HEADER TRANSFERASE/CELL CYCLE 02-OCT-12 4BCI
TITLE STRUCTURE OF CDK9 IN COMPLEX WITH CYCLIN T AND A 2-AMINO-4-HETEROARYL-
TITLE 2 PYRIMIDINE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN-DEPENDENT KINASE 9;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 2-330;
COMPND 5 SYNONYM: C-2K, CELL DIVISION CYCLE 2-LIKE PROTEIN KINASE 4, CELL
COMPND 6 DIVISION PROTEIN KINASE 9, SERINE/THREONINE-PROTEIN KINASE PITALRE,
COMPND 7 TAT-ASSOCIATED KINASE COMPLEX CATALYTIC SUBUNIT;
COMPND 8 EC: 2.7.11.22, 2.7.11.23;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: CYCLIN-T1;
COMPND 12 CHAIN: B;
COMPND 13 FRAGMENT: RESIDUES 2-259;
COMPND 14 SYNONYM: CYCT1, CYCLIN-T;
COMPND 15 ENGINEERED: YES;
COMPND 16 MUTATION: 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_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PVL1392;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PVL1392
KEYWDS TRANSFERASE-CELL CYCLE COMPLEX, CDK-CYCLIN COMPLEX, TRANSCRIPTION-
KEYWDS 2 PROTEIN BINDING, STRUCTURE-BASED DRUG DESIGN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.HOLE,S.BAUMLI,S.WANG,J.A.ENDICOTT,M.E.M.NOBLE
REVDAT 3 15-MAY-19 4BCI 1 REMARK LINK
REVDAT 2 27-FEB-13 4BCI 1 JRNL
REVDAT 1 09-JAN-13 4BCI 0
JRNL AUTH A.J.HOLE,S.BAUMLI,H.SHAO,S.SHI,C.PEPPER,P.M.FISCHER,S.WANG,
JRNL AUTH 2 J.A.ENDICOTT,M.E.M.NOBLE
JRNL TITL COMPARATIVE STRUCTURAL AND FUNCTIONAL STUDIES OF 4-(THIAZOL-
JRNL TITL 2 5-YL)-2-(PHENYLAMINO)PYRIMIDINE-5-CARBONITRILE CDK9
JRNL TITL 3 INHIBITORS SUGGEST THE BASIS FOR ISOTYPE SELECTIVITY.
JRNL REF J.MED.CHEM. V. 56 660 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 23252711
JRNL DOI 10.1021/JM301495V
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.43
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 20201
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.190
REMARK 3 FREE R VALUE TEST SET COUNT : 1024
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) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1393
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.3260
REMARK 3 BIN FREE R VALUE SET COUNT : 82
REMARK 3 BIN FREE R VALUE : 0.4290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4562
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 8
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 110.6
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.03600
REMARK 3 B22 (A**2) : -4.03600
REMARK 3 B33 (A**2) : 13.09300
REMARK 3 B12 (A**2) : -4.03600
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): 1.356
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.343
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.295
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 38.216
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4695 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4542 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6370 ; 1.125 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10432 ; 0.625 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 557 ; 4.964 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 218 ;33.551 ;23.945
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 835 ;15.486 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;16.850 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 710 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5210 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1088 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 40 ; 0.355 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 30 ; 0.193 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 70 ; 0.207 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 4 ; 0.222 ; 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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 4695 ; 6.644 ; 6.802
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4542 ; 1.688 ; 6.941
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 206 ;13.678 ;14.215
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9 ; 7.943 ;31.125
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 15037 ;12.045 ;65.719
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
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 5 A 326
REMARK 3 ORIGIN FOR THE GROUP (A): 48.3031 -17.9323 -1.7599
REMARK 3 T TENSOR
REMARK 3 T11: 0.5303 T22: 0.3980
REMARK 3 T33: 0.2543 T12: -0.0647
REMARK 3 T13: -0.1139 T23: 0.0711
REMARK 3 L TENSOR
REMARK 3 L11: 2.1473 L22: 2.5227
REMARK 3 L33: 2.7809 L12: -0.0395
REMARK 3 L13: 0.2999 L23: -0.4457
REMARK 3 S TENSOR
REMARK 3 S11: 0.2740 S12: -0.1927 S13: -0.7254
REMARK 3 S21: 0.4150 S22: -0.2090 S23: -0.1377
REMARK 3 S31: 0.6603 S32: 0.1117 S33: -0.0650
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 8 B 259
REMARK 3 ORIGIN FOR THE GROUP (A): 21.6827 3.5791 -19.9134
REMARK 3 T TENSOR
REMARK 3 T11: 0.3178 T22: 0.4115
REMARK 3 T33: 0.0504 T12: -0.0686
REMARK 3 T13: -0.0584 T23: -0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 3.6174 L22: 2.4917
REMARK 3 L33: 1.7101 L12: -1.6870
REMARK 3 L13: -0.8550 L23: -0.0325
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: 0.0416 S13: 0.3658
REMARK 3 S21: 0.0844 S22: 0.0927 S23: -0.2140
REMARK 3 S31: -0.1638 S32: -0.0031 S33: -0.0814
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 4BCI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-OCT-12.
REMARK 100 THE DEPOSITION ID IS D_1290054249.
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 : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20202
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.970
REMARK 200 RESOLUTION RANGE LOW (A) : 60.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.630
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.68
REMARK 200 R MERGE FOR SHELL (I) : 0.59000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.290
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN AT 4C USING 10-16%
REMARK 280 PEG 1000, 100MM NAK-PHOSPHATE PH 6.2, 500MM NACL, 4MM TCEP AS
REMARK 280 THE PRECIPITANT SOLUTION. THEY WERE SUBSEQUENTLY SOAKED IN THE
REMARK 280 PRESENCE OF COMPOUND., TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 87.05500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 50.26123
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 33.08700
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 87.05500
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 50.26123
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 33.08700
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 87.05500
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 50.26123
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 33.08700
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 100.52246
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 66.17400
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 100.52246
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 66.17400
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 100.52246
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 66.17400
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
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 GLY A 0
REMARK 465 PRO A 1
REMARK 465 ALA A 2
REMARK 465 LYS A 3
REMARK 465 GLN A 4
REMARK 465 LYS A 88
REMARK 465 ALA A 89
REMARK 465 SER A 90
REMARK 465 PRO A 91
REMARK 465 TYR A 92
REMARK 465 ASN A 93
REMARK 465 ARG A 94
REMARK 465 CYS A 95
REMARK 465 LYS A 96
REMARK 465 LYS A 178
REMARK 465 ASN A 179
REMARK 465 SER A 180
REMARK 465 GLN A 181
REMARK 465 MET A 327
REMARK 465 LEU A 328
REMARK 465 SER A 329
REMARK 465 THR A 330
REMARK 465 GLY B 0
REMARK 465 PRO B 1
REMARK 465 GLU B 2
REMARK 465 GLY B 3
REMARK 465 GLU B 4
REMARK 465 ARG B 5
REMARK 465 LYS B 6
REMARK 465 ASN B 7
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 CYS A 10 58.74 -165.37
REMARK 500 LEU A 22 -50.99 -125.00
REMARK 500 ALA A 23 139.46 -170.81
REMARK 500 ARG A 86 -168.72 -105.37
REMARK 500 ASP A 149 42.69 -155.24
REMARK 500 ALA A 152 -37.06 -38.18
REMARK 500 ASP A 167 77.79 63.16
REMARK 500 VAL A 190 132.80 82.12
REMARK 500 ARG A 225 14.20 57.04
REMARK 500 GLN A 230 73.03 -106.91
REMARK 500 LEU A 244 -43.44 -135.62
REMARK 500 ASN A 255 3.70 90.92
REMARK 500 ASN A 258 0.74 -66.63
REMARK 500 LYS A 264 4.77 -69.51
REMARK 500 GLU A 266 82.55 44.55
REMARK 500 VAL A 268 -176.15 -66.35
REMARK 500 LYS A 269 -17.41 -144.22
REMARK 500 ASP A 285 125.53 -38.25
REMARK 500 LEU A 296 49.75 -86.93
REMARK 500 ASN B 21 48.08 -83.92
REMARK 500 GLU B 116 153.26 -48.93
REMARK 500 THR B 121 12.56 -65.88
REMARK 500 LEU B 163 41.61 -72.38
REMARK 500 VAL B 164 -6.51 -157.61
REMARK 500 ARG B 165 80.86 49.61
REMARK 500 ASN B 250 -18.15 70.37
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 T3E A 1327
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PF6 RELATED DB: PDB
REMARK 900 IN SILICO STRUCTURE OF PROTEIN KINASE 9
REMARK 900 RELATED ID: 4BCF RELATED DB: PDB
REMARK 900 STRUCTURE OF CDK9 IN COMPLEX WITH CYCLIN T AND A 2 -AMINO-4-
REMARK 900 HETEROARYL-PYRIMIDINE INHIBITOR
REMARK 900 RELATED ID: 4BCG RELATED DB: PDB
REMARK 900 STRUCTURE OF CDK9 IN COMPLEX WITH CYCLIN T AND A 2 -AMINO-4-
REMARK 900 HETEROARYL-PYRIMIDINE INHIBITOR
REMARK 900 RELATED ID: 4BCH RELATED DB: PDB
REMARK 900 STRUCTURE OF CDK9 IN COMPLEX WITH CYCLIN T AND A 2 -AMINO-4-
REMARK 900 HETEROARYL-PYRIMIDINE INHIBITOR
REMARK 900 RELATED ID: 4BCJ RELATED DB: PDB
REMARK 900 STRUCTURE OF CDK9 IN COMPLEX WITH CYCLIN T AND A 2 -AMINO-4-
REMARK 900 HETEROARYL-PYRIMIDINE INHIBITOR
REMARK 900 RELATED ID: 4BCK RELATED DB: PDB
REMARK 900 STRUCTURE OF CDK2 IN COMPLEX WITH CYCLIN A AND A 2 -AMINO-4-
REMARK 900 HETEROARYL-PYRIMIDINE INHIBITOR
REMARK 900 RELATED ID: 4BCM RELATED DB: PDB
REMARK 900 STRUCTURE OF CDK2 IN COMPLEX WITH CYCLIN A AND A 2 -AMINO-4-
REMARK 900 HETEROARYL-PYRIMIDINE INHIBITOR
REMARK 900 RELATED ID: 4BCN RELATED DB: PDB
REMARK 900 STRUCTURE OF CDK2 IN COMPLEX WITH CYCLIN A AND A 2 -AMINO-4-
REMARK 900 HETEROARYL-PYRIMIDINE INHIBITOR
REMARK 900 RELATED ID: 4BCO RELATED DB: PDB
REMARK 900 STRUCTURE OF CDK2 IN COMPLEX WITH CYCLIN A AND A 2 -AMINO-4-
REMARK 900 HETEROARYL-PYRIMIDINE INHIBITOR
REMARK 900 RELATED ID: 4BCP RELATED DB: PDB
REMARK 900 STRUCTURE OF CDK2 IN COMPLEX WITH CYCLIN A AND A 2 -AMINO-4-
REMARK 900 HETEROARYL-PYRIMIDINE INHIBITOR
REMARK 900 RELATED ID: 4BCQ RELATED DB: PDB
REMARK 900 STRUCTURE OF CDK2 IN COMPLEX WITH CYCLIN A AND A 2 -AMINO-4-
REMARK 900 HETEROARYL-PYRIMIDINE INHIBITOR
DBREF 4BCI A 2 330 UNP P50750 CDK9_HUMAN 2 330
DBREF 4BCI B 2 259 UNP O60563 CCNT1_HUMAN 2 259
SEQADV 4BCI GLY A 0 UNP P50750 EXPRESSION TAG
SEQADV 4BCI PRO A 1 UNP P50750 EXPRESSION TAG
SEQADV 4BCI GLY B 0 UNP O60563 EXPRESSION TAG
SEQADV 4BCI PRO B 1 UNP O60563 EXPRESSION TAG
SEQADV 4BCI ARG B 77 UNP O60563 GLN 77 ENGINEERED MUTATION
SEQADV 4BCI GLY B 96 UNP O60563 GLU 96 ENGINEERED MUTATION
SEQADV 4BCI LEU B 241 UNP O60563 PHE 241 ENGINEERED MUTATION
SEQRES 1 A 331 GLY PRO ALA LYS GLN TYR ASP SER VAL GLU CYS PRO PHE
SEQRES 2 A 331 CYS ASP GLU VAL SER LYS TYR GLU LYS LEU ALA LYS ILE
SEQRES 3 A 331 GLY GLN GLY THR PHE GLY GLU VAL PHE LYS ALA ARG HIS
SEQRES 4 A 331 ARG LYS THR GLY GLN LYS VAL ALA LEU LYS LYS VAL LEU
SEQRES 5 A 331 MET GLU ASN GLU LYS GLU GLY PHE PRO ILE THR ALA LEU
SEQRES 6 A 331 ARG GLU ILE LYS ILE LEU GLN LEU LEU LYS HIS GLU ASN
SEQRES 7 A 331 VAL VAL ASN LEU ILE GLU ILE CYS ARG THR LYS ALA SER
SEQRES 8 A 331 PRO TYR ASN ARG CYS LYS GLY SER ILE TYR LEU VAL PHE
SEQRES 9 A 331 ASP PHE CYS GLU HIS ASP LEU ALA GLY LEU LEU SER ASN
SEQRES 10 A 331 VAL LEU VAL LYS PHE THR LEU SER GLU ILE LYS ARG VAL
SEQRES 11 A 331 MET GLN MET LEU LEU ASN GLY LEU TYR TYR ILE HIS ARG
SEQRES 12 A 331 ASN LYS ILE LEU HIS ARG ASP MET LYS ALA ALA ASN VAL
SEQRES 13 A 331 LEU ILE THR ARG ASP GLY VAL LEU LYS LEU ALA ASP PHE
SEQRES 14 A 331 GLY LEU ALA ARG ALA PHE SER LEU ALA LYS ASN SER GLN
SEQRES 15 A 331 PRO ASN ARG TYR TPO ASN ARG VAL VAL THR LEU TRP TYR
SEQRES 16 A 331 ARG PRO PRO GLU LEU LEU LEU GLY GLU ARG ASP TYR GLY
SEQRES 17 A 331 PRO PRO ILE ASP LEU TRP GLY ALA GLY CYS ILE MET ALA
SEQRES 18 A 331 GLU MET TRP THR ARG SER PRO ILE MET GLN GLY ASN THR
SEQRES 19 A 331 GLU GLN HIS GLN LEU ALA LEU ILE SER GLN LEU CYS GLY
SEQRES 20 A 331 SER ILE THR PRO GLU VAL TRP PRO ASN VAL ASP ASN TYR
SEQRES 21 A 331 GLU LEU TYR GLU LYS LEU GLU LEU VAL LYS GLY GLN LYS
SEQRES 22 A 331 ARG LYS VAL LYS ASP ARG LEU LYS ALA TYR VAL ARG ASP
SEQRES 23 A 331 PRO TYR ALA LEU ASP LEU ILE ASP LYS LEU LEU VAL LEU
SEQRES 24 A 331 ASP PRO ALA GLN ARG ILE ASP SER ASP ASP ALA LEU ASN
SEQRES 25 A 331 HIS ASP PHE PHE TRP SER ASP PRO MET PRO SER ASP LEU
SEQRES 26 A 331 LYS GLY MET LEU SER THR
SEQRES 1 B 260 GLY PRO GLU GLY GLU ARG LYS ASN ASN ASN LYS ARG TRP
SEQRES 2 B 260 TYR PHE THR ARG GLU GLN LEU GLU ASN SER PRO SER ARG
SEQRES 3 B 260 ARG PHE GLY VAL ASP PRO ASP LYS GLU LEU SER TYR ARG
SEQRES 4 B 260 GLN GLN ALA ALA ASN LEU LEU GLN ASP MET GLY GLN ARG
SEQRES 5 B 260 LEU ASN VAL SER GLN LEU THR ILE ASN THR ALA ILE VAL
SEQRES 6 B 260 TYR MET HIS ARG PHE TYR MET ILE GLN SER PHE THR ARG
SEQRES 7 B 260 PHE PRO GLY ASN SER VAL ALA PRO ALA ALA LEU PHE LEU
SEQRES 8 B 260 ALA ALA LYS VAL GLU GLY GLN PRO LYS LYS LEU GLU HIS
SEQRES 9 B 260 VAL ILE LYS VAL ALA HIS THR CYS LEU HIS PRO GLN GLU
SEQRES 10 B 260 SER LEU PRO ASP THR ARG SER GLU ALA TYR LEU GLN GLN
SEQRES 11 B 260 VAL GLN ASP LEU VAL ILE LEU GLU SER ILE ILE LEU GLN
SEQRES 12 B 260 THR LEU GLY PHE GLU LEU THR ILE ASP HIS PRO HIS THR
SEQRES 13 B 260 HIS VAL VAL LYS CYS THR GLN LEU VAL ARG ALA SER LYS
SEQRES 14 B 260 ASP LEU ALA GLN THR SER TYR PHE MET ALA THR ASN SER
SEQRES 15 B 260 LEU HIS LEU THR THR PHE SER LEU GLN TYR THR PRO PRO
SEQRES 16 B 260 VAL VAL ALA CYS VAL CYS ILE HIS LEU ALA CYS LYS TRP
SEQRES 17 B 260 SER ASN TRP GLU ILE PRO VAL SER THR ASP GLY LYS HIS
SEQRES 18 B 260 TRP TRP GLU TYR VAL ASP ALA THR VAL THR LEU GLU LEU
SEQRES 19 B 260 LEU ASP GLU LEU THR HIS GLU LEU LEU GLN ILE LEU GLU
SEQRES 20 B 260 LYS THR PRO ASN ARG LEU LYS ARG ILE TRP ASN TRP ARG
MODRES 4BCI TPO A 186 THR PHOSPHOTHREONINE
HET TPO A 186 11
HET T3E A1327 27
HETNAM TPO PHOSPHOTHREONINE
HETNAM T3E 3-[[5-CYANO-4-[4-METHYL-2-(METHYLAMINO)-1,3-THIAZOL-5-
HETNAM 2 T3E YL]PYRIMIDIN-2-YL]AMINO]BENZENESULFONAMIDE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 T3E C16 H15 N7 O2 S2
FORMUL 4 HOH *8(H2 O)
HELIX 1 1 PRO A 60 LEU A 73 1 14
HELIX 2 2 LEU A 110 ASN A 116 1 7
HELIX 3 3 THR A 122 ASN A 143 1 22
HELIX 4 4 LYS A 151 ALA A 153 5 3
HELIX 5 5 THR A 191 ARG A 195 5 5
HELIX 6 6 PRO A 196 LEU A 201 1 6
HELIX 7 7 PRO A 208 ARG A 225 1 18
HELIX 8 8 THR A 233 GLY A 246 1 14
HELIX 9 9 ASN A 255 TYR A 259 5 5
HELIX 10 10 LYS A 274 ALA A 281 1 8
HELIX 11 11 ASP A 285 LEU A 296 1 12
HELIX 12 12 ASP A 305 HIS A 312 1 8
HELIX 13 13 ASP A 313 TRP A 316 5 4
HELIX 14 14 THR B 15 ASN B 21 1 7
HELIX 15 15 SER B 22 PHE B 27 1 6
HELIX 16 16 ASP B 30 LEU B 52 1 23
HELIX 17 17 SER B 55 GLN B 73 1 19
HELIX 18 18 PRO B 79 GLU B 95 1 17
HELIX 19 19 LYS B 100 HIS B 113 1 14
HELIX 20 20 SER B 123 LEU B 144 1 22
HELIX 21 21 HIS B 152 LEU B 163 1 12
HELIX 22 22 SER B 167 THR B 185 1 19
HELIX 23 23 THR B 186 GLN B 190 5 5
HELIX 24 24 THR B 192 SER B 208 1 17
HELIX 25 25 HIS B 220 VAL B 225 5 6
HELIX 26 26 THR B 230 THR B 248 1 19
HELIX 27 27 ARG B 251 TRP B 256 5 6
SHEET 1 AA 5 TYR A 19 LYS A 24 0
SHEET 2 AA 5 VAL A 33 HIS A 38 -1 O LYS A 35 N LEU A 22
SHEET 3 AA 5 LYS A 44 LYS A 49 -1 O VAL A 45 N ALA A 36
SHEET 4 AA 5 TYR A 100 ASP A 104 -1 O LEU A 101 N LYS A 48
SHEET 5 AA 5 LEU A 81 CYS A 85 -1 N ILE A 82 O VAL A 102
SHEET 1 AB 3 HIS A 108 ASP A 109 0
SHEET 2 AB 3 VAL A 155 ILE A 157 -1 O ILE A 157 N HIS A 108
SHEET 3 AB 3 LEU A 163 LEU A 165 -1 O LYS A 164 N LEU A 156
SHEET 1 AC 2 ILE A 145 LEU A 146 0
SHEET 2 AC 2 ARG A 172 ALA A 173 -1 O ARG A 172 N LEU A 146
LINK N TPO A 186 C TYR A 185 1555 1555 1.34
LINK C TPO A 186 N ASN A 187 1555 1555 1.34
CISPEP 1 ASP A 318 PRO A 319 0 -5.60
SITE 1 AC1 8 ILE A 25 PHE A 30 VAL A 79 PHE A 103
SITE 2 AC1 8 CYS A 106 GLU A 107 LEU A 156 ASP A 167
CRYST1 174.110 174.110 99.261 90.00 90.00 120.00 H 3 9
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 0.005743 0.003316 0.000000 0.00000
SCALE2 0.000000 0.006632 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010074 0.00000
(ATOM LINES ARE NOT SHOWN.)
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