HEADER VIRAL PROTEIN 01-APR-25 9QQN TITLE JUNIN VIRUS GP1-GP2 HETERODIMER IN COMPLEX WITH FAB OF JUN1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PRE-GLYCOPROTEIN POLYPROTEIN GP COMPLEX; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: PRE-GP-C; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: CHAINS: C; COMPND 8 CHAIN: C; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: CHAINS: D; COMPND 12 CHAIN: D; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MAMMARENAVIRUS JUNINENSE; SOURCE 3 ORGANISM_TAXID: 2169991; SOURCE 4 GENE: GPC; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 9 ORGANISM_TAXID: 10090; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 14 ORGANISM_TAXID: 10090; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS JUNIN VIRUS, GLYCOPROTEIN, STABILIZED PROTOMER, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR T.A.BOWDEN,G.C.PAESEN REVDAT 1 11-JUN-25 9QQN 0 JRNL AUTH G.C.PAESEN,W.M.NG,G.SUTTON,K.J.DOORES,T.A.BOWDEN JRNL TITL STRUCTURE AND STABILIZATION OF THE ANTIGENIC GLYCOPROTEIN JRNL TITL 2 BUILDING BLOCKS OF THE NEW WORLD MAMMARENAVIRUS SPIKE JRNL TITL 3 COMPLEX JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.55 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.1_5286 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 80.32 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 42767 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.203 REMARK 3 R VALUE (WORKING SET) : 0.201 REMARK 3 FREE R VALUE : 0.237 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.870 REMARK 3 FREE R VALUE TEST SET COUNT : 2082 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 80.3200 - 6.2900 0.99 2814 135 0.1825 0.2111 REMARK 3 2 6.2900 - 4.9900 1.00 2747 150 0.1759 0.1898 REMARK 3 3 4.9900 - 4.3600 1.00 2725 143 0.1490 0.1862 REMARK 3 4 4.3600 - 3.9600 1.00 2743 150 0.1688 0.1919 REMARK 3 5 3.9600 - 3.6800 1.00 2712 133 0.1844 0.2117 REMARK 3 6 3.6800 - 3.4600 1.00 2747 141 0.2114 0.2687 REMARK 3 7 3.4600 - 3.2900 1.00 2715 115 0.2101 0.2591 REMARK 3 8 3.2900 - 3.1400 1.00 2742 129 0.2214 0.2709 REMARK 3 9 3.1400 - 3.0200 1.00 2710 134 0.2322 0.2867 REMARK 3 10 3.0200 - 2.9200 1.00 2705 133 0.2667 0.3477 REMARK 3 11 2.9200 - 2.8300 1.00 2716 144 0.2734 0.3479 REMARK 3 12 2.8300 - 2.7500 1.00 2724 140 0.2911 0.3431 REMARK 3 13 2.7500 - 2.6800 0.99 2669 144 0.3092 0.3083 REMARK 3 14 2.6700 - 2.6100 0.98 2603 159 0.3389 0.4181 REMARK 3 15 2.6100 - 2.5500 0.95 2613 132 0.3576 0.4105 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.396 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.136 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 62.39 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 78.07 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.003 6383 REMARK 3 ANGLE : 0.584 8668 REMARK 3 CHIRALITY : 0.041 1014 REMARK 3 PLANARITY : 0.005 1065 REMARK 3 DIHEDRAL : 16.505 2496 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9QQN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-APR-25. REMARK 100 THE DEPOSITION ID IS D_1292146776. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-AUG-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43012 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550 REMARK 200 RESOLUTION RANGE LOW (A) : 112.660 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 4.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.05 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5 MM YTTRIUM(III) CHLORIDE REMARK 280 HEXAHYDRATE, 0.5 MM ERBIUM(III) CHLORIDE HEXAHYDRATE, 0.5 MM REMARK 280 TERBIUM(III) CHLORIDE HEXAHYDRATE, 0.5 MM YTTERBIUM(III) REMARK 280 CHLORIDE HEXAHYDRATE 0.1 M MOPSO/BIS-TRIS, PH 6.5 10% W/V PEG REMARK 280 8000, 20% V/V 1,5-PENTANEDIOL, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 294K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 113.23400 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.51500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 113.23400 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.51500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 13900 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 36670 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 GLY A 2 REMARK 465 GLN A 3 REMARK 465 PHE A 4 REMARK 465 ILE A 5 REMARK 465 SER A 6 REMARK 465 PHE A 7 REMARK 465 MET A 8 REMARK 465 GLN A 9 REMARK 465 GLU A 10 REMARK 465 ILE A 11 REMARK 465 PRO A 12 REMARK 465 THR A 13 REMARK 465 PHE A 14 REMARK 465 LEU A 15 REMARK 465 GLN A 16 REMARK 465 GLU A 17 REMARK 465 ALA A 18 REMARK 465 LEU A 19 REMARK 465 ASN A 20 REMARK 465 ILE A 21 REMARK 465 ALA A 22 REMARK 465 LEU A 23 REMARK 465 VAL A 24 REMARK 465 ALA A 25 REMARK 465 VAL A 26 REMARK 465 SER A 27 REMARK 465 LEU A 28 REMARK 465 ILE A 29 REMARK 465 ALA A 30 REMARK 465 ILE A 31 REMARK 465 ILE A 32 REMARK 465 LYS A 33 REMARK 465 GLY A 34 REMARK 465 ILE A 35 REMARK 465 VAL A 36 REMARK 465 ASN A 37 REMARK 465 LEU A 38 REMARK 465 TYR A 39 REMARK 465 LYS A 40 REMARK 465 SER A 41 REMARK 465 GLY A 42 REMARK 465 LEU A 43 REMARK 465 PHE A 44 REMARK 465 GLN A 45 REMARK 465 PHE A 46 REMARK 465 PHE A 47 REMARK 465 VAL A 48 REMARK 465 PHE A 49 REMARK 465 LEU A 50 REMARK 465 ALA A 51 REMARK 465 LEU A 52 REMARK 465 ALA A 53 REMARK 465 GLY A 54 REMARK 465 ARG A 55 REMARK 465 SER A 56 REMARK 465 CYS A 57 REMARK 465 THR A 58 REMARK 465 GLU A 59 REMARK 465 ILE A 243 REMARK 465 GLN A 244 REMARK 465 LEU A 245 REMARK 465 PRO A 246 REMARK 465 ARG A 247 REMARK 465 ARG A 248 REMARK 465 ARG A 249 REMARK 465 ARG A 250 REMARK 465 ARG A 251 REMARK 465 ALA A 252 REMARK 465 PHE A 253 REMARK 465 PHE A 254 REMARK 465 SER A 255 REMARK 465 TRP A 256 REMARK 465 SER A 257 REMARK 465 LEU A 258 REMARK 465 THR A 259 REMARK 465 ASP A 260 REMARK 465 SER A 261 REMARK 465 SER A 262 REMARK 465 GLY A 263 REMARK 465 LYS A 264 REMARK 465 ASP A 265 REMARK 465 THR A 266 REMARK 465 PRO A 267 REMARK 465 GLY A 268 REMARK 465 GLY A 269 REMARK 465 TYR A 270 REMARK 465 CYS A 271 REMARK 465 LEU A 272 REMARK 465 GLU A 273 REMARK 465 GLU A 274 REMARK 465 TRP A 275 REMARK 465 MET A 276 REMARK 465 LEU A 277 REMARK 465 VAL A 278 REMARK 465 ALA A 279 REMARK 465 ALA A 280 REMARK 465 LYS A 281 REMARK 465 MET A 282 REMARK 465 LYS A 283 REMARK 465 CYS A 284 REMARK 465 PHE A 285 REMARK 465 GLY A 286 REMARK 465 ASN A 287 REMARK 465 THR A 288 REMARK 465 ALA A 289 REMARK 465 VAL A 290 REMARK 465 ALA A 291 REMARK 465 LYS A 292 REMARK 465 CYS A 293 REMARK 465 ASN A 294 REMARK 465 LEU A 295 REMARK 465 ASN A 296 REMARK 465 HIS A 297 REMARK 465 ASP A 298 REMARK 465 SER A 299 REMARK 465 GLU A 300 REMARK 465 PHE A 301 REMARK 465 CYS A 302 REMARK 465 ASP A 303 REMARK 465 MET A 304 REMARK 465 LEU A 305 REMARK 465 ARG A 306 REMARK 465 LEU A 307 REMARK 465 PHE A 308 REMARK 465 ASP A 309 REMARK 465 TYR A 310 REMARK 465 ASN A 311 REMARK 465 LYS A 312 REMARK 465 ASN A 313 REMARK 465 ALA A 314 REMARK 465 ILE A 315 REMARK 465 LYS A 316 REMARK 465 THR A 317 REMARK 465 LEU A 318 REMARK 465 ASN A 319 REMARK 465 ASP A 320 REMARK 465 GLU A 321 REMARK 465 THR A 322 REMARK 465 LYS A 323 REMARK 465 LYS A 324 REMARK 465 GLN A 325 REMARK 465 VAL A 326 REMARK 465 ASN A 327 REMARK 465 LEU A 328 REMARK 465 CYS A 329 REMARK 465 GLY A 330 REMARK 465 GLN A 331 REMARK 465 THR A 332 REMARK 465 ILE A 333 REMARK 465 ASN A 334 REMARK 465 ALA A 335 REMARK 465 LEU A 336 REMARK 465 ILE A 337 REMARK 465 SER A 338 REMARK 465 ASP A 339 REMARK 465 ASN A 340 REMARK 465 LEU A 341 REMARK 465 LEU A 342 REMARK 465 MET A 343 REMARK 465 LYS A 344 REMARK 465 ASN A 345 REMARK 465 LYS A 346 REMARK 465 ILE A 347 REMARK 465 ARG A 348 REMARK 465 GLU A 349 REMARK 465 LEU A 350 REMARK 465 MET A 351 REMARK 465 SER A 352 REMARK 465 VAL A 353 REMARK 465 PRO A 354 REMARK 465 TYR A 355 REMARK 465 CYS A 356 REMARK 465 ASN A 357 REMARK 465 TYR A 358 REMARK 465 THR A 359 REMARK 465 LYS A 360 REMARK 465 PHE A 361 REMARK 465 TRP A 362 REMARK 465 TYR A 363 REMARK 465 VAL A 364 REMARK 465 ASN A 365 REMARK 465 HIS A 366 REMARK 465 THR A 367 REMARK 465 LEU A 368 REMARK 465 SER A 369 REMARK 465 GLY A 370 REMARK 465 GLN A 371 REMARK 465 HIS A 372 REMARK 465 SER A 373 REMARK 465 LEU A 374 REMARK 465 PRO A 375 REMARK 465 ARG A 376 REMARK 465 CYS A 377 REMARK 465 TRP A 378 REMARK 465 LEU A 379 REMARK 465 ILE A 380 REMARK 465 LYS A 381 REMARK 465 ASN A 382 REMARK 465 ASN A 383 REMARK 465 SER A 384 REMARK 465 TYR A 385 REMARK 465 LEU A 386 REMARK 465 ASN A 387 REMARK 465 ILE A 388 REMARK 465 SER A 389 REMARK 465 ASP A 390 REMARK 465 PHE A 391 REMARK 465 ARG A 392 REMARK 465 ASN A 393 REMARK 465 ASP A 394 REMARK 465 TRP A 395 REMARK 465 ILE A 396 REMARK 465 LEU A 397 REMARK 465 GLU A 398 REMARK 465 SER A 399 REMARK 465 ASP A 400 REMARK 465 PHE A 401 REMARK 465 LEU A 402 REMARK 465 ILE A 403 REMARK 465 SER A 404 REMARK 465 GLU A 405 REMARK 465 MET A 406 REMARK 465 LEU A 407 REMARK 465 SER A 408 REMARK 465 LYS A 409 REMARK 465 GLU A 410 REMARK 465 TYR A 411 REMARK 465 SER A 412 REMARK 465 ASP A 413 REMARK 465 ARG A 414 REMARK 465 GLN A 415 REMARK 465 GLY A 416 REMARK 465 SER A 417 REMARK 465 GLY A 418 REMARK 465 ASP A 419 REMARK 465 ASP A 420 REMARK 465 ASP A 421 REMARK 465 ASP A 422 REMARK 465 LYS A 423 REMARK 465 GLY A 424 REMARK 465 SER A 425 REMARK 465 GLY A 426 REMARK 465 TRP A 427 REMARK 465 SER A 428 REMARK 465 HIS A 429 REMARK 465 PRO A 430 REMARK 465 GLN A 431 REMARK 465 PHE A 432 REMARK 465 GLU A 433 REMARK 465 LYS A 434 REMARK 465 GLY A 435 REMARK 465 GLY A 436 REMARK 465 GLY A 437 REMARK 465 SER A 438 REMARK 465 GLY A 439 REMARK 465 GLY A 440 REMARK 465 GLY A 441 REMARK 465 SER A 442 REMARK 465 GLY A 443 REMARK 465 GLY A 444 REMARK 465 SER A 445 REMARK 465 ALA A 446 REMARK 465 TRP A 447 REMARK 465 SER A 448 REMARK 465 HIS A 449 REMARK 465 PRO A 450 REMARK 465 GLN A 451 REMARK 465 PHE A 452 REMARK 465 GLU A 453 REMARK 465 LYS A 454 REMARK 465 MET B 1 REMARK 465 GLY B 2 REMARK 465 GLN B 3 REMARK 465 PHE B 4 REMARK 465 ILE B 5 REMARK 465 SER B 6 REMARK 465 PHE B 7 REMARK 465 MET B 8 REMARK 465 GLN B 9 REMARK 465 GLU B 10 REMARK 465 ILE B 11 REMARK 465 PRO B 12 REMARK 465 THR B 13 REMARK 465 PHE B 14 REMARK 465 LEU B 15 REMARK 465 GLN B 16 REMARK 465 GLU B 17 REMARK 465 ALA B 18 REMARK 465 LEU B 19 REMARK 465 ASN B 20 REMARK 465 ILE B 21 REMARK 465 ALA B 22 REMARK 465 LEU B 23 REMARK 465 VAL B 24 REMARK 465 ALA B 25 REMARK 465 VAL B 26 REMARK 465 SER B 27 REMARK 465 LEU B 28 REMARK 465 ILE B 29 REMARK 465 ALA B 30 REMARK 465 ILE B 31 REMARK 465 ILE B 32 REMARK 465 LYS B 33 REMARK 465 GLY B 34 REMARK 465 ILE B 35 REMARK 465 VAL B 36 REMARK 465 ASN B 37 REMARK 465 LEU B 38 REMARK 465 TYR B 39 REMARK 465 LYS B 40 REMARK 465 SER B 41 REMARK 465 GLY B 42 REMARK 465 LEU B 43 REMARK 465 PHE B 44 REMARK 465 GLN B 45 REMARK 465 PHE B 46 REMARK 465 PHE B 47 REMARK 465 VAL B 48 REMARK 465 PHE B 49 REMARK 465 LEU B 50 REMARK 465 ALA B 51 REMARK 465 LEU B 52 REMARK 465 ALA B 53 REMARK 465 GLY B 54 REMARK 465 ARG B 55 REMARK 465 SER B 56 REMARK 465 CYS B 57 REMARK 465 THR B 58 REMARK 465 GLU B 59 REMARK 465 GLU B 60 REMARK 465 ALA B 61 REMARK 465 PHE B 62 REMARK 465 LYS B 63 REMARK 465 ILE B 64 REMARK 465 GLY B 65 REMARK 465 LEU B 66 REMARK 465 HIS B 67 REMARK 465 THR B 68 REMARK 465 GLU B 69 REMARK 465 PHE B 70 REMARK 465 GLN B 71 REMARK 465 THR B 72 REMARK 465 VAL B 73 REMARK 465 SER B 74 REMARK 465 PHE B 75 REMARK 465 SER B 76 REMARK 465 MET B 77 REMARK 465 VAL B 78 REMARK 465 GLY B 79 REMARK 465 LEU B 80 REMARK 465 PHE B 81 REMARK 465 SER B 82 REMARK 465 ASN B 83 REMARK 465 ASN B 84 REMARK 465 PRO B 85 REMARK 465 HIS B 86 REMARK 465 ASP B 87 REMARK 465 CYS B 88 REMARK 465 PRO B 89 REMARK 465 LEU B 90 REMARK 465 LEU B 91 REMARK 465 CYS B 92 REMARK 465 THR B 93 REMARK 465 LEU B 94 REMARK 465 ASN B 95 REMARK 465 LYS B 96 REMARK 465 SER B 97 REMARK 465 HIS B 98 REMARK 465 LEU B 99 REMARK 465 TYR B 100 REMARK 465 ILE B 101 REMARK 465 LYS B 102 REMARK 465 GLY B 103 REMARK 465 GLY B 104 REMARK 465 ASN B 105 REMARK 465 ALA B 106 REMARK 465 SER B 107 REMARK 465 PHE B 108 REMARK 465 GLN B 109 REMARK 465 ILE B 110 REMARK 465 SER B 111 REMARK 465 PHE B 112 REMARK 465 ASP B 113 REMARK 465 ASP B 114 REMARK 465 ILE B 115 REMARK 465 ALA B 116 REMARK 465 VAL B 117 REMARK 465 LEU B 118 REMARK 465 LEU B 119 REMARK 465 PRO B 120 REMARK 465 GLN B 121 REMARK 465 TYR B 122 REMARK 465 ASP B 123 REMARK 465 VAL B 124 REMARK 465 ILE B 125 REMARK 465 ILE B 126 REMARK 465 GLN B 127 REMARK 465 HIS B 128 REMARK 465 PRO B 129 REMARK 465 ALA B 130 REMARK 465 ASP B 131 REMARK 465 MET B 132 REMARK 465 SER B 133 REMARK 465 TRP B 134 REMARK 465 CYS B 135 REMARK 465 SER B 136 REMARK 465 LYS B 137 REMARK 465 SER B 138 REMARK 465 ASP B 139 REMARK 465 ASP B 140 REMARK 465 GLN B 141 REMARK 465 ILE B 142 REMARK 465 TRP B 143 REMARK 465 LEU B 144 REMARK 465 SER B 145 REMARK 465 GLN B 146 REMARK 465 TRP B 147 REMARK 465 PHE B 148 REMARK 465 MET B 149 REMARK 465 ASN B 150 REMARK 465 ALA B 151 REMARK 465 VAL B 152 REMARK 465 GLY B 153 REMARK 465 HIS B 154 REMARK 465 ASP B 155 REMARK 465 TRP B 156 REMARK 465 HIS B 157 REMARK 465 LEU B 158 REMARK 465 ASP B 159 REMARK 465 PRO B 160 REMARK 465 PRO B 161 REMARK 465 PHE B 162 REMARK 465 LEU B 163 REMARK 465 CYS B 164 REMARK 465 ARG B 165 REMARK 465 ASN B 166 REMARK 465 ARG B 167 REMARK 465 THR B 168 REMARK 465 LYS B 169 REMARK 465 THR B 170 REMARK 465 GLU B 171 REMARK 465 GLY B 172 REMARK 465 PHE B 173 REMARK 465 ILE B 174 REMARK 465 PHE B 175 REMARK 465 GLN B 176 REMARK 465 VAL B 177 REMARK 465 ASN B 178 REMARK 465 THR B 179 REMARK 465 SER B 180 REMARK 465 LYS B 181 REMARK 465 THR B 182 REMARK 465 GLY B 183 REMARK 465 VAL B 184 REMARK 465 ASN B 185 REMARK 465 GLU B 186 REMARK 465 ASN B 187 REMARK 465 TYR B 188 REMARK 465 ALA B 189 REMARK 465 LYS B 190 REMARK 465 LYS B 191 REMARK 465 PHE B 192 REMARK 465 LYS B 193 REMARK 465 THR B 194 REMARK 465 GLY B 195 REMARK 465 MET B 196 REMARK 465 HIS B 197 REMARK 465 HIS B 198 REMARK 465 LEU B 199 REMARK 465 TYR B 200 REMARK 465 ARG B 201 REMARK 465 GLU B 202 REMARK 465 TYR B 203 REMARK 465 PRO B 204 REMARK 465 ASP B 205 REMARK 465 SER B 206 REMARK 465 CYS B 207 REMARK 465 LEU B 208 REMARK 465 ASN B 209 REMARK 465 GLY B 210 REMARK 465 LYS B 211 REMARK 465 LEU B 212 REMARK 465 CYS B 213 REMARK 465 LEU B 214 REMARK 465 MET B 215 REMARK 465 LYS B 216 REMARK 465 ALA B 217 REMARK 465 GLN B 218 REMARK 465 PRO B 219 REMARK 465 THR B 220 REMARK 465 SER B 221 REMARK 465 TRP B 222 REMARK 465 PRO B 223 REMARK 465 LEU B 224 REMARK 465 GLN B 225 REMARK 465 CYS B 226 REMARK 465 PRO B 227 REMARK 465 LEU B 228 REMARK 465 ASP B 229 REMARK 465 HIS B 230 REMARK 465 VAL B 231 REMARK 465 ASN B 232 REMARK 465 THR B 233 REMARK 465 LEU B 234 REMARK 465 HIS B 235 REMARK 465 PHE B 236 REMARK 465 LEU B 237 REMARK 465 THR B 238 REMARK 465 ARG B 239 REMARK 465 GLY B 240 REMARK 465 LYS B 241 REMARK 465 ASN B 242 REMARK 465 ILE B 243 REMARK 465 GLN B 244 REMARK 465 LEU B 245 REMARK 465 PRO B 246 REMARK 465 ARG B 247 REMARK 465 ARG B 248 REMARK 465 ARG B 249 REMARK 465 ARG B 250 REMARK 465 ARG B 251 REMARK 465 ASP B 260 REMARK 465 SER B 261 REMARK 465 SER B 262 REMARK 465 GLY B 263 REMARK 465 LYS B 264 REMARK 465 ASP B 265 REMARK 465 THR B 266 REMARK 465 PRO B 267 REMARK 465 GLY B 268 REMARK 465 LEU B 318 REMARK 465 ASN B 319 REMARK 465 ASP B 320 REMARK 465 GLU B 321 REMARK 465 THR B 322 REMARK 465 LYS B 323 REMARK 465 LYS B 324 REMARK 465 GLN B 325 REMARK 465 VAL B 326 REMARK 465 ASN B 327 REMARK 465 ASP B 413 REMARK 465 ARG B 414 REMARK 465 GLN B 415 REMARK 465 GLY B 416 REMARK 465 SER B 417 REMARK 465 GLY B 418 REMARK 465 ASP B 419 REMARK 465 ASP B 420 REMARK 465 ASP B 421 REMARK 465 ASP B 422 REMARK 465 LYS B 423 REMARK 465 GLY B 424 REMARK 465 SER B 425 REMARK 465 GLY B 426 REMARK 465 TRP B 427 REMARK 465 SER B 428 REMARK 465 HIS B 429 REMARK 465 PRO B 430 REMARK 465 GLN B 431 REMARK 465 PHE B 432 REMARK 465 GLU B 433 REMARK 465 LYS B 434 REMARK 465 GLY B 435 REMARK 465 GLY B 436 REMARK 465 GLY B 437 REMARK 465 SER B 438 REMARK 465 GLY B 439 REMARK 465 GLY B 440 REMARK 465 GLY B 441 REMARK 465 SER B 442 REMARK 465 GLY B 443 REMARK 465 GLY B 444 REMARK 465 SER B 445 REMARK 465 ALA B 446 REMARK 465 TRP B 447 REMARK 465 SER B 448 REMARK 465 HIS B 449 REMARK 465 PRO B 450 REMARK 465 GLN B 451 REMARK 465 PHE B 452 REMARK 465 GLU B 453 REMARK 465 LYS B 454 REMARK 465 GLU C -2 REMARK 465 THR C -1 REMARK 465 GLY C 0 REMARK 465 ASN C 212 REMARK 465 GLU C 213 REMARK 465 CYS C 214 REMARK 465 GLU D -2 REMARK 465 ALA D 145 REMARK 465 GLN D 146 REMARK 465 THR D 147 REMARK 465 ASN D 148 REMARK 465 ASP D 229 REMARK 465 CYS D 230 REMARK 465 GLY D 231 REMARK 465 THR D 232 REMARK 465 LYS D 233 REMARK 465 HIS D 234 REMARK 465 HIS D 235 REMARK 465 HIS D 236 REMARK 465 HIS D 237 REMARK 465 HIS D 238 REMARK 465 HIS D 239 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 83 36.41 -90.62 REMARK 500 ILE A 174 147.18 -172.27 REMARK 500 THR A 179 -4.90 66.41 REMARK 500 CYS A 213 80.75 -151.52 REMARK 500 LEU B 258 -80.78 -72.54 REMARK 500 ASP B 298 31.26 -140.25 REMARK 500 THR B 359 -61.75 -123.12 REMARK 500 PHE B 391 34.31 -141.87 REMARK 500 ALA C 51 -28.49 69.26 REMARK 500 ASN C 138 76.45 58.34 REMARK 500 GLN D 1 127.82 -35.21 REMARK 500 ILE D 51 -60.08 -109.32 REMARK 500 THR D 55 -161.74 -105.59 REMARK 500 TYR D 113 42.25 -99.97 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9GHI RELATED DB: PDB REMARK 900 RELATED ID: 9GHJ RELATED DB: PDB DBREF 9QQN A 1 416 UNP C1K9J9 C1K9J9_JUNIN 1 416 DBREF 9QQN B 1 416 UNP C1K9J9 C1K9J9_JUNIN 1 416 DBREF 9QQN C -2 214 PDB 9QQN 9QQN -2 214 DBREF 9QQN D -2 239 PDB 9QQN 9QQN -2 239 SEQADV 9QQN CYS A 88 UNP C1K9J9 LEU 88 CONFLICT SEQADV 9QQN ARG A 249 UNP C1K9J9 SER 249 CONFLICT SEQADV 9QQN ARG A 250 UNP C1K9J9 LEU 250 CONFLICT SEQADV 9QQN ARG A 251 UNP C1K9J9 LYS 251 CONFLICT SEQADV 9QQN CYS A 329 UNP C1K9J9 MET 329 CONFLICT SEQADV 9QQN SER A 417 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY A 418 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN ASP A 419 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN ASP A 420 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN ASP A 421 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN ASP A 422 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN LYS A 423 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY A 424 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN SER A 425 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY A 426 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN TRP A 427 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN SER A 428 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN HIS A 429 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN PRO A 430 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLN A 431 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN PHE A 432 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLU A 433 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN LYS A 434 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY A 435 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY A 436 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY A 437 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN SER A 438 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY A 439 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY A 440 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY A 441 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN SER A 442 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY A 443 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY A 444 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN SER A 445 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN ALA A 446 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN TRP A 447 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN SER A 448 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN HIS A 449 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN PRO A 450 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLN A 451 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN PHE A 452 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLU A 453 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN LYS A 454 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN CYS B 88 UNP C1K9J9 LEU 88 CONFLICT SEQADV 9QQN ARG B 249 UNP C1K9J9 SER 249 CONFLICT SEQADV 9QQN ARG B 250 UNP C1K9J9 LEU 250 CONFLICT SEQADV 9QQN ARG B 251 UNP C1K9J9 LYS 251 CONFLICT SEQADV 9QQN CYS B 329 UNP C1K9J9 MET 329 CONFLICT SEQADV 9QQN SER B 417 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY B 418 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN ASP B 419 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN ASP B 420 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN ASP B 421 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN ASP B 422 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN LYS B 423 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY B 424 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN SER B 425 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY B 426 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN TRP B 427 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN SER B 428 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN HIS B 429 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN PRO B 430 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLN B 431 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN PHE B 432 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLU B 433 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN LYS B 434 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY B 435 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY B 436 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY B 437 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN SER B 438 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY B 439 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY B 440 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY B 441 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN SER B 442 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY B 443 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLY B 444 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN SER B 445 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN ALA B 446 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN TRP B 447 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN SER B 448 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN HIS B 449 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN PRO B 450 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLN B 451 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN PHE B 452 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN GLU B 453 UNP C1K9J9 EXPRESSION TAG SEQADV 9QQN LYS B 454 UNP C1K9J9 EXPRESSION TAG SEQRES 1 A 454 MET GLY GLN PHE ILE SER PHE MET GLN GLU ILE PRO THR SEQRES 2 A 454 PHE LEU GLN GLU ALA LEU ASN ILE ALA LEU VAL ALA VAL SEQRES 3 A 454 SER LEU ILE ALA ILE ILE LYS GLY ILE VAL ASN LEU TYR SEQRES 4 A 454 LYS SER GLY LEU PHE GLN PHE PHE VAL PHE LEU ALA LEU SEQRES 5 A 454 ALA GLY ARG SER CYS THR GLU GLU ALA PHE LYS ILE GLY SEQRES 6 A 454 LEU HIS THR GLU PHE GLN THR VAL SER PHE SER MET VAL SEQRES 7 A 454 GLY LEU PHE SER ASN ASN PRO HIS ASP CYS PRO LEU LEU SEQRES 8 A 454 CYS THR LEU ASN LYS SER HIS LEU TYR ILE LYS GLY GLY SEQRES 9 A 454 ASN ALA SER PHE GLN ILE SER PHE ASP ASP ILE ALA VAL SEQRES 10 A 454 LEU LEU PRO GLN TYR ASP VAL ILE ILE GLN HIS PRO ALA SEQRES 11 A 454 ASP MET SER TRP CYS SER LYS SER ASP ASP GLN ILE TRP SEQRES 12 A 454 LEU SER GLN TRP PHE MET ASN ALA VAL GLY HIS ASP TRP SEQRES 13 A 454 HIS LEU ASP PRO PRO PHE LEU CYS ARG ASN ARG THR LYS SEQRES 14 A 454 THR GLU GLY PHE ILE PHE GLN VAL ASN THR SER LYS THR SEQRES 15 A 454 GLY VAL ASN GLU ASN TYR ALA LYS LYS PHE LYS THR GLY SEQRES 16 A 454 MET HIS HIS LEU TYR ARG GLU TYR PRO ASP SER CYS LEU SEQRES 17 A 454 ASN GLY LYS LEU CYS LEU MET LYS ALA GLN PRO THR SER SEQRES 18 A 454 TRP PRO LEU GLN CYS PRO LEU ASP HIS VAL ASN THR LEU SEQRES 19 A 454 HIS PHE LEU THR ARG GLY LYS ASN ILE GLN LEU PRO ARG SEQRES 20 A 454 ARG ARG ARG ARG ALA PHE PHE SER TRP SER LEU THR ASP SEQRES 21 A 454 SER SER GLY LYS ASP THR PRO GLY GLY TYR CYS LEU GLU SEQRES 22 A 454 GLU TRP MET LEU VAL ALA ALA LYS MET LYS CYS PHE GLY SEQRES 23 A 454 ASN THR ALA VAL ALA LYS CYS ASN LEU ASN HIS ASP SER SEQRES 24 A 454 GLU PHE CYS ASP MET LEU ARG LEU PHE ASP TYR ASN LYS SEQRES 25 A 454 ASN ALA ILE LYS THR LEU ASN ASP GLU THR LYS LYS GLN SEQRES 26 A 454 VAL ASN LEU CYS GLY GLN THR ILE ASN ALA LEU ILE SER SEQRES 27 A 454 ASP ASN LEU LEU MET LYS ASN LYS ILE ARG GLU LEU MET SEQRES 28 A 454 SER VAL PRO TYR CYS ASN TYR THR LYS PHE TRP TYR VAL SEQRES 29 A 454 ASN HIS THR LEU SER GLY GLN HIS SER LEU PRO ARG CYS SEQRES 30 A 454 TRP LEU ILE LYS ASN ASN SER TYR LEU ASN ILE SER ASP SEQRES 31 A 454 PHE ARG ASN ASP TRP ILE LEU GLU SER ASP PHE LEU ILE SEQRES 32 A 454 SER GLU MET LEU SER LYS GLU TYR SER ASP ARG GLN GLY SEQRES 33 A 454 SER GLY ASP ASP ASP ASP LYS GLY SER GLY TRP SER HIS SEQRES 34 A 454 PRO GLN PHE GLU LYS GLY GLY GLY SER GLY GLY GLY SER SEQRES 35 A 454 GLY GLY SER ALA TRP SER HIS PRO GLN PHE GLU LYS SEQRES 1 B 454 MET GLY GLN PHE ILE SER PHE MET GLN GLU ILE PRO THR SEQRES 2 B 454 PHE LEU GLN GLU ALA LEU ASN ILE ALA LEU VAL ALA VAL SEQRES 3 B 454 SER LEU ILE ALA ILE ILE LYS GLY ILE VAL ASN LEU TYR SEQRES 4 B 454 LYS SER GLY LEU PHE GLN PHE PHE VAL PHE LEU ALA LEU SEQRES 5 B 454 ALA GLY ARG SER CYS THR GLU GLU ALA PHE LYS ILE GLY SEQRES 6 B 454 LEU HIS THR GLU PHE GLN THR VAL SER PHE SER MET VAL SEQRES 7 B 454 GLY LEU PHE SER ASN ASN PRO HIS ASP CYS PRO LEU LEU SEQRES 8 B 454 CYS THR LEU ASN LYS SER HIS LEU TYR ILE LYS GLY GLY SEQRES 9 B 454 ASN ALA SER PHE GLN ILE SER PHE ASP ASP ILE ALA VAL SEQRES 10 B 454 LEU LEU PRO GLN TYR ASP VAL ILE ILE GLN HIS PRO ALA SEQRES 11 B 454 ASP MET SER TRP CYS SER LYS SER ASP ASP GLN ILE TRP SEQRES 12 B 454 LEU SER GLN TRP PHE MET ASN ALA VAL GLY HIS ASP TRP SEQRES 13 B 454 HIS LEU ASP PRO PRO PHE LEU CYS ARG ASN ARG THR LYS SEQRES 14 B 454 THR GLU GLY PHE ILE PHE GLN VAL ASN THR SER LYS THR SEQRES 15 B 454 GLY VAL ASN GLU ASN TYR ALA LYS LYS PHE LYS THR GLY SEQRES 16 B 454 MET HIS HIS LEU TYR ARG GLU TYR PRO ASP SER CYS LEU SEQRES 17 B 454 ASN GLY LYS LEU CYS LEU MET LYS ALA GLN PRO THR SER SEQRES 18 B 454 TRP PRO LEU GLN CYS PRO LEU ASP HIS VAL ASN THR LEU SEQRES 19 B 454 HIS PHE LEU THR ARG GLY LYS ASN ILE GLN LEU PRO ARG SEQRES 20 B 454 ARG ARG ARG ARG ALA PHE PHE SER TRP SER LEU THR ASP SEQRES 21 B 454 SER SER GLY LYS ASP THR PRO GLY GLY TYR CYS LEU GLU SEQRES 22 B 454 GLU TRP MET LEU VAL ALA ALA LYS MET LYS CYS PHE GLY SEQRES 23 B 454 ASN THR ALA VAL ALA LYS CYS ASN LEU ASN HIS ASP SER SEQRES 24 B 454 GLU PHE CYS ASP MET LEU ARG LEU PHE ASP TYR ASN LYS SEQRES 25 B 454 ASN ALA ILE LYS THR LEU ASN ASP GLU THR LYS LYS GLN SEQRES 26 B 454 VAL ASN LEU CYS GLY GLN THR ILE ASN ALA LEU ILE SER SEQRES 27 B 454 ASP ASN LEU LEU MET LYS ASN LYS ILE ARG GLU LEU MET SEQRES 28 B 454 SER VAL PRO TYR CYS ASN TYR THR LYS PHE TRP TYR VAL SEQRES 29 B 454 ASN HIS THR LEU SER GLY GLN HIS SER LEU PRO ARG CYS SEQRES 30 B 454 TRP LEU ILE LYS ASN ASN SER TYR LEU ASN ILE SER ASP SEQRES 31 B 454 PHE ARG ASN ASP TRP ILE LEU GLU SER ASP PHE LEU ILE SEQRES 32 B 454 SER GLU MET LEU SER LYS GLU TYR SER ASP ARG GLN GLY SEQRES 33 B 454 SER GLY ASP ASP ASP ASP LYS GLY SER GLY TRP SER HIS SEQRES 34 B 454 PRO GLN PHE GLU LYS GLY GLY GLY SER GLY GLY GLY SER SEQRES 35 B 454 GLY GLY SER ALA TRP SER HIS PRO GLN PHE GLU LYS SEQRES 1 C 217 GLU THR GLY SER VAL VAL MET THR GLN SER GLN LYS PHE SEQRES 2 C 217 MET SER THR SER VAL GLY ASP ARG VAL SER ILE THR CYS SEQRES 3 C 217 LYS ALA SER GLN ILE VAL GLY THR SER VAL ALA TRP TYR SEQRES 4 C 217 GLN GLN LYS ALA GLY GLN SER PRO LYS LEU LEU ILE TYR SEQRES 5 C 217 TRP ALA SER THR ARG HIS THR GLY VAL PRO ASP ARG PHE SEQRES 6 C 217 THR ALA GLY GLY SER GLY THR ASP PHE THR LEU THR ILE SEQRES 7 C 217 THR ASN VAL GLN SER GLU ASP LEU ALA ASP TYR PHE CYS SEQRES 8 C 217 GLN GLN TYR ALA THR TYR PRO LEU THR PHE GLY SER GLY SEQRES 9 C 217 THR LYS LEU GLU LEU LYS ARG THR ASP ALA ALA PRO THR SEQRES 10 C 217 VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU THR SER SEQRES 11 C 217 GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR SEQRES 12 C 217 PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER SEQRES 13 C 217 GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN SEQRES 14 C 217 ASP SER LYS ASP SER THR TYR SER MET SER SER THR LEU SEQRES 15 C 217 THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR SEQRES 16 C 217 THR CYS GLU ALA THR HIS LYS THR SER THR SER PRO ILE SEQRES 17 C 217 VAL LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 D 242 GLU THR GLY GLN ILE GLN LEU VAL GLN SER VAL GLU THR SEQRES 2 D 242 GLY GLY GLY LEU VAL ARG PRO GLY ASN SER LEU LYS LEU SEQRES 3 D 242 SER CYS VAL THR SER GLY PHE THR PHE SER ASN TYR GLN SEQRES 4 D 242 MET HIS TRP LEU ARG GLN PRO PRO GLY LYS ARG LEU GLU SEQRES 5 D 242 TRP ILE ALA VAL ILE THR VAL LYS SER ASP ASN TYR GLY SEQRES 6 D 242 ALA ASN TYR VAL GLU SER VAL LYS GLY ARG PHE ALA ILE SEQRES 7 D 242 SER ARG ASP ASP SER LYS SER SER VAL TYR LEU GLU MET SEQRES 8 D 242 ASN ARG LEU ARG GLU GLU ASP THR ALA THR TYR PHE CYS SEQRES 9 D 242 SER ARG SER GLY ILE TYR ASP GLY TYR TYR ALA TYR ALA SEQRES 10 D 242 MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SEQRES 11 D 242 SER ALA THR THR LYS GLY PRO SER VAL TYR PRO LEU ALA SEQRES 12 D 242 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU SEQRES 13 D 242 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR SEQRES 14 D 242 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS SEQRES 15 D 242 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SEQRES 16 D 242 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER SEQRES 17 D 242 GLN THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER SEQRES 18 D 242 THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS GLY SEQRES 19 D 242 THR LYS HIS HIS HIS HIS HIS HIS HET NAG E 1 14 HET NAG E 2 14 HET BMA E 3 11 HET FUC E 4 10 HET NAG F 1 14 HET NAG F 2 14 HET FUC F 3 10 HET NAG G 1 14 HET NAG G 2 14 HET BMA G 3 11 HET MAN G 4 11 HET NAG H 1 14 HET NAG H 2 14 HET BMA H 3 11 HET MAN H 4 11 HET MAN H 5 11 HET NAG I 1 14 HET NAG I 2 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 5 NAG 10(C8 H15 N O6) FORMUL 5 BMA 3(C6 H12 O6) FORMUL 5 FUC 2(C6 H12 O5) FORMUL 7 MAN 3(C6 H12 O6) FORMUL 10 HOH *175(H2 O) HELIX 1 AA1 SER A 76 ASN A 83 1 8 HELIX 2 AA2 HIS A 128 CYS A 135 5 8 HELIX 3 AA3 SER A 138 GLY A 153 1 16 HELIX 4 AA4 THR A 182 VAL A 184 5 3 HELIX 5 AA5 ASN A 185 TYR A 200 1 16 HELIX 6 AA6 ASP A 229 GLY A 240 1 12 HELIX 7 AA7 GLU B 273 LEU B 277 5 5 HELIX 8 AA8 GLY B 286 LYS B 292 1 7 HELIX 9 AA9 SER B 299 ILE B 315 1 17 HELIX 10 AB1 THR B 332 LEU B 336 5 5 HELIX 11 AB2 SER B 338 MET B 351 1 14 HELIX 12 AB3 ILE B 388 ASP B 390 5 3 HELIX 13 AB4 PHE B 391 SER B 412 1 22 HELIX 14 AB5 GLN C 79 LEU C 83 5 5 HELIX 15 AB6 SER C 121 SER C 127 1 7 HELIX 16 AB7 LYS C 183 HIS C 189 1 7 HELIX 17 AB8 THR D 31 TYR D 35 5 5 HELIX 18 AB9 VAL D 56 ASN D 60 5 5 HELIX 19 AC1 GLU D 67 LYS D 70 5 4 HELIX 20 AC2 ARG D 92 THR D 96 5 5 SHEET 1 AA1 4 PHE A 62 LYS A 63 0 SHEET 2 AA1 4 THR A 68 SER A 74 -1 O PHE A 70 N PHE A 62 SHEET 3 AA1 4 LYS B 360 HIS B 366 -1 O ASN B 365 N GLU A 69 SHEET 4 AA1 4 ARG B 376 CYS B 377 -1 O ARG B 376 N TRP B 362 SHEET 1 AA2 7 LEU A 90 THR A 93 0 SHEET 2 AA2 7 LEU A 99 GLY A 103 -1 O TYR A 100 N CYS A 92 SHEET 3 AA2 7 ALA A 106 ASP A 113 -1 O PHE A 108 N ILE A 101 SHEET 4 AA2 7 LEU A 214 PRO A 219 -1 O GLN A 218 N GLN A 109 SHEET 5 AA2 7 PHE A 175 VAL A 177 -1 N VAL A 177 O MET A 215 SHEET 6 AA2 7 PHE A 162 CYS A 164 -1 N LEU A 163 O GLN A 176 SHEET 7 AA2 7 VAL A 124 ILE A 126 -1 N ILE A 126 O PHE A 162 SHEET 1 AA3 2 TYR B 270 LEU B 272 0 SHEET 2 AA3 2 LYS B 283 PHE B 285 -1 O PHE B 285 N TYR B 270 SHEET 1 AA4 2 ILE B 380 LYS B 381 0 SHEET 2 AA4 2 SER B 384 TYR B 385 -1 O SER B 384 N LYS B 381 SHEET 1 AA5 4 MET C 4 THR C 5 0 SHEET 2 AA5 4 ARG C 18 ALA C 25 -1 O LYS C 24 N THR C 5 SHEET 3 AA5 4 ASP C 70 THR C 76 -1 O PHE C 71 N CYS C 23 SHEET 4 AA5 4 PHE C 62 GLY C 66 -1 N THR C 63 O THR C 74 SHEET 1 AA6 6 PHE C 10 THR C 13 0 SHEET 2 AA6 6 THR C 102 LEU C 106 1 O GLU C 105 N MET C 11 SHEET 3 AA6 6 ASP C 85 GLN C 90 -1 N TYR C 86 O THR C 102 SHEET 4 AA6 6 VAL C 33 GLN C 38 -1 N GLN C 38 O ASP C 85 SHEET 5 AA6 6 LYS C 45 TYR C 49 -1 O LYS C 45 N GLN C 37 SHEET 6 AA6 6 THR C 53 ARG C 54 -1 O THR C 53 N TYR C 49 SHEET 1 AA7 4 PHE C 10 THR C 13 0 SHEET 2 AA7 4 THR C 102 LEU C 106 1 O GLU C 105 N MET C 11 SHEET 3 AA7 4 ASP C 85 GLN C 90 -1 N TYR C 86 O THR C 102 SHEET 4 AA7 4 THR C 97 PHE C 98 -1 O THR C 97 N GLN C 90 SHEET 1 AA8 4 THR C 114 PHE C 118 0 SHEET 2 AA8 4 GLY C 129 PHE C 139 -1 O VAL C 133 N PHE C 118 SHEET 3 AA8 4 TYR C 173 THR C 182 -1 O LEU C 181 N ALA C 130 SHEET 4 AA8 4 VAL C 159 TRP C 163 -1 N SER C 162 O SER C 176 SHEET 1 AA9 4 SER C 153 ARG C 155 0 SHEET 2 AA9 4 ASN C 145 ILE C 150 -1 N ILE C 150 O SER C 153 SHEET 3 AA9 4 TYR C 192 HIS C 198 -1 O GLU C 195 N LYS C 147 SHEET 4 AA9 4 SER C 201 PHE C 209 -1 O LYS C 207 N CYS C 194 SHEET 1 AB1 4 GLN D 3 VAL D 8 0 SHEET 2 AB1 4 LEU D 21 SER D 28 -1 O SER D 24 N SER D 7 SHEET 3 AB1 4 SER D 83 MET D 88 -1 O LEU D 86 N LEU D 23 SHEET 4 AB1 4 PHE D 73 ASP D 78 -1 N ALA D 74 O GLU D 87 SHEET 1 AB2 6 LEU D 14 VAL D 15 0 SHEET 2 AB2 6 THR D 122 VAL D 126 1 O THR D 125 N VAL D 15 SHEET 3 AB2 6 ALA D 97 TYR D 107 -1 N TYR D 99 O THR D 122 SHEET 4 AB2 6 GLN D 36 GLN D 42 -1 N HIS D 38 O SER D 102 SHEET 5 AB2 6 GLU D 49 ILE D 54 -1 O GLU D 49 N ARG D 41 SHEET 6 AB2 6 ALA D 63 TYR D 65 -1 O ASN D 64 N VAL D 53 SHEET 1 AB3 4 LEU D 14 VAL D 15 0 SHEET 2 AB3 4 THR D 122 VAL D 126 1 O THR D 125 N VAL D 15 SHEET 3 AB3 4 ALA D 97 TYR D 107 -1 N TYR D 99 O THR D 122 SHEET 4 AB3 4 TYR D 110 TRP D 118 -1 O TYR D 110 N TYR D 107 SHEET 1 AB4 4 SER D 135 LEU D 139 0 SHEET 2 AB4 4 MET D 150 TYR D 160 -1 O LEU D 156 N TYR D 137 SHEET 3 AB4 4 LEU D 189 PRO D 199 -1 O TYR D 190 N TYR D 160 SHEET 4 AB4 4 VAL D 178 THR D 180 -1 N HIS D 179 O SER D 195 SHEET 1 AB5 4 SER D 135 LEU D 139 0 SHEET 2 AB5 4 MET D 150 TYR D 160 -1 O LEU D 156 N TYR D 137 SHEET 3 AB5 4 LEU D 189 PRO D 199 -1 O TYR D 190 N TYR D 160 SHEET 4 AB5 4 VAL D 184 GLN D 186 -1 N GLN D 186 O LEU D 189 SHEET 1 AB6 3 THR D 166 TRP D 169 0 SHEET 2 AB6 3 THR D 209 HIS D 214 -1 O ASN D 211 N THR D 168 SHEET 3 AB6 3 THR D 219 LYS D 224 -1 O LYS D 223 N CYS D 210 SSBOND 1 CYS A 88 CYS B 329 1555 1555 2.03 SSBOND 2 CYS A 92 CYS A 226 1555 1555 2.03 SSBOND 3 CYS A 135 CYS A 164 1555 1555 2.03 SSBOND 4 CYS A 207 CYS A 213 1555 1555 2.04 SSBOND 5 CYS B 271 CYS B 284 1555 1555 2.04 SSBOND 6 CYS B 293 CYS B 302 1555 1555 2.04 SSBOND 7 CYS B 356 CYS B 377 1555 1555 2.03 SSBOND 8 CYS C 23 CYS C 88 1555 1555 2.04 SSBOND 9 CYS C 134 CYS C 194 1555 1555 2.03 SSBOND 10 CYS D 25 CYS D 101 1555 1555 2.04 SSBOND 11 CYS D 155 CYS D 210 1555 1555 2.03 LINK ND2 ASN A 95 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN A 166 C1 NAG F 1 1555 1555 1.44 LINK ND2 ASN A 178 C1 NAG G 1 1555 1555 1.45 LINK ND2 ASN B 357 C1 NAG H 1 1555 1555 1.44 LINK ND2 ASN B 365 C1 NAG I 1 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45 LINK O6 NAG E 1 C1 FUC E 4 1555 1555 1.44 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.45 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45 LINK O6 NAG F 1 C1 FUC F 3 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44 LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.45 LINK O3 BMA G 3 C1 MAN G 4 1555 1555 1.46 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.45 LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.45 LINK O3 BMA H 3 C1 MAN H 4 1555 1555 1.45 LINK O6 BMA H 3 C1 MAN H 5 1555 1555 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 CISPEP 1 TYR C 94 PRO C 95 0 -2.74 CISPEP 2 TYR C 140 PRO C 141 0 -0.25 CISPEP 3 PHE D 161 PRO D 162 0 -1.72 CISPEP 4 GLU D 163 PRO D 164 0 1.68 CISPEP 5 TRP D 203 PRO D 204 0 0.47 CRYST1 226.468 73.030 80.734 90.00 95.78 90.00 C 1 2 1 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.004416 0.000000 0.000447 0.00000 SCALE2 0.000000 0.013693 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012450 0.00000