HEADER TRANSFERASE 16-APR-04 1V1K
TITLE CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6-BIS ANILINO
TITLE 2 PYRIMIDINE CDK4 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: P33 PROTEIN KINASE;
COMPND 5 EC: 2.7.1.37;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS SERINE/THREONINE-PROTEIN KINASE, MITOSIS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.F.BEATTIE,G.A.BREAULT,R.P.A.ELLSTON,S.GREEN,P.J.JEWSBURY,
AUTHOR 2 C.J.MIDGLEY,R.T.NAVEN,C.A.MINSHULL,R.A.PAUPTIT,J.A.TUCKER,J.E.PEASE
REVDAT 3 13-JUL-11 1V1K 1 VERSN
REVDAT 2 24-FEB-09 1V1K 1 VERSN
REVDAT 1 04-MAY-04 1V1K 0
SPRSDE 04-MAY-04 1V1K 1H06
JRNL AUTH J.F.BEATTIE,G.A.BREAULT,R.P.A.ELLSTON,S.GREEN,P.J.JEWSBURY,
JRNL AUTH 2 C.J.MIDGLEY,R.T.NAVEN,C.A.MINSHULL,R.A.PAUPTIT,J.A.TUCKER,
JRNL AUTH 3 J.E.PEASE
JRNL TITL CYCLIN-DEPENDENT KINASE 4 INHIBITORS AS A TREATMENT FOR
JRNL TITL 2 CANCER. PART 1: IDENTIFICATION AND OPTIMISATION OF
JRNL TITL 3 SUBSTITUTED 4,6-BIS ANILINO PYRIMIDINES
JRNL REF BIOORG.MED.CHEM.LETT. V. 13 2955 2003
JRNL REFN ISSN 0960-894X
JRNL PMID 12941311
JRNL DOI 10.1016/S0960-894X(03)00202-6
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH U.SCHULZE-GAHMEN,H.DE BONDT,S.-H.KIM
REMARK 1 TITL HIGH-RESOLUTION CRYSTAL STRUCTURES OF HUMAN
REMARK 1 TITL 2 CYCLIN-DEPENDENT KINASE 2 WITH AND WITHOUT ATP: BOUND
REMARK 1 TITL 3 WATERS AND NATURAL LIGAND AS A GUIDE FOR INHIBITOR DESIGN
REMARK 1 REF J.MED.CHEM. V. 39 4540 1996
REMARK 1 REFN ISSN 0022-2623
REMARK 1 PMID 8917641
REMARK 1 DOI 10.1021/JM960402A
REMARK 2
REMARK 2 RESOLUTION. 2.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.17
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.4
REMARK 3 NUMBER OF REFLECTIONS : 11329
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 596
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.31
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.37
REMARK 3 REFLECTION IN BIN (WORKING SET) : 701
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 32
REMARK 3 BIN FREE R VALUE : 0.3560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2176
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 108
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 24.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.21000
REMARK 3 B22 (A**2) : -0.58000
REMARK 3 B33 (A**2) : 0.37000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.542
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.297
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.198
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.172
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.923
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.875
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2268 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3080 ; 1.497 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 274 ; 5.557 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 348 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1679 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 932 ; 0.235 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 98 ; 0.155 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 36 ; 0.218 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.142 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1389 ; 0.675 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2236 ; 1.260 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 879 ; 1.985 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 844 ; 3.174 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 298
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6380 4.6834 13.1932
REMARK 3 T TENSOR
REMARK 3 T11: 0.0046 T22: 0.0487
REMARK 3 T33: 0.0162 T12: 0.0002
REMARK 3 T13: 0.0078 T23: 0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 0.3862 L22: 2.0698
REMARK 3 L33: 0.7740 L12: 0.0723
REMARK 3 L13: -0.1771 L23: -0.1395
REMARK 3 S TENSOR
REMARK 3 S11: 0.0265 S12: 0.0025 S13: -0.0571
REMARK 3 S21: -0.0376 S22: -0.0456 S23: -0.1343
REMARK 3 S31: 0.1182 S32: 0.1409 S33: 0.0191
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 38 - 46, AND 151 - 162 ARE
REMARK 3 NOT VISIBLE IN THE ELECTRON DENSITY MAP.
REMARK 4
REMARK 4 1V1K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-APR-04.
REMARK 100 THE PDBE ID CODE IS EBI-15010.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-97
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11954
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.310
REMARK 200 RESOLUTION RANGE LOW (A) : 51.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.31
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.23300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.300
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 10MG/ML
REMARK 280 WELL BUFFER CONTAINING 17.5% PEG3350,
REMARK 280 200MM HEPES, PH7.0, 100MM AMMONIUM ACETATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 27.17105
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.91900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.46605
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.91900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.17105
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.46600
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: PQS
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 ASP A 38
REMARK 465 THR A 39
REMARK 465 GLU A 40
REMARK 465 THR A 41
REMARK 465 GLU A 42
REMARK 465 GLY A 43
REMARK 465 VAL A 44
REMARK 465 PRO A 45
REMARK 465 SER A 46
REMARK 465 ALA A 151
REMARK 465 PHE A 152
REMARK 465 GLY A 153
REMARK 465 VAL A 154
REMARK 465 PRO A 155
REMARK 465 VAL A 156
REMARK 465 ARG A 157
REMARK 465 THR A 158
REMARK 465 TYR A 159
REMARK 465 THR A 160
REMARK 465 HIS A 161
REMARK 465 GLU A 162
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 GLU A 12 CG CD OE1 OE2
REMARK 470 THR A 14 OG1 CG2
REMARK 470 TYR A 15 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 25 CG CD1 CD2
REMARK 470 ARG A 36 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 37 CG CD1 CD2
REMARK 470 ARG A 50 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 56 CG CD CE NZ
REMARK 470 GLU A 57 CG CD OE1 OE2
REMARK 470 GLU A 73 CG CD OE1 OE2
REMARK 470 ASN A 74 CG OD1 ND2
REMARK 470 LYS A 75 CG CD CE NZ
REMARK 470 ARG A 122 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 150 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 164 CG1 CG2
REMARK 470 ARG A 297 CG CD NE CZ NH1 NH2
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 ASP A 86 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 206 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 288 CB - CG - OD2 ANGL. DEV. = 7.1 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 36 -88.73 -34.83
REMARK 500 ALA A 48 -62.00 -96.56
REMARK 500 ARG A 50 -70.34 -55.20
REMARK 500 GLU A 73 52.76 34.72
REMARK 500 ARG A 126 -21.37 88.54
REMARK 500 ASP A 127 43.44 -146.91
REMARK 500 PHE A 146 -165.85 -54.40
REMARK 500 LEU A 148 -14.44 -160.16
REMARK 500 TYR A 179 44.15 -100.42
REMARK 500 THR A 182 -18.88 -49.52
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 3FP A 299
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AQ1 RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE INHIBITOR STAUROSPORINE
REMARK 900 RELATED ID: 1B38 RELATED DB: PDB
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2
REMARK 900 RELATED ID: 1B39 RELATED DB: PDB
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 PHOSPHORYLATED
REMARK 900 ON THR 160
REMARK 900 RELATED ID: 1BUH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CDK2 KINASE
REMARK 900 COMPLEX WITHCELL CYCLE-REGULATORY PROTEIN
REMARK 900 CKSHS1
REMARK 900 RELATED ID: 1CKP RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE INHIBITOR PURVALANOL B
REMARK 900 RELATED ID: 1DI8 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2
REMARK 900 (CDK2) IN COMPLEX WITH 4-[3-
REMARK 900 HYDROXYANILINO]-6,7-DIMETHOXYQUINAZOLINE
REMARK 900 RELATED ID: 1DM2 RELATED DB: PDB
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE INHIBITOR HYMENIALDISINE
REMARK 900 RELATED ID: 1E1V RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE INHIBITOR NU2058
REMARK 900 RELATED ID: 1E1X RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE INHIBITOR NU6027
REMARK 900 RELATED ID: 1E9H RELATED DB: PDB
REMARK 900 THR 160 PHOSPHORYLATED CDK2 - HUMAN CYCLIN
REMARK 900 A3 COMPLEX WITH THE INHIBITOR INDIRUBIN-5-
REMARK 900 SULPHONATE BOUND
REMARK 900 RELATED ID: 1F5Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MURINE GAMMA HERPESVIRUS
REMARK 900 CYCLIN COMPLEXED TO HUMAN CYCLIN DEPENDANT
REMARK 900 KINASE 2
REMARK 900 RELATED ID: 1FIN RELATED DB: PDB
REMARK 900 CYCLIN A - CYCLIN-DEPENDENT KINASE 2 COMPLEX
REMARK 900 RELATED ID: 1FQ1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF KINASE ASSOCIATED
REMARK 900 PHOSPHATASE (KAP) INCOMPLEX WITH PHOSPHO-CDK2
REMARK 900 RELATED ID: 1FVT RELATED DB: PDB
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2
REMARK 900 (CDK2) INCOMPLEX WITH AN OXINDOLE INHIBITOR
REMARK 900 RELATED ID: 1FVV RELATED DB: PDB
REMARK 900 THE STRUCTURE OF CDK2/CYCLIN A IN COMPLEX
REMARK 900 WITH AN OXINDOLEINHIBITOR
REMARK 900 RELATED ID: 1G5S RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLIN DEPENDENT
REMARK 900 KINASE 2 (CDK2)IN COMPLEX WITH THE
REMARK 900 INHIBITOR H717
REMARK 900 RELATED ID: 1GIH RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE CDK4INHIBITOR
REMARK 900 RELATED ID: 1GII RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE CDK4INHIBITOR
REMARK 900 RELATED ID: 1GIJ RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE CDK4INHIBITOR
REMARK 900 RELATED ID: 1GY3 RELATED DB: PDB
REMARK 900 PCDK2/CYCLIN A IN COMPLEX WITH MGADP,
REMARK 900 NITRATE AND PEPTIDE SUBSTRATE
REMARK 900 RELATED ID: 1GZ8 RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE INHIBITOR 2-AMINO-6-(3'-METHYL-
REMARK 900 2'-OXO)BUTOXYPURINE
REMARK 900 RELATED ID: 1H00 RELATED DB: PDB
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6
REMARK 900 -BIS ANILINO PYRIMIDINE CDK4 INHIBITOR
REMARK 900 RELATED ID: 1H01 RELATED DB: PDB
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 2, 4
REMARK 900 -BIS ANILINO PYRIMIDINE CDK4 INHIBITOR
REMARK 900 RELATED ID: 1H07 RELATED DB: PDB
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6
REMARK 900 -BIS ANILINO PYRIMIDINE CDK4 INHIBITOR
REMARK 900 RELATED ID: 1H08 RELATED DB: PDB
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 2, 4
REMARK 900 -BIS ANILINO PYRIMIDINE CDK4 INHIBITOR
REMARK 900 RELATED ID: 1H0V RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN
REMARK 900 COMPLEX WITH THE INHIBITOR 2-AMINO-6-[(R
REMARK 900 )-PYRROLIDINO-5'-YL]METHOXYPURINE
REMARK 900 RELATED ID: 1H0W RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN
REMARK 900 COMPLEX WITH THE INHIBITOR 2-AMINO-6-[
REMARK 900 CYCLOHEX-3-ENYL]METHOXYPURINE
REMARK 900 RELATED ID: 1H1P RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/
REMARK 900 CYCLIN A COMPLEXED WITH THE INHIBITOR NU2058
REMARK 900 RELATED ID: 1H1Q RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/
REMARK 900 CYCLIN A COMPLEXED WITH THE INHIBITOR NU6094
REMARK 900 RELATED ID: 1H1R RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/
REMARK 900 CYCLIN A COMPLEXED WITH THE INHIBITOR NU6086
REMARK 900 RELATED ID: 1H1S RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/
REMARK 900 CYCLIN A COMPLEXED WITH THE INHIBITOR NU6102
REMARK 900 RELATED ID: 1H24 RELATED DB: PDB
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH A 9 RESIDUE
REMARK 900 RECRUITMENT PEPTIDE FROM E2F
REMARK 900 RELATED ID: 1H25 RELATED DB: PDB
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE
REMARK 900 RECRUITMENT PEPTIDE FROM E2F
REMARK 900 RELATED ID: 1H26 RELATED DB: PDB
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE
REMARK 900 RECRUITMENT PEPTIDE FROM P53
REMARK 900 RELATED ID: 1H27 RELATED DB: PDB
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE
REMARK 900 RECRUITMENT PEPTIDE FROM P27
REMARK 900 RELATED ID: 1H28 RELATED DB: PDB
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE
REMARK 900 RECRUITMENT PEPTIDE FROM P107
REMARK 900 RELATED ID: 1HCK RELATED DB: PDB
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2
REMARK 900 RELATED ID: 1HCL RELATED DB: PDB
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2
REMARK 900 RELATED ID: 1JST RELATED DB: PDB
REMARK 900 PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND
REMARK 900 TO CYCLIN A
REMARK 900 RELATED ID: 1JSU RELATED DB: PDB
REMARK 900 P27(KIP1)/CYCLIN A/CDK2 COMPLEX
REMARK 900 RELATED ID: 1JSV RELATED DB: PDB
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2
REMARK 900 (CDK2) INCOMPLEX WITH 4-[(6-AMINO-4-
REMARK 900 PYRIMIDINYL)AMINO]BENZENESULFONAMIDE
REMARK 900 RELATED ID: 1JVP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 (
REMARK 900 UNPHOSPHORYLATED) INCOMPLEX WITH PKF049-365
REMARK 900 RELATED ID: 1KE5 RELATED DB: PDB
REMARK 900 CDK2 COMPLEXED WITH N-METHYL-4-{[(2-OXO-
REMARK 900 1,2-DIHYDRO-3H-INDOL-3-YLIDENE)METHYL]
REMARK 900 AMINO}BENZENESULFONAMIDE
REMARK 900 RELATED ID: 1KE6 RELATED DB: PDB
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED
REMARK 900 WITH N-METHYL-{4-[2-(7-OXO-6,7-DIHYDRO
REMARK 900 -8H-[1,3]THIAZOLO[5,4-E]INDOL-8-
REMARK 900 YLIDENE)HYDRAZINO]PHENYL}METHANESULFONAMIDE
REMARK 900 RELATED ID: 1KE7 RELATED DB: PDB
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED
REMARK 900 WITH 3-{[(2,2-DIOXIDO-1,3-DIHYDRO-2-
REMARK 900 BENZOTHIEN-5-YL)AMINO]METHYLENE}-5-(1,3-
REMARK 900 OXAZOL-5-YL)-1,3-DIHYDRO-2H-INDOL-2-
REMARK 900 ONE
REMARK 900 RELATED ID: 1KE8 RELATED DB: PDB
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED
REMARK 900 WITH 4-{[(2-OXO-1,2-DIHYDRO-3H-INDOL-3
REMARK 900 -YLIDENE)METHYL]AMINO}-N-(1,3-THIAZOL-2-
REMARK 900 YL)BENZENESULFONAMIDE
REMARK 900 RELATED ID: 1KE9 RELATED DB: PDB
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED
REMARK 900 WITH 3-{[4-({[AMINO(IMINO)METHYL]
REMARK 900 AMINOSULFONYL)ANILINO]METHYLENE}-2-OXO-2,3-
REMARK 900 DIHYDRO-1H-INDOLE
REMARK 900 RELATED ID: 1OGU RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/
REMARK 900 CYCLIN A COMPLEXED WITH A 2-ARYLAMINO-4-
REMARK 900 CYCLOHEXYLMETHYL-5-NITROSO-6-AMINOPYRIMIDINE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 1OI9 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/
REMARK 900 CYCLIN A COMPLEXED WITH A 6-
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR
REMARK 900 RELATED ID: 1OIQ RELATED DB: PDB
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS
REMARK 900 OF CYCLIN-DEPENDENT KINASE INHIBITORS
REMARK 900 IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION
REMARK 900 RELATED ID: 1OIR RELATED DB: PDB
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS
REMARK 900 OF CYCLIN-DEPENDENT KINASE INHIBITORS
REMARK 900 IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION
REMARK 900 RELATED ID: 1OIT RELATED DB: PDB
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS
REMARK 900 OF CYCLIN-DEPENDENT KINASE INHIBITORS
REMARK 900 IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION
REMARK 900 RELATED ID: 1OIU RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/
REMARK 900 CYCLIN A COMPLEXED WITH A 6-
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR
REMARK 900 RELATED ID: 1OIY RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/
REMARK 900 CYCLIN A COMPLEXED WITH A 6-
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR
REMARK 900 RELATED ID: 1OKU RELATED DB: PDB
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ALA-
REMARK 900 ALA-ABU-ARG-ER-LEU-ILE-(P-F-PHE)-NH2
REMARK 900 RELATED ID: 1OKV RELATED DB: PDB
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG-
REMARK 900 ARG-LEU-ILE-PHE-NH2
REMARK 900 RELATED ID: 1OKW RELATED DB: PDB
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR AC-ARG-
REMARK 900 ARG-LEU-ASN-(M-CL-PHE)-NH2
REMARK 900 RELATED ID: 1OL1 RELATED DB: PDB
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-CIT-
REMARK 900 CIT-LEU-ILE-(P-F-PHE)-NH2
REMARK 900 RELATED ID: 1OL2 RELATED DB: PDB
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG-
REMARK 900 ARG-LEU-ASN-(P-F-PHE)-NH2
REMARK 900 RELATED ID: 1P2A RELATED DB: PDB
REMARK 900 THE STRUCTURE OF CYCLIN DEPENDENT KINASE 2
REMARK 900 (CKD2) WITH ATRISUBSTITUTED NAPHTHOSTYRIL
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 1P5E RELATED DB: PDB
REMARK 900 THE STRUCURE OF PHOSPHO-CDK2/CYCLIN A IN
REMARK 900 COMPLEX WITH THEINHIBITOR 4,5,6,7-
REMARK 900 TETRABROMOBENZOTRIAZOLE (TBS)
REMARK 900 RELATED ID: 1PF8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLIN-DEPENDENT
REMARK 900 KINASE 2COMPLEXED WITH A NUCLEOSIDE INHIBITOR
REMARK 900 RELATED ID: 1PKD RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF UCN-01 IN COMPLEX
REMARK 900 WITH PHOSPHO-CDK2/CYCLIN A
REMARK 900 RELATED ID: 1PW2 RELATED DB: PDB
REMARK 900 APO STRUCTURE OF HUMAN CYCLIN-DEPENDENT
REMARK 900 KINASE 2
REMARK 900 RELATED ID: 1PXI RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THEINHIBITOR 4-(2,5-DICHLORO-THIOPHEN-
REMARK 900 3-YL)-PYRIMIDIN-2-YLAMINE
REMARK 900 RELATED ID: 1PXJ RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THEINHIBITOR 4-(2,4-DIMETHYL-THIAZOL-
REMARK 900 5-YL)-PYRIMIDIN-2-YLAMINE
REMARK 900 RELATED ID: 1PXK RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THEINHIBITOR N-[4-(2,4-DIMETHYL-
REMARK 900 THIAZOL-5-YL)PYRIMIDIN-2-YL]-N'-
REMARK 900 HYDROXYIMINOFORMAMIDE
REMARK 900 RELATED ID: 1PXL RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THEINHIBITOR [4-(2,4-DIMETHYL-THIAZOL-
REMARK 900 5-YL)-PYRIMIDIN-2-YL]-(4-TRIFLUOROMETHYL-
REMARK 900 PHENYL)-AMINE
REMARK 900 RELATED ID: 1PXM RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THEINHIBITOR 3-[4-(2,4-DIMETHYL-
REMARK 900 THIAZOL-5-YL)-PYRIMIDIN-2-YLAMINO]-PHENOL
REMARK 900 RELATED ID: 1PXN RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THEINHIBITOR 4-[4-(4-METHYL-2-
REMARK 900 METHYLAMINO-THIAZOL-5-YL)-PYRIMIDIN-2-
REMARK 900 YLAMINO]-PHENOL
REMARK 900 RELATED ID: 1PXO RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THEINHIBITOR [4-(2-AMINO-4-METHYL-
REMARK 900 THIAZOL-5-YL)-PYRIMIDIN-2-YL]-(3-NITRO-
REMARK 900 PHENYL)-AMINE
REMARK 900 RELATED ID: 1PXP RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THEINHIBITOR N-[4-(2,4-DIMETHYL-
REMARK 900 THIAZOL-5-YL)-PYRIMIDIN-2-YL]-N',N'-
REMARK 900 DIMETHYL-BENZENE-1,4-DIAMINE
REMARK 900 RELATED ID: 1QMZ RELATED DB: PDB
REMARK 900 PHOSPHORYLATED CDK2-CYCLYIN A-SUBSTRATE
REMARK 900 PEPTIDE COMPLEX
REMARK 900 RELATED ID: 1R78 RELATED DB: PDB
REMARK 900 CDK2 COMPLEX WITH A 4-ALKYNYL OXINDOLE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 1URC RELATED DB: PDB
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG-
REMARK 900 ARG-LEU-ASN-(P-F-PHE)-NH2
REMARK 900 RELATED ID: 1URW RELATED DB: PDB
REMARK 900 CDK2 IN COMPLEX WITH AN IMIDAZO[1,2-B]
REMARK 900 PYRIDAZINE
DBREF 1V1K A 0 0 PDB 1V1K 1V1K 0 0
DBREF 1V1K A 1 298 UNP P24941 CDK2_HUMAN 1 298
SEQRES 1 A 299 ACE MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU
SEQRES 2 A 299 GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU
SEQRES 3 A 299 THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP
SEQRES 4 A 299 THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU
SEQRES 5 A 299 ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL
SEQRES 6 A 299 LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR
SEQRES 7 A 299 LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE
SEQRES 8 A 299 MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU
SEQRES 9 A 299 ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA
SEQRES 10 A 299 PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS
SEQRES 11 A 299 PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS
SEQRES 12 A 299 LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO
SEQRES 13 A 299 VAL ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR
SEQRES 14 A 299 ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER
SEQRES 15 A 299 THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA
SEQRES 16 A 299 GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER
SEQRES 17 A 299 GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY
SEQRES 18 A 299 THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET
SEQRES 19 A 299 PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN
SEQRES 20 A 299 ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY
SEQRES 21 A 299 ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN
SEQRES 22 A 299 LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE
SEQRES 23 A 299 PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU
HET ACE A 0 3
HET 3FP A 299 33
HETNAM ACE ACETYL GROUP
HETNAM 3FP (2R)-1-(DIMETHYLAMINO)-3-{4-[(6-{[2-FLUORO-5-
HETNAM 2 3FP (TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDIN-4-YL)
HETNAM 3 3FP AMINO]PHENOXY}PROPAN-2-OL
HETSYN 3FP 1-(DIMETHYLAMINO)-3-{4-[(6-{[2-FLUORO-5-
HETSYN 2 3FP (TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDIN-4-YL)
HETSYN 3 3FP AMINO]PHENOXY}PROPAN-2-OL
FORMUL 2 ACE C2 H4 O
FORMUL 3 3FP C22 H23 N5 O2 F4
FORMUL 4 HOH *108(H2 O)
HELIX 1 1 THR A 47 SER A 53 1 7
HELIX 2 2 LEU A 54 LEU A 58 5 5
HELIX 3 3 LEU A 87 SER A 94 1 8
HELIX 4 4 PRO A 100 SER A 120 1 21
HELIX 5 5 LYS A 129 GLN A 131 5 3
HELIX 6 6 ALA A 170 LEU A 175 1 6
HELIX 7 7 THR A 182 ARG A 199 1 18
HELIX 8 8 SER A 207 GLY A 220 1 14
HELIX 9 9 GLY A 229 MET A 233 5 5
HELIX 10 10 ASP A 247 VAL A 251 5 5
HELIX 11 11 ASP A 256 LEU A 267 1 12
HELIX 12 12 SER A 276 LEU A 281 1 6
HELIX 13 13 ALA A 282 GLN A 287 5 6
SHEET 1 AA 5 PHE A 4 GLY A 13 0
SHEET 2 AA 5 GLY A 16 ASN A 23 -1 O GLY A 16 N GLY A 13
SHEET 3 AA 5 VAL A 29 ILE A 35 -1 O VAL A 30 N ALA A 21
SHEET 4 AA 5 LYS A 75 GLU A 81 -1 O LEU A 76 N ILE A 35
SHEET 5 AA 5 LEU A 66 THR A 72 -1 N LEU A 67 O VAL A 79
SHEET 1 AB 3 GLN A 85 ASP A 86 0
SHEET 2 AB 3 LEU A 133 ILE A 135 -1 O ILE A 135 N GLN A 85
SHEET 3 AB 3 ILE A 141 LEU A 143 -1 O LYS A 142 N LEU A 134
LINK C ACE A 0 N MET A 1 1555 1555 1.34
SITE 1 AC1 15 ILE A 10 GLY A 11 GLU A 12 GLY A 13
SITE 2 AC1 15 VAL A 18 ALA A 31 GLU A 81 LEU A 83
SITE 3 AC1 15 ASP A 86 LYS A 89 GLN A 131 LEU A 134
SITE 4 AC1 15 ALA A 144 ASP A 145 HOH A2108
CRYST1 54.342 72.932 73.838 90.00 90.00 90.00 P 21 21 21 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 0.018402 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013711 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013543 0.00000
HETATM 1 C ACE A 0 28.269 -20.514 16.716 1.00 33.81 C
HETATM 2 O ACE A 0 27.387 -21.205 17.259 1.00 34.15 O
HETATM 3 CH3 ACE A 0 29.614 -20.321 17.359 1.00 33.68 C
(ATOM LINES ARE NOT SHOWN.)
END
