HEADER TRANSFERASE 04-JAN-07 2OFV
TITLE CRYSTAL STRUCTURE OF AMINOQUINAZOLINE 1 BOUND TO LCK
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE LCK;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LCK KINASE DOMAIN, RESIDUES 231-497;
COMPND 5 SYNONYM: P56-LCK, LYMPHOCYTE CELL-SPECIFIC PROTEIN-TYROSINE KINASE,
COMPND 6 LSK, T CELL- SPECIFIC PROTEIN-TYROSINE KINASE;
COMPND 7 EC: 2.7.10.2;
COMPND 8 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: LCK;
SOURCE 6 EXPRESSION_SYSTEM: INSECT CELL;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS LCK, KINASE DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.HUANG
REVDAT 3 30-AUG-23 2OFV 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2OFV 1 VERSN
REVDAT 1 27-FEB-07 2OFV 0
JRNL AUTH E.F.DIMAURO,J.NEWCOMB,J.J.NUNES,J.E.BEMIS,C.BOUCHER,
JRNL AUTH 2 J.L.BUCHANAN,W.H.BUCKNER,V.J.CEE,L.CHAI,H.L.DEAK,
JRNL AUTH 3 L.F.EPSTEIN,T.FAUST,P.GALLANT,S.D.GEUNS-MEYER,A.GORE,Y.GU,
JRNL AUTH 4 B.HENKLE,B.L.HODOUS,F.HSIEH,X.HUANG,J.L.KIM,J.H.LEE,
JRNL AUTH 5 M.W.MARTIN,C.E.MASSE,D.C.MCGOWAN,D.METZ,D.MOHN,
JRNL AUTH 6 K.A.MORGENSTERN,A.OLIVEIRA-DOS-SANTOS,V.F.PATEL,D.POWERS,
JRNL AUTH 7 P.E.ROSE,S.SCHNEIDER,S.A.TOMLINSON,Y.-Y.TUDOR,S.M.TURCI,
JRNL AUTH 8 A.A.WELCHER,R.D.WHITE,H.ZHAO,L.ZHU,X.ZHU
JRNL TITL DISCOVERY OF AMINOQUINAZOLINES AS POTENT, ORALLY
JRNL TITL 2 BIOAVAILABLE INHIBITORS OF LCK: SYNTHESIS, SAR, AND IN VIVO
JRNL TITL 3 ANTI-INFLAMMATORY ACTIVITY
JRNL REF J.MED.CHEM. V. 49 5671 2006
JRNL REFN ISSN 0022-2623
JRNL PMID 16970394
JRNL DOI 10.1021/JM0605482
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 41284
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.274
REMARK 3 FREE R VALUE : 0.301
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 3878
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 271
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.460
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2OFV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1000041083.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : 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) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41290
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 55.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.28100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1QPC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3 M MGACETATE, 5-12.5% PEG8000, PH
REMARK 280 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 71.33000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.44500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 71.33000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.44500
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER.
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 APPLY THE FOLLOWING TO CHAINS: A, 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 THR A 226
REMARK 465 GLN A 227
REMARK 465 LYS A 228
REMARK 465 PRO A 229
REMARK 465 GLN A 230
REMARK 465 SER A 279
REMARK 465 MET A 280
REMARK 465 SER A 281
REMARK 465 PRO A 282
REMARK 465 ASP A 283
REMARK 465 ALA A 284
REMARK 465 PHE A 285
REMARK 465 ARG A 387
REMARK 465 LEU A 388
REMARK 465 ILE A 389
REMARK 465 GLU A 390
REMARK 465 ASP A 391
REMARK 465 ASN A 392
REMARK 465 GLU A 393
REMARK 465 TYR A 394
REMARK 465 THR A 395
REMARK 465 ALA A 396
REMARK 465 ARG A 397
REMARK 465 GLU A 398
REMARK 465 GLY A 399
REMARK 465 ALA A 400
REMARK 465 LYS A 401
REMARK 465 PHE A 402
REMARK 465 PRO A 403
REMARK 465 THR A 499
REMARK 465 ALA A 500
REMARK 465 THR A 501
REMARK 465 GLU A 502
REMARK 465 THR B 226
REMARK 465 GLN B 227
REMARK 465 LYS B 228
REMARK 465 PRO B 229
REMARK 465 GLN B 230
REMARK 465 LYS B 231
REMARK 465 SER B 279
REMARK 465 MET B 280
REMARK 465 SER B 281
REMARK 465 PRO B 282
REMARK 465 ASP B 283
REMARK 465 ASN B 392
REMARK 465 GLU B 393
REMARK 465 TYR B 394
REMARK 465 THR B 395
REMARK 465 ALA B 396
REMARK 465 ARG B 397
REMARK 465 GLU B 398
REMARK 465 GLY B 399
REMARK 465 ALA B 400
REMARK 465 LYS B 401
REMARK 465 PHE B 402
REMARK 465 GLY B 443
REMARK 465 MET B 444
REMARK 465 THR B 445
REMARK 465 ASN B 446
REMARK 465 PRO B 447
REMARK 465 GLU B 448
REMARK 465 VAL B 449
REMARK 465 ARG B 455
REMARK 465 ALA B 500
REMARK 465 THR B 501
REMARK 465 GLU B 502
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 LYS A 231 CG CD CE NZ
REMARK 470 GLN A 277 CG CD OE1 NE2
REMARK 470 LEU A 286 CG CD1 CD2
REMARK 470 THR A 308 OG1 CG2
REMARK 470 GLN A 309 CG CD OE1 NE2
REMARK 470 ASP A 374 CG OD1 OD2
REMARK 470 ILE A 404 CG1 CG2 CD1
REMARK 470 ILE A 450 CG1 CG2 CD1
REMARK 470 GLU A 454 CG CD OE1 OE2
REMARK 470 LYS B 276 CG CD CE NZ
REMARK 470 GLN B 277 CG CD OE1 NE2
REMARK 470 PHE B 285 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN B 298 CG CD OE1 NE2
REMARK 470 GLN B 309 CG CD OE1 NE2
REMARK 470 LYS B 335 CG CD CE NZ
REMARK 470 ASP B 374 CG OD1 OD2
REMARK 470 LEU B 376 CG CD1 CD2
REMARK 470 GLU B 390 CG CD OE1 OE2
REMARK 470 ASP B 391 CG OD1 OD2
REMARK 470 PRO B 403 CG CD
REMARK 470 ILE B 404 CG1 CG2 CD1
REMARK 470 LYS B 405 CG CD CE NZ
REMARK 470 HIS B 436 CG ND1 CD2 CE1 NE2
REMARK 470 ILE B 450 CG1 CG2 CD1
REMARK 470 ARG B 461 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 463 CG OD1 OD2
REMARK 470 GLU B 468 CG CD OE1 OE2
REMARK 470 LEU B 472 CG CD1 CD2
REMARK 470 LYS B 478 CG CD CE NZ
REMARK 470 ARG B 491 CG CD NE CZ NH1 NH2
REMARK 470 THR B 499 OG1 CG2
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 LYS B 335 N - CA - C ANGL. DEV. = -17.2 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 ARG A 363 -17.57 81.39
REMARK 500 ASP A 364 47.95 -141.72
REMARK 500 PHE A 383 29.24 -146.70
REMARK 500 LEU A 385 16.66 54.91
REMARK 500 ASN A 464 2.99 80.08
REMARK 500 TRP B 238 4.24 -152.54
REMARK 500 THR B 330 150.74 -49.00
REMARK 500 ILE B 334 7.63 55.53
REMARK 500 ILE B 338 -38.22 -32.42
REMARK 500 ARG B 363 -17.06 73.02
REMARK 500 SER B 373 -173.73 -65.59
REMARK 500 ASP B 382 105.80 -160.36
REMARK 500 PHE B 383 28.72 -148.26
REMARK 500 ASN B 464 -1.07 105.35
REMARK 500 TRP B 477 36.17 -91.48
REMARK 500 ASP B 496 38.13 -70.98
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 242 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 242 B 503
DBREF 2OFV A 226 502 UNP P06239 LCK_HUMAN 226 502
DBREF 2OFV B 226 502 UNP P06239 LCK_HUMAN 226 502
SEQADV 2OFV THR A 226 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV GLN A 227 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV LYS A 228 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV PRO A 229 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV GLN A 230 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV LYS A 231 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV THR A 499 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV ALA A 500 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV THR A 501 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV GLU A 502 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV THR B 226 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV GLN B 227 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV LYS B 228 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV PRO B 229 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV GLN B 230 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV LYS B 231 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV THR B 499 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV ALA B 500 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV THR B 501 UNP P06239 CLONING ARTIFACT
SEQADV 2OFV GLU B 502 UNP P06239 CLONING ARTIFACT
SEQRES 1 A 277 THR GLN LYS PRO GLN LYS PRO TRP TRP GLU ASP GLU TRP
SEQRES 2 A 277 GLU VAL PRO ARG GLU THR LEU LYS LEU VAL GLU ARG LEU
SEQRES 3 A 277 GLY ALA GLY GLN PHE GLY GLU VAL TRP MET GLY TYR TYR
SEQRES 4 A 277 ASN GLY HIS THR LYS VAL ALA VAL LYS SER LEU LYS GLN
SEQRES 5 A 277 GLY SER MET SER PRO ASP ALA PHE LEU ALA GLU ALA ASN
SEQRES 6 A 277 LEU MET LYS GLN LEU GLN HIS GLN ARG LEU VAL ARG LEU
SEQRES 7 A 277 TYR ALA VAL VAL THR GLN GLU PRO ILE TYR ILE ILE THR
SEQRES 8 A 277 GLU TYR MET GLU ASN GLY SER LEU VAL ASP PHE LEU LYS
SEQRES 9 A 277 THR PRO SER GLY ILE LYS LEU THR ILE ASN LYS LEU LEU
SEQRES 10 A 277 ASP MET ALA ALA GLN ILE ALA GLU GLY MET ALA PHE ILE
SEQRES 11 A 277 GLU GLU ARG ASN TYR ILE HIS ARG ASP LEU ARG ALA ALA
SEQRES 12 A 277 ASN ILE LEU VAL SER ASP THR LEU SER CYS LYS ILE ALA
SEQRES 13 A 277 ASP PHE GLY LEU ALA ARG LEU ILE GLU ASP ASN GLU TYR
SEQRES 14 A 277 THR ALA ARG GLU GLY ALA LYS PHE PRO ILE LYS TRP THR
SEQRES 15 A 277 ALA PRO GLU ALA ILE ASN TYR GLY THR PHE THR ILE LYS
SEQRES 16 A 277 SER ASP VAL TRP SER PHE GLY ILE LEU LEU THR GLU ILE
SEQRES 17 A 277 VAL THR HIS GLY ARG ILE PRO TYR PRO GLY MET THR ASN
SEQRES 18 A 277 PRO GLU VAL ILE GLN ASN LEU GLU ARG GLY TYR ARG MET
SEQRES 19 A 277 VAL ARG PRO ASP ASN CYS PRO GLU GLU LEU TYR GLN LEU
SEQRES 20 A 277 MET ARG LEU CYS TRP LYS GLU ARG PRO GLU ASP ARG PRO
SEQRES 21 A 277 THR PHE ASP TYR LEU ARG SER VAL LEU GLU ASP PHE PHE
SEQRES 22 A 277 THR ALA THR GLU
SEQRES 1 B 277 THR GLN LYS PRO GLN LYS PRO TRP TRP GLU ASP GLU TRP
SEQRES 2 B 277 GLU VAL PRO ARG GLU THR LEU LYS LEU VAL GLU ARG LEU
SEQRES 3 B 277 GLY ALA GLY GLN PHE GLY GLU VAL TRP MET GLY TYR TYR
SEQRES 4 B 277 ASN GLY HIS THR LYS VAL ALA VAL LYS SER LEU LYS GLN
SEQRES 5 B 277 GLY SER MET SER PRO ASP ALA PHE LEU ALA GLU ALA ASN
SEQRES 6 B 277 LEU MET LYS GLN LEU GLN HIS GLN ARG LEU VAL ARG LEU
SEQRES 7 B 277 TYR ALA VAL VAL THR GLN GLU PRO ILE TYR ILE ILE THR
SEQRES 8 B 277 GLU TYR MET GLU ASN GLY SER LEU VAL ASP PHE LEU LYS
SEQRES 9 B 277 THR PRO SER GLY ILE LYS LEU THR ILE ASN LYS LEU LEU
SEQRES 10 B 277 ASP MET ALA ALA GLN ILE ALA GLU GLY MET ALA PHE ILE
SEQRES 11 B 277 GLU GLU ARG ASN TYR ILE HIS ARG ASP LEU ARG ALA ALA
SEQRES 12 B 277 ASN ILE LEU VAL SER ASP THR LEU SER CYS LYS ILE ALA
SEQRES 13 B 277 ASP PHE GLY LEU ALA ARG LEU ILE GLU ASP ASN GLU TYR
SEQRES 14 B 277 THR ALA ARG GLU GLY ALA LYS PHE PRO ILE LYS TRP THR
SEQRES 15 B 277 ALA PRO GLU ALA ILE ASN TYR GLY THR PHE THR ILE LYS
SEQRES 16 B 277 SER ASP VAL TRP SER PHE GLY ILE LEU LEU THR GLU ILE
SEQRES 17 B 277 VAL THR HIS GLY ARG ILE PRO TYR PRO GLY MET THR ASN
SEQRES 18 B 277 PRO GLU VAL ILE GLN ASN LEU GLU ARG GLY TYR ARG MET
SEQRES 19 B 277 VAL ARG PRO ASP ASN CYS PRO GLU GLU LEU TYR GLN LEU
SEQRES 20 B 277 MET ARG LEU CYS TRP LYS GLU ARG PRO GLU ASP ARG PRO
SEQRES 21 B 277 THR PHE ASP TYR LEU ARG SER VAL LEU GLU ASP PHE PHE
SEQRES 22 B 277 THR ALA THR GLU
HET 242 A 503 31
HET 242 B 503 31
HETNAM 242 3-(2-AMINOQUINAZOLIN-6-YL)-4-METHYL-N-[3-
HETNAM 2 242 (TRIFLUOROMETHYL)PHENYL]BENZAMIDE
HETSYN 242 AMINOQUINAZOLINE 1
FORMUL 3 242 2(C23 H17 F3 N4 O)
FORMUL 5 HOH *271(H2 O)
HELIX 1 1 PRO A 241 GLU A 243 5 3
HELIX 2 2 LEU A 286 LEU A 295 1 10
HELIX 3 3 SER A 323 LYS A 329 1 7
HELIX 4 4 THR A 330 LYS A 335 1 6
HELIX 5 5 THR A 337 ARG A 358 1 22
HELIX 6 6 ARG A 366 ALA A 368 5 3
HELIX 7 7 ALA A 408 GLY A 415 1 8
HELIX 8 8 THR A 418 THR A 435 1 18
HELIX 9 9 THR A 445 GLU A 454 1 10
HELIX 10 10 PRO A 466 TRP A 477 1 12
HELIX 11 11 ARG A 480 ARG A 484 5 5
HELIX 12 12 THR A 486 ASP A 496 1 11
HELIX 13 13 PRO B 241 GLU B 243 5 3
HELIX 14 14 PHE B 285 LEU B 295 1 11
HELIX 15 15 SER B 323 LEU B 328 1 6
HELIX 16 16 THR B 337 ARG B 358 1 22
HELIX 17 17 ARG B 366 ALA B 368 5 3
HELIX 18 18 PRO B 403 THR B 407 5 5
HELIX 19 19 ALA B 408 GLY B 415 1 8
HELIX 20 20 THR B 418 VAL B 434 1 17
HELIX 21 21 PRO B 466 TRP B 477 1 12
HELIX 22 22 ARG B 480 ARG B 484 5 5
HELIX 23 23 THR B 486 ASP B 496 1 11
SHEET 1 A 5 LEU A 245 GLY A 254 0
SHEET 2 A 5 GLY A 257 TYR A 264 -1 O VAL A 259 N LEU A 251
SHEET 3 A 5 THR A 268 LEU A 275 -1 O VAL A 272 N TRP A 260
SHEET 4 A 5 ILE A 312 THR A 316 -1 O ILE A 312 N LEU A 275
SHEET 5 A 5 LEU A 303 VAL A 307 -1 N TYR A 304 O ILE A 315
SHEET 1 B 2 ILE A 370 VAL A 372 0
SHEET 2 B 2 CYS A 378 ILE A 380 -1 O LYS A 379 N LEU A 371
SHEET 1 C 5 LEU B 245 GLY B 254 0
SHEET 2 C 5 GLY B 257 TYR B 264 -1 O VAL B 259 N LEU B 251
SHEET 3 C 5 THR B 268 LEU B 275 -1 O VAL B 272 N TRP B 260
SHEET 4 C 5 ILE B 312 THR B 316 -1 O ILE B 314 N LYS B 273
SHEET 5 C 5 LEU B 303 VAL B 307 -1 N ALA B 305 O ILE B 315
SHEET 1 D 2 ILE B 370 VAL B 372 0
SHEET 2 D 2 CYS B 378 ILE B 380 -1 O LYS B 379 N LEU B 371
CISPEP 1 GLU A 310 PRO A 311 0 -0.92
CISPEP 2 GLU B 310 PRO B 311 0 0.31
SITE 1 AC1 20 VAL A 259 ALA A 271 VAL A 272 LYS A 273
SITE 2 AC1 20 GLU A 288 MET A 292 LEU A 295 LEU A 300
SITE 3 AC1 20 VAL A 301 ILE A 314 THR A 316 GLU A 317
SITE 4 AC1 20 TYR A 318 MET A 319 HIS A 362 ILE A 380
SITE 5 AC1 20 ALA A 381 ASP A 382 PHE A 383 HOH A 630
SITE 1 AC2 21 VAL B 259 ALA B 271 LYS B 273 GLU B 288
SITE 2 AC2 21 MET B 292 LEU B 300 VAL B 301 ILE B 314
SITE 3 AC2 21 THR B 316 GLU B 317 TYR B 318 MET B 319
SITE 4 AC2 21 GLY B 322 TYR B 360 LEU B 371 ILE B 380
SITE 5 AC2 21 ALA B 381 ASP B 382 PHE B 383 ILE B 389
SITE 6 AC2 21 HOH B 518
CRYST1 142.660 66.890 78.510 90.00 112.00 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007010 0.000000 0.002832 0.00000
SCALE2 0.000000 0.014950 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013738 0.00000
(ATOM LINES ARE NOT SHOWN.)
END