HEADER TRANSFERASE/TRANSFERASE INHIBITOR 05-AUG-10 3OAW
TITLE 4-METHYLPTERIDINEONES AS ORALLY ACTIVE AND SELECTIVE PI3K/MTOR DUAL
TITLE 2 INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE 3-KINASE CATALYTIC
COMPND 3 SUBUNIT GAMMA ISOFORM;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: UNP RESIDUES 144-1102;
COMPND 6 SYNONYM: PTDINS-3-KINASE SUBUNIT GAMMA, PI3-KINASE SUBUNIT GAMMA,
COMPND 7 PI3K-GAMMA, PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE 3-KINASE 110 KDA
COMPND 8 CATALYTIC SUBUNIT GAMMA, PTDINS-3-KINASE SUBUNIT P110-GAMMA, P120-
COMPND 9 PI3K;
COMPND 10 EC: 2.7.1.153;
COMPND 11 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: PIK3CG;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS PHOSPHOINOSITIDE KINASE, TRANSFERASE-TRANSFERASE, INHIBITION,
KEYWDS 2 INHIBITOR COMPLEX., TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.KNIGHTON,S.E.GREASLEY,C.M.-L.RODGERS
REVDAT 3 21-FEB-24 3OAW 1 REMARK SEQADV
REVDAT 2 06-OCT-10 3OAW 1 JRNL
REVDAT 1 22-SEP-10 3OAW 0
JRNL AUTH K.K.LIU,S.BAGRODIA,S.BAILEY,H.CHENG,H.CHEN,L.GAO,S.GREASLEY,
JRNL AUTH 2 J.E.HOFFMAN,Q.HU,T.O.JOHNSON,D.KNIGHTON,Z.LIU,M.A.MARX,
JRNL AUTH 3 M.D.NAMBU,S.NINKOVIC,B.PASCUAL,K.RAFIDI,C.M.RODGERS,
JRNL AUTH 4 G.L.SMITH,S.SUN,H.WANG,A.YANG,J.YUAN,A.ZOU
JRNL TITL 4-METHYLPTERIDINONES AS ORALLY ACTIVE AND SELECTIVE
JRNL TITL 2 PI3K/MTOR DUAL INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 20 6096 2010
JRNL REFN ISSN 0960-894X
JRNL PMID 20817449
JRNL DOI 10.1016/J.BMCL.2010.08.045
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.5
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) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 25960
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1309
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 : 13
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.86
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.20
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2627
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2580
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2489
REMARK 3 BIN R VALUE (WORKING SET) : 0.2534
REMARK 3 BIN FREE R VALUE : 0.3412
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.25
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 138
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 : 6754
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 29
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 90.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 87.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.28190
REMARK 3 B22 (A**2) : -13.03130
REMARK 3 B33 (A**2) : 10.74940
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -8.50210
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.411
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.897
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6927 ; 2.000 ; NULL
REMARK 3 BOND ANGLES : 9381 ; 2.000 ; NULL
REMARK 3 TORSION ANGLES : 2430 ; 2.000 ; NULL
REMARK 3 TRIGONAL CARBON PLANES : 175 ; 2.000 ; NULL
REMARK 3 GENERAL PLANES : 978 ; 5.000 ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : 6927 ; 20.000 ; NULL
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 : 902 ; 5.000 ; NULL
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 : 7951 ; 4.000 ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.65
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 22.62
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3OAW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000060884.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : PH8.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94892
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.650
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.7900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: BUSTER 2.9.5
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PROPANE, 0.2M (NH4)2SO4,
REMARK 280 16-18% (W/V) PEG3350, 10% (V/V) ETHYLENE GLYCOL AND 10MM TCEP,
REMARK 280 PH PH8.2, VAPOR DIFFUSION, TEMPERATURE 286K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 71.37650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.83100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 71.37650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.83100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 143
REMARK 465 ALA A 253
REMARK 465 LYS A 254
REMARK 465 LYS A 255
REMARK 465 LYS A 256
REMARK 465 SER A 257
REMARK 465 LEU A 258
REMARK 465 MET A 259
REMARK 465 ASP A 260
REMARK 465 ILE A 261
REMARK 465 PRO A 262
REMARK 465 GLU A 263
REMARK 465 SER A 264
REMARK 465 GLN A 265
REMARK 465 SER A 266
REMARK 465 GLU A 267
REMARK 465 GLN A 268
REMARK 465 GLU A 322
REMARK 465 TRP A 323
REMARK 465 PRO A 324
REMARK 465 LEU A 325
REMARK 465 VAL A 326
REMARK 465 ASP A 327
REMARK 465 ASP A 328
REMARK 465 CYS A 329
REMARK 465 THR A 330
REMARK 465 GLY A 331
REMARK 465 VAL A 332
REMARK 465 THR A 333
REMARK 465 GLY A 334
REMARK 465 TYR A 335
REMARK 465 HIS A 336
REMARK 465 GLU A 337
REMARK 465 GLN A 338
REMARK 465 LEU A 339
REMARK 465 THR A 340
REMARK 465 ILE A 341
REMARK 465 HIS A 342
REMARK 465 GLY A 343
REMARK 465 LYS A 344
REMARK 465 ASP A 345
REMARK 465 HIS A 346
REMARK 465 GLU A 347
REMARK 465 SER A 348
REMARK 465 VAL A 349
REMARK 465 PHE A 350
REMARK 465 THR A 351
REMARK 465 VAL A 352
REMARK 465 PRO A 374
REMARK 465 ARG A 375
REMARK 465 ASN A 376
REMARK 465 THR A 377
REMARK 465 ASP A 378
REMARK 465 GLY A 436
REMARK 465 LYS A 437
REMARK 465 ALA A 438
REMARK 465 PRO A 439
REMARK 465 ALA A 440
REMARK 465 LEU A 441
REMARK 465 SER A 442
REMARK 465 SER A 443
REMARK 465 LYS A 444
REMARK 465 ALA A 445
REMARK 465 SER A 446
REMARK 465 ALA A 447
REMARK 465 GLU A 448
REMARK 465 SER A 449
REMARK 465 PRO A 450
REMARK 465 SER A 451
REMARK 465 SER A 452
REMARK 465 GLU A 453
REMARK 465 SER A 454
REMARK 465 LYS A 455
REMARK 465 GLY A 456
REMARK 465 LYS A 457
REMARK 465 LYS A 490
REMARK 465 GLY A 491
REMARK 465 GLU A 492
REMARK 465 ASP A 493
REMARK 465 GLN A 494
REMARK 465 GLY A 495
REMARK 465 SER A 496
REMARK 465 LYS A 531
REMARK 465 HIS A 532
REMARK 465 GLN A 533
REMARK 465 PRO A 534
REMARK 465 THR A 535
REMARK 465 PRO A 536
REMARK 465 ASP A 537
REMARK 465 PRO A 538
REMARK 465 GLU A 539
REMARK 465 GLY A 540
REMARK 465 ASP A 541
REMARK 465 ARG A 542
REMARK 465 VAL A 543
REMARK 465 ALA A 754
REMARK 465 GLU A 755
REMARK 465 LYS A 756
REMARK 465 TYR A 757
REMARK 465 ASP A 758
REMARK 465 VAL A 759
REMARK 465 LYS A 973
REMARK 465 SER A 974
REMARK 465 PHE A 975
REMARK 465 LEU A 976
REMARK 465 GLY A 977
REMARK 465 ILE A 978
REMARK 465 ASN A 979
REMARK 465 LYS A 980
REMARK 465 GLU A 981
REMARK 465 ILE A 1094
REMARK 465 LYS A 1095
REMARK 465 GLN A 1096
REMARK 465 GLY A 1097
REMARK 465 GLU A 1098
REMARK 465 LYS A 1099
REMARK 465 HIS A 1100
REMARK 465 SER A 1101
REMARK 465 ALA A 1102
REMARK 465 HIS A 1103
REMARK 465 HIS A 1104
REMARK 465 HIS A 1105
REMARK 465 HIS A 1106
REMARK 465 HIS A 1107
REMARK 465 HIS A 1108
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 226 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 270 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 459 CG CD OE1 NE2
REMARK 470 ARG A 477 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 522 CG OD1 ND2
REMARK 470 TYR A 523 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 CYS A 524 SG
REMARK 470 HIS A 525 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 768 CG CD CE NZ
REMARK 470 GLN A 778 CG CD OE1 NE2
REMARK 470 TYR A 972 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 982 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1000 CG CD CE NZ
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 ASP A 164 97.76 -40.97
REMARK 500 ASP A 171 36.72 -97.86
REMARK 500 HIS A 199 56.84 36.20
REMARK 500 ASN A 217 86.21 -173.78
REMARK 500 ARG A 226 -76.00 -160.61
REMARK 500 SER A 227 -61.36 -122.93
REMARK 500 PHE A 248 -27.91 -151.20
REMARK 500 GLU A 284 87.00 -69.22
REMARK 500 GLN A 391 -13.20 72.41
REMARK 500 TRP A 410 -44.14 -132.40
REMARK 500 PHE A 473 14.12 80.25
REMARK 500 ASP A 509 93.08 -63.53
REMARK 500 ASP A 521 104.88 -33.57
REMARK 500 ASN A 522 37.95 -81.25
REMARK 500 TYR A 523 -109.65 -14.86
REMARK 500 HIS A 525 -54.44 -122.33
REMARK 500 PRO A 526 92.81 -11.89
REMARK 500 ALA A 545 -150.00 -104.13
REMARK 500 ALA A 560 45.46 -91.54
REMARK 500 PHE A 578 42.32 -91.86
REMARK 500 GLU A 615 -59.67 -9.25
REMARK 500 SER A 777 -45.53 -152.74
REMARK 500 ALA A 797 52.93 -103.55
REMARK 500 ILE A 798 -52.87 -21.89
REMARK 500 LEU A 823 4.55 -69.42
REMARK 500 CYS A 863 43.03 38.89
REMARK 500 LEU A 865 76.70 -114.96
REMARK 500 LYS A 875 16.14 54.06
REMARK 500 SER A 894 -70.53 -69.33
REMARK 500 VAL A 896 -93.26 -135.24
REMARK 500 GLU A 956 -6.80 -54.50
REMARK 500 GLN A1041 -27.22 67.24
REMARK 500 THR A1043 -84.37 -117.76
REMARK 500 SER A1044 -26.63 56.57
REMARK 500 LYS A1045 -30.29 98.40
REMARK 500 LEU A1092 -70.47 -108.85
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 OAW A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ML9 RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH SMALL MOLECULE.
REMARK 900 RELATED ID: 3ML8 RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH SMALL MOLECULE.
DBREF 3OAW A 144 1102 UNP P48736 PK3CG_HUMAN 144 1102
SEQADV 3OAW MET A 143 UNP P48736 INITIATING METHIONINE
SEQADV 3OAW HIS A 1103 UNP P48736 EXPRESSION TAG
SEQADV 3OAW HIS A 1104 UNP P48736 EXPRESSION TAG
SEQADV 3OAW HIS A 1105 UNP P48736 EXPRESSION TAG
SEQADV 3OAW HIS A 1106 UNP P48736 EXPRESSION TAG
SEQADV 3OAW HIS A 1107 UNP P48736 EXPRESSION TAG
SEQADV 3OAW HIS A 1108 UNP P48736 EXPRESSION TAG
SEQRES 1 A 966 MET SER GLU GLU SER GLN ALA PHE GLN ARG GLN LEU THR
SEQRES 2 A 966 ALA LEU ILE GLY TYR ASP VAL THR ASP VAL SER ASN VAL
SEQRES 3 A 966 HIS ASP ASP GLU LEU GLU PHE THR ARG ARG GLY LEU VAL
SEQRES 4 A 966 THR PRO ARG MET ALA GLU VAL ALA SER ARG ASP PRO LYS
SEQRES 5 A 966 LEU TYR ALA MET HIS PRO TRP VAL THR SER LYS PRO LEU
SEQRES 6 A 966 PRO GLU TYR LEU TRP LYS LYS ILE ALA ASN ASN CYS ILE
SEQRES 7 A 966 PHE ILE VAL ILE HIS ARG SER THR THR SER GLN THR ILE
SEQRES 8 A 966 LYS VAL SER PRO ASP ASP THR PRO GLY ALA ILE LEU GLN
SEQRES 9 A 966 SER PHE PHE THR LYS MET ALA LYS LYS LYS SER LEU MET
SEQRES 10 A 966 ASP ILE PRO GLU SER GLN SER GLU GLN ASP PHE VAL LEU
SEQRES 11 A 966 ARG VAL CYS GLY ARG ASP GLU TYR LEU VAL GLY GLU THR
SEQRES 12 A 966 PRO ILE LYS ASN PHE GLN TRP VAL ARG HIS CYS LEU LYS
SEQRES 13 A 966 ASN GLY GLU GLU ILE HIS VAL VAL LEU ASP THR PRO PRO
SEQRES 14 A 966 ASP PRO ALA LEU ASP GLU VAL ARG LYS GLU GLU TRP PRO
SEQRES 15 A 966 LEU VAL ASP ASP CYS THR GLY VAL THR GLY TYR HIS GLU
SEQRES 16 A 966 GLN LEU THR ILE HIS GLY LYS ASP HIS GLU SER VAL PHE
SEQRES 17 A 966 THR VAL SER LEU TRP ASP CYS ASP ARG LYS PHE ARG VAL
SEQRES 18 A 966 LYS ILE ARG GLY ILE ASP ILE PRO VAL LEU PRO ARG ASN
SEQRES 19 A 966 THR ASP LEU THR VAL PHE VAL GLU ALA ASN ILE GLN HIS
SEQRES 20 A 966 GLY GLN GLN VAL LEU CYS GLN ARG ARG THR SER PRO LYS
SEQRES 21 A 966 PRO PHE THR GLU GLU VAL LEU TRP ASN VAL TRP LEU GLU
SEQRES 22 A 966 PHE SER ILE LYS ILE LYS ASP LEU PRO LYS GLY ALA LEU
SEQRES 23 A 966 LEU ASN LEU GLN ILE TYR CYS GLY LYS ALA PRO ALA LEU
SEQRES 24 A 966 SER SER LYS ALA SER ALA GLU SER PRO SER SER GLU SER
SEQRES 25 A 966 LYS GLY LYS VAL GLN LEU LEU TYR TYR VAL ASN LEU LEU
SEQRES 26 A 966 LEU ILE ASP HIS ARG PHE LEU LEU ARG ARG GLY GLU TYR
SEQRES 27 A 966 VAL LEU HIS MET TRP GLN ILE SER GLY LYS GLY GLU ASP
SEQRES 28 A 966 GLN GLY SER PHE ASN ALA ASP LYS LEU THR SER ALA THR
SEQRES 29 A 966 ASN PRO ASP LYS GLU ASN SER MET SER ILE SER ILE LEU
SEQRES 30 A 966 LEU ASP ASN TYR CYS HIS PRO ILE ALA LEU PRO LYS HIS
SEQRES 31 A 966 GLN PRO THR PRO ASP PRO GLU GLY ASP ARG VAL ARG ALA
SEQRES 32 A 966 GLU MET PRO ASN GLN LEU ARG LYS GLN LEU GLU ALA ILE
SEQRES 33 A 966 ILE ALA THR ASP PRO LEU ASN PRO LEU THR ALA GLU ASP
SEQRES 34 A 966 LYS GLU LEU LEU TRP HIS PHE ARG TYR GLU SER LEU LYS
SEQRES 35 A 966 HIS PRO LYS ALA TYR PRO LYS LEU PHE SER SER VAL LYS
SEQRES 36 A 966 TRP GLY GLN GLN GLU ILE VAL ALA LYS THR TYR GLN LEU
SEQRES 37 A 966 LEU ALA ARG ARG GLU VAL TRP ASP GLN SER ALA LEU ASP
SEQRES 38 A 966 VAL GLY LEU THR MET GLN LEU LEU ASP CYS ASN PHE SER
SEQRES 39 A 966 ASP GLU ASN VAL ARG ALA ILE ALA VAL GLN LYS LEU GLU
SEQRES 40 A 966 SER LEU GLU ASP ASP ASP VAL LEU HIS TYR LEU LEU GLN
SEQRES 41 A 966 LEU VAL GLN ALA VAL LYS PHE GLU PRO TYR HIS ASP SER
SEQRES 42 A 966 ALA LEU ALA ARG PHE LEU LEU LYS ARG GLY LEU ARG ASN
SEQRES 43 A 966 LYS ARG ILE GLY HIS PHE LEU PHE TRP PHE LEU ARG SER
SEQRES 44 A 966 GLU ILE ALA GLN SER ARG HIS TYR GLN GLN ARG PHE ALA
SEQRES 45 A 966 VAL ILE LEU GLU ALA TYR LEU ARG GLY CYS GLY THR ALA
SEQRES 46 A 966 MET LEU HIS ASP PHE THR GLN GLN VAL GLN VAL ILE GLU
SEQRES 47 A 966 MET LEU GLN LYS VAL THR LEU ASP ILE LYS SER LEU SER
SEQRES 48 A 966 ALA GLU LYS TYR ASP VAL SER SER GLN VAL ILE SER GLN
SEQRES 49 A 966 LEU LYS GLN LYS LEU GLU ASN LEU GLN ASN SER GLN LEU
SEQRES 50 A 966 PRO GLU SER PHE ARG VAL PRO TYR ASP PRO GLY LEU LYS
SEQRES 51 A 966 ALA GLY ALA LEU ALA ILE GLU LYS CYS LYS VAL MET ALA
SEQRES 52 A 966 SER LYS LYS LYS PRO LEU TRP LEU GLU PHE LYS CYS ALA
SEQRES 53 A 966 ASP PRO THR ALA LEU SER ASN GLU THR ILE GLY ILE ILE
SEQRES 54 A 966 PHE LYS HIS GLY ASP ASP LEU ARG GLN ASP MET LEU ILE
SEQRES 55 A 966 LEU GLN ILE LEU ARG ILE MET GLU SER ILE TRP GLU THR
SEQRES 56 A 966 GLU SER LEU ASP LEU CYS LEU LEU PRO TYR GLY CYS ILE
SEQRES 57 A 966 SER THR GLY ASP LYS ILE GLY MET ILE GLU ILE VAL LYS
SEQRES 58 A 966 ASP ALA THR THR ILE ALA LYS ILE GLN GLN SER THR VAL
SEQRES 59 A 966 GLY ASN THR GLY ALA PHE LYS ASP GLU VAL LEU ASN HIS
SEQRES 60 A 966 TRP LEU LYS GLU LYS SER PRO THR GLU GLU LYS PHE GLN
SEQRES 61 A 966 ALA ALA VAL GLU ARG PHE VAL TYR SER CYS ALA GLY TYR
SEQRES 62 A 966 CYS VAL ALA THR PHE VAL LEU GLY ILE GLY ASP ARG HIS
SEQRES 63 A 966 ASN ASP ASN ILE MET ILE THR GLU THR GLY ASN LEU PHE
SEQRES 64 A 966 HIS ILE ASP PHE GLY HIS ILE LEU GLY ASN TYR LYS SER
SEQRES 65 A 966 PHE LEU GLY ILE ASN LYS GLU ARG VAL PRO PHE VAL LEU
SEQRES 66 A 966 THR PRO ASP PHE LEU PHE VAL MET GLY THR SER GLY LYS
SEQRES 67 A 966 LYS THR SER PRO HIS PHE GLN LYS PHE GLN ASP ILE CYS
SEQRES 68 A 966 VAL LYS ALA TYR LEU ALA LEU ARG HIS HIS THR ASN LEU
SEQRES 69 A 966 LEU ILE ILE LEU PHE SER MET MET LEU MET THR GLY MET
SEQRES 70 A 966 PRO GLN LEU THR SER LYS GLU ASP ILE GLU TYR ILE ARG
SEQRES 71 A 966 ASP ALA LEU THR VAL GLY LYS ASN GLU GLU ASP ALA LYS
SEQRES 72 A 966 LYS TYR PHE LEU ASP GLN ILE GLU VAL CYS ARG ASP LYS
SEQRES 73 A 966 GLY TRP THR VAL GLN PHE ASN TRP PHE LEU HIS LEU VAL
SEQRES 74 A 966 LEU GLY ILE LYS GLN GLY GLU LYS HIS SER ALA HIS HIS
SEQRES 75 A 966 HIS HIS HIS HIS
HET OAW A 1 21
HETNAM OAW 2-AMINO-4-METHYL-8-(1-METHYLETHYL)-6-(1H-PYRAZOL-4-YL)
HETNAM 2 OAW PTERIDIN-7(8H)-ONE
FORMUL 2 OAW C13 H15 N7 O
FORMUL 3 HOH *29(H2 O)
HELIX 1 1 SER A 144 GLY A 159 1 16
HELIX 2 2 ASP A 164 VAL A 168 5 5
HELIX 3 3 ASP A 171 LEU A 180 1 10
HELIX 4 4 LEU A 180 ARG A 191 1 12
HELIX 5 5 ASP A 192 HIS A 199 1 8
HELIX 6 6 PRO A 208 LYS A 213 1 6
HELIX 7 7 GLY A 242 SER A 247 1 6
HELIX 8 8 PRO A 286 ASN A 289 5 4
HELIX 9 9 PHE A 290 ASN A 299 1 10
HELIX 10 10 SER A 353 CYS A 357 5 5
HELIX 11 11 LYS A 421 LEU A 423 5 3
HELIX 12 12 ASN A 498 THR A 503 5 6
HELIX 13 13 PRO A 548 ALA A 560 1 13
HELIX 14 14 THR A 568 PHE A 578 1 11
HELIX 15 15 PHE A 578 LEU A 583 1 6
HELIX 16 16 HIS A 585 LYS A 587 5 3
HELIX 17 17 ALA A 588 SER A 594 1 7
HELIX 18 18 GLN A 600 ALA A 612 1 13
HELIX 19 19 ARG A 614 SER A 620 1 7
HELIX 20 20 ASP A 623 LEU A 630 1 8
HELIX 21 21 ASP A 637 SER A 650 1 14
HELIX 22 22 GLU A 652 ALA A 666 1 15
HELIX 23 23 VAL A 667 GLU A 670 5 4
HELIX 24 24 SER A 675 ASN A 688 1 14
HELIX 25 25 ASN A 688 SER A 706 1 19
HELIX 26 26 TYR A 709 ARG A 722 1 14
HELIX 27 27 GLY A 725 LEU A 752 1 28
HELIX 28 28 SER A 760 GLN A 775 1 16
HELIX 29 29 ASP A 837 THR A 857 1 21
HELIX 30 30 ILE A 888 VAL A 896 1 9
HELIX 31 31 GLU A 905 LYS A 914 1 10
HELIX 32 32 THR A 917 GLY A 943 1 27
HELIX 33 33 HIS A 948 ASP A 950 5 3
HELIX 34 34 THR A 988 MET A 995 1 8
HELIX 35 35 SER A 1003 HIS A 1022 1 20
HELIX 36 36 HIS A 1023 GLY A 1038 1 16
HELIX 37 37 GLU A 1049 LEU A 1055 1 7
HELIX 38 38 ASN A 1060 GLY A 1079 1 20
HELIX 39 39 TRP A 1080 VAL A 1091 1 12
SHEET 1 A 4 SER A 230 VAL A 235 0
SHEET 2 A 4 ILE A 220 HIS A 225 -1 N ILE A 222 O ILE A 233
SHEET 3 A 4 ILE A 303 ASP A 308 1 O VAL A 305 N HIS A 225
SHEET 4 A 4 VAL A 271 VAL A 274 -1 N VAL A 271 O ASP A 308
SHEET 1 B 4 GLU A 407 LYS A 419 0
SHEET 2 B 4 LYS A 360 ASP A 369 -1 N VAL A 363 O LEU A 414
SHEET 3 B 4 SER A 515 LEU A 520 -1 O SER A 517 N GLY A 367
SHEET 4 B 4 GLY A 478 HIS A 483 -1 N GLY A 478 O LEU A 520
SHEET 1 C 3 GLN A 392 ARG A 398 0
SHEET 2 C 3 THR A 380 HIS A 389 -1 N HIS A 389 O GLN A 392
SHEET 3 C 3 LYS A 402 PRO A 403 -1 O LYS A 402 N VAL A 381
SHEET 1 D 5 GLN A 392 ARG A 398 0
SHEET 2 D 5 THR A 380 HIS A 389 -1 N HIS A 389 O GLN A 392
SHEET 3 D 5 LEU A 428 TYR A 434 -1 O GLN A 432 N GLU A 384
SHEET 4 D 5 LEU A 460 LEU A 467 -1 O LEU A 461 N ILE A 433
SHEET 5 D 5 TRP A 485 GLN A 486 -1 O TRP A 485 N TYR A 463
SHEET 1 E 4 PHE A 783 VAL A 785 0
SHEET 2 E 4 ASP A 788 LEU A 796 -1 O ALA A 793 N PHE A 783
SHEET 3 E 4 LEU A 811 CYS A 817 -1 O LYS A 816 N GLY A 794
SHEET 4 E 4 LYS A 802 VAL A 803 -1 N LYS A 802 O TRP A 812
SHEET 1 F 6 PHE A 783 VAL A 785 0
SHEET 2 F 6 ASP A 788 LEU A 796 -1 O ALA A 793 N PHE A 783
SHEET 3 F 6 LEU A 811 CYS A 817 -1 O LYS A 816 N GLY A 794
SHEET 4 F 6 ILE A 828 HIS A 834 -1 O ILE A 830 N LEU A 813
SHEET 5 F 6 ILE A 876 GLU A 880 -1 O ILE A 879 N ILE A 831
SHEET 6 F 6 CYS A 869 GLY A 873 -1 N ILE A 870 O MET A 878
SHEET 1 G 3 ALA A 885 THR A 887 0
SHEET 2 G 3 ILE A 952 THR A 955 -1 O ILE A 954 N THR A 886
SHEET 3 G 3 LEU A 960 HIS A 962 -1 O PHE A 961 N MET A 953
CISPEP 1 CYS A 524 HIS A 525 0 1.32
SITE 1 AC1 11 MET A 804 ILE A 831 ASP A 836 ASP A 841
SITE 2 AC1 11 TYR A 867 ILE A 879 GLU A 880 VAL A 882
SITE 3 AC1 11 MET A 953 ILE A 963 ASP A 964
CRYST1 142.753 67.662 106.031 90.00 95.83 90.00 C 1 2 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 0.007005 0.000000 0.000715 0.00000
SCALE2 0.000000 0.014779 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009480 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
