HEADER TRANSFERASE 16-SEP-14 4V0I
TITLE WATER NETWORK DETERMINES SELECTIVITY FOR A SERIES OF PYRIMIDONE
TITLE 2 INDOLINE AMIDE PI3KBETA INHIBITORS OVER PI3K-DELTA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE 3-KINASE CATALYTIC
COMPND 3 SUBUNIT DELTA ISOFORM;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: CATALYTIC SUBUNIT DELTA ISOFORM, RESIDUES 106-1043;
COMPND 6 SYNONYM: PI3-KINASE SUBUNIT DELTA, PI3K-DELTA, PI3KDELTA, PTDINS-3-
COMPND 7 KINASE SUBUNIT DELTA, PHOSPHATIDYLINOSITOL 4\,5-BISPHOSPHATE 3-KINASE
COMPND 8 110 KDA CATALYTIC SUBUNIT DELTA, PTDINS-3-KINAS SUBUNIT P110-DELTA,
COMPND 9 P110DELTA;
COMPND 10 EC: 2.7.1.153;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PACSG2
KEYWDS TRANSFERASE, PI3K, KINASE SELECTIVITY
EXPDTA X-RAY DIFFRACTION
AUTHOR D.ROBINSON,T.BERTRAND,J.C.CARRY,F.HALLEY,A.KARLSSON,M.MATHIEU,
AUTHOR 2 H.MINOUX,M.A.PERRIN,B.ROBERT,L.SCHIO,W.SHERMAN
REVDAT 5 10-JAN-24 4V0I 1 REMARK
REVDAT 4 08-MAY-19 4V0I 1 REMARK
REVDAT 3 24-APR-19 4V0I 1 SOURCE
REVDAT 2 05-OCT-16 4V0I 1 JRNL
REVDAT 1 30-SEP-15 4V0I 0
JRNL AUTH D.ROBINSON,T.BERTRAND,J.CARRY,F.HALLEY,A.KARLSSON,M.MATHIEU,
JRNL AUTH 2 H.MINOUX,M.PERRIN,B.ROBERT,L.SCHIO,W.SHERMAN
JRNL TITL DIFFERENTIAL WATER THERMODYNAMICS DETERMINE PI3K-BETA/DELTA
JRNL TITL 2 SELECTIVITY FOR SOLVENT-EXPOSED LIGAND MODIFICATIONS.
JRNL REF J.CHEM.INF.MODEL. V. 56 886 2016
JRNL REFN ISSN 1549-9596
JRNL PMID 27144736
JRNL DOI 10.1021/ACS.JCIM.5B00641
REMARK 2
REMARK 2 RESOLUTION. 2.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.7
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 60472
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 + TEST SET) : 0.266
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 3070
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.54
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.61
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.84
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4196
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2176
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4003
REMARK 3 BIN R VALUE (WORKING SET) : 0.2166
REMARK 3 BIN FREE R VALUE : 0.2389
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 193
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 : 12462
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.38360
REMARK 3 B22 (A**2) : -4.15310
REMARK 3 B33 (A**2) : 2.76950
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -4.54310
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.385
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.586
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.298
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.673
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.309
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.880
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.853
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 12787 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 17251 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 4489 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 310 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1824 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 12787 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1594 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 14175 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 0.95
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.80
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.02
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY
REMARK 4
REMARK 4 4V0I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1290061778.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111) OR
REMARK 200 SI(311)
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60528
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.540
REMARK 200 RESOLUTION RANGE LOW (A) : 216.430
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: PDB ENTRY 2WXF
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000 5-10%, ETHYLENE GLYCOL 10-20%,
REMARK 280 CARBOXYLIC ACIDS 100MM, IN MES-IMIDAZOLE 100MM BUFFER PH 6.5 AT
REMARK 280 19C, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 108.21500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 105
REMARK 465 GLY A 106
REMARK 465 ASP A 107
REMARK 465 ARG A 108
REMARK 465 VAL A 109
REMARK 465 SER A 174
REMARK 465 ALA A 175
REMARK 465 ARG A 176
REMARK 465 GLY A 177
REMARK 465 TRP A 178
REMARK 465 ARG A 179
REMARK 465 ALA A 180
REMARK 465 GLY A 181
REMARK 465 LEU A 182
REMARK 465 LEU A 183
REMARK 465 ARG A 184
REMARK 465 PHE A 228
REMARK 465 ARG A 229
REMARK 465 GLN A 230
REMARK 465 PRO A 231
REMARK 465 LEU A 232
REMARK 465 VAL A 233
REMARK 465 GLU A 234
REMARK 465 PRO A 292
REMARK 465 ALA A 293
REMARK 465 PRO A 294
REMARK 465 GLN A 295
REMARK 465 VAL A 296
REMARK 465 GLN A 297
REMARK 465 LYS A 298
REMARK 465 PRO A 299
REMARK 465 ARG A 300
REMARK 465 ALA A 301
REMARK 465 LYS A 302
REMARK 465 PRO A 303
REMARK 465 PRO A 304
REMARK 465 PRO A 305
REMARK 465 ILE A 306
REMARK 465 PRO A 307
REMARK 465 ALA A 308
REMARK 465 LYS A 309
REMARK 465 LYS A 310
REMARK 465 PRO A 311
REMARK 465 SER A 312
REMARK 465 SER A 313
REMARK 465 VAL A 314
REMARK 465 SER A 315
REMARK 465 LEU A 316
REMARK 465 TRP A 317
REMARK 465 SER A 318
REMARK 465 LEU A 319
REMARK 465 GLU A 320
REMARK 465 GLU A 329
REMARK 465 GLY A 330
REMARK 465 ARG A 331
REMARK 465 LYS A 332
REMARK 465 VAL A 333
REMARK 465 ASN A 334
REMARK 465 ALA A 335
REMARK 465 ASP A 336
REMARK 465 GLU A 337
REMARK 465 ARG A 338
REMARK 465 MET A 339
REMARK 465 LYS A 340
REMARK 465 LEU A 341
REMARK 465 VAL A 342
REMARK 465 VAL A 358
REMARK 465 SER A 359
REMARK 465 SER A 360
REMARK 465 SER A 361
REMARK 465 GLU A 362
REMARK 465 VAL A 363
REMARK 465 ASN A 364
REMARK 465 VAL A 365
REMARK 465 CYS A 366
REMARK 465 SER A 367
REMARK 465 GLU A 368
REMARK 465 PRO A 369
REMARK 465 VAL A 370
REMARK 465 TRP A 371
REMARK 465 LYS A 372
REMARK 465 GLN A 373
REMARK 465 ARG A 374
REMARK 465 LEU A 375
REMARK 465 GLU A 376
REMARK 465 PHE A 377
REMARK 465 VAL A 397
REMARK 465 VAL A 398
REMARK 465 GLU A 399
REMARK 465 LYS A 400
REMARK 465 ALA A 401
REMARK 465 LYS A 402
REMARK 465 LYS A 403
REMARK 465 ALA A 404
REMARK 465 ARG A 405
REMARK 465 SER A 406
REMARK 465 THR A 407
REMARK 465 LYS A 408
REMARK 465 LYS A 409
REMARK 465 LYS A 410
REMARK 465 SER A 411
REMARK 465 LYS A 412
REMARK 465 LYS A 413
REMARK 465 ALA A 414
REMARK 465 VAL A 445
REMARK 465 PRO A 446
REMARK 465 ASP A 447
REMARK 465 GLU A 448
REMARK 465 LYS A 449
REMARK 465 GLY A 450
REMARK 465 GLU A 451
REMARK 465 PRO A 480
REMARK 465 HIS A 481
REMARK 465 GLY A 495
REMARK 465 ARG A 496
REMARK 465 HIS A 497
REMARK 465 GLY A 498
REMARK 465 GLU A 499
REMARK 465 ARG A 500
REMARK 465 GLY A 501
REMARK 465 ARG A 502
REMARK 465 ILE A 503
REMARK 465 THR A 504
REMARK 465 GLU A 505
REMARK 465 GLU A 506
REMARK 465 GLU A 507
REMARK 465 GLN A 508
REMARK 465 LEU A 509
REMARK 465 GLN A 510
REMARK 465 LEU A 511
REMARK 465 ARG A 512
REMARK 465 GLU A 513
REMARK 465 ILE A 514
REMARK 465 LEU A 515
REMARK 465 GLU A 516
REMARK 465 ARG A 517
REMARK 465 ARG A 518
REMARK 465 GLY A 519
REMARK 465 SER A 520
REMARK 465 GLY A 521
REMARK 465 GLU A 522
REMARK 465 LEU A 523
REMARK 465 TYR A 524
REMARK 465 ASN A 840
REMARK 465 LYS A 841
REMARK 465 SER A 842
REMARK 465 ASN A 843
REMARK 465 MET A 844
REMARK 465 ALA A 845
REMARK 465 ALA A 846
REMARK 465 ASN A 918
REMARK 465 PHE A 919
REMARK 465 LYS A 920
REMARK 465 THR A 921
REMARK 465 LYS A 922
REMARK 465 PHE A 923
REMARK 465 GLY A 924
REMARK 465 ILE A 925
REMARK 465 ASN A 926
REMARK 465 ARG A 927
REMARK 465 GLU A 928
REMARK 465 ARG A 929
REMARK 465 VAL A 930
REMARK 465 TRP A 1027
REMARK 465 LYS A 1028
REMARK 465 THR A 1029
REMARK 465 LYS A 1030
REMARK 465 VAL A 1031
REMARK 465 ASN A 1032
REMARK 465 TRP A 1033
REMARK 465 LEU A 1034
REMARK 465 ALA A 1035
REMARK 465 HIS A 1036
REMARK 465 ASN A 1037
REMARK 465 VAL A 1038
REMARK 465 SER A 1039
REMARK 465 LYS A 1040
REMARK 465 ASP A 1041
REMARK 465 ASN A 1042
REMARK 465 ARG A 1043
REMARK 465 GLN A 1044
REMARK 465 GLY B 105
REMARK 465 GLY B 106
REMARK 465 ASP B 107
REMARK 465 ARG B 108
REMARK 465 VAL B 109
REMARK 465 LYS B 110
REMARK 465 ARG B 176
REMARK 465 GLY B 177
REMARK 465 TRP B 178
REMARK 465 ARG B 179
REMARK 465 ALA B 180
REMARK 465 GLY B 181
REMARK 465 LEU B 182
REMARK 465 LEU B 183
REMARK 465 ARG B 184
REMARK 465 PHE B 228
REMARK 465 ARG B 229
REMARK 465 GLN B 230
REMARK 465 PRO B 231
REMARK 465 LEU B 232
REMARK 465 VAL B 233
REMARK 465 GLU B 234
REMARK 465 PRO B 292
REMARK 465 ALA B 293
REMARK 465 PRO B 294
REMARK 465 GLN B 295
REMARK 465 VAL B 296
REMARK 465 GLN B 297
REMARK 465 LYS B 298
REMARK 465 PRO B 299
REMARK 465 ARG B 300
REMARK 465 ALA B 301
REMARK 465 LYS B 302
REMARK 465 PRO B 303
REMARK 465 PRO B 304
REMARK 465 PRO B 305
REMARK 465 ILE B 306
REMARK 465 PRO B 307
REMARK 465 ALA B 308
REMARK 465 LYS B 309
REMARK 465 LYS B 310
REMARK 465 PRO B 311
REMARK 465 SER B 312
REMARK 465 SER B 313
REMARK 465 VAL B 314
REMARK 465 SER B 315
REMARK 465 LEU B 316
REMARK 465 TRP B 317
REMARK 465 SER B 318
REMARK 465 LEU B 319
REMARK 465 ASP B 336
REMARK 465 GLU B 337
REMARK 465 ARG B 338
REMARK 465 VAL B 397
REMARK 465 VAL B 398
REMARK 465 GLU B 399
REMARK 465 LYS B 400
REMARK 465 ALA B 401
REMARK 465 LYS B 402
REMARK 465 LYS B 403
REMARK 465 ALA B 404
REMARK 465 ARG B 405
REMARK 465 SER B 406
REMARK 465 THR B 407
REMARK 465 LYS B 408
REMARK 465 LYS B 409
REMARK 465 LYS B 410
REMARK 465 SER B 411
REMARK 465 LYS B 412
REMARK 465 LYS B 413
REMARK 465 ALA B 414
REMARK 465 VAL B 445
REMARK 465 PRO B 446
REMARK 465 ASP B 447
REMARK 465 GLU B 448
REMARK 465 LYS B 449
REMARK 465 GLY B 450
REMARK 465 GLU B 451
REMARK 465 PRO B 480
REMARK 465 HIS B 481
REMARK 465 GLY B 495
REMARK 465 ARG B 496
REMARK 465 HIS B 497
REMARK 465 GLY B 498
REMARK 465 GLU B 499
REMARK 465 ARG B 500
REMARK 465 GLY B 501
REMARK 465 ARG B 502
REMARK 465 ILE B 503
REMARK 465 THR B 504
REMARK 465 GLU B 505
REMARK 465 GLU B 506
REMARK 465 GLU B 507
REMARK 465 GLN B 508
REMARK 465 LEU B 509
REMARK 465 GLN B 510
REMARK 465 LEU B 511
REMARK 465 ARG B 512
REMARK 465 GLU B 513
REMARK 465 ILE B 514
REMARK 465 LEU B 515
REMARK 465 GLU B 516
REMARK 465 ARG B 517
REMARK 465 ARG B 518
REMARK 465 GLY B 519
REMARK 465 SER B 520
REMARK 465 GLY B 521
REMARK 465 GLU B 522
REMARK 465 LEU B 523
REMARK 465 TYR B 524
REMARK 465 ASN B 840
REMARK 465 LYS B 841
REMARK 465 SER B 842
REMARK 465 ASN B 843
REMARK 465 MET B 844
REMARK 465 ALA B 845
REMARK 465 ALA B 846
REMARK 465 ASN B 918
REMARK 465 PHE B 919
REMARK 465 LYS B 920
REMARK 465 THR B 921
REMARK 465 LYS B 922
REMARK 465 PHE B 923
REMARK 465 GLY B 924
REMARK 465 ILE B 925
REMARK 465 ASN B 926
REMARK 465 ARG B 927
REMARK 465 GLU B 928
REMARK 465 ARG B 929
REMARK 465 VAL B 930
REMARK 465 TRP B 1027
REMARK 465 LYS B 1028
REMARK 465 THR B 1029
REMARK 465 LYS B 1030
REMARK 465 VAL B 1031
REMARK 465 ASN B 1032
REMARK 465 TRP B 1033
REMARK 465 LEU B 1034
REMARK 465 ALA B 1035
REMARK 465 HIS B 1036
REMARK 465 ASN B 1037
REMARK 465 VAL B 1038
REMARK 465 SER B 1039
REMARK 465 LYS B 1040
REMARK 465 ASP B 1041
REMARK 465 ASN B 1042
REMARK 465 ARG B 1043
REMARK 465 GLN B 1044
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 LEU A 452 CG CD1 CD2
REMARK 470 LEU B 452 CG CD1 CD2
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 LYS A 111 -36.73 -142.12
REMARK 500 ASN A 187 -24.59 96.94
REMARK 500 ALA A 189 118.66 -164.68
REMARK 500 ILE A 418 -60.90 -108.21
REMARK 500 ASP A 430 -7.82 76.81
REMARK 500 MET A 534 32.76 -95.01
REMARK 500 GLU A 742 -94.24 -76.14
REMARK 500 LYS A 755 -76.78 27.44
REMARK 500 ASP A 911 85.54 53.53
REMARK 500 LEU A 989 85.48 -153.49
REMARK 500 SER A 990 -31.06 -142.95
REMARK 500 SER B 174 149.07 -179.99
REMARK 500 ILE B 328 -86.18 -80.99
REMARK 500 ARG B 331 57.24 -144.54
REMARK 500 LYS B 340 -168.58 -113.63
REMARK 500 GLU B 368 77.87 -118.78
REMARK 500 LYS B 372 14.20 52.69
REMARK 500 ASP B 378 44.68 -82.18
REMARK 500 ILE B 418 -60.90 -108.38
REMARK 500 ASP B 430 -7.80 76.77
REMARK 500 MET B 534 32.88 -95.10
REMARK 500 GLU B 742 -87.72 -84.13
REMARK 500 LYS B 755 -88.14 52.30
REMARK 500 ASP B 911 81.89 54.75
REMARK 500 LEU B 989 85.54 -153.38
REMARK 500 SER B 990 -31.01 -142.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2078 DISTANCE = 7.88 ANGSTROMS
REMARK 525 HOH B2061 DISTANCE = 8.02 ANGSTROMS
REMARK 525 HOH B2062 DISTANCE = 8.17 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J82 A 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J82 B 1500
DBREF 4V0I A 106 1044 UNP O35904 PK3CD_MOUSE 106 1043
DBREF 4V0I B 106 1044 UNP O35904 PK3CD_MOUSE 106 1043
SEQADV 4V0I GLY A 105 UNP O35904 EXPRESSION TAG
SEQADV 4V0I GLY B 105 UNP O35904 EXPRESSION TAG
SEQRES 1 A 940 GLY GLY ASP ARG VAL LYS LYS LEU ILE ASN SER GLN ILE
SEQRES 2 A 940 SER LEU LEU ILE GLY LYS GLY LEU HIS GLU PHE ASP SER
SEQRES 3 A 940 LEU ARG ASP PRO GLU VAL ASN ASP PHE ARG THR LYS MET
SEQRES 4 A 940 ARG GLN PHE CYS GLU GLU ALA ALA ALA HIS ARG GLN GLN
SEQRES 5 A 940 LEU GLY TRP VAL GLU TRP LEU GLN TYR SER PHE PRO LEU
SEQRES 6 A 940 GLN LEU GLU PRO SER ALA ARG GLY TRP ARG ALA GLY LEU
SEQRES 7 A 940 LEU ARG VAL SER ASN ARG ALA LEU LEU VAL ASN VAL LYS
SEQRES 8 A 940 PHE GLU GLY SER GLU GLU SER PHE THR PHE GLN VAL SER
SEQRES 9 A 940 THR LYS ASP MET PRO LEU ALA LEU MET ALA CYS ALA LEU
SEQRES 10 A 940 ARG LYS LYS ALA THR VAL PHE ARG GLN PRO LEU VAL GLU
SEQRES 11 A 940 GLN PRO GLU GLU TYR ALA LEU GLN VAL ASN GLY ARG HIS
SEQRES 12 A 940 GLU TYR LEU TYR GLY ASN TYR PRO LEU CYS HIS PHE GLN
SEQRES 13 A 940 TYR ILE CYS SER CYS LEU HIS SER GLY LEU THR PRO HIS
SEQRES 14 A 940 LEU THR MET VAL HIS SER SER SER ILE LEU ALA MET ARG
SEQRES 15 A 940 ASP GLU GLN SER ASN PRO ALA PRO GLN VAL GLN LYS PRO
SEQRES 16 A 940 ARG ALA LYS PRO PRO PRO ILE PRO ALA LYS LYS PRO SER
SEQRES 17 A 940 SER VAL SER LEU TRP SER LEU GLU GLN PRO PHE SER ILE
SEQRES 18 A 940 GLU LEU ILE GLU GLY ARG LYS VAL ASN ALA ASP GLU ARG
SEQRES 19 A 940 MET LYS LEU VAL VAL GLN ALA GLY LEU PHE HIS GLY ASN
SEQRES 20 A 940 GLU MET LEU CYS LYS THR VAL SER SER SER GLU VAL ASN
SEQRES 21 A 940 VAL CYS SER GLU PRO VAL TRP LYS GLN ARG LEU GLU PHE
SEQRES 22 A 940 ASP ILE SER VAL CYS ASP LEU PRO ARG MET ALA ARG LEU
SEQRES 23 A 940 CYS PHE ALA LEU TYR ALA VAL VAL GLU LYS ALA LYS LYS
SEQRES 24 A 940 ALA ARG SER THR LYS LYS LYS SER LYS LYS ALA ASP CYS
SEQRES 25 A 940 PRO ILE ALA TRP ALA ASN LEU MET LEU PHE ASP TYR LYS
SEQRES 26 A 940 ASP GLN LEU LYS THR GLY GLU ARG CYS LEU TYR MET TRP
SEQRES 27 A 940 PRO SER VAL PRO ASP GLU LYS GLY GLU LEU LEU ASN PRO
SEQRES 28 A 940 ALA GLY THR VAL ARG GLY ASN PRO ASN THR GLU SER ALA
SEQRES 29 A 940 ALA ALA LEU VAL ILE TYR LEU PRO GLU VAL ALA PRO HIS
SEQRES 30 A 940 PRO VAL TYR PHE PRO ALA LEU GLU LYS ILE LEU GLU LEU
SEQRES 31 A 940 GLY ARG HIS GLY GLU ARG GLY ARG ILE THR GLU GLU GLU
SEQRES 32 A 940 GLN LEU GLN LEU ARG GLU ILE LEU GLU ARG ARG GLY SER
SEQRES 33 A 940 GLY GLU LEU TYR GLU HIS GLU LYS ASP LEU VAL TRP LYS
SEQRES 34 A 940 MET ARG HIS GLU VAL GLN GLU HIS PHE PRO GLU ALA LEU
SEQRES 35 A 940 ALA ARG LEU LEU LEU VAL THR LYS TRP ASN LYS HIS GLU
SEQRES 36 A 940 ASP VAL ALA GLN MET LEU TYR LEU LEU CYS SER TRP PRO
SEQRES 37 A 940 GLU LEU PRO VAL LEU SER ALA LEU GLU LEU LEU ASP PHE
SEQRES 38 A 940 SER PHE PRO ASP CYS TYR VAL GLY SER PHE ALA ILE LYS
SEQRES 39 A 940 SER LEU ARG LYS LEU THR ASP ASP GLU LEU PHE GLN TYR
SEQRES 40 A 940 LEU LEU GLN LEU VAL GLN VAL LEU LYS TYR GLU SER TYR
SEQRES 41 A 940 LEU ASP CYS GLU LEU THR LYS PHE LEU LEU GLY ARG ALA
SEQRES 42 A 940 LEU ALA ASN ARG LYS ILE GLY HIS PHE LEU PHE TRP HIS
SEQRES 43 A 940 LEU ARG SER GLU MET HIS VAL PRO SER VAL ALA LEU ARG
SEQRES 44 A 940 PHE GLY LEU ILE MET GLU ALA TYR CYS ARG GLY SER THR
SEQRES 45 A 940 HIS HIS MET LYS VAL LEU MET LYS GLN GLY GLU ALA LEU
SEQRES 46 A 940 SER LYS LEU LYS ALA LEU ASN ASP PHE VAL LYS VAL SER
SEQRES 47 A 940 SER GLN LYS THR THR LYS PRO GLN THR LYS GLU MET MET
SEQRES 48 A 940 HIS MET CYS MET ARG GLN GLU THR TYR MET GLU ALA LEU
SEQRES 49 A 940 SER HIS LEU GLN SER PRO LEU ASP PRO SER THR LEU LEU
SEQRES 50 A 940 GLU GLU VAL CYS VAL GLU GLN CYS THR PHE MET ASP SER
SEQRES 51 A 940 LYS MET LYS PRO LEU TRP ILE MET TYR SER SER GLU GLU
SEQRES 52 A 940 ALA GLY SER ALA GLY ASN VAL GLY ILE ILE PHE LYS ASN
SEQRES 53 A 940 GLY ASP ASP LEU ARG GLN ASP MET LEU THR LEU GLN MET
SEQRES 54 A 940 ILE GLN LEU MET ASP VAL LEU TRP LYS GLN GLU GLY LEU
SEQRES 55 A 940 ASP LEU ARG MET THR PRO TYR GLY CYS LEU PRO THR GLY
SEQRES 56 A 940 ASP ARG THR GLY LEU ILE GLU VAL VAL LEU HIS SER ASP
SEQRES 57 A 940 THR ILE ALA ASN ILE GLN LEU ASN LYS SER ASN MET ALA
SEQRES 58 A 940 ALA THR ALA ALA PHE ASN LYS ASP ALA LEU LEU ASN TRP
SEQRES 59 A 940 LEU LYS SER LYS ASN PRO GLY GLU ALA LEU ASP ARG ALA
SEQRES 60 A 940 ILE GLU GLU PHE THR LEU SER CYS ALA GLY TYR CYS VAL
SEQRES 61 A 940 ALA THR TYR VAL LEU GLY ILE GLY ASP ARG HIS SER ASP
SEQRES 62 A 940 ASN ILE MET ILE ARG GLU SER GLY GLN LEU PHE HIS ILE
SEQRES 63 A 940 ASP PHE GLY HIS PHE LEU GLY ASN PHE LYS THR LYS PHE
SEQRES 64 A 940 GLY ILE ASN ARG GLU ARG VAL PRO PHE ILE LEU THR TYR
SEQRES 65 A 940 ASP PHE VAL HIS VAL ILE GLN GLN GLY LYS THR ASN ASN
SEQRES 66 A 940 SER GLU LYS PHE GLU ARG PHE ARG GLY TYR CYS GLU ARG
SEQRES 67 A 940 ALA TYR THR ILE LEU ARG ARG HIS GLY LEU LEU PHE LEU
SEQRES 68 A 940 HIS LEU PHE ALA LEU MET ARG ALA ALA GLY LEU PRO GLU
SEQRES 69 A 940 LEU SER CYS SER LYS ASP ILE GLN TYR LEU LYS ASP SER
SEQRES 70 A 940 LEU ALA LEU GLY LYS THR GLU GLU GLU ALA LEU LYS HIS
SEQRES 71 A 940 PHE ARG VAL LYS PHE ASN GLU ALA LEU ARG GLU SER TRP
SEQRES 72 A 940 LYS THR LYS VAL ASN TRP LEU ALA HIS ASN VAL SER LYS
SEQRES 73 A 940 ASP ASN ARG GLN
SEQRES 1 B 940 GLY GLY ASP ARG VAL LYS LYS LEU ILE ASN SER GLN ILE
SEQRES 2 B 940 SER LEU LEU ILE GLY LYS GLY LEU HIS GLU PHE ASP SER
SEQRES 3 B 940 LEU ARG ASP PRO GLU VAL ASN ASP PHE ARG THR LYS MET
SEQRES 4 B 940 ARG GLN PHE CYS GLU GLU ALA ALA ALA HIS ARG GLN GLN
SEQRES 5 B 940 LEU GLY TRP VAL GLU TRP LEU GLN TYR SER PHE PRO LEU
SEQRES 6 B 940 GLN LEU GLU PRO SER ALA ARG GLY TRP ARG ALA GLY LEU
SEQRES 7 B 940 LEU ARG VAL SER ASN ARG ALA LEU LEU VAL ASN VAL LYS
SEQRES 8 B 940 PHE GLU GLY SER GLU GLU SER PHE THR PHE GLN VAL SER
SEQRES 9 B 940 THR LYS ASP MET PRO LEU ALA LEU MET ALA CYS ALA LEU
SEQRES 10 B 940 ARG LYS LYS ALA THR VAL PHE ARG GLN PRO LEU VAL GLU
SEQRES 11 B 940 GLN PRO GLU GLU TYR ALA LEU GLN VAL ASN GLY ARG HIS
SEQRES 12 B 940 GLU TYR LEU TYR GLY ASN TYR PRO LEU CYS HIS PHE GLN
SEQRES 13 B 940 TYR ILE CYS SER CYS LEU HIS SER GLY LEU THR PRO HIS
SEQRES 14 B 940 LEU THR MET VAL HIS SER SER SER ILE LEU ALA MET ARG
SEQRES 15 B 940 ASP GLU GLN SER ASN PRO ALA PRO GLN VAL GLN LYS PRO
SEQRES 16 B 940 ARG ALA LYS PRO PRO PRO ILE PRO ALA LYS LYS PRO SER
SEQRES 17 B 940 SER VAL SER LEU TRP SER LEU GLU GLN PRO PHE SER ILE
SEQRES 18 B 940 GLU LEU ILE GLU GLY ARG LYS VAL ASN ALA ASP GLU ARG
SEQRES 19 B 940 MET LYS LEU VAL VAL GLN ALA GLY LEU PHE HIS GLY ASN
SEQRES 20 B 940 GLU MET LEU CYS LYS THR VAL SER SER SER GLU VAL ASN
SEQRES 21 B 940 VAL CYS SER GLU PRO VAL TRP LYS GLN ARG LEU GLU PHE
SEQRES 22 B 940 ASP ILE SER VAL CYS ASP LEU PRO ARG MET ALA ARG LEU
SEQRES 23 B 940 CYS PHE ALA LEU TYR ALA VAL VAL GLU LYS ALA LYS LYS
SEQRES 24 B 940 ALA ARG SER THR LYS LYS LYS SER LYS LYS ALA ASP CYS
SEQRES 25 B 940 PRO ILE ALA TRP ALA ASN LEU MET LEU PHE ASP TYR LYS
SEQRES 26 B 940 ASP GLN LEU LYS THR GLY GLU ARG CYS LEU TYR MET TRP
SEQRES 27 B 940 PRO SER VAL PRO ASP GLU LYS GLY GLU LEU LEU ASN PRO
SEQRES 28 B 940 ALA GLY THR VAL ARG GLY ASN PRO ASN THR GLU SER ALA
SEQRES 29 B 940 ALA ALA LEU VAL ILE TYR LEU PRO GLU VAL ALA PRO HIS
SEQRES 30 B 940 PRO VAL TYR PHE PRO ALA LEU GLU LYS ILE LEU GLU LEU
SEQRES 31 B 940 GLY ARG HIS GLY GLU ARG GLY ARG ILE THR GLU GLU GLU
SEQRES 32 B 940 GLN LEU GLN LEU ARG GLU ILE LEU GLU ARG ARG GLY SER
SEQRES 33 B 940 GLY GLU LEU TYR GLU HIS GLU LYS ASP LEU VAL TRP LYS
SEQRES 34 B 940 MET ARG HIS GLU VAL GLN GLU HIS PHE PRO GLU ALA LEU
SEQRES 35 B 940 ALA ARG LEU LEU LEU VAL THR LYS TRP ASN LYS HIS GLU
SEQRES 36 B 940 ASP VAL ALA GLN MET LEU TYR LEU LEU CYS SER TRP PRO
SEQRES 37 B 940 GLU LEU PRO VAL LEU SER ALA LEU GLU LEU LEU ASP PHE
SEQRES 38 B 940 SER PHE PRO ASP CYS TYR VAL GLY SER PHE ALA ILE LYS
SEQRES 39 B 940 SER LEU ARG LYS LEU THR ASP ASP GLU LEU PHE GLN TYR
SEQRES 40 B 940 LEU LEU GLN LEU VAL GLN VAL LEU LYS TYR GLU SER TYR
SEQRES 41 B 940 LEU ASP CYS GLU LEU THR LYS PHE LEU LEU GLY ARG ALA
SEQRES 42 B 940 LEU ALA ASN ARG LYS ILE GLY HIS PHE LEU PHE TRP HIS
SEQRES 43 B 940 LEU ARG SER GLU MET HIS VAL PRO SER VAL ALA LEU ARG
SEQRES 44 B 940 PHE GLY LEU ILE MET GLU ALA TYR CYS ARG GLY SER THR
SEQRES 45 B 940 HIS HIS MET LYS VAL LEU MET LYS GLN GLY GLU ALA LEU
SEQRES 46 B 940 SER LYS LEU LYS ALA LEU ASN ASP PHE VAL LYS VAL SER
SEQRES 47 B 940 SER GLN LYS THR THR LYS PRO GLN THR LYS GLU MET MET
SEQRES 48 B 940 HIS MET CYS MET ARG GLN GLU THR TYR MET GLU ALA LEU
SEQRES 49 B 940 SER HIS LEU GLN SER PRO LEU ASP PRO SER THR LEU LEU
SEQRES 50 B 940 GLU GLU VAL CYS VAL GLU GLN CYS THR PHE MET ASP SER
SEQRES 51 B 940 LYS MET LYS PRO LEU TRP ILE MET TYR SER SER GLU GLU
SEQRES 52 B 940 ALA GLY SER ALA GLY ASN VAL GLY ILE ILE PHE LYS ASN
SEQRES 53 B 940 GLY ASP ASP LEU ARG GLN ASP MET LEU THR LEU GLN MET
SEQRES 54 B 940 ILE GLN LEU MET ASP VAL LEU TRP LYS GLN GLU GLY LEU
SEQRES 55 B 940 ASP LEU ARG MET THR PRO TYR GLY CYS LEU PRO THR GLY
SEQRES 56 B 940 ASP ARG THR GLY LEU ILE GLU VAL VAL LEU HIS SER ASP
SEQRES 57 B 940 THR ILE ALA ASN ILE GLN LEU ASN LYS SER ASN MET ALA
SEQRES 58 B 940 ALA THR ALA ALA PHE ASN LYS ASP ALA LEU LEU ASN TRP
SEQRES 59 B 940 LEU LYS SER LYS ASN PRO GLY GLU ALA LEU ASP ARG ALA
SEQRES 60 B 940 ILE GLU GLU PHE THR LEU SER CYS ALA GLY TYR CYS VAL
SEQRES 61 B 940 ALA THR TYR VAL LEU GLY ILE GLY ASP ARG HIS SER ASP
SEQRES 62 B 940 ASN ILE MET ILE ARG GLU SER GLY GLN LEU PHE HIS ILE
SEQRES 63 B 940 ASP PHE GLY HIS PHE LEU GLY ASN PHE LYS THR LYS PHE
SEQRES 64 B 940 GLY ILE ASN ARG GLU ARG VAL PRO PHE ILE LEU THR TYR
SEQRES 65 B 940 ASP PHE VAL HIS VAL ILE GLN GLN GLY LYS THR ASN ASN
SEQRES 66 B 940 SER GLU LYS PHE GLU ARG PHE ARG GLY TYR CYS GLU ARG
SEQRES 67 B 940 ALA TYR THR ILE LEU ARG ARG HIS GLY LEU LEU PHE LEU
SEQRES 68 B 940 HIS LEU PHE ALA LEU MET ARG ALA ALA GLY LEU PRO GLU
SEQRES 69 B 940 LEU SER CYS SER LYS ASP ILE GLN TYR LEU LYS ASP SER
SEQRES 70 B 940 LEU ALA LEU GLY LYS THR GLU GLU GLU ALA LEU LYS HIS
SEQRES 71 B 940 PHE ARG VAL LYS PHE ASN GLU ALA LEU ARG GLU SER TRP
SEQRES 72 B 940 LYS THR LYS VAL ASN TRP LEU ALA HIS ASN VAL SER LYS
SEQRES 73 B 940 ASP ASN ARG GLN
HET J82 A1500 26
HET J82 B1500 26
HETNAM J82 2-[2-(2-METHYL-2,3-DIHYDRO-INDOL-1-YL)-2-OXO-ETHYL]-6-
HETNAM 2 J82 MORPHOLIN-4-YL-3H-PYRIMIDIN-4-ONE
FORMUL 3 J82 2(C19 H22 N4 O3)
FORMUL 5 HOH *140(H2 O)
HELIX 1 1 LEU A 112 GLY A 122 1 11
HELIX 2 2 LEU A 125 SER A 130 1 6
HELIX 3 3 ASP A 133 GLN A 155 1 23
HELIX 4 4 GLY A 158 PHE A 167 1 10
HELIX 5 5 MET A 212 VAL A 227 1 16
HELIX 6 6 GLN A 235 GLU A 237 5 3
HELIX 7 7 PRO A 255 HIS A 258 5 4
HELIX 8 8 PHE A 259 HIS A 267 1 9
HELIX 9 9 SER A 279 GLN A 289 1 11
HELIX 10 10 ALA A 487 LEU A 494 1 8
HELIX 11 11 GLU A 525 MET A 534 1 10
HELIX 12 12 MET A 534 PHE A 542 1 9
HELIX 13 13 ALA A 545 THR A 553 1 9
HELIX 14 14 LYS A 557 SER A 570 1 14
HELIX 15 15 PRO A 575 LEU A 582 1 8
HELIX 16 16 ASP A 589 SER A 599 1 11
HELIX 17 17 THR A 604 LEU A 619 1 16
HELIX 18 18 CYS A 627 ASN A 640 1 14
HELIX 19 19 ASN A 640 SER A 653 1 14
HELIX 20 20 VAL A 657 SER A 675 1 19
HELIX 21 21 SER A 675 THR A 706 1 32
HELIX 22 22 THR A 707 ARG A 720 1 14
HELIX 23 23 GLN A 721 SER A 729 1 9
HELIX 24 24 VAL A 746 CYS A 749 5 4
HELIX 25 25 LEU A 784 GLN A 803 1 20
HELIX 26 26 ILE A 834 LEU A 839 1 6
HELIX 27 27 PHE A 850 LYS A 852 5 3
HELIX 28 28 ASP A 853 ASN A 863 1 11
HELIX 29 29 GLU A 866 GLY A 890 1 25
HELIX 30 30 THR A 935 GLN A 943 1 9
HELIX 31 31 ASN A 949 ARG A 969 1 21
HELIX 32 32 HIS A 970 MET A 981 1 12
HELIX 33 33 CYS A 991 LEU A 1002 1 12
HELIX 34 34 THR A 1007 GLU A 1025 1 19
HELIX 35 35 LEU B 112 GLY B 122 1 11
HELIX 36 36 LEU B 125 SER B 130 1 6
HELIX 37 37 ASP B 133 GLN B 155 1 23
HELIX 38 38 GLY B 158 PHE B 167 1 10
HELIX 39 39 MET B 212 VAL B 227 1 16
HELIX 40 40 GLN B 235 GLU B 237 5 3
HELIX 41 41 PRO B 255 HIS B 258 5 4
HELIX 42 42 PHE B 259 HIS B 267 1 9
HELIX 43 43 SER B 279 GLN B 289 1 11
HELIX 44 44 ALA B 487 LEU B 494 1 8
HELIX 45 45 GLU B 525 MET B 534 1 10
HELIX 46 46 MET B 534 PHE B 542 1 9
HELIX 47 47 ALA B 545 THR B 553 1 9
HELIX 48 48 LYS B 557 SER B 570 1 14
HELIX 49 49 PRO B 575 LEU B 582 1 8
HELIX 50 50 ASP B 589 SER B 599 1 11
HELIX 51 51 THR B 604 LEU B 619 1 16
HELIX 52 52 CYS B 627 ASN B 640 1 14
HELIX 53 53 ASN B 640 SER B 653 1 14
HELIX 54 54 VAL B 660 SER B 675 1 16
HELIX 55 55 SER B 675 THR B 706 1 32
HELIX 56 56 THR B 707 ARG B 720 1 14
HELIX 57 57 GLN B 721 LEU B 728 1 8
HELIX 58 58 VAL B 746 CYS B 749 5 4
HELIX 59 59 LEU B 784 GLN B 803 1 20
HELIX 60 60 ILE B 834 LEU B 839 1 6
HELIX 61 61 PHE B 850 LYS B 852 5 3
HELIX 62 62 ASP B 853 ASN B 863 1 11
HELIX 63 63 GLU B 866 GLY B 890 1 25
HELIX 64 64 THR B 935 GLN B 943 1 9
HELIX 65 65 ASN B 949 ARG B 969 1 21
HELIX 66 66 HIS B 970 MET B 981 1 12
HELIX 67 67 CYS B 991 LEU B 1002 1 12
HELIX 68 68 THR B 1007 GLU B 1025 1 19
SHEET 1 AA 5 SER A 202 SER A 208 0
SHEET 2 AA 5 ALA A 189 PHE A 196 -1 O LEU A 190 N VAL A 207
SHEET 3 AA 5 HIS A 273 HIS A 278 1 O LEU A 274 N LYS A 195
SHEET 4 AA 5 TYR A 239 VAL A 243 -1 O ALA A 240 N VAL A 277
SHEET 5 AA 5 TYR A 249 LEU A 250 -1 O LEU A 250 N LEU A 241
SHEET 1 AB 3 GLU A 326 LEU A 327 0
SHEET 2 AB 3 VAL A 472 TYR A 474 -1 O TYR A 474 N GLU A 326
SHEET 3 AB 3 GLU A 436 CYS A 438 -1 O ARG A 437 N ILE A 473
SHEET 1 AC 5 GLU A 352 MET A 353 0
SHEET 2 AC 5 GLN A 344 HIS A 349 -1 N HIS A 349 O GLU A 352
SHEET 3 AC 5 ARG A 389 TYR A 395 -1 O ARG A 389 N PHE A 348
SHEET 4 AC 5 PRO A 417 MET A 424 -1 N ILE A 418 O LEU A 394
SHEET 5 AC 5 TRP A 442 PRO A 443 -1 O TRP A 442 N TRP A 420
SHEET 1 AD 2 LEU A 731 SER A 733 0
SHEET 2 AD 2 ASP A 736 LEU A 741 -1 N ASP A 736 O SER A 733
SHEET 1 AE 2 GLU A 743 VAL A 744 0
SHEET 2 AE 2 LEU A 759 SER A 765 -1 O SER A 764 N GLU A 743
SHEET 1 AF 2 THR A 750 PHE A 751 0
SHEET 2 AF 2 LEU A 759 SER A 765 -1 O TRP A 760 N THR A 750
SHEET 1 AG 5 CYS A 815 GLY A 819 0
SHEET 2 AG 5 THR A 822 GLU A 826 -1 O THR A 822 N THR A 818
SHEET 3 AG 5 GLY A 769 ASN A 780 -1 O ILE A 777 N ILE A 825
SHEET 4 AG 5 LEU A 759 SER A 765 -1 O LEU A 759 N PHE A 778
SHEET 5 AG 5 THR A 750 PHE A 751 -1 O THR A 750 N TRP A 760
SHEET 1 AH 5 CYS A 815 GLY A 819 0
SHEET 2 AH 5 THR A 822 GLU A 826 -1 O THR A 822 N THR A 818
SHEET 3 AH 5 GLY A 769 ASN A 780 -1 O ILE A 777 N ILE A 825
SHEET 4 AH 5 LEU A 759 SER A 765 -1 O LEU A 759 N PHE A 778
SHEET 5 AH 5 GLU A 743 VAL A 744 -1 O GLU A 743 N SER A 764
SHEET 1 AI 3 SER A 831 THR A 833 0
SHEET 2 AI 3 ILE A 899 ARG A 902 -1 O ILE A 901 N ASP A 832
SHEET 3 AI 3 LEU A 907 HIS A 909 -1 O PHE A 908 N MET A 900
SHEET 1 BA 5 SER B 202 GLN B 206 0
SHEET 2 BA 5 LEU B 191 PHE B 196 -1 O VAL B 192 N PHE B 205
SHEET 3 BA 5 HIS B 273 HIS B 278 1 O LEU B 274 N LYS B 195
SHEET 4 BA 5 TYR B 239 VAL B 243 -1 O ALA B 240 N VAL B 277
SHEET 5 BA 5 TYR B 249 LEU B 250 -1 O LEU B 250 N LEU B 241
SHEET 1 BB 4 VAL B 370 SER B 380 0
SHEET 2 BB 4 PRO B 322 GLY B 330 -1 O PHE B 323 N PHE B 377
SHEET 3 BB 4 LEU B 471 TYR B 474 -1 O VAL B 472 N ILE B 328
SHEET 4 BB 4 GLU B 436 CYS B 438 -1 O ARG B 437 N ILE B 473
SHEET 1 BC 2 GLU B 352 MET B 353 0
SHEET 2 BC 2 LYS B 340 HIS B 349 -1 N HIS B 349 O GLU B 352
SHEET 1 BD 2 VAL B 358 SER B 359 0
SHEET 2 BD 2 LYS B 340 HIS B 349 -1 O ALA B 345 N VAL B 358
SHEET 1 BE 2 VAL B 363 ASN B 364 0
SHEET 2 BE 2 LYS B 340 HIS B 349 -1 O LEU B 341 N VAL B 363
SHEET 1 BF 5 TRP B 442 PRO B 443 0
SHEET 2 BF 5 PRO B 417 MET B 424 -1 O TRP B 420 N TRP B 442
SHEET 3 BF 5 ARG B 389 TYR B 395 -1 O LEU B 390 N LEU B 423
SHEET 4 BF 5 LYS B 340 HIS B 349 -1 O VAL B 342 N TYR B 395
SHEET 5 BF 5 GLU B 352 MET B 353 -1 O GLU B 352 N HIS B 349
SHEET 1 BG 5 TRP B 442 PRO B 443 0
SHEET 2 BG 5 PRO B 417 MET B 424 -1 O TRP B 420 N TRP B 442
SHEET 3 BG 5 ARG B 389 TYR B 395 -1 O LEU B 390 N LEU B 423
SHEET 4 BG 5 LYS B 340 HIS B 349 -1 O VAL B 342 N TYR B 395
SHEET 5 BG 5 VAL B 358 SER B 359 -1 O VAL B 358 N ALA B 345
SHEET 1 BH 2 LEU B 731 SER B 733 0
SHEET 2 BH 2 ASP B 736 LEU B 741 -1 N ASP B 736 O SER B 733
SHEET 1 BI 2 GLU B 743 VAL B 744 0
SHEET 2 BI 2 LEU B 759 SER B 765 -1 O SER B 764 N GLU B 743
SHEET 1 BJ 2 THR B 750 PHE B 751 0
SHEET 2 BJ 2 LEU B 759 SER B 765 -1 O TRP B 760 N THR B 750
SHEET 1 BK 5 CYS B 815 GLY B 819 0
SHEET 2 BK 5 THR B 822 GLU B 826 -1 O THR B 822 N THR B 818
SHEET 3 BK 5 GLY B 769 ASN B 780 -1 O ILE B 777 N ILE B 825
SHEET 4 BK 5 LEU B 759 SER B 765 -1 O LEU B 759 N PHE B 778
SHEET 5 BK 5 THR B 750 PHE B 751 -1 O THR B 750 N TRP B 760
SHEET 1 BL 5 CYS B 815 GLY B 819 0
SHEET 2 BL 5 THR B 822 GLU B 826 -1 O THR B 822 N THR B 818
SHEET 3 BL 5 GLY B 769 ASN B 780 -1 O ILE B 777 N ILE B 825
SHEET 4 BL 5 LEU B 759 SER B 765 -1 O LEU B 759 N PHE B 778
SHEET 5 BL 5 GLU B 743 VAL B 744 -1 O GLU B 743 N SER B 764
SHEET 1 BM 3 SER B 831 THR B 833 0
SHEET 2 BM 3 ILE B 899 ARG B 902 -1 O ILE B 901 N ASP B 832
SHEET 3 BM 3 LEU B 907 HIS B 909 -1 O PHE B 908 N MET B 900
CISPEP 1 SER A 186 ASN A 187 0 0.21
CISPEP 2 THR A 434 GLY A 435 0 0.26
CISPEP 3 THR B 434 GLY B 435 0 0.28
SITE 1 AC1 14 PHE A 751 MET A 752 PRO A 758 TRP A 760
SITE 2 AC1 14 ILE A 777 LYS A 779 TYR A 813 GLU A 826
SITE 3 AC1 14 VAL A 827 VAL A 828 MET A 900 ILE A 910
SITE 4 AC1 14 ASP A 911 HOH A2054
SITE 1 AC2 13 PHE B 751 MET B 752 PRO B 758 TRP B 760
SITE 2 AC2 13 ILE B 777 LYS B 779 ILE B 825 GLU B 826
SITE 3 AC2 13 VAL B 827 VAL B 828 MET B 900 ILE B 910
SITE 4 AC2 13 ASP B 911
CRYST1 62.000 216.430 76.970 90.00 113.29 90.00 P 1 21 1 4
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 0.016129 0.000000 0.006943 0.00000
SCALE2 0.000000 0.004620 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014145 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
