0.01822  44  LEU B C   
5170 O O   . LEU B 52  ? 1.96296 1.15525 0.75595 0.75868  0.14030  0.02414  44  LEU B O   
5171 C CB  . LEU B 52  ? 1.99549 1.05728 0.73210 0.74175  0.14615  0.01379  44  LEU B CB  
5172 C CG  . LEU B 52  ? 2.14224 1.14503 0.85999 0.73662  0.14888  0.00452  44  LEU B CG  
5173 C CD1 . LEU B 52  ? 2.14247 1.05416 0.79640 0.73373  0.15558  0.01369  44  LEU B CD1 
5174 C CD2 . LEU B 52  ? 2.04606 1.06464 0.79951 0.70923  0.16075  -0.01179 44  LEU B CD2 
5175 N N   . GLY B 53  ? 1.93891 1.14355 0.76739 0.71812  0.15540  0.01649  45  GLY B N   
5176 C CA  . GLY B 53  ? 1.84272 1.07392 0.68513 0.71012  0.16023  0.02292  45  GLY B CA  
5177 C C   . GLY B 53  ? 1.81730 1.01196 0.64428 0.68901  0.16773  0.02039  45  GLY B C   
5178 O O   . GLY B 53  ? 1.83404 0.99996 0.65967 0.66950  0.17382  0.00972  45  GLY B O   
5179 N N   . ALA B 54  ? 1.85905 1.05903 0.67609 0.69161  0.16838  0.02622  46  ALA B N   
5180 C CA  . ALA B 54  ? 1.86541 1.03665 0.66126 0.67143  0.17629  0.02282  46  ALA B CA  
5181 C C   . ALA B 54  ? 1.83512 1.05128 0.66004 0.66359  0.17631  0.02337  46  ALA B C   
5182 O O   . ALA B 54  ? 1.82740 1.08729 0.67900 0.67786  0.17050  0.02947  46  ALA B O   
5183 C CB  . ALA B 54  ? 1.89753 1.01755 0.63609 0.68355  0.17275  0.03033  46  ALA B CB  
5184 N N   . SER B 55  ? 1.84185 1.05115 0.66826 0.63717  0.18290  0.01574  47  SER B N   
5185 C CA  . SER B 55  ? 1.81315 1.06481 0.67548 0.62340  0.18130  0.01246  47  SER B CA  
5186 C C   . SER B 55  ? 1.85582 1.08796 0.69461 0.59957  0.18803  0.00424  47  SER B C   
5187 O O   . SER B 55  ? 1.82071 1.00929 0.62794 0.58449  0.19911  -0.00274 47  SER B O   
5188 C CB  . SER B 55  ? 1.76636 1.04752 0.67982 0.61334  0.18260  0.00364  47  SER B CB  
5189 O OG  . SER B 55  ? 1.76016 1.01547 0.67182 0.60207  0.18903  -0.01120 47  SER B OG  
5190 N N   . SER B 56  ? 1.93280 1.19753 0.78548 0.59526  0.18300  0.00334  48  SER B N   
5191 C CA  . SER B 56  ? 1.79019 1.05307 0.62976 0.56955  0.18992  -0.00883 48  SER B CA  
5192 C C   . SER B 56  ? 1.74155 1.04040 0.64276 0.54578  0.19539  -0.03157 48  SER B C   
5193 O O   . SER B 56  ? 1.69970 1.04377 0.65210 0.55021  0.18687  -0.03364 48  SER B O   
5194 C CB  . SER B 56  ? 1.80530 1.08860 0.62882 0.58052  0.17868  -0.00239 48  SER B CB  
5195 O OG  . SER B 56  ? 1.99191 1.22705 0.74417 0.59723  0.17272  0.01420  48  SER B OG  
5196 N N   . LEU B 57  ? 1.75070 1.02920 0.65006 0.52165  0.20869  -0.05046 49  LEU B N   
5197 C CA  . LEU B 57  ? 1.71130 1.02082 0.67080 0.50020  0.21144  -0.07946 49  LEU B CA  
5198 C C   . LEU B 57  ? 1.72370 1.04938 0.68085 0.47193  0.22124  -0.10112 49  LEU B C   
5199 O O   . LEU B 57  ? 1.75386 1.10624 0.76085 0.45160  0.22449  -0.13241 49  LEU B O   
5200 C CB  . LEU B 57  ? 1.71448 0.99959 0.67989 0.49350  0.21869  -0.09465 49  LEU B CB  
5201 C CG  . LEU B 57  ? 1.71236 0.97969 0.66992 0.52074  0.21074  -0.07592 49  LEU B CG  
5202 C CD1 . LEU B 57  ? 1.71188 0.96519 0.68534 0.51386  0.21522  -0.09907 49  LEU B CD1 
5203 C CD2 . LEU B 57  ? 1.67480 0.97565 0.66913 0.54151  0.19482  -0.06004 49  LEU B CD2 
5204 N N   . SER B 58  ? 1.76640 1.07724 0.66643 0.47224  0.22406  -0.08703 50  SER B N   
5205 C CA  . SER B 58  ? 1.78628 1.11661 0.67227 0.44873  0.23182  -0.10350 50  SER B CA  
5206 C C   . SER B 58  ? 1.82695 1.14775 0.65555 0.46769  0.22164  -0.07851 50  SER B C   
5207 O O   . SER B 58  ? 1.85853 1.13896 0.64186 0.49218  0.21453  -0.05097 50  SER B O   
5208 C CB  . SER B 58  ? 1.82833 1.13016 0.68117 0.41390  0.25626  -0.12340 50  SER B CB  
5209 O OG  . SER B 58  ? 1.84028 1.17326 0.69126 0.38759  0.26555  -0.14624 50  SER B OG  
5210 N N   . GLY B 59  ? 1.82713 1.18680 0.66115 0.45910  0.21849  -0.09144 51  GLY B N   
5211 C CA  . GLY B 59  ? 1.86746 1.22765 0.65091 0.47856  0.20474  -0.07465 51  GLY B CA  
5212 C C   . GLY B 59  ? 1.81250 1.23690 0.66201 0.49834  0.18550  -0.08158 51  GLY B C   
5213 O O   . GLY B 59  ? 1.74818 1.20963 0.67875 0.49347  0.18485  -0.09637 51  GLY B O   
5214 N N   . ARG B 60  ? 1.90986 1.34441 0.72499 0.52035  0.16937  -0.07219 52  ARG B N   
5215 C CA  . ARG B 60  ? 1.82218 1.32230 0.69763 0.53836  0.15169  -0.08370 52  ARG B CA  
5216 C C   . ARG B 60  ? 1.76482 1.27900 0.70111 0.55686  0.14607  -0.07428 52  ARG B C   
5217 O O   . ARG B 60  ? 1.69950 1.26309 0.71696 0.55031  0.14522  -0.09046 52  ARG B O   
5218 C CB  . ARG B 60  ? 1.85703 1.35611 0.67158 0.56414  0.13272  -0.07515 52  ARG B CB  
5219 C CG  . ARG B 60  ? 1.81872 1.39134 0.69578 0.58109  0.11505  -0.09456 52  ARG B CG  
5220 C CD  . ARG B 60  ? 1.87323 1.44296 0.69589 0.61768  0.09019  -0.08565 52  ARG B CD  
5221 N NE  . ARG B 60  ? 1.94574 1.49836 0.68721 0.61312  0.08513  -0.08743 52  ARG B NE  
5222 C CZ  . ARG B 60  ? 1.94462 1.55379 0.70193 0.60841  0.07755  -0.11420 52  ARG B CZ  
5223 N NH1 . ARG B 60  ? 1.87128 1.55821 0.73062 0.60693  0.07409  -0.14360 52  ARG B NH1 
5224 N NH2 . ARG B 60  ? 2.02339 1.60909 0.69132 0.60404  0.07413  -0.11168 52  ARG B NH2 
5225 N N   A CYS B 61  ? 1.90749 1.37755 0.80355 0.57800  0.14307  -0.04948 53  CYS B N   
5226 N N   B CYS B 61  ? 1.86360 1.33377 0.75956 0.57815  0.14297  -0.04945 53  CYS B N   
5227 C CA  A CYS B 61  ? 1.81929 1.29974 0.75727 0.59717  0.13936  -0.03861 53  CYS B CA  
5228 C CA  B CYS B 61  ? 1.81387 1.29431 0.75181 0.59720  0.13934  -0.03859 53  CYS B CA  
5229 C C   A CYS B 61  ? 1.73908 1.18508 0.68402 0.58414  0.15341  -0.03164 53  CYS B C   
5230 C C   B CYS B 61  ? 1.82172 1.26788 0.76688 0.58390  0.15347  -0.03181 53  CYS B C   
5231 O O   A CYS B 61  ? 1.78233 1.17617 0.67142 0.57644  0.16151  -0.02502 53  CYS B O   
5232 O O   B CYS B 61  ? 1.84251 1.23681 0.73222 0.57582  0.16170  -0.02545 53  CYS B O   
5233 C CB  A CYS B 61  ? 1.83596 1.29815 0.72873 0.63252  0.12416  -0.02229 53  CYS B CB  
5234 C CB  B CYS B 61  ? 1.77616 1.23746 0.66872 0.63250  0.12438  -0.02196 53  CYS B CB  
5235 S SG  A CYS B 61  ? 1.82027 1.30041 0.75850 0.65369  0.12340  -0.01317 53  CYS B SG  
5236 S SG  B CYS B 61  ? 1.82455 1.30521 0.67724 0.65374  0.10206  -0.02935 53  CYS B SG  
5237 N N   . TRP B 62  ? 1.67035 1.14257 0.67903 0.58161  0.15589  -0.03353 54  TRP B N   
5238 C CA  . TRP B 62  ? 1.67505 1.12148 0.69619 0.57304  0.16474  -0.02935 54  TRP B CA  
5239 C C   . TRP B 62  ? 1.68476 1.13093 0.71158 0.59509  0.16229  -0.01132 54  TRP B C   
5240 O O   . TRP B 62  ? 1.62819 1.08295 0.69412 0.59007  0.16520  -0.00921 54  TRP B O   
5241 C CB  . TRP B 62  ? 1.61394 1.08575 0.69927 0.55037  0.16737  -0.04793 54  TRP B CB  
5242 C CG  . TRP B 62  ? 1.62309 1.09114 0.70550 0.52512  0.17380  -0.07150 54  TRP B CG  
5243 C CD1 . TRP B 62  ? 1.67111 1.11553 0.69506 0.51602  0.18102  -0.07545 54  TRP B CD1 
5244 C CD2 . TRP B 62  ? 1.58934 1.07945 0.73126 0.50421  0.17413  -0.09706 54  TRP B CD2 
5245 N NE1 . TRP B 62  ? 1.65744 1.11339 0.70112 0.48800  0.18950  -0.10353 54  TRP B NE1 
5246 C CE2 . TRP B 62  ? 1.60953 1.09611 0.72959 0.48204  0.18373  -0.11976 54  TRP B CE2 
5247 C CE3 . TRP B 62  ? 1.55309 1.06215 0.76280 0.50213  0.16658  -0.10332 54  TRP B CE3 
5248 C CZ2 . TRP B 62  ? 1.58731 1.09777 0.75907 0.45923  0.18557  -0.15390 54  TRP B CZ2 
5249 C CZ3 . TRP B 62  ? 1.53484 1.05967 0.79364 0.48273  0.16448  -0.13408 54  TRP B CZ3 
5250 C CH2 . TRP B 62  ? 1.54809 1.07800 0.79202 0.46214  0.17367  -0.16178 54  TRP B CH2 
5251 N N   . ALA B 63  ? 1.68790 1.12342 0.67464 0.61930  0.15609  0.00010  55  ALA B N   
5252 C CA  . ALA B 63  ? 1.74180 1.18406 0.73181 0.64175  0.15434  0.01207  55  ALA B CA  
5253 C C   . ALA B 63  ? 1.77772 1.17018 0.72502 0.64871  0.15826  0.02110  55  ALA B C   
5254 O O   . ALA B 63  ? 1.78100 1.13711 0.70568 0.63227  0.16427  0.01684  55  ALA B O   
5255 C CB  . ALA B 63  ? 1.79484 1.26135 0.77612 0.66642  0.14225  0.01091  55  ALA B CB  
5256 N N   . GLY B 64  ? 1.82835 1.22412 0.77029 0.67057  0.15639  0.02886  56  GLY B N   
5257 C CA  . GLY B 64  ? 1.85166 1.20669 0.75884 0.68125  0.15861  0.03402  56  GLY B CA  
5258 C C   . GLY B 64  ? 1.89793 1.25164 0.78223 0.71257  0.14888  0.03689  56  GLY B C   
5259 O O   . GLY B 64  ? 1.90613 1.29496 0.80443 0.72631  0.13989  0.03338  56  GLY B O   
5260 N N   . SER B 65  ? 1.88783 1.20571 0.74349 0.72474  0.14926  0.03864  57  SER B N   
5261 C CA  . SER B 65  ? 1.91629 1.22565 0.75028 0.75710  0.13756  0.03739  57  SER B CA  
5262 C C   . SER B 65  ? 1.91031 1.20338 0.73793 0.76543  0.14297  0.03463  57  SER B C   
5263 O O   . SER B 65  ? 1.88802 1.15801 0.71429 0.74491  0.15213  0.03522  57  SER B O   
5264 C CB  . SER B 65  ? 1.96421 1.22145 0.74776 0.76748  0.12430  0.04135  57  SER B CB  
5265 O OG  . SER B 65  ? 2.00989 1.20795 0.75859 0.74558  0.13401  0.04568  57  SER B OG  
5266 N N   . LEU B 66  ? 1.89838 1.21168 0.73110 0.79169  0.13420  0.02900  58  LEU B N   
5267 C CA  . LEU B 66  ? 1.87490 1.18664 0.71145 0.79602  0.13212  0.02568  58  LEU B CA  
5268 C C   . LEU B 66  ? 1.91675 1.19730 0.72716 0.82219  0.11355  0.02024  58  LEU B C   
5269 O O   . LEU B 66  ? 1.99411 1.29996 0.81070 0.84535  0.10079  0.01369  58  LEU B O   
5270 C CB  . LEU B 66  ? 1.86530 1.24461 0.74015 0.79865  0.14004  0.02074  58  LEU B CB  
5271 C CG  . LEU B 66  ? 1.83147 1.23564 0.72594 0.77642  0.15696  0.02802  58  LEU B CG  
5272 C CD1 . LEU B 66  ? 1.84805 1.31488 0.76868 0.78169  0.16831  0.02432  58  LEU B CD1 
5273 C CD2 . LEU B 66  ? 1.76235 1.14004 0.65123 0.75860  0.16109  0.03208  58  LEU B CD2 
5274 N N   . TRP B 67  ? 1.95849 1.18611 0.74350 0.81815  0.11102  0.02045  59  TRP B N   
5275 C CA  . TRP B 67  ? 2.04875 1.23460 0.80636 0.83992  0.09278  0.01535  59  TRP B CA  
5276 C C   . TRP B 67  ? 2.00503 1.21059 0.78632 0.84344  0.09078  0.00210  59  TRP B C   
5277 O O   . TRP B 67  ? 1.99561 1.22983 0.80118 0.82579  0.10454  0.00044  59  TRP B O   
5278 C CB  . TRP B 67  ? 2.11938 1.21465 0.82167 0.83051  0.09405  0.02574  59  TRP B CB  
5279 C CG  . TRP B 67  ? 2.12544 1.19807 0.80136 0.82161  0.10124  0.03750  59  TRP B CG  
5280 C CD1 . TRP B 67  ? 2.12738 1.19383 0.80497 0.79305  0.12224  0.04004  59  TRP B CD1 
5281 C CD2 . TRP B 67  ? 2.20793 1.26548 0.85466 0.84104  0.08503  0.04478  59  TRP B CD2 
5282 N NE1 . TRP B 67  ? 2.19147 1.25131 0.84922 0.78334  0.12086  0.04939  59  TRP B NE1 
5283 C CE2 . TRP B 67  ? 2.22532 1.27798 0.86106 0.81351  0.09790  0.05401  59  TRP B CE2 
5284 C CE3 . TRP B 67  ? 2.24943 1.31141 0.88662 0.87032  0.05771  0.04130  59  TRP B CE3 
5285 C CZ2 . TRP B 67  ? 2.23041 1.28028 0.84097 0.81686  0.08497  0.06236  59  TRP B CZ2 
5286 C CZ3 . TRP B 67  ? 2.20805 1.25975 0.81755 0.88065  0.04334  0.04901  59  TRP B CZ3 
5287 C CH2 . TRP B 67  ? 2.26137 1.30512 0.85404 0.85597  0.05670  0.06169  59  TRP B CH2 
5288 N N   . LEU B 68  ? 2.13274 1.32314 0.90764 0.86660  0.07185  -0.00868 60  LEU B N   
5289 C CA  . LEU B 68  ? 2.08225 1.27354 0.87347 0.87080  0.06764  -0.02421 60  LEU B CA  
5290 C C   . LEU B 68  ? 2.18940 1.30062 0.94410 0.88079  0.05206  -0.02478 60  LEU B C   
5291 O O   . LEU B 68  ? 2.25708 1.34704 0.99057 0.90144  0.03256  -0.02261 60  LEU B O   
5292 C CB  . LEU B 68  ? 2.01543 1.28588 0.85046 0.89156  0.05982  -0.04383 60  LEU B CB  
5293 C CG  . LEU B 68  ? 2.07520 1.36034 0.93339 0.89708  0.05607  -0.06418 60  LEU B CG  
5294 C CD1 . LEU B 68  ? 1.97776 1.27157 0.84457 0.87179  0.07520  -0.06147 60  LEU B CD1 
5295 C CD2 . LEU B 68  ? 1.99638 1.35961 0.89526 0.91923  0.04846  -0.08747 60  LEU B CD2 
5296 N N   . PHE B 69  ? 2.23112 1.29940 0.98042 0.86640  0.05962  -0.02877 61  PHE B N   
5297 C CA  . PHE B 69  ? 2.28756 1.26851 1.00255 0.87025  0.04991  -0.02863 61  PHE B CA  
5298 C C   . PHE B 69  ? 2.28808 1.28503 1.03989 0.87914  0.04234  -0.05256 61  PHE B C   
5299 O O   . PHE B 69  ? 2.23792 1.24563 1.01167 0.85974  0.05826  -0.06169 61  PHE B O   
5300 C CB  . PHE B 69  ? 2.32286 1.22904 0.99830 0.84054  0.07126  -0.01424 61  PHE B CB  
5301 C CG  . PHE B 69  ? 2.41267 1.27879 1.03871 0.83506  0.07537  0.00795  61  PHE B CG  
5302 C CD1 . PHE B 69  ? 2.36473 1.28200 1.00410 0.82480  0.08745  0.01442  61  PHE B CD1 
5303 C CD2 . PHE B 69  ? 2.49050 1.26608 1.05594 0.83955  0.06631  0.02239  61  PHE B CD2 
5304 C CE1 . PHE B 69  ? 2.36354 1.24769 0.96110 0.82092  0.09074  0.03142  61  PHE B CE1 
5305 C CE2 . PHE B 69  ? 2.58513 1.32665 1.10234 0.83390  0.06948  0.04220  61  PHE B CE2 
5306 C CZ  . PHE B 69  ? 2.53732 1.33557 1.07273 0.82557  0.08175  0.04517  61  PHE B CZ  
5307 N N   . LYS B 70  ? 2.33636 1.33815 1.09859 0.90834  0.01693  -0.06576 62  LYS B N   
5308 C CA  . LYS B 70  ? 2.35136 1.36481 1.15050 0.92143  0.00554  -0.09245 62  LYS B CA  
5309 C C   . LYS B 70  ? 2.42125 1.33430 1.19204 0.91145  0.00612  -0.08915 62  LYS B C   
5310 O O   . LYS B 70  ? 2.42434 1.34140 1.22878 0.91044  0.00690  -0.11115 62  LYS B O   
5311 C CB  . LYS B 70  ? 2.33200 1.38633 1.15568 0.95653  -0.02298 -0.11072 62  LYS B CB  
5312 C CG  . LYS B 70  ? 2.29126 1.45292 1.15495 0.96454  -0.01870 -0.12240 62  LYS B CG  
5313 C CD  . LYS B 70  ? 2.33029 1.53329 1.21870 0.99804  -0.04572 -0.14305 62  LYS B CD  
5314 C CE  . LYS B 70  ? 2.23743 1.54466 1.16488 1.00191  -0.03575 -0.15508 62  LYS B CE  
5315 N NZ  . LYS B 70  ? 2.17665 1.52068 1.12594 1.03254  -0.06153 -0.17502 62  LYS B NZ  
5316 N N   . ASP B 71  ? 2.50703 1.33317 1.21767 0.90360  0.00698  -0.06368 63  ASP B N   
5317 C CA  . ASP B 71  ? 2.64080 1.35914 1.31124 0.88411  0.01796  -0.05371 63  ASP B CA  
5318 C C   . ASP B 71  ? 2.69659 1.40086 1.34561 0.84900  0.05122  -0.04016 63  ASP B C   
5319 O O   . ASP B 71  ? 2.70922 1.39677 1.31683 0.84256  0.05698  -0.01815 63  ASP B O   
5320 C CB  . ASP B 71  ? 2.70410 1.32975 1.31539 0.89819  -0.00383 -0.03430 63  ASP B CB  
5321 C CG  . ASP B 71  ? 2.81108 1.32423 1.39022 0.88527  0.00054  -0.02938 63  ASP B CG  
5322 O OD1 . ASP B 71  ? 2.79505 1.28288 1.37746 0.85541  0.03037  -0.03333 63  ASP B OD1 
5323 O OD2 . ASP B 71  ? 2.88579 1.33699 1.43904 0.90469  -0.02637 -0.02333 63  ASP B OD2 
5324 N N   . PRO B 72  ? 2.72174 1.43767 1.40308 0.82573  0.07275  -0.05685 64  PRO B N   
5325 C CA  . PRO B 72  ? 2.62758 1.34689 1.30298 0.79303  0.10193  -0.05190 64  PRO B CA  
5326 C C   . PRO B 72  ? 2.70460 1.31090 1.31462 0.76898  0.12157  -0.03465 64  PRO B C   
5327 O O   . PRO B 72  ? 2.61194 1.21625 1.20136 0.74820  0.14115  -0.02480 64  PRO B O   
5328 C CB  . PRO B 72  ? 2.46828 1.23914 1.20576 0.77973  0.11173  -0.08206 64  PRO B CB  
5329 C CG  . PRO B 72  ? 2.62541 1.35999 1.37686 0.79587  0.09698  -0.09882 64  PRO B CG  
5330 C CD  . PRO B 72  ? 2.69267 1.42308 1.42321 0.82980  0.06843  -0.08591 64  PRO B CD  
5331 N N   . CYS B 73  ? 2.80270 1.31584 1.38063 0.77125  0.11647  -0.03171 65  CYS B N   
5332 C CA  . CYS B 73  ? 2.83796 1.22484 1.34292 0.74563  0.13688  -0.01312 65  CYS B CA  
5333 C C   . CYS B 73  ? 2.87881 1.21439 1.30850 0.75673  0.12349  0.02235  65  CYS B C   
5334 O O   . CYS B 73  ? 2.96263 1.18576 1.31904 0.73732  0.13560  0.04399  65  CYS B O   
5335 C CB  . CYS B 73  ? 2.86622 1.17237 1.36839 0.74278  0.13465  -0.02227 65  CYS B CB  
5336 S SG  . CYS B 73  ? 2.81967 1.18838 1.41508 0.72937  0.14852  -0.06941 65  CYS B SG  
5337 N N   . ALA B 74  ? 2.84057 1.25692 1.28786 0.78395  0.10016  0.02692  66  ALA B N   
5338 C CA  . ALA B 74  ? 2.82742 1.22491 1.21940 0.79593  0.08443  0.05346  66  ALA B CA  
5339 C C   . ALA B 74  ? 2.83184 1.26029 1.21241 0.77682  0.10768  0.06197  66  ALA B C   
5340 O O   . ALA B 74  ? 2.87298 1.25018 1.18925 0.76906  0.10892  0.08627  66  ALA B O   
5341 C CB  . ALA B 74  ? 2.80167 1.27335 1.23014 0.83552  0.04683  0.04505  66  ALA B CB  
5342 N N   . ALA B 75  ? 2.69160 1.20398 1.13420 0.76848  0.12331  0.04195  67  ALA B N   
5343 C CA  . ALA B 75  ? 2.62869 1.18668 1.07948 0.75259  0.14270  0.04333  67  ALA B CA  
5344 C C   . ALA B 75  ? 2.71023 1.17547 1.10089 0.71860  0.17465  0.05218  67  ALA B C   
5345 O O   . ALA B 75  ? 2.70928 1.09939 1.07797 0.69727  0.19137  0.04712  67  ALA B O   
5346 C CB  . ALA B 75  ? 2.52799 1.18601 1.05926 0.74520  0.15018  0.01852  67  ALA B CB  
5347 N N   . PRO B 76  ? 2.69281 1.19086 1.07229 0.69496  0.18410  0.06299  68  PRO B N   
5348 C CA  . PRO B 76  ? 2.61134 1.19951 1.02362 0.71508  0.16784  0.06581  68  PRO B CA  
5349 C C   . PRO B 76  ? 2.73572 1.30691 1.10468 0.74908  0.13722  0.08944  68  PRO B C   
5350 O O   . PRO B 76  ? 2.68439 1.33234 1.08622 0.76637  0.12404  0.08785  68  PRO B O   
5351 C CB  . PRO B 76  ? 2.46094 1.07858 0.87803 0.67043  0.19278  0.06314  68  PRO B CB  
5352 C CG  . PRO B 76  ? 2.57704 1.09633 0.92180 0.63673  0.21149  0.07641  68  PRO B CG  
5353 C CD  . PRO B 76  ? 2.65724 1.10804 0.99369 0.64432  0.21333  0.06982  68  PRO B CD  
5354 N N   . ASN B 77  ? 2.95973 1.43896 1.26255 0.75378  0.12612  0.10712  69  ASN B N   
5355 C CA  . ASN B 77  ? 2.97203 1.44220 1.23597 0.76867  0.09785  0.12231  69  ASN B CA  
5356 C C   . ASN B 77  ? 2.97233 1.54017 1.29730 0.80735  0.06716  0.10628  69  ASN B C   
5357 O O   . ASN B 77  ? 2.91169 1.49937 1.27286 0.82908  0.05166  0.09118  69  ASN B O   
5358 C CB  . ASN B 77  ? 3.06960 1.43727 1.27312 0.76705  0.08730  0.13535  69  ASN B CB  
5359 C CG  . ASN B 77  ? 3.17733 1.51098 1.32211 0.76934  0.06729  0.15437  69  ASN B CG  
5360 O OD1 . ASN B 77  ? 3.20019 1.49596 1.32284 0.79193  0.03750  0.15836  69  ASN B OD1 
5361 N ND2 . ASN B 77  ? 3.21464 1.56408 1.33652 0.74621  0.08160  0.16430  69  ASN B ND2 
5362 N N   . GLU B 78  ? 3.05307 1.67991 1.38939 0.81318  0.05962  0.10797  70  GLU B N   
5363 C CA  . GLU B 78  ? 2.93004 1.65131 1.32274 0.84651  0.03538  0.09196  70  GLU B CA  
5364 C C   . GLU B 78  ? 3.03189 1.73542 1.41419 0.87925  -0.00076 0.08589  70  GLU B C   
5365 O O   . GLU B 78  ? 2.95781 1.72904 1.39413 0.90650  -0.01772 0.06586  70  GLU B O   
5366 C CB  . GLU B 78  ? 2.79648 1.56583 1.19269 0.84325  0.03437  0.09639  70  GLU B CB  
5367 C CG  . GLU B 78  ? 2.82839 1.63740 1.25163 0.81660  0.06370  0.09763  70  GLU B CG  
5368 C CD  . GLU B 78  ? 2.91103 1.66408 1.28331 0.77457  0.08883  0.11259  70  GLU B CD  
5369 O OE1 . GLU B 78  ? 2.91610 1.61167 1.23130 0.76465  0.08303  0.12513  70  GLU B OE1 
5370 O OE2 . GLU B 78  ? 2.89470 1.67399 1.29668 0.74513  0.11539  0.10493  70  GLU B OE2 
5371 N N   . GLY B 79  ? 3.07199 1.68706 1.38675 0.87552  -0.01213 0.10221  71  GLY B N   
5372 C CA  . GLY B 79  ? 3.12890 1.71362 1.42373 0.90761  -0.05103 0.09899  71  GLY B CA  
5373 C C   . GLY B 79  ? 3.19698 1.77791 1.52457 0.92529  -0.06307 0.08341  71  GLY B C   
5374 O O   . GLY B 79  ? 3.22149 1.80611 1.55589 0.95918  -0.09962 0.07189  71  GLY B O   
5375 N N   . PHE B 80  ? 3.15624 1.73143 1.50577 0.90447  -0.03560 0.08037  72  PHE B N   
5376 C CA  . PHE B 80  ? 3.08564 1.65739 1.47067 0.91589  -0.04298 0.06402  72  PHE B CA  
5377 C C   . PHE B 80  ? 3.01050 1.67970 1.47104 0.91367  -0.02556 0.04306  72  PHE B C   
5378 O O   . PHE B 80  ? 2.97442 1.62990 1.45267 0.89694  -0.00606 0.03724  72  PHE B O   
5379 C CB  . PHE B 80  ? 3.14458 1.60594 1.48073 0.89085  -0.02673 0.07917  72  PHE B CB  
5380 C CG  . PHE B 80  ? 3.29104 1.64803 1.54927 0.89144  -0.04457 0.10192  72  PHE B CG  
5381 C CD1 . PHE B 80  ? 3.33312 1.65286 1.52917 0.87340  -0.03645 0.12515  72  PHE B CD1 
5382 C CD2 . PHE B 80  ? 3.34690 1.64257 1.59434 0.90891  -0.06996 0.10009  72  PHE B CD2 
5383 C CE1 . PHE B 80  ? 3.40372 1.62782 1.52386 0.87193  -0.05285 0.14766  72  PHE B CE1 
5384 C CE2 . PHE B 80  ? 3.39286 1.58733 1.56450 0.90893  -0.08750 0.12374  72  PHE B CE2 
5385 C CZ  . PHE B 80  ? 3.48573 1.64441 1.59126 0.88991  -0.07853 0.14835  72  PHE B CZ  
5386 N N   . CYS B 81  ? 3.01019 1.77432 1.51410 0.92929  -0.03246 0.03126  73  CYS B N   
5387 C CA  . CYS B 81  ? 2.82439 1.68714 1.39761 0.92736  -0.01749 0.01365  73  CYS B CA  
5388 C C   . CYS B 81  ? 2.76022 1.69616 1.38570 0.96089  -0.04383 -0.01198 73  CYS B C   
5389 O O   . CYS B 81  ? 2.82239 1.74218 1.43270 0.98734  -0.07496 -0.01665 73  CYS B O   
5390 C CB  . CYS B 81  ? 2.70610 1.61804 1.28839 0.91235  0.00251  0.02204  73  CYS B CB  
5391 S SG  . CYS B 81  ? 2.64397 1.63460 1.25323 0.94136  -0.02008 0.01218  73  CYS B SG  
5392 N N   . SER B 82  ? 2.56780 1.58232 1.25217 0.95920  -0.03177 -0.02945 74  SER B N   
5393 C CA  . SER B 82  ? 2.46935 1.56638 1.21141 0.98622  -0.04908 -0.05819 74  SER B CA  
5394 C C   . SER B 82  ? 2.45629 1.63360 1.22698 0.99300  -0.04638 -0.06274 74  SER B C   
5395 O O   . SER B 82  ? 2.51231 1.73199 1.30842 1.02167  -0.07101 -0.08336 74  SER B O   
5396 C CB  . SER B 82  ? 2.39258 1.53134 1.17842 0.97804  -0.03468 -0.07468 74  SER B CB  
5397 O OG  . SER B 82  ? 2.44257 1.50924 1.20856 0.97129  -0.03629 -0.07346 74  SER B OG  
5398 N N   . ALA B 83  ? 2.36051 1.55872 1.13196 0.96767  -0.01813 -0.04710 75  ALA B N   
5399 C CA  . ALA B 83  ? 2.15864 1.42890 0.96021 0.96820  -0.00961 -0.04927 75  ALA B CA  
5400 C C   . ALA B 83  ? 2.20191 1.45089 0.98134 0.93860  0.01604  -0.02491 75  ALA B C   
5401 O O   . ALA B 83  ? 2.22692 1.42657 0.98253 0.91553  0.03172  -0.01202 75  ALA B O   
5402 C CB  . ALA B 83  ? 2.06706 1.42877 0.93018 0.97035  0.00156  -0.07095 75  ALA B CB  
5403 N N   . GLY B 84  ? 2.14737 1.43647 0.94080 0.93973  0.01954  -0.02318 76  GLY B N   
5404 C CA  . GLY B 84  ? 2.02418 1.30558 0.80814 0.91415  0.04206  -0.00541 76  GLY B CA  
5405 C C   . GLY B 84  ? 1.96021 1.31424 0.78543 0.91799  0.04698  -0.01421 76  GLY B C   
5406 O O   . GLY B 84  ? 1.97082 1.36594 0.81836 0.94435  0.02725  -0.03273 76  GLY B O   
5407 N N   . VAL B 85  ? 1.91433 1.28601 0.75373 0.89149  0.07181  -0.00526 77  VAL B N   
5408 C CA  . VAL B 85  ? 1.87063 1.31127 0.75397 0.88382  0.08091  -0.01310 77  VAL B CA  
5409 C C   . VAL B 85  ? 1.95908 1.38463 0.83855 0.84623  0.09579  0.00433  77  VAL B C   
5410 O O   . VAL B 85  ? 1.94661 1.32830 0.80377 0.82675  0.10779  0.01680  77  VAL B O   
5411 C CB  . VAL B 85  ? 1.83089 1.34540 0.76519 0.88065  0.09853  -0.02737 77  VAL B CB  
5412 C CG1 . VAL B 85  ? 1.84919 1.35690 0.78378 0.85089  0.12326  -0.01272 77  VAL B CG1 
5413 C CG2 . VAL B 85  ? 1.80042 1.38955 0.78600 0.87478  0.10276  -0.04107 77  VAL B CG2 
5414 N N   . GLN B 86  ? 1.90866 1.37448 0.81520 0.83762  0.09409  -0.00001 78  GLN B N   
5415 C CA  . GLN B 86  ? 1.84583 1.31206 0.76254 0.80344  0.10630  0.00957  78  GLN B CA  
5416 C C   . GLN B 86  ? 1.78675 1.31000 0.76018 0.78101  0.12716  0.00741  78  GLN B C   
5417 O O   . GLN B 86  ? 1.79444 1.37719 0.80838 0.78989  0.12862  -0.00697 78  GLN B O   
5418 C CB  . GLN B 86  ? 1.87357 1.35026 0.78598 0.80963  0.08974  0.00303  78  GLN B CB  
5419 C CG  . GLN B 86  ? 1.89280 1.36073 0.80616 0.77713  0.09895  0.00956  78  GLN B CG  
5420 C CD  . GLN B 86  ? 1.94896 1.34754 0.79575 0.77313  0.09209  0.02098  78  GLN B CD  
5421 O OE1 . GLN B 86  ? 2.02259 1.37396 0.81682 0.79710  0.07634  0.02655  78  GLN B OE1 
5422 N NE2 . GLN B 86  ? 1.94451 1.33504 0.79296 0.74134  0.10442  0.02335  78  GLN B NE2 
5423 N N   . THR B 87  ? 1.78580 1.28954 0.76136 0.75299  0.14226  0.01978  79  THR B N   
5424 C CA  . THR B 87  ? 1.75523 1.29623 0.77628 0.72812  0.15953  0.02326  79  THR B CA  
5425 C C   . THR B 87  ? 1.80798 1.36633 0.85869 0.70902  0.15821  0.01894  79  THR B C   
5426 O O   . THR B 87  ? 1.78744 1.32138 0.81310 0.71162  0.14642  0.01585  79  THR B O   
5427 C CB  . THR B 87  ? 1.79011 1.29832 0.79707 0.71364  0.17006  0.03613  79  THR B CB  
5428 O OG1 . THR B 87  ? 1.84189 1.30288 0.82473 0.70246  0.16546  0.03839  79  THR B OG1 
5429 C CG2 . THR B 87  ? 1.75897 1.25700 0.74047 0.73251  0.17153  0.03645  79  THR B CG2 
5430 N N   . GLU B 88  ? 1.73646 1.33334 0.83633 0.68952  0.17045  0.01840  80  GLU B N   
5431 C CA  . GLU B 88  ? 1.64607 1.26670 0.78632 0.67094  0.16961  0.00974  80  GLU B CA  
5432 C C   . GLU B 88  ? 1.66520 1.24487 0.79502 0.65100  0.16889  0.01583  80  GLU B C   
5433 O O   . GLU B 88  ? 1.67002 1.25813 0.81482 0.64127  0.16286  0.00448  80  GLU B O   
5434 C CB  . GLU B 88  ? 1.59415 1.26331 0.79200 0.65506  0.18452  0.00657  80  GLU B CB  
5435 C CG  . GLU B 88  ? 1.65389 1.30211 0.86667 0.62911  0.19722  0.02338  80  GLU B CG  
5436 C CD  . GLU B 88  ? 1.73272 1.41887 0.99930 0.60864  0.21332  0.02269  80  GLU B CD  
5437 O OE1 . GLU B 88  ? 1.76260 1.48226 1.03697 0.61275  0.22612  0.02040  80  GLU B OE1 
5438 O OE2 . GLU B 88  ? 1.71054 1.39322 1.01349 0.58731  0.21394  0.02199  80  GLU B OE2 
5439 N N   . ALA B 89  ? 1.67609 1.21799 0.78315 0.64632  0.17393  0.02856  81  ALA B N   
5440 C CA  . ALA B 89  ? 1.70025 1.20632 0.80207 0.62904  0.17279  0.02860  81  ALA B CA  
5441 C C   . ALA B 89  ? 1.67839 1.13944 0.73216 0.63816  0.17226  0.03378  81  ALA B C   
5442 O O   . ALA B 89  ? 1.70471 1.16340 0.73421 0.65713  0.17326  0.03997  81  ALA B O   
5443 C CB  . ALA B 89  ? 1.58774 1.10065 0.73106 0.61043  0.17790  0.03384  81  ALA B CB  
5444 N N   . GLY B 90  ? 1.62540 1.05633 0.67198 0.62415  0.17130  0.02671  82  GLY B N   
5445 C CA  . GLY B 90  ? 1.64546 1.03413 0.65377 0.62765  0.17241  0.02491  82  GLY B CA  
5446 C C   . GLY B 90  ? 1.65080 1.03398 0.65653 0.63685  0.17394  0.03328  82  GLY B C   
5447 O O   . GLY B 90  ? 1.63349 1.03744 0.66739 0.63289  0.17459  0.04149  82  GLY B O   
5448 N N   . VAL B 91  ? 1.69380 1.04798 0.66443 0.64827  0.17468  0.03128  83  VAL B N   
5449 C CA  . VAL B 91  ? 1.67471 1.02294 0.63640 0.65908  0.17483  0.03451  83  VAL B CA  
5450 C C   . VAL B 91  ? 1.67428 0.99689 0.63980 0.64788  0.17212  0.01915  83  VAL B C   
5451 O O   . VAL B 91  ? 1.71077 1.00934 0.66562 0.63779  0.17511  0.00478  83  VAL B O   
5452 C CB  . VAL B 91  ? 1.71131 1.05103 0.63976 0.68152  0.17591  0.03583  83  VAL B CB  
5453 C CG1 . VAL B 91  ? 1.77308 1.13931 0.70209 0.69424  0.17534  0.04234  83  VAL B CG1 
5454 C CG2 . VAL B 91  ? 1.72141 1.01947 0.62521 0.67862  0.17443  0.02519  83  VAL B CG2 
5455 N N   . ALA B 92  ? 1.70839 1.03567 0.68713 0.64932  0.16646  0.02090  84  ALA B N   
5456 C CA  . ALA B 92  ? 1.70908 1.01889 0.69853 0.64370  0.15880  0.00148  84  ALA B CA  
5457 C C   . ALA B 92  ? 1.75136 1.04916 0.71464 0.66115  0.15694  -0.00497 84  ALA B C   
5458 O O   . ALA B 92  ? 1.82018 1.10859 0.79561 0.64915  0.15159  -0.02593 84  ALA B O   
5459 C CB  . ALA B 92  ? 1.70080 1.01926 0.72041 0.63821  0.14772  0.00641  84  ALA B CB  
5460 N N   . ASP B 93  ? 1.70270 1.01421 0.64541 0.67821  0.15829  0.01281  85  ASP B N   
5461 C CA  . ASP B 93  ? 1.72015 1.03206 0.64240 0.69311  0.15474  0.00799  85  ASP B CA  
5462 C C   . ASP B 93  ? 1.74021 1.07233 0.64327 0.70727  0.16296  0.02326  85  ASP B C   
5463 O O   . ASP B 93  ? 1.72299 1.07174 0.62895 0.70640  0.17092  0.03783  85  ASP B O   
5464 C CB  . ASP B 93  ? 1.73577 1.04576 0.65062 0.70521  0.14394  0.00512  85  ASP B CB  
5465 C CG  . ASP B 93  ? 1.75081 1.06781 0.65355 0.71593  0.13564  -0.00542 85  ASP B CG  
5466 O OD1 . ASP B 93  ? 1.74297 1.06342 0.65758 0.70628  0.13614  -0.01476 85  ASP B OD1 
5467 O OD2 . ASP B 93  ? 1.77580 1.09237 0.65544 0.73469  0.12796  -0.00426 85  ASP B OD2 
5468 N N   . LEU B 94  ? 1.76423 1.10308 0.66138 0.71457  0.15800  0.01768  86  LEU B N   
5469 C CA  . LEU B 94  ? 1.75049 1.11209 0.63963 0.72795  0.16209  0.02383  86  LEU B CA  
5470 C C   . LEU B 94  ? 1.77310 1.14957 0.65456 0.73988  0.15610  0.01565  86  LEU B C   
5471 O O   . LEU B 94  ? 1.81388 1.17674 0.70041 0.73513  0.14656  0.00169  86  LEU B O   
5472 C CB  . LEU B 94  ? 1.74731 1.09086 0.64184 0.72279  0.15979  0.01886  86  LEU B CB  
5473 C CG  . LEU B 94  ? 1.76450 1.12815 0.65519 0.73848  0.16169  0.02363  86  LEU B CG  
5474 C CD1 . LEU B 94  ? 1.74452 1.13728 0.63933 0.74112  0.17192  0.03491  86  LEU B CD1 
5475 C CD2 . LEU B 94  ? 1.82562 1.15585 0.70789 0.73789  0.15628  0.01994  86  LEU B CD2 
5476 N N   . THR B 95  ? 1.77272 1.18199 0.64663 0.75352  0.16159  0.02007  87  THR B N   
5477 C CA  . THR B 95  ? 1.80387 1.23543 0.67257 0.76568  0.15657  0.00893  87  THR B CA  
5478 C C   . THR B 95  ? 1.79411 1.26172 0.66861 0.77655  0.16232  0.00613  87  THR B C   
5479 O O   . THR B 95  ? 1.79056 1.27934 0.66581 0.77591  0.17409  0.01698  87  THR B O   
5480 C CB  . THR B 95  ? 1.83735 1.27905 0.68114 0.77169  0.15719  0.01505  87  THR B CB  
5481 O OG1 . THR B 95  ? 1.82451 1.28906 0.66492 0.78316  0.15039  0.00022  87  THR B OG1 
5482 C CG2 . THR B 95  ? 1.82182 1.28505 0.64549 0.76978  0.17332  0.03713  87  THR B CG2 
5483 N N   . TRP B 96  ? 1.80330 1.28014 0.68573 0.78554  0.15388  -0.01205 88  TRP B N   
5484 C CA  . TRP B 96  ? 1.81383 1.33380 0.70389 0.79943  0.15670  -0.02317 88  TRP B CA  
5485 C C   . TRP B 96  ? 1.82738 1.39254 0.70209 0.80114  0.16922  -0.01774 88  TRP B C   
5486 O O   . TRP B 96  ? 1.89027 1.45055 0.74737 0.80069  0.16571  -0.01654 88  TRP B O   
5487 C CB  . TRP B 96  ? 1.82476 1.33936 0.72721 0.80762  0.14348  -0.04680 88  TRP B CB  
5488 C CG  . TRP B 96  ? 1.82930 1.30803 0.74098 0.80933  0.13484  -0.05270 88  TRP B CG  
5489 C CD1 . TRP B 96  ? 1.83662 1.26594 0.74926 0.79987  0.12713  -0.05890 88  TRP B CD1 
5490 C CD2 . TRP B 96  ? 1.83640 1.32416 0.75410 0.82214  0.13295  -0.05477 88  TRP B CD2 
5491 N NE1 . TRP B 96  ? 1.85456 1.25362 0.76471 0.80629  0.12144  -0.06034 88  TRP B NE1 
5492 C CE2 . TRP B 96  ? 1.85432 1.28852 0.76781 0.82246  0.12193  -0.05847 88  TRP B CE2 
5493 C CE3 . TRP B 96  ? 1.83380 1.37053 0.76046 0.83300  0.13976  -0.05640 88  TRP B CE3 
5494 C CZ2 . TRP B 96  ? 1.87375 1.29704 0.78609 0.83801  0.11311  -0.06155 88  TRP B CZ2 
5495 C CZ3 . TRP B 96  ? 1.84489 1.37963 0.78038 0.84759  0.13082  -0.06422 88  TRP B CZ3 
5496 C CH2 . TRP B 96  ? 1.86645 1.34274 0.79229 0.85222  0.11540  -0.06564 88  TRP B CH2 
5497 N N   . VAL B 97  ? 1.83071 1.43820 0.70967 0.80165  0.18365  -0.01545 89  VAL B N   
5498 C CA  . VAL B 97  ? 1.85376 1.51335 0.71795 0.79868  0.19982  -0.01444 89  VAL B CA  
5499 C C   . VAL B 97  ? 1.88043 1.58575 0.76555 0.81210  0.19693  -0.04374 89  VAL B C   
5500 O O   . VAL B 97  ? 1.85790 1.59967 0.76402 0.81498  0.20497  -0.05463 89  VAL B O   
5501 C CB  . VAL B 97  ? 1.85721 1.53822 0.71482 0.78340  0.22232  0.00437  89  VAL B CB  
5502 C CG1 . VAL B 97  ? 1.89060 1.62399 0.72887 0.77328  0.24322  0.00638  89  VAL B CG1 
5503 C CG2 . VAL B 97  ? 1.85246 1.48578 0.69187 0.77107  0.22292  0.03098  89  VAL B CG2 
5504 N N   . GLY B 98  ? 1.84550 1.56014 0.87374 0.78684  0.10208  -0.01978 90  GLY B N   
5505 C CA  . GLY B 98  ? 1.82019 1.53127 0.84167 0.80658  0.10735  -0.02308 90  GLY B CA  
5506 C C   . GLY B 98  ? 1.91271 1.60866 0.93184 0.81871  0.10003  -0.02303 90  GLY B C   
5507 O O   . GLY B 98  ? 1.87743 1.53313 0.88598 0.80760  0.08851  -0.02677 90  GLY B O   
5508 N N   . GLU B 99  ? 1.78562 1.51391 0.81542 0.84047  0.10716  -0.01870 91  GLU B N   
5509 C CA  . GLU B 99  ? 1.79045 1.50640 0.81619 0.85796  0.10287  -0.01770 91  GLU B CA  
5510 C C   . GLU B 99  ? 1.76147 1.51020 0.80116 0.86927  0.09996  -0.01064 91  GLU B C   
5511 O O   . GLU B 99  ? 1.72876 1.45562 0.75913 0.87556  0.09141  -0.00808 91  GLU B O   
5512 C CB  . GLU B 99  ? 1.80429 1.52846 0.83080 0.87751  0.11303  -0.02115 91  GLU B CB  
5513 C CG  . GLU B 99  ? 1.77065 1.46260 0.78286 0.86881  0.11428  -0.03062 91  GLU B CG  
5514 C CD  . GLU B 99  ? 1.83667 1.47542 0.83367 0.85726  0.10364  -0.03677 91  GLU B CD  
5515 O OE1 . GLU B 99  ? 1.87163 1.49344 0.86535 0.86828  0.10194  -0.03540 91  GLU B OE1 
5516 O OE2 . GLU B 99  ? 1.80609 1.42151 0.79618 0.83711  0.09787  -0.04301 91  GLU B OE2 
5517 N N   . ARG B 100 ? 1.73512 1.53564 0.79698 0.87235  0.10769  -0.00819 92  ARG B N   
5518 C CA  . ARG B 100 ? 1.71021 1.55417 0.79278 0.88542  0.10511  -0.00443 92  ARG B CA  
5519 C C   . ARG B 100 ? 1.73149 1.59635 0.82558 0.86706  0.10281  -0.00449 92  ARG B C   
5520 O O   . ARG B 100 ? 1.70942 1.60932 0.82104 0.87564  0.09795  -0.00375 92  ARG B O   
5521 C CB  . ARG B 100 ? 1.67288 1.57000 0.78140 0.90708  0.11767  -0.00432 92  ARG B CB  
5522 C CG  . ARG B 100 ? 1.75394 1.64083 0.85745 0.93045  0.11600  -0.00369 92  ARG B CG  
5523 C CD  . ARG B 100 ? 1.74388 1.68963 0.87956 0.95214  0.12598  -0.00414 92  ARG B CD  
5524 N NE  . ARG B 100 ? 1.81995 1.76174 0.95492 0.97563  0.12014  -0.00235 92  ARG B NE  
5525 C CZ  . ARG B 100 ? 1.87851 1.78775 0.99718 0.98473  0.12368  -0.00426 92  ARG B CZ  
5526 N NH1 . ARG B 100 ? 1.81365 1.69322 0.91596 0.97297  0.13155  -0.00915 92  ARG B NH1 
5527 N NH2 . ARG B 100 ? 1.85956 1.76679 0.97921 1.00592  0.11891  -0.00185 92  ARG B NH2 
5528 N N   . GLY B 101 ? 1.75944 1.60548 0.84555 0.84308  0.10540  -0.00607 93  GLY B N   
5529 C CA  . GLY B 101 ? 1.65375 1.51726 0.74998 0.82236  0.10503  -0.00638 93  GLY B CA  
5530 C C   . GLY B 101 ? 1.62643 1.44820 0.70715 0.80397  0.08837  -0.00769 93  GLY B C   
5531 O O   . GLY B 101 ? 1.66996 1.44185 0.73117 0.79781  0.08147  -0.00903 93  GLY B O   
5532 N N   . ILE B 102 ? 1.58055 1.42431 0.67177 0.79453  0.08257  -0.00858 94  ILE B N   
5533 C CA  . ILE B 102 ? 1.65056 1.46036 0.73102 0.77379  0.06713  -0.01022 94  ILE B CA  
5534 C C   . ILE B 102 ? 1.56789 1.40070 0.66123 0.74878  0.06844  -0.01189 94  ILE B C   
5535 O O   . ILE B 102 ? 1.55149 1.43322 0.66714 0.74983  0.06866  -0.01175 94  ILE B O   
5536 C CB  . ILE B 102 ? 1.58717 1.39743 0.66225 0.78955  0.05550  -0.00927 94  ILE B CB  
5537 C CG1 . ILE B 102 ? 1.55107 1.33590 0.61135 0.81477  0.05564  -0.00562 94  ILE B CG1 
5538 C CG2 . ILE B 102 ? 1.54924 1.32741 0.61573 0.76631  0.04146  -0.01073 94  ILE B CG2 
5539 C CD1 . ILE B 102 ? 1.57035 1.36258 0.62534 0.83731  0.04704  -0.00221 94  ILE B CD1 
5540 N N   . LEU B 103 ? 1.48919 1.28982 0.57659 0.72452  0.06714  -0.01275 95  LEU B N   
5541 C CA  . LEU B 103 ? 1.52270 1.33550 0.61913 0.69884  0.06814  -0.01325 95  LEU B CA  
5542 C C   . LEU B 103 ? 1.51626 1.30545 0.61201 0.67856  0.05042  -0.01695 95  LEU B C   
5543 O O   . LEU B 103 ? 1.54912 1.29182 0.63475 0.67193  0.04168  -0.01954 95  LEU B O   
5544 C CB  . LEU B 103 ? 1.44733 1.23801 0.53672 0.68746  0.07649  -0.01172 95  LEU B CB  
5545 C CG  . LEU B 103 ? 1.44884 1.25166 0.54424 0.66562  0.08219  -0.00961 95  LEU B CG  
5546 C CD1 . LEU B 103 ? 1.47093 1.32814 0.58004 0.67451  0.10139  -0.00515 95  LEU B CD1 
5547 C CD2 . LEU B 103 ? 1.56101 1.33036 0.64415 0.65496  0.08475  -0.00860 95  LEU B CD2 
5548 N N   . VAL B 104 ? 1.46621 1.28840 0.57387 0.66851  0.04602  -0.01812 96  VAL B N   
5549 C CA  . VAL B 104 ? 1.41709 1.22685 0.52725 0.65119  0.02841  -0.02175 96  VAL B CA  
5550 C C   . VAL B 104 ? 1.36361 1.17563 0.48254 0.62234  0.02677  -0.02427 96  VAL B C   
5551 O O   . VAL B 104 ? 1.35669 1.20449 0.50275 0.61407  0.03659  -0.02040 96  VAL B O   
5552 C CB  . VAL B 104 ? 1.48197 1.33287 0.61095 0.66154  0.01899  -0.02053 96  VAL B CB  
5553 C CG1 . VAL B 104 ? 1.51068 1.34033 0.62827 0.65189  0.00214  -0.02387 96  VAL B CG1 
5554 C CG2 . VAL B 104 ? 1.40527 1.26762 0.52991 0.69430  0.02410  -0.01663 96  VAL B CG2 
5555 N N   . ALA B 105 ? 1.36679 1.14412 0.48586 0.60097  0.01420  -0.02858 97  ALA B N   
5556 C CA  . ALA B 105 ? 1.32792 1.10365 0.45539 0.57339  0.00897  -0.03243 97  ALA B CA  
5557 C C   . ALA B 105 ? 1.34946 1.14396 0.48683 0.56485  -0.00583 -0.03706 97  ALA B C   
5558 O O   . ALA B 105 ? 1.42477 1.19062 0.56028 0.55982  -0.01601 -0.03976 97  ALA B O   
5559 C CB  . ALA B 105 ? 1.36844 1.09477 0.49113 0.55708  0.00550  -0.03570 97  ALA B CB  
5560 N N   . SER B 106 ? 1.30834 1.15363 0.48508 0.55455  -0.00688 -0.03643 98  SER B N   
5561 C CA  . SER B 106 ? 1.29982 1.17817 0.50167 0.54709  -0.02182 -0.04128 98  SER B CA  
5562 C C   . SER B 106 ? 1.28834 1.15678 0.49999 0.51759  -0.03130 -0.04896 98  SER B C   
5563 O O   . SER B 106 ? 1.33745 1.19168 0.55313 0.50114  -0.02416 -0.04876 98  SER B O   
5564 C CB  . SER B 106 ? 1.31220 1.25475 0.55928 0.55126  -0.01881 -0.04006 98  SER B CB  
5565 O OG  . SER B 106 ? 1.26997 1.24639 0.53779 0.54881  -0.03501 -0.04653 98  SER B OG  
5566 N N   . ASP B 107 ? 1.32698 1.20295 0.54114 0.51271  -0.04661 -0.05524 99  ASP B N   
5567 C CA  . ASP B 107 ? 1.27211 1.15061 0.50320 0.48534  -0.05738 -0.06482 99  ASP B CA  
5568 C C   . ASP B 107 ? 1.21759 1.14621 0.50125 0.46818  -0.05427 -0.06789 99  ASP B C   
5569 O O   . ASP B 107 ? 1.23813 1.15916 0.53718 0.44352  -0.05510 -0.07323 99  ASP B O   
5570 C CB  . ASP B 107 ? 1.29457 1.17919 0.51758 0.48820  -0.07329 -0.07052 99  ASP B CB  
5571 C CG  . ASP B 107 ? 1.26662 1.09599 0.44975 0.49379  -0.07488 -0.06876 99  ASP B CG  
5572 O OD1 . ASP B 107 ? 1.26395 1.05412 0.44599 0.47493  -0.07182 -0.07136 99  ASP B OD1 
5573 O OD2 . ASP B 107 ? 1.28119 1.10995 0.45715 0.51086  -0.07723 -0.06346 99  ASP B OD2 
5574 N N   . SER B 108 ? 1.20995 1.18742 0.52196 0.48110  -0.05020 -0.06531 100 SER B N   
5575 C CA  . SER B 108 ? 1.19560 1.22841 0.56503 0.46706  -0.04532 -0.06957 100 SER B CA  
5576 C C   . SER B 108 ? 1.22987 1.24570 0.61001 0.44965  -0.02827 -0.06409 100 SER B C   
5577 O O   . SER B 108 ? 1.24770 1.29619 0.67517 0.42926  -0.02419 -0.06898 100 SER B O   
5578 C CB  . SER B 108 ? 1.23031 1.31141 0.62183 0.48870  -0.04117 -0.06701 100 SER B CB  
5579 O OG  . SER B 108 ? 1.22233 1.28151 0.58845 0.50791  -0.02527 -0.05502 100 SER B OG  
5580 N N   . GLY B 109 ? 1.20981 1.17660 0.54783 0.45824  -0.01852 -0.05479 101 GLY B N   
5581 C CA  . GLY B 109 ? 1.23118 1.17747 0.56823 0.44840  -0.00141 -0.04676 101 GLY B CA  
5582 C C   . GLY B 109 ? 1.30827 1.27415 0.65054 0.46556  0.01788  -0.03633 101 GLY B C   
5583 O O   . GLY B 109 ? 1.33119 1.29269 0.68144 0.45763  0.03524  -0.02823 101 GLY B O   
5584 N N   . ALA B 110 ? 1.31170 1.29779 0.64864 0.48937  0.01566  -0.03597 102 ALA B N   
5585 C CA  . ALA B 110 ? 1.30278 1.31002 0.64362 0.50975  0.03292  -0.02777 102 ALA B CA  
5586 C C   . ALA B 110 ? 1.32757 1.28778 0.61222 0.53306  0.03626  -0.02239 102 ALA B C   
5587 O O   . ALA B 110 ? 1.29048 1.21859 0.54299 0.53982  0.02174  -0.02688 102 ALA B O   
5588 C CB  . ALA B 110 ? 1.25104 1.31518 0.62773 0.52168  0.02717  -0.03291 102 ALA B CB  
5589 N N   . VAL B 111 ? 1.37056 1.32616 0.64462 0.54389  0.05589  -0.01383 103 VAL B N   
5590 C CA  . VAL B 111 ? 1.38324 1.31200 0.61515 0.57183  0.06218  -0.01052 103 VAL B CA  
5591 C C   . VAL B 111 ? 1.39780 1.37468 0.65616 0.59169  0.06947  -0.00882 103 VAL B C   
5592 O O   . VAL B 111 ? 1.39915 1.41832 0.69737 0.58466  0.08379  -0.00531 103 VAL B O   
5593 C CB  . VAL B 111 ? 1.45489 1.35118 0.65671 0.57330  0.07868  -0.00373 103 VAL B CB  
5594 C CG1 . VAL B 111 ? 1.48748 1.35886 0.64833 0.60194  0.08486  -0.00340 103 VAL B CG1 
5595 C CG2 . VAL B 111 ? 1.46892 1.32255 0.64936 0.55400  0.07035  -0.00621 103 VAL B CG2 
5596 N N   . GLU B 112 ? 1.43861 1.40978 0.67839 0.61522  0.06051  -0.01145 104 GLU B N   
5597 C CA  . GLU B 112 ? 1.50352 1.52036 0.76759 0.63763  0.06434  -0.01086 104 GLU B CA  
5598 C C   . GLU B 112 ? 1.46477 1.45157 0.68889 0.66787  0.07038  -0.00868 104 GLU B C   
5599 O O   . GLU B 112 ? 1.47356 1.40829 0.65555 0.67289  0.06216  -0.01084 104 GLU B O   
5600 C CB  . GLU B 112 ? 1.48602 1.53757 0.77737 0.63757  0.04484  -0.01695 104 GLU B CB  
5601 C CG  . GLU B 112 ? 1.49143 1.50219 0.74958 0.63596  0.02532  -0.02025 104 GLU B CG  
5602 C CD  . GLU B 112 ? 1.56261 1.60908 0.84573 0.63352  0.00608  -0.02610 104 GLU B CD  
5603 O OE1 . GLU B 112 ? 1.61019 1.71664 0.94155 0.63039  0.00586  -0.03002 104 GLU B OE1 
5604 O OE2 . GLU B 112 ? 1.63996 1.65517 0.89447 0.63528  -0.00830 -0.02754 104 GLU B OE2 
5605 N N   . LEU B 113 ? 1.50669 1.52594 0.74664 0.68626  0.08562  -0.00577 105 LEU B N   
5606 C CA  . LEU B 113 ? 1.57110 1.57185 0.78154 0.71757  0.09334  -0.00498 105 LEU B CA  
5607 C C   . LEU B 113 ? 1.61598 1.65618 0.85042 0.74025  0.08575  -0.00646 105 LEU B C   
5608 O O   . LEU B 113 ? 1.51073 1.60996 0.79165 0.74011  0.09198  -0.00680 105 LEU B O   
5609 C CB  . LEU B 113 ? 1.56517 1.57468 0.77505 0.72198  0.11805  -0.00076 105 LEU B CB  
5610 C CG  . LEU B 113 ? 1.46858 1.46891 0.65538 0.75422  0.12909  -0.00152 105 LEU B CG  
5611 C CD1 . LEU B 113 ? 1.48772 1.42231 0.61976 0.76405  0.12277  -0.00590 105 LEU B CD1 
5612 C CD2 . LEU B 113 ? 1.48241 1.50609 0.67817 0.75728  0.15497  0.00298  105 LEU B CD2 
5613 N N   . TRP B 114 ? 1.65152 1.66006 0.85662 0.75902  0.07306  -0.00751 106 TRP B N   
5614 C CA  . TRP B 114 ? 1.68542 1.72186 0.90336 0.78648  0.06481  -0.00730 106 TRP B CA  
5615 C C   . TRP B 114 ? 1.72011 1.74134 0.91780 0.81734  0.07837  -0.00635 106 TRP B C   
5616 O O   . TRP B 114 ? 1.72460 1.69033 0.88080 0.82065  0.08421  -0.00734 106 TRP B O   
5617 C CB  . TRP B 114 ? 1.71748 1.72682 0.91483 0.78857  0.04388  -0.00698 106 TRP B CB  
5618 C CG  . TRP B 114 ? 1.71560 1.74642 0.93540 0.76113  0.02965  -0.00973 106 TRP B CG  
5619 C CD1 . TRP B 114 ? 1.68154 1.68436 0.89146 0.73131  0.02724  -0.01180 106 TRP B CD1 
5620 C CD2 . TRP B 114 ? 1.65299 1.73950 0.91002 0.76187  0.01505  -0.01260 106 TRP B CD2 
5621 N NE1 . TRP B 114 ? 1.63481 1.67057 0.87350 0.71276  0.01319  -0.01567 106 TRP B NE1 
5622 C CE2 . TRP B 114 ? 1.62307 1.71118 0.89077 0.73076  0.00512  -0.01691 106 TRP B CE2 
5623 C CE3 . TRP B 114 ? 1.57440 1.71106 0.85737 0.78678  0.00847  -0.01338 106 TRP B CE3 
5624 C CZ2 . TRP B 114 ? 1.63966 1.77788 0.94263 0.72339  -0.01082 -0.02301 106 TRP B CZ2 
5625 C CZ3 . TRP B 114 ? 1.56835 1.75589 0.88575 0.78037  -0.00834 -0.01931 106 TRP B CZ3 
5626 C CH2 . TRP B 114 ? 1.61709 1.80538 0.94411 0.74875  -0.01778 -0.02457 106 TRP B CH2 
5627 N N   . GLU B 115 ? 1.85682 1.92771 1.08526 0.83902  0.08293  -0.00641 107 GLU B N   
5628 C CA  . GLU B 115 ? 1.86711 1.93451 1.08494 0.86990  0.09722  -0.00671 107 GLU B CA  
5629 C C   . GLU B 115 ? 1.87181 1.92434 1.07468 0.90087  0.08466  -0.00513 107 GLU B C   
5630 O O   . GLU B 115 ? 1.79272 1.88787 1.02399 0.90940  0.07125  -0.00423 107 GLU B O   
5631 C CB  . GLU B 115 ? 1.84514 1.97951 1.11027 0.87433  0.11222  -0.00822 107 GLU B CB  
5632 C CG  . GLU B 115 ? 1.83554 1.96548 1.08888 0.89942  0.13218  -0.00950 107 GLU B CG  
5633 C CD  . GLU B 115 ? 1.85689 1.96186 1.08784 0.88569  0.15236  -0.00907 107 GLU B CD  
5634 O OE1 . GLU B 115 ? 1.88692 1.95389 1.09352 0.86195  0.14793  -0.00768 107 GLU B OE1 
5635 O OE2 . GLU B 115 ? 1.88572 2.00912 1.12661 0.89367  0.16927  -0.00823 107 GLU B OE2 
5636 N N   . LEU B 116 ? 1.80396 1.79821 0.96671 0.91211  0.08695  -0.00354 108 LEU B N   
5637 C CA  . LEU B 116 ? 1.78554 1.75805 0.93368 0.93398  0.07710  0.00188  108 LEU B CA  
5638 C C   . LEU B 116 ? 1.76894 1.79040 0.94678 0.95720  0.08455  0.00152  108 LEU B C   
5639 O O   . LEU B 116 ? 1.78190 1.82201 0.97296 0.95366  0.10089  -0.00173 108 LEU B O   
5640 C CB  . LEU B 116 ? 1.81609 1.71507 0.92285 0.92429  0.07786  0.00402  108 LEU B CB  
5641 C CG  . LEU B 116 ? 1.83527 1.69495 0.91755 0.93784  0.06907  0.00962  108 LEU B CG  
5642 C CD1 . LEU B 116 ? 1.78132 1.63470 0.85520 0.93634  0.05462  0.01337  108 LEU B CD1 
5643 C CD2 . LEU B 116 ? 1.81930 1.61340 0.87027 0.92581  0.07298  0.00861  108 LEU B CD2 
5644 N N   . ASP B 117 ? 1.75515 1.79698 0.94262 0.97924  0.07294  0.00492  109 ASP B N   
5645 C CA  . ASP B 117 ? 1.76750 1.86734 0.99138 1.00218  0.07585  0.00322  109 ASP B CA  
5646 C C   . ASP B 117 ? 1.81557 1.89103 1.02642 1.01015  0.08968  0.00318  109 ASP B C   
5647 O O   . ASP B 117 ? 1.81177 1.82474 0.98504 0.99897  0.09351  0.00468  109 ASP B O   
5648 C CB  . ASP B 117 ? 1.74132 1.85894 0.97024 1.02210  0.05704  0.00751  109 ASP B CB  
5649 C CG  . ASP B 117 ? 1.75657 1.95800 1.03915 1.03868  0.05260  0.00219  109 ASP B CG  
5650 O OD1 . ASP B 117 ? 1.79645 2.05038 1.11927 1.02924  0.06029  -0.00547 109 ASP B OD1 
5651 O OD2 . ASP B 117 ? 1.78249 1.99658 1.06750 1.05999  0.04215  0.00497  109 ASP B OD2 
5652 N N   . GLU B 118 ? 1.83265 1.95833 1.07673 1.02852  0.09604  0.00012  110 GLU B N   
5653 C CA  . GLU B 118 ? 1.86524 1.97608 1.10241 1.04122  0.10765  -0.00096 110 GLU B CA  
5654 C C   . GLU B 118 ? 1.89958 1.95650 1.10215 1.05397  0.09766  0.00484  110 GLU B C   
5655 O O   . GLU B 118 ? 1.92683 1.94221 1.10764 1.05557  0.10620  0.00384  110 GLU B O   
5656 C CB  . GLU B 118 ? 1.87807 2.06147 1.16407 1.05859  0.11491  -0.00631 110 GLU B CB  
5657 C CG  . GLU B 118 ? 1.91430 2.09048 1.19875 1.06947  0.13002  -0.00944 110 GLU B CG  
5658 C CD  . GLU B 118 ? 2.06455 2.22749 1.34025 1.05194  0.14979  -0.01277 110 GLU B CD  
5659 O OE1 . GLU B 118 ? 2.09180 2.25239 1.36386 1.03033  0.15321  -0.01216 110 GLU B OE1 
5660 O OE2 . GLU B 118 ? 2.03101 2.18610 1.30287 1.06033  0.16167  -0.01610 110 GLU B OE2 
5661 N N   . ASN B 119 ? 1.88364 1.94212 1.08220 1.06220  0.08113  0.01026  111 ASN B N   
5662 C CA  . ASN B 119 ? 1.85289 1.85914 1.01725 1.07286  0.07312  0.01765  111 ASN B CA  
5663 C C   . ASN B 119 ? 1.82077 1.76502 0.94623 1.05171  0.06879  0.02179  111 ASN B C   
5664 O O   . ASN B 119 ? 1.85688 1.74663 0.95108 1.05498  0.06767  0.02719  111 ASN B O   
5665 C CB  . ASN B 119 ? 1.80700 1.85139 0.98732 1.09473  0.05858  0.02173  111 ASN B CB  
5666 C CG  . ASN B 119 ? 1.83150 1.91475 1.03890 1.12001  0.06201  0.01884  111 ASN B CG  
5667 O OD1 . ASN B 119 ? 1.83086 1.92804 1.05452 1.12054  0.07608  0.01245  111 ASN B OD1 
5668 N ND2 . ASN B 119 ? 1.85535 1.95660 1.06726 1.14118  0.04940  0.02316  111 ASN B ND2 
5669 N N   . GLU B 120 ? 1.80273 1.75524 0.93229 1.03062  0.06771  0.01887  112 GLU B N   
5670 C CA  . GLU B 120 ? 1.82041 1.72283 0.91905 1.00886  0.06226  0.02121  112 GLU B CA  
5671 C C   . GLU B 120 ? 1.80816 1.70666 0.89603 1.01668  0.04797  0.02821  112 GLU B C   
5672 O O   . GLU B 120 ? 1.86413 1.70337 0.91720 1.00885  0.04708  0.03274  112 GLU B O   
5673 C CB  . GLU B 120 ? 1.83172 1.66409 0.89672 0.99683  0.07061  0.02040  112 GLU B CB  
5674 C CG  . GLU B 120 ? 1.85075 1.68698 0.92414 0.99031  0.08361  0.01317  112 GLU B CG  
5675 C CD  . GLU B 120 ? 1.91528 1.68748 0.96043 0.97650  0.08894  0.00979  112 GLU B CD  
5676 O OE1 . GLU B 120 ? 1.96034 1.68430 0.98205 0.97490  0.08504  0.01323  112 GLU B OE1 
5677 O OE2 . GLU B 120 ? 1.85777 1.62987 0.90611 0.96684  0.09741  0.00319  112 GLU B OE2 
5678 N N   . THR B 121 ? 1.75294 1.71448 0.87179 1.03062  0.03761  0.02821  113 THR B N   
5679 C CA  . THR B 121 ? 1.77233 1.74328 0.88573 1.04003  0.02208  0.03397  113 THR B CA  
5680 C C   . THR B 121 ? 1.74425 1.77315 0.88860 1.03216  0.00882  0.02938  113 THR B C   
5681 O O   . THR B 121 ? 1.73643 1.79426 0.88770 1.04178  -0.00637 0.03147  113 THR B O   
5682 C CB  . THR B 121 ? 1.78562 1.77960 0.90810 1.06869  0.01910  0.03749  113 THR B CB  
5683 O OG1 . THR B 121 ? 1.76799 1.83301 0.93701 1.07951  0.01956  0.03003  113 THR B OG1 
5684 C CG2 . THR B 121 ? 1.82887 1.76411 0.92238 1.07685  0.03133  0.04221  113 THR B CG2 
5685 N N   . LEU B 122 ? 1.72116 1.76561 0.88339 1.01477  0.01445  0.02291  114 LEU B N   
5686 C CA  . LEU B 122 ? 1.73523 1.83996 0.93579 1.00635  0.00426  0.01683  114 LEU B CA  
5687 C C   . LEU B 122 ? 1.66225 1.75524 0.86696 0.98433  0.01729  0.01119  114 LEU B C   
5688 O O   . LEU B 122 ? 1.70891 1.79045 0.91252 0.98264  0.03538  0.00846  114 LEU B O   
5689 C CB  . LEU B 122 ? 1.67844 1.86538 0.93073 1.02517  0.00055  0.01080  114 LEU B CB  
5690 C CG  . LEU B 122 ? 1.67940 1.93952 0.98576 1.01490  -0.00371 0.00052  114 LEU B CG  
5691 C CD1 . LEU B 122 ? 1.64383 1.91608 0.94992 0.99962  -0.02614 0.00024  114 LEU B CD1 
5692 C CD2 . LEU B 122 ? 1.57637 1.91523 0.93713 1.03364  -0.00216 -0.00788 114 LEU B CD2 
5693 N N   . ILE B 123 ? 1.61500 1.70811 0.82169 0.95468  0.00828  0.00933  115 ILE B N   
5694 C CA  . ILE B 123 ? 1.63778 1.71446 0.84490 0.91712  0.01880  0.00445  115 ILE B CA  
5695 C C   . ILE B 123 ? 1.59860 1.74395 0.85733 0.89311  0.01396  -0.00264 115 ILE B C   
5696 O O   . ILE B 123 ? 1.61503 1.78251 0.88438 0.88552  -0.00445 -0.00408 115 ILE B O   
5697 C CB  . ILE B 123 ? 1.65594 1.66377 0.81884 0.89938  0.01356  0.00761  115 ILE B CB  
5698 C CG1 . ILE B 123 ? 1.66866 1.61129 0.78623 0.92469  0.01763  0.01372  115 ILE B CG1 
5699 C CG2 . ILE B 123 ? 1.64764 1.63553 0.80792 0.86519  0.02375  0.00253  115 ILE B CG2 
5700 C CD1 . ILE B 123 ? 1.60202 1.48416 0.68128 0.91205  0.01031  0.01732  115 ILE B CD1 
5701 N N   . VAL B 124 ? 1.61785 1.79582 0.90786 0.88249  0.03084  -0.00729 116 VAL B N   
5702 C CA  . VAL B 124 ? 1.56163 1.80863 0.90925 0.86069  0.03130  -0.01487 116 VAL B CA  
5703 C C   . VAL B 124 ? 1.65909 1.88644 1.00643 0.82545  0.04592  -0.01529 116 VAL B C   
5704 O O   . VAL B 124 ? 1.65985 1.84172 0.97423 0.82704  0.06164  -0.01128 116 VAL B O   
5705 C CB  . VAL B 124 ? 1.46366 1.77530 0.85680 0.88159  0.04055  -0.01955 116 VAL B CB  
5706 C CG1 . VAL B 124 ? 1.49648 1.80353 0.87229 0.92411  0.03393  -0.01608 116 VAL B CG1 
5707 C CG2 . VAL B 124 ? 1.46319 1.77857 0.86768 0.87277  0.06810  -0.01969 116 VAL B CG2 
5708 N N   . SER B 125 ? 1.63073 1.89204 1.01403 0.79607  0.04059  -0.02068 117 SER B N   
5709 C CA  . SER B 125 ? 1.59277 1.83927 0.98098 0.76111  0.05290  -0.02041 117 SER B CA  
5710 C C   . SER B 125 ? 1.50771 1.78619 0.92651 0.75906  0.07870  -0.01981 117 SER B C   
5711 O O   . SER B 125 ? 1.49792 1.84119 0.96808 0.76568  0.08152  -0.02572 117 SER B O   
5712 C CB  . SER B 125 ? 1.52813 1.80164 0.94799 0.73287  0.03857  -0.02725 117 SER B CB  
5713 O OG  . SER B 125 ? 1.57095 1.82453 0.99300 0.70078  0.05009  -0.02583 117 SER B OG  
5714 N N   . LYS B 126 ? 1.49375 1.72938 0.88177 0.75116  0.09690  -0.01355 118 LYS B N   
5715 C CA  . LYS B 126 ? 1.50859 1.76603 0.91733 0.74625  0.12467  -0.01054 118 LYS B CA  
5716 C C   . LYS B 126 ? 1.42692 1.69501 0.86363 0.70950  0.13172  -0.00972 118 LYS B C   
5717 O O   . LYS B 126 ? 1.38378 1.70898 0.87744 0.69892  0.14252  -0.01321 118 LYS B O   
5718 C CB  . LYS B 126 ? 1.54261 1.74745 0.89814 0.76080  0.14000  -0.00446 118 LYS B CB  
5719 C CG  . LYS B 126 ? 1.59519 1.78677 0.92516 0.79735  0.13678  -0.00591 118 LYS B CG  
5720 C CD  . LYS B 126 ? 1.64097 1.89140 1.01124 0.81905  0.14834  -0.00877 118 LYS B CD  
5721 C CE  . LYS B 126 ? 1.53846 1.83577 0.94571 0.83084  0.12835  -0.01459 118 LYS B CE  
5722 N NZ  . LYS B 126 ? 1.54830 1.89647 0.98835 0.85803  0.13809  -0.01853 118 LYS B NZ  
5723 N N   . PHE B 127 ? 1.40745 1.62243 0.80782 0.69100  0.12625  -0.00609 119 PHE B N   
5724 C CA  . PHE B 127 ? 1.42318 1.63926 0.84542 0.65598  0.12888  -0.00529 119 PHE B CA  
5725 C C   . PHE B 127 ? 1.43807 1.62218 0.84043 0.64249  0.10333  -0.00967 119 PHE B C   
5726 O O   . PHE B 127 ? 1.43224 1.57128 0.78667 0.65721  0.09112  -0.00924 119 PHE B O   
5727 C CB  . PHE B 127 ? 1.47484 1.66021 0.87436 0.64668  0.15331  0.00492  119 PHE B CB  
5728 C CG  . PHE B 127 ? 1.47910 1.59422 0.81262 0.65029  0.14908  0.00908  119 PHE B CG  
5729 C CD1 . PHE B 127 ? 1.42449 1.50316 0.74089 0.62894  0.13477  0.00798  119 PHE B CD1 
5730 C CD2 . PHE B 127 ? 1.49521 1.58267 0.78635 0.67465  0.16022  0.01232  119 PHE B CD2 
5731 C CE1 . PHE B 127 ? 1.45054 1.46818 0.71049 0.63228  0.13069  0.00946  119 PHE B CE1 
5732 C CE2 . PHE B 127 ? 1.48643 1.51268 0.72069 0.67776  0.15577  0.01298  119 PHE B CE2 
5733 C CZ  . PHE B 127 ? 1.47794 1.47009 0.69755 0.65660  0.14079  0.01135  119 PHE B CZ  
5734 N N   . CYS B 128 ? 1.36437 1.57365 0.80621 0.61535  0.09657  -0.01494 120 CYS B N   
5735 C CA  . CYS B 128 ? 1.37993 1.56269 0.81006 0.59576  0.07575  -0.01981 120 CYS B CA  
5736 C C   . CYS B 128 ? 1.35723 1.54545 0.81831 0.56238  0.08544  -0.01942 120 CYS B C   
5737 O O   . CYS B 128 ? 1.32716 1.56686 0.84553 0.54714  0.08355  -0.02774 120 CYS B O   
5738 C CB  . CYS B 128 ? 1.38621 1.60417 0.83810 0.60187  0.05188  -0.03035 120 CYS B CB  
5739 S SG  . CYS B 128 ? 1.32516 1.52182 0.77148 0.57588  0.02850  -0.03825 120 CYS B SG  
5740 N N   . LYS B 129 ? 1.30123 1.43888 0.72681 0.55275  0.09567  -0.01079 121 LYS B N   
5741 C CA  . LYS B 129 ? 1.29084 1.42635 0.73899 0.52589  0.11185  -0.00551 121 LYS B CA  
5742 C C   . LYS B 129 ? 1.31190 1.41462 0.75018 0.50265  0.09536  -0.00999 121 LYS B C   
5743 O O   . LYS B 129 ? 1.36429 1.41243 0.75001 0.50691  0.08832  -0.00712 121 LYS B O   
5744 C CB  . LYS B 129 ? 1.37824 1.48226 0.79144 0.53497  0.13600  0.00841  121 LYS B CB  
5745 C CG  . LYS B 129 ? 1.41383 1.55495 0.84497 0.55338  0.15774  0.01308  121 LYS B CG  
5746 C CD  . LYS B 129 ? 1.36220 1.55735 0.86075 0.53540  0.17622  0.01319  121 LYS B CD  
5747 C CE  . LYS B 129 ? 1.34521 1.58862 0.87200 0.55441  0.19304  0.01296  121 LYS B CE  
5748 N NZ  . LYS B 129 ? 1.33877 1.63305 0.93412 0.53461  0.21432  0.01239  121 LYS B NZ  
5749 N N   . TYR B 130 ? 1.29989 1.43675 0.78998 0.47890  0.08994  -0.01852 122 TYR B N   
5750 C CA  . TYR B 130 ? 1.28985 1.40447 0.78224 0.45400  0.07527  -0.02501 122 TYR B CA  
5751 C C   . TYR B 130 ? 1.24386 1.32732 0.73284 0.43570  0.09381  -0.01414 122 TYR B C   
5752 O O   . TYR B 130 ? 1.23580 1.34521 0.77548 0.41304  0.10391  -0.01579 122 TYR B O   
5753 C CB  . TYR B 130 ? 1.25469 1.42314 0.80709 0.43783  0.06257  -0.04067 122 TYR B CB  
5754 C CG  . TYR B 130 ? 1.23029 1.43442 0.78757 0.45764  0.04381  -0.05088 122 TYR B CG  
5755 C CD1 . TYR B 130 ? 1.24822 1.42795 0.76867 0.46538  0.02019  -0.05635 122 TYR B CD1 
5756 C CD2 . TYR B 130 ? 1.20560 1.46832 0.80486 0.46935  0.05019  -0.05494 122 TYR B CD2 
5757 C CE1 . TYR B 130 ? 1.25949 1.46909 0.78023 0.48574  0.00365  -0.06338 122 TYR B CE1 
5758 C CE2 . TYR B 130 ? 1.20367 1.49960 0.80593 0.49028  0.03180  -0.06376 122 TYR B CE2 
5759 C CZ  . TYR B 130 ? 1.26890 1.53690 0.82980 0.49916  0.00849  -0.06695 122 TYR B CZ  
5760 O OH  . TYR B 130 ? 1.24491 1.54247 0.80439 0.52186  -0.00894 -0.07331 122 TYR B OH  
5761 N N   . GLU B 131 ? 1.26312 1.29266 0.69465 0.44616  0.09819  -0.00395 123 GLU B N   
5762 C CA  . GLU B 131 ? 1.30004 1.29489 0.71631 0.43551  0.11598  0.00900  123 GLU B CA  
5763 C C   . GLU B 131 ? 1.27321 1.21995 0.66037 0.42280  0.09920  0.00520  123 GLU B C   
5764 O O   . GLU B 131 ? 1.27990 1.20752 0.67294 0.40631  0.10916  0.01243  123 GLU B O   
5765 C CB  . GLU B 131 ? 1.31241 1.28709 0.68594 0.45923  0.13443  0.02230  123 GLU B CB  
5766 C CG  . GLU B 131 ? 1.32481 1.34379 0.73402 0.46450  0.16017  0.02986  123 GLU B CG  
5767 C CD  . GLU B 131 ? 1.34780 1.37602 0.79405 0.44240  0.18396  0.04022  123 GLU B CD  
5768 O OE1 . GLU B 131 ? 1.39692 1.38338 0.80901 0.44064  0.19557  0.05342  123 GLU B OE1 
5769 O OE2 . GLU B 131 ? 1.39347 1.47024 0.90331 0.42734  0.19074  0.03456  123 GLU B OE2 
5770 N N   . HIS B 132 ? 1.29000 1.21696 0.64755 0.43057  0.07611  -0.00522 124 HIS B N   
5771 C CA  . HIS B 132 ? 1.27914 1.16456 0.61309 0.41832  0.05834  -0.01224 124 HIS B CA  
5772 C C   . HIS B 132 ? 1.26049 1.17202 0.64089 0.39392  0.04502  -0.02460 124 HIS B C   
5773 O O   . HIS B 132 ? 1.21196 1.17245 0.63244 0.39289  0.04270  -0.03115 124 HIS B O   
5774 C CB  . HIS B 132 ? 1.25722 1.10961 0.54111 0.43693  0.04277  -0.01835 124 HIS B CB  
5775 C CG  . HIS B 132 ? 1.32193 1.13473 0.55556 0.45520  0.05175  -0.01063 124 HIS B CG  
5776 N ND1 . HIS B 132 ? 1.31773 1.09368 0.52848 0.44869  0.05562  -0.00587 124 HIS B ND1 
5777 C CD2 . HIS B 132 ? 1.35074 1.15522 0.55218 0.48074  0.05654  -0.00838 124 HIS B CD2 
5778 C CE1 . HIS B 132 ? 1.35043 1.09925 0.51636 0.46973  0.06171  -0.00184 124 HIS B CE1 
5779 N NE2 . HIS B 132 ? 1.35687 1.12208 0.51722 0.48888  0.06286  -0.00379 124 HIS B NE2 
5780 N N   . ASP B 133 ? 1.21691 1.09799 0.59201 0.37620  0.03582  -0.02914 125 ASP B N   
5781 C CA  . ASP B 133 ? 1.19235 1.09259 0.60994 0.35107  0.02376  -0.04212 125 ASP B CA  
5782 C C   . ASP B 133 ? 1.17750 1.06229 0.57262 0.35163  -0.00067 -0.05619 125 ASP B C   
5783 O O   . ASP B 133 ? 1.15823 1.05551 0.58179 0.33226  -0.01276 -0.06882 125 ASP B O   
5784 C CB  . ASP B 133 ? 1.19640 1.07388 0.62775 0.33038  0.03257  -0.03717 125 ASP B CB  
5785 C CG  . ASP B 133 ? 1.20796 1.11114 0.67954 0.32260  0.05755  -0.02566 125 ASP B CG  
5786 O OD1 . ASP B 133 ? 1.21621 1.14895 0.69568 0.33646  0.06994  -0.01975 125 ASP B OD1 
5787 O OD2 . ASP B 133 ? 1.27510 1.16835 0.77166 0.30261  0.06535  -0.02295 125 ASP B OD2 
5788 N N   . ASP B 134 ? 1.18808 1.04652 0.53529 0.37269  -0.00642 -0.05470 126 ASP B N   
5789 C CA  . ASP B 134 ? 1.18094 1.02061 0.50292 0.37529  -0.02615 -0.06620 126 ASP B CA  
5790 C C   . ASP B 134 ? 1.25300 1.08262 0.53752 0.40278  -0.02602 -0.06205 126 ASP B C   
5791 O O   . ASP B 134 ? 1.31850 1.15675 0.59845 0.41832  -0.01162 -0.05166 126 ASP B O   
5792 C CB  . ASP B 134 ? 1.19468 0.98679 0.49330 0.36315  -0.03331 -0.07109 126 ASP B CB  
5793 C CG  . ASP B 134 ? 1.20253 0.98555 0.49606 0.35402  -0.05211 -0.08582 126 ASP B CG  
5794 O OD1 . ASP B 134 ? 1.15838 0.96550 0.45530 0.36141  -0.06002 -0.09050 126 ASP B OD1 
5795 O OD2 . ASP B 134 ? 1.20820 0.96012 0.49340 0.34066  -0.05836 -0.09230 126 ASP B OD2 
5796 N N   . ILE B 135 ? 1.29260 1.10384 0.55221 0.40839  -0.04008 -0.06982 127 ILE B N   
5797 C CA  . ILE B 135 ? 1.24881 1.04221 0.47101 0.43382  -0.04054 -0.06687 127 ILE B CA  
5798 C C   . ILE B 135 ? 1.33199 1.09540 0.52460 0.44792  -0.02710 -0.05866 127 ILE B C   
5799 O O   . ILE B 135 ? 1.28710 1.01582 0.46315 0.43916  -0.02652 -0.06045 127 ILE B O   
5800 C CB  . ILE B 135 ? 1.25741 1.01800 0.45239 0.43221  -0.05425 -0.07605 127 ILE B CB  
5801 C CG1 . ILE B 135 ? 1.22707 1.01983 0.44480 0.42357  -0.06731 -0.08356 127 ILE B CG1 
5802 C CG2 . ILE B 135 ? 1.22604 0.95945 0.40092 0.45042  -0.05074 -0.07056 127 ILE B CG2 
5803 C CD1 . ILE B 135 ? 1.19101 0.95326 0.39373 0.41333  -0.07830 -0.09219 127 ILE B CD1 
5804 N N   . VAL B 136 ? 1.35605 1.13393 0.54230 0.47009  -0.01736 -0.05101 128 VAL B N   
5805 C CA  . VAL B 136 ? 1.34107 1.08876 0.49161 0.48914  -0.00614 -0.04569 128 VAL B CA  
5806 C C   . VAL B 136 ? 1.34137 1.05426 0.48575 0.49146  -0.01554 -0.04987 128 VAL B C   
5807 O O   . VAL B 136 ? 1.34605 1.07016 0.49258 0.50182  -0.02056 -0.05020 128 VAL B O   
5808 C CB  . VAL B 136 ? 1.28966 1.06968 0.45012 0.50835  0.00852  -0.03617 128 VAL B CB  
5809 C CG1 . VAL B 136 ? 1.31219 1.06425 0.43900 0.52418  0.02164  -0.03139 128 VAL B CG1 
5810 C CG2 . VAL B 136 ? 1.27618 1.10605 0.48499 0.49534  0.01662  -0.03109 128 VAL B CG2 
5811 N N   . SER B 137 ? 1.32007 0.99444 0.46154 0.48133  -0.01778 -0.05272 129 SER B N   
5812 C CA  . SER B 137 ? 1.35149 0.99186 0.49442 0.47672  -0.02641 -0.05837 129 SER B CA  
5813 C C   . SER B 137 ? 1.42989 1.04782 0.56127 0.49319  -0.02047 -0.05587 129 SER B C   
5814 O O   . SER B 137 ? 1.47555 1.07100 0.60437 0.49666  -0.02473 -0.05861 129 SER B O   
5815 C CB  . SER B 137 ? 1.30964 0.92776 0.46067 0.45316  -0.03503 -0.06593 129 SER B CB  
5816 O OG  . SER B 137 ? 1.46239 1.07152 0.60818 0.45001  -0.03052 -0.06441 129 SER B OG  
5817 N N   . THR B 138 ? 1.38238 1.00512 0.50537 0.50317  -0.01052 -0.05087 130 THR B N   
5818 C CA  . THR B 138 ? 1.50022 1.10350 0.61187 0.51842  -0.00579 -0.04994 130 THR B CA  
5819 C C   . THR B 138 ? 1.45515 1.08226 0.55784 0.53711  0.00872  -0.04148 130 THR B C   
5820 O O   . THR B 138 ? 1.44343 1.09166 0.54654 0.53273  0.01618  -0.03640 130 THR B O   
5821 C CB  . THR B 138 ? 1.45258 1.02601 0.56330 0.50624  -0.01199 -0.05601 130 THR B CB  
5822 O OG1 . THR B 138 ? 1.45669 1.01696 0.55588 0.52159  -0.00824 -0.05591 130 THR B OG1 
5823 C CG2 . THR B 138 ? 1.44765 1.02681 0.55869 0.49474  -0.01021 -0.05434 130 THR B CG2 
5824 N N   . VAL B 139 ? 1.44951 1.07249 0.54352 0.55729  0.01356  -0.03981 131 VAL B N   
5825 C CA  . VAL B 139 ? 1.45877 1.10077 0.54368 0.57703  0.02814  -0.03278 131 VAL B CA  
5826 C C   . VAL B 139 ? 1.44556 1.06142 0.51905 0.58865  0.02733  -0.03616 131 VAL B C   
5827 O O   . VAL B 139 ? 1.44877 1.03866 0.52159 0.58676  0.01749  -0.04227 131 VAL B O   
5828 C CB  . VAL B 139 ? 1.47587 1.15345 0.56398 0.59440  0.03595  -0.02729 131 VAL B CB  
5829 C CG1 . VAL B 139 ? 1.48723 1.20173 0.58430 0.58660  0.04202  -0.02289 131 VAL B CG1 
5830 C CG2 . VAL B 139 ? 1.52480 1.19382 0.61442 0.60118  0.02632  -0.03049 131 VAL B CG2 
5831 N N   . SER B 140 ? 1.46802 1.09171 0.53181 0.60009  0.03823  -0.03207 132 SER B N   
5832 C CA  . SER B 140 ? 1.49714 1.10299 0.54848 0.61318  0.03863  -0.03557 132 SER B CA  
5833 C C   . SER B 140 ? 1.47527 1.10563 0.51802 0.63053  0.05547  -0.02786 132 SER B C   
5834 O O   . SER B 140 ? 1.46505 1.10951 0.50615 0.62516  0.06457  -0.02146 132 SER B O   
5835 C CB  . SER B 140 ? 1.43928 1.01716 0.48714 0.59988  0.02808  -0.04336 132 SER B CB  
5836 O OG  . SER B 140 ? 1.53108 1.09261 0.56835 0.61066  0.02557  -0.04949 132 SER B OG  
5837 N N   . VAL B 141 ? 1.48439 1.11959 0.52144 0.65049  0.06071  -0.02773 133 VAL B N   
5838 C CA  . VAL B 141 ? 1.50899 1.16816 0.53857 0.66860  0.07769  -0.02135 133 VAL B CA  
5839 C C   . VAL B 141 ? 1.52917 1.16969 0.54345 0.67001  0.07684  -0.02539 133 VAL B C   
5840 O O   . VAL B 141 ? 1.53157 1.14363 0.54139 0.66680  0.06337  -0.03547 133 VAL B O   
5841 C CB  . VAL B 141 ? 1.52308 1.19574 0.55372 0.69000  0.08274  -0.02069 133 VAL B CB  
5842 C CG1 . VAL B 141 ? 1.56479 1.20673 0.58522 0.69730  0.07332  -0.02935 133 VAL B CG1 
5843 C CG2 . VAL B 141 ? 1.54207 1.24994 0.57219 0.70630  0.10267  -0.01305 133 VAL B CG2 
5844 N N   . LEU B 142 ? 1.54498 1.20200 0.55108 0.67441  0.09121  -0.01780 134 LEU B N   
5845 C CA  . LEU B 142 ? 1.56951 1.21340 0.55774 0.67891  0.09186  -0.02036 134 LEU B CA  
5846 C C   . LEU B 142 ? 1.59709 1.24280 0.57595 0.69891  0.09569  -0.02515 134 LEU B C   
5847 O O   . LEU B 142 ? 1.59935 1.26273 0.58556 0.71057  0.10319  -0.02254 134 LEU B O   
5848 C CB  . LEU B 142 ? 1.58120 1.24195 0.56162 0.67768  0.10855  -0.00789 134 LEU B CB  
5849 C CG  . LEU B 142 ? 1.58113 1.23766 0.56803 0.65763  0.10544  -0.00327 134 LEU B CG  
5850 C CD1 . LEU B 142 ? 1.57589 1.25098 0.55436 0.65801  0.12682  0.01212  134 LEU B CD1 
5851 C CD2 . LEU B 142 ? 1.55108 1.17541 0.53342 0.64593  0.08586  -0.01339 134 LEU B CD2 
5852 N N   . SER B 143 ? 1.61859 1.24809 0.58191 0.70331  0.09019  -0.03281 135 SER B N   
5853 C CA  . SER B 143 ? 1.64624 1.27149 0.59923 0.71953  0.08973  -0.04183 135 SER B CA  
5854 C C   . SER B 143 ? 1.66552 1.31958 0.61768 0.73799  0.10913  -0.03386 135 SER B C   
5855 O O   . SER B 143 ? 1.67844 1.33125 0.63075 0.75014  0.10839  -0.04058 135 SER B O   
5856 C CB  . SER B 143 ? 1.66925 1.28184 0.60440 0.72202  0.08405  -0.04960 135 SER B CB  
5857 O OG  . SER B 143 ? 1.68262 1.30833 0.60606 0.72445  0.09674  -0.03820 135 SER B OG  
5858 N N   . SER B 144 ? 1.66928 1.34854 0.62132 0.73957  0.12692  -0.02035 136 SER B N   
5859 C CA  . SER B 144 ? 1.68596 1.39882 0.64147 0.75520  0.14850  -0.01168 136 SER B CA  
5860 C C   . SER B 144 ? 1.66813 1.39441 0.64334 0.75970  0.14753  -0.01218 136 SER B C   
5861 O O   . SER B 144 ? 1.68606 1.42355 0.66215 0.77678  0.15346  -0.01524 136 SER B O   
5862 C CB  . SER B 144 ? 1.68999 1.42597 0.64505 0.75100  0.16840  0.00342  136 SER B CB  
5863 O OG  . SER B 144 ? 1.65909 1.39343 0.62642 0.73270  0.16381  0.00837  136 SER B OG  
5864 N N   . GLY B 145 ? 1.63637 1.36179 0.62593 0.74587  0.13999  -0.00972 137 GLY B N   
5865 C CA  . GLY B 145 ? 1.61934 1.36255 0.62724 0.75062  0.13962  -0.00841 137 GLY B CA  
5866 C C   . GLY B 145 ? 1.61393 1.40112 0.63728 0.75290  0.15937  0.00241  137 GLY B C   
5867 O O   . GLY B 145 ? 1.60218 1.41285 0.64283 0.76014  0.16046  0.00287  137 GLY B O   
5868 N N   . THR B 146 ? 1.62487 1.42385 0.64238 0.74779  0.17531  0.01078  138 THR B N   
5869 C CA  . THR B 146 ? 1.62409 1.46532 0.65673 0.74711  0.19916  0.02215  138 THR B CA  
5870 C C   . THR B 146 ? 1.60299 1.44036 0.63873 0.72532  0.19827  0.02800  138 THR B C   
5871 O O   . THR B 146 ? 1.59891 1.47099 0.65042 0.72157  0.21786  0.03674  138 THR B O   
5872 C CB  . THR B 146 ? 1.65836 1.51388 0.68035 0.75674  0.22215  0.02971  138 THR B CB  
5873 O OG1 . THR B 146 ? 1.66954 1.49644 0.66876 0.74588  0.21969  0.03352  138 THR B OG1 
5874 C CG2 . THR B 146 ? 1.68340 1.53833 0.69818 0.77711  0.22223  0.02261  138 THR B CG2 
5875 N N   . GLN B 147 ? 1.61448 1.41269 0.63789 0.71144  0.17780  0.02271  139 GLN B N   
5876 C CA  . GLN B 147 ? 1.57212 1.35980 0.59657 0.68986  0.17316  0.02643  139 GLN B CA  
5877 C C   . GLN B 147 ? 1.54703 1.30402 0.57415 0.67836  0.14571  0.01491  139 GLN B C   
5878 O O   . GLN B 147 ? 1.55053 1.28470 0.57151 0.68573  0.13186  0.00549  139 GLN B O   
5879 C CB  . GLN B 147 ? 1.59397 1.36351 0.59764 0.68459  0.18046  0.03374  139 GLN B CB  
5880 C CG  . GLN B 147 ? 1.64756 1.44506 0.64755 0.69297  0.21093  0.04812  139 GLN B CG  
5881 C CD  . GLN B 147 ? 1.64962 1.42592 0.62498 0.68988  0.21767  0.05686  139 GLN B CD  
5882 O OE1 . GLN B 147 ? 1.64783 1.39033 0.60896 0.68424  0.19813  0.05003  139 GLN B OE1 
5883 N NE2 . GLN B 147 ? 1.67684 1.47422 0.64815 0.69439  0.24660  0.07221  139 GLN B NE2 
5884 N N   . ALA B 148 ? 1.56513 1.32199 0.60151 0.66038  0.13963  0.01569  140 ALA B N   
5885 C CA  . ALA B 148 ? 1.52739 1.25660 0.56837 0.64589  0.11563  0.00570  140 ALA B CA  
5886 C C   . ALA B 148 ? 1.48800 1.20785 0.52897 0.62435  0.11280  0.00868  140 ALA B C   
5887 O O   . ALA B 148 ? 1.50503 1.24637 0.54567 0.62141  0.13087  0.01962  140 ALA B O   
5888 C CB  . ALA B 148 ? 1.47818 1.22413 0.53470 0.65026  0.10901  0.00148  140 ALA B CB  
5889 N N   . VAL B 149 ? 1.46396 1.15278 0.50593 0.61006  0.09244  -0.00053 141 VAL B N   
5890 C CA  . VAL B 149 ? 1.46921 1.14526 0.51254 0.58894  0.08587  -0.00022 141 VAL B CA  
5891 C C   . VAL B 149 ? 1.43800 1.10958 0.49741 0.57530  0.06880  -0.00918 141 VAL B C   
5892 O O   . VAL B 149 ? 1.47608 1.13356 0.53951 0.57949  0.05683  -0.01767 141 VAL B O   
5893 C CB  . VAL B 149 ? 1.48593 1.12986 0.51539 0.58503  0.07807  -0.00358 141 VAL B CB  
5894 C CG1 . VAL B 149 ? 1.50658 1.12426 0.53803 0.58615  0.05947  -0.01746 141 VAL B CG1 
5895 C CG2 . VAL B 149 ? 1.48091 1.11348 0.50981 0.56647  0.07396  -0.00148 141 VAL B CG2 
5896 N N   . SER B 150 ? 1.47385 1.15662 0.54059 0.56002  0.06888  -0.00677 142 SER B N   
5897 C CA  . SER B 150 ? 1.41755 1.10075 0.49919 0.54576  0.05351  -0.01482 142 SER B CA  
5898 C C   . SER B 150 ? 1.39510 1.05494 0.47744 0.52427  0.04283  -0.01890 142 SER B C   
5899 O O   . SER B 150 ? 1.39048 1.04390 0.46125 0.52163  0.05143  -0.01196 142 SER B O   
5900 C CB  . SER B 150 ? 1.36991 1.09373 0.46101 0.54851  0.06172  -0.01091 142 SER B CB  
5901 O OG  . SER B 150 ? 1.37698 1.11685 0.46574 0.54173  0.07667  -0.00217 142 SER B OG  
5902 N N   . GLY B 151 ? 1.40700 1.05442 0.50161 0.51065  0.02578  -0.02904 143 GLY B N   
5903 C CA  . GLY B 151 ? 1.40076 1.02855 0.50025 0.48950  0.01399  -0.03521 143 GLY B CA  
5904 C C   . GLY B 151 ? 1.42626 1.06779 0.54054 0.47588  0.00462  -0.04094 143 GLY B C   
5905 O O   . GLY B 151 ? 1.45545 1.09502 0.57878 0.47676  -0.00424 -0.04687 143 GLY B O   
5906 N N   . SER B 152 ? 1.35513 1.00911 0.46969 0.46465  0.00700  -0.03908 144 SER B N   
5907 C CA  . SER B 152 ? 1.38308 1.05668 0.51066 0.45237  -0.00178 -0.04579 144 SER B CA  
5908 C C   . SER B 152 ? 1.33361 0.98363 0.46784 0.43043  -0.01528 -0.05509 144 SER B C   
5909 O O   . SER B 152 ? 1.33899 0.96273 0.46500 0.42638  -0.01480 -0.05379 144 SER B O   
5910 C CB  . SER B 152 ? 1.33399 1.05253 0.50181 0.44442  0.00978  -0.03606 144 SER B CB  
5911 O OG  . SER B 152 ? 1.33278 1.07491 0.53811 0.42379  -0.00077 -0.04312 144 SER B OG  
5912 N N   . LYS B 153 ? 1.35217 1.01366 0.50153 0.41792  -0.02721 -0.06447 145 LYS B N   
5913 C CA  . LYS B 153 ? 1.33135 0.97620 0.49029 0.39623  -0.04018 -0.07537 145 LYS B CA  
5914 C C   . LYS B 153 ? 1.30664 0.96333 0.49435 0.37873  -0.03458 -0.06975 145 LYS B C   
5915 O O   . LYS B 153 ? 1.30239 0.93947 0.49390 0.36308  -0.04324 -0.07746 145 LYS B O   
5916 C CB  . LYS B 153 ? 1.28786 0.94920 0.46403 0.38715  -0.05242 -0.08505 145 LYS B CB  
5917 C CG  . LYS B 153 ? 1.34455 0.98977 0.52774 0.38864  -0.05799 -0.08673 145 LYS B CG  
5918 C CD  . LYS B 153 ? 1.24017 0.90032 0.43617 0.38090  -0.06793 -0.09372 145 LYS B CD  
5919 C CE  . LYS B 153 ? 1.24327 0.88321 0.43981 0.38475  -0.06964 -0.09298 145 LYS B CE  
5920 N NZ  . LYS B 153 ? 1.23871 0.84744 0.44340 0.36791  -0.07443 -0.09953 145 LYS B NZ  
5921 N N   . ASP B 154 ? 1.24569 0.93258 0.45529 0.38110  -0.01947 -0.05692 146 ASP B N   
5922 C CA  . ASP B 154 ? 1.22636 0.92219 0.46434 0.36611  -0.00849 -0.04808 146 ASP B CA  
5923 C C   . ASP B 154 ? 1.25711 0.91395 0.46017 0.37439  -0.00152 -0.03960 146 ASP B C   
5924 O O   . ASP B 154 ? 1.26131 0.91871 0.48051 0.36548  0.01032  -0.02877 146 ASP B O   
5925 C CB  . ASP B 154 ? 1.26228 1.00283 0.53537 0.36696  0.00790  -0.03766 146 ASP B CB  
5926 C CG  . ASP B 154 ? 1.32270 1.06395 0.57033 0.39066  0.02404  -0.02480 146 ASP B CG  
5927 O OD1 . ASP B 154 ? 1.32145 1.02608 0.52313 0.40588  0.02388  -0.02272 146 ASP B OD1 
5928 O OD2 . ASP B 154 ? 1.34225 1.12263 0.61787 0.39395  0.03645  -0.01863 146 ASP B OD2 
5929 N N   . ILE B 155 ? 1.31301 0.93829 0.47046 0.39203  -0.00770 -0.04436 147 ILE B N   
5930 C CA  . ILE B 155 ? 1.41691 1.00209 0.53547 0.40167  -0.00801 -0.04268 147 ILE B CA  
5931 C C   . ILE B 155 ? 1.42337 1.01042 0.51948 0.42159  0.01107  -0.02634 147 ILE B C   
5932 O O   . ILE B 155 ? 1.42597 0.98404 0.48746 0.43461  0.01055  -0.02530 147 ILE B O   
5933 C CB  . ILE B 155 ? 1.35238 0.92164 0.48549 0.38299  -0.01322 -0.04354 147 ILE B CB  
5934 C CG1 . ILE B 155 ? 1.25499 0.82516 0.41127 0.36338  -0.03120 -0.06109 147 ILE B CG1 
5935 C CG2 . ILE B 155 ? 1.31301 0.84334 0.40491 0.39579  -0.01551 -0.04226 147 ILE B CG2 
5936 C CD1 . ILE B 155 ? 1.24817 0.80764 0.42659 0.34359  -0.03598 -0.06322 147 ILE B CD1 
5937 N N   . CYS B 156 ? 1.35506 0.97778 0.47470 0.42387  0.02674  -0.01529 148 CYS B N   
5938 C CA  . CYS B 156 ? 1.35152 0.98139 0.45522 0.44126  0.04847  0.00129  148 CYS B CA  
5939 C C   . CYS B 156 ? 1.40251 1.02943 0.47286 0.46639  0.04832  -0.00352 148 CYS B C   
5940 O O   . CYS B 156 ? 1.38013 1.01639 0.45804 0.46749  0.03722  -0.01489 148 CYS B O   
5941 C CB  . CYS B 156 ? 1.34565 1.01750 0.49620 0.43057  0.06677  0.01352  148 CYS B CB  
5942 S SG  . CYS B 156 ? 1.41604 1.08615 0.60310 0.40422  0.07513  0.02319  148 CYS B SG  
5943 N N   . ILE B 157 ? 1.45613 1.07071 0.49840 0.48403  0.05975  0.00512  149 ILE B N   
5944 C CA  . ILE B 157 ? 1.40200 1.02507 0.44456 0.50145  0.06356  0.00458  149 ILE B CA  
5945 C C   . ILE B 157 ? 1.43012 1.07745 0.46143 0.51524  0.09129  0.02191  149 ILE B C   
5946 O O   . ILE B 157 ? 1.45511 1.09389 0.46961 0.51553  0.10628  0.03592  149 ILE B O   
5947 C CB  . ILE B 157 ? 1.40947 1.00343 0.44417 0.50698  0.05211  -0.00226 149 ILE B CB  
5948 C CG1 . ILE B 157 ? 1.38084 0.95505 0.43132 0.49311  0.02817  -0.01932 149 ILE B CG1 
5949 C CG2 . ILE B 157 ? 1.42512 1.02660 0.45486 0.52644  0.05880  -0.00147 149 ILE B CG2 
5950 C CD1 . ILE B 157 ? 1.38724 0.93630 0.43263 0.49784  0.01659  -0.02779 149 ILE B CD1 
5951 N N   . LYS B 158 ? 1.42784 1.10442 0.46878 0.52661  0.09922  0.02180  150 LYS B N   
5952 C CA  . LYS B 158 ? 1.44681 1.15600 0.49630 0.53631  0.12603  0.03666  150 LYS B CA  
5953 C C   . LYS B 158 ? 1.48191 1.19453 0.51711 0.55957  0.12999  0.03424  150 LYS B C   
5954 O O   . LYS B 158 ? 1.46334 1.17082 0.50787 0.56233  0.11171  0.02120  150 LYS B O   
5955 C CB  . LYS B 158 ? 1.41700 1.17192 0.52703 0.51944  0.12853  0.03734  150 LYS B CB  
5956 C CG  . LYS B 158 ? 1.39739 1.15900 0.54686 0.49037  0.12681  0.04048  150 LYS B CG  
5957 C CD  . LYS B 158 ? 1.37814 1.19167 0.58955 0.47642  0.13673  0.04264  150 LYS B CD  
5958 C CE  . LYS B 158 ? 1.34460 1.16990 0.59817 0.45000  0.12085  0.03289  150 LYS B CE  
5959 N NZ  . LYS B 158 ? 1.39114 1.20328 0.66124 0.42910  0.13000  0.04162  150 LYS B NZ  
5960 N N   . VAL B 159 ? 1.54896 1.27043 0.57201 0.57248  0.15292  0.04738  151 VAL B N   
5961 C CA  . VAL B 159 ? 1.55690 1.28714 0.57633 0.59256  0.15896  0.04656  151 VAL B CA  
5962 C C   . VAL B 159 ? 1.56554 1.34168 0.60043 0.60259  0.18206  0.05287  151 VAL B C   
5963 O O   . VAL B 159 ? 1.56403 1.36281 0.61899 0.59231  0.20278  0.06611  151 VAL B O   
5964 C CB  . VAL B 159 ? 1.54571 1.25654 0.54132 0.60135  0.16811  0.05514  151 VAL B CB  
5965 C CG1 . VAL B 159 ? 1.56703 1.29122 0.55810 0.62211  0.17768  0.05511  151 VAL B CG1 
5966 C CG2 . VAL B 159 ? 1.54163 1.21298 0.52581 0.59490  0.14427  0.04530  151 VAL B CG2 
5967 N N   . TRP B 160 ? 1.50837 1.29960 0.55325 0.61650  0.17611  0.04409  152 TRP B N   
5968 C CA  . TRP B 160 ? 1.50563 1.34502 0.57378 0.62769  0.19263  0.04536  152 TRP B CA  
5969 C C   . TRP B 160 ? 1.59123 1.44330 0.65237 0.64861  0.21051  0.05029  152 TRP B C   
5970 O O   . TRP B 160 ? 1.63181 1.45403 0.67477 0.65587  0.19889  0.04644  152 TRP B O   
5971 C CB  . TRP B 160 ? 1.49077 1.33859 0.57754 0.62879  0.17031  0.03187  152 TRP B CB  
5972 C CG  . TRP B 160 ? 1.44837 1.29338 0.56044 0.60301  0.15123  0.02766  152 TRP B CG  
5973 C CD1 . TRP B 160 ? 1.43979 1.24406 0.52699 0.59424  0.13125  0.01959  152 TRP B CD1 
5974 C CD2 . TRP B 160 ? 1.44507 1.33186 0.61438 0.58255  0.15058  0.02936  152 TRP B CD2 
5975 N NE1 . TRP B 160 ? 1.48664 1.30359 0.60957 0.57013  0.11877  0.01707  152 TRP B NE1 
5976 C CE2 . TRP B 160 ? 1.48025 1.34765 0.65351 0.56262  0.12958  0.02238  152 TRP B CE2 
5977 C CE3 . TRP B 160 ? 1.42348 1.36388 0.64325 0.57910  0.16554  0.03403  152 TRP B CE3 
5978 C CZ2 . TRP B 160 ? 1.41404 1.31342 0.63757 0.54022  0.12266  0.01972  152 TRP B CZ2 
5979 C CZ3 . TRP B 160 ? 1.41255 1.38551 0.68452 0.55646  0.15812  0.03043  152 TRP B CZ3 
5980 C CH2 . TRP B 160 ? 1.37255 1.32495 0.64517 0.53762  0.13666  0.02326  152 TRP B CH2 
5981 N N   . ASP B 161 ? 1.63317 1.53125 0.72237 0.65313  0.23522  0.05771  153 ASP B N   
5982 C CA  . ASP B 161 ? 1.58118 1.50370 0.66751 0.67735  0.25502  0.05921  153 ASP B CA  
5983 C C   . ASP B 161 ? 1.61847 1.57818 0.74443 0.68428  0.24536  0.04928  153 ASP B C   
5984 O O   . ASP B 161 ? 1.56254 1.56638 0.74489 0.66908  0.25029  0.05207  153 ASP B O   
5985 C CB  . ASP B 161 ? 1.62645 1.57462 0.72852 0.67273  0.28877  0.07586  153 ASP B CB  
5986 C CG  . ASP B 161 ? 1.77654 1.74136 0.86879 0.69589  0.30962  0.07864  153 ASP B CG  
5987 O OD1 . ASP B 161 ? 1.74635 1.71613 0.84218 0.71130  0.29599  0.06739  153 ASP B OD1 
5988 O OD2 . ASP B 161 ? 1.83398 1.80506 0.92123 0.69500  0.33738  0.09322  153 ASP B OD2 
5989 N N   . LEU B 162 ? 1.63896 1.58049 0.74508 0.70252  0.22851  0.03841  154 LEU B N   
5990 C CA  . LEU B 162 ? 1.55699 1.52492 0.68539 0.71645  0.21802  0.02848  154 LEU B CA  
5991 C C   . LEU B 162 ? 1.62578 1.64681 0.78987 0.72992  0.23949  0.03175  154 LEU B C   
5992 O O   . LEU B 162 ? 1.63442 1.69508 0.84258 0.73075  0.23184  0.02746  154 LEU B O   
5993 C CB  . LEU B 162 ? 1.53317 1.45986 0.64052 0.72564  0.19355  0.02061  154 LEU B CB  
5994 C CG  . LEU B 162 ? 1.56609 1.44173 0.65384 0.70791  0.16938  0.01656  154 LEU B CG  
5995 C CD1 . LEU B 162 ? 1.55467 1.39617 0.63046 0.71791  0.15017  0.00851  154 LEU B CD1 
5996 C CD2 . LEU B 162 ? 1.49145 1.37503 0.59115 0.69207  0.15907  0.01376  154 LEU B CD2 
5997 N N   . ALA B 163 ? 1.64651 1.66927 0.79372 0.73978  0.26428  0.03878  155 ALA B N   
5998 C CA  . ALA B 163 ? 1.63965 1.71246 0.81716 0.75320  0.29073  0.04209  155 ALA B CA  
5999 C C   . ALA B 163 ? 1.63411 1.75472 0.87479 0.72759  0.30260  0.04956  155 ALA B C   
6000 O O   . ALA B 163 ? 1.58358 1.75655 0.87488 0.73235  0.30738  0.04524  155 ALA B O   
6001 C CB  . ALA B 163 ? 1.76329 1.81732 0.91360 0.75842  0.30695  0.05046  155 ALA B CB  
6002 N N   . GLN B 164 ? 1.66239 1.76575 0.90195 0.70200  0.30690  0.05914  156 GLN B N   
6003 C CA  . GLN B 164 ? 1.60516 1.74696 0.90312 0.67490  0.32278  0.06702  156 GLN B CA  
6004 C C   . GLN B 164 ? 1.52995 1.68041 0.86532 0.65146  0.29642  0.05934  156 GLN B C   
6005 O O   . GLN B 164 ? 1.48509 1.67917 0.88201 0.63142  0.30484  0.05952  156 GLN B O   
6006 C CB  . GLN B 164 ? 1.58143 1.69584 0.85366 0.66279  0.34626  0.08371  156 GLN B CB  
6007 C CG  . GLN B 164 ? 1.72237 1.83130 0.95640 0.68601  0.37457  0.09205  156 GLN B CG  
6008 C CD  . GLN B 164 ? 1.80455 1.89254 1.01740 0.67484  0.40129  0.11127  156 GLN B CD  
6009 O OE1 . GLN B 164 ? 1.70611 1.76844 0.91663 0.65312  0.39446  0.11816  156 GLN B OE1 
6010 N NE2 . GLN B 164 ? 1.76536 1.86320 0.96081 0.69103  0.43293  0.12069  156 GLN B NE2 
6011 N N   . GLN B 165 ? 1.50143 1.61256 0.80230 0.65343  0.26699  0.05183  157 GLN B N   
6012 C CA  . GLN B 165 ? 1.54087 1.65591 0.86803 0.63499  0.23925  0.04300  157 GLN B CA  
6013 C C   . GLN B 165 ? 1.56693 1.67548 0.91509 0.60248  0.24346  0.04960  157 GLN B C   
6014 O O   . GLN B 165 ? 1.52356 1.66003 0.91912 0.58304  0.23075  0.04244  157 GLN B O   
6015 C CB  . GLN B 165 ? 1.46669 1.64085 0.85049 0.63941  0.23177  0.03303  157 GLN B CB  
6016 C CG  . GLN B 165 ? 1.50025 1.68572 0.86993 0.67298  0.23129  0.02795  157 GLN B CG  
6017 C CD  . GLN B 165 ? 1.43080 1.67841 0.85808 0.67921  0.22436  0.01853  157 GLN B CD  
6018 O OE1 . GLN B 165 ? 1.40703 1.69312 0.88731 0.65809  0.22000  0.01410  157 GLN B OE1 
6019 N NE2 . GLN B 165 ? 1.44466 1.70331 0.86280 0.70951  0.22268  0.01410  157 GLN B NE2 
6020 N N   . VAL B 166 ? 1.56904 1.64137 0.88193 0.59808  0.25986  0.06216  158 VAL B N   
6021 C CA  . VAL B 166 ? 1.48836 1.54440 0.81294 0.56958  0.26531  0.07081  158 VAL B CA  
6022 C C   . VAL B 166 ? 1.47313 1.46556 0.73324 0.57214  0.25247  0.07353  158 VAL B C   
6023 O O   . VAL B 166 ? 1.48898 1.45424 0.69854 0.59590  0.24499  0.06928  158 VAL B O   
6024 C CB  . VAL B 166 ? 1.48500 1.56181 0.83481 0.56119  0.30233  0.08631  158 VAL B CB  
6025 C CG1 . VAL B 166 ? 1.47509 1.61783 0.89129 0.56007  0.31673  0.08130  158 VAL B CG1 
6026 C CG2 . VAL B 166 ? 1.52933 1.57454 0.81958 0.58219  0.32333  0.09954  158 VAL B CG2 
6027 N N   . VAL B 167 ? 1.46754 1.43823 0.73213 0.54879  0.25058  0.07919  159 VAL B N   
6028 C CA  . VAL B 167 ? 1.48884 1.40149 0.69782 0.54885  0.23903  0.08185  159 VAL B CA  
6029 C C   . VAL B 167 ? 1.53227 1.42551 0.71014 0.55513  0.26714  0.10066  159 VAL B C   
6030 O O   . VAL B 167 ? 1.55197 1.46632 0.76705 0.53978  0.29127  0.11352  159 VAL B O   
6031 C CB  . VAL B 167 ? 1.45136 1.35111 0.68261 0.52148  0.22014  0.07687  159 VAL B CB  
6032 C CG1 . VAL B 167 ? 1.45824 1.30225 0.63434 0.52496  0.20155  0.07369  159 VAL B CG1 
6033 C CG2 . VAL B 167 ? 1.41159 1.34458 0.68778 0.51152  0.19923  0.06102  159 VAL B CG2 
6034 N N   . LEU B 168 ? 1.56678 1.42175 0.67948 0.57727  0.26471  0.10162  160 LEU B N   
6035 C CA  . LEU B 168 ? 1.59872 1.42997 0.66876 0.58794  0.28850  0.11922  160 LEU B CA  
6036 C C   . LEU B 168 ? 1.65283 1.44370 0.70365 0.57319  0.27985  0.12594  160 LEU B C   
6037 O O   . LEU B 168 ? 1.62387 1.41338 0.68692 0.56123  0.30264  0.14460  160 LEU B O   
6038 C CB  . LEU B 168 ? 1.62828 1.43995 0.63732 0.62038  0.28660  0.11318  160 LEU B CB  
6039 C CG  . LEU B 168 ? 1.62924 1.47703 0.65373 0.63803  0.29598  0.10693  160 LEU B CG  
6040 C CD1 . LEU B 168 ? 1.64616 1.47125 0.64832 0.65355  0.27950  0.09904  160 LEU B CD1 
6041 C CD2 . LEU B 168 ? 1.64673 1.53393 0.70488 0.63516  0.33244  0.12300  160 LEU B CD2 
6042 N N   . SER B 169 ? 1.61104 1.37006 0.63482 0.57417  0.24909  0.11113  161 SER B N   
6043 C CA  . SER B 169 ? 1.61205 1.33033 0.61334 0.56351  0.23534  0.11312  161 SER B CA  
6044 C C   . SER B 169 ? 1.54325 1.26264 0.58134 0.54040  0.20845  0.09799  161 SER B C   
6045 O O   . SER B 169 ? 1.51518 1.25129 0.56838 0.54263  0.19272  0.08213  161 SER B O   
6046 C CB  . SER B 169 ? 1.61078 1.29298 0.56680 0.58022  0.21853  0.10594  161 SER B CB  
6047 O OG  . SER B 169 ? 1.64651 1.33470 0.58843 0.59740  0.23657  0.11560  161 SER B OG  
6048 N N   . SER B 170 ? 1.53944 1.24074 0.58993 0.52016  0.20433  0.10335  162 SER B N   
6049 C CA  . SER B 170 ? 1.51703 1.21285 0.59589 0.49796  0.17865  0.08902  162 SER B CA  
6050 C C   . SER B 170 ? 1.54679 1.19585 0.58825 0.49713  0.16495  0.08879  162 SER B C   
6051 O O   . SER B 170 ? 1.59065 1.22609 0.63234 0.48991  0.17963  0.10557  162 SER B O   
6052 C CB  . SER B 170 ? 1.49964 1.22875 0.64581 0.47079  0.18807  0.09315  162 SER B CB  
6053 O OG  . SER B 170 ? 1.45045 1.17797 0.62286 0.45119  0.16305  0.07737  162 SER B OG  
6054 N N   . TYR B 171 ? 1.50000 1.12521 0.51154 0.50497  0.13878  0.07043  163 TYR B N   
6055 C CA  . TYR B 171 ? 1.51380 1.09581 0.48569 0.50891  0.12249  0.06542  163 TYR B CA  
6056 C C   . TYR B 171 ? 1.49639 1.07049 0.49553 0.48659  0.09811  0.04954  163 TYR B C   
6057 O O   . TYR B 171 ? 1.51493 1.09341 0.51888 0.48601  0.08050  0.03121  163 TYR B O   
6058 C CB  . TYR B 171 ? 1.51523 1.08672 0.48003 0.52293  0.10729  0.05218  163 TYR B CB  
6059 C CG  . TYR B 171 ? 1.54895 1.12962 0.49861 0.54237  0.12637  0.06381  163 TYR B CG  
6060 C CD1 . TYR B 171 ? 1.58983 1.16196 0.51651 0.54946  0.14766  0.08476  163 TYR B CD1 
6061 C CD2 . TYR B 171 ? 1.54320 1.13906 0.50052 0.55426  0.12348  0.05445  163 TYR B CD2 
6062 C CE1 . TYR B 171 ? 1.62309 1.20414 0.53551 0.56728  0.16558  0.09504  163 TYR B CE1 
6063 C CE2 . TYR B 171 ? 1.57557 1.18006 0.51833 0.57243  0.14028  0.06368  163 TYR B CE2 
6064 C CZ  . TYR B 171 ? 1.61518 1.21329 0.53562 0.57873  0.16122  0.08344  163 TYR B CZ  
6065 O OH  . TYR B 171 ? 1.70246 1.30968 0.60816 0.59655  0.17826  0.09233  163 TYR B OH  
6066 N N   . ARG B 172 ? 1.48500 0.91273 0.53804 0.35082  0.11922  -0.16817 164 ARG B N   
6067 C CA  . ARG B 172 ? 1.46659 0.89516 0.52555 0.34541  0.10692  -0.16575 164 ARG B CA  
6068 C C   . ARG B 172 ? 1.46511 0.85735 0.50889 0.35330  0.09939  -0.14217 164 ARG B C   
6069 O O   . ARG B 172 ? 1.48678 0.85129 0.51639 0.34979  0.11021  -0.13966 164 ARG B O   
6070 C CB  . ARG B 172 ? 1.48525 0.91888 0.54770 0.32813  0.12386  -0.18787 164 ARG B CB  
6071 C CG  . ARG B 172 ? 1.46886 0.90683 0.53792 0.32227  0.11262  -0.18828 164 ARG B CG  
6072 C CD  . ARG B 172 ? 1.52528 0.96194 0.59442 0.30423  0.13204  -0.21111 164 ARG B CD  
6073 N NE  . ARG B 172 ? 1.53505 1.01577 0.62093 0.29361  0.13648  -0.24149 164 ARG B NE  
6074 C CZ  . ARG B 172 ? 1.53798 1.05317 0.63699 0.29207  0.12038  -0.25137 164 ARG B CZ  
6075 N NH1 . ARG B 172 ? 1.48919 0.99853 0.58918 0.29871  0.10086  -0.23297 164 ARG B NH1 
6076 N NH2 . ARG B 172 ? 1.55189 1.10806 0.66155 0.28472  0.12464  -0.28094 164 ARG B NH2 
6077 N N   . ALA B 173 ? 1.44606 0.83770 0.49063 0.36473  0.08277  -0.12716 165 ALA B N   
6078 C CA  . ALA B 173 ? 1.44490 0.81095 0.47759 0.37343  0.07375  -0.10944 165 ALA B CA  
6079 C C   . ALA B 173 ? 1.42115 0.79754 0.46571 0.37111  0.05985  -0.10802 165 ALA B C   
6080 O O   . ALA B 173 ? 1.46318 0.82103 0.49738 0.37486  0.05909  -0.10129 165 ALA B O   
6081 C CB  . ALA B 173 ? 1.44100 0.80304 0.46976 0.38336  0.06621  -0.09969 165 ALA B CB  
6082 N N   . HIS B 174 ? 1.39721 0.80063 0.45976 0.36735  0.05022  -0.11408 166 HIS B N   
6083 C CA  . HIS B 174 ? 1.37506 0.78910 0.44934 0.36476  0.03796  -0.11288 166 HIS B CA  
6084 C C   . HIS B 174 ? 1.38865 0.80745 0.46671 0.35560  0.04285  -0.12212 166 HIS B C   
6085 O O   . HIS B 174 ? 1.41070 0.82811 0.48424 0.34915  0.05622  -0.13256 166 HIS B O   
6086 C CB  . HIS B 174 ? 1.35881 0.79185 0.44371 0.36639  0.02853  -0.11433 166 HIS B CB  
6087 C CG  . HIS B 174 ? 1.36118 0.78279 0.43884 0.37513  0.02410  -0.10482 166 HIS B CG  
6088 N ND1 . HIS B 174 ? 1.36341 0.76985 0.43367 0.37910  0.01723  -0.09758 166 HIS B ND1 
6089 C CD2 . HIS B 174 ? 1.36973 0.79006 0.44188 0.38199  0.02656  -0.10305 166 HIS B CD2 
6090 C CE1 . HIS B 174 ? 1.37293 0.76816 0.43365 0.38539  0.01630  -0.09249 166 HIS B CE1 
6091 N NE2 . HIS B 174 ? 1.37653 0.77816 0.43779 0.38828  0.02182  -0.09416 166 HIS B NE2 
6092 N N   . ALA B 175 ? 1.37369 0.79748 0.45915 0.35388  0.03435  -0.12031 167 ALA B N   
6093 C CA  . ALA B 175 ? 1.36484 0.79099 0.45284 0.34611  0.03781  -0.12787 167 ALA B CA  
6094 C C   . ALA B 175 ? 1.36549 0.81574 0.46824 0.34035  0.02926  -0.13458 167 ALA B C   
6095 O O   . ALA B 175 ? 1.34576 0.79870 0.45116 0.33400  0.03043  -0.14031 167 ALA B O   
6096 C CB  . ALA B 175 ? 1.37143 0.77910 0.45029 0.35279  0.03652  -0.11909 167 ALA B CB  
6097 N N   . ALA B 176 ? 1.33553 0.79860 0.44351 0.34426  0.02203  -0.13330 168 ALA B N   
6098 C CA  . ALA B 176 ? 1.37561 0.85372 0.48858 0.34455  0.01391  -0.13702 168 ALA B CA  
6099 C C   . ALA B 176 ? 1.41994 0.90858 0.53205 0.35269  0.01015  -0.13687 168 ALA B C   
6100 O O   . ALA B 176 ? 1.45455 0.93752 0.56171 0.35812  0.01397  -0.13407 168 ALA B O   
6101 C CB  . ALA B 176 ? 1.33060 0.79590 0.43943 0.34858  0.00728  -0.12856 168 ALA B CB  
6102 N N   . GLN B 177 ? 1.50347 1.00227 0.61451 0.35732  0.00322  -0.13903 169 GLN B N   
6103 C CA  . GLN B 177 ? 1.46992 0.97622 0.57336 0.37176  -0.00147 -0.13859 169 GLN B CA  
6104 C C   . GLN B 177 ? 1.52610 1.01265 0.62212 0.38010  -0.00022 -0.12620 169 GLN B C   
6105 O O   . GLN B 177 ? 1.55019 1.01274 0.63868 0.38039  -0.00131 -0.11657 169 GLN B O   
6106 C CB  . GLN B 177 ? 1.45144 0.95922 0.54864 0.37793  -0.00863 -0.13752 169 GLN B CB  
6107 C CG  . GLN B 177 ? 1.57940 1.11053 0.67998 0.37313  -0.01121 -0.15209 169 GLN B CG  
6108 C CD  . GLN B 177 ? 1.58900 1.11712 0.68054 0.37872  -0.01737 -0.14999 169 GLN B CD  
6109 O OE1 . GLN B 177 ? 1.64042 1.14622 0.71760 0.39049  -0.01925 -0.13813 169 GLN B OE1 
6110 N NE2 . GLN B 177 ? 1.44739 0.99290 0.54151 0.37145  -0.01922 -0.16242 169 GLN B NE2 
6111 N N   . VAL B 178 ? 1.42842 0.92026 0.51889 0.39060  0.00197  -0.12793 170 VAL B N   
6112 C CA  . VAL B 178 ? 1.47265 0.94472 0.55227 0.40072  0.00385  -0.11698 170 VAL B CA  
6113 C C   . VAL B 178 ? 1.48712 0.94725 0.55213 0.41514  -0.00125 -0.10999 170 VAL B C   
6114 O O   . VAL B 178 ? 1.43801 0.91236 0.49527 0.43171  -0.00524 -0.11440 170 VAL B O   
6115 C CB  . VAL B 178 ? 1.40400 0.88563 0.48062 0.40839  0.00979  -0.12195 170 VAL B CB  
6116 C CG1 . VAL B 178 ? 1.42060 0.87873 0.48421 0.41814  0.01261  -0.11027 170 VAL B CG1 
6117 C CG2 . VAL B 178 ? 1.37595 0.86389 0.46124 0.39395  0.01873  -0.13052 170 VAL B CG2 
6118 N N   . THR B 179 ? 1.42674 0.85802 0.48141 0.41259  -0.00067 -0.10058 171 THR B N   
6119 C CA  . THR B 179 ? 1.41268 0.82032 0.44597 0.42342  -0.00156 -0.09381 171 THR B CA  
6120 C C   . THR B 179 ? 1.48824 0.87872 0.50317 0.43986  0.00191  -0.08675 171 THR B C   
6121 O O   . THR B 179 ? 1.54314 0.93369 0.54345 0.45997  -0.00039 -0.08527 171 THR B O   
6122 C CB  . THR B 179 ? 1.41827 0.80136 0.44429 0.41100  0.00103  -0.09043 171 THR B CB  
6123 O OG1 . THR B 179 ? 1.45885 0.85997 0.50268 0.39790  -0.00167 -0.09686 171 THR B OG1 
6124 C CG2 . THR B 179 ? 1.44667 0.80226 0.44770 0.41772  0.00392  -0.08549 171 THR B CG2 
6125 N N   . CYS B 180 ? 1.46949 0.84300 0.48036 0.43519  0.00692  -0.08238 172 CYS B N   
6126 C CA  . CYS B 180 ? 1.47616 0.82595 0.46603 0.44858  0.01233  -0.07490 172 CYS B CA  
6127 C C   . CYS B 180 ? 1.51367 0.87250 0.51326 0.44538  0.01563  -0.07593 172 CYS B C   
6128 O O   . CYS B 180 ? 1.46596 0.82976 0.47838 0.43036  0.01547  -0.07880 172 CYS B O   
6129 C CB  . CYS B 180 ? 1.49327 0.80127 0.45849 0.44310  0.01826  -0.06881 172 CYS B CB  
6130 S SG  . CYS B 180 ? 1.53912 0.80812 0.46958 0.46080  0.02725  -0.05903 172 CYS B SG  
6131 N N   . VAL B 181 ? 1.56824 0.92415 0.55487 0.46423  0.01874  -0.07294 173 VAL B N   
6132 C CA  . VAL B 181 ? 1.55995 0.91320 0.54565 0.46477  0.02493  -0.07179 173 VAL B CA  
6133 C C   . VAL B 181 ? 1.61980 0.93989 0.57609 0.48150  0.03091  -0.06238 173 VAL B C   
6134 O O   . VAL B 181 ? 1.67332 0.99266 0.61353 0.50600  0.03019  -0.05963 173 VAL B O   
6135 C CB  . VAL B 181 ? 1.52505 0.91279 0.52417 0.47079  0.02588  -0.08084 173 VAL B CB  
6136 C CG1 . VAL B 181 ? 1.51866 0.93199 0.54130 0.45305  0.02259  -0.09062 173 VAL B CG1 
6137 C CG2 . VAL B 181 ? 1.56785 0.97320 0.55688 0.49765  0.02370  -0.08379 173 VAL B CG2 
6138 N N   . ALA B 182 ? 1.57004 0.86328 0.51684 0.47027  0.03658  -0.05822 174 ALA B N   
6139 C CA  . ALA B 182 ? 1.56654 0.82139 0.48198 0.48151  0.04469  -0.04993 174 ALA B CA  
6140 C C   . ALA B 182 ? 1.69402 0.94638 0.60726 0.48292  0.05085  -0.04885 174 ALA B C   
6141 O O   . ALA B 182 ? 1.64310 0.89835 0.56783 0.46459  0.05071  -0.05227 174 ALA B O   
6142 C CB  . ALA B 182 ? 1.58357 0.80415 0.48155 0.46675  0.04774  -0.04868 174 ALA B CB  
6143 N N   . ALA B 183 ? 1.70001 0.94756 0.59677 0.50644  0.05634  -0.04426 175 ALA B N   
6144 C CA  . ALA B 183 ? 1.61482 0.85575 0.50386 0.51126  0.06511  -0.04227 175 ALA B CA  
6145 C C   . ALA B 183 ? 1.66715 0.86566 0.53361 0.50095  0.07141  -0.03716 175 ALA B C   
6146 O O   . ALA B 183 ? 1.66380 0.83245 0.50902 0.50201  0.07327  -0.03312 175 ALA B O   
6147 C CB  . ALA B 183 ? 1.64421 0.89242 0.51919 0.54144  0.06993  -0.03937 175 ALA B CB  
6148 N N   . SER B 184 ? 1.66500 0.85949 0.53293 0.49103  0.07568  -0.03847 176 SER B N   
6149 C CA  . SER B 184 ? 1.66505 0.82240 0.50877 0.48352  0.08247  -0.03596 176 SER B CA  
6150 C C   . SER B 184 ? 1.71309 0.83795 0.52377 0.50504  0.09280  -0.02714 176 SER B C   
6151 O O   . SER B 184 ? 1.72293 0.85977 0.53191 0.52664  0.09684  -0.02349 176 SER B O   
6152 C CB  . SER B 184 ? 1.71736 0.87747 0.56505 0.47580  0.08501  -0.03811 176 SER B CB  
6153 O OG  . SER B 184 ? 1.73622 0.85841 0.55436 0.47219  0.09097  -0.03673 176 SER B OG  
6154 N N   . PRO B 185 ? 1.78509 0.86880 0.56678 0.50035  0.09876  -0.02457 177 PRO B N   
6155 C CA  . PRO B 185 ? 1.80428 0.84747 0.54718 0.52209  0.11092  -0.01446 177 PRO B CA  
6156 C C   . PRO B 185 ? 1.82450 0.86325 0.55707 0.53723  0.11984  -0.00978 177 PRO B C   
6157 O O   . PRO B 185 ? 1.85449 0.88652 0.56960 0.56516  0.12619  -0.00155 177 PRO B O   
6158 C CB  . PRO B 185 ? 1.83795 0.83709 0.55315 0.50293  0.11841  -0.01710 177 PRO B CB  
6159 C CG  . PRO B 185 ? 1.80648 0.82397 0.54174 0.48024  0.10834  -0.02700 177 PRO B CG  
6160 C CD  . PRO B 185 ? 1.75047 0.81899 0.52696 0.47679  0.09601  -0.03170 177 PRO B CD  
6161 N N   . HIS B 186 ? 1.81177 0.85496 0.55311 0.52100  0.12055  -0.01504 178 HIS B N   
6162 C CA  . HIS B 186 ? 1.84147 0.86756 0.56488 0.53065  0.13227  -0.01084 178 HIS B CA  
6163 C C   . HIS B 186 ? 1.81094 0.87039 0.55972 0.52683  0.13090  -0.01505 178 HIS B C   
6164 O O   . HIS B 186 ? 1.83844 0.88346 0.57233 0.53351  0.14202  -0.01201 178 HIS B O   
6165 C CB  . HIS B 186 ? 1.87745 0.85993 0.57148 0.51577  0.13901  -0.01263 178 HIS B CB  
6166 C CG  . HIS B 186 ? 1.91601 0.85922 0.58023 0.51569  0.14477  -0.00990 178 HIS B CG  
6167 N ND1 . HIS B 186 ? 1.96169 0.87477 0.59528 0.54232  0.15559  0.00222  178 HIS B ND1 
6168 C CD2 . HIS B 186 ? 1.92657 0.85047 0.58000 0.49457  0.14348  -0.01745 178 HIS B CD2 
6169 C CE1 . HIS B 186 ? 1.99772 0.87071 0.60284 0.53604  0.16165  0.00324  178 HIS B CE1 
6170 N NE2 . HIS B 186 ? 1.97440 0.85606 0.59370 0.50421  0.15508  -0.01021 178 HIS B NE2 
6171 N N   . LYS B 187 ? 1.76480 0.86265 0.54653 0.51704  0.12027  -0.02135 179 LYS B N   
6172 C CA  . LYS B 187 ? 1.74248 0.86535 0.54366 0.51150  0.12158  -0.02545 179 LYS B CA  
6173 C C   . LYS B 187 ? 1.77134 0.93767 0.60053 0.51702  0.11825  -0.03050 179 LYS B C   
6174 O O   . LYS B 187 ? 1.79327 0.97612 0.63866 0.51058  0.10646  -0.03373 179 LYS B O   
6175 C CB  . LYS B 187 ? 1.78359 0.90462 0.59198 0.49034  0.11298  -0.03014 179 LYS B CB  
6176 C CG  . LYS B 187 ? 1.76118 0.84748 0.54387 0.48194  0.11335  -0.03062 179 LYS B CG  
6177 C CD  . LYS B 187 ? 1.75106 0.83482 0.53115 0.47115  0.10724  -0.03518 179 LYS B CD  
6178 C CE  . LYS B 187 ? 1.77900 0.83809 0.53532 0.46094  0.10310  -0.04145 179 LYS B CE  
6179 N NZ  . LYS B 187 ? 1.78464 0.84478 0.53491 0.45563  0.09703  -0.04677 179 LYS B NZ  
6180 N N   . ASP B 188 ? 1.71957 0.90497 0.55409 0.52698  0.12987  -0.03332 180 ASP B N   
6181 C CA  . ASP B 188 ? 1.70751 0.93953 0.56841 0.53119  0.13025  -0.04334 180 ASP B CA  
6182 C C   . ASP B 188 ? 1.66378 0.91181 0.54650 0.51001  0.12413  -0.04999 180 ASP B C   
6183 O O   . ASP B 188 ? 1.78217 1.06000 0.68540 0.50713  0.11530  -0.05702 180 ASP B O   
6184 C CB  . ASP B 188 ? 1.71938 0.96929 0.58143 0.54338  0.14891  -0.04918 180 ASP B CB  
6185 C CG  . ASP B 188 ? 1.77990 1.03066 0.62675 0.57096  0.15478  -0.04542 180 ASP B CG  
6186 O OD1 . ASP B 188 ? 1.75107 1.00895 0.59528 0.58501  0.14344  -0.04290 180 ASP B OD1 
6187 O OD2 . ASP B 188 ? 1.98439 1.22689 0.81988 0.58010  0.17163  -0.04438 180 ASP B OD2 
6188 N N   . SER B 189 ? 1.69903 0.92581 0.57397 0.49813  0.12916  -0.04738 181 SER B N   
6189 C CA  . SER B 189 ? 1.71296 0.94751 0.60078 0.48238  0.12755  -0.05172 181 SER B CA  
6190 C C   . SER B 189 ? 1.69092 0.92592 0.58807 0.47173  0.10882  -0.05043 181 SER B C   
6191 O O   . SER B 189 ? 1.72954 0.97635 0.63986 0.46150  0.10568  -0.05441 181 SER B O   
6192 C CB  . SER B 189 ? 1.68293 0.88838 0.55131 0.47932  0.13936  -0.04705 181 SER B CB  
6193 O OG  . SER B 189 ? 1.76312 0.93632 0.61024 0.48021  0.13231  -0.03883 181 SER B OG  
6194 N N   . VAL B 190 ? 1.62185 0.84291 0.51099 0.47348  0.09945  -0.04613 182 VAL B N   
6195 C CA  . VAL B 190 ? 1.68880 0.91021 0.58611 0.46148  0.08483  -0.04735 182 VAL B CA  
6196 C C   . VAL B 190 ? 1.71131 0.94910 0.62035 0.46439  0.07756  -0.04930 182 VAL B C   
6197 O O   . VAL B 190 ? 1.73562 0.96856 0.63370 0.47915  0.08211  -0.04633 182 VAL B O   
6198 C CB  . VAL B 190 ? 1.67735 0.86830 0.55288 0.45769  0.08305  -0.04481 182 VAL B CB  
6199 C CG1 . VAL B 190 ? 1.62510 0.81528 0.50262 0.44756  0.07071  -0.04911 182 VAL B CG1 
6200 C CG2 . VAL B 190 ? 1.68110 0.85460 0.54095 0.45826  0.08918  -0.04268 182 VAL B CG2 
6201 N N   . PHE B 191 ? 1.61629 0.87102 0.54386 0.45317  0.06726  -0.05357 183 PHE B N   
6202 C CA  . PHE B 191 ? 1.59644 0.86269 0.53290 0.45391  0.05975  -0.05526 183 PHE B CA  
6203 C C   . PHE B 191 ? 1.54413 0.81937 0.49417 0.43998  0.05006  -0.05939 183 PHE B C   
6204 O O   . PHE B 191 ? 1.58555 0.86748 0.54336 0.43306  0.04902  -0.06149 183 PHE B O   
6205 C CB  . PHE B 191 ? 1.58320 0.87497 0.52856 0.46730  0.06120  -0.05835 183 PHE B CB  
6206 C CG  . PHE B 191 ? 1.55488 0.87549 0.52049 0.46018  0.06241  -0.06653 183 PHE B CG  
6207 C CD1 . PHE B 191 ? 1.53068 0.87032 0.51496 0.44938  0.05421  -0.07192 183 PHE B CD1 
6208 C CD2 . PHE B 191 ? 1.55397 0.88024 0.51756 0.46346  0.07451  -0.06994 183 PHE B CD2 
6209 C CE1 . PHE B 191 ? 1.53294 0.89407 0.53162 0.44175  0.05782  -0.08048 183 PHE B CE1 
6210 C CE2 . PHE B 191 ? 1.58808 0.93592 0.56640 0.45445  0.07979  -0.07965 183 PHE B CE2 
6211 C CZ  . PHE B 191 ? 1.57643 0.94044 0.57132 0.44356  0.07132  -0.08489 183 PHE B CZ  
6212 N N   . LEU B 192 ? 1.51947 0.79122 0.46805 0.43806  0.04462  -0.06002 184 LEU B N   
6213 C CA  . LEU B 192 ? 1.51564 0.79706 0.47602 0.42585  0.03657  -0.06481 184 LEU B CA  
6214 C C   . LEU B 192 ? 1.53685 0.84636 0.51797 0.42702  0.03241  -0.06790 184 LEU B C   
6215 O O   . LEU B 192 ? 1.56879 0.88765 0.55061 0.43815  0.03447  -0.06719 184 LEU B O   
6216 C CB  . LEU B 192 ? 1.55315 0.81238 0.49651 0.41987  0.03657  -0.06576 184 LEU B CB  
6217 C CG  . LEU B 192 ? 1.61884 0.85780 0.54429 0.41160  0.03929  -0.06875 184 LEU B CG  
6218 C CD1 . LEU B 192 ? 1.60986 0.82258 0.51254 0.40500  0.04499  -0.07100 184 LEU B CD1 
6219 C CD2 . LEU B 192 ? 1.58692 0.84405 0.52487 0.40073  0.03226  -0.07624 184 LEU B CD2 
6220 N N   . SER B 193 ? 1.47174 0.79572 0.46787 0.41684  0.02675  -0.07235 185 SER B N   
6221 C CA  . SER B 193 ? 1.43872 0.78677 0.45248 0.41465  0.02233  -0.07686 185 SER B CA  
6222 C C   . SER B 193 ? 1.43167 0.78122 0.45139 0.40352  0.01679  -0.07996 185 SER B C   
6223 O O   . SER B 193 ? 1.46560 0.80918 0.48279 0.39804  0.01599  -0.08067 185 SER B O   
6224 C CB  . SER B 193 ? 1.45244 0.82452 0.48184 0.41342  0.02549  -0.08176 185 SER B CB  
6225 O OG  . SER B 193 ? 1.40708 0.77992 0.44252 0.40444  0.02542  -0.08331 185 SER B OG  
6226 N N   . CYS B 194 ? 1.43293 0.79177 0.45897 0.40174  0.01324  -0.08251 186 CYS B N   
6227 C CA  . CYS B 194 ? 1.40092 0.76594 0.43475 0.39111  0.00923  -0.08675 186 CYS B CA  
6228 C C   . CYS B 194 ? 1.38536 0.77050 0.43292 0.39070  0.00625  -0.09052 186 CYS B C   
6229 O O   . CYS B 194 ? 1.39067 0.78311 0.43747 0.39933  0.00627  -0.09065 186 CYS B O   
6230 C CB  . CYS B 194 ? 1.41838 0.76560 0.43759 0.38554  0.01085  -0.08742 186 CYS B CB  
6231 S SG  . CYS B 194 ? 1.44121 0.77110 0.44281 0.39537  0.01403  -0.08288 186 CYS B SG  
6232 N N   . SER B 195 ? 1.37123 0.76675 0.42975 0.38203  0.00377  -0.09465 187 SER B N   
6233 C CA  . SER B 195 ? 1.37552 0.79004 0.44694 0.37890  0.00192  -0.09995 187 SER B CA  
6234 C C   . SER B 195 ? 1.39456 0.81053 0.46959 0.37083  -0.00024 -0.10279 187 SER B C   
6235 O O   . SER B 195 ? 1.39702 0.80500 0.46743 0.36674  -0.00006 -0.10259 187 SER B O   
6236 C CB  . SER B 195 ? 1.36806 0.79424 0.44879 0.37640  0.00532  -0.10338 187 SER B CB  
6237 O OG  . SER B 195 ? 1.40047 0.84343 0.49178 0.36986  0.00533  -0.11102 187 SER B OG  
6238 N N   . GLU B 196 ? 1.42785 0.85697 0.51092 0.36770  -0.00156 -0.10757 188 GLU B N   
6239 C CA  . GLU B 196 ? 1.41456 0.84649 0.50098 0.36049  -0.00244 -0.11096 188 GLU B CA  
6240 C C   . GLU B 196 ? 1.42113 0.85747 0.51492 0.35669  -0.00150 -0.11272 188 GLU B C   
6241 O O   . GLU B 196 ? 1.48252 0.92313 0.57954 0.35203  -0.00167 -0.11609 188 GLU B O   
6242 C CB  . GLU B 196 ? 1.37915 0.82149 0.46805 0.35995  -0.00392 -0.11559 188 GLU B CB  
6243 C CG  . GLU B 196 ? 1.40853 0.84790 0.48690 0.36973  -0.00577 -0.11361 188 GLU B CG  
6244 C CD  . GLU B 196 ? 1.49352 0.93857 0.56714 0.37194  -0.00831 -0.11748 188 GLU B CD  
6245 O OE1 . GLU B 196 ? 1.48311 0.93787 0.56455 0.36352  -0.00833 -0.12335 188 GLU B OE1 
6246 O OE2 . GLU B 196 ? 1.54117 0.97878 0.60027 0.38389  -0.00991 -0.11436 188 GLU B OE2 
6247 N N   . ASP B 197 ? 1.33230 0.76570 0.42572 0.36023  0.00047  -0.11032 189 ASP B N   
6248 C CA  . ASP B 197 ? 1.36082 0.79069 0.45314 0.36211  0.00190  -0.10940 189 ASP B CA  
6249 C C   . ASP B 197 ? 1.33964 0.76666 0.42662 0.36485  -0.00155 -0.10837 189 ASP B C   
6250 O O   . ASP B 197 ? 1.34540 0.77157 0.42881 0.37040  -0.00223 -0.10798 189 ASP B O   
6251 C CB  . ASP B 197 ? 1.34637 0.76922 0.43459 0.36500  0.00781  -0.10732 189 ASP B CB  
6252 C CG  . ASP B 197 ? 1.34844 0.76259 0.42929 0.37041  0.00851  -0.10243 189 ASP B CG  
6253 O OD1 . ASP B 197 ? 1.34895 0.76121 0.42716 0.37184  0.00429  -0.10073 189 ASP B OD1 
6254 O OD2 . ASP B 197 ? 1.36519 0.77214 0.44075 0.37215  0.01529  -0.10105 189 ASP B OD2 
6255 N N   . ASN B 198 ? 1.36709 0.79208 0.45069 0.36147  -0.00268 -0.10914 190 ASN B N   
6256 C CA  . ASN B 198 ? 1.39986 0.82642 0.47815 0.35771  -0.00384 -0.11361 190 ASN B CA  
6257 C C   . ASN B 198 ? 1.37640 0.79410 0.44551 0.36410  -0.00439 -0.11038 190 ASN B C   
6258 O O   . ASN B 198 ? 1.38864 0.81214 0.45302 0.36114  -0.00605 -0.11674 190 ASN B O   
6259 C CB  . ASN B 198 ? 1.34703 0.79081 0.43171 0.35433  -0.00565 -0.12168 190 ASN B CB  
6260 C CG  . ASN B 198 ? 1.38773 0.84255 0.46959 0.34405  -0.00486 -0.13266 190 ASN B CG  
6261 O OD1 . ASN B 198 ? 1.44946 0.89434 0.52330 0.33603  -0.00082 -0.13418 190 ASN B OD1 
6262 N ND2 . ASN B 198 ? 1.56887 1.04488 0.65530 0.34401  -0.00753 -0.14202 190 ASN B ND2 
6263 N N   . ARG B 199 ? 1.36290 0.76948 0.42886 0.37117  -0.00220 -0.10301 191 ARG B N   
6264 C CA  . ARG B 199 ? 1.37632 0.77065 0.43100 0.37816  -0.00096 -0.09878 191 ARG B CA  
6265 C C   . ARG B 199 ? 1.43733 0.81965 0.48368 0.37739  0.00176  -0.09634 191 ARG B C   
6266 O O   . ARG B 199 ? 1.43269 0.81445 0.48217 0.37791  0.00372  -0.09411 191 ARG B O   
6267 C CB  . ARG B 199 ? 1.37803 0.76548 0.43122 0.38490  0.00351  -0.09329 191 ARG B CB  
6268 C CG  . ARG B 199 ? 1.38084 0.76936 0.43312 0.38939  0.00348  -0.09337 191 ARG B CG  
6269 C CD  . ARG B 199 ? 1.39443 0.76720 0.43665 0.39474  0.01200  -0.08803 191 ARG B CD  
6270 N NE  . ARG B 199 ? 1.40746 0.77210 0.44089 0.40199  0.01422  -0.08619 191 ARG B NE  
6271 C CZ  . ARG B 199 ? 1.44019 0.80299 0.47592 0.39785  0.02078  -0.08766 191 ARG B CZ  
6272 N NH1 . ARG B 199 ? 1.39218 0.76644 0.44179 0.38504  0.02467  -0.09336 191 ARG B NH1 
6273 N NH2 . ARG B 199 ? 1.42957 0.77688 0.44951 0.40871  0.02376  -0.08413 191 ARG B NH2 
6274 N N   . ILE B 200 ? 1.50847 0.88190 0.54245 0.37737  0.00193  -0.09766 192 ILE B N   
6275 C CA  . ILE B 200 ? 1.48659 0.84147 0.50680 0.38030  0.00643  -0.09340 192 ILE B CA  
6276 C C   . ILE B 200 ? 1.47530 0.82118 0.48771 0.38940  0.00826  -0.08841 192 ILE B C   
6277 O O   . ILE B 200 ? 1.63097 0.97798 0.63690 0.39073  0.00518  -0.09165 192 ILE B O   
6278 C CB  . ILE B 200 ? 1.48533 0.83283 0.49278 0.37073  0.00806  -0.10028 192 ILE B CB  
6279 C CG1 . ILE B 200 ? 1.52665 0.88324 0.53960 0.35914  0.00847  -0.10740 192 ILE B CG1 
6280 C CG2 . ILE B 200 ? 1.52144 0.84427 0.51139 0.37504  0.01440  -0.09464 192 ILE B CG2 
6281 C CD1 . ILE B 200 ? 1.56174 0.92714 0.56885 0.34392  0.00986  -0.12171 192 ILE B CD1 
6282 N N   . LEU B 201 ? 1.44829 0.78822 0.46057 0.39572  0.01359  -0.08225 193 LEU B N   
6283 C CA  . LEU B 201 ? 1.50935 0.83803 0.51202 0.40312  0.01905  -0.07744 193 LEU B CA  
6284 C C   . LEU B 201 ? 1.56019 0.87141 0.54731 0.40727  0.02374  -0.07418 193 LEU B C   
6285 O O   . LEU B 201 ? 1.48574 0.79715 0.47439 0.40911  0.02673  -0.07271 193 LEU B O   
6286 C CB  . LEU B 201 ? 1.50664 0.84459 0.51966 0.40342  0.02532  -0.07662 193 LEU B CB  
6287 C CG  . LEU B 201 ? 1.41442 0.76558 0.43986 0.39854  0.02326  -0.08009 193 LEU B CG  
6288 C CD1 . LEU B 201 ? 1.41028 0.77038 0.44326 0.39466  0.03285  -0.08322 193 LEU B CD1 
6289 C CD2 . LEU B 201 ? 1.45657 0.79882 0.47256 0.40297  0.02037  -0.07848 193 LEU B CD2 
6290 N N   . LEU B 202 ? 1.57346 0.86983 0.54389 0.41046  0.02430  -0.07342 194 LEU B N   
6291 C CA  . LEU B 202 ? 1.57626 0.85192 0.52845 0.41602  0.03124  -0.06925 194 LEU B CA  
6292 C C   . LEU B 202 ? 1.53519 0.80695 0.48601 0.42279  0.04024  -0.06376 194 LEU B C   
6293 O O   . LEU B 202 ? 1.58933 0.85794 0.53618 0.42527  0.04088  -0.06256 194 LEU B O   
6294 C CB  . LEU B 202 ? 1.53843 0.80209 0.47194 0.41501  0.02804  -0.07334 194 LEU B CB  
6295 C CG  . LEU B 202 ? 1.59782 0.83678 0.50872 0.42092  0.03554  -0.06935 194 LEU B CG  
6296 C CD1 . LEU B 202 ? 1.64895 0.87689 0.55569 0.42112  0.04204  -0.06632 194 LEU B CD1 
6297 C CD2 . LEU B 202 ? 1.59153 0.82389 0.48383 0.41783  0.03109  -0.07707 194 LEU B CD2 
6298 N N   . TRP B 203 ? 1.51077 0.78349 0.46331 0.42594  0.04828  -0.06160 195 TRP B N   
6299 C CA  . TRP B 203 ? 1.53187 0.80778 0.48593 0.42835  0.06049  -0.06051 195 TRP B CA  
6300 C C   . TRP B 203 ? 1.67513 0.92620 0.60624 0.43600  0.06948  -0.05538 195 TRP B C   
6301 O O   . TRP B 203 ? 1.68425 0.92220 0.60375 0.43919  0.06721  -0.05356 195 TRP B O   
6302 C CB  . TRP B 203 ? 1.55694 0.85505 0.52528 0.42991  0.06398  -0.06516 195 TRP B CB  
6303 C CG  . TRP B 203 ? 1.56264 0.88395 0.55123 0.42211  0.05724  -0.07114 195 TRP B CG  
6304 C CD1 . TRP B 203 ? 1.52261 0.85417 0.52282 0.41720  0.04601  -0.07253 195 TRP B CD1 
6305 C CD2 . TRP B 203 ? 1.54160 0.87613 0.53874 0.41702  0.06371  -0.07771 195 TRP B CD2 
6306 N NE1 . TRP B 203 ? 1.50498 0.85599 0.52093 0.41085  0.04352  -0.07837 195 TRP B NE1 
6307 C CE2 . TRP B 203 ? 1.52123 0.87432 0.53543 0.41012  0.05408  -0.08220 195 TRP B CE2 
6308 C CE3 . TRP B 203 ? 1.56945 0.89945 0.55959 0.41607  0.07931  -0.08158 195 TRP B CE3 
6309 C CZ2 . TRP B 203 ? 1.48856 0.85584 0.51260 0.40264  0.05825  -0.09050 195 TRP B CZ2 
6310 C CZ3 . TRP B 203 ? 1.50658 0.84968 0.50634 0.40717  0.08534  -0.09109 195 TRP B CZ3 
6311 C CH2 . TRP B 203 ? 1.48550 0.84716 0.50184 0.40069  0.07421  -0.09554 195 TRP B CH2 
6312 N N   . ASP B 204 ? 1.71366 0.95191 0.63242 0.43989  0.08124  -0.05292 196 ASP B N   
6313 C CA  . ASP B 204 ? 1.63263 0.84579 0.52771 0.44794  0.09392  -0.04792 196 ASP B CA  
6314 C C   . ASP B 204 ? 1.66734 0.87806 0.55849 0.44834  0.11186  -0.04934 196 ASP B C   
6315 O O   . ASP B 204 ? 1.67412 0.86542 0.55096 0.44856  0.11688  -0.04587 196 ASP B O   
6316 C CB  . ASP B 204 ? 1.75016 0.93802 0.62351 0.45095  0.08860  -0.04366 196 ASP B CB  
6317 C CG  . ASP B 204 ? 1.80393 0.96666 0.65344 0.45811  0.09738  -0.03945 196 ASP B CG  
6318 O OD1 . ASP B 204 ? 1.76934 0.92668 0.61315 0.46310  0.11282  -0.03733 196 ASP B OD1 
6319 O OD2 . ASP B 204 ? 1.77374 0.92223 0.60828 0.45891  0.08985  -0.03993 196 ASP B OD2 
6320 N N   . THR B 205 ? 1.65451 0.88462 0.55655 0.44916  0.12254  -0.05588 197 THR B N   
6321 C CA  . THR B 205 ? 1.69363 0.93286 0.59986 0.44478  0.14288  -0.06470 197 THR B CA  
6322 C C   . THR B 205 ? 1.77192 0.97637 0.65085 0.44855  0.16293  -0.05898 197 THR B C   
6323 O O   . THR B 205 ? 1.75918 0.96241 0.63749 0.44244  0.18447  -0.06652 197 THR B O   
6324 C CB  . THR B 205 ? 1.68915 0.96608 0.61598 0.44723  0.14816  -0.07746 197 THR B CB  
6325 O OG1 . THR B 205 ? 1.69048 0.96031 0.60649 0.46019  0.14951  -0.07202 197 THR B OG1 
6326 C CG2 . THR B 205 ? 1.68649 0.99478 0.63619 0.44442  0.13058  -0.08342 197 THR B CG2 
6327 N N   . ARG B 206 ? 1.79646 0.97226 0.65270 0.45721  0.15826  -0.04781 198 ARG B N   
6328 C CA  . ARG B 206 ? 1.77045 0.90563 0.59409 0.46294  0.17465  -0.03974 198 ARG B CA  
6329 C C   . ARG B 206 ? 1.77670 0.88595 0.58301 0.46179  0.17652  -0.03440 198 ARG B C   
6330 O O   . ARG B 206 ? 1.92801 1.00556 0.70974 0.46378  0.19856  -0.03059 198 ARG B O   
6331 C CB  . ARG B 206 ? 1.77551 0.88874 0.57929 0.47224  0.16557  -0.03142 198 ARG B CB  
6332 C CG  . ARG B 206 ? 1.76286 0.88881 0.57305 0.47717  0.16985  -0.03393 198 ARG B CG  
6333 C CD  . ARG B 206 ? 1.77469 0.87441 0.56241 0.48439  0.16340  -0.02699 198 ARG B CD  
6334 N NE  . ARG B 206 ? 1.80255 0.90826 0.59736 0.48018  0.14091  -0.02792 198 ARG B NE  
6335 C CZ  . ARG B 206 ? 1.77954 0.87370 0.56407 0.48190  0.13432  -0.02713 198 ARG B CZ  
6336 N NH1 . ARG B 206 ? 1.79090 0.86466 0.55588 0.49026  0.14669  -0.02336 198 ARG B NH1 
6337 N NH2 . ARG B 206 ? 1.76246 0.86469 0.55519 0.47417  0.11751  -0.03128 198 ARG B NH2 
6338 N N   . CYS B 207 ? 1.75856 0.87848 0.57521 0.46000  0.15630  -0.03399 199 CYS B N   
6339 C CA  . CYS B 207 ? 1.80875 0.90521 0.60768 0.46359  0.15500  -0.02831 199 CYS B CA  
6340 C C   . CYS B 207 ? 1.78795 0.88781 0.59429 0.45330  0.17275  -0.03451 199 CYS B C   
6341 O O   . CYS B 207 ? 1.77540 0.91077 0.61148 0.44169  0.17661  -0.04699 199 CYS B O   
6342 C CB  . CYS B 207 ? 1.77280 0.88679 0.58488 0.46529  0.12844  -0.02888 199 CYS B CB  
6343 S SG  . CYS B 207 ? 1.85405 0.96847 0.66068 0.47170  0.11017  -0.02821 199 CYS B SG  
6344 N N   . PRO B 208 ? 1.82835 0.88966 0.60549 0.45815  0.18509  -0.02726 200 PRO B N   
6345 C CA  . PRO B 208 ? 1.82255 0.88111 0.60379 0.44634  0.20393  -0.03426 200 PRO B CA  
6346 C C   . PRO B 208 ? 1.78120 0.87013 0.58818 0.44054  0.18486  -0.03994 200 PRO B C   
6347 O O   . PRO B 208 ? 1.80684 0.91407 0.63300 0.42571  0.19622  -0.05268 200 PRO B O   
6348 C CB  . PRO B 208 ? 1.89044 0.88587 0.62231 0.45799  0.22283  -0.02034 200 PRO B CB  
6349 C CG  . PRO B 208 ? 1.89902 0.87729 0.60785 0.47994  0.19955  -0.00715 200 PRO B CG  
6350 C CD  . PRO B 208 ? 1.89747 0.91240 0.63243 0.47689  0.18317  -0.01283 200 PRO B CD  
6351 N N   . LYS B 209 ? 1.81667 0.91109 0.62403 0.45167  0.15832  -0.03290 201 LYS B N   
6352 C CA  . LYS B 209 ? 1.69435 0.82338 0.53054 0.44668  0.13731  -0.03856 201 LYS B CA  
6353 C C   . LYS B 209 ? 1.65741 0.82318 0.52147 0.44395  0.11687  -0.04301 201 LYS B C   
6354 O O   . LYS B 209 ? 1.64397 0.80972 0.50438 0.45261  0.10000  -0.03910 201 LYS B O   
6355 C CB  . LYS B 209 ? 1.71276 0.81977 0.52766 0.46189  0.12680  -0.02963 201 LYS B CB  
6356 C CG  . LYS B 209 ? 1.76645 0.83894 0.55677 0.46349  0.14572  -0.02567 201 LYS B CG  
6357 C CD  . LYS B 209 ? 1.76669 0.82517 0.53990 0.48153  0.13247  -0.01815 201 LYS B CD  
6358 C CE  . LYS B 209 ? 1.81375 0.83106 0.55757 0.48427  0.15353  -0.01267 201 LYS B CE  
6359 N NZ  . LYS B 209 ? 1.81440 0.83178 0.55212 0.50002  0.13822  -0.00872 201 LYS B NZ  
6360 N N   . PRO B 210 ? 1.62204 0.81906 0.51250 0.43263  0.11946  -0.05285 202 PRO B N   
6361 C CA  . PRO B 210 ? 1.62978 0.84891 0.53634 0.43302  0.10614  -0.05447 202 PRO B CA  
6362 C C   . PRO B 210 ? 1.57693 0.81575 0.50100 0.43147  0.08377  -0.05528 202 PRO B C   
6363 O O   . PRO B 210 ? 1.65886 0.90026 0.58407 0.43339  0.07560  -0.05428 202 PRO B O   
6364 C CB  . PRO B 210 ? 1.58425 0.83262 0.51206 0.42524  0.11482  -0.06582 202 PRO B CB  
6365 C CG  . PRO B 210 ? 1.58297 0.83735 0.51731 0.41542  0.12588  -0.07458 202 PRO B CG  
6366 C CD  . PRO B 210 ? 1.62240 0.83401 0.52579 0.42040  0.13698  -0.06484 202 PRO B CD  
6367 N N   . ALA B 211 ? 1.55360 0.80403 0.48940 0.42705  0.07686  -0.05807 203 ALA B N   
6368 C CA  . ALA B 211 ? 1.59506 0.86845 0.55103 0.42267  0.05921  -0.06148 203 ALA B CA  
6369 C C   . ALA B 211 ? 1.57456 0.83746 0.51789 0.43059  0.04914  -0.05849 203 ALA B C   
6370 O O   . ALA B 211 ? 1.62177 0.86162 0.54312 0.44067  0.05452  -0.05317 203 ALA B O   
6371 C CB  . ALA B 211 ? 1.57954 0.87375 0.55520 0.41394  0.05821  -0.06779 203 ALA B CB  
6372 N N   . SER B 212 ? 1.57764 0.85219 0.52727 0.42943  0.03610  -0.06257 204 SER B N   
6373 C CA  . SER B 212 ? 1.61991 0.89610 0.56078 0.43568  0.02485  -0.06583 204 SER B CA  
6374 C C   . SER B 212 ? 1.58210 0.88381 0.54250 0.42568  0.01458  -0.07451 204 SER B C   
6375 O O   . SER B 212 ? 1.62158 0.92692 0.58784 0.41728  0.01453  -0.07720 204 SER B O   
6376 C CB  . SER B 212 ? 1.70573 0.96649 0.62504 0.44199  0.02416  -0.06570 204 SER B CB  
6377 O OG  . SER B 212 ? 1.78283 1.05138 0.69262 0.44881  0.01354  -0.07201 204 SER B OG  
6378 N N   . GLN B 213 ? 1.59059 0.90673 0.55777 0.42745  0.00787  -0.07843 205 GLN B N   
6379 C CA  . GLN B 213 ? 1.60758 0.94929 0.59188 0.41720  -0.00022 -0.08810 205 GLN B CA  
6380 C C   . GLN B 213 ? 1.64534 0.99699 0.62190 0.41278  -0.00643 -0.09859 205 GLN B C   
6381 O O   . GLN B 213 ? 1.70544 1.05688 0.66686 0.42316  -0.01068 -0.10109 205 GLN B O   
6382 C CB  . GLN B 213 ? 1.57712 0.93153 0.56845 0.42218  -0.00416 -0.08972 205 GLN B CB  
6383 C CG  . GLN B 213 ? 1.55427 0.90394 0.55556 0.41938  0.00268  -0.08395 205 GLN B CG  
6384 C CD  . GLN B 213 ? 1.52204 0.88276 0.52923 0.42278  -0.00051 -0.08637 205 GLN B CD  
6385 O OE1 . GLN B 213 ? 1.57049 0.91627 0.56722 0.43166  0.00512  -0.08051 205 GLN B OE1 
6386 N NE2 . GLN B 213 ? 1.49555 0.88022 0.51682 0.41523  -0.00756 -0.09536 205 GLN B NE2 
6387 N N   . ILE B 214 ? 2.12763 0.84128 0.65242 0.38385  0.10205  0.12938  206 ILE B N   
6388 C CA  . ILE B 214 ? 2.11581 0.90881 0.64929 0.39008  0.04357  0.12730  206 ILE B CA  
6389 C C   . ILE B 214 ? 2.14224 1.00399 0.77234 0.39062  0.01518  0.10744  206 ILE B C   
6390 O O   . ILE B 214 ? 2.14687 1.00792 0.82891 0.36957  0.03657  0.07642  206 ILE B O   
6391 C CB  . ILE B 214 ? 2.20728 1.01150 0.70334 0.35466  0.04397  0.09449  206 ILE B CB  
6392 C CG1 . ILE B 214 ? 2.05528 0.84294 0.58280 0.31898  0.08390  0.04737  206 ILE B CG1 
6393 C CG2 . ILE B 214 ? 2.21038 0.97906 0.61592 0.35726  0.05144  0.12017  206 ILE B CG2 
6394 C CD1 . ILE B 214 ? 1.95765 0.80749 0.55669 0.30503  0.05975  0.00664  206 ILE B CD1 
6395 N N   . GLY B 215 ? 2.22865 1.15129 0.87850 0.41317  -0.02993 0.12269  207 GLY B N   
6396 C CA  . GLY B 215 ? 2.18469 1.17068 0.91718 0.40998  -0.05500 0.10443  207 GLY B CA  
6397 C C   . GLY B 215 ? 2.32779 1.38826 1.06920 0.43208  -0.10141 0.11730  207 GLY B C   
6398 O O   . GLY B 215 ? 2.42469 1.50392 1.10728 0.44167  -0.12214 0.12996  207 GLY B O   
6399 N N   . CYS B 216 ? 2.32797 1.43726 1.14013 0.43778  -0.11626 0.11020  208 CYS B N   
6400 C CA  . CYS B 216 ? 2.39476 1.59526 1.23455 0.45457  -0.15842 0.11047  208 CYS B CA  
6401 C C   . CYS B 216 ? 2.48896 1.69268 1.31296 0.51193  -0.16739 0.15267  208 CYS B C   
6402 O O   . CYS B 216 ? 2.52728 1.64527 1.31769 0.53288  -0.13426 0.18180  208 CYS B O   
6403 C CB  . CYS B 216 ? 2.39002 1.63628 1.31007 0.43323  -0.16338 0.08182  208 CYS B CB  
6404 S SG  . CYS B 216 ? 2.60120 1.82212 1.53264 0.37714  -0.14925 0.03980  208 CYS B SG  
6405 N N   . SER B 217 ? 2.50969 1.80936 1.35639 0.53679  -0.20837 0.15273  209 SER B N   
6406 C CA  . SER B 217 ? 2.54375 1.86779 1.37647 0.60370  -0.22835 0.19178  209 SER B CA  
6407 C C   . SER B 217 ? 2.55902 1.82087 1.43098 0.63246  -0.19596 0.21253  209 SER B C   
6408 O O   . SER B 217 ? 2.56082 1.76086 1.41215 0.65119  -0.16464 0.24114  209 SER B O   
6409 C CB  . SER B 217 ? 2.47358 1.93840 1.34923 0.61793  -0.27815 0.17122  209 SER B CB  
6410 O OG  . SER B 217 ? 2.47465 1.99671 1.30083 0.59865  -0.30643 0.15620  209 SER B OG  
6411 N N   . ALA B 218 ? 2.65125 1.95110 1.61147 0.61016  -0.19010 0.18237  210 ALA B N   
6412 C CA  . ALA B 218 ? 2.56532 1.82398 1.57762 0.62928  -0.15896 0.19121  210 ALA B CA  
6413 C C   . ALA B 218 ? 2.56046 1.73359 1.57671 0.58279  -0.11089 0.17673  210 ALA B C   
6414 O O   . ALA B 218 ? 2.46234 1.63427 1.46732 0.53554  -0.10983 0.15117  210 ALA B O   
6415 C CB  . ALA B 218 ? 2.46840 1.83176 1.57256 0.62982  -0.18153 0.16246  210 ALA B CB  
6416 N N   . PRO B 219 ? 2.47293 1.57619 1.50580 0.59636  -0.06886 0.18953  211 PRO B N   
6417 C CA  . PRO B 219 ? 2.39558 1.44048 1.44241 0.55193  -0.02414 0.16800  211 PRO B CA  
6418 C C   . PRO B 219 ? 2.22233 1.32910 1.34876 0.51539  -0.02915 0.12993  211 PRO B C   
6419 O O   . PRO B 219 ? 2.15718 1.27697 1.34040 0.52537  -0.01549 0.12582  211 PRO B O   
6420 C CB  . PRO B 219 ? 2.40831 1.39788 1.46504 0.56343  0.02472  0.18359  211 PRO B CB  
6421 C CG  . PRO B 219 ? 2.44347 1.47718 1.53183 0.61648  0.00136  0.20507  211 PRO B CG  
6422 C CD  . PRO B 219 ? 2.46981 1.56895 1.52497 0.64261  -0.05756 0.21478  211 PRO B CD  
6423 N N   . GLY B 220 ? 2.01608 1.15270 1.13936 0.47465  -0.04593 0.10348  212 GLY B N   
6424 C CA  . GLY B 220 ? 1.88834 1.07055 1.06589 0.43773  -0.05116 0.07055  212 GLY B CA  
6425 C C   . GLY B 220 ? 1.76407 0.90433 0.96056 0.41318  -0.01263 0.05579  212 GLY B C   
6426 O O   . GLY B 220 ? 1.82302 0.91132 1.01196 0.42672  0.02215  0.06761  212 GLY B O   
6427 N N   . TYR B 221 ? 1.63685 0.79734 0.85191 0.37802  -0.01649 0.02976  213 TYR B N   
6428 C CA  . TYR B 221 ? 1.54995 0.68965 0.78161 0.35468  0.01281  0.01157  213 TYR B CA  
6429 C C   . TYR B 221 ? 1.55046 0.64642 0.73643 0.34913  0.02790  0.00715  213 TYR B C   
6430 O O   . TYR B 221 ? 1.64957 0.73370 0.79146 0.35391  0.01061  0.01373  213 TYR B O   
6431 C CB  . TYR B 221 ? 1.46650 0.63852 0.71924 0.32542  -0.00013 -0.00928 213 TYR B CB  
6432 C CG  . TYR B 221 ? 1.44896 0.67015 0.75273 0.32312  -0.00702 -0.01388 213 TYR B CG  
6433 C CD1 . TYR B 221 ? 1.41316 0.64367 0.76533 0.32847  0.01841  -0.01639 213 TYR B CD1 
6434 C CD2 . TYR B 221 ? 1.41175 0.67516 0.71872 0.31271  -0.03525 -0.02176 213 TYR B CD2 
6435 C CE1 . TYR B 221 ? 1.38310 0.66545 0.78817 0.32701  0.01372  -0.02570 213 TYR B CE1 
6436 C CE2 . TYR B 221 ? 1.40025 0.72132 0.75979 0.30783  -0.03959 -0.03394 213 TYR B CE2 
6437 C CZ  . TYR B 221 ? 1.38452 0.71615 0.79469 0.31692  -0.01621 -0.03539 213 TYR B CZ  
6438 O OH  . TYR B 221 ? 1.37367 0.76829 0.84133 0.31265  -0.01901 -0.05222 213 TYR B OH  
6439 N N   . LEU B 222 ? 1.53851 0.62079 0.73772 0.33695  0.06035  -0.00912 214 LEU B N   
6440 C CA  . LEU B 222 ? 1.54008 0.59096 0.70781 0.33158  0.08578  -0.02100 214 LEU B CA  
6441 C C   . LEU B 222 ? 1.47959 0.53622 0.61495 0.32394  0.06230  -0.03451 214 LEU B C   
6442 O O   . LEU B 222 ? 1.43760 0.51586 0.58124 0.31597  0.04126  -0.04376 214 LEU B O   
6443 C CB  . LEU B 222 ? 1.47981 0.54159 0.68148 0.31448  0.12364  -0.04583 214 LEU B CB  
6444 C CG  . LEU B 222 ? 1.45883 0.51351 0.69885 0.31584  0.15643  -0.03860 214 LEU B CG  
6445 C CD1 . LEU B 222 ? 1.43132 0.51724 0.70924 0.28554  0.19511  -0.06891 214 LEU B CD1 
6446 C CD2 . LEU B 222 ? 1.52373 0.52834 0.73482 0.33546  0.17225  -0.01047 214 LEU B CD2 
6447 N N   . PRO B 223 ? 1.50443 0.53508 0.59825 0.32597  0.06933  -0.03699 215 PRO B N   
6448 C CA  . PRO B 223 ? 1.56024 0.59509 0.62740 0.32094  0.05283  -0.05545 215 PRO B CA  
6449 C C   . PRO B 223 ? 1.45726 0.54006 0.56123 0.30511  0.06569  -0.08194 215 PRO B C   
6450 O O   . PRO B 223 ? 1.51277 0.61359 0.64433 0.29291  0.09792  -0.09298 215 PRO B O   
6451 C CB  . PRO B 223 ? 1.54408 0.54740 0.56459 0.32326  0.06270  -0.04939 215 PRO B CB  
6452 C CG  . PRO B 223 ? 1.57292 0.54742 0.59520 0.32416  0.10267  -0.03987 215 PRO B CG  
6453 C CD  . PRO B 223 ? 1.55038 0.53916 0.61549 0.33333  0.09715  -0.02248 215 PRO B CD  
6454 N N   . THR B 224 ? 1.47310 0.57785 0.57856 0.30600  0.04093  -0.09115 216 THR B N   
6455 C CA  . THR B 224 ? 1.45695 0.61431 0.59744 0.30250  0.04241  -0.11238 216 THR B CA  
6456 C C   . THR B 224 ? 1.49641 0.67055 0.63002 0.30858  0.02870  -0.12621 216 THR B C   
6457 O O   . THR B 224 ? 1.49619 0.72244 0.66308 0.30500  0.04191  -0.15213 216 THR B O   
6458 C CB  . THR B 224 ? 1.44723 0.60557 0.59167 0.30694  0.02778  -0.10678 216 THR B CB  
6459 O OG1 . THR B 224 ? 1.51050 0.62542 0.61764 0.31220  0.00205  -0.09125 216 THR B OG1 
6460 C CG2 . THR B 224 ? 1.45342 0.61234 0.62191 0.29851  0.04745  -0.10264 216 THR B CG2 
6461 N N   . SER B 225 ? 1.52397 0.66104 0.62108 0.31591  0.00553  -0.11498 217 SER B N   
6462 C CA  . SER B 225 ? 1.53735 0.68129 0.62741 0.32349  -0.00643 -0.12760 217 SER B CA  
6463 C C   . SER B 225 ? 1.54758 0.66166 0.60630 0.31534  -0.00535 -0.12541 217 SER B C   
6464 O O   . SER B 225 ? 1.57925 0.65267 0.60381 0.31232  -0.01000 -0.10848 217 SER B O   
6465 C CB  . SER B 225 ? 1.53540 0.65403 0.60412 0.33759  -0.02960 -0.11999 217 SER B CB  
6466 O OG  . SER B 225 ? 1.60262 0.67495 0.64234 0.32902  -0.03820 -0.10088 217 SER B OG  
6467 N N   . LEU B 226 ? 1.53760 0.67468 0.60601 0.31354  0.00010  -0.14586 218 LEU B N   
6468 C CA  . LEU B 226 ? 1.55151 0.66559 0.58775 0.30315  0.00352  -0.14949 218 LEU B CA  
6469 C C   . LEU B 226 ? 1.54970 0.67707 0.59459 0.30841  -0.00551 -0.16959 218 LEU B C   
6470 O O   . LEU B 226 ? 1.53626 0.71294 0.62258 0.31574  0.00088  -0.19349 218 LEU B O   
6471 C CB  . LEU B 226 ? 1.52821 0.65764 0.56930 0.28723  0.03390  -0.16011 218 LEU B CB  
6472 C CG  . LEU B 226 ? 1.54720 0.64384 0.56630 0.28466  0.05008  -0.13890 218 LEU B CG  
6473 C CD1 . LEU B 226 ? 1.54968 0.65499 0.57387 0.26531  0.08878  -0.15300 218 LEU B CD1 
6474 C CD2 . LEU B 226 ? 1.62648 0.66081 0.57839 0.29388  0.03473  -0.11372 218 LEU B CD2 
6475 N N   . ALA B 227 ? 1.56955 0.65743 0.57696 0.30455  -0.01781 -0.16508 219 ALA B N   
6476 C CA  . ALA B 227 ? 1.63025 0.71907 0.64028 0.30701  -0.02153 -0.18545 219 ALA B CA  
6477 C C   . ALA B 227 ? 1.64061 0.70987 0.61346 0.28605  -0.01718 -0.19194 219 ALA B C   
6478 O O   . ALA B 227 ? 1.65620 0.68846 0.58603 0.27748  -0.02781 -0.17688 219 ALA B O   
6479 C CB  . ALA B 227 ? 1.61670 0.66914 0.61431 0.32148  -0.03814 -0.17649 219 ALA B CB  
6480 N N   . TRP B 228 ? 1.63578 0.73600 0.62399 0.27641  -0.00172 -0.21800 220 TRP B N   
6481 C CA  . TRP B 228 ? 1.69968 0.78881 0.65334 0.25490  0.00390  -0.23120 220 TRP B CA  
6482 C C   . TRP B 228 ? 1.72611 0.78738 0.66871 0.25560  -0.00834 -0.23951 220 TRP B C   
6483 O O   . TRP B 228 ? 1.70417 0.76332 0.67601 0.27602  -0.01290 -0.24559 220 TRP B O   
6484 C CB  . TRP B 228 ? 1.67487 0.81016 0.65675 0.24217  0.02707  -0.26407 220 TRP B CB  
6485 C CG  . TRP B 228 ? 1.67406 0.81994 0.64373 0.22642  0.04882  -0.26011 220 TRP B CG  
6486 C CD1 . TRP B 228 ? 1.64109 0.82916 0.65548 0.22513  0.06797  -0.27424 220 TRP B CD1 
6487 C CD2 . TRP B 228 ? 1.72288 0.83220 0.62410 0.20814  0.05755  -0.24327 220 TRP B CD2 
6488 N NE1 . TRP B 228 ? 1.66860 0.83928 0.64735 0.20473  0.09230  -0.26658 220 TRP B NE1 
6489 C CE2 . TRP B 228 ? 1.72423 0.84022 0.62716 0.19759  0.08573  -0.24384 220 TRP B CE2 
6490 C CE3 . TRP B 228 ? 1.80836 0.88169 0.64251 0.19957  0.04484  -0.22882 220 TRP B CE3 
6491 C CZ2 . TRP B 228 ? 1.78668 0.85558 0.61574 0.18325  0.10342  -0.22391 220 TRP B CZ2 
6492 C CZ3 . TRP B 228 ? 1.82880 0.87169 0.59317 0.18817  0.05614  -0.20979 220 TRP B CZ3 
6493 C CH2 . TRP B 228 ? 1.84088 0.87199 0.59727 0.18235  0.08615  -0.20429 220 TRP B CH2 
6494 N N   . HIS B 229 ? 1.76500 0.80469 0.66185 0.23396  -0.01179 -0.24122 221 HIS B N   
6495 C CA  . HIS B 229 ? 1.82158 0.83791 0.70699 0.22289  -0.01407 -0.25965 221 HIS B CA  
6496 C C   . HIS B 229 ? 1.82793 0.87094 0.74064 0.21838  0.00261  -0.29485 221 HIS B C   
6497 O O   . HIS B 229 ? 1.83903 0.91510 0.74871 0.20342  0.01469  -0.30699 221 HIS B O   
6498 C CB  . HIS B 229 ? 1.84297 0.84687 0.67390 0.19613  -0.02312 -0.25640 221 HIS B CB  
6499 C CG  . HIS B 229 ? 1.91462 0.88872 0.73466 0.18056  -0.02406 -0.27249 221 HIS B CG  
6500 N ND1 . HIS B 229 ? 1.96953 0.93961 0.79789 0.16730  -0.00945 -0.30475 221 HIS B ND1 
6501 C CD2 . HIS B 229 ? 1.95210 0.89761 0.75377 0.17174  -0.03280 -0.26530 221 HIS B CD2 
6502 C CE1 . HIS B 229 ? 1.99388 0.92776 0.80717 0.15085  -0.00700 -0.31517 221 HIS B CE1 
6503 N NE2 . HIS B 229 ? 1.99285 0.91268 0.78933 0.15076  -0.02052 -0.29231 221 HIS B NE2 
6504 N N   . PRO B 230 ? 1.82310 0.84973 0.76062 0.23218  0.00610  -0.31335 222 PRO B N   
6505 C CA  . PRO B 230 ? 1.86624 0.92426 0.83958 0.23525  0.02181  -0.35109 222 PRO B CA  
6506 C C   . PRO B 230 ? 1.97068 1.04087 0.92400 0.20003  0.03530  -0.38139 222 PRO B C   
6507 O O   . PRO B 230 ? 1.87092 0.98157 0.85469 0.19606  0.05076  -0.41482 222 PRO B O   
6508 C CB  . PRO B 230 ? 1.93215 0.95044 0.92166 0.26529  0.01977  -0.35643 222 PRO B CB  
6509 C CG  . PRO B 230 ? 1.86110 0.83538 0.82743 0.27931  0.00357  -0.31699 222 PRO B CG  
6510 C CD  . PRO B 230 ? 1.84887 0.82105 0.77734 0.24677  -0.00205 -0.29999 222 PRO B CD  
6511 N N   . GLN B 231 ? 2.05397 1.09791 0.95871 0.17352  0.02971  -0.37408 223 GLN B N   
6512 C CA  . GLN B 231 ? 2.10911 1.16684 0.98873 0.13742  0.04041  -0.40492 223 GLN B CA  
6513 C C   . GLN B 231 ? 2.10304 1.18713 0.93015 0.11131  0.03350  -0.38938 223 GLN B C   
6514 O O   . GLN B 231 ? 2.13001 1.24663 0.94064 0.08587  0.04473  -0.41305 223 GLN B O   
6515 C CB  . GLN B 231 ? 2.18766 1.20078 1.05310 0.12514  0.04227  -0.41761 223 GLN B CB  
6516 C CG  . GLN B 231 ? 2.21414 1.19427 1.11998 0.14989  0.05568  -0.43901 223 GLN B CG  
6517 C CD  . GLN B 231 ? 2.27405 1.18275 1.16443 0.15523  0.05610  -0.42781 223 GLN B CD  
6518 O OE1 . GLN B 231 ? 2.21868 1.10589 1.08283 0.15085  0.04353  -0.39859 223 GLN B OE1 
6519 N NE2 . GLN B 231 ? 2.29797 1.16602 1.20371 0.16462  0.07341  -0.45280 223 GLN B NE2 
6520 N N   . GLN B 232 ? 1.99810 1.06843 0.79617 0.11911  0.01549  -0.35148 224 GLN B N   
6521 C CA  . GLN B 232 ? 2.02968 1.11892 0.77413 0.10825  0.00679  -0.32723 224 GLN B CA  
6522 C C   . GLN B 232 ? 2.08346 1.17582 0.84315 0.12699  0.01671  -0.30957 224 GLN B C   
6523 O O   . GLN B 232 ? 2.07073 1.14637 0.85576 0.15277  0.01022  -0.28796 224 GLN B O   
6524 C CB  . GLN B 232 ? 1.99006 1.06949 0.69923 0.11052  -0.01778 -0.29964 224 GLN B CB  
6525 C CG  . GLN B 232 ? 2.01778 1.11458 0.70229 0.07981  -0.02566 -0.32193 224 GLN B CG  
6526 C CD  . GLN B 232 ? 2.07245 1.13145 0.78993 0.07896  -0.02017 -0.33916 224 GLN B CD  
6527 O OE1 . GLN B 232 ? 2.14125 1.17264 0.89792 0.08959  -0.00290 -0.35566 224 GLN B OE1 
6528 N NE2 . GLN B 232 ? 2.01919 1.07842 0.71915 0.06680  -0.03392 -0.33571 224 GLN B NE2 
6529 N N   . SER B 233 ? 2.36512 1.47943 1.10804 0.11017  0.03482  -0.32111 225 SER B N   
6530 C CA  . SER B 233 ? 2.45293 1.57197 1.20656 0.11627  0.05397  -0.31366 225 SER B CA  
6531 C C   . SER B 233 ? 2.44069 1.52625 1.13808 0.12704  0.04633  -0.26747 225 SER B C   
6532 O O   . SER B 233 ? 2.35237 1.42918 1.05870 0.13325  0.06505  -0.25845 225 SER B O   
6533 C CB  . SER B 233 ? 2.38181 1.52961 1.12690 0.08880  0.07924  -0.34361 225 SER B CB  
6534 O OG  . SER B 233 ? 2.46195 1.61973 1.22791 0.08882  0.10328  -0.34683 225 SER B OG  
6535 N N   . GLU B 234 ? 2.25385 1.32805 0.89954 0.12920  0.02115  -0.24292 226 GLU B N   
6536 C CA  . GLU B 234 ? 2.26167 1.31288 0.84441 0.14355  0.01014  -0.19802 226 GLU B CA  
6537 C C   . GLU B 234 ? 2.23501 1.27962 0.83217 0.16910  -0.01717 -0.17555 226 GLU B C   
6538 O O   . GLU B 234 ? 2.33235 1.37043 0.88638 0.18638  -0.03119 -0.13845 226 GLU B O   
6539 C CB  . GLU B 234 ? 2.30972 1.38183 0.82125 0.12610  -0.00030 -0.18803 226 GLU B CB  
6540 C CG  . GLU B 234 ? 2.31344 1.38051 0.78956 0.10184  0.02977  -0.19889 226 GLU B CG  
6541 C CD  . GLU B 234 ? 2.56727 1.64650 0.95849 0.09351  0.01949  -0.17216 226 GLU B CD  
6542 O OE1 . GLU B 234 ? 2.62968 1.69722 0.98084 0.12067  0.00066  -0.12562 226 GLU B OE1 
6543 O OE2 . GLU B 234 ? 2.57274 1.67988 0.94258 0.06280  0.02939  -0.19725 226 GLU B OE2 
6544 N N   . VAL B 235 ? 2.09195 1.13864 0.74667 0.17327  -0.02366 -0.19472 227 VAL B N   
6545 C CA  . VAL B 235 ? 2.00706 1.04428 0.67762 0.19287  -0.04464 -0.17742 227 VAL B CA  
6546 C C   . VAL B 235 ? 1.94885 0.96953 0.68245 0.20950  -0.03302 -0.18294 227 VAL B C   
6547 O O   . VAL B 235 ? 1.92795 0.95862 0.70295 0.20432  -0.01791 -0.20791 227 VAL B O   
6548 C CB  . VAL B 235 ? 1.96161 1.01828 0.62742 0.17631  -0.06546 -0.19245 227 VAL B CB  
6549 C CG1 . VAL B 235 ? 2.05965 1.15532 0.68106 0.15048  -0.07186 -0.20354 227 VAL B CG1 
6550 C CG2 . VAL B 235 ? 1.91095 0.94751 0.62481 0.16997  -0.05644 -0.22010 227 VAL B CG2 
6551 N N   . PHE B 236 ? 1.85871 0.86572 0.60122 0.23003  -0.04124 -0.16066 228 PHE B N   
6552 C CA  . PHE B 236 ? 1.79707 0.79954 0.59774 0.24619  -0.03532 -0.16102 228 PHE B CA  
6553 C C   . PHE B 236 ? 1.77584 0.76435 0.57479 0.25625  -0.05383 -0.14562 228 PHE B C   
6554 O O   . PHE B 236 ? 1.80955 0.80380 0.56971 0.25234  -0.07048 -0.13436 228 PHE B O   
6555 C CB  . PHE B 236 ? 1.76403 0.77320 0.58391 0.25430  -0.01270 -0.15499 228 PHE B CB  
6556 C CG  . PHE B 236 ? 1.77516 0.75927 0.55162 0.26537  -0.00921 -0.12734 228 PHE B CG  
6557 C CD1 . PHE B 236 ? 1.73781 0.71331 0.53230 0.28276  -0.01362 -0.11219 228 PHE B CD1 
6558 C CD2 . PHE B 236 ? 1.85360 0.81984 0.56696 0.26011  0.00101  -0.11486 228 PHE B CD2 
6559 C CE1 . PHE B 236 ? 1.73096 0.69897 0.51453 0.29246  -0.00823 -0.08035 228 PHE B CE1 
6560 C CE2 . PHE B 236 ? 1.83179 0.77726 0.51556 0.27496  0.00574  -0.07950 228 PHE B CE2 
6561 C CZ  . PHE B 236 ? 1.78849 0.74013 0.51958 0.29103  0.00126  -0.06171 228 PHE B CZ  
6562 N N   . VAL B 237 ? 1.69768 0.68241 0.54203 0.26739  -0.05199 -0.14461 229 VAL B N   
6563 C CA  . VAL B 237 ? 1.74227 0.71322 0.59100 0.27457  -0.06323 -0.13132 229 VAL B CA  
6564 C C   . VAL B 237 ? 1.74384 0.72689 0.62719 0.29117  -0.05172 -0.11816 229 VAL B C   
6565 O O   . VAL B 237 ? 1.73346 0.74190 0.65508 0.29505  -0.03844 -0.12573 229 VAL B O   
6566 C CB  . VAL B 237 ? 1.74698 0.69676 0.60829 0.26770  -0.06798 -0.13951 229 VAL B CB  
6567 C CG1 . VAL B 237 ? 1.74113 0.67756 0.56814 0.24291  -0.07376 -0.15702 229 VAL B CG1 
6568 C CG2 . VAL B 237 ? 1.67606 0.63254 0.57439 0.28099  -0.05896 -0.14497 229 VAL B CG2 
6569 N N   . PHE B 238 ? 1.69856 0.68407 0.58437 0.29605  -0.05574 -0.09966 230 PHE B N   
6570 C CA  . PHE B 238 ? 1.67635 0.67101 0.59740 0.30746  -0.04196 -0.09037 230 PHE B CA  
6571 C C   . PHE B 238 ? 1.71030 0.71018 0.65733 0.30431  -0.05304 -0.08126 230 PHE B C   
6572 O O   . PHE B 238 ? 1.70716 0.72081 0.65502 0.29319  -0.06780 -0.07097 230 PHE B O   
6573 C CB  . PHE B 238 ? 1.62119 0.62371 0.54139 0.31137  -0.02773 -0.07076 230 PHE B CB  
6574 C CG  . PHE B 238 ? 1.71886 0.73979 0.64958 0.31509  -0.04166 -0.04284 230 PHE B CG  
6575 C CD1 . PHE B 238 ? 1.73305 0.76791 0.63377 0.31460  -0.06040 -0.03106 230 PHE B CD1 
6576 C CD2 . PHE B 238 ? 1.70832 0.74174 0.68078 0.32092  -0.03610 -0.03171 230 PHE B CD2 
6577 C CE1 . PHE B 238 ? 1.76243 0.82949 0.67748 0.32528  -0.07660 -0.00903 230 PHE B CE1 
6578 C CE2 . PHE B 238 ? 1.75197 0.81043 0.74086 0.32910  -0.04904 -0.01051 230 PHE B CE2 
6579 C CZ  . PHE B 238 ? 1.79453 0.87283 0.75605 0.33404  -0.07079 0.00071  230 PHE B CZ  
6580 N N   . GLY B 239 ? 1.67342 0.67498 0.64379 0.31065  -0.04595 -0.08680 231 GLY B N   
6581 C CA  . GLY B 239 ? 1.63168 0.63087 0.61865 0.30771  -0.04934 -0.08007 231 GLY B CA  
6582 C C   . GLY B 239 ? 1.59243 0.62162 0.61853 0.31029  -0.03416 -0.07070 231 GLY B C   
6583 O O   . GLY B 239 ? 1.59582 0.64503 0.63844 0.31501  -0.01619 -0.07717 231 GLY B O   
6584 N N   . ASP B 240 ? 1.60477 0.65079 0.65576 0.30088  -0.03787 -0.05765 232 ASP B N   
6585 C CA  . ASP B 240 ? 1.51034 0.58109 0.60239 0.30354  -0.02072 -0.04944 232 ASP B CA  
6586 C C   . ASP B 240 ? 1.53812 0.61875 0.65139 0.29645  -0.01274 -0.05789 232 ASP B C   
6587 O O   . ASP B 240 ? 1.57095 0.63350 0.65846 0.29567  -0.02176 -0.06579 232 ASP B O   
6588 C CB  . ASP B 240 ? 1.53268 0.62489 0.64298 0.30412  -0.02983 -0.03278 232 ASP B CB  
6589 C CG  . ASP B 240 ? 1.50867 0.62183 0.63358 0.28662  -0.04559 -0.03607 232 ASP B CG  
6590 O OD1 . ASP B 240 ? 1.55838 0.65107 0.66492 0.27138  -0.04850 -0.04695 232 ASP B OD1 
6591 O OD2 . ASP B 240 ? 1.49632 0.64529 0.64835 0.28943  -0.05313 -0.02903 232 ASP B OD2 
6592 N N   . GLU B 241 ? 1.52656 0.63105 0.68051 0.29340  0.00511  -0.05581 233 GLU B N   
6593 C CA  . GLU B 241 ? 1.46777 0.59153 0.64447 0.28321  0.01690  -0.06602 233 GLU B CA  
6594 C C   . GLU B 241 ? 1.48366 0.61375 0.66958 0.26519  0.00623  -0.06091 233 GLU B C   
6595 O O   . GLU B 241 ? 1.50267 0.64373 0.69615 0.25282  0.01427  -0.06814 233 GLU B O   
6596 C CB  . GLU B 241 ? 1.36991 0.51549 0.58762 0.28276  0.04845  -0.07273 233 GLU B CB  
6597 C CG  . GLU B 241 ? 1.38320 0.53192 0.63300 0.28598  0.05575  -0.05769 233 GLU B CG  
6598 C CD  . GLU B 241 ? 1.42139 0.57225 0.70558 0.28692  0.09417  -0.06376 233 GLU B CD  
6599 O OE1 . GLU B 241 ? 1.43032 0.58799 0.71529 0.27834  0.11774  -0.08489 233 GLU B OE1 
6600 O OE2 . GLU B 241 ? 1.42236 0.56998 0.73271 0.29715  0.10202  -0.05026 233 GLU B OE2 
6601 N N   . ASN B 242 ? 1.52614 0.65665 0.71073 0.26109  -0.00947 -0.05283 234 ASN B N   
6602 C CA  . ASN B 242 ? 1.45065 0.59764 0.64829 0.23775  -0.01654 -0.05644 234 ASN B CA  
6603 C C   . ASN B 242 ? 1.51993 0.62764 0.66510 0.22113  -0.02960 -0.06097 234 ASN B C   
6604 O O   . ASN B 242 ? 1.56198 0.67570 0.70818 0.19342  -0.03028 -0.06943 234 ASN B O   
6605 C CB  . ASN B 242 ? 1.45340 0.64171 0.68806 0.24395  -0.02461 -0.05236 234 ASN B CB  
6606 C CG  . ASN B 242 ? 1.44031 0.66801 0.70796 0.21883  -0.02545 -0.06571 234 ASN B CG  
6607 O OD1 . ASN B 242 ? 1.44848 0.67749 0.72889 0.19894  -0.00998 -0.07468 234 ASN B OD1 
6608 N ND2 . ASN B 242 ? 1.40771 0.67568 0.68915 0.21757  -0.04269 -0.07109 234 ASN B ND2 
6609 N N   . GLY B 243 ? 1.56026 0.62738 0.66144 0.23575  -0.03562 -0.05918 235 GLY B N   
6610 C CA  . GLY B 243 ? 1.64711 0.65851 0.69140 0.22572  -0.04240 -0.06305 235 GLY B CA  
6611 C C   . GLY B 243 ? 1.65795 0.66421 0.68579 0.21780  -0.05410 -0.06866 235 GLY B C   
6612 O O   . GLY B 243 ? 1.75670 0.71070 0.73760 0.20394  -0.05407 -0.07589 235 GLY B O   
6613 N N   . THR B 244 ? 1.58606 0.64047 0.64518 0.22670  -0.06193 -0.06560 236 THR B N   
6614 C CA  . THR B 244 ? 1.61873 0.68568 0.66229 0.22147  -0.07590 -0.07169 236 THR B CA  
6615 C C   . THR B 244 ? 1.62013 0.65354 0.62929 0.24128  -0.07748 -0.07045 236 THR B C   
6616 O O   . THR B 244 ? 1.64077 0.67920 0.66157 0.26451  -0.07080 -0.06156 236 THR B O   
6617 C CB  . THR B 244 ? 1.57154 0.70791 0.65613 0.22993  -0.08650 -0.06552 236 THR B CB  
6618 O OG1 . THR B 244 ? 1.56904 0.74497 0.69074 0.20968  -0.08462 -0.07507 236 THR B OG1 
6619 C CG2 . THR B 244 ? 1.54695 0.70949 0.61155 0.22872  -0.10414 -0.07103 236 THR B CG2 
6620 N N   . VAL B 245 ? 1.60017 0.60048 0.56936 0.22847  -0.08143 -0.08395 237 VAL B N   
6621 C CA  . VAL B 245 ? 1.73866 0.71650 0.67717 0.24210  -0.08325 -0.08978 237 VAL B CA  
6622 C C   . VAL B 245 ? 1.71677 0.73691 0.65059 0.23092  -0.09604 -0.09432 237 VAL B C   
6623 O O   . VAL B 245 ? 1.69296 0.73155 0.62465 0.20316  -0.10152 -0.10820 237 VAL B O   
6624 C CB  . VAL B 245 ? 1.74536 0.65305 0.64100 0.23979  -0.07637 -0.10373 237 VAL B CB  
6625 C CG1 . VAL B 245 ? 1.72356 0.61472 0.59167 0.24669  -0.07719 -0.11792 237 VAL B CG1 
6626 C CG2 . VAL B 245 ? 1.69856 0.57754 0.59449 0.26279  -0.06919 -0.09576 237 VAL B CG2 
6627 N N   . SER B 246 ? 1.62913 0.66677 0.55790 0.24970  -0.09863 -0.08516 238 SER B N   
6628 C CA  . SER B 246 ? 1.72265 0.80487 0.63820 0.24766  -0.11320 -0.08253 238 SER B CA  
6629 C C   . SER B 246 ? 1.73910 0.79662 0.61194 0.24624  -0.10965 -0.09486 238 SER B C   
6630 O O   . SER B 246 ? 1.71199 0.73444 0.57810 0.26055  -0.09483 -0.09566 238 SER B O   
6631 C CB  . SER B 246 ? 1.70653 0.82263 0.64263 0.27287  -0.11628 -0.05539 238 SER B CB  
6632 O OG  . SER B 246 ? 1.79701 0.94689 0.77732 0.27289  -0.12057 -0.04956 238 SER B OG  
6633 N N   . LEU B 247 ? 1.75804 0.84295 0.60608 0.22713  -0.12156 -0.10931 239 LEU B N   
6634 C CA  . LEU B 247 ? 1.82708 0.89953 0.63250 0.22004  -0.11841 -0.12469 239 LEU B CA  
6635 C C   . LEU B 247 ? 1.78082 0.89308 0.56375 0.23495  -0.12877 -0.10287 239 LEU B C   
6636 O O   . LEU B 247 ? 1.83849 1.01159 0.62281 0.23408  -0.15004 -0.09561 239 LEU B O   
6637 C CB  . LEU B 247 ? 1.83756 0.91559 0.62540 0.18485  -0.12124 -0.15772 239 LEU B CB  
6638 C CG  . LEU B 247 ? 1.84804 0.92703 0.59371 0.17017  -0.11860 -0.17959 239 LEU B CG  
6639 C CD1 . LEU B 247 ? 1.88846 0.90894 0.62082 0.18567  -0.09935 -0.18561 239 LEU B CD1 
6640 C CD2 . LEU B 247 ? 1.87508 0.95501 0.60764 0.12987  -0.11445 -0.21799 239 LEU B CD2 
6641 N N   . VAL B 248 ? 1.77568 0.85567 0.53505 0.24849  -0.11293 -0.09474 240 VAL B N   
6642 C CA  . VAL B 248 ? 1.91733 1.00802 0.64088 0.26557  -0.11358 -0.06702 240 VAL B CA  
6643 C C   . VAL B 248 ? 1.95895 1.04590 0.62614 0.24859  -0.10952 -0.08393 240 VAL B C   
6644 O O   . VAL B 248 ? 1.91364 0.96879 0.57882 0.23355  -0.09230 -0.11445 240 VAL B O   
6645 C CB  . VAL B 248 ? 1.84600 0.89536 0.58012 0.28612  -0.08831 -0.04737 240 VAL B CB  
6646 C CG1 . VAL B 248 ? 1.85059 0.87988 0.52872 0.29707  -0.07580 -0.02372 240 VAL B CG1 
6647 C CG2 . VAL B 248 ? 1.79379 0.85487 0.57849 0.30324  -0.09233 -0.02774 240 VAL B CG2 
6648 N N   . ASP B 249 ? 1.98483 1.10582 0.60653 0.25450  -0.12534 -0.06451 241 ASP B N   
6649 C CA  . ASP B 249 ? 2.11201 1.22930 0.66572 0.24071  -0.11954 -0.07173 241 ASP B CA  
6650 C C   . ASP B 249 ? 2.23836 1.31842 0.75369 0.26310  -0.10173 -0.03302 241 ASP B C   
6651 O O   . ASP B 249 ? 2.32853 1.42330 0.83516 0.29398  -0.11741 0.00619  241 ASP B O   
6652 C CB  . ASP B 249 ? 2.18567 1.37904 0.71884 0.22685  -0.14983 -0.08002 241 ASP B CB  
6653 C CG  . ASP B 249 ? 2.24911 1.45982 0.74470 0.19886  -0.14098 -0.09732 241 ASP B CG  
6654 O OD1 . ASP B 249 ? 2.30687 1.47533 0.77412 0.20048  -0.11647 -0.08464 241 ASP B OD1 
6655 O OD2 . ASP B 249 ? 2.13592 1.40357 0.62909 0.17136  -0.15551 -0.12745 241 ASP B OD2 
6656 N N   . THR B 250 ? 2.29442 1.32825 0.79348 0.24770  -0.06695 -0.04616 242 THR B N   
6657 C CA  . THR B 250 ? 2.34821 1.33017 0.80029 0.25729  -0.03745 -0.01756 242 THR B CA  
6658 C C   . THR B 250 ? 2.47066 1.47773 0.86460 0.26187  -0.05270 0.01198  242 THR B C   
6659 O O   . THR B 250 ? 2.47575 1.45092 0.83661 0.28921  -0.04594 0.05551  242 THR B O   
6660 C CB  . THR B 250 ? 2.24517 1.19000 0.70054 0.22957  0.00466  -0.05164 242 THR B CB  
6661 O OG1 . THR B 250 ? 2.38699 1.36807 0.84039 0.19859  0.00103  -0.08401 242 THR B OG1 
6662 C CG2 . THR B 250 ? 2.09588 1.03297 0.62109 0.23063  0.01836  -0.07939 242 THR B CG2 
6663 N N   . LYS B 251 ? 2.61068 1.67408 0.99538 0.23664  -0.07095 -0.01231 243 LYS B N   
6664 C CA  . LYS B 251 ? 2.65882 1.76505 0.98729 0.23460  -0.08755 0.00696  243 LYS B CA  
6665 C C   . LYS B 251 ? 2.68691 1.84817 1.01989 0.27457  -0.12718 0.04607  243 LYS B C   
6666 O O   . LYS B 251 ? 2.74291 1.90367 1.02766 0.29758  -0.13151 0.08659  243 LYS B O   
6667 C CB  . LYS B 251 ? 2.61919 1.78430 0.94979 0.19364  -0.09659 -0.03894 243 LYS B CB  
6668 C CG  . LYS B 251 ? 2.72415 1.92355 0.98906 0.17766  -0.09906 -0.03135 243 LYS B CG  
6669 C CD  . LYS B 251 ? 2.73316 1.98400 1.00512 0.13150  -0.09785 -0.08480 243 LYS B CD  
6670 C CE  . LYS B 251 ? 2.78717 2.06168 0.99103 0.10971  -0.09004 -0.08226 243 LYS B CE  
6671 N NZ  . LYS B 251 ? 2.73429 2.07228 0.95095 0.06556  -0.09055 -0.13759 243 LYS B NZ  
6672 N N   . SER B 252 ? 2.51920 1.72678 0.90857 0.28287  -0.15358 0.03256  244 SER B N   
6673 C CA  . SER B 252 ? 2.51225 1.79812 0.92203 0.31656  -0.19500 0.05503  244 SER B CA  
6674 C C   . SER B 252 ? 2.51382 1.75548 0.94925 0.36218  -0.18897 0.09494  244 SER B C   
6675 O O   . SER B 252 ? 2.51478 1.81280 0.96127 0.40056  -0.21803 0.12290  244 SER B O   
6676 C CB  . SER B 252 ? 2.48524 1.84244 0.93802 0.29378  -0.22039 0.01140  244 SER B CB  
6677 O OG  . SER B 252 ? 2.53224 1.99571 0.99257 0.31388  -0.26220 0.01877  244 SER B OG  
6678 N N   . THR B 253 ? 2.51821 1.67150 0.96741 0.35762  -0.15238 0.09246  245 THR B N   
6679 C CA  . THR B 253 ? 2.54584 1.64300 1.01950 0.39138  -0.13376 0.12308  245 THR B CA  
6680 C C   . THR B 253 ? 2.54212 1.70268 1.07519 0.41910  -0.16725 0.12818  245 THR B C   
6681 O O   . THR B 253 ? 2.47832 1.61586 1.03438 0.45519  -0.15957 0.15880  245 THR B O   
6682 C CB  . THR B 253 ? 2.60934 1.65036 1.03204 0.41584  -0.11056 0.16575  245 THR B CB  
6683 O OG1 . THR B 253 ? 2.59965 1.56058 1.04003 0.42784  -0.07264 0.17776  245 THR B OG1 
6684 C CG2 . THR B 253 ? 2.50032 1.60167 0.91430 0.45807  -0.14470 0.20241  245 THR B CG2 
6685 N N   . SER B 254 ? 2.57439 1.80702 1.13144 0.39899  -0.19777 0.09390  246 SER B N   
6686 C CA  . SER B 254 ? 2.45130 1.75770 1.06931 0.41285  -0.22807 0.08525  246 SER B CA  
6687 C C   . SER B 254 ? 2.34872 1.66845 1.02574 0.36362  -0.22084 0.03564  246 SER B C   
6688 O O   . SER B 254 ? 2.43633 1.75621 1.08782 0.32664  -0.21733 0.00443  246 SER B O   
6689 C CB  . SER B 254 ? 2.42626 1.83972 1.02906 0.43506  -0.27242 0.09028  246 SER B CB  
6690 O OG  . SER B 254 ? 2.34102 1.83644 1.01703 0.44701  -0.29651 0.07704  246 SER B OG  
6691 N N   . CYS B 255 ? 2.30937 1.63272 1.05697 0.36398  -0.21592 0.02935  247 CYS B N   
6692 C CA  . CYS B 255 ? 2.24826 1.56354 1.04368 0.32293  -0.20435 -0.00965 247 CYS B CA  
6693 C C   . CYS B 255 ? 2.18978 1.58789 0.99713 0.29171  -0.22766 -0.04706 247 CYS B C   
6694 O O   . CYS B 255 ? 2.14009 1.62074 0.98319 0.30310  -0.25089 -0.04928 247 CYS B O   
6695 C CB  . CYS B 255 ? 2.22965 1.52836 1.08690 0.33306  -0.19224 -0.00216 247 CYS B CB  
6696 S SG  . CYS B 255 ? 2.27231 1.47716 1.12146 0.35656  -0.15580 0.02762  247 CYS B SG  
6697 N N   . VAL B 256 ? 2.20726 1.58580 0.98828 0.25248  -0.21826 -0.08016 248 VAL B N   
6698 C CA  . VAL B 256 ? 2.20384 1.65289 0.98309 0.21287  -0.23179 -0.12348 248 VAL B CA  
6699 C C   . VAL B 256 ? 2.10816 1.56963 0.94225 0.18332  -0.22410 -0.15247 248 VAL B C   
6700 O O   . VAL B 256 ? 2.11147 1.66664 0.96665 0.16278  -0.24074 -0.18132 248 VAL B O   
6701 C CB  . VAL B 256 ? 2.16404 1.57321 0.89544 0.17970  -0.21641 -0.15126 248 VAL B CB  
6702 C CG1 . VAL B 256 ? 2.21086 1.61365 0.88177 0.20189  -0.22169 -0.12634 248 VAL B CG1 
6703 C CG2 . VAL B 256 ? 2.11587 1.42305 0.85560 0.16345  -0.18389 -0.16465 248 VAL B CG2 
6704 N N   . LEU B 257 ? 1.98467 1.36037 0.83759 0.17976  -0.19892 -0.14776 249 LEU B N   
6705 C CA  . LEU B 257 ? 1.93541 1.30305 0.82825 0.15210  -0.18637 -0.16917 249 LEU B CA  
6706 C C   . LEU B 257 ? 1.89070 1.17257 0.79843 0.16984  -0.16611 -0.14571 249 LEU B C   
6707 O O   . LEU B 257 ? 1.85219 1.06348 0.73270 0.18257  -0.15278 -0.13523 249 LEU B O   
6708 C CB  . LEU B 257 ? 1.98905 1.33414 0.85922 0.09900  -0.16949 -0.21541 249 LEU B CB  
6709 C CG  . LEU B 257 ? 2.00881 1.32312 0.90030 0.06249  -0.14800 -0.23934 249 LEU B CG  
6710 C CD1 . LEU B 257 ? 1.83963 1.25779 0.78197 0.05464  -0.16287 -0.25054 249 LEU B CD1 
6711 C CD2 . LEU B 257 ? 2.02215 1.29169 0.87798 0.01025  -0.12333 -0.28391 249 LEU B CD2 
6712 N N   . SER B 258 ? 1.83468 1.13353 0.78613 0.16867  -0.16375 -0.14289 250 SER B N   
6713 C CA  . SER B 258 ? 1.78169 1.01355 0.74974 0.17649  -0.14431 -0.12818 250 SER B CA  
6714 C C   . SER B 258 ? 1.78578 1.00528 0.76479 0.13559  -0.12995 -0.15455 250 SER B C   
6715 O O   . SER B 258 ? 1.77251 1.04956 0.75785 0.10197  -0.13461 -0.18557 250 SER B O   
6716 C CB  . SER B 258 ? 1.68837 0.94731 0.69381 0.21403  -0.14974 -0.09727 250 SER B CB  
6717 O OG  . SER B 258 ? 1.73487 1.08088 0.78268 0.21372  -0.16535 -0.10388 250 SER B OG  
6718 N N   . SER B 259 ? 1.80412 0.95345 0.78077 0.13626  -0.11124 -0.14507 251 SER B N   
6719 C CA  . SER B 259 ? 1.77036 0.88424 0.74244 0.09828  -0.09142 -0.16349 251 SER B CA  
6720 C C   . SER B 259 ? 1.73111 0.80125 0.71323 0.11613  -0.08023 -0.14050 251 SER B C   
6721 O O   . SER B 259 ? 1.72107 0.75510 0.69336 0.15112  -0.08105 -0.11890 251 SER B O   
6722 C CB  . SER B 259 ? 1.80326 0.83828 0.71861 0.06823  -0.07326 -0.18560 251 SER B CB  
6723 O OG  . SER B 259 ? 1.91902 0.91640 0.81964 0.02443  -0.04941 -0.20580 251 SER B OG  
6724 N N   . ALA B 260 ? 1.74036 0.82193 0.74199 0.08934  -0.06849 -0.14993 252 ALA B N   
6725 C CA  . ALA B 260 ? 1.75192 0.79449 0.75633 0.09581  -0.05479 -0.13369 252 ALA B CA  
6726 C C   . ALA B 260 ? 1.78183 0.71273 0.71613 0.08331  -0.03538 -0.13290 252 ALA B C   
6727 O O   . ALA B 260 ? 1.82136 0.71614 0.72794 0.04007  -0.01523 -0.15073 252 ALA B O   
6728 C CB  . ALA B 260 ? 1.74362 0.84765 0.79485 0.06894  -0.04837 -0.14787 252 ALA B CB  
6729 N N   . VAL B 261 ? 1.82747 0.79826 0.67189 0.27291  0.08372  -0.08060 253 VAL B N   
6730 C CA  . VAL B 261 ? 1.89410 0.80749 0.70046 0.28454  0.08396  -0.07978 253 VAL B CA  
6731 C C   . VAL B 261 ? 1.94707 0.84242 0.72772 0.29989  0.09619  -0.06349 253 VAL B C   
6732 O O   . VAL B 261 ? 1.95914 0.81420 0.72233 0.29351  0.10723  -0.05060 253 VAL B O   
6733 C CB  . VAL B 261 ? 1.84956 0.75757 0.64080 0.30395  0.06806  -0.09598 253 VAL B CB  
6734 C CG1 . VAL B 261 ? 1.91692 0.76531 0.67434 0.31452  0.06707  -0.09684 253 VAL B CG1 
6735 C CG2 . VAL B 261 ? 1.79643 0.73408 0.61116 0.29201  0.05604  -0.11237 253 VAL B CG2 
6736 N N   . HIS B 262 ? 1.90983 0.83402 0.68843 0.31912  0.09332  -0.06389 254 HIS B N   
6737 C CA  . HIS B 262 ? 1.91785 0.83036 0.66892 0.33795  0.10142  -0.05207 254 HIS B CA  
6738 C C   . HIS B 262 ? 1.86398 0.81321 0.63480 0.33113  0.11402  -0.04396 254 HIS B C   
6739 O O   . HIS B 262 ? 1.80239 0.79256 0.61137 0.31736  0.11175  -0.04970 254 HIS B O   
6740 C CB  . HIS B 262 ? 1.89424 0.81131 0.62964 0.36567  0.08682  -0.06056 254 HIS B CB  
6741 C CG  . HIS B 262 ? 1.89294 0.78471 0.61922 0.37308  0.07424  -0.06758 254 HIS B CG  
6742 N ND1 . HIS B 262 ? 1.97571 0.81321 0.66421 0.38340  0.07688  -0.06157 254 HIS B ND1 
6743 C CD2 . HIS B 262 ? 1.86433 0.78402 0.62091 0.37112  0.05877  -0.07751 254 HIS B CD2 
6744 C CE1 . HIS B 262 ? 1.92941 0.76393 0.62848 0.38745  0.06293  -0.06834 254 HIS B CE1 
6745 N NE2 . HIS B 262 ? 1.91720 0.80328 0.65714 0.38003  0.05254  -0.07823 254 HIS B NE2 
6746 N N   . SER B 263 ? 1.91132 0.84667 0.65592 0.34164  0.12666  -0.03117 255 SER B N   
6747 C CA  . SER B 263 ? 1.91052 0.87817 0.66634 0.34111  0.14045  -0.02434 255 SER B CA  
6748 C C   . SER B 263 ? 1.93761 0.93432 0.69502 0.36365  0.12862  -0.03494 255 SER B C   
6749 O O   . SER B 263 ? 1.93607 0.96801 0.71372 0.36349  0.13520  -0.03543 255 SER B O   
6750 C CB  . SER B 263 ? 1.90162 0.84132 0.62507 0.34256  0.16006  -0.00585 255 SER B CB  
6751 O OG  . SER B 263 ? 1.96572 0.86930 0.64341 0.36557  0.15417  -0.00294 255 SER B OG  
6752 N N   . GLN B 264 ? 2.00486 0.98861 0.74634 0.38191  0.11119  -0.04286 256 GLN B N   
6753 C CA  . GLN B 264 ? 1.88188 0.90830 0.66067 0.39527  0.09189  -0.04552 256 GLN B CA  
6754 C C   . GLN B 264 ? 1.78609 0.83099 0.59553 0.39512  0.07047  -0.05303 256 GLN B C   
6755 O O   . GLN B 264 ? 1.81302 0.83725 0.61372 0.38612  0.07062  -0.05694 256 GLN B O   
6756 C CB  . GLN B 264 ? 1.82700 0.83775 0.58358 0.41354  0.08949  -0.03650 256 GLN B CB  
6757 C CG  . GLN B 264 ? 1.95434 0.95430 0.68156 0.41503  0.11133  -0.02805 256 GLN B CG  
6758 C CD  . GLN B 264 ? 1.98213 0.99697 0.71080 0.43310  0.10364  -0.02577 256 GLN B CD  
6759 O OE1 . GLN B 264 ? 1.99853 1.00118 0.72037 0.44702  0.08822  -0.02372 256 GLN B OE1 
6760 N NE2 . GLN B 264 ? 1.97032 1.01113 0.70665 0.43390  0.11431  -0.02725 256 GLN B NE2 
6761 N N   . CYS B 265 ? 1.68781 0.76934 0.52983 0.40511  0.05341  -0.05519 257 CYS B N   
6762 C CA  . CYS B 265 ? 1.65085 0.76090 0.52593 0.40616  0.03444  -0.06083 257 CYS B CA  
6763 C C   . CYS B 265 ? 1.69770 0.78238 0.55848 0.40757  0.02936  -0.06063 257 CYS B C   
6764 O O   . CYS B 265 ? 1.73398 0.78253 0.56363 0.41707  0.03191  -0.05413 257 CYS B O   
6765 C CB  . CYS B 265 ? 1.63944 0.77545 0.53584 0.42138  0.01830  -0.05989 257 CYS B CB  
6766 S SG  . CYS B 265 ? 1.67399 0.83240 0.59657 0.42808  -0.00267 -0.06266 257 CYS B SG  
6767 N N   . VAL B 266 ? 1.67813 0.78216 0.55997 0.40009  0.02195  -0.06786 258 VAL B N   
6768 C CA  . VAL B 266 ? 1.62733 0.71557 0.50180 0.40177  0.01606  -0.07092 258 VAL B CA  
6769 C C   . VAL B 266 ? 1.60599 0.71987 0.50141 0.41706  -0.00054 -0.06944 258 VAL B C   
6770 O O   . VAL B 266 ? 1.62175 0.77510 0.54781 0.41521  -0.00863 -0.07367 258 VAL B O   
6771 C CB  . VAL B 266 ? 1.64610 0.74307 0.52929 0.38545  0.01806  -0.08126 258 VAL B CB  
6772 C CG1 . VAL B 266 ? 1.71871 0.79307 0.58916 0.38719  0.01437  -0.08655 258 VAL B CG1 
6773 C CG2 . VAL B 266 ? 1.67652 0.75597 0.54403 0.36938  0.03314  -0.08387 258 VAL B CG2 
6774 N N   . THR B 267 ? 1.63560 0.72590 0.51186 0.43235  -0.00528 -0.06341 259 THR B N   
6775 C CA  . THR B 267 ? 1.64092 0.75099 0.53145 0.44950  -0.02095 -0.06089 259 THR B CA  
6776 C C   . THR B 267 ? 1.61484 0.73132 0.51189 0.45380  -0.02764 -0.06576 259 THR B C   
6777 O O   . THR B 267 ? 1.66081 0.80414 0.57685 0.46535  -0.03967 -0.06584 259 THR B O   
6778 C CB  . THR B 267 ? 1.62207 0.70389 0.48527 0.46540  -0.02378 -0.05235 259 THR B CB  
6779 O OG1 . THR B 267 ? 1.75053 0.78588 0.57652 0.46644  -0.01573 -0.04950 259 THR B OG1 
6780 C CG2 . THR B 267 ? 1.64362 0.72667 0.50339 0.46475  -0.01862 -0.04894 259 THR B CG2 
6781 N N   . GLY B 268 ? 1.61531 0.70698 0.49588 0.44593  -0.02015 -0.07062 260 GLY B N   
6782 C CA  . GLY B 268 ? 1.63966 0.73523 0.52386 0.45084  -0.02511 -0.07744 260 GLY B CA  
6783 C C   . GLY B 268 ? 1.66194 0.74255 0.53865 0.43553  -0.01691 -0.08756 260 GLY B C   
6784 O O   . GLY B 268 ? 1.70583 0.75207 0.56027 0.42486  -0.00688 -0.08705 260 GLY B O   
6785 N N   . LEU B 269 ? 1.63612 0.74117 0.52898 0.43514  -0.02096 -0.09719 261 LEU B N   
6786 C CA  . LEU B 269 ? 1.67911 0.77153 0.56459 0.42310  -0.01641 -0.11024 261 LEU B CA  
6787 C C   . LEU B 269 ? 1.74245 0.84178 0.63063 0.43604  -0.02220 -0.11806 261 LEU B C   
6788 O O   . LEU B 269 ? 1.72900 0.87077 0.63974 0.44453  -0.02793 -0.11831 261 LEU B O   
6789 C CB  . LEU B 269 ? 1.61844 0.74523 0.52327 0.40640  -0.01463 -0.11643 261 LEU B CB  
6790 C CG  . LEU B 269 ? 1.62184 0.73452 0.51901 0.39085  -0.00650 -0.11330 261 LEU B CG  
6791 C CD1 . LEU B 269 ? 1.61868 0.77532 0.53963 0.37952  -0.00800 -0.11587 261 LEU B CD1 
6792 C CD2 . LEU B 269 ? 1.69207 0.75663 0.56099 0.37893  0.00122  -0.12105 261 LEU B CD2 
6793 N N   . VAL B 270 ? 1.72639 0.78401 0.59150 0.43853  -0.02033 -0.12433 262 VAL B N   
6794 C CA  . VAL B 270 ? 1.77423 0.83169 0.63858 0.45315  -0.02506 -0.13303 262 VAL B CA  
6795 C C   . VAL B 270 ? 1.79370 0.82309 0.64518 0.44292  -0.02191 -0.14962 262 VAL B C   
6796 O O   . VAL B 270 ? 1.82084 0.80152 0.64948 0.43399  -0.01739 -0.14936 262 VAL B O   
6797 C CB  . VAL B 270 ? 1.83152 0.86157 0.67925 0.47220  -0.02905 -0.12341 262 VAL B CB  
6798 C CG1 . VAL B 270 ? 1.76825 0.79990 0.61677 0.48859  -0.03362 -0.13285 262 VAL B CG1 
6799 C CG2 . VAL B 270 ? 1.81151 0.86563 0.66930 0.48150  -0.03400 -0.10874 262 VAL B CG2 
6800 N N   . PHE B 271 ? 1.86616 0.92421 0.73042 0.44480  -0.02423 -0.16402 263 PHE B N   
6801 C CA  . PHE B 271 ? 1.84142 0.87841 0.69571 0.43689  -0.02358 -0.18380 263 PHE B CA  
6802 C C   . PHE B 271 ? 1.86141 0.86403 0.70234 0.45349  -0.02611 -0.19001 263 PHE B C   
6803 O O   . PHE B 271 ? 1.84321 0.85941 0.68945 0.47292  -0.02910 -0.18242 263 PHE B O   
6804 C CB  . PHE B 271 ? 1.82012 0.90738 0.69175 0.43238  -0.02485 -0.19683 263 PHE B CB  
6805 C CG  . PHE B 271 ? 1.74900 0.85628 0.62696 0.41126  -0.02322 -0.19717 263 PHE B CG  
6806 C CD1 . PHE B 271 ? 1.78079 0.85697 0.64419 0.39297  -0.02236 -0.20920 263 PHE B CD1 
6807 C CD2 . PHE B 271 ? 1.69735 0.85299 0.59567 0.40990  -0.02356 -0.18605 263 PHE B CD2 
6808 C CE1 . PHE B 271 ? 1.76052 0.85556 0.62859 0.37406  -0.02181 -0.20989 263 PHE B CE1 
6809 C CE2 . PHE B 271 ? 1.67710 0.85127 0.58092 0.39129  -0.02282 -0.18628 263 PHE B CE2 
6810 C CZ  . PHE B 271 ? 1.70828 0.85319 0.59646 0.37359  -0.02192 -0.19811 263 PHE B CZ  
6811 N N   . SER B 272 ? 1.95932 0.91736 0.78399 0.44607  -0.02582 -0.20410 264 SER B N   
6812 C CA  . SER B 272 ? 2.02986 0.94957 0.84257 0.46013  -0.02881 -0.21338 264 SER B CA  
6813 C C   . SER B 272 ? 2.05570 1.00966 0.88143 0.47071  -0.03140 -0.23251 264 SER B C   
6814 O O   . SER B 272 ? 2.01557 1.01156 0.85340 0.46236  -0.03059 -0.24131 264 SER B O   
6815 C CB  . SER B 272 ? 2.06215 0.91796 0.85449 0.44705  -0.02813 -0.22096 264 SER B CB  
6816 O OG  . SER B 272 ? 2.09135 0.94986 0.88701 0.43329  -0.02994 -0.24325 264 SER B OG  
6817 N N   . PRO B 273 ? 2.12225 1.05986 0.94460 0.49006  -0.03414 -0.23964 265 PRO B N   
6818 C CA  . PRO B 273 ? 2.15942 1.12677 0.99154 0.50213  -0.03503 -0.25953 265 PRO B CA  
6819 C C   . PRO B 273 ? 2.16053 1.10307 0.98503 0.49149  -0.03662 -0.28563 265 PRO B C   
6820 O O   . PRO B 273 ? 2.15411 1.12279 0.98435 0.50057  -0.03668 -0.30415 265 PRO B O   
6821 C CB  . PRO B 273 ? 2.21679 1.16992 1.04731 0.52737  -0.03750 -0.25648 265 PRO B CB  
6822 C CG  . PRO B 273 ? 2.12828 1.04958 0.94781 0.52764  -0.03877 -0.23273 265 PRO B CG  
6823 C CD  . PRO B 273 ? 2.09566 0.98763 0.90400 0.50276  -0.03626 -0.22880 265 PRO B CD  
6824 N N   . HIS B 274 ? 2.19976 1.09255 1.01093 0.47316  -0.03793 -0.28708 266 HIS B N   
6825 C CA  . HIS B 274 ? 2.17885 1.03908 0.98222 0.45978  -0.04170 -0.31188 266 HIS B CA  
6826 C C   . HIS B 274 ? 2.16050 1.07260 0.97217 0.45281  -0.04197 -0.32998 266 HIS B C   
6827 O O   . HIS B 274 ? 2.10572 1.06973 0.92762 0.44911  -0.03853 -0.31798 266 HIS B O   
6828 C CB  . HIS B 274 ? 2.18877 0.99859 0.97940 0.43712  -0.04207 -0.30521 266 HIS B CB  
6829 C CG  . HIS B 274 ? 2.24848 0.99372 1.02570 0.44150  -0.04251 -0.29381 266 HIS B CG  
6830 N ND1 . HIS B 274 ? 2.26158 0.95390 1.03288 0.44468  -0.04793 -0.30971 266 HIS B ND1 
6831 C CD2 . HIS B 274 ? 2.25404 0.97792 1.02178 0.44288  -0.03842 -0.26812 266 HIS B CD2 
6832 C CE1 . HIS B 274 ? 2.31464 0.95574 1.07427 0.44765  -0.04709 -0.29255 266 HIS B CE1 
6833 N NE2 . HIS B 274 ? 2.36774 1.02758 1.12289 0.44682  -0.04089 -0.26703 266 HIS B NE2 
6834 N N   . SER B 275 ? 2.19696 1.09422 1.00377 0.45089  -0.04650 -0.35791 267 SER B N   
6835 C CA  . SER B 275 ? 2.16950 1.10909 0.97814 0.44244  -0.04806 -0.37869 267 SER B CA  
6836 C C   . SER B 275 ? 2.18893 1.14213 0.99721 0.41739  -0.04874 -0.37024 267 SER B C   
6837 O O   . SER B 275 ? 2.12700 1.13927 0.94340 0.41491  -0.04614 -0.36569 267 SER B O   
6838 C CB  . SER B 275 ? 2.19979 1.10710 0.99989 0.44200  -0.05461 -0.41072 267 SER B CB  
6839 O OG  . SER B 275 ? 2.22680 1.13256 1.02907 0.46709  -0.05309 -0.42055 267 SER B OG  
6840 N N   . VAL B 276 ? 2.17119 1.07060 0.97054 0.39981  -0.05194 -0.36733 268 VAL B N   
6841 C CA  . VAL B 276 ? 2.14622 1.04980 0.94459 0.37684  -0.05145 -0.35519 268 VAL B CA  
6842 C C   . VAL B 276 ? 2.14271 1.02774 0.94112 0.37991  -0.04467 -0.32550 268 VAL B C   
6843 O O   . VAL B 276 ? 2.20885 1.03396 0.99632 0.37710  -0.04449 -0.31994 268 VAL B O   
6844 C CB  . VAL B 276 ? 2.16907 1.02728 0.95658 0.35369  -0.05971 -0.37414 268 VAL B CB  
6845 C CG1 . VAL B 276 ? 2.20234 0.98128 0.98035 0.35120  -0.06188 -0.37429 268 VAL B CG1 
6846 C CG2 . VAL B 276 ? 2.12091 0.99524 0.90830 0.33090  -0.05993 -0.36564 268 VAL B CG2 
6847 N N   . PRO B 277 ? 2.08676 1.02206 0.89716 0.38612  -0.03920 -0.30541 269 PRO B N   
6848 C CA  . PRO B 277 ? 2.07539 1.00010 0.88648 0.39639  -0.03382 -0.27967 269 PRO B CA  
6849 C C   . PRO B 277 ? 2.06224 0.95363 0.86366 0.37981  -0.02983 -0.26393 269 PRO B C   
6850 O O   . PRO B 277 ? 2.11503 1.01581 0.91691 0.36072  -0.03009 -0.26778 269 PRO B O   
6851 C CB  . PRO B 277 ? 2.01446 1.00810 0.84472 0.40697  -0.03143 -0.26824 269 PRO B CB  
6852 C CG  . PRO B 277 ? 1.99003 1.02400 0.82666 0.39101  -0.03332 -0.27916 269 PRO B CG  
6853 C CD  . PRO B 277 ? 2.09022 1.09375 0.91399 0.38317  -0.03890 -0.30622 269 PRO B CD  
6854 N N   . PHE B 278 ? 2.03241 0.88601 0.82349 0.38813  -0.02607 -0.24683 270 PHE B N   
6855 C CA  . PHE B 278 ? 2.00166 0.82781 0.78136 0.37763  -0.01930 -0.22760 270 PHE B CA  
6856 C C   . PHE B 278 ? 1.93571 0.81371 0.72951 0.38482  -0.01578 -0.20855 270 PHE B C   
6857 O O   . PHE B 278 ? 1.90828 0.82378 0.71588 0.40247  -0.01876 -0.20545 270 PHE B O   
6858 C CB  . PHE B 278 ? 2.06545 0.82689 0.82435 0.38473  -0.01691 -0.21758 270 PHE B CB  
6859 C CG  . PHE B 278 ? 2.17845 0.87701 0.92452 0.37365  -0.02009 -0.23250 270 PHE B CG  
6860 C CD1 . PHE B 278 ? 2.20514 0.88124 0.94723 0.34919  -0.01979 -0.24186 270 PHE B CD1 
6861 C CD2 . PHE B 278 ? 2.25776 0.91741 0.99754 0.38712  -0.02449 -0.23709 270 PHE B CD2 
6862 C CE1 . PHE B 278 ? 2.30589 0.92122 1.03990 0.33733  -0.02471 -0.25557 270 PHE B CE1 
6863 C CE2 . PHE B 278 ? 2.32916 0.92892 1.06157 0.37619  -0.02891 -0.25061 270 PHE B CE2 
6864 C CZ  . PHE B 278 ? 2.36780 0.94484 1.09815 0.35074  -0.02939 -0.25970 270 PHE B CZ  
6865 N N   . LEU B 279 ? 1.91715 0.79508 0.70821 0.37165  -0.00979 -0.19699 271 LEU B N   
6866 C CA  . LEU B 279 ? 1.86222 0.78286 0.66713 0.37682  -0.00681 -0.17891 271 LEU B CA  
6867 C C   . LEU B 279 ? 1.88037 0.76145 0.66525 0.38179  0.00003  -0.16049 271 LEU B C   
6868 O O   . LEU B 279 ? 1.90992 0.75059 0.67623 0.36781  0.00767  -0.15843 271 LEU B O   
6869 C CB  . LEU B 279 ? 1.83538 0.79051 0.65309 0.35885  -0.00530 -0.18172 271 LEU B CB  
6870 C CG  . LEU B 279 ? 1.78604 0.78477 0.62170 0.36199  -0.00314 -0.16530 271 LEU B CG  
6871 C CD1 . LEU B 279 ? 1.74619 0.79295 0.60460 0.37942  -0.00964 -0.16129 271 LEU B CD1 
6872 C CD2 . LEU B 279 ? 1.75783 0.78348 0.60323 0.34352  -0.00182 -0.16892 271 LEU B CD2 
6873 N N   . ALA B 280 ? 1.86731 0.75845 0.65378 0.40128  -0.00262 -0.14810 272 ALA B N   
6874 C CA  . ALA B 280 ? 1.87825 0.74336 0.64550 0.40943  0.00224  -0.12937 272 ALA B CA  
6875 C C   . ALA B 280 ? 1.90876 0.81843 0.69356 0.40741  0.00403  -0.11861 272 ALA B C   
6876 O O   . ALA B 280 ? 1.79474 0.75714 0.60816 0.41348  -0.00316 -0.11966 272 ALA B O   
6877 C CB  . ALA B 280 ? 1.89323 0.74865 0.65310 0.43144  -0.00425 -0.12363 272 ALA B CB  
6878 N N   . SER B 281 ? 1.92420 0.81186 0.69247 0.39959  0.01384  -0.10925 273 SER B N   
6879 C CA  . SER B 281 ? 1.86736 0.79174 0.65073 0.39761  0.01664  -0.09980 273 SER B CA  
6880 C C   . SER B 281 ? 1.83947 0.73998 0.59928 0.41072  0.02054  -0.08394 273 SER B C   
6881 O O   . SER B 281 ? 1.86755 0.71239 0.59060 0.40985  0.03027  -0.07935 273 SER B O   
6882 C CB  . SER B 281 ? 1.81436 0.74097 0.59976 0.37705  0.02576  -0.10510 273 SER B CB  
6883 O OG  . SER B 281 ? 1.90389 0.76957 0.65391 0.36867  0.03790  -0.10454 273 SER B OG  
6884 N N   . LEU B 282 ? 1.80243 0.74146 0.58142 0.42281  0.01266  -0.07643 274 LEU B N   
6885 C CA  . LEU B 282 ? 1.81708 0.74311 0.57713 0.43771  0.01243  -0.06283 274 LEU B CA  
6886 C C   . LEU B 282 ? 1.82878 0.77913 0.60067 0.43091  0.01882  -0.05862 274 LEU B C   
6887 O O   . LEU B 282 ? 1.82530 0.81441 0.62890 0.41877  0.01811  -0.06558 274 LEU B O   
6888 C CB  . LEU B 282 ? 1.75870 0.71209 0.53506 0.45602  -0.00339 -0.06040 274 LEU B CB  
6889 C CG  . LEU B 282 ? 1.78822 0.71956 0.55113 0.46720  -0.00985 -0.06362 274 LEU B CG  
6890 C CD1 . LEU B 282 ? 1.79537 0.72290 0.56687 0.45472  -0.00683 -0.07724 274 LEU B CD1 
6891 C CD2 . LEU B 282 ? 1.75773 0.72504 0.54155 0.48390  -0.02458 -0.06261 274 LEU B CD2 
6892 N N   . SER B 283 ? 1.77975 0.70969 0.52669 0.43964  0.02444  -0.04821 275 SER B N   
6893 C CA  . SER B 283 ? 1.82538 0.77663 0.58120 0.43443  0.03241  -0.04523 275 SER B CA  
6894 C C   . SER B 283 ? 1.85023 0.78813 0.58349 0.45103  0.03239  -0.03485 275 SER B C   
6895 O O   . SER B 283 ? 1.93436 0.83340 0.63335 0.46489  0.03019  -0.02824 275 SER B O   
6896 C CB  . SER B 283 ? 1.83300 0.76367 0.57270 0.41650  0.05114  -0.04775 275 SER B CB  
6897 O OG  . SER B 283 ? 1.83177 0.77790 0.57221 0.41396  0.06185  -0.04349 275 SER B OG  
6898 N N   . GLU B 284 ? 1.79527 0.76414 0.54640 0.45022  0.03435  -0.03452 276 GLU B N   
6899 C CA  . GLU B 284 ? 1.79771 0.76127 0.53162 0.46447  0.03519  -0.02760 276 GLU B CA  
6900 C C   . GLU B 284 ? 1.88180 0.80719 0.57208 0.46033  0.05825  -0.01991 276 GLU B C   
6901 O O   . GLU B 284 ? 1.89932 0.81779 0.56952 0.47183  0.06218  -0.01363 276 GLU B O   
6902 C CB  . GLU B 284 ? 1.72663 0.74023 0.49933 0.46468  0.02744  -0.03307 276 GLU B CB  
6903 C CG  . GLU B 284 ? 1.68440 0.72912 0.49058 0.47326  0.00464  -0.03763 276 GLU B CG  
6904 C CD  . GLU B 284 ? 1.75467 0.84593 0.60110 0.46981  -0.00327 -0.04474 276 GLU B CD  
6905 O OE1 . GLU B 284 ? 1.76681 0.86662 0.61277 0.46776  0.00536  -0.04600 276 GLU B OE1 
6906 O OE2 . GLU B 284 ? 1.83313 0.95103 0.70938 0.47020  -0.01754 -0.04908 276 GLU B OE2 
6907 N N   . ASP B 285 ? 1.85140 0.75314 0.52607 0.44443  0.07324  -0.02059 277 ASP B N   
6908 C CA  . ASP B 285 ? 1.95029 0.80732 0.57517 0.43886  0.09734  -0.01069 277 ASP B CA  
6909 C C   . ASP B 285 ? 1.98871 0.78589 0.56459 0.45104  0.09689  -0.00207 277 ASP B C   
6910 O O   . ASP B 285 ? 2.08266 0.83474 0.60979 0.44593  0.11638  0.00980  277 ASP B O   
6911 C CB  . ASP B 285 ? 1.91704 0.76962 0.54235 0.41642  0.11294  -0.01566 277 ASP B CB  
6912 C CG  . ASP B 285 ? 2.00772 0.83218 0.63320 0.40766  0.10677  -0.02369 277 ASP B CG  
6913 O OD1 . ASP B 285 ? 1.99239 0.80531 0.61735 0.42077  0.09051  -0.02676 277 ASP B OD1 
6914 O OD2 . ASP B 285 ? 2.03329 0.86198 0.68345 0.38303  0.11471  -0.02265 277 ASP B OD2 
6915 N N   . CYS B 286 ? 1.97322 0.77037 0.55978 0.46597  0.07593  -0.00550 278 CYS B N   
6916 C CA  . CYS B 286 ? 2.03318 0.77652 0.57582 0.48321  0.07110  0.00181  278 CYS B CA  
6917 C C   . CYS B 286 ? 2.11943 0.80691 0.62913 0.47379  0.08107  -0.00007 278 CYS B C   
6918 O O   . CYS B 286 ? 2.20499 0.83856 0.67285 0.48084  0.08625  0.01267  278 CYS B O   
6919 C CB  . CYS B 286 ? 2.06130 0.78179 0.56508 0.49604  0.08021  0.01545  278 CYS B CB  
6920 S SG  . CYS B 286 ? 2.01325 0.79311 0.55535 0.50765  0.06864  0.01164  278 CYS B SG  
6921 N N   . SER B 287 ? 2.09730 0.80382 0.64164 0.45541  0.08076  -0.01306 279 SER B N   
6922 C CA  . SER B 287 ? 2.06245 0.73105 0.60781 0.43868  0.08595  -0.01544 279 SER B CA  
6923 C C   . SER B 287 ? 2.02586 0.71668 0.60485 0.43697  0.06960  -0.03390 279 SER B C   
6924 O O   . SER B 287 ? 2.02301 0.77667 0.64553 0.43078  0.06150  -0.04093 279 SER B O   
6925 C CB  . SER B 287 ? 2.14575 0.82659 0.71178 0.40937  0.10290  -0.00735 279 SER B CB  
6926 O OG  . SER B 287 ? 2.08436 0.81259 0.68975 0.39608  0.09964  -0.02304 279 SER B OG  
6927 N N   . LEU B 288 ? 2.24690 0.89915 0.81808 0.43906  0.06349  -0.03672 280 LEU B N   
6928 C CA  . LEU B 288 ? 2.19041 0.86745 0.79742 0.43153  0.05033  -0.05220 280 LEU B CA  
6929 C C   . LEU B 288 ? 2.20645 0.85564 0.81659 0.40877  0.05973  -0.06260 280 LEU B C   
6930 O O   . LEU B 288 ? 2.21880 0.82076 0.81021 0.39787  0.07211  -0.05051 280 LEU B O   
6931 C CB  . LEU B 288 ? 2.12097 0.77280 0.71807 0.44608  0.03907  -0.05124 280 LEU B CB  
6932 C CG  . LEU B 288 ? 2.11718 0.79079 0.74580 0.44212  0.02719  -0.06819 280 LEU B CG  
6933 C CD1 . LEU B 288 ? 2.06917 0.81567 0.73569 0.44852  0.01544  -0.07354 280 LEU B CD1 
6934 C CD2 . LEU B 288 ? 2.21746 0.85122 0.83158 0.45372  0.02041  -0.06821 280 LEU B CD2 
6935 N N   . ALA B 289 ? 2.10273 0.79461 0.74843 0.39696  0.05202  -0.07844 281 ALA B N   
6936 C CA  . ALA B 289 ? 2.11430 0.78467 0.76630 0.37541  0.05538  -0.09268 281 ALA B CA  
6937 C C   . ALA B 289 ? 2.06945 0.77051 0.74957 0.37531  0.03969  -0.10957 281 ALA B C   
6938 O O   . ALA B 289 ? 2.04449 0.80425 0.75012 0.38561  0.03011  -0.11060 281 ALA B O   
6939 C CB  . ALA B 289 ? 2.01776 0.72982 0.69312 0.35504  0.06354  -0.09053 281 ALA B CB  
6940 N N   . VAL B 290 ? 2.11764 0.77767 0.79357 0.36454  0.03734  -0.12194 282 VAL B N   
6941 C CA  . VAL B 290 ? 2.08988 0.77394 0.78832 0.36350  0.02406  -0.14177 282 VAL B CA  
6942 C C   . VAL B 290 ? 2.10749 0.78254 0.81194 0.33913  0.02477  -0.15810 282 VAL B C   
6943 O O   . VAL B 290 ? 2.16667 0.78072 0.85292 0.32456  0.03215  -0.15637 282 VAL B O   
6944 C CB  . VAL B 290 ? 2.09004 0.73391 0.77867 0.37577  0.01717  -0.14457 282 VAL B CB  
6945 C CG1 . VAL B 290 ? 2.08170 0.75262 0.79191 0.37768  0.00524  -0.16635 282 VAL B CG1 
6946 C CG2 . VAL B 290 ? 2.08574 0.73310 0.76376 0.39894  0.01604  -0.12763 282 VAL B CG2 
6947 N N   . LEU B 291 ? 2.01024 0.74194 0.73937 0.33441  0.01701  -0.17207 283 LEU B N   
6948 C CA  . LEU B 291 ? 2.06055 0.79789 0.79600 0.31139  0.01577  -0.18733 283 LEU B CA  
6949 C C   . LEU B 291 ? 2.05809 0.81192 0.80638 0.30942  0.00239  -0.21023 283 LEU B C   
6950 O O   . LEU B 291 ? 2.03437 0.81453 0.79277 0.32772  -0.00375 -0.21260 283 LEU B O   
6951 C CB  . LEU B 291 ? 2.04068 0.83748 0.79214 0.30768  0.01927  -0.18073 283 LEU B CB  
6952 C CG  . LEU B 291 ? 2.00710 0.80514 0.75089 0.31571  0.03110  -0.15920 283 LEU B CG  
6953 C CD1 . LEU B 291 ? 1.89729 0.76224 0.66547 0.31464  0.03076  -0.15452 283 LEU B CD1 
6954 C CD2 . LEU B 291 ? 2.04684 0.81385 0.79460 0.29496  0.04259  -0.14178 283 LEU B CD2 
6955 N N   . ASP B 292 ? 2.09764 0.83656 0.84469 0.28793  -0.00195 -0.22712 284 ASP B N   
6956 C CA  . ASP B 292 ? 2.13508 0.89096 0.89151 0.28323  -0.01535 -0.25202 284 ASP B CA  
6957 C C   . ASP B 292 ? 2.08737 0.92077 0.86253 0.28304  -0.01939 -0.25540 284 ASP B C   
6958 O O   . ASP B 292 ? 2.03225 0.90336 0.81661 0.28911  -0.01278 -0.23770 284 ASP B O   
6959 C CB  . ASP B 292 ? 2.16433 0.86278 0.91027 0.25903  -0.02091 -0.26863 284 ASP B CB  
6960 C CG  . ASP B 292 ? 2.15694 0.87790 0.92960 0.22893  -0.01615 -0.25295 284 ASP B CG  
6961 O OD1 . ASP B 292 ? 2.08092 0.85057 0.86645 0.23057  -0.00826 -0.23574 284 ASP B OD1 
6962 O OD2 . ASP B 292 ? 2.19710 0.89070 0.98371 0.20341  -0.02089 -0.25681 284 ASP B OD2 
6963 N N   . SER B 293 ? 2.14549 1.00130 0.92626 0.27673  -0.03046 -0.27706 285 SER B N   
6964 C CA  . SER B 293 ? 2.08303 1.01058 0.87926 0.27558  -0.03570 -0.28137 285 SER B CA  
6965 C C   . SER B 293 ? 2.11018 1.05333 0.90746 0.25813  -0.03322 -0.27272 285 SER B C   
6966 O O   . SER B 293 ? 2.05607 1.05983 0.86915 0.26226  -0.03344 -0.26397 285 SER B O   
6967 C CB  . SER B 293 ? 2.13562 1.07289 0.93044 0.27044  -0.04788 -0.30775 285 SER B CB  
6968 O OG  . SER B 293 ? 2.18282 1.06792 0.96394 0.24850  -0.05505 -0.32377 285 SER B OG  
6969 N N   . SER B 294 ? 2.10050 1.00290 0.89775 0.23638  -0.03085 -0.26948 286 SER B N   
6970 C CA  . SER B 294 ? 2.03621 0.97575 0.86811 0.21146  -0.02794 -0.25175 286 SER B CA  
6971 C C   . SER B 294 ? 1.99241 0.92271 0.83352 0.21314  -0.01203 -0.22442 286 SER B C   
6972 O O   . SER B 294 ? 1.98176 0.92663 0.85075 0.19125  -0.00679 -0.20970 286 SER B O   
6973 C CB  . SER B 294 ? 1.98799 0.91111 0.83548 0.18152  -0.03666 -0.26154 286 SER B CB  
6974 O OG  . SER B 294 ? 2.04892 0.90444 0.88670 0.17621  -0.03374 -0.26287 286 SER B OG  
6975 N N   . LEU B 295 ? 2.01037 0.91934 0.82884 0.23885  -0.00492 -0.21836 287 LEU B N   
6976 C CA  . LEU B 295 ? 2.02983 0.93638 0.84984 0.24727  0.00890  -0.19416 287 LEU B CA  
6977 C C   . LEU B 295 ? 2.04561 0.91397 0.87314 0.22757  0.01913  -0.17916 287 LEU B C   
6978 O O   . LEU B 295 ? 2.00554 0.89189 0.84687 0.22335  0.03078  -0.15884 287 LEU B O   
6979 C CB  . LEU B 295 ? 1.85569 0.82651 0.70018 0.24710  0.01041  -0.18295 287 LEU B CB  
6980 C CG  . LEU B 295 ? 1.78262 0.79543 0.62369 0.26561  0.00150  -0.19232 287 LEU B CG  
6981 C CD1 . LEU B 295 ? 1.72674 0.80197 0.59940 0.25810  -0.00002 -0.18180 287 LEU B CD1 
6982 C CD2 . LEU B 295 ? 1.77854 0.78246 0.60579 0.29326  0.00404  -0.18666 287 LEU B CD2 
6983 N N   . SER B 296 ? 2.02331 0.84065 0.84240 0.21674  0.01519  -0.18853 288 SER B N   
6984 C CA  . SER B 296 ? 2.06756 0.84004 0.89217 0.19840  0.02461  -0.17296 288 SER B CA  
6985 C C   . SER B 296 ? 2.13383 0.85404 0.92692 0.21982  0.03185  -0.16316 288 SER B C   
6986 O O   . SER B 296 ? 2.13054 0.82971 0.89906 0.24224  0.02371  -0.17871 288 SER B O   
6987 C CB  . SER B 296 ? 2.05178 0.79600 0.88811 0.17388  0.01419  -0.18756 288 SER B CB  
6988 O OG  . SER B 296 ? 2.05786 0.85137 0.91855 0.15773  0.00380  -0.19998 288 SER B OG  
6989 N N   . GLU B 297 ? 2.14608 0.84805 0.93996 0.21367  0.04672  -0.13787 289 GLU B N   
6990 C CA  . GLU B 297 ? 2.16143 0.81813 0.92456 0.23379  0.05469  -0.12308 289 GLU B CA  
6991 C C   . GLU B 297 ? 2.19662 0.78399 0.94619 0.23059  0.04824  -0.12977 289 GLU B C   
6992 O O   . GLU B 297 ? 2.23697 0.80056 1.00486 0.20336  0.05019  -0.12361 289 GLU B O   
6993 C CB  . GLU B 297 ? 2.23009 0.89391 0.99804 0.22613  0.07322  -0.09362 289 GLU B CB  
6994 C CG  . GLU B 297 ? 2.25855 0.88499 0.99200 0.24864  0.08110  -0.07666 289 GLU B CG  
6995 C CD  . GLU B 297 ? 2.27661 0.91251 1.00900 0.24368  0.10033  -0.04823 289 GLU B CD  
6996 O OE1 . GLU B 297 ? 2.20135 0.88739 0.95886 0.23164  0.10781  -0.04389 289 GLU B OE1 
6997 O OE2 . GLU B 297 ? 2.33784 0.93166 1.04363 0.25290  0.10786  -0.03033 289 GLU B OE2 
6998 N N   . LEU B 298 ? 2.22707 0.78395 0.94869 0.25751  0.04031  -0.14175 290 LEU B N   
6999 C CA  . LEU B 298 ? 2.26149 0.74781 0.96749 0.26115  0.03293  -0.14938 290 LEU B CA  
7000 C C   . LEU B 298 ? 2.31873 0.76218 0.99826 0.27969  0.04118  -0.12639 290 LEU B C   
7001 O O   . LEU B 298 ? 2.36947 0.75120 1.04310 0.27320  0.04035  -0.11906 290 LEU B O   
7002 C CB  . LEU B 298 ? 2.26070 0.74588 0.95529 0.28050  0.01733  -0.18205 290 LEU B CB  
7003 C CG  . LEU B 298 ? 2.27122 0.80074 0.98529 0.26622  0.00752  -0.20632 290 LEU B CG  
7004 C CD1 . LEU B 298 ? 2.21567 0.76582 0.92756 0.28641  -0.00555 -0.23108 290 LEU B CD1 
7005 C CD2 . LEU B 298 ? 2.25523 0.76175 0.99198 0.23196  0.00290  -0.21031 290 LEU B CD2 
7006 N N   . PHE B 299 ? 2.29827 0.77184 0.96268 0.30216  0.04709  -0.11581 291 PHE B N   
7007 C CA  . PHE B 299 ? 2.31656 0.75709 0.95224 0.32328  0.05324  -0.09434 291 PHE B CA  
7008 C C   . PHE B 299 ? 2.29942 0.78742 0.93167 0.32993  0.06457  -0.07628 291 PHE B C   
7009 O O   . PHE B 299 ? 2.21868 0.76533 0.86847 0.32770  0.06379  -0.08595 291 PHE B O   
7010 C CB  . PHE B 299 ? 2.36633 0.79280 0.98627 0.35304  0.04034  -0.10848 291 PHE B CB  
7011 C CG  . PHE B 299 ? 2.46537 0.86072 1.06295 0.37139  0.04232  -0.08649 291 PHE B CG  
7012 C CD1 . PHE B 299 ? 2.50556 0.83002 1.08938 0.36335  0.04665  -0.07001 291 PHE B CD1 
7013 C CD2 . PHE B 299 ? 2.41334 0.85161 1.00593 0.39525  0.03851  -0.08068 291 PHE B CD2 
7014 C CE1 . PHE B 299 ? 2.51466 0.81435 1.07774 0.37991  0.04767  -0.04839 291 PHE B CE1 
7015 C CE2 . PHE B 299 ? 2.37604 0.78660 0.94600 0.41192  0.03870  -0.06166 291 PHE B CE2 
7016 C CZ  . PHE B 299 ? 2.46987 0.81241 1.02409 0.40478  0.04349  -0.04563 291 PHE B CZ  
7017 N N   . ARG B 300 ? 2.38233 0.84417 0.99188 0.33821  0.07412  -0.05072 292 ARG B N   
7018 C CA  . ARG B 300 ? 2.30648 0.80435 0.90503 0.34853  0.08442  -0.03352 292 ARG B CA  
7019 C C   . ARG B 300 ? 2.26729 0.72134 0.82887 0.36866  0.08727  -0.01249 292 ARG B C   
7020 O O   . ARG B 300 ? 2.32660 0.72647 0.87946 0.35989  0.09042  0.00150  292 ARG B O   
7021 C CB  . ARG B 300 ? 2.26622 0.79574 0.88740 0.32103  0.10003  -0.01959 292 ARG B CB  
7022 C CG  . ARG B 300 ? 2.29145 0.84436 0.89683 0.32970  0.11388  0.00149  292 ARG B CG  
7023 C CD  . ARG B 300 ? 2.27384 0.88664 0.90904 0.31358  0.12302  0.00048  292 ARG B CD  
7024 N NE  . ARG B 300 ? 2.20392 0.86429 0.85019 0.32776  0.11150  -0.01983 292 ARG B NE  
7025 C CZ  . ARG B 300 ? 2.18196 0.89445 0.86149 0.31480  0.11157  -0.02938 292 ARG B CZ  
7026 N NH1 . ARG B 300 ? 2.20343 0.92984 0.91015 0.28738  0.12227  -0.02220 292 ARG B NH1 
7027 N NH2 . ARG B 300 ? 2.09385 0.84533 0.78171 0.32925  0.10027  -0.04493 292 ARG B NH2 
7028 N N   . SER B 301 ? 2.25392 0.73037 0.79580 0.39428  0.08476  -0.01008 293 SER B N   
7029 C CA  . SER B 301 ? 2.28401 0.72628 0.78792 0.41745  0.08459  0.00864  293 SER B CA  
7030 C C   . SER B 301 ? 2.31745 0.79661 0.80684 0.42529  0.09381  0.02264  293 SER B C   
7031 O O   . SER B 301 ? 2.24479 0.77307 0.74529 0.43491  0.08808  0.00816  293 SER B O   
7032 C CB  . SER B 301 ? 2.28120 0.71999 0.77928 0.44302  0.06650  -0.00583 293 SER B CB  
7033 O OG  . SER B 301 ? 2.31273 0.73518 0.78254 0.46124  0.06426  0.01207  293 SER B OG  
7034 N N   . GLN B 302 ? 2.30496 0.75989 0.76956 0.42214  0.10713  0.04998  294 GLN B N   
7035 C CA  . GLN B 302 ? 2.29889 0.78033 0.74012 0.43250  0.11681  0.06494  294 GLN B CA  
7036 C C   . GLN B 302 ? 2.33462 0.78637 0.73382 0.46311  0.10673  0.07454  294 GLN B C   
7037 O O   . GLN B 302 ? 2.35511 0.81090 0.72381 0.47181  0.11530  0.09273  294 GLN B O   
7038 C CB  . GLN B 302 ? 2.33065 0.80719 0.76917 0.40968  0.13973  0.09060  294 GLN B CB  
7039 C CG  . GLN B 302 ? 2.30608 0.80456 0.78841 0.37721  0.14904  0.08444  294 GLN B CG  
7040 C CD  . GLN B 302 ? 2.25484 0.81857 0.76120 0.37326  0.15354  0.07147  294 GLN B CD  
7041 O OE1 . GLN B 302 ? 2.35650 0.94930 0.89491 0.36734  0.14363  0.04874  294 GLN B OE1 
7042 N NE2 . GLN B 302 ? 2.30296 0.89020 0.79316 0.37742  0.16847  0.08608  294 GLN B NE2 
7043 N N   . ALA B 303 ? 2.34371 0.76834 0.74123 0.47961  0.08906  0.06232  295 ALA B N   
7044 C CA  . ALA B 303 ? 2.36804 0.78834 0.74909 0.49864  0.07761  0.06547  295 ALA B CA  
7045 C C   . ALA B 303 ? 2.33424 0.79964 0.70456 0.51893  0.07112  0.05869  295 ALA B C   
7046 O O   . ALA B 303 ? 2.36383 0.82565 0.71305 0.53055  0.07045  0.06934  295 ALA B O   
7047 C CB  . ALA B 303 ? 2.36232 0.77999 0.76632 0.50260  0.06067  0.04736  295 ALA B CB  
7048 N N   . HIS B 304 ? 2.27529 0.78244 0.66408 0.52220  0.06548  0.04053  296 HIS B N   
7049 C CA  . HIS B 304 ? 2.23727 0.78935 0.62541 0.54010  0.05665  0.02934  296 HIS B CA  
7050 C C   . HIS B 304 ? 2.24186 0.80677 0.62223 0.53720  0.07155  0.04128  296 HIS B C   
7051 O O   . HIS B 304 ? 2.24528 0.80800 0.62416 0.51783  0.08815  0.05228  296 HIS B O   
7052 C CB  . HIS B 304 ? 2.17625 0.77805 0.59824 0.53797  0.04301  0.01444  296 HIS B CB  
7053 C CG  . HIS B 304 ? 2.14785 0.77207 0.59774 0.54172  0.02361  0.00574  296 HIS B CG  
7054 N ND1 . HIS B 304 ? 2.15034 0.78870 0.59064 0.56023  0.00891  0.00302  296 HIS B ND1 
7055 C CD2 . HIS B 304 ? 2.15556 0.79110 0.64222 0.53047  0.01793  -0.00383 296 HIS B CD2 
7056 C CE1 . HIS B 304 ? 2.13073 0.78721 0.60130 0.56086  -0.00461 -0.00425 296 HIS B CE1 
7057 N NE2 . HIS B 304 ? 2.17851 0.83385 0.67692 0.54354  0.00097  -0.00908 296 HIS B NE2 
7058 N N   . ARG B 305 ? 2.23997 0.82571 0.62089 0.55337  0.06502  0.03912  297 ARG B N   
7059 C CA  . ARG B 305 ? 2.24072 0.85287 0.62225 0.55197  0.07555  0.04856  297 ARG B CA  
7060 C C   . ARG B 305 ? 2.17483 0.84204 0.59997 0.55832  0.06342  0.03301  297 ARG B C   
7061 O O   . ARG B 305 ? 2.16728 0.86391 0.59893 0.55466  0.07177  0.03722  297 ARG B O   
7062 C CB  . ARG B 305 ? 2.30339 0.89917 0.65608 0.56518  0.07411  0.05994  297 ARG B CB  
7063 C CG  . ARG B 305 ? 2.35617 0.90190 0.67709 0.55713  0.08358  0.08138  297 ARG B CG  
7064 C CD  . ARG B 305 ? 2.45831 0.99256 0.75469 0.57107  0.07920  0.09315  297 ARG B CD  
7065 N NE  . ARG B 305 ? 2.41270 0.95907 0.71742 0.59243  0.05597  0.07444  297 ARG B NE  
7066 C CZ  . ARG B 305 ? 2.40126 0.92721 0.70561 0.59908  0.04230  0.06915  297 ARG B CZ  
7067 N NH1 . ARG B 305 ? 2.42656 0.91515 0.72562 0.58680  0.04760  0.08061  297 ARG B NH1 
7068 N NH2 . ARG B 305 ? 2.37728 0.92257 0.69075 0.61732  0.02255  0.05264  297 ARG B NH2 
7069 N N   . ASP B 306 ? 2.13077 0.81344 0.58719 0.56706  0.04364  0.01855  298 ASP B N   
7070 C CA  . ASP B 306 ? 2.06069 0.80119 0.57029 0.56687  0.02876  0.01020  298 ASP B CA  
7071 C C   . ASP B 306 ? 2.01439 0.77485 0.55714 0.55273  0.02250  0.00652  298 ASP B C   
7072 O O   . ASP B 306 ? 2.04196 0.76759 0.56197 0.54386  0.03150  0.00965  298 ASP B O   
7073 C CB  . ASP B 306 ? 2.05070 0.80567 0.57161 0.58886  0.00747  0.00298  298 ASP B CB  
7074 C CG  . ASP B 306 ? 2.00917 0.81345 0.56294 0.59016  -0.00142 -0.00150 298 ASP B CG  
7075 O OD1 . ASP B 306 ? 1.96301 0.80472 0.55044 0.57352  0.00134  -0.00343 298 ASP B OD1 
7076 O OD2 . ASP B 306 ? 2.02580 0.83149 0.57016 0.60702  -0.01108 -0.00500 298 ASP B OD2 
7077 N N   . PHE B 307 ? 1.95221 0.76897 0.54536 0.54888  0.00790  -0.00054 299 PHE B N   
7078 C CA  . PHE B 307 ? 1.89609 0.74998 0.53012 0.53090  0.00389  -0.00709 299 PHE B CA  
7079 C C   . PHE B 307 ? 1.91912 0.75796 0.54609 0.53394  -0.00566 -0.00725 299 PHE B C   
7080 O O   . PHE B 307 ? 1.99068 0.82510 0.60797 0.54898  -0.01846 -0.00642 299 PHE B O   
7081 C CB  . PHE B 307 ? 1.84402 0.75753 0.52910 0.53017  -0.01113 -0.01470 299 PHE B CB  
7082 C CG  . PHE B 307 ? 1.83299 0.77283 0.53288 0.52418  -0.00392 -0.01746 299 PHE B CG  
7083 C CD1 . PHE B 307 ? 1.85022 0.77239 0.52639 0.51487  0.01790  -0.01365 299 PHE B CD1 
7084 C CD2 . PHE B 307 ? 1.78855 0.77187 0.52483 0.52783  -0.01893 -0.02400 299 PHE B CD2 
7085 C CE1 . PHE B 307 ? 1.82941 0.78021 0.51886 0.51051  0.02454  -0.01646 299 PHE B CE1 
7086 C CE2 . PHE B 307 ? 1.75712 0.76412 0.50530 0.52354  -0.01353 -0.02770 299 PHE B CE2 
7087 C CZ  . PHE B 307 ? 1.78596 0.77840 0.51139 0.51530  0.00831  -0.02416 299 PHE B CZ  
7088 N N   . VAL B 308 ? 1.89016 0.73492 0.53197 0.51543  0.00137  -0.01351 300 VAL B N   
7089 C CA  . VAL B 308 ? 1.88968 0.73263 0.53721 0.51407  -0.00612 -0.01931 300 VAL B CA  
7090 C C   . VAL B 308 ? 1.85802 0.76187 0.55931 0.51249  -0.02062 -0.02765 300 VAL B C   
7091 O O   . VAL B 308 ? 1.82671 0.76512 0.56305 0.49729  -0.01661 -0.03369 300 VAL B O   
7092 C CB  . VAL B 308 ? 1.91203 0.72766 0.55137 0.49585  0.00843  -0.02492 300 VAL B CB  
7093 C CG1 . VAL B 308 ? 1.92771 0.73031 0.56690 0.49832  0.00142  -0.03171 300 VAL B CG1 
7094 C CG2 . VAL B 308 ? 2.00795 0.76632 0.59778 0.49329  0.02722  -0.01663 300 VAL B CG2 
7095 N N   . ARG B 309 ? 1.86462 0.78001 0.56889 0.52796  -0.03618 -0.02801 301 ARG B N   
7096 C CA  . ARG B 309 ? 1.83754 0.80650 0.58518 0.53182  -0.05068 -0.03347 301 ARG B CA  
7097 C C   . ARG B 309 ? 1.87276 0.86215 0.64547 0.52595  -0.05186 -0.04306 301 ARG B C   
7098 O O   . ARG B 309 ? 1.81439 0.84481 0.62573 0.51698  -0.05307 -0.04903 301 ARG B O   
7099 C CB  . ARG B 309 ? 1.86805 0.83862 0.60111 0.55338  -0.06698 -0.02915 301 ARG B CB  
7100 C CG  . ARG B 309 ? 1.85014 0.83381 0.59361 0.55428  -0.06844 -0.02857 301 ARG B CG  
7101 C CD  . ARG B 309 ? 1.80714 0.83339 0.59164 0.54818  -0.07372 -0.03233 301 ARG B CD  
7102 N NE  . ARG B 309 ? 1.70564 0.72699 0.49253 0.53485  -0.05977 -0.03093 301 ARG B NE  
7103 C CZ  . ARG B 309 ? 1.66254 0.72099 0.48488 0.52521  -0.06055 -0.03628 301 ARG B CZ  
7104 N NH1 . ARG B 309 ? 1.62648 0.72053 0.47832 0.53098  -0.07612 -0.04057 301 ARG B NH1 
7105 N NH2 . ARG B 309 ? 1.72942 0.78807 0.55466 0.51046  -0.04583 -0.03739 301 ARG B NH2 
7106 N N   . ASP B 310 ? 1.86984 0.83175 0.62102 0.53213  -0.05162 -0.04524 302 ASP B N   
7107 C CA  . ASP B 310 ? 1.86902 0.84842 0.64250 0.53054  -0.05307 -0.05599 302 ASP B CA  
7108 C C   . ASP B 310 ? 1.88543 0.81881 0.63260 0.52714  -0.04497 -0.06008 302 ASP B C   
7109 O O   . ASP B 310 ? 1.92858 0.81720 0.63705 0.53330  -0.04244 -0.05295 302 ASP B O   
7110 C CB  . ASP B 310 ? 1.87606 0.88308 0.66223 0.54884  -0.06706 -0.05789 302 ASP B CB  
7111 C CG  . ASP B 310 ? 1.82622 0.87284 0.64845 0.54728  -0.06826 -0.06812 302 ASP B CG  
7112 O OD1 . ASP B 310 ? 1.82187 0.86706 0.65260 0.53342  -0.05908 -0.07563 302 ASP B OD1 
7113 O OD2 . ASP B 310 ? 1.85329 0.93177 0.69245 0.56045  -0.07830 -0.06919 302 ASP B OD2 
7114 N N   . ALA B 311 ? 1.85015 0.79353 0.61671 0.51814  -0.04143 -0.07198 303 ALA B N   
7115 C CA  . ALA B 311 ? 1.91599 0.81963 0.66588 0.51460  -0.03606 -0.08030 303 ALA B CA  
7116 C C   . ALA B 311 ? 1.91261 0.84269 0.68625 0.52193  -0.04151 -0.09349 303 ALA B C   
7117 O O   . ALA B 311 ? 1.90497 0.88328 0.70970 0.51892  -0.04336 -0.09851 303 ALA B O   
7118 C CB  . ALA B 311 ? 1.89047 0.77479 0.63638 0.49294  -0.02447 -0.08451 303 ALA B CB  
7119 N N   . THR B 312 ? 1.90116 0.80017 0.66021 0.53207  -0.04339 -0.09911 304 THR B N   
7120 C CA  . THR B 312 ? 1.89221 0.81121 0.66995 0.54244  -0.04749 -0.11307 304 THR B CA  
7121 C C   . THR B 312 ? 1.99686 0.86745 0.75841 0.54095  -0.04452 -0.12370 304 THR B C   
7122 O O   . THR B 312 ? 2.00700 0.83098 0.74192 0.54666  -0.04510 -0.11631 304 THR B O   
7123 C CB  . THR B 312 ? 1.88176 0.82488 0.66601 0.56488  -0.05720 -0.10860 304 THR B CB  
7124 O OG1 . THR B 312 ? 2.03124 0.98633 0.82924 0.57640  -0.05891 -0.12257 304 THR B OG1 
7125 C CG2 . THR B 312 ? 1.98656 0.89302 0.74095 0.57638  -0.06180 -0.09713 304 THR B CG2 
7126 N N   . TRP B 313 ? 2.05084 0.93165 0.82752 0.53365  -0.04194 -0.14095 305 TRP B N   
7127 C CA  . TRP B 313 ? 2.09440 0.93153 0.86083 0.53131  -0.04061 -0.15551 305 TRP B CA  
7128 C C   . TRP B 313 ? 2.15636 0.99187 0.92646 0.55409  -0.04674 -0.16277 305 TRP B C   
7129 O O   . TRP B 313 ? 2.12138 1.00487 0.91135 0.56706  -0.04972 -0.16582 305 TRP B O   
7130 C CB  . TRP B 313 ? 2.02966 0.88219 0.80999 0.51487  -0.03685 -0.17341 305 TRP B CB  
7131 C CG  . TRP B 313 ? 1.97707 0.82677 0.75391 0.49202  -0.03092 -0.16824 305 TRP B CG  
7132 C CD1 . TRP B 313 ? 1.92277 0.81632 0.71421 0.48429  -0.02893 -0.15998 305 TRP B CD1 
7133 C CD2 . TRP B 313 ? 2.01659 0.81567 0.77555 0.47410  -0.02628 -0.17153 305 TRP B CD2 
7134 N NE1 . TRP B 313 ? 1.98261 0.85841 0.76622 0.46345  -0.02288 -0.15841 305 TRP B NE1 
7135 C CE2 . TRP B 313 ? 1.98227 0.79986 0.74507 0.45661  -0.02083 -0.16523 305 TRP B CE2 
7136 C CE3 . TRP B 313 ? 2.07968 0.81822 0.82153 0.47105  -0.02655 -0.17912 305 TRP B CE3 
7137 C CZ2 . TRP B 313 ? 2.00948 0.78757 0.75765 0.43659  -0.01482 -0.16657 305 TRP B CZ2 
7138 C CZ3 . TRP B 313 ? 2.10715 0.80459 0.83567 0.45034  -0.02133 -0.17963 305 TRP B CZ3 
7139 C CH2 . TRP B 313 ? 2.07259 0.78977 0.80326 0.43346  -0.01510 -0.17355 305 TRP B CH2 
7140 N N   . SER B 314 ? 2.27976 1.06103 1.03244 0.55896  -0.04827 -0.16520 306 SER B N   
7141 C CA  . SER B 314 ? 2.33429 1.10545 1.09047 0.58059  -0.05403 -0.17359 306 SER B CA  
7142 C C   . SER B 314 ? 2.37749 1.17483 1.15445 0.58328  -0.05318 -0.19753 306 SER B C   
7143 O O   . SER B 314 ? 2.40299 1.18192 1.17931 0.56843  -0.05029 -0.21188 306 SER B O   
7144 C CB  . SER B 314 ? 2.32596 1.02953 1.06068 0.58204  -0.05566 -0.17022 306 SER B CB  
7145 O OG  . SER B 314 ? 2.34906 1.04372 1.08917 0.60406  -0.06186 -0.17677 306 SER B OG  
7146 N N   . PRO B 315 ? 2.29143 1.13312 1.08625 0.60230  -0.05547 -0.20321 307 PRO B N   
7147 C CA  . PRO B 315 ? 2.23759 1.10521 1.04875 0.60781  -0.05329 -0.22651 307 PRO B CA  
7148 C C   . PRO B 315 ? 2.22234 1.04338 1.02820 0.61595  -0.05558 -0.24417 307 PRO B C   
7149 O O   . PRO B 315 ? 2.18606 1.01584 0.99975 0.61508  -0.05340 -0.26653 307 PRO B O   
7150 C CB  . PRO B 315 ? 2.19538 1.11800 1.02444 0.62866  -0.05436 -0.22415 307 PRO B CB  
7151 C CG  . PRO B 315 ? 2.19381 1.10888 1.01530 0.63792  -0.06015 -0.20184 307 PRO B CG  
7152 C CD  . PRO B 315 ? 2.20956 1.07858 1.00865 0.61975  -0.06011 -0.18831 307 PRO B CD  
7153 N N   . LEU B 316 ? 2.24947 1.02259 1.04208 0.62372  -0.06026 -0.23403 308 LEU B N   
7154 C CA  . LEU B 316 ? 2.27716 1.00063 1.06695 0.63412  -0.06409 -0.24755 308 LEU B CA  
7155 C C   . LEU B 316 ? 2.31823 0.98365 1.09442 0.61293  -0.06368 -0.25169 308 LEU B C   
7156 O O   . LEU B 316 ? 2.36751 1.00238 1.14800 0.61468  -0.06585 -0.27262 308 LEU B O   
7157 C CB  . LEU B 316 ? 2.29782 1.00131 1.08174 0.65335  -0.07006 -0.23180 308 LEU B CB  
7158 C CG  . LEU B 316 ? 2.27836 1.02810 1.07922 0.67882  -0.07233 -0.23392 308 LEU B CG  
7159 C CD1 . LEU B 316 ? 2.21168 1.02898 1.02539 0.67618  -0.06803 -0.23153 308 LEU B CD1 
7160 C CD2 . LEU B 316 ? 2.29132 1.02403 1.08404 0.69358  -0.07932 -0.21470 308 LEU B CD2 
7161 N N   . ASN B 317 ? 2.30172 0.95167 1.06281 0.59422  -0.06104 -0.23318 309 ASN B N   
7162 C CA  . ASN B 317 ? 2.34017 0.93327 1.08741 0.57257  -0.05973 -0.23292 309 ASN B CA  
7163 C C   . ASN B 317 ? 2.33352 0.94970 1.07693 0.54968  -0.05346 -0.22602 309 ASN B C   
7164 O O   . ASN B 317 ? 2.39817 1.01107 1.12769 0.54443  -0.05038 -0.20328 309 ASN B O   
7165 C CB  . ASN B 317 ? 2.40663 0.94149 1.13532 0.57602  -0.06226 -0.21321 309 ASN B CB  
7166 C CG  . ASN B 317 ? 2.47509 0.94659 1.19182 0.55499  -0.06081 -0.21166 309 ASN B CG  
7167 O OD1 . ASN B 317 ? 2.51013 0.97737 1.23336 0.53796  -0.05948 -0.22836 309 ASN B OD1 
7168 N ND2 . ASN B 317 ? 2.53180 0.95345 1.23134 0.55570  -0.06141 -0.19113 309 ASN B ND2 
7169 N N   . HIS B 318 ? 2.44511 1.08198 1.19957 0.53680  -0.05185 -0.24594 310 HIS B N   
7170 C CA  . HIS B 318 ? 2.44146 1.11295 1.19859 0.51677  -0.04664 -0.24336 310 HIS B CA  
7171 C C   . HIS B 318 ? 2.40998 1.03731 1.14910 0.49604  -0.04268 -0.22799 310 HIS B C   
7172 O O   . HIS B 318 ? 2.40031 1.05613 1.13996 0.48246  -0.03762 -0.21941 310 HIS B O   
7173 C CB  . HIS B 318 ? 2.41042 1.10630 1.18068 0.50816  -0.04734 -0.27053 310 HIS B CB  
7174 C CG  . HIS B 318 ? 2.38595 1.13669 1.17269 0.52671  -0.04785 -0.28323 310 HIS B CG  
7175 N ND1 . HIS B 318 ? 2.45332 1.21204 1.24745 0.52963  -0.04972 -0.31141 310 HIS B ND1 
7176 C CD2 . HIS B 318 ? 2.33379 1.13306 1.13044 0.54348  -0.04648 -0.27206 310 HIS B CD2 
7177 C CE1 . HIS B 318 ? 2.45449 1.26521 1.26106 0.54779  -0.04785 -0.31614 310 HIS B CE1 
7178 N NE2 . HIS B 318 ? 2.32877 1.16456 1.13840 0.55624  -0.04618 -0.29189 310 HIS B NE2 
7179 N N   . SER B 319 ? 2.36948 0.92996 1.09459 0.49370  -0.04439 -0.22412 311 SER B N   
7180 C CA  . SER B 319 ? 2.43986 0.95075 1.14582 0.47534  -0.03914 -0.20694 311 SER B CA  
7181 C C   . SER B 319 ? 2.45166 0.96485 1.14041 0.48445  -0.03466 -0.17838 311 SER B C   
7182 O O   . SER B 319 ? 2.32185 0.80749 0.99337 0.47029  -0.02733 -0.16193 311 SER B O   
7183 C CB  . SER B 319 ? 2.40752 0.84609 1.10846 0.46891  -0.04309 -0.21260 311 SER B CB  
7184 O OG  . SER B 319 ? 2.47195 0.90414 1.18572 0.45438  -0.04715 -0.23868 311 SER B OG  
7185 N N   . LEU B 320 ? 2.39655 0.94123 1.08925 0.50726  -0.03884 -0.17341 312 LEU B N   
7186 C CA  . LEU B 320 ? 2.32964 0.87707 1.00529 0.51918  -0.03769 -0.14902 312 LEU B CA  
7187 C C   . LEU B 320 ? 2.28556 0.89789 0.97004 0.51979  -0.03550 -0.14304 312 LEU B C   
7188 O O   . LEU B 320 ? 2.26312 0.92625 0.97000 0.52982  -0.03986 -0.15384 312 LEU B O   
7189 C CB  . LEU B 320 ? 2.40717 0.94617 1.08405 0.54350  -0.04591 -0.14875 312 LEU B CB  
7190 C CG  . LEU B 320 ? 2.46560 0.97560 1.11781 0.55363  -0.04655 -0.12506 312 LEU B CG  
7191 C CD1 . LEU B 320 ? 2.50113 0.97558 1.15426 0.57085  -0.05447 -0.12715 312 LEU B CD1 
7192 C CD2 . LEU B 320 ? 2.32840 0.88995 0.97827 0.56454  -0.04784 -0.11342 312 LEU B CD2 
7193 N N   . LEU B 321 ? 2.30827 0.91740 0.97668 0.50976  -0.02863 -0.12618 313 LEU B N   
7194 C CA  . LEU B 321 ? 2.20099 0.86570 0.87787 0.50911  -0.02691 -0.11823 313 LEU B CA  
7195 C C   . LEU B 321 ? 2.18741 0.84462 0.84106 0.52147  -0.02747 -0.09750 313 LEU B C   
7196 O O   . LEU B 321 ? 2.20602 0.81170 0.83066 0.51778  -0.02168 -0.08535 313 LEU B O   
7197 C CB  . LEU B 321 ? 2.13783 0.80552 0.81710 0.48559  -0.01809 -0.12005 313 LEU B CB  
7198 C CG  . LEU B 321 ? 2.05236 0.76855 0.74049 0.48209  -0.01525 -0.11049 313 LEU B CG  
7199 C CD1 . LEU B 321 ? 1.99747 0.77890 0.71713 0.49238  -0.02321 -0.11689 313 LEU B CD1 
7200 C CD2 . LEU B 321 ? 2.04143 0.75609 0.73239 0.45879  -0.00622 -0.11392 313 LEU B CD2 
7201 N N   . THR B 322 ? 2.10546 0.81141 0.77129 0.53545  -0.03438 -0.09384 314 THR B N   
7202 C CA  . THR B 322 ? 2.09264 0.79895 0.73835 0.55022  -0.03865 -0.07803 314 THR B CA  
7203 C C   . THR B 322 ? 2.04115 0.78693 0.69222 0.54480  -0.03697 -0.07001 314 THR B C   
7204 O O   . THR B 322 ? 2.02350 0.82189 0.70735 0.54371  -0.04109 -0.07663 314 THR B O   
7205 C CB  . THR B 322 ? 2.11864 0.84613 0.77598 0.57201  -0.05045 -0.08207 314 THR B CB  
7206 O OG1 . THR B 322 ? 2.17893 0.86111 0.82745 0.57814  -0.05172 -0.08692 314 THR B OG1 
7207 C CG2 . THR B 322 ? 2.10667 0.84690 0.74923 0.58667  -0.05753 -0.06974 314 THR B CG2 
7208 N N   . THR B 323 ? 2.05921 0.77984 0.67974 0.54266  -0.03099 -0.05632 315 THR B N   
7209 C CA  . THR B 323 ? 2.01887 0.77076 0.64092 0.53978  -0.02966 -0.04826 315 THR B CA  
7210 C C   . THR B 323 ? 2.02826 0.78228 0.62728 0.55835  -0.03803 -0.03872 315 THR B C   
7211 O O   . THR B 323 ? 2.10073 0.81669 0.67098 0.56914  -0.03925 -0.03504 315 THR B O   
7212 C CB  . THR B 323 ? 2.03530 0.75765 0.63793 0.52356  -0.01447 -0.04209 315 THR B CB  
7213 O OG1 . THR B 323 ? 2.10254 0.76319 0.66286 0.52732  -0.00735 -0.03312 315 THR B OG1 
7214 C CG2 . THR B 323 ? 2.07214 0.79981 0.69932 0.50315  -0.00733 -0.05352 315 THR B CG2 
7215 N N   . VAL B 324 ? 1.98264 0.77939 0.59632 0.56131  -0.04433 -0.03586 316 VAL B N   
7216 C CA  . VAL B 324 ? 2.00233 0.80322 0.59185 0.57681  -0.05268 -0.02890 316 VAL B CA  
7217 C C   . VAL B 324 ? 2.02141 0.83453 0.61030 0.57015  -0.04802 -0.02135 316 VAL B C   
7218 O O   . VAL B 324 ? 1.92211 0.76350 0.54918 0.55551  -0.04388 -0.02425 316 VAL B O   
7219 C CB  . VAL B 324 ? 1.95953 0.80309 0.57412 0.59077  -0.06974 -0.03533 316 VAL B CB  
7220 C CG1 . VAL B 324 ? 1.99624 0.82457 0.61110 0.60061  -0.07370 -0.04174 316 VAL B CG1 
7221 C CG2 . VAL B 324 ? 2.00310 0.90112 0.66825 0.58337  -0.07440 -0.04002 316 VAL B CG2 
7222 N N   . GLY B 325 ? 2.01891 0.82174 0.58858 0.57609  -0.04589 -0.01742 317 GLY B N   
7223 C CA  . GLY B 325 ? 1.99760 0.81651 0.58470 0.56911  -0.03947 -0.01316 317 GLY B CA  
7224 C C   . GLY B 325 ? 1.99317 0.83512 0.59036 0.57999  -0.04940 -0.01554 317 GLY B C   
7225 O O   . GLY B 325 ? 2.00193 0.84526 0.58791 0.59171  -0.05955 -0.02257 317 GLY B O   
7226 N N   . TRP B 326 ? 1.97235 0.82554 0.58786 0.57921  -0.04599 -0.01318 318 TRP B N   
7227 C CA  . TRP B 326 ? 1.96381 0.83094 0.58999 0.59266  -0.05477 -0.01872 318 TRP B CA  
7228 C C   . TRP B 326 ? 2.01402 0.83113 0.58912 0.60650  -0.04391 -0.02055 318 TRP B C   
7229 O O   . TRP B 326 ? 2.12814 0.95061 0.69674 0.62033  -0.05240 -0.02552 318 TRP B O   
7230 C CB  . TRP B 326 ? 1.95556 0.85125 0.60660 0.58803  -0.05444 -0.02030 318 TRP B CB  
7231 C CG  . TRP B 326 ? 1.88171 0.82997 0.58172 0.58015  -0.06831 -0.02601 318 TRP B CG  
7232 C CD1 . TRP B 326 ? 1.88077 0.85549 0.60281 0.57895  -0.08080 -0.03038 318 TRP B CD1 
7233 C CD2 . TRP B 326 ? 1.82598 0.80521 0.55489 0.57428  -0.07059 -0.02878 318 TRP B CD2 
7234 N NE1 . TRP B 326 ? 1.79046 0.80852 0.55363 0.57258  -0.08928 -0.03576 318 TRP B NE1 
7235 C CE2 . TRP B 326 ? 1.74477 0.76628 0.51361 0.56911  -0.08410 -0.03493 318 TRP B CE2 
7236 C CE3 . TRP B 326 ? 1.82569 0.79981 0.54764 0.57441  -0.06229 -0.02666 318 TRP B CE3 
7237 C CZ2 . TRP B 326 ? 1.70049 0.75705 0.50283 0.56322  -0.08994 -0.03927 318 TRP B CZ2 
7238 C CZ3 . TRP B 326 ? 1.78076 0.79105 0.53622 0.56905  -0.06917 -0.03107 318 TRP B CZ3 
7239 C CH2 . TRP B 326 ? 1.71034 0.76043 0.50568 0.56299  -0.08304 -0.03742 318 TRP B CH2 
7240 N N   . ASP B 327 ? 2.05381 0.82285 0.58562 0.60325  -0.02737 -0.01510 319 ASP B N   
7241 C CA  . ASP B 327 ? 2.13711 0.85072 0.60578 0.61712  -0.01773 -0.01034 319 ASP B CA  
7242 C C   . ASP B 327 ? 2.15859 0.86102 0.60696 0.62844  -0.03040 -0.01556 319 ASP B C   
7243 O O   . ASP B 327 ? 2.24191 0.89210 0.63607 0.64164  -0.02424 -0.01024 319 ASP B O   
7244 C CB  . ASP B 327 ? 2.17866 0.83979 0.60553 0.60881  0.00530  0.00068  319 ASP B CB  
7245 C CG  . ASP B 327 ? 2.17262 0.82570 0.60120 0.59352  0.00721  0.00047  319 ASP B CG  
7246 O OD1 . ASP B 327 ? 2.12102 0.81898 0.58822 0.58754  -0.00818 -0.00634 319 ASP B OD1 
7247 O OD2 . ASP B 327 ? 2.22461 0.82440 0.61052 0.58827  0.02380  0.00897  319 ASP B OD2 
7248 N N   . HIS B 328 ? 2.11117 0.85753 0.59712 0.62521  -0.04710 -0.02395 320 HIS B N   
7249 C CA  . HIS B 328 ? 2.14879 0.88986 0.62155 0.63832  -0.06162 -0.02841 320 HIS B CA  
7250 C C   . HIS B 328 ? 2.22096 0.90807 0.64894 0.63972  -0.05354 -0.02216 320 HIS B C   
7251 O O   . HIS B 328 ? 2.28700 0.95925 0.70684 0.65120  -0.06300 -0.02048 320 HIS B O   
7252 C CB  . HIS B 328 ? 2.16413 0.89548 0.61664 0.65894  -0.07141 -0.03262 320 HIS B CB  
7253 C CG  . HIS B 328 ? 2.21465 0.95773 0.66974 0.67230  -0.09003 -0.04023 320 HIS B CG  
7254 N ND1 . HIS B 328 ? 2.17075 0.96919 0.67443 0.66993  -0.10559 -0.04920 320 HIS B ND1 
7255 C CD2 . HIS B 328 ? 2.27693 0.99015 0.70692 0.68528  -0.09621 -0.03597 320 HIS B CD2 
7256 C CE1 . HIS B 328 ? 2.26167 1.05621 0.75450 0.68562  -0.11925 -0.05448 320 HIS B CE1 
7257 N NE2 . HIS B 328 ? 2.31194 1.05978 0.77034 0.69308  -0.11450 -0.04464 320 HIS B NE2 
7258 N N   . GLN B 329 ? 2.19015 0.85671 0.61046 0.62447  -0.03858 -0.01541 321 GLN B N   
7259 C CA  . GLN B 329 ? 2.22647 0.85360 0.64134 0.61644  -0.03236 -0.00555 321 GLN B CA  
7260 C C   . GLN B 329 ? 2.20276 0.85894 0.65628 0.60989  -0.04154 -0.01270 321 GLN B C   
7261 O O   . GLN B 329 ? 2.14779 0.84452 0.62611 0.60225  -0.04400 -0.01725 321 GLN B O   
7262 C CB  . GLN B 329 ? 2.25387 0.84329 0.65051 0.60130  -0.01154 0.00594  321 GLN B CB  
7263 C CG  . GLN B 329 ? 2.31948 0.86380 0.68518 0.60467  -0.00191 0.02321  321 GLN B CG  
7264 C CD  . GLN B 329 ? 2.35140 0.85550 0.70680 0.58606  0.01690  0.03925  321 GLN B CD  
7265 O OE1 . GLN B 329 ? 2.40039 0.86360 0.74863 0.58120  0.01956  0.05293  321 GLN B OE1 
7266 N NE2 . GLN B 329 ? 2.32569 0.84108 0.68351 0.57486  0.02953  0.03830  321 GLN B NE2 
7267 N N   . VAL B 330 ? 2.30917 0.94650 0.77228 0.61366  -0.04677 -0.01281 322 VAL B N   
7268 C CA  . VAL B 330 ? 2.18448 0.83915 0.68528 0.60797  -0.05149 -0.02149 322 VAL B CA  
7269 C C   . VAL B 330 ? 2.23070 0.83332 0.72456 0.59690  -0.04082 -0.01744 322 VAL B C   
7270 O O   . VAL B 330 ? 2.41820 0.99123 0.90914 0.60515  -0.04549 -0.01570 322 VAL B O   
7271 C CB  . VAL B 330 ? 2.17565 0.85572 0.69790 0.62472  -0.06770 -0.02905 322 VAL B CB  
7272 C CG1 . VAL B 330 ? 2.22977 0.93090 0.79088 0.62108  -0.07048 -0.03985 322 VAL B CG1 
7273 C CG2 . VAL B 330 ? 2.18291 0.90826 0.71097 0.63505  -0.07903 -0.03272 322 VAL B CG2 
7274 N N   . VAL B 331 ? 2.22481 0.81558 0.71781 0.57866  -0.02765 -0.01579 323 VAL B N   
7275 C CA  . VAL B 331 ? 2.27065 0.80860 0.75752 0.56437  -0.01662 -0.01191 323 VAL B CA  
7276 C C   . VAL B 331 ? 2.31197 0.86097 0.83482 0.55845  -0.02199 -0.02815 323 VAL B C   
7277 O O   . VAL B 331 ? 2.23006 0.82831 0.78136 0.55452  -0.02523 -0.03934 323 VAL B O   
7278 C CB  . VAL B 331 ? 2.27249 0.79383 0.74452 0.54719  0.00020  -0.00409 323 VAL B CB  
7279 C CG1 . VAL B 331 ? 2.32165 0.78747 0.79049 0.53056  0.01062  0.00102  323 VAL B CG1 
7280 C CG2 . VAL B 331 ? 2.28773 0.80321 0.72472 0.55509  0.00680  0.00999  323 VAL B CG2 
7281 N N   . HIS B 332 ? 2.38268 0.88777 0.90578 0.55816  -0.02314 -0.02910 324 HIS B N   
7282 C CA  . HIS B 332 ? 2.30568 0.80979 0.85865 0.55285  -0.02722 -0.04666 324 HIS B CA  
7283 C C   . HIS B 332 ? 2.34013 0.79751 0.88964 0.53103  -0.01662 -0.04650 324 HIS B C   
7284 O O   . HIS B 332 ? 2.39887 0.80066 0.92797 0.52795  -0.01219 -0.03203 324 HIS B O   
7285 C CB  . HIS B 332 ? 2.34067 0.82930 0.89997 0.57053  -0.03844 -0.05024 324 HIS B CB  
7286 C CG  . HIS B 332 ? 2.31502 0.84450 0.87743 0.59145  -0.04903 -0.04941 324 HIS B CG  
7287 N ND1 . HIS B 332 ? 2.26311 0.85320 0.85233 0.59673  -0.05486 -0.06119 324 HIS B ND1 
7288 C CD2 . HIS B 332 ? 2.34772 0.86653 0.89214 0.60772  -0.05543 -0.03813 324 HIS B CD2 
7289 C CE1 . HIS B 332 ? 2.32153 0.93504 0.90950 0.61492  -0.06449 -0.05750 324 HIS B CE1 
7290 N NE2 . HIS B 332 ? 2.37633 0.94749 0.93651 0.62211  -0.06541 -0.04456 324 HIS B NE2 
7291 N N   . HIS B 333 ? 2.31832 0.79827 0.88927 0.51578  -0.01339 -0.06119 325 HIS B N   
7292 C CA  . HIS B 333 ? 2.36951 0.81232 0.94041 0.49211  -0.00378 -0.06365 325 HIS B CA  
7293 C C   . HIS B 333 ? 2.39556 0.82142 0.98934 0.48701  -0.01078 -0.08400 325 HIS B C   
7294 O O   . HIS B 333 ? 2.37039 0.83867 0.98696 0.49727  -0.01946 -0.10109 325 HIS B O   
7295 C CB  . HIS B 333 ? 2.33532 0.81680 0.91447 0.47794  0.00393  -0.06762 325 HIS B CB  
7296 C CG  . HIS B 333 ? 2.36359 0.86691 0.92406 0.48436  0.00975  -0.05155 325 HIS B CG  
7297 N ND1 . HIS B 333 ? 2.34679 0.81352 0.87932 0.47635  0.02342  -0.03379 325 HIS B ND1 
7298 C CD2 . HIS B 333 ? 2.27021 0.82732 0.83713 0.49798  0.00353  -0.05064 325 HIS B CD2 
7299 C CE1 . HIS B 333 ? 2.28935 0.78695 0.80928 0.48644  0.02543  -0.02501 325 HIS B CE1 
7300 N NE2 . HIS B 333 ? 2.22332 0.77580 0.76503 0.49896  0.01224  -0.03527 325 HIS B NE2 
7301 N N   . VAL B 334 ? 2.46523 0.83120 1.05414 0.47163  -0.00710 -0.08167 326 VAL B N   
7302 C CA  . VAL B 334 ? 2.46178 0.80679 1.07257 0.46062  -0.01307 -0.10386 326 VAL B CA  
7303 C C   . VAL B 334 ? 2.48222 0.83136 1.09941 0.43539  -0.00575 -0.11182 326 VAL B C   
7304 O O   . VAL B 334 ? 2.55860 0.87673 1.15941 0.42071  0.00538  -0.09362 326 VAL B O   
7305 C CB  . VAL B 334 ? 2.51478 0.78968 1.12207 0.45903  -0.01688 -0.09719 326 VAL B CB  
7306 C CG1 . VAL B 334 ? 2.53271 0.80645 1.13677 0.48480  -0.02539 -0.09158 326 VAL B CG1 
7307 C CG2 . VAL B 334 ? 2.63544 0.85580 1.22351 0.44114  -0.00587 -0.07120 326 VAL B CG2 
7308 N N   . VAL B 335 ? 2.40279 0.79135 1.04284 0.43104  -0.01126 -0.13709 327 VAL B N   
7309 C CA  . VAL B 335 ? 2.41618 0.82157 1.06526 0.40838  -0.00658 -0.14807 327 VAL B CA  
7310 C C   . VAL B 335 ? 2.56580 0.93078 1.22713 0.39181  -0.01313 -0.16809 327 VAL B C   
7311 O O   . VAL B 335 ? 2.56459 0.93937 1.24095 0.40101  -0.02349 -0.18916 327 VAL B O   
7312 C CB  . VAL B 335 ? 2.37067 0.85572 1.03738 0.41470  -0.00889 -0.16012 327 VAL B CB  
7313 C CG1 . VAL B 335 ? 2.28289 0.78832 0.95762 0.39226  -0.00409 -0.16843 327 VAL B CG1 
7314 C CG2 . VAL B 335 ? 2.33429 0.85878 0.99440 0.43290  -0.00645 -0.14218 327 VAL B CG2 
7315 N N   . PRO B 336 ? 2.70579 1.02390 1.36238 0.36669  -0.00754 -0.16252 328 PRO B N   
7316 C CA  . PRO B 336 ? 2.71305 0.98802 1.38329 0.34837  -0.01596 -0.18104 328 PRO B CA  
7317 C C   . PRO B 336 ? 2.63685 0.95475 1.32395 0.33739  -0.02249 -0.21063 328 PRO B C   
7318 O O   . PRO B 336 ? 2.61090 0.97211 1.30983 0.35227  -0.03065 -0.23123 328 PRO B O   
7319 C CB  . PRO B 336 ? 2.74493 0.95948 1.40543 0.32421  -0.00619 -0.15810 328 PRO B CB  
7320 C CG  . PRO B 336 ? 2.72470 0.97342 1.37025 0.32411  0.00856  -0.13990 328 PRO B CG  
7321 C CD  . PRO B 336 ? 2.62412 0.92767 1.26380 0.35414  0.00710  -0.13805 328 PRO B CD  
# 
