HEADER CELL CYCLE 19-JUN-18 6GUB
TITLE CDK2/CYCLINA IN COMPLEX WITH FLAVOPIRIDOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: CELL DIVISION PROTEIN KINASE 2,P33 PROTEIN KINASE;
COMPND 5 EC: 2.7.11.22;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CYCLIN-A2;
COMPND 9 CHAIN: B, D;
COMPND 10 SYNONYM: CYCLIN-A;
COMPND 11 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: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX6P1;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 11 ORGANISM_COMMON: BOVINE;
SOURCE 12 ORGANISM_TAXID: 9913;
SOURCE 13 GENE: CCNA2;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET21D
KEYWDS CDK2, CYCLINA, INHIBITOR, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.WOOD,S.KOROLCHUK,N.J.TATUM,L.Z.WANG,J.A.ENDICOTT,M.E.M.NOBLE,
AUTHOR 2 M.P.MARTIN
REVDAT 4 17-JAN-24 6GUB 1 REMARK
REVDAT 3 03-APR-19 6GUB 1 SOURCE
REVDAT 2 30-JAN-19 6GUB 1 JRNL
REVDAT 1 05-DEC-18 6GUB 0
JRNL AUTH D.J.WOOD,S.KOROLCHUK,N.J.TATUM,L.Z.WANG,J.A.ENDICOTT,
JRNL AUTH 2 M.E.M.NOBLE,M.P.MARTIN
JRNL TITL DIFFERENCES IN THE CONFORMATIONAL ENERGY LANDSCAPE OF CDK1
JRNL TITL 2 AND CDK2 SUGGEST A MECHANISM FOR ACHIEVING SELECTIVE CDK
JRNL TITL 3 INHIBITION.
JRNL REF CELL CHEM BIOL V. 26 121 2019
JRNL REFN ESSN 2451-9448
JRNL PMID 30472117
JRNL DOI 10.1016/J.CHEMBIOL.2018.10.015
REMARK 2
REMARK 2 RESOLUTION. 2.52 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.52
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 101.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 50176
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2638
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) : 2.52
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3668
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.3160
REMARK 3 BIN FREE R VALUE SET COUNT : 184
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8918
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 72
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.35000
REMARK 3 B22 (A**2) : 0.61000
REMARK 3 B33 (A**2) : 1.74000
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): 0.403
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.259
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9199 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8704 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12500 ; 1.666 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20213 ; 3.671 ; 2.994
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1102 ; 6.128 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 396 ;41.358 ;24.066
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1602 ;17.630 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;21.449 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1421 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9936 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1811 ; 0.007 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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): 4426 ; 3.604 ; 4.561
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4425 ; 3.596 ; 4.560
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5522 ; 5.725 ; 6.824
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5523 ; 5.725 ; 6.825
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4773 ; 4.150 ; 4.965
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4774 ; 4.150 ; 4.965
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6979 ; 6.738 ; 7.291
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 9752 ; 9.190 ;52.362
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 9752 ; 9.190 ;52.360
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6GUB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUN-18.
REMARK 100 THE DEPOSITION ID IS D_1200010574.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52814
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.520
REMARK 200 RESOLUTION RANGE LOW (A) : 101.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.20000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.52
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
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: 1H1S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 5MG PER ML. 0.6 TO 0.8M
REMARK 280 KCL, 0.9 TO 1.2M (NH402SO4, AND 100MM HEPES (PH 7.0), 0.5MM
REMARK 280 INHIBITOR, VAPOR DIFFUSION, SITTING 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 37.59200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.98650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 68.11200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.98650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.59200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 68.11200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 ASP A 38
REMARK 465 THR A 39
REMARK 465 GLU A 40
REMARK 465 ARG A 297
REMARK 465 LEU A 298
REMARK 465 GLY B 171
REMARK 465 HIS B 433
REMARK 465 HIS B 434
REMARK 465 HIS B 435
REMARK 465 HIS B 436
REMARK 465 HIS B 437
REMARK 465 HIS B 438
REMARK 465 GLY C -3
REMARK 465 PRO C -2
REMARK 465 GLY C -1
REMARK 465 PRO C 241
REMARK 465 LYS C 242
REMARK 465 TRP C 243
REMARK 465 ALA C 244
REMARK 465 ARG C 245
REMARK 465 ARG C 297
REMARK 465 LEU C 298
REMARK 465 GLY D 171
REMARK 465 HIS D 433
REMARK 465 HIS D 434
REMARK 465 HIS D 435
REMARK 465 HIS D 436
REMARK 465 HIS D 437
REMARK 465 HIS D 438
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 GLU A 8 137.09 179.97
REMARK 500 GLU A 73 2.09 85.79
REMARK 500 ASN A 74 -23.20 -151.59
REMARK 500 THR A 97 -2.43 87.49
REMARK 500 ASP A 127 51.62 -160.66
REMARK 500 ASP A 145 84.77 49.15
REMARK 500 VAL A 163 -71.28 -115.17
REMARK 500 SER A 181 -155.80 -147.49
REMARK 500 LYS A 242 76.92 -103.28
REMARK 500 THR A 290 -169.73 -121.79
REMARK 500 VAL B 175 71.68 25.76
REMARK 500 ASN B 431 65.01 66.01
REMARK 500 GLU C 8 134.78 -178.38
REMARK 500 THR C 41 -82.96 -126.49
REMARK 500 ASN C 74 -24.34 -150.99
REMARK 500 ASP C 127 54.83 -160.88
REMARK 500 ASP C 145 85.25 46.89
REMARK 500 VAL C 163 -72.83 -117.80
REMARK 500 SER C 181 -156.53 -147.89
REMARK 500 ARG C 199 -14.73 87.75
REMARK 500 LYS C 237 -145.00 -106.66
REMARK 500 SER C 239 115.38 168.40
REMARK 500 ASP C 247 -154.40 -139.52
REMARK 500 HIS C 295 7.93 -64.45
REMARK 500 VAL D 175 71.36 25.96
REMARK 500 LEU D 320 1.49 -67.16
REMARK 500 ASN D 431 74.93 68.97
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 F9Z A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F9Z C 301
DBREF 6GUB A 1 298 UNP P24941 CDK2_HUMAN 1 298
DBREF 6GUB B 172 432 UNP P30274 CCNA2_BOVIN 170 430
DBREF 6GUB C 1 298 UNP P24941 CDK2_HUMAN 1 298
DBREF 6GUB D 172 432 UNP P30274 CCNA2_BOVIN 170 430
SEQADV 6GUB GLY A -3 UNP P24941 EXPRESSION TAG
SEQADV 6GUB PRO A -2 UNP P24941 EXPRESSION TAG
SEQADV 6GUB GLY A -1 UNP P24941 EXPRESSION TAG
SEQADV 6GUB SER A 0 UNP P24941 EXPRESSION TAG
SEQADV 6GUB GLY B 171 UNP P30274 EXPRESSION TAG
SEQADV 6GUB HIS B 433 UNP P30274 EXPRESSION TAG
SEQADV 6GUB HIS B 434 UNP P30274 EXPRESSION TAG
SEQADV 6GUB HIS B 435 UNP P30274 EXPRESSION TAG
SEQADV 6GUB HIS B 436 UNP P30274 EXPRESSION TAG
SEQADV 6GUB HIS B 437 UNP P30274 EXPRESSION TAG
SEQADV 6GUB HIS B 438 UNP P30274 EXPRESSION TAG
SEQADV 6GUB GLY C -3 UNP P24941 EXPRESSION TAG
SEQADV 6GUB PRO C -2 UNP P24941 EXPRESSION TAG
SEQADV 6GUB GLY C -1 UNP P24941 EXPRESSION TAG
SEQADV 6GUB SER C 0 UNP P24941 EXPRESSION TAG
SEQADV 6GUB GLY D 171 UNP P30274 EXPRESSION TAG
SEQADV 6GUB HIS D 433 UNP P30274 EXPRESSION TAG
SEQADV 6GUB HIS D 434 UNP P30274 EXPRESSION TAG
SEQADV 6GUB HIS D 435 UNP P30274 EXPRESSION TAG
SEQADV 6GUB HIS D 436 UNP P30274 EXPRESSION TAG
SEQADV 6GUB HIS D 437 UNP P30274 EXPRESSION TAG
SEQADV 6GUB HIS D 438 UNP P30274 EXPRESSION TAG
SEQRES 1 A 302 GLY PRO GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS
SEQRES 2 A 302 ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG
SEQRES 3 A 302 ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE
SEQRES 4 A 302 ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR ALA
SEQRES 5 A 302 ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO
SEQRES 6 A 302 ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN
SEQRES 7 A 302 LYS LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU
SEQRES 8 A 302 LYS LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO
SEQRES 9 A 302 LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN
SEQRES 10 A 302 GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG
SEQRES 11 A 302 ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY
SEQRES 12 A 302 ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE
SEQRES 13 A 302 GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR
SEQRES 14 A 302 LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS
SEQRES 15 A 302 TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS
SEQRES 16 A 302 ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO
SEQRES 17 A 302 GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG
SEQRES 18 A 302 THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL
SEQRES 19 A 302 THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP
SEQRES 20 A 302 ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP
SEQRES 21 A 302 GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR
SEQRES 22 A 302 ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA
SEQRES 23 A 302 HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS
SEQRES 24 A 302 LEU ARG LEU
SEQRES 1 B 268 GLY VAL ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS
SEQRES 2 B 268 THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS
SEQRES 3 B 268 VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER
SEQRES 4 B 268 MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY
SEQRES 5 B 268 GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA
SEQRES 6 B 268 VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL
SEQRES 7 B 268 LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET
SEQRES 8 B 268 LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU
SEQRES 9 B 268 VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR
SEQRES 10 B 268 LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS
SEQRES 11 B 268 VAL LEU ALA PHE ASP LEU ALA ALA PRO THR ILE ASN GLN
SEQRES 12 B 268 PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN
SEQRES 13 B 268 CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU
SEQRES 14 B 268 SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO
SEQRES 15 B 268 SER VAL ILE ALA ALA ALA ALA PHE HIS LEU ALA LEU TYR
SEQRES 16 B 268 THR VAL THR GLY GLN SER TRP PRO GLU SER LEU VAL GLN
SEQRES 17 B 268 LYS THR GLY TYR THR LEU GLU THR LEU LYS PRO CYS LEU
SEQRES 18 B 268 LEU ASP LEU HIS GLN THR TYR LEU ARG ALA PRO GLN HIS
SEQRES 19 B 268 ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS
SEQRES 20 B 268 TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU
SEQRES 21 B 268 ASN VAL HIS HIS HIS HIS HIS HIS
SEQRES 1 C 302 GLY PRO GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS
SEQRES 2 C 302 ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG
SEQRES 3 C 302 ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE
SEQRES 4 C 302 ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR ALA
SEQRES 5 C 302 ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO
SEQRES 6 C 302 ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN
SEQRES 7 C 302 LYS LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU
SEQRES 8 C 302 LYS LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO
SEQRES 9 C 302 LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN
SEQRES 10 C 302 GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG
SEQRES 11 C 302 ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY
SEQRES 12 C 302 ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE
SEQRES 13 C 302 GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR
SEQRES 14 C 302 LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS
SEQRES 15 C 302 TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS
SEQRES 16 C 302 ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO
SEQRES 17 C 302 GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG
SEQRES 18 C 302 THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL
SEQRES 19 C 302 THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP
SEQRES 20 C 302 ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP
SEQRES 21 C 302 GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR
SEQRES 22 C 302 ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA
SEQRES 23 C 302 HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS
SEQRES 24 C 302 LEU ARG LEU
SEQRES 1 D 268 GLY VAL ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS
SEQRES 2 D 268 THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS
SEQRES 3 D 268 VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER
SEQRES 4 D 268 MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY
SEQRES 5 D 268 GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA
SEQRES 6 D 268 VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL
SEQRES 7 D 268 LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET
SEQRES 8 D 268 LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU
SEQRES 9 D 268 VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR
SEQRES 10 D 268 LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS
SEQRES 11 D 268 VAL LEU ALA PHE ASP LEU ALA ALA PRO THR ILE ASN GLN
SEQRES 12 D 268 PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN
SEQRES 13 D 268 CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU
SEQRES 14 D 268 SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO
SEQRES 15 D 268 SER VAL ILE ALA ALA ALA ALA PHE HIS LEU ALA LEU TYR
SEQRES 16 D 268 THR VAL THR GLY GLN SER TRP PRO GLU SER LEU VAL GLN
SEQRES 17 D 268 LYS THR GLY TYR THR LEU GLU THR LEU LYS PRO CYS LEU
SEQRES 18 D 268 LEU ASP LEU HIS GLN THR TYR LEU ARG ALA PRO GLN HIS
SEQRES 19 D 268 ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS
SEQRES 20 D 268 TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU
SEQRES 21 D 268 ASN VAL HIS HIS HIS HIS HIS HIS
MODRES 6GUB TPO A 160 THR MODIFIED RESIDUE
MODRES 6GUB TPO C 160 THR MODIFIED RESIDUE
HET TPO A 160 11
HET TPO C 160 11
HET F9Z A 301 28
HET F9Z C 301 28
HETNAM TPO PHOSPHOTHREONINE
HETNAM F9Z 2-(2-CHLOROPHENYL)-8-[(3~{R},4~{R})-1-METHYL-3-
HETNAM 2 F9Z OXIDANYL-PIPERIDIN-4-YL]-5,7-BIS(OXIDANYL)CHROMEN-4-
HETNAM 3 F9Z ONE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 TPO 2(C4 H10 N O6 P)
FORMUL 5 F9Z 2(C21 H20 CL N O5)
FORMUL 7 HOH *72(H2 O)
HELIX 1 AA1 PRO A 45 LEU A 58 1 14
HELIX 2 AA2 LEU A 87 SER A 94 1 8
HELIX 3 AA3 PRO A 100 HIS A 121 1 22
HELIX 4 AA4 LYS A 129 GLN A 131 5 3
HELIX 5 AA5 THR A 165 ARG A 169 5 5
HELIX 6 AA6 ALA A 170 LEU A 175 1 6
HELIX 7 AA7 THR A 182 ARG A 199 1 18
HELIX 8 AA8 SER A 207 GLY A 220 1 14
HELIX 9 AA9 GLY A 229 MET A 233 5 5
HELIX 10 AB1 ASP A 247 VAL A 252 1 6
HELIX 11 AB2 ASP A 256 LEU A 267 1 12
HELIX 12 AB3 SER A 276 LEU A 281 1 6
HELIX 13 AB4 ALA A 282 GLN A 287 5 6
HELIX 14 AB5 TYR B 178 CYS B 193 1 16
HELIX 15 AB6 THR B 207 TYR B 225 1 19
HELIX 16 AB7 GLN B 228 MET B 246 1 19
HELIX 17 AB8 LEU B 249 GLY B 251 5 3
HELIX 18 AB9 LYS B 252 GLU B 269 1 18
HELIX 19 AC1 GLU B 274 ILE B 281 1 8
HELIX 20 AC2 THR B 287 ALA B 303 1 17
HELIX 21 AC3 THR B 310 LEU B 320 1 11
HELIX 22 AC4 ASN B 326 LEU B 341 1 16
HELIX 23 AC5 ASP B 343 LEU B 348 1 6
HELIX 24 AC6 LEU B 351 GLY B 369 1 19
HELIX 25 AC7 PRO B 373 GLY B 381 1 9
HELIX 26 AC8 LEU B 387 ALA B 401 1 15
HELIX 27 AC9 PRO B 402 HIS B 404 5 3
HELIX 28 AD1 GLN B 407 TYR B 413 1 7
HELIX 29 AD2 LYS B 414 HIS B 419 5 6
HELIX 30 AD3 GLY B 420 LEU B 424 5 5
HELIX 31 AD4 PRO C 45 LEU C 58 1 14
HELIX 32 AD5 LEU C 87 SER C 94 1 8
HELIX 33 AD6 PRO C 100 HIS C 121 1 22
HELIX 34 AD7 LYS C 129 GLN C 131 5 3
HELIX 35 AD8 THR C 165 ARG C 169 5 5
HELIX 36 AD9 ALA C 170 LEU C 175 1 6
HELIX 37 AE1 THR C 182 ARG C 199 1 18
HELIX 38 AE2 SER C 207 GLY C 220 1 14
HELIX 39 AE3 GLY C 229 MET C 233 5 5
HELIX 40 AE4 ASP C 256 LEU C 267 1 12
HELIX 41 AE5 SER C 276 LEU C 281 1 6
HELIX 42 AE6 ALA C 282 GLN C 287 5 6
HELIX 43 AE7 TYR D 178 CYS D 193 1 16
HELIX 44 AE8 THR D 207 TYR D 225 1 19
HELIX 45 AE9 GLN D 228 MET D 246 1 19
HELIX 46 AF1 LEU D 249 GLY D 251 5 3
HELIX 47 AF2 LYS D 252 GLU D 269 1 18
HELIX 48 AF3 GLU D 274 ILE D 281 1 8
HELIX 49 AF4 THR D 287 LEU D 302 1 16
HELIX 50 AF5 THR D 310 LEU D 320 1 11
HELIX 51 AF6 ASN D 326 LEU D 341 1 16
HELIX 52 AF7 ASP D 343 LEU D 348 1 6
HELIX 53 AF8 LEU D 351 GLY D 369 1 19
HELIX 54 AF9 PRO D 373 GLY D 381 1 9
HELIX 55 AG1 LEU D 387 ALA D 401 1 15
HELIX 56 AG2 PRO D 402 HIS D 404 5 3
HELIX 57 AG3 GLN D 407 ASN D 415 1 9
HELIX 58 AG4 SER D 416 HIS D 419 5 4
HELIX 59 AG5 GLY D 420 LEU D 424 5 5
SHEET 1 AA1 5 PHE A 4 GLY A 13 0
SHEET 2 AA1 5 GLY A 16 ASN A 23 -1 O LYS A 20 N GLU A 8
SHEET 3 AA1 5 VAL A 29 ILE A 35 -1 O LEU A 32 N TYR A 19
SHEET 4 AA1 5 LEU A 76 GLU A 81 -1 O LEU A 76 N ILE A 35
SHEET 5 AA1 5 LEU A 66 HIS A 71 -1 N LEU A 67 O VAL A 79
SHEET 1 AA2 3 GLN A 85 ASP A 86 0
SHEET 2 AA2 3 LEU A 133 ILE A 135 -1 O ILE A 135 N GLN A 85
SHEET 3 AA2 3 ILE A 141 LEU A 143 -1 O LYS A 142 N LEU A 134
SHEET 1 AA3 2 VAL A 123 LEU A 124 0
SHEET 2 AA3 2 ARG A 150 ALA A 151 -1 O ARG A 150 N LEU A 124
SHEET 1 AA4 5 PHE C 4 GLY C 13 0
SHEET 2 AA4 5 GLY C 16 ASN C 23 -1 O LYS C 20 N VAL C 7
SHEET 3 AA4 5 VAL C 29 ARG C 36 -1 O LEU C 32 N TYR C 19
SHEET 4 AA4 5 LYS C 75 GLU C 81 -1 O LEU C 76 N ILE C 35
SHEET 5 AA4 5 LEU C 66 ILE C 70 -1 N LEU C 67 O VAL C 79
SHEET 1 AA5 3 GLN C 85 ASP C 86 0
SHEET 2 AA5 3 LEU C 133 ILE C 135 -1 O ILE C 135 N GLN C 85
SHEET 3 AA5 3 ILE C 141 LEU C 143 -1 O LYS C 142 N LEU C 134
SHEET 1 AA6 2 VAL C 123 LEU C 124 0
SHEET 2 AA6 2 ARG C 150 ALA C 151 -1 O ARG C 150 N LEU C 124
LINK C TYR A 159 N TPO A 160 1555 1555 1.33
LINK C TPO A 160 N HIS A 161 1555 1555 1.34
LINK C TYR C 159 N TPO C 160 1555 1555 1.33
LINK C TPO C 160 N HIS C 161 1555 1555 1.34
CISPEP 1 VAL A 154 PRO A 155 0 -14.69
CISPEP 2 GLN B 323 PRO B 324 0 -5.52
CISPEP 3 ASP B 345 PRO B 346 0 8.56
CISPEP 4 VAL C 154 PRO C 155 0 -11.90
CISPEP 5 GLN D 323 PRO D 324 0 2.17
CISPEP 6 ASP D 345 PRO D 346 0 9.44
SITE 1 AC1 13 ILE A 10 TYR A 15 ALA A 31 LYS A 33
SITE 2 AC1 13 VAL A 64 PHE A 80 GLU A 81 PHE A 82
SITE 3 AC1 13 LEU A 83 HIS A 84 LEU A 134 ASP A 145
SITE 4 AC1 13 HOH A 409
SITE 1 AC2 13 ILE C 10 ALA C 31 LYS C 33 VAL C 64
SITE 2 AC2 13 PHE C 80 GLU C 81 LEU C 83 HIS C 84
SITE 3 AC2 13 GLN C 131 ASN C 132 LEU C 134 ASP C 145
SITE 4 AC2 13 HOH C 405
CRYST1 75.184 136.224 149.973 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013301 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007341 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006668 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
