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Database: PDB
Entry: 1FIN
LinkDB: 1FIN
Original site: 1FIN 
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              
SOURCE  24 WAS PRODUCED BY THE CLEAVAGE OF FULL-LENGTH CYCLIN A BY              
SOURCE  25 SUBTILISIN                                                           
KEYWDS    COMPLEX (TRANSFERASE/CYCLIN), CYCLIN, CDK, PHOSPHORYLATION            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.D.JEFFREY,A.A.RUSSO,N.P.PAVLETICH                                   
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,            
JRNL        AUTH 2 J.MASSAGUE,N.P.PAVLETICH                                     
JRNL        TITL   MECHANISM OF CDK ACTIVATION REVEALED BY THE                  
JRNL        TITL 2 STRUCTURE OF A CYCLINA-CDK2 COMPLEX.                         
JRNL        REF    NATURE                        V. 376   313 1995              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   7630397                                                      
JRNL        DOI    10.1038/376313A0                                             
REMARK   1                                                                      
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. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
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. = -16.5 DEGREES          
REMARK 500    PRO B 346   C   -  N   -  CD  ANGL. DEV. = -19.1 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 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                                                                             
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