HEADER COMPLEX (TRANSFERASE/CYCLIN) 14-JUL-96 1FIN
TITLE CYCLIN A-CYCLIN-DEPENDENT KINASE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: CDK2;
COMPND 5 EC: 2.7.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CYCLIN A;
COMPND 9 CHAIN: B, D;
COMPND 10 FRAGMENT: RESIDUES 173 - 432;
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 CELL_LINE: SF9;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS VECTOR;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 13 MOL_ID: 2;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606;
SOURCE 17 CELL_LINE: SF9;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 23 OTHER_DETAILS: THE FRAGMENT USED IN THE CRYSTALLIZATION WAS PRODUCED
SOURCE 24 BY THE CLEAVAGE OF FULL-LENGTH CYCLIN A BY SUBTILISIN
KEYWDS COMPLEX (TRANSFERASE-CYCLIN), CYCLIN, CDK, PHOSPHORYLATION, COMPLEX
KEYWDS 2 (TRANSFERASE-CYCLIN) COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.D.JEFFREY,A.A.RUSSO,N.P.PAVLETICH
REVDAT 3 07-FEB-24 1FIN 1 REMARK
REVDAT 2 24-FEB-09 1FIN 1 VERSN
REVDAT 1 27-JAN-97 1FIN 0
JRNL AUTH P.D.JEFFREY,A.A.RUSSO,K.POLYAK,E.GIBBS,J.HURWITZ,J.MASSAGUE,
JRNL AUTH 2 N.P.PAVLETICH
JRNL TITL MECHANISM OF CDK ACTIVATION REVEALED BY THE STRUCTURE OF A
JRNL TITL 2 CYCLINA-CDK2 COMPLEX.
JRNL REF NATURE V. 376 313 1995
JRNL REFN ISSN 0028-0836
JRNL PMID 7630397
JRNL DOI 10.1038/376313A0
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 3 NUMBER OF REFLECTIONS : 70208
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8998
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 416
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.013 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 1.770 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FIN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173301.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-FEB-95
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.920
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86466
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 200 DATA REDUNDANCY : 7.800
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+2/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+1/3
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 142.93333
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 71.46667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 142.93333
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 71.46667
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 142.93333
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 71.46667
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 142.93333
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 71.46667
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: 4170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22830 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: 4050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 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 GLU B 174 N - CA - C ANGL. DEV. = 19.9 DEGREES
REMARK 500 PRO B 176 C - N - CD ANGL. DEV. = -24.3 DEGREES
REMARK 500 PRO B 346 C - N - CD ANGL. DEV. = -26.9 DEGREES
REMARK 500 PRO D 346 C - N - CD ANGL. DEV. = -18.8 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 GLU A 8 141.83 -172.73
REMARK 500 LEU A 37 104.34 85.81
REMARK 500 THR A 39 43.20 -71.99
REMARK 500 GLU A 40 -41.39 -165.28
REMARK 500 GLU A 42 -52.42 -155.85
REMARK 500 LEU A 58 79.82 -103.49
REMARK 500 THR A 72 -142.88 -150.62
REMARK 500 GLU A 73 -89.44 -45.07
REMARK 500 LEU A 96 -66.71 97.18
REMARK 500 ASP A 127 41.34 -152.91
REMARK 500 PRO A 130 -35.93 -38.97
REMARK 500 ASP A 145 70.41 60.17
REMARK 500 PRO A 155 130.00 -27.17
REMARK 500 GLN A 287 20.39 -61.63
REMARK 500 ASP A 288 11.17 -161.13
REMARK 500 VAL A 289 154.41 -47.48
REMARK 500 GLU B 174 18.54 -31.38
REMARK 500 PRO B 176 -24.48 -26.15
REMARK 500 LYS B 194 128.72 -34.70
REMARK 500 PRO B 204 -73.53 -62.03
REMARK 500 SER B 245 18.57 -152.38
REMARK 500 ARG B 250 -34.48 -37.18
REMARK 500 TYR B 271 115.86 -163.90
REMARK 500 ASP B 284 19.09 58.85
REMARK 500 PHE B 304 17.71 52.05
REMARK 500 ASP B 345 -49.19 -21.99
REMARK 500 TRP B 372 102.26 -40.91
REMARK 500 GLU C 12 -172.31 -176.04
REMARK 500 THR C 14 -97.78 74.70
REMARK 500 LEU C 37 131.70 84.67
REMARK 500 GLU C 42 -55.25 -139.07
REMARK 500 ASN C 74 -73.84 -70.22
REMARK 500 THR C 97 -50.05 -164.26
REMARK 500 ARG C 126 -0.73 67.73
REMARK 500 ASP C 127 53.08 -148.13
REMARK 500 ASP C 145 80.37 60.06
REMARK 500 PHE C 152 -141.83 -87.26
REMARK 500 PRO C 204 63.33 -68.84
REMARK 500 GLU C 224 0.19 -58.92
REMARK 500 PRO C 228 -23.72 -37.30
REMARK 500 PRO C 234 -15.20 -45.03
REMARK 500 VAL C 289 140.09 -32.88
REMARK 500 PRO C 294 172.41 -56.35
REMARK 500 ARG C 297 36.36 -87.27
REMARK 500 GLU D 174 82.21 -157.43
REMARK 500 PRO D 176 -70.38 -30.23
REMARK 500 CYS D 193 41.09 -83.65
REMARK 500 ASP D 345 -64.79 -18.53
REMARK 500 LEU D 348 -8.83 -59.76
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 ATP A 299
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C 299
DBREF 1FIN A 1 298 UNP P24941 CDK2_HUMAN 1 298
DBREF 1FIN B 173 432 UNP P20248 CCNA2_HUMAN 173 432
DBREF 1FIN C 1 298 UNP P24941 CDK2_HUMAN 1 298
DBREF 1FIN D 173 432 UNP P20248 CCNA2_HUMAN 173 432
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
SEQRES 1 B 260 ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR
SEQRES 2 B 260 LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY
SEQRES 3 B 260 TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG
SEQRES 4 B 260 ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU
SEQRES 5 B 260 TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN
SEQRES 6 B 260 TYR ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG
SEQRES 7 B 260 GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU
SEQRES 8 B 260 ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA
SEQRES 9 B 260 GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS
SEQRES 10 B 260 GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU
SEQRES 11 B 260 THR PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU
SEQRES 12 B 260 THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS
SEQRES 13 B 260 VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU
SEQRES 14 B 260 ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL
SEQRES 15 B 260 ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL
SEQRES 16 B 260 THR GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR
SEQRES 17 B 260 GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP
SEQRES 18 B 260 LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN
SEQRES 19 B 260 GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS
SEQRES 20 B 260 GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU
SEQRES 1 C 298 MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY
SEQRES 2 C 298 THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR
SEQRES 3 C 298 GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR
SEQRES 4 C 298 GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE
SEQRES 5 C 298 SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS
SEQRES 6 C 298 LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU
SEQRES 7 C 298 VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET
SEQRES 8 C 298 ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE
SEQRES 9 C 298 LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE
SEQRES 10 C 298 CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO
SEQRES 11 C 298 GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU
SEQRES 12 C 298 ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL
SEQRES 13 C 298 ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG
SEQRES 14 C 298 ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR
SEQRES 15 C 298 ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU
SEQRES 16 C 298 MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU
SEQRES 17 C 298 ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR
SEQRES 18 C 298 PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO
SEQRES 19 C 298 ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP
SEQRES 20 C 298 PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG
SEQRES 21 C 298 SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS
SEQRES 22 C 298 ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE
SEQRES 23 C 298 GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU
SEQRES 1 D 260 ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR
SEQRES 2 D 260 LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY
SEQRES 3 D 260 TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG
SEQRES 4 D 260 ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU
SEQRES 5 D 260 TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN
SEQRES 6 D 260 TYR ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG
SEQRES 7 D 260 GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU
SEQRES 8 D 260 ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA
SEQRES 9 D 260 GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS
SEQRES 10 D 260 GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU
SEQRES 11 D 260 THR PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU
SEQRES 12 D 260 THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS
SEQRES 13 D 260 VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU
SEQRES 14 D 260 ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL
SEQRES 15 D 260 ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL
SEQRES 16 D 260 THR GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR
SEQRES 17 D 260 GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP
SEQRES 18 D 260 LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN
SEQRES 19 D 260 GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS
SEQRES 20 D 260 GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU
HET ATP A 299 31
HET ATP C 299 31
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 5 ATP 2(C10 H16 N5 O13 P3)
FORMUL 7 HOH *416(H2 O)
HELIX 1 1 SER A 46 GLU A 57 1 12
HELIX 2 2 LEU A 87 ALA A 93 1 7
HELIX 3 3 LEU A 101 HIS A 121 1 21
HELIX 4 4 PRO A 130 ASN A 132 5 3
HELIX 5 5 PHE A 146 LEU A 148 5 3
HELIX 6 6 LEU A 166 TYR A 168 5 3
HELIX 7 7 PRO A 171 LEU A 174 1 4
HELIX 8 8 THR A 182 THR A 198 1 17
HELIX 9 9 GLU A 208 LEU A 219 1 12
HELIX 10 10 VAL A 230 SER A 232 5 3
HELIX 11 11 PHE A 248 VAL A 251 1 4
HELIX 12 12 GLU A 257 MET A 266 1 10
HELIX 13 13 ALA A 277 ALA A 282 1 6
HELIX 14 14 PRO A 284 PHE A 286 5 3
HELIX 15 15 PRO B 176 CYS B 193 5 18
HELIX 16 16 ASN B 208 TYR B 225 1 18
HELIX 17 17 ASN B 229 SER B 244 1 16
HELIX 18 18 ARG B 250 GLU B 268 5 19
HELIX 19 19 VAL B 275 THR B 282 1 8
HELIX 20 20 LYS B 288 LEU B 302 1 15
HELIX 21 21 VAL B 311 HIS B 321 1 11
HELIX 22 22 CYS B 327 ILE B 342 1 16
HELIX 23 23 ALA B 344 LYS B 349 1 6
HELIX 24 24 PRO B 352 THR B 368 1 17
HELIX 25 25 GLU B 374 THR B 380 1 7
HELIX 26 26 LEU B 384 GLN B 403 1 20
HELIX 27 27 SER B 408 LYS B 414 1 7
HELIX 28 28 SER B 416 TYR B 418 5 3
HELIX 29 29 VAL B 421 LEU B 423 5 3
HELIX 30 30 SER C 46 LEU C 55 1 10
HELIX 31 31 LEU C 87 SER C 94 1 8
HELIX 32 32 LEU C 101 HIS C 121 1 21
HELIX 33 33 PRO C 130 ASN C 132 5 3
HELIX 34 34 LEU C 166 TYR C 168 5 3
HELIX 35 35 PRO C 171 LEU C 174 1 4
HELIX 36 36 THR C 182 THR C 198 1 17
HELIX 37 37 GLU C 208 LEU C 219 1 12
HELIX 38 38 VAL C 230 SER C 232 5 3
HELIX 39 39 PHE C 248 VAL C 251 1 4
HELIX 40 40 GLU C 257 MET C 266 1 10
HELIX 41 41 ALA C 277 ALA C 282 1 6
HELIX 42 42 PRO C 284 ASP C 288 5 5
HELIX 43 43 VAL D 175 GLU D 190 1 16
HELIX 44 44 ASN D 208 TYR D 225 1 18
HELIX 45 45 ASN D 229 LEU D 243 1 15
HELIX 46 46 ARG D 250 GLU D 268 1 19
HELIX 47 47 VAL D 275 ILE D 281 1 7
HELIX 48 48 LYS D 288 VAL D 301 1 14
HELIX 49 49 VAL D 311 HIS D 321 1 11
HELIX 50 50 CYS D 327 ILE D 342 1 16
HELIX 51 51 ALA D 344 LYS D 349 1 6
HELIX 52 52 PRO D 352 VAL D 367 1 16
HELIX 53 53 GLU D 374 THR D 380 1 7
HELIX 54 54 LEU D 384 GLN D 403 1 20
HELIX 55 55 SER D 408 LYS D 414 1 7
HELIX 56 56 SER D 416 TYR D 418 5 3
HELIX 57 57 VAL D 421 LEU D 423 5 3
SHEET 1 A 5 LEU A 66 HIS A 71 0
SHEET 2 A 5 LEU A 76 GLU A 81 -1 N VAL A 79 O LEU A 67
SHEET 3 A 5 VAL A 29 ILE A 35 -1 N ILE A 35 O LEU A 76
SHEET 4 A 5 GLY A 16 ASN A 23 -1 N ALA A 21 O VAL A 30
SHEET 5 A 5 PHE A 4 LYS A 9 -1 N GLU A 8 O LYS A 20
SHEET 1 B 2 LEU A 133 ILE A 135 0
SHEET 2 B 2 ILE A 141 LEU A 143 -1 N LYS A 142 O LEU A 134
SHEET 1 C 5 LEU C 66 HIS C 71 0
SHEET 2 C 5 LEU C 76 GLU C 81 -1 N VAL C 79 O LEU C 67
SHEET 3 C 5 VAL C 29 ILE C 35 -1 N ILE C 35 O LEU C 76
SHEET 4 C 5 VAL C 18 ASN C 23 -1 N ALA C 21 O VAL C 30
SHEET 5 C 5 PHE C 4 LYS C 9 -1 N GLU C 8 O LYS C 20
SHEET 1 D 2 LEU C 133 ILE C 135 0
SHEET 2 D 2 ILE C 141 LEU C 143 -1 N LYS C 142 O LEU C 134
CISPEP 1 GLN B 323 PRO B 324 0 -1.06
CISPEP 2 GLN D 323 PRO D 324 0 0.64
SITE 1 AC1 12 ILE A 10 GLU A 12 GLY A 13 GLU A 81
SITE 2 AC1 12 PHE A 82 LEU A 83 GLN A 131 ASN A 132
SITE 3 AC1 12 LEU A 134 ASP A 145 HOH A 424 HOH A 429
SITE 1 AC2 13 ILE C 10 GLY C 11 GLU C 12 GLY C 13
SITE 2 AC2 13 THR C 14 VAL C 18 ALA C 31 VAL C 64
SITE 3 AC2 13 GLU C 81 PHE C 82 LEU C 83 HOH C 318
SITE 4 AC2 13 HOH C 338
CRYST1 185.100 185.100 214.400 90.00 90.00 120.00 P 62 2 2 24
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 0.005402 0.003119 0.000000 0.00000
SCALE2 0.000000 0.006238 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004664 0.00000
(ATOM LINES ARE NOT SHOWN.)
END