HEADER TRANSFERASE 31-MAR-06 2GK9
TITLE HUMAN PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE, TYPE II, GAMMA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE, TYPE II, GAMMA;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 2.7.1.68;
COMPND 5 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: PIP5K2C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4
KEYWDS PHOSPHOINOSITIDE, KINASE, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS
KEYWDS 2 CONSORTIUM, SGC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.UPPENBERG,M.HOGBOM,D.OGG,C.ARROWSMITH,H.BERGLUND,R.COLLINS,M.EHN,
AUTHOR 2 S.FLODIN,A.FLORES,S.GRASLUND,L.HOLMBERG-SCHIAVONE,A.EDWARDS,
AUTHOR 3 M.HAMMARSTROM,T.KOTENYOVA,P.NILSSON-EHLE,P.NORDLUND,T.NYMAN,
AUTHOR 4 C.PERSSON,J.SAGEMARK,P.STENMARK,M.SUNDSTROM,A.G.THORSELL,S.VAN DEN
AUTHOR 5 BERG,J.WEIGELT,B.M.HALLBERG,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 6 14-FEB-24 2GK9 1 SHEET
REVDAT 5 18-OCT-17 2GK9 1 REMARK
REVDAT 4 24-FEB-09 2GK9 1 VERSN
REVDAT 3 17-APR-07 2GK9 1 SEQRES SEQADV DBREF
REVDAT 2 09-MAY-06 2GK9 1 REMARK
REVDAT 1 02-MAY-06 2GK9 0
JRNL AUTH A.G.THORSELL,J.UPPENBERG,M.HOGBOM,D.OGG,C.ARROWSMITH,
JRNL AUTH 2 H.BERGLUND,R.COLLINS,A.EDWARDS,M.EHN,S.FLODIN,A.FLORES,
JRNL AUTH 3 S.GRASLUND,M.HAMMARSTROM,T.KOTENYOVA,P.NILSSON-EHLE,
JRNL AUTH 4 P.NORDLUND,T.NYMAN,J.SAGEMARK,P.STENMARK,M.SUNDSTROM,
JRNL AUTH 5 S.VAN DEN BERG,J.WEIGELT,L.HOLMBERG-SCHIAVONE,C.PERSSON,
JRNL AUTH 6 B.M.HALLBERG
JRNL TITL STRUCTURE OF HUMAN PHOSPHATIDYLINOSITOL-4-PHOSPHATE
JRNL TITL 2 5-KINASE, TYPE II, GAMMA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 CROSS-VALIDATION METHOD : RFREE
REMARK 3 FREE R VALUE TEST SET SELECTION : NO TWIN REFLECTIONS
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.261
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.261
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.297
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1890
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 39963
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8233
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 ANGLE DISTANCES (A) : NULL
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NO TWIN REFLECTIONS IN SAME SET. TWIN
REMARK 3 OPERATOR= H,-K,-L ; AND TWIN FRACTION = 0.50
REMARK 4
REMARK 4 2GK9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037222.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.953
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40823
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 2.550
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07910
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.2300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.18
REMARK 200 R MERGE FOR SHELL (I) : 0.66300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.130
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG3350 0.3 M DI
REMARK 280 -AMMONIUMTARTRATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 273K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 94.55500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 141.83250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 47.27750
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SER A 30
REMARK 465 MET A 31
REMARK 465 HIS A 32
REMARK 465 PHE A 33
REMARK 465 VAL A 34
REMARK 465 GLN A 35
REMARK 465 GLN A 36
REMARK 465 LYS A 37
REMARK 465 VAL A 38
REMARK 465 LYS A 39
REMARK 465 VAL A 40
REMARK 465 PHE A 41
REMARK 465 ARG A 42
REMARK 465 ALA A 43
REMARK 465 ALA A 44
REMARK 465 GLY A 136
REMARK 465 SER A 137
REMARK 465 ASP A 138
REMARK 465 GLY A 139
REMARK 465 ARG A 140
REMARK 465 SER A 222
REMARK 465 LEU A 223
REMARK 465 VAL A 224
REMARK 465 SER A 225
REMARK 465 ARG A 226
REMARK 465 GLU A 227
REMARK 465 ALA A 228
REMARK 465 SER A 229
REMARK 465 ASP A 230
REMARK 465 LYS A 231
REMARK 465 GLU A 232
REMARK 465 LYS A 233
REMARK 465 VAL A 234
REMARK 465 LYS A 235
REMARK 465 GLU A 236
REMARK 465 LEU A 237
REMARK 465 PRO A 238
REMARK 465 PHE A 245
REMARK 465 LEU A 246
REMARK 465 GLY A 255
REMARK 465 GLU A 256
REMARK 465 GLU A 257
REMARK 465 GLU A 258
REMARK 465 ILE A 291
REMARK 465 ARG A 292
REMARK 465 GLY A 293
REMARK 465 SER A 294
REMARK 465 GLU A 295
REMARK 465 PRO A 296
REMARK 465 GLU A 297
REMARK 465 GLU A 298
REMARK 465 GLU A 299
REMARK 465 ALA A 300
REMARK 465 PRO A 301
REMARK 465 VAL A 302
REMARK 465 ARG A 303
REMARK 465 GLU A 304
REMARK 465 ASP A 305
REMARK 465 GLU A 306
REMARK 465 SER A 307
REMARK 465 GLU A 308
REMARK 465 VAL A 309
REMARK 465 ASP A 310
REMARK 465 GLY A 311
REMARK 465 ASP A 312
REMARK 465 CYS A 313
REMARK 465 SER A 314
REMARK 465 LEU A 315
REMARK 465 THR A 316
REMARK 465 GLY A 317
REMARK 465 PRO A 318
REMARK 465 PRO A 319
REMARK 465 ALA A 320
REMARK 465 LEU A 321
REMARK 465 VAL A 322
REMARK 465 GLY A 323
REMARK 465 SER A 324
REMARK 465 TYR A 325
REMARK 465 GLY A 326
REMARK 465 THR A 327
REMARK 465 SER A 328
REMARK 465 PRO A 329
REMARK 465 GLU A 330
REMARK 465 GLY A 331
REMARK 465 ILE A 332
REMARK 465 GLY A 333
REMARK 465 GLY A 334
REMARK 465 TYR A 335
REMARK 465 ILE A 336
REMARK 465 HIS A 337
REMARK 465 SER A 338
REMARK 465 HIS A 339
REMARK 465 ARG A 340
REMARK 465 PRO A 341
REMARK 465 LEU A 342
REMARK 465 GLY A 343
REMARK 465 PRO A 344
REMARK 465 GLY A 345
REMARK 465 GLU A 346
REMARK 465 PHE A 347
REMARK 465 GLU A 348
REMARK 465 SER A 349
REMARK 465 PHE A 350
REMARK 465 ILE A 351
REMARK 465 ASP A 352
REMARK 465 VAL A 353
REMARK 465 TYR A 354
REMARK 465 ALA A 355
REMARK 465 ILE A 356
REMARK 465 ARG A 357
REMARK 465 SER A 358
REMARK 465 ALA A 359
REMARK 465 GLU A 360
REMARK 465 GLY A 361
REMARK 465 ALA A 362
REMARK 465 PRO A 363
REMARK 465 GLN A 364
REMARK 465 LYS A 365
REMARK 465 THR A 377
REMARK 465 GLN A 378
REMARK 465 TYR A 379
REMARK 465 ASP A 380
REMARK 465 ALA A 381
REMARK 465 LYS A 382
REMARK 465 LYS A 383
REMARK 465 LYS A 384
REMARK 465 ALA A 385
REMARK 465 ALA A 386
REMARK 465 HIS A 387
REMARK 465 ALA A 388
REMARK 465 ALA A 389
REMARK 465 LYS A 390
REMARK 465 THR A 391
REMARK 465 VAL A 392
REMARK 465 LYS A 393
REMARK 465 HIS A 394
REMARK 465 GLY A 395
REMARK 465 ALA A 396
REMARK 465 GLY A 397
REMARK 465 ALA A 398
REMARK 465 GLU A 399
REMARK 465 ILE A 400
REMARK 465 SER A 401
REMARK 465 THR A 402
REMARK 465 VAL A 403
REMARK 465 ASN A 418
REMARK 465 ILE A 419
REMARK 465 PHE A 420
REMARK 465 ALA A 421
REMARK 465 SER B 30
REMARK 465 MET B 31
REMARK 465 HIS B 32
REMARK 465 PHE B 33
REMARK 465 VAL B 34
REMARK 465 GLN B 35
REMARK 465 GLN B 36
REMARK 465 LYS B 37
REMARK 465 VAL B 38
REMARK 465 LYS B 39
REMARK 465 VAL B 40
REMARK 465 PHE B 41
REMARK 465 ARG B 42
REMARK 465 ALA B 43
REMARK 465 ALA B 44
REMARK 465 GLY B 136
REMARK 465 SER B 137
REMARK 465 ASP B 138
REMARK 465 GLY B 139
REMARK 465 SER B 222
REMARK 465 LEU B 223
REMARK 465 VAL B 224
REMARK 465 SER B 225
REMARK 465 ARG B 226
REMARK 465 GLU B 227
REMARK 465 ALA B 228
REMARK 465 SER B 229
REMARK 465 ASP B 230
REMARK 465 LYS B 231
REMARK 465 GLU B 232
REMARK 465 LYS B 233
REMARK 465 VAL B 234
REMARK 465 LYS B 235
REMARK 465 GLU B 236
REMARK 465 LEU B 237
REMARK 465 PRO B 238
REMARK 465 ILE B 291
REMARK 465 ARG B 292
REMARK 465 GLY B 293
REMARK 465 SER B 294
REMARK 465 GLU B 295
REMARK 465 PRO B 296
REMARK 465 GLU B 297
REMARK 465 GLU B 298
REMARK 465 GLU B 299
REMARK 465 ALA B 300
REMARK 465 PRO B 301
REMARK 465 VAL B 302
REMARK 465 ARG B 303
REMARK 465 GLU B 304
REMARK 465 ASP B 305
REMARK 465 GLU B 306
REMARK 465 SER B 307
REMARK 465 GLU B 308
REMARK 465 VAL B 309
REMARK 465 ASP B 310
REMARK 465 GLY B 311
REMARK 465 ASP B 312
REMARK 465 CYS B 313
REMARK 465 SER B 314
REMARK 465 LEU B 315
REMARK 465 THR B 316
REMARK 465 GLY B 317
REMARK 465 PRO B 318
REMARK 465 PRO B 319
REMARK 465 ALA B 320
REMARK 465 LEU B 321
REMARK 465 VAL B 322
REMARK 465 GLY B 323
REMARK 465 SER B 324
REMARK 465 TYR B 325
REMARK 465 GLY B 326
REMARK 465 THR B 327
REMARK 465 SER B 328
REMARK 465 PRO B 329
REMARK 465 GLU B 330
REMARK 465 GLY B 331
REMARK 465 ILE B 332
REMARK 465 GLY B 333
REMARK 465 GLY B 334
REMARK 465 TYR B 335
REMARK 465 ILE B 336
REMARK 465 HIS B 337
REMARK 465 SER B 338
REMARK 465 HIS B 339
REMARK 465 ARG B 340
REMARK 465 PRO B 341
REMARK 465 LEU B 342
REMARK 465 GLY B 343
REMARK 465 PRO B 344
REMARK 465 GLY B 345
REMARK 465 GLU B 346
REMARK 465 PHE B 347
REMARK 465 GLU B 348
REMARK 465 SER B 349
REMARK 465 PHE B 350
REMARK 465 ILE B 351
REMARK 465 ASP B 352
REMARK 465 VAL B 353
REMARK 465 TYR B 354
REMARK 465 ALA B 355
REMARK 465 ILE B 356
REMARK 465 ARG B 357
REMARK 465 SER B 358
REMARK 465 ALA B 359
REMARK 465 GLU B 360
REMARK 465 GLY B 361
REMARK 465 ALA B 362
REMARK 465 PRO B 363
REMARK 465 GLN B 364
REMARK 465 LYS B 365
REMARK 465 THR B 377
REMARK 465 GLN B 378
REMARK 465 TYR B 379
REMARK 465 ASP B 380
REMARK 465 ALA B 381
REMARK 465 LYS B 382
REMARK 465 LYS B 383
REMARK 465 LYS B 384
REMARK 465 ALA B 385
REMARK 465 ALA B 386
REMARK 465 HIS B 387
REMARK 465 ALA B 388
REMARK 465 ALA B 389
REMARK 465 LYS B 390
REMARK 465 THR B 391
REMARK 465 VAL B 392
REMARK 465 LYS B 393
REMARK 465 HIS B 394
REMARK 465 GLY B 395
REMARK 465 ALA B 396
REMARK 465 GLY B 397
REMARK 465 ALA B 398
REMARK 465 GLU B 399
REMARK 465 ILE B 400
REMARK 465 SER B 401
REMARK 465 THR B 402
REMARK 465 VAL B 403
REMARK 465 ASN B 418
REMARK 465 ILE B 419
REMARK 465 PHE B 420
REMARK 465 ALA B 421
REMARK 465 SER C 30
REMARK 465 MET C 31
REMARK 465 HIS C 32
REMARK 465 PHE C 33
REMARK 465 VAL C 34
REMARK 465 GLN C 35
REMARK 465 GLN C 36
REMARK 465 LYS C 37
REMARK 465 VAL C 38
REMARK 465 LYS C 39
REMARK 465 VAL C 40
REMARK 465 PHE C 41
REMARK 465 ARG C 42
REMARK 465 ALA C 43
REMARK 465 ALA C 44
REMARK 465 GLU C 135
REMARK 465 GLY C 136
REMARK 465 SER C 137
REMARK 465 ASP C 138
REMARK 465 GLY C 139
REMARK 465 LEU C 219
REMARK 465 LYS C 220
REMARK 465 GLY C 221
REMARK 465 SER C 222
REMARK 465 LEU C 223
REMARK 465 VAL C 224
REMARK 465 SER C 225
REMARK 465 ARG C 226
REMARK 465 GLU C 227
REMARK 465 ALA C 228
REMARK 465 SER C 229
REMARK 465 ASP C 230
REMARK 465 LYS C 231
REMARK 465 GLU C 232
REMARK 465 LYS C 233
REMARK 465 VAL C 234
REMARK 465 LYS C 235
REMARK 465 GLU C 236
REMARK 465 LEU C 237
REMARK 465 PRO C 238
REMARK 465 ASP C 244
REMARK 465 PHE C 245
REMARK 465 ILE C 291
REMARK 465 ARG C 292
REMARK 465 GLY C 293
REMARK 465 SER C 294
REMARK 465 GLU C 295
REMARK 465 PRO C 296
REMARK 465 GLU C 297
REMARK 465 GLU C 298
REMARK 465 GLU C 299
REMARK 465 ALA C 300
REMARK 465 PRO C 301
REMARK 465 VAL C 302
REMARK 465 ARG C 303
REMARK 465 GLU C 304
REMARK 465 ASP C 305
REMARK 465 GLU C 306
REMARK 465 SER C 307
REMARK 465 GLU C 308
REMARK 465 VAL C 309
REMARK 465 ASP C 310
REMARK 465 GLY C 311
REMARK 465 ASP C 312
REMARK 465 CYS C 313
REMARK 465 SER C 314
REMARK 465 LEU C 315
REMARK 465 THR C 316
REMARK 465 GLY C 317
REMARK 465 PRO C 318
REMARK 465 PRO C 319
REMARK 465 ALA C 320
REMARK 465 LEU C 321
REMARK 465 VAL C 322
REMARK 465 GLY C 323
REMARK 465 SER C 324
REMARK 465 TYR C 325
REMARK 465 GLY C 326
REMARK 465 THR C 327
REMARK 465 SER C 328
REMARK 465 PRO C 329
REMARK 465 GLU C 330
REMARK 465 GLY C 331
REMARK 465 ILE C 332
REMARK 465 GLY C 333
REMARK 465 GLY C 334
REMARK 465 TYR C 335
REMARK 465 ILE C 336
REMARK 465 HIS C 337
REMARK 465 SER C 338
REMARK 465 HIS C 339
REMARK 465 ARG C 340
REMARK 465 PRO C 341
REMARK 465 LEU C 342
REMARK 465 GLY C 343
REMARK 465 PRO C 344
REMARK 465 GLY C 345
REMARK 465 GLU C 346
REMARK 465 PHE C 347
REMARK 465 GLU C 348
REMARK 465 SER C 349
REMARK 465 PHE C 350
REMARK 465 ILE C 351
REMARK 465 ASP C 352
REMARK 465 VAL C 353
REMARK 465 TYR C 354
REMARK 465 ALA C 355
REMARK 465 ILE C 356
REMARK 465 ARG C 357
REMARK 465 SER C 358
REMARK 465 ALA C 359
REMARK 465 GLU C 360
REMARK 465 GLY C 361
REMARK 465 ALA C 362
REMARK 465 PRO C 363
REMARK 465 GLN C 364
REMARK 465 LYS C 365
REMARK 465 GLN C 378
REMARK 465 TYR C 379
REMARK 465 ASP C 380
REMARK 465 ALA C 381
REMARK 465 LYS C 382
REMARK 465 LYS C 383
REMARK 465 LYS C 384
REMARK 465 ALA C 385
REMARK 465 ALA C 386
REMARK 465 HIS C 387
REMARK 465 ALA C 388
REMARK 465 ALA C 389
REMARK 465 LYS C 390
REMARK 465 THR C 391
REMARK 465 VAL C 392
REMARK 465 LYS C 393
REMARK 465 HIS C 394
REMARK 465 GLY C 395
REMARK 465 ALA C 396
REMARK 465 GLY C 397
REMARK 465 ALA C 398
REMARK 465 GLU C 399
REMARK 465 ILE C 400
REMARK 465 SER C 401
REMARK 465 THR C 402
REMARK 465 VAL C 403
REMARK 465 ASN C 418
REMARK 465 ILE C 419
REMARK 465 PHE C 420
REMARK 465 ALA C 421
REMARK 465 SER D 30
REMARK 465 MET D 31
REMARK 465 HIS D 32
REMARK 465 PHE D 33
REMARK 465 VAL D 34
REMARK 465 GLN D 35
REMARK 465 GLN D 36
REMARK 465 LYS D 37
REMARK 465 VAL D 38
REMARK 465 LYS D 39
REMARK 465 VAL D 40
REMARK 465 PHE D 41
REMARK 465 ARG D 42
REMARK 465 ALA D 43
REMARK 465 ALA D 44
REMARK 465 GLY D 136
REMARK 465 SER D 137
REMARK 465 ASP D 138
REMARK 465 GLY D 139
REMARK 465 SER D 222
REMARK 465 LEU D 223
REMARK 465 VAL D 224
REMARK 465 SER D 225
REMARK 465 ARG D 226
REMARK 465 GLU D 227
REMARK 465 ALA D 228
REMARK 465 SER D 229
REMARK 465 ASP D 230
REMARK 465 LYS D 231
REMARK 465 GLU D 232
REMARK 465 LYS D 233
REMARK 465 VAL D 234
REMARK 465 LYS D 235
REMARK 465 GLU D 236
REMARK 465 LEU D 237
REMARK 465 PRO D 238
REMARK 465 ILE D 291
REMARK 465 ARG D 292
REMARK 465 GLY D 293
REMARK 465 SER D 294
REMARK 465 GLU D 295
REMARK 465 PRO D 296
REMARK 465 GLU D 297
REMARK 465 GLU D 298
REMARK 465 GLU D 299
REMARK 465 ALA D 300
REMARK 465 PRO D 301
REMARK 465 VAL D 302
REMARK 465 ARG D 303
REMARK 465 GLU D 304
REMARK 465 ASP D 305
REMARK 465 GLU D 306
REMARK 465 SER D 307
REMARK 465 GLU D 308
REMARK 465 VAL D 309
REMARK 465 ASP D 310
REMARK 465 GLY D 311
REMARK 465 ASP D 312
REMARK 465 CYS D 313
REMARK 465 SER D 314
REMARK 465 LEU D 315
REMARK 465 THR D 316
REMARK 465 GLY D 317
REMARK 465 PRO D 318
REMARK 465 PRO D 319
REMARK 465 ALA D 320
REMARK 465 LEU D 321
REMARK 465 VAL D 322
REMARK 465 GLY D 323
REMARK 465 SER D 324
REMARK 465 TYR D 325
REMARK 465 GLY D 326
REMARK 465 THR D 327
REMARK 465 SER D 328
REMARK 465 PRO D 329
REMARK 465 GLU D 330
REMARK 465 GLY D 331
REMARK 465 ILE D 332
REMARK 465 GLY D 333
REMARK 465 GLY D 334
REMARK 465 TYR D 335
REMARK 465 ILE D 336
REMARK 465 HIS D 337
REMARK 465 SER D 338
REMARK 465 HIS D 339
REMARK 465 ARG D 340
REMARK 465 PRO D 341
REMARK 465 LEU D 342
REMARK 465 GLY D 343
REMARK 465 PRO D 344
REMARK 465 GLY D 345
REMARK 465 GLU D 346
REMARK 465 PHE D 347
REMARK 465 GLU D 348
REMARK 465 SER D 349
REMARK 465 PHE D 350
REMARK 465 ILE D 351
REMARK 465 ASP D 352
REMARK 465 VAL D 353
REMARK 465 TYR D 354
REMARK 465 ALA D 355
REMARK 465 ILE D 356
REMARK 465 ARG D 357
REMARK 465 SER D 358
REMARK 465 ALA D 359
REMARK 465 GLU D 360
REMARK 465 GLY D 361
REMARK 465 ALA D 362
REMARK 465 PRO D 363
REMARK 465 GLN D 364
REMARK 465 LYS D 365
REMARK 465 THR D 377
REMARK 465 GLN D 378
REMARK 465 TYR D 379
REMARK 465 ASP D 380
REMARK 465 ALA D 381
REMARK 465 LYS D 382
REMARK 465 LYS D 383
REMARK 465 LYS D 384
REMARK 465 ALA D 385
REMARK 465 ALA D 386
REMARK 465 HIS D 387
REMARK 465 ALA D 388
REMARK 465 ALA D 389
REMARK 465 LYS D 390
REMARK 465 THR D 391
REMARK 465 VAL D 392
REMARK 465 LYS D 393
REMARK 465 HIS D 394
REMARK 465 GLY D 395
REMARK 465 ALA D 396
REMARK 465 GLY D 397
REMARK 465 ALA D 398
REMARK 465 GLU D 399
REMARK 465 ILE D 400
REMARK 465 SER D 401
REMARK 465 THR D 402
REMARK 465 VAL D 403
REMARK 465 ASN D 418
REMARK 465 ILE D 419
REMARK 465 PHE D 420
REMARK 465 ALA D 421
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO D 130 C - N - CD ANGL. DEV. = -12.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 68 -169.51 -67.51
REMARK 500 LEU A 88 31.07 72.49
REMARK 500 PHE A 89 -76.83 -92.93
REMARK 500 ARG A 91 -17.28 -148.61
REMARK 500 ASN A 93 -53.25 -127.48
REMARK 500 PRO A 95 164.75 -46.44
REMARK 500 CYS A 104 74.27 41.35
REMARK 500 THR A 127 -38.79 -132.72
REMARK 500 PHE A 185 97.35 -62.51
REMARK 500 ARG A 210 -74.73 -113.47
REMARK 500 LYS A 220 -73.45 -114.59
REMARK 500 LEU A 240 125.04 -37.67
REMARK 500 ASN A 249 72.77 68.20
REMARK 500 VAL A 252 78.69 -109.59
REMARK 500 LYS A 277 -6.61 70.74
REMARK 500 ILE A 278 127.12 -35.25
REMARK 500 ASP A 374 62.67 -69.08
REMARK 500 PHE A 412 -76.24 -80.35
REMARK 500 PHE B 76 0.38 -67.19
REMARK 500 LEU B 88 33.83 83.93
REMARK 500 PHE B 89 -86.31 -115.87
REMARK 500 ARG B 91 -37.97 -141.76
REMARK 500 ASN B 93 -7.19 -149.17
REMARK 500 LEU B 126 28.26 -148.84
REMARK 500 PRO B 130 158.31 -49.05
REMARK 500 LEU B 142 88.49 -173.42
REMARK 500 SER B 144 155.01 -45.36
REMARK 500 MET B 188 116.92 -162.35
REMARK 500 ARG B 210 -67.20 -97.13
REMARK 500 LYS B 220 -81.11 -126.25
REMARK 500 ARG B 241 173.56 -54.90
REMARK 500 ASN B 249 67.11 70.11
REMARK 500 GLN B 250 -179.67 -63.47
REMARK 500 ILE B 254 -63.66 -124.18
REMARK 500 GLU B 256 -75.24 -88.73
REMARK 500 LYS B 267 -73.83 -61.47
REMARK 500 MET B 279 -76.49 -84.23
REMARK 500 ILE B 373 -9.19 -146.49
REMARK 500 ILE B 375 34.34 -93.36
REMARK 500 GLN B 407 -70.48 -68.70
REMARK 500 PHE B 412 -76.20 -80.38
REMARK 500 ALA C 56 -71.79 -48.50
REMARK 500 SER C 80 118.95 -172.31
REMARK 500 HIS C 90 -118.42 64.12
REMARK 500 ARG C 91 -7.30 85.82
REMARK 500 ASN C 93 -18.36 73.00
REMARK 500 LEU C 126 -25.03 -149.64
REMARK 500 PHE C 141 132.69 -33.44
REMARK 500 SER C 164 -72.10 -70.71
REMARK 500 ASN C 179 72.92 -151.59
REMARK 500
REMARK 500 THIS ENTRY HAS 84 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 MET A 279 ASP A 280 -139.65
REMARK 500 ARG B 91 GLU B 92 -130.23
REMARK 500 ARG D 128 ASN D 129 -144.55
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2GK9 A 32 421 UNP Q8TBX8 Q8TBX8_HUMAN 32 421
DBREF 2GK9 B 32 421 UNP Q8TBX8 Q8TBX8_HUMAN 32 421
DBREF 2GK9 C 32 421 UNP Q8TBX8 Q8TBX8_HUMAN 32 421
DBREF 2GK9 D 32 421 UNP Q8TBX8 Q8TBX8_HUMAN 32 421
SEQADV 2GK9 SER A 30 UNP Q8TBX8 CLONING ARTIFACT
SEQADV 2GK9 MET A 31 UNP Q8TBX8 CLONING ARTIFACT
SEQADV 2GK9 SER B 30 UNP Q8TBX8 CLONING ARTIFACT
SEQADV 2GK9 MET B 31 UNP Q8TBX8 CLONING ARTIFACT
SEQADV 2GK9 SER C 30 UNP Q8TBX8 CLONING ARTIFACT
SEQADV 2GK9 MET C 31 UNP Q8TBX8 CLONING ARTIFACT
SEQADV 2GK9 SER D 30 UNP Q8TBX8 CLONING ARTIFACT
SEQADV 2GK9 MET D 31 UNP Q8TBX8 CLONING ARTIFACT
SEQRES 1 A 392 SER MET HIS PHE VAL GLN GLN LYS VAL LYS VAL PHE ARG
SEQRES 2 A 392 ALA ALA ASP PRO LEU VAL GLY VAL PHE LEU TRP GLY VAL
SEQRES 3 A 392 ALA HIS SER ILE ASN GLU LEU SER GLN VAL PRO PRO PRO
SEQRES 4 A 392 VAL MET LEU LEU PRO ASP ASP PHE LYS ALA SER SER LYS
SEQRES 5 A 392 ILE LYS VAL ASN ASN HIS LEU PHE HIS ARG GLU ASN LEU
SEQRES 6 A 392 PRO SER HIS PHE LYS PHE LYS GLU TYR CYS PRO GLN VAL
SEQRES 7 A 392 PHE ARG ASN LEU ARG ASP ARG PHE GLY ILE ASP ASP GLN
SEQRES 8 A 392 ASP TYR LEU VAL SER LEU THR ARG ASN PRO PRO SER GLU
SEQRES 9 A 392 SER GLU GLY SER ASP GLY ARG PHE LEU ILE SER TYR ASP
SEQRES 10 A 392 ARG THR LEU VAL ILE LYS GLU VAL SER SER GLU ASP ILE
SEQRES 11 A 392 ALA ASP MET HIS SER ASN LEU SER ASN TYR HIS GLN TYR
SEQRES 12 A 392 ILE VAL LYS CYS HIS GLY ASN THR LEU LEU PRO GLN PHE
SEQRES 13 A 392 LEU GLY MET TYR ARG VAL SER VAL ASP ASN GLU ASP SER
SEQRES 14 A 392 TYR MET LEU VAL MET ARG ASN MET PHE SER HIS ARG LEU
SEQRES 15 A 392 PRO VAL HIS ARG LYS TYR ASP LEU LYS GLY SER LEU VAL
SEQRES 16 A 392 SER ARG GLU ALA SER ASP LYS GLU LYS VAL LYS GLU LEU
SEQRES 17 A 392 PRO THR LEU ARG ASP MET ASP PHE LEU ASN LYS ASN GLN
SEQRES 18 A 392 LYS VAL TYR ILE GLY GLU GLU GLU LYS LYS ILE PHE LEU
SEQRES 19 A 392 GLU LYS LEU LYS ARG ASP VAL GLU PHE LEU VAL GLN LEU
SEQRES 20 A 392 LYS ILE MET ASP TYR SER LEU LEU LEU GLY ILE HIS ASP
SEQRES 21 A 392 ILE ILE ARG GLY SER GLU PRO GLU GLU GLU ALA PRO VAL
SEQRES 22 A 392 ARG GLU ASP GLU SER GLU VAL ASP GLY ASP CYS SER LEU
SEQRES 23 A 392 THR GLY PRO PRO ALA LEU VAL GLY SER TYR GLY THR SER
SEQRES 24 A 392 PRO GLU GLY ILE GLY GLY TYR ILE HIS SER HIS ARG PRO
SEQRES 25 A 392 LEU GLY PRO GLY GLU PHE GLU SER PHE ILE ASP VAL TYR
SEQRES 26 A 392 ALA ILE ARG SER ALA GLU GLY ALA PRO GLN LYS GLU VAL
SEQRES 27 A 392 TYR PHE MET GLY LEU ILE ASP ILE LEU THR GLN TYR ASP
SEQRES 28 A 392 ALA LYS LYS LYS ALA ALA HIS ALA ALA LYS THR VAL LYS
SEQRES 29 A 392 HIS GLY ALA GLY ALA GLU ILE SER THR VAL HIS PRO GLU
SEQRES 30 A 392 GLN TYR ALA LYS ARG PHE LEU ASP PHE ILE THR ASN ILE
SEQRES 31 A 392 PHE ALA
SEQRES 1 B 392 SER MET HIS PHE VAL GLN GLN LYS VAL LYS VAL PHE ARG
SEQRES 2 B 392 ALA ALA ASP PRO LEU VAL GLY VAL PHE LEU TRP GLY VAL
SEQRES 3 B 392 ALA HIS SER ILE ASN GLU LEU SER GLN VAL PRO PRO PRO
SEQRES 4 B 392 VAL MET LEU LEU PRO ASP ASP PHE LYS ALA SER SER LYS
SEQRES 5 B 392 ILE LYS VAL ASN ASN HIS LEU PHE HIS ARG GLU ASN LEU
SEQRES 6 B 392 PRO SER HIS PHE LYS PHE LYS GLU TYR CYS PRO GLN VAL
SEQRES 7 B 392 PHE ARG ASN LEU ARG ASP ARG PHE GLY ILE ASP ASP GLN
SEQRES 8 B 392 ASP TYR LEU VAL SER LEU THR ARG ASN PRO PRO SER GLU
SEQRES 9 B 392 SER GLU GLY SER ASP GLY ARG PHE LEU ILE SER TYR ASP
SEQRES 10 B 392 ARG THR LEU VAL ILE LYS GLU VAL SER SER GLU ASP ILE
SEQRES 11 B 392 ALA ASP MET HIS SER ASN LEU SER ASN TYR HIS GLN TYR
SEQRES 12 B 392 ILE VAL LYS CYS HIS GLY ASN THR LEU LEU PRO GLN PHE
SEQRES 13 B 392 LEU GLY MET TYR ARG VAL SER VAL ASP ASN GLU ASP SER
SEQRES 14 B 392 TYR MET LEU VAL MET ARG ASN MET PHE SER HIS ARG LEU
SEQRES 15 B 392 PRO VAL HIS ARG LYS TYR ASP LEU LYS GLY SER LEU VAL
SEQRES 16 B 392 SER ARG GLU ALA SER ASP LYS GLU LYS VAL LYS GLU LEU
SEQRES 17 B 392 PRO THR LEU ARG ASP MET ASP PHE LEU ASN LYS ASN GLN
SEQRES 18 B 392 LYS VAL TYR ILE GLY GLU GLU GLU LYS LYS ILE PHE LEU
SEQRES 19 B 392 GLU LYS LEU LYS ARG ASP VAL GLU PHE LEU VAL GLN LEU
SEQRES 20 B 392 LYS ILE MET ASP TYR SER LEU LEU LEU GLY ILE HIS ASP
SEQRES 21 B 392 ILE ILE ARG GLY SER GLU PRO GLU GLU GLU ALA PRO VAL
SEQRES 22 B 392 ARG GLU ASP GLU SER GLU VAL ASP GLY ASP CYS SER LEU
SEQRES 23 B 392 THR GLY PRO PRO ALA LEU VAL GLY SER TYR GLY THR SER
SEQRES 24 B 392 PRO GLU GLY ILE GLY GLY TYR ILE HIS SER HIS ARG PRO
SEQRES 25 B 392 LEU GLY PRO GLY GLU PHE GLU SER PHE ILE ASP VAL TYR
SEQRES 26 B 392 ALA ILE ARG SER ALA GLU GLY ALA PRO GLN LYS GLU VAL
SEQRES 27 B 392 TYR PHE MET GLY LEU ILE ASP ILE LEU THR GLN TYR ASP
SEQRES 28 B 392 ALA LYS LYS LYS ALA ALA HIS ALA ALA LYS THR VAL LYS
SEQRES 29 B 392 HIS GLY ALA GLY ALA GLU ILE SER THR VAL HIS PRO GLU
SEQRES 30 B 392 GLN TYR ALA LYS ARG PHE LEU ASP PHE ILE THR ASN ILE
SEQRES 31 B 392 PHE ALA
SEQRES 1 C 392 SER MET HIS PHE VAL GLN GLN LYS VAL LYS VAL PHE ARG
SEQRES 2 C 392 ALA ALA ASP PRO LEU VAL GLY VAL PHE LEU TRP GLY VAL
SEQRES 3 C 392 ALA HIS SER ILE ASN GLU LEU SER GLN VAL PRO PRO PRO
SEQRES 4 C 392 VAL MET LEU LEU PRO ASP ASP PHE LYS ALA SER SER LYS
SEQRES 5 C 392 ILE LYS VAL ASN ASN HIS LEU PHE HIS ARG GLU ASN LEU
SEQRES 6 C 392 PRO SER HIS PHE LYS PHE LYS GLU TYR CYS PRO GLN VAL
SEQRES 7 C 392 PHE ARG ASN LEU ARG ASP ARG PHE GLY ILE ASP ASP GLN
SEQRES 8 C 392 ASP TYR LEU VAL SER LEU THR ARG ASN PRO PRO SER GLU
SEQRES 9 C 392 SER GLU GLY SER ASP GLY ARG PHE LEU ILE SER TYR ASP
SEQRES 10 C 392 ARG THR LEU VAL ILE LYS GLU VAL SER SER GLU ASP ILE
SEQRES 11 C 392 ALA ASP MET HIS SER ASN LEU SER ASN TYR HIS GLN TYR
SEQRES 12 C 392 ILE VAL LYS CYS HIS GLY ASN THR LEU LEU PRO GLN PHE
SEQRES 13 C 392 LEU GLY MET TYR ARG VAL SER VAL ASP ASN GLU ASP SER
SEQRES 14 C 392 TYR MET LEU VAL MET ARG ASN MET PHE SER HIS ARG LEU
SEQRES 15 C 392 PRO VAL HIS ARG LYS TYR ASP LEU LYS GLY SER LEU VAL
SEQRES 16 C 392 SER ARG GLU ALA SER ASP LYS GLU LYS VAL LYS GLU LEU
SEQRES 17 C 392 PRO THR LEU ARG ASP MET ASP PHE LEU ASN LYS ASN GLN
SEQRES 18 C 392 LYS VAL TYR ILE GLY GLU GLU GLU LYS LYS ILE PHE LEU
SEQRES 19 C 392 GLU LYS LEU LYS ARG ASP VAL GLU PHE LEU VAL GLN LEU
SEQRES 20 C 392 LYS ILE MET ASP TYR SER LEU LEU LEU GLY ILE HIS ASP
SEQRES 21 C 392 ILE ILE ARG GLY SER GLU PRO GLU GLU GLU ALA PRO VAL
SEQRES 22 C 392 ARG GLU ASP GLU SER GLU VAL ASP GLY ASP CYS SER LEU
SEQRES 23 C 392 THR GLY PRO PRO ALA LEU VAL GLY SER TYR GLY THR SER
SEQRES 24 C 392 PRO GLU GLY ILE GLY GLY TYR ILE HIS SER HIS ARG PRO
SEQRES 25 C 392 LEU GLY PRO GLY GLU PHE GLU SER PHE ILE ASP VAL TYR
SEQRES 26 C 392 ALA ILE ARG SER ALA GLU GLY ALA PRO GLN LYS GLU VAL
SEQRES 27 C 392 TYR PHE MET GLY LEU ILE ASP ILE LEU THR GLN TYR ASP
SEQRES 28 C 392 ALA LYS LYS LYS ALA ALA HIS ALA ALA LYS THR VAL LYS
SEQRES 29 C 392 HIS GLY ALA GLY ALA GLU ILE SER THR VAL HIS PRO GLU
SEQRES 30 C 392 GLN TYR ALA LYS ARG PHE LEU ASP PHE ILE THR ASN ILE
SEQRES 31 C 392 PHE ALA
SEQRES 1 D 392 SER MET HIS PHE VAL GLN GLN LYS VAL LYS VAL PHE ARG
SEQRES 2 D 392 ALA ALA ASP PRO LEU VAL GLY VAL PHE LEU TRP GLY VAL
SEQRES 3 D 392 ALA HIS SER ILE ASN GLU LEU SER GLN VAL PRO PRO PRO
SEQRES 4 D 392 VAL MET LEU LEU PRO ASP ASP PHE LYS ALA SER SER LYS
SEQRES 5 D 392 ILE LYS VAL ASN ASN HIS LEU PHE HIS ARG GLU ASN LEU
SEQRES 6 D 392 PRO SER HIS PHE LYS PHE LYS GLU TYR CYS PRO GLN VAL
SEQRES 7 D 392 PHE ARG ASN LEU ARG ASP ARG PHE GLY ILE ASP ASP GLN
SEQRES 8 D 392 ASP TYR LEU VAL SER LEU THR ARG ASN PRO PRO SER GLU
SEQRES 9 D 392 SER GLU GLY SER ASP GLY ARG PHE LEU ILE SER TYR ASP
SEQRES 10 D 392 ARG THR LEU VAL ILE LYS GLU VAL SER SER GLU ASP ILE
SEQRES 11 D 392 ALA ASP MET HIS SER ASN LEU SER ASN TYR HIS GLN TYR
SEQRES 12 D 392 ILE VAL LYS CYS HIS GLY ASN THR LEU LEU PRO GLN PHE
SEQRES 13 D 392 LEU GLY MET TYR ARG VAL SER VAL ASP ASN GLU ASP SER
SEQRES 14 D 392 TYR MET LEU VAL MET ARG ASN MET PHE SER HIS ARG LEU
SEQRES 15 D 392 PRO VAL HIS ARG LYS TYR ASP LEU LYS GLY SER LEU VAL
SEQRES 16 D 392 SER ARG GLU ALA SER ASP LYS GLU LYS VAL LYS GLU LEU
SEQRES 17 D 392 PRO THR LEU ARG ASP MET ASP PHE LEU ASN LYS ASN GLN
SEQRES 18 D 392 LYS VAL TYR ILE GLY GLU GLU GLU LYS LYS ILE PHE LEU
SEQRES 19 D 392 GLU LYS LEU LYS ARG ASP VAL GLU PHE LEU VAL GLN LEU
SEQRES 20 D 392 LYS ILE MET ASP TYR SER LEU LEU LEU GLY ILE HIS ASP
SEQRES 21 D 392 ILE ILE ARG GLY SER GLU PRO GLU GLU GLU ALA PRO VAL
SEQRES 22 D 392 ARG GLU ASP GLU SER GLU VAL ASP GLY ASP CYS SER LEU
SEQRES 23 D 392 THR GLY PRO PRO ALA LEU VAL GLY SER TYR GLY THR SER
SEQRES 24 D 392 PRO GLU GLY ILE GLY GLY TYR ILE HIS SER HIS ARG PRO
SEQRES 25 D 392 LEU GLY PRO GLY GLU PHE GLU SER PHE ILE ASP VAL TYR
SEQRES 26 D 392 ALA ILE ARG SER ALA GLU GLY ALA PRO GLN LYS GLU VAL
SEQRES 27 D 392 TYR PHE MET GLY LEU ILE ASP ILE LEU THR GLN TYR ASP
SEQRES 28 D 392 ALA LYS LYS LYS ALA ALA HIS ALA ALA LYS THR VAL LYS
SEQRES 29 D 392 HIS GLY ALA GLY ALA GLU ILE SER THR VAL HIS PRO GLU
SEQRES 30 D 392 GLN TYR ALA LYS ARG PHE LEU ASP PHE ILE THR ASN ILE
SEQRES 31 D 392 PHE ALA
HELIX 1 1 ASP A 45 SER A 63 1 19
HELIX 2 2 LEU A 72 LYS A 77 5 6
HELIX 3 3 CYS A 104 ARG A 114 1 11
HELIX 4 4 ASP A 118 ARG A 128 1 11
HELIX 5 5 SER A 155 CYS A 176 1 22
HELIX 6 6 LYS A 259 VAL A 274 1 16
HELIX 7 7 HIS A 404 PHE A 415 1 12
HELIX 8 8 ASP B 45 VAL B 65 1 21
HELIX 9 9 LEU B 72 ALA B 78 5 7
HELIX 10 10 CYS B 104 PHE B 115 1 12
HELIX 11 11 ASP B 118 ARG B 128 1 11
HELIX 12 12 SER B 155 HIS B 177 1 23
HELIX 13 13 MET B 243 LYS B 248 1 6
HELIX 14 14 LYS B 259 LEU B 276 1 18
HELIX 15 15 HIS B 404 PHE B 415 1 12
HELIX 16 16 PRO C 46 SER C 63 1 18
HELIX 17 17 LEU C 72 LYS C 77 5 6
HELIX 18 18 CYS C 104 PHE C 115 1 12
HELIX 19 19 ASP C 118 SER C 125 1 8
HELIX 20 20 GLU C 157 HIS C 177 1 21
HELIX 21 21 GLU C 258 LEU C 276 1 19
HELIX 22 22 HIS C 404 PHE C 415 1 12
HELIX 23 23 ASP D 45 GLN D 64 1 20
HELIX 24 24 LEU D 72 ALA D 78 1 7
HELIX 25 25 CYS D 104 PHE D 115 1 12
HELIX 26 26 ASP D 118 ARG D 128 1 11
HELIX 27 27 SER D 155 HIS D 177 1 23
HELIX 28 28 ARG D 241 PHE D 245 5 5
HELIX 29 29 GLY D 255 LEU D 276 1 22
HELIX 30 30 HIS D 404 PHE D 415 1 12
SHEET 1 A12 LEU A 149 GLU A 153 0
SHEET 2 A12 TYR A 199 ARG A 204 -1 O MET A 203 N VAL A 150
SHEET 3 A12 PHE A 185 ARG A 190 -1 N TYR A 189 O MET A 200
SHEET 4 A12 LYS A 99 TYR A 103 -1 N TYR A 103 O MET A 188
SHEET 5 A12 SER A 79 ASN A 85 -1 N ILE A 82 O PHE A 100
SHEET 6 A12 SER D 79 HIS D 87 -1 O ASN D 85 N LYS A 81
SHEET 7 A12 HIS D 97 TYR D 103 -1 O PHE D 98 N VAL D 84
SHEET 8 A12 PHE D 185 VAL D 193 -1 O SER D 192 N LYS D 99
SHEET 9 A12 TYR D 199 ARG D 204 -1 O VAL D 202 N GLY D 187
SHEET 10 A12 LEU D 149 VAL D 154 -1 N VAL D 154 O TYR D 199
SHEET 11 A12 LEU D 142 ILE D 143 -1 N LEU D 142 O ILE D 151
SHEET 12 A12 SER D 132 GLU D 133 -1 N SER D 132 O ILE D 143
SHEET 1 B 2 ASP A 218 LEU A 219 0
SHEET 2 B 2 LEU A 283 LEU A 284 -1 O LEU A 283 N LEU A 219
SHEET 1 C 4 HIS B 97 LYS B 101 0
SHEET 2 C 4 LYS B 81 ASN B 85 -1 N ILE B 82 O PHE B 100
SHEET 3 C 4 LYS C 81 ASN C 85 -1 O LYS C 83 N LYS B 83
SHEET 4 C 4 HIS C 97 LYS C 101 -1 O PHE C 100 N ILE C 82
SHEET 1 D 3 LEU B 149 VAL B 154 0
SHEET 2 D 3 GLU B 196 ARG B 204 -1 O MET B 203 N VAL B 150
SHEET 3 D 3 PHE B 185 VAL B 193 -1 N LEU B 186 O VAL B 202
SHEET 1 E 2 ASP B 218 LEU B 219 0
SHEET 2 E 2 LEU B 283 LEU B 284 -1 O LEU B 283 N LEU B 219
SHEET 1 F 2 ILE B 287 HIS B 288 0
SHEET 2 F 2 VAL B 367 TYR B 368 -1 O VAL B 367 N HIS B 288
SHEET 1 G 3 LEU C 149 VAL C 154 0
SHEET 2 G 3 SER C 198 ARG C 204 -1 O MET C 203 N VAL C 150
SHEET 3 G 3 PHE C 185 VAL C 191 -1 N GLY C 187 O VAL C 202
SHEET 1 H 2 ARG C 215 TYR C 217 0
SHEET 2 H 2 LEU C 283 ILE C 287 -1 O ILE C 287 N ARG C 215
SHEET 1 I 3 ARG D 215 LEU D 219 0
SHEET 2 I 3 LEU D 283 HIS D 288 -1 O LEU D 283 N LEU D 219
SHEET 3 I 3 VAL D 367 PHE D 369 -1 O PHE D 369 N GLY D 286
CRYST1 95.390 95.390 189.110 90.00 90.00 90.00 P 43 16
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 0.010483 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010483 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005288 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
