HEADER TRANSFERASE 04-JUL-03 1PXI
TITLE HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 4-(2,5-
TITLE 2 DICHLORO-THIOPHEN-3-YL)-PYRIMIDIN-2-YLAMINE
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.-;
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 GENE: CDK2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: HI5;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS PROTEIN KINASE, CELL CYCLE, PHOSPHORYLATION, CELL DIVISION, MITOSIS,
KEYWDS 2 INHIBITION, TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, ATP-
KEYWDS 3 BINDING, 3D-STRUCTURE.
EXPDTA X-RAY DIFFRACTION
AUTHOR S.Y.WU,I.MCNAE,G.KONTOPIDIS,S.J.MCCLUE,C.MCINNES,K.J.STEWART,S.WANG,
AUTHOR 2 D.I.ZHELEVA,H.MARRIAGE,D.P.LANE,P.TAYLOR,P.M.FISCHER,M.D.WALKINSHAW
REVDAT 3 16-AUG-23 1PXI 1 REMARK
REVDAT 2 24-FEB-09 1PXI 1 VERSN
REVDAT 1 09-DEC-03 1PXI 0
JRNL AUTH S.Y.WU,I.MCNAE,G.KONTOPIDIS,S.J.MCCLUE,C.MCINNES,
JRNL AUTH 2 K.J.STEWART,S.WANG,D.I.ZHELEVA,H.MARRIAGE,D.P.LANE,P.TAYLOR,
JRNL AUTH 3 P.M.FISCHER,M.D.WALKINSHAW
JRNL TITL DISCOVERY OF A NOVEL FAMILY OF CDK INHIBITORS WITH THE
JRNL TITL 2 PROGRAM LIDAEUS: STRUCTURAL BASIS FOR LIGAND-INDUCED
JRNL TITL 3 DISORDERING OF THE ACTIVATION LOOP
JRNL REF STRUCTURE V. 11 399 2003
JRNL REFN ISSN 0969-2126
JRNL PMID 12679018
JRNL DOI 10.1016/S0969-2126(03)00060-1
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1552241.760
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 20564
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 SET) : 0.203
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 998
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.07
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3248
REMARK 3 BIN R VALUE (WORKING SET) : 0.2130
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 160
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2365
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 251
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.31000
REMARK 3 B22 (A**2) : -1.27000
REMARK 3 B33 (A**2) : 1.59000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.09
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.11
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.790
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.530 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.440 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.220 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.240 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 45.82
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CK1_PAR.TXT
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CK1_TOP.TXT
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 37 - 40 ARE NOT VISIBLE IN THE
REMARK 3 ELECTRON DENSITY MAP
REMARK 4
REMARK 4 1PXI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019669.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-SEP-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.488
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 : 20770
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 12.05
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.24400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.610
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1HCL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, NA-HEPES, PH 7.8, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 26.74950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.17800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.70200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.17800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.74950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.70200
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 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 LEU A 37
REMARK 465 ASP A 38
REMARK 465 THR A 39
REMARK 465 GLU A 40
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 6 97.11 -61.44
REMARK 500 VAL A 44 108.50 62.93
REMARK 500 ARG A 126 -11.29 78.53
REMARK 500 ASP A 127 48.99 -142.15
REMARK 500 HIS A 161 -1.80 76.59
REMARK 500 PRO A 254 40.18 -99.39
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 CK1 A 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AQ1 RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR
REMARK 900 STAUROSPORINE
REMARK 900 RELATED ID: 1B39 RELATED DB: PDB
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 PHOSPHORYLATED ON THR 160
REMARK 900 RELATED ID: 1CKP RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR
REMARK 900 PURVALANOL B
REMARK 900 RELATED ID: 1DI8 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN COMPLEX WITH 4-
REMARK 900 [3-HYDROXYANILINO]-6,7-DIMETHOXYQUINAZOLINE
REMARK 900 RELATED ID: 1DM2 RELATED DB: PDB
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR
REMARK 900 HYMENIALDISINE
REMARK 900 RELATED ID: 1E1V RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 2058
REMARK 900 RELATED ID: 1E1X RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 6027
REMARK 900 RELATED ID: 1E9H RELATED DB: PDB
REMARK 900 THR 160 PHOSPHORYLATED CDK2 - HUMAN CYCLIN A3 COMPLEX WITH THE
REMARK 900 INHIBITOR INDIRUBIN-5-SULPHONATE BOUND
REMARK 900 RELATED ID: 1FIN RELATED DB: PDB
REMARK 900 CYCLIN A - CYCLIN-DEPENDENT KINASE 2 COMPLEX
REMARK 900 RELATED ID: 1FVT RELATED DB: PDB
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN COMPLEX WITH
REMARK 900 AN OXINDOLE INHIBITOR
REMARK 900 RELATED ID: 1FVV RELATED DB: PDB
REMARK 900 THE STRUCTURE OF CDK2/CYCLIN A IN COMPLEX WITH AN OXINDOLE INHIBITOR
REMARK 900 RELATED ID: 1G5S RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2) IN
REMARK 900 COMPLEX WITH THE INHIBITOR H717
REMARK 900 RELATED ID: 1GIH RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4 INHIBITOR
REMARK 900 RELATED ID: 1GII RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4 INHIBITOR
REMARK 900 RELATED ID: 1GIJ RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4 INHIBITOR
REMARK 900 RELATED ID: 1GZ8 RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 2-
REMARK 900 AMINO-6-(3'-METHYL-2'-OXO)BUTOXYPURINE
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: 1JSV RELATED DB: PDB
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN COMPLEX WITH 4-
REMARK 900 [(6-AMINO-4-PYRIMIDINYL) AMINO]BENZENESULFONAMIDE
REMARK 900 RELATED ID: 1JVP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 (UNPHOSPHORYLATED) IN COMPLEX WITH
REMARK 900 PKF049-365
REMARK 900 RELATED ID: 1KE5 RELATED DB: PDB
REMARK 900 CDK2 COMPLEXED WITH N-METHYL-4-{[(2-OXO-1,2-DIHYDRO-3H-INDOL-3-
REMARK 900 YLIDENE)METHYL]AMINO}BENZENESULFONAMIDE
REMARK 900 RELATED ID: 1KE6 RELATED DB: PDB
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH N-METHYL-{4-[2-(7-
REMARK 900 OXO-6,7-DIHYDRO-8H-[1,3]THIAZOLO[5,4-E]INDOL-8- YLIDENE)HYDRAZINO]
REMARK 900 PHENYL}METHANESULFONAMIDE
REMARK 900 RELATED ID: 1KE7 RELATED DB: PDB
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[(2,2- DIOXIDO-1,
REMARK 900 3-DIHYDRO-2-BENZOTHIEN-5-YL)AMINO]METHYLENE}-5-(1,3-OXAZOL-5-YL)-1,
REMARK 900 3-DIHYDRO-2H-INDOL-2-ONE
REMARK 900 RELATED ID: 1KE8 RELATED DB: PDB
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 4-{[(2-OXO- 1,2-
REMARK 900 DIHYDRO-3H-INDOL-3-YLIDENE)METHYL]AMINO}-N-(1,3-THIAZOL-2-YL)
REMARK 900 BENZENESULFONAMIDE
REMARK 900 RELATED ID: 1KE9 RELATED DB: PDB
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[4-({
REMARK 900 [AMINO(IMINO)METHYL]AMINOSULFONYL)ANILINO]METHYLENE}-2-OXO-2,3-
REMARK 900 DIHYDRO-1H-INDOLE
DBREF 1PXI A 1 298 UNP P24941 CDK2_HUMAN 1 298
SEQRES 1 A 298 MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY
SEQRES 2 A 298 THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR
SEQRES 3 A 298 GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR
SEQRES 4 A 298 GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE
SEQRES 5 A 298 SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS
SEQRES 6 A 298 LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU
SEQRES 7 A 298 VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET
SEQRES 8 A 298 ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE
SEQRES 9 A 298 LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE
SEQRES 10 A 298 CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO
SEQRES 11 A 298 GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU
SEQRES 12 A 298 ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL
SEQRES 13 A 298 ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG
SEQRES 14 A 298 ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR
SEQRES 15 A 298 ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU
SEQRES 16 A 298 MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU
SEQRES 17 A 298 ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR
SEQRES 18 A 298 PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO
SEQRES 19 A 298 ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP
SEQRES 20 A 298 PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG
SEQRES 21 A 298 SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS
SEQRES 22 A 298 ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE
SEQRES 23 A 298 GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU
HET CK1 A 500 14
HETNAM CK1 4-(2,5-DICHLOROTHIEN-3-YL)PYRIMIDIN-2-AMINE
HETSYN CK1 4-(2,5-DICHLORO-THIOPHEN-3-YL)-PYRIMIDIN-2-YLAMINE
FORMUL 2 CK1 C8 H5 CL2 N3 S
FORMUL 3 HOH *251(H2 O)
HELIX 1 1 PRO A 45 LYS A 56 1 12
HELIX 2 2 LEU A 87 ALA A 93 1 7
HELIX 3 3 PRO A 100 HIS A 121 1 22
HELIX 4 4 LYS A 129 GLN A 131 5 3
HELIX 5 5 GLY A 147 PHE A 152 1 6
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 252 1 6
HELIX 11 11 ASP A 256 LEU A 267 1 12
HELIX 12 12 SER A 276 ALA A 282 1 7
HELIX 13 13 HIS A 283 GLN A 287 5 5
SHEET 1 A 5 PHE A 4 GLU A 12 0
SHEET 2 A 5 VAL A 17 ASN A 23 -1 O LYS A 20 N GLU A 8
SHEET 3 A 5 VAL A 29 ILE A 35 -1 O VAL A 30 N ALA A 21
SHEET 4 A 5 LYS A 75 GLU A 81 -1 O LEU A 78 N LYS A 33
SHEET 5 A 5 LEU A 66 THR A 72 -1 N ASP A 68 O VAL A 79
SHEET 1 B 3 GLN A 85 ASP A 86 0
SHEET 2 B 3 LEU A 133 ILE A 135 -1 O ILE A 135 N GLN A 85
SHEET 3 B 3 ILE A 141 LEU A 143 -1 O LYS A 142 N LEU A 134
CISPEP 1 PRO A 253 PRO A 254 0 0.09
SITE 1 AC1 16 GLU A 12 VAL A 18 ALA A 31 LYS A 33
SITE 2 AC1 16 VAL A 64 GLU A 81 LEU A 83 LEU A 134
SITE 3 AC1 16 ALA A 144 HOH A 501 HOH A 502 HOH A 503
SITE 4 AC1 16 HOH A 506 HOH A 507 HOH A 508 HOH A 509
CRYST1 53.499 71.404 72.356 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 0.018692 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014005 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013821 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
