HEADER TRANSFERASE/TRANSFERASE INHIBITOR 13-JUN-12 4FKI
TITLE CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CELL DIVISION PROTEIN KINASE 2, P33 PROTEIN KINASE;
COMPND 5 EC: 2.7.11.22;
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, CDKN2;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HIGH-FIVE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFB1
KEYWDS ALPHA AND BETA PROTEIN (A+B), TRANSFERASE, TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.N.KANG,J.A.STUCKEY
REVDAT 4 29-NOV-23 4FKI 1 REMARK
REVDAT 3 13-SEP-23 4FKI 1 REMARK SEQADV LINK
REVDAT 2 22-MAY-13 4FKI 1 SOURCE
REVDAT 1 08-MAY-13 4FKI 0
JRNL AUTH Y.N.KANG,J.A.STUCKEY
JRNL TITL CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE
JRNL TITL 2 INHIBITOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.1
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 37134
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1853
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 : 19
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.64
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.55
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2772
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1829
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2644
REMARK 3 BIN R VALUE (WORKING SET) : 0.1813
REMARK 3 BIN FREE R VALUE : 0.2159
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.62
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 128
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 : 2281
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.02420
REMARK 3 B22 (A**2) : -4.63450
REMARK 3 B33 (A**2) : 2.61030
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) : 0.190
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.090
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2775 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3980 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1262 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 49 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 400 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2775 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 325 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3334 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.01
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.56
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.84
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|0 - 36}
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1899 -6.4685 35.2180
REMARK 3 T TENSOR
REMARK 3 T11: -0.1096 T22: -0.0120
REMARK 3 T33: -0.0040 T12: 0.0199
REMARK 3 T13: -0.0412 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 8.3155 L22: 3.7805
REMARK 3 L33: 3.2165 L12: 0.1067
REMARK 3 L13: -1.7663 L23: 0.4833
REMARK 3 S TENSOR
REMARK 3 S11: -0.0274 S12: -0.5407 S13: -0.5006
REMARK 3 S21: 0.1374 S22: -0.0645 S23: -0.4228
REMARK 3 S31: 0.1711 S32: 0.3301 S33: 0.0919
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|45 - 137}
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3754 -0.8996 21.4650
REMARK 3 T TENSOR
REMARK 3 T11: -0.0516 T22: -0.0423
REMARK 3 T33: -0.0167 T12: -0.0160
REMARK 3 T13: 0.0027 T23: -0.0375
REMARK 3 L TENSOR
REMARK 3 L11: 0.5946 L22: 0.7207
REMARK 3 L33: 2.0679 L12: -0.2690
REMARK 3 L13: 0.4353 L23: 0.1539
REMARK 3 S TENSOR
REMARK 3 S11: -0.0444 S12: -0.1016 S13: 0.0979
REMARK 3 S21: 0.0427 S22: 0.0018 S23: -0.1555
REMARK 3 S31: 0.0044 S32: -0.0045 S33: 0.0426
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|138 - 153}
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1206 -1.3742 20.0409
REMARK 3 T TENSOR
REMARK 3 T11: -0.0343 T22: 0.0025
REMARK 3 T33: 0.0033 T12: -0.0162
REMARK 3 T13: -0.0158 T23: -0.0542
REMARK 3 L TENSOR
REMARK 3 L11: 1.3683 L22: 0.0000
REMARK 3 L33: 3.5103 L12: 0.1287
REMARK 3 L13: 0.6762 L23: 0.1106
REMARK 3 S TENSOR
REMARK 3 S11: 0.0263 S12: 0.0421 S13: -0.0049
REMARK 3 S21: 0.1481 S22: -0.0290 S23: -0.0965
REMARK 3 S31: -0.0667 S32: 0.3060 S33: 0.0028
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {A|157 - 241}
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3046 -12.6264 3.6369
REMARK 3 T TENSOR
REMARK 3 T11: -0.0040 T22: -0.0484
REMARK 3 T33: -0.0371 T12: 0.0162
REMARK 3 T13: 0.0058 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 1.5230 L22: 0.5268
REMARK 3 L33: 0.7943 L12: -0.2828
REMARK 3 L13: -0.0785 L23: 0.5762
REMARK 3 S TENSOR
REMARK 3 S11: 0.1021 S12: 0.0524 S13: -0.0713
REMARK 3 S21: 0.0301 S22: -0.0562 S23: -0.0480
REMARK 3 S31: 0.1359 S32: 0.0270 S33: -0.0459
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {A|242 - 298}
REMARK 3 ORIGIN FOR THE GROUP (A): -12.5989 -2.4502 5.1786
REMARK 3 T TENSOR
REMARK 3 T11: -0.0025 T22: 0.0023
REMARK 3 T33: -0.0367 T12: 0.0005
REMARK 3 T13: 0.0119 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 1.5248 L22: 0.8031
REMARK 3 L33: 0.6238 L12: -0.6706
REMARK 3 L13: 0.4238 L23: 0.1317
REMARK 3 S TENSOR
REMARK 3 S11: 0.0954 S12: -0.0049 S13: 0.0011
REMARK 3 S21: -0.1131 S22: -0.0651 S23: 0.0395
REMARK 3 S31: -0.0424 S32: -0.1926 S33: -0.0302
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4FKI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1000073012.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-OCT-09
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 : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : DIAMOND [111]
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37210
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.43900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2R3I
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: 15-20% PEG3350, 0.2M AMMONIUM ACETATE,
REMARK 280 0.1M HEPES, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K,
REMARK 280 PH 7.8, VAPOR DIFFUSION, SITTING DROP
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 26.71300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.15500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.78300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.15500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.71300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.78300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LEU A 37
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 VAL A 154
REMARK 465 PRO A 155
REMARK 465 VAL A 156
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 2 CG CD OE1 OE2
REMARK 470 GLU A 12 CG CD OE1 OE2
REMARK 470 ARG A 36 CG CD NE CZ NH1 NH2
REMARK 470 SER A 46 OG
REMARK 470 THR A 72 OG1 CG2
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 THR A 160 OG1 CG2
REMARK 470 LYS A 178 CG CD CE NZ
REMARK 470 ARG A 297 CG CD NE CZ NH1 NH2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 6 CE NZ
REMARK 480 GLU A 51 CD OE1 OE2
REMARK 480 ARG A 150 CZ NH1 NH2
REMARK 480 LYS A 242 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 126 -16.53 82.47
REMARK 500 ASP A 127 47.50 -141.49
REMARK 500 TYR A 179 66.65 -115.27
REMARK 500 PRO A 254 42.23 -106.80
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 09K A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EK3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APO CDK2
REMARK 900 RELATED ID: 4EK4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 4EK5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 4EK6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 4EK8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH THIAZOLYLPYRIMIDINE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 4FKG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 4FKJ RELATED DB: PDB
REMARK 900 RELATED ID: 4FKL RELATED DB: PDB
REMARK 900 RELATED ID: 4FKO RELATED DB: PDB
REMARK 900 RELATED ID: 4FKP RELATED DB: PDB
REMARK 900 RELATED ID: 4FKQ RELATED DB: PDB
REMARK 900 RELATED ID: 4FKR RELATED DB: PDB
REMARK 900 RELATED ID: 4FKS RELATED DB: PDB
REMARK 900 RELATED ID: 4FKT RELATED DB: PDB
REMARK 900 RELATED ID: 4FKU RELATED DB: PDB
REMARK 900 RELATED ID: 4FKV RELATED DB: PDB
REMARK 900 RELATED ID: 4FKW RELATED DB: PDB
DBREF 4FKI A 1 298 UNP P24941 CDK2_HUMAN 1 298
SEQADV 4FKI ACE A 0 UNP P24941 ACETYLATION
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 09K A 301 23
HETNAM ACE ACETYL GROUP
HETNAM 09K N-(5-CYCLOPROPYL-1H-PYRAZOL-3-YL)-2-[4-
HETNAM 2 09K (TRIFLUOROMETHOXY)PHENYL]ACETAMIDE
FORMUL 1 ACE C2 H4 O
FORMUL 2 09K C15 H14 F3 N3 O2
FORMUL 3 HOH *190(H2 O)
HELIX 1 1 SER A 46 LYS A 56 1 11
HELIX 2 2 LEU A 87 SER A 94 1 8
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 GLY A 153 1 7
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 LEU A 32 N TYR A 19
SHEET 4 A 5 LYS A 75 GLU A 81 -1 O LEU A 76 N ILE A 35
SHEET 5 A 5 LEU A 66 THR A 72 -1 N ILE A 70 O TYR A 77
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
LINK C ACE A 0 N MET A 1 1555 1555 1.33
CISPEP 1 PRO A 253 PRO A 254 0 7.67
SITE 1 AC1 14 GLU A 8 LYS A 9 ILE A 10 ALA A 31
SITE 2 AC1 14 GLU A 81 PHE A 82 LEU A 83 HIS A 84
SITE 3 AC1 14 LYS A 89 LEU A 134 HOH A 424 HOH A 471
SITE 4 AC1 14 HOH A 487 HOH A 578
CRYST1 53.426 71.566 72.310 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 0.018717 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013973 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013829 0.00000
HETATM 1 C ACE A 0 14.289 -2.014 39.647 1.00 52.79 C
ANISOU 1 C ACE A 0 4358 8598 7101 -262 -1319 -555 C
HETATM 2 O ACE A 0 13.234 -1.472 39.992 1.00 52.24 O
ANISOU 2 O ACE A 0 4475 8551 6822 -347 -1310 -676 O
HETATM 3 CH3 ACE A 0 15.592 -1.216 39.563 1.00 56.05 C
ANISOU 3 CH3 ACE A 0 4483 9056 7758 -420 -1318 -793 C
(ATOM LINES ARE NOT SHOWN.)
END
