HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 21-DEC-12 4IJ3 TITLE OXIDOREDUCTASE FRAGMENT OF HUMAN QSOX1 IN COMPLEX WITH A FAB FRAGMENT TITLE 2 FROM AN ANTI- HUMAN QSOX1 ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: SULFHYDRYL OXIDASE 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: OXIDOREDUCTASE FRAGMENT, UNP RESIDUES 33-272; COMPND 5 SYNONYM: HQSOX, QUIESCIN Q6; COMPND 6 EC: 1.8.3.2; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: LIGHT CHAIN OF FAB FRAGMENT; COMPND 10 CHAIN: B; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: HEAVY CHAIN OF FAB FRAGMENT; COMPND 14 CHAIN: C; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: HSQSOX1, QSCN6, QSOX1, UNQ2520/PRO6013; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 13 ORGANISM_COMMON: MOUSE; SOURCE 14 ORGANISM_TAXID: 10090; SOURCE 15 CELL: HYBRIDOMA; SOURCE 16 MOL_ID: 3; SOURCE 17 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 18 ORGANISM_COMMON: MOUSE; SOURCE 19 ORGANISM_TAXID: 10090; SOURCE 20 CELL: HYBRIDOMA KEYWDS INHIBITOR, ANTIBODY BINDING, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR KEYWDS 2 COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR D.FASS,I.GROSSMAN REVDAT 1 06-NOV-13 4IJ3 0 JRNL AUTH I.GROSSMAN,A.ALON,T.ILANI,D.FASS JRNL TITL AN INHIBITORY ANTIBODY BLOCKS THE FIRST STEP IN THE JRNL TITL 2 DITHIOL/DISULFIDE RELAY MECHANISM OF THE ENZYME QSOX1. JRNL REF J.MOL.BIOL. V. 425 4366 2013 JRNL REFN ISSN 0022-2836 JRNL PMID 23867277 JRNL DOI 10.1016/J.JMB.2013.07.011 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.9 REMARK 3 NUMBER OF REFLECTIONS : 37341 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.202 REMARK 3 FREE R VALUE : 0.237 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2622 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.3951 REMARK 3 BIN FREE R VALUE : 0.5492 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 23 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5154 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 10 REMARK 3 SOLVENT ATOMS : 350 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 55.29 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : 1.44 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4IJ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JAN-13. REMARK 100 THE RCSB ID CODE IS RCSB076815. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-FEB-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : OSMIC MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++ REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37560 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 200 DATA REDUNDANCY : 5.100 REMARK 200 R MERGE (I) : 0.09200 REMARK 200 R SYM (I) : 0.09200 REMARK 200 FOR THE DATA SET : 14.3500 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 3.80 REMARK 200 R MERGE FOR SHELL (I) : 0.36300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.960 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: 3Q6O, 3OKD REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.47 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 19% W/V PEG 4000, 0.4 M AMMONIUM REMARK 280 PHOSPHATE DIBASIC, PH 8, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+5/6 REMARK 290 6555 X-Y,X,Z+1/6 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 18.42167 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.84333 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 27.63250 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 46.05417 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 9.21083 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5840 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 29690 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 GLY A 29 REMARK 465 SER A 30 REMARK 465 HIS A 31 REMARK 465 MET A 32 REMARK 465 SER A 33 REMARK 465 ALA A 34 REMARK 465 GLU A 272 REMARK 465 GLY C 221 REMARK 465 CYS C 222 REMARK 465 LYS C 223 REMARK 465 PRO C 224 REMARK 465 CYS C 225 REMARK 465 ILE C 226 REMARK 465 CYS C 227 REMARK 465 THR C 228 REMARK 465 VAL C 229 REMARK 465 PRO C 230 REMARK 465 GLU C 231 REMARK 465 VAL C 232 REMARK 465 SER C 233 REMARK 465 SER C 234 REMARK 465 VAL C 235 REMARK 465 PHE C 236 REMARK 465 ILE C 237 REMARK 465 PHE C 238 REMARK 465 PRO C 239 REMARK 465 PRO C 240 REMARK 465 LYS C 241 REMARK 465 PRO C 242 REMARK 465 LYS C 243 REMARK 465 ASP C 244 REMARK 465 VAL C 245 REMARK 465 LEU C 246 REMARK 465 THR C 247 REMARK 465 ILE C 248 REMARK 465 THR C 249 REMARK 465 LEU C 250 REMARK 465 THR C 251 REMARK 465 PRO C 252 REMARK 465 LYS C 253 REMARK 465 VAL C 254 REMARK 465 THR C 255 REMARK 465 CYS C 256 REMARK 465 VAL C 257 REMARK 465 VAL C 258 REMARK 465 VAL C 259 REMARK 465 ASP C 260 REMARK 465 ILE C 261 REMARK 465 SER C 262 REMARK 465 LYS C 263 REMARK 465 ASP C 264 REMARK 465 ASP C 265 REMARK 465 PRO C 266 REMARK 465 GLU C 267 REMARK 465 VAL C 268 REMARK 465 GLN C 269 REMARK 465 PHE C 270 REMARK 465 SER C 271 REMARK 465 TRP C 272 REMARK 465 PHE C 273 REMARK 465 VAL C 274 REMARK 465 ASP C 275 REMARK 465 ASP C 276 REMARK 465 VAL C 277 REMARK 465 GLU C 278 REMARK 465 VAL C 279 REMARK 465 HIS C 280 REMARK 465 THR C 281 REMARK 465 ALA C 282 REMARK 465 GLN C 283 REMARK 465 THR C 284 REMARK 465 GLN C 285 REMARK 465 PRO C 286 REMARK 465 ARG C 287 REMARK 465 GLU C 288 REMARK 465 GLU C 289 REMARK 465 GLN C 290 REMARK 465 PHE C 291 REMARK 465 ASN C 292 REMARK 465 SER C 293 REMARK 465 THR C 294 REMARK 465 PHE C 295 REMARK 465 ARG C 296 REMARK 465 SER C 297 REMARK 465 VAL C 298 REMARK 465 SER C 299 REMARK 465 GLU C 300 REMARK 465 LEU C 301 REMARK 465 PRO C 302 REMARK 465 ILE C 303 REMARK 465 MET C 304 REMARK 465 HIS C 305 REMARK 465 GLN C 306 REMARK 465 ASP C 307 REMARK 465 TRP C 308 REMARK 465 LEU C 309 REMARK 465 ASN C 310 REMARK 465 GLY C 311 REMARK 465 LYS C 312 REMARK 465 GLU C 313 REMARK 465 PHE C 314 REMARK 465 LYS C 315 REMARK 465 CYS C 316 REMARK 465 ARG C 317 REMARK 465 VAL C 318 REMARK 465 ASN C 319 REMARK 465 SER C 320 REMARK 465 ALA C 321 REMARK 465 ALA C 322 REMARK 465 PHE C 323 REMARK 465 PRO C 324 REMARK 465 ALA C 325 REMARK 465 PRO C 326 REMARK 465 ILE C 327 REMARK 465 GLU C 328 REMARK 465 LYS C 329 REMARK 465 THR C 330 REMARK 465 ILE C 331 REMARK 465 SER C 332 REMARK 465 LYS C 333 REMARK 465 THR C 334 REMARK 465 LYS C 335 REMARK 465 GLY C 336 REMARK 465 ARG C 337 REMARK 465 PRO C 338 REMARK 465 LYS C 339 REMARK 465 ALA C 340 REMARK 465 PRO C 341 REMARK 465 GLN C 342 REMARK 465 VAL C 343 REMARK 465 TYR C 344 REMARK 465 THR C 345 REMARK 465 ILE C 346 REMARK 465 PRO C 347 REMARK 465 PRO C 348 REMARK 465 PRO C 349 REMARK 465 LYS C 350 REMARK 465 GLU C 351 REMARK 465 GLN C 352 REMARK 465 MET C 353 REMARK 465 ALA C 354 REMARK 465 LYS C 355 REMARK 465 ASP C 356 REMARK 465 LYS C 357 REMARK 465 VAL C 358 REMARK 465 SER C 359 REMARK 465 LEU C 360 REMARK 465 THR C 361 REMARK 465 CYS C 362 REMARK 465 MET C 363 REMARK 465 ILE C 364 REMARK 465 THR C 365 REMARK 465 ASP C 366 REMARK 465 PHE C 367 REMARK 465 PHE C 368 REMARK 465 PRO C 369 REMARK 465 GLU C 370 REMARK 465 ASP C 371 REMARK 465 ILE C 372 REMARK 465 THR C 373 REMARK 465 VAL C 374 REMARK 465 GLU C 375 REMARK 465 TRP C 376 REMARK 465 GLN C 377 REMARK 465 TRP C 378 REMARK 465 ASN C 379 REMARK 465 GLY C 380 REMARK 465 GLN C 381 REMARK 465 PRO C 382 REMARK 465 ALA C 383 REMARK 465 GLU C 384 REMARK 465 ASN C 385 REMARK 465 TYR C 386 REMARK 465 LYS C 387 REMARK 465 ASN C 388 REMARK 465 THR C 389 REMARK 465 GLN C 390 REMARK 465 PRO C 391 REMARK 465 ILE C 392 REMARK 465 MET C 393 REMARK 465 ASN C 394 REMARK 465 THR C 395 REMARK 465 ASN C 396 REMARK 465 GLY C 397 REMARK 465 SER C 398 REMARK 465 TYR C 399 REMARK 465 PHE C 400 REMARK 465 VAL C 401 REMARK 465 TYR C 402 REMARK 465 SER C 403 REMARK 465 LYS C 404 REMARK 465 LEU C 405 REMARK 465 ASN C 406 REMARK 465 VAL C 407 REMARK 465 GLN C 408 REMARK 465 LYS C 409 REMARK 465 SER C 410 REMARK 465 ASN C 411 REMARK 465 TRP C 412 REMARK 465 GLU C 413 REMARK 465 ALA C 414 REMARK 465 GLY C 415 REMARK 465 ASN C 416 REMARK 465 THR C 417 REMARK 465 PHE C 418 REMARK 465 THR C 419 REMARK 465 CYS C 420 REMARK 465 SER C 421 REMARK 465 VAL C 422 REMARK 465 LEU C 423 REMARK 465 HIS C 424 REMARK 465 GLU C 425 REMARK 465 GLY C 426 REMARK 465 LEU C 427 REMARK 465 HIS C 428 REMARK 465 ASN C 429 REMARK 465 HIS C 430 REMARK 465 HIS C 431 REMARK 465 THR C 432 REMARK 465 GLU C 433 REMARK 465 LYS C 434 REMARK 465 SER C 435 REMARK 465 LEU C 436 REMARK 465 SER C 437 REMARK 465 HIS C 438 REMARK 465 SER C 439 REMARK 465 PRO C 440 REMARK 465 GLY C 441 REMARK 465 LYS C 442 REMARK 465 GLN C 443 REMARK 465 LEU C 444 REMARK 465 ASP C 445 REMARK 465 GLU C 446 REMARK 465 THR C 447 REMARK 465 CYS C 448 REMARK 465 ALA C 449 REMARK 465 GLU C 450 REMARK 465 ALA C 451 REMARK 465 GLN C 452 REMARK 465 ASP C 453 REMARK 465 GLY C 454 REMARK 465 GLU C 455 REMARK 465 LEU C 456 REMARK 465 ASP C 457 REMARK 465 GLY C 458 REMARK 465 LEU C 459 REMARK 465 TRP C 460 REMARK 465 THR C 461 REMARK 465 THR C 462 REMARK 465 ILE C 463 REMARK 465 THR C 464 REMARK 465 ILE C 465 REMARK 465 PHE C 466 REMARK 465 ILE C 467 REMARK 465 SER C 468 REMARK 465 LEU C 469 REMARK 465 PHE C 470 REMARK 465 LEU C 471 REMARK 465 LEU C 472 REMARK 465 SER C 473 REMARK 465 VAL C 474 REMARK 465 CYS C 475 REMARK 465 TYR C 476 REMARK 465 SER C 477 REMARK 465 ALA C 478 REMARK 465 ALA C 479 REMARK 465 VAL C 480 REMARK 465 THR C 481 REMARK 465 LEU C 482 REMARK 465 PHE C 483 REMARK 465 LYS C 484 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ARG A 271 CG CD NE CZ NH1 NH2 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 PRO A 41 30.53 -77.32 REMARK 500 ASN A 114 76.24 60.95 REMARK 500 ASN A 130 -166.72 -172.44 REMARK 500 ASP A 159 -115.88 -94.54 REMARK 500 ALA A 223 -59.75 -29.20 REMARK 500 SER A 267 -74.26 -39.91 REMARK 500 SER B 30 -132.10 62.45 REMARK 500 ALA B 51 -43.40 71.57 REMARK 500 THR B 69 -18.21 -142.43 REMARK 500 ALA B 84 -173.45 177.41 REMARK 500 SER B 201 146.12 -170.31 REMARK 500 SER C 15 12.23 50.51 REMARK 500 PRO C 41 129.20 -32.75 REMARK 500 LYS C 43 -165.56 -118.38 REMARK 500 ASP C 88 0.10 -66.12 REMARK 500 ALA C 134 53.48 -115.37 REMARK 500 ASP C 178 11.80 57.25 REMARK 500 LYS C 210 109.90 -169.70 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 301 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3Q6O RELATED DB: PDB REMARK 900 OXIDOREDUCTASE FRAGMENT OF HUMAN QSOX1 DBREF 4IJ3 A 33 272 UNP O00391 QSOX1_HUMAN 33 272 DBREF 4IJ3 B 1 214 PDB 4IJ3 4IJ3 1 214 DBREF 4IJ3 C 1 484 PDB 4IJ3 4IJ3 1 484 SEQADV 4IJ3 GLY A 29 UNP O00391 EXPRESSION TAG SEQADV 4IJ3 SER A 30 UNP O00391 EXPRESSION TAG SEQADV 4IJ3 HIS A 31 UNP O00391 EXPRESSION TAG SEQADV 4IJ3 MET A 32 UNP O00391 EXPRESSION TAG SEQRES 1 A 244 GLY SER HIS MET SER ALA LEU TYR SER PRO SER ASP PRO SEQRES 2 A 244 LEU THR LEU LEU GLN ALA ASP THR VAL ARG GLY ALA VAL SEQRES 3 A 244 LEU GLY SER ARG SER ALA TRP ALA VAL GLU PHE PHE ALA SEQRES 4 A 244 SER TRP CYS GLY HIS CYS ILE ALA PHE ALA PRO THR TRP SEQRES 5 A 244 LYS ALA LEU ALA GLU ASP VAL LYS ALA TRP ARG PRO ALA SEQRES 6 A 244 LEU TYR LEU ALA ALA LEU ASP CYS ALA GLU GLU THR ASN SEQRES 7 A 244 SER ALA VAL CYS ARG ASP PHE ASN ILE PRO GLY PHE PRO SEQRES 8 A 244 THR VAL ARG PHE PHE LYS ALA PHE THR LYS ASN GLY SER SEQRES 9 A 244 GLY ALA VAL PHE PRO VAL ALA GLY ALA ASP VAL GLN THR SEQRES 10 A 244 LEU ARG GLU ARG LEU ILE ASP ALA LEU GLU SER HIS HIS SEQRES 11 A 244 ASP THR TRP PRO PRO ALA CYS PRO PRO LEU GLU PRO ALA SEQRES 12 A 244 LYS LEU GLU GLU ILE ASP GLY PHE PHE ALA ARG ASN ASN SEQRES 13 A 244 GLU GLU TYR LEU ALA LEU ILE PHE GLU LYS GLY GLY SER SEQRES 14 A 244 TYR LEU GLY ARG GLU VAL ALA LEU ASP LEU SER GLN HIS SEQRES 15 A 244 LYS GLY VAL ALA VAL ARG ARG VAL LEU ASN THR GLU ALA SEQRES 16 A 244 ASN VAL VAL ARG LYS PHE GLY VAL THR ASP PHE PRO SER SEQRES 17 A 244 CYS TYR LEU LEU PHE ARG ASN GLY SER VAL SER ARG VAL SEQRES 18 A 244 PRO VAL LEU MET GLU SER ARG SER PHE TYR THR ALA TYR SEQRES 19 A 244 LEU GLN ARG LEU SER GLY LEU THR ARG GLU SEQRES 1 B 214 ASP VAL VAL MET THR GLN SER HIS LYS PHE MET SER THR SEQRES 2 B 214 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 B 214 GLN ASP VAL SER THR ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 B 214 SER GLY GLN SER PRO LYS LEU LEU ILE HIS SER ALA SER SEQRES 5 B 214 TYR ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 B 214 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER VAL SEQRES 7 B 214 GLN ALA GLU ASP LEU ALA VAL TYR TYR CYS GLN GLN HIS SEQRES 8 B 214 TYR SER ILE PRO LEU THR PHE GLY ALA GLY THR LYS LEU SEQRES 9 B 214 GLU LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 B 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 B 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 B 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 B 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 B 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 B 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 B 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 B 214 PHE ASN ARG ASN GLU CYS SEQRES 1 C 484 GLN VAL GLN LEU LYS GLN SER GLY PRO GLY LEU VAL ALA SEQRES 2 C 484 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY SEQRES 3 C 484 PHE SER LEU THR GLY TYR GLY VAL ASN TRP VAL ARG GLN SEQRES 4 C 484 SER PRO GLY LYS GLY LEU GLU TRP LEU GLY MET ILE TRP SEQRES 5 C 484 GLY ASP GLY ARG THR ASP TYR LYS SER ALA LEU LYS SER SEQRES 6 C 484 ARG LEU SER ILE THR LYS ASP ASN SER LYS SER GLN VAL SEQRES 7 C 484 PHE LEU LYS MET ASN SER LEU GLN THR ASP ASP THR ALA SEQRES 8 C 484 ARG TYR PHE CYS ALA SER ASP TYR TYR GLY SER GLY SER SEQRES 9 C 484 PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 C 484 ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA SEQRES 11 C 484 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU SEQRES 12 C 484 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR SEQRES 13 C 484 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS SEQRES 14 C 484 THR PHE PRO ALA VAL LEU GLU SER ASP LEU TYR THR LEU SEQRES 15 C 484 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER SEQRES 16 C 484 GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER SEQRES 17 C 484 THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS GLY SEQRES 18 C 484 CYS LYS PRO CYS ILE CYS THR VAL PRO GLU VAL SER SER SEQRES 19 C 484 VAL PHE ILE PHE PRO PRO LYS PRO LYS ASP VAL LEU THR SEQRES 20 C 484 ILE THR LEU THR PRO LYS VAL THR CYS VAL VAL VAL ASP SEQRES 21 C 484 ILE SER LYS ASP ASP PRO GLU VAL GLN PHE SER TRP PHE SEQRES 22 C 484 VAL ASP ASP VAL GLU VAL HIS THR ALA GLN THR GLN PRO SEQRES 23 C 484 ARG GLU GLU GLN PHE ASN SER THR PHE ARG SER VAL SER SEQRES 24 C 484 GLU LEU PRO ILE MET HIS GLN ASP TRP LEU ASN GLY LYS SEQRES 25 C 484 GLU PHE LYS CYS ARG VAL ASN SER ALA ALA PHE PRO ALA SEQRES 26 C 484 PRO ILE GLU LYS THR ILE SER LYS THR LYS GLY ARG PRO SEQRES 27 C 484 LYS ALA PRO GLN VAL TYR THR ILE PRO PRO PRO LYS GLU SEQRES 28 C 484 GLN MET ALA LYS ASP LYS VAL SER LEU THR CYS MET ILE SEQRES 29 C 484 THR ASP PHE PHE PRO GLU ASP ILE THR VAL GLU TRP GLN SEQRES 30 C 484 TRP ASN GLY GLN PRO ALA GLU ASN TYR LYS ASN THR GLN SEQRES 31 C 484 PRO ILE MET ASN THR ASN GLY SER TYR PHE VAL TYR SER SEQRES 32 C 484 LYS LEU ASN VAL GLN LYS SER ASN TRP GLU ALA GLY ASN SEQRES 33 C 484 THR PHE THR CYS SER VAL LEU HIS GLU GLY LEU HIS ASN SEQRES 34 C 484 HIS HIS THR GLU LYS SER LEU SER HIS SER PRO GLY LYS SEQRES 35 C 484 GLN LEU ASP GLU THR CYS ALA GLU ALA GLN ASP GLY GLU SEQRES 36 C 484 LEU ASP GLY LEU TRP THR THR ILE THR ILE PHE ILE SER SEQRES 37 C 484 LEU PHE LEU LEU SER VAL CYS TYR SER ALA ALA VAL THR SEQRES 38 C 484 LEU PHE LYS HET PO4 A 301 5 HET PO4 B 301 5 HETNAM PO4 PHOSPHATE ION FORMUL 4 PO4 2(O4 P 3-) FORMUL 6 HOH *350(H2 O) HELIX 1 1 THR A 49 LEU A 55 1 7 HELIX 2 2 CYS A 70 VAL A 87 1 18 HELIX 3 3 LYS A 88 ARG A 91 5 4 HELIX 4 4 GLU A 103 THR A 105 5 3 HELIX 5 5 ASN A 106 ASN A 114 1 9 HELIX 6 6 ASP A 142 SER A 156 1 15 HELIX 7 7 LYS A 172 GLY A 178 1 7 HELIX 8 8 GLY A 178 ASN A 183 1 6 HELIX 9 9 TYR A 198 LEU A 207 1 10 HELIX 10 10 GLU A 222 PHE A 229 1 8 HELIX 11 11 SER A 255 ARG A 265 1 11 HELIX 12 12 GLN B 79 LEU B 83 5 5 HELIX 13 13 SER B 121 THR B 126 1 6 HELIX 14 14 LYS B 183 GLU B 187 1 5 HELIX 15 15 ASN B 212 CYS B 214 5 3 HELIX 16 16 SER C 61 LYS C 64 5 4 HELIX 17 17 GLN C 86 THR C 90 5 5 HELIX 18 18 PRO C 205 SER C 208 5 4 SHEET 1 A 5 THR A 43 LEU A 45 0 SHEET 2 A 5 LEU A 94 ASP A 100 1 O ALA A 98 N LEU A 45 SHEET 3 A 5 ALA A 60 PHE A 66 1 N ALA A 62 O ALA A 97 SHEET 4 A 5 THR A 120 PHE A 124 -1 O PHE A 124 N TRP A 61 SHEET 5 A 5 ALA A 134 PHE A 136 -1 O ALA A 134 N PHE A 123 SHEET 1 B 4 VAL A 213 LEU A 219 0 SHEET 2 B 4 TYR A 187 GLU A 193 1 N ALA A 189 O ALA A 214 SHEET 3 B 4 SER A 236 PHE A 241 -1 O TYR A 238 N LEU A 190 SHEET 4 B 4 VAL A 246 ARG A 248 -1 O SER A 247 N LEU A 239 SHEET 1 C 4 MET B 4 THR B 5 0 SHEET 2 C 4 VAL B 19 ALA B 25 -1 O LYS B 24 N THR B 5 SHEET 3 C 4 ASP B 70 ILE B 75 -1 O PHE B 73 N ILE B 21 SHEET 4 C 4 PHE B 62 GLY B 66 -1 N THR B 63 O THR B 74 SHEET 1 D 6 PHE B 10 THR B 13 0 SHEET 2 D 6 THR B 102 LEU B 106 1 O GLU B 105 N THR B 13 SHEET 3 D 6 VAL B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 D 6 VAL B 33 GLN B 38 -1 N ALA B 34 O GLN B 89 SHEET 5 D 6 LYS B 45 HIS B 49 -1 O ILE B 48 N TRP B 35 SHEET 6 D 6 TYR B 53 ARG B 54 -1 O TYR B 53 N HIS B 49 SHEET 1 E 4 PHE B 10 THR B 13 0 SHEET 2 E 4 THR B 102 LEU B 106 1 O GLU B 105 N THR B 13 SHEET 3 E 4 VAL B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 E 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 F 4 THR B 114 PHE B 118 0 SHEET 2 F 4 GLY B 129 PHE B 139 -1 O VAL B 133 N PHE B 118 SHEET 3 F 4 TYR B 173 THR B 182 -1 O LEU B 181 N ALA B 130 SHEET 4 F 4 VAL B 159 TRP B 163 -1 N SER B 162 O SER B 176 SHEET 1 G 4 SER B 153 ARG B 155 0 SHEET 2 G 4 ASN B 145 ILE B 150 -1 N TRP B 148 O ARG B 155 SHEET 3 G 4 SER B 191 HIS B 198 -1 O GLU B 195 N LYS B 147 SHEET 4 G 4 SER B 201 ASN B 210 -1 O LYS B 207 N CYS B 194 SHEET 1 H 4 GLN C 3 SER C 7 0 SHEET 2 H 4 LEU C 18 SER C 25 -1 O THR C 21 N SER C 7 SHEET 3 H 4 GLN C 77 MET C 82 -1 O MET C 82 N LEU C 18 SHEET 4 H 4 LEU C 67 ASP C 72 -1 N THR C 70 O PHE C 79 SHEET 1 I 6 LEU C 11 VAL C 12 0 SHEET 2 I 6 THR C 112 VAL C 116 1 O THR C 115 N VAL C 12 SHEET 3 I 6 ALA C 91 ASP C 98 -1 N ALA C 91 O VAL C 114 SHEET 4 I 6 VAL C 34 GLN C 39 -1 N VAL C 37 O PHE C 94 SHEET 5 I 6 LEU C 45 ILE C 51 -1 O LEU C 48 N TRP C 36 SHEET 6 I 6 THR C 57 TYR C 59 -1 O ASP C 58 N MET C 50 SHEET 1 J 4 LEU C 11 VAL C 12 0 SHEET 2 J 4 THR C 112 VAL C 116 1 O THR C 115 N VAL C 12 SHEET 3 J 4 ALA C 91 ASP C 98 -1 N ALA C 91 O VAL C 114 SHEET 4 J 4 PHE C 105 TRP C 108 -1 O TYR C 107 N SER C 97 SHEET 1 K 4 SER C 125 LEU C 129 0 SHEET 2 K 4 MET C 140 TYR C 150 -1 O GLY C 144 N LEU C 129 SHEET 3 K 4 LEU C 179 PRO C 189 -1 O VAL C 188 N VAL C 141 SHEET 4 K 4 VAL C 168 THR C 170 -1 N HIS C 169 O SER C 185 SHEET 1 L 4 SER C 125 LEU C 129 0 SHEET 2 L 4 MET C 140 TYR C 150 -1 O GLY C 144 N LEU C 129 SHEET 3 L 4 LEU C 179 PRO C 189 -1 O VAL C 188 N VAL C 141 SHEET 4 L 4 VAL C 174 GLU C 176 -1 N GLU C 176 O LEU C 179 SHEET 1 M 3 THR C 156 TRP C 159 0 SHEET 2 M 3 THR C 199 HIS C 204 -1 O ASN C 201 N THR C 158 SHEET 3 M 3 THR C 209 LYS C 214 -1 O VAL C 211 N VAL C 202 SSBOND 1 CYS A 70 CYS A 73 1555 1555 2.06 SSBOND 2 CYS A 101 CYS A 110 1555 1555 2.03 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.02 SSBOND 4 CYS B 134 CYS B 194 1555 1555 2.03 SSBOND 5 CYS B 214 CYS C 220 1555 1555 2.04 SSBOND 6 CYS C 22 CYS C 95 1555 1555 2.04 SSBOND 7 CYS C 145 CYS C 200 1555 1555 2.03 CISPEP 1 ARG A 91 PRO A 92 0 0.16 CISPEP 2 PHE A 118 PRO A 119 0 -0.19 CISPEP 3 PHE A 234 PRO A 235 0 0.15 CISPEP 4 ILE B 94 PRO B 95 0 0.37 CISPEP 5 TYR B 140 PRO B 141 0 0.23 CISPEP 6 PHE C 151 PRO C 152 0 -0.23 CISPEP 7 GLU C 153 PRO C 154 0 -6.77 CISPEP 8 TRP C 193 PRO C 194 0 0.13 SITE 1 AC1 9 SER A 57 ARG A 58 HOH A 426 HOH A 428 SITE 2 AC1 9 HOH A 429 HOH A 527 HOH A 528 HOH A 530 SITE 3 AC1 9 LYS C 214 SITE 1 AC2 3 GLU B 185 ARG B 188 HIS B 189 CRYST1 209.311 209.311 55.265 90.00 90.00 120.00 P 61 6 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 0.004778 0.002758 0.000000 0.00000 SCALE2 0.000000 0.005517 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018095 0.00000