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Database: PDB
Entry: 2C5X
LinkDB: 2C5X
Original site: 2C5X 
HEADER    TRANSFERASE/INHIBITOR                   03-NOV-05   2C5X              
TITLE     DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2        
TITLE    2 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CYCLIN DEPENDENT KINASE 2, P33 PROTEIN KINASE;              
COMPND   5 EC: 2.7.1.37;                                                        
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 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE/INHIBITOR, INHIBITION, ACTIVE, INACTIVE, CDK2, CELL       
KEYWDS   2 CYCLE, CELL DIVISION, KINASE, MITOSIS, SERINE/THREONINE-PROTEIN      
KEYWDS   3 KINASE, TRANSFERASE, ATP-BINDING, COMPLEX (TRANSFERASE-INHIBITOR),   
KEYWDS   4 TRANSFERASE-INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.KONTOPIDIS,C.MCINNES,S.R.PANDALANENI,I.MCNAE,D.GIBSON,M.MEZNA,      
AUTHOR   2 M.THOMAS,G.WOOD,S.WANG,M.D.WALKINSHAW,P.M.FISCHER                    
REVDAT   3   03-APR-19 2C5X    1       SOURCE                                   
REVDAT   2   24-FEB-09 2C5X    1       VERSN                                    
REVDAT   1   01-MAR-06 2C5X    0                                                
JRNL        AUTH   G.KONTOPIDIS,C.MCINNES,S.R.PANDALANENI,I.MCNAE,D.GIBSON,     
JRNL        AUTH 2 M.MEZNA,M.THOMAS,G.WOOD,S.WANG,M.D.WALKINSHAW,P.M.FISCHER    
JRNL        TITL   DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE    
JRNL        TITL 2 CDK2 PROVIDES INSIGHTS FOR DRUG DESIGN.                      
JRNL        REF    CHEM.BIOL.                    V.  13   201 2006              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   16492568                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2005.11.011                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 27911                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1197                            
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.97                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1975                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4110                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 91                           
REMARK   3   BIN FREE R VALUE                    : 0.3650                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8923                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 88                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.31000                                             
REMARK   3    B22 (A**2) : -2.45000                                             
REMARK   3    B33 (A**2) : 5.76000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.445         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.338         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.517        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.865                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9230 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12538 ; 2.918 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1108 ;12.688 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   396 ;43.654 ;23.965       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1618 ;26.959 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;25.885 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1412 ; 0.204 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6898 ; 0.019 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  5860 ; 0.370 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6380 ; 0.387 ; 0.500       
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):    60 ; 0.331 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.549 ; 0.500       
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):  5653 ; 3.432 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9066 ; 5.455 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3956 ; 9.316 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3472 ;12.919 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     296      2                      
REMARK   3           1     C      1       C     296      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1180 ;  0.27 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1188 ;  0.69 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1180 ;  0.70 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1188 ;  4.15 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B    175       B     432      2                      
REMARK   3           1     D    175       D     432      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):   1027 ;  0.20 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):   1048 ;  0.58 ;  0.50           
REMARK   3   TIGHT THERMAL      2    B (A**2):   1027 ;  0.66 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    B (A**2):   1048 ;  3.98 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
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 2C5X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-NOV-05.                  
REMARK 100 THE DEPOSITION ID IS D_1290026247.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUN-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.80                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.44                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29878                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.16000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.73000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1OL1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 3350, 0.1M NA3-CIT, PH 7.80      
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       37.16700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       77.45550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.17600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       77.45550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.16700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.17600            
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: PQS                                                   
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: PQS                                                   
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     ARG A   297                                                      
REMARK 465     LEU A   298                                                      
REMARK 465     GLU B   174                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     GLU D   174                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HIS C   268     O    TYR C   269              1.27            
REMARK 500   O    VAL B   175     N    ASP B   177              1.64            
REMARK 500   O    VAL C   230     N    SER C   232              1.90            
REMARK 500   O    THR B   282     CG2  THR B   285              1.94            
REMARK 500   O    GLU C    40     NZ   LYS D   288              1.96            
REMARK 500   O    THR A    14     N    GLY A    16              2.01            
REMARK 500   O    HIS D   419     O    HOH D  2015              2.04            
REMARK 500   NE2  HIS A    71     ND1  HIS B   296              2.04            
REMARK 500   O    THR C   165     O    HOH C  2012              2.04            
REMARK 500   OE2  GLU A   224     OG1  THR A   231              2.07            
REMARK 500   O    ARG C   260     OG   SER C   264              2.09            
REMARK 500   OD1  ASN B   415     N    LYS B   417              2.10            
REMARK 500   OD1  ASN D   415     N    LYS D   417              2.11            
REMARK 500   N    ILE C    70     O    TYR C    77              2.11            
REMARK 500   O    THR C   165     O    HOH C  2013              2.13            
REMARK 500   CB   VAL C   164     O    HOH C  2013              2.14            
REMARK 500   O    TYR C   159     N    HIS C   161              2.14            
REMARK 500   OG1  THR D   383     OG   SER D   386              2.14            
REMARK 500   O    HIS B   419     N    VAL B   421              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   ND2  ASN B   431     OD1  ASP C   210     2664     1.73            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    THR A  14   N   -  CA  -  C   ANGL. DEV. = -22.4 DEGREES          
REMARK 500    VAL A  30   CG1 -  CB  -  CG2 ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    LEU A  32   CB  -  CG  -  CD1 ANGL. DEV. = -17.1 DEGREES          
REMARK 500    PRO A  61   C   -  N   -  CA  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    PRO A 102   C   -  N   -  CA  ANGL. DEV. =  10.8 DEGREES          
REMARK 500    LEU A 108   CB  -  CG  -  CD1 ANGL. DEV. = -15.1 DEGREES          
REMARK 500    LEU A 124   CB  -  CA  -  C   ANGL. DEV. = -11.8 DEGREES          
REMARK 500    LEU A 124   CB  -  CG  -  CD1 ANGL. DEV. = -14.3 DEGREES          
REMARK 500    LEU A 133   CB  -  CG  -  CD1 ANGL. DEV. = -10.5 DEGREES          
REMARK 500    LEU A 255   CB  -  CG  -  CD1 ANGL. DEV. = -12.6 DEGREES          
REMARK 500    ARG A 274   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    LEU A 281   CB  -  CG  -  CD2 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    PRO A 284   C   -  N   -  CA  ANGL. DEV. =  11.3 DEGREES          
REMARK 500    LEU B 186   CA  -  CB  -  CG  ANGL. DEV. = -17.3 DEGREES          
REMARK 500    LEU B 186   CB  -  CG  -  CD1 ANGL. DEV. =  10.4 DEGREES          
REMARK 500    VAL B 248   CB  -  CA  -  C   ANGL. DEV. = -11.5 DEGREES          
REMARK 500    LEU B 302   CB  -  CG  -  CD1 ANGL. DEV. = -13.4 DEGREES          
REMARK 500    LEU B 332   CB  -  CG  -  CD1 ANGL. DEV. = -11.9 DEGREES          
REMARK 500    LEU B 339   CB  -  CG  -  CD2 ANGL. DEV. = -12.5 DEGREES          
REMARK 500    PRO B 346   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    LEU B 376   CB  -  CG  -  CD2 ANGL. DEV. =  11.1 DEGREES          
REMARK 500    VAL C  18   CB  -  CA  -  C   ANGL. DEV. = -12.5 DEGREES          
REMARK 500    LEU C  25   CA  -  CB  -  CG  ANGL. DEV. = -15.4 DEGREES          
REMARK 500    LEU C  25   CB  -  CG  -  CD2 ANGL. DEV. = -13.7 DEGREES          
REMARK 500    VAL C  64   CB  -  CA  -  C   ANGL. DEV. = -13.7 DEGREES          
REMARK 500    PRO C 102   C   -  N   -  CA  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    LEU C 124   CB  -  CA  -  C   ANGL. DEV. = -12.5 DEGREES          
REMARK 500    LEU C 124   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    LEU C 124   CB  -  CG  -  CD1 ANGL. DEV. = -11.1 DEGREES          
REMARK 500    LEU C 133   CB  -  CG  -  CD2 ANGL. DEV. = -11.4 DEGREES          
REMARK 500    CYS C 177   CA  -  CB  -  SG  ANGL. DEV. = -11.6 DEGREES          
REMARK 500    LEU C 189   CB  -  CG  -  CD1 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    PRO C 204   C   -  N   -  CA  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ASP C 206   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP C 270   N   -  CA  -  CB  ANGL. DEV. =  11.3 DEGREES          
REMARK 500    ASP C 270   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG C 274   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    PRO D 176   C   -  N   -  CA  ANGL. DEV. = -23.1 DEGREES          
REMARK 500    PRO D 176   C   -  N   -  CD  ANGL. DEV. =  19.4 DEGREES          
REMARK 500    ASP D 181   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    LEU D 227   CB  -  CG  -  CD1 ANGL. DEV. = -14.2 DEGREES          
REMARK 500    LEU D 232   CB  -  CG  -  CD1 ANGL. DEV. = -15.3 DEGREES          
REMARK 500    MET D 246   CG  -  SD  -  CE  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    ARG D 250   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    LEU D 320   CA  -  CB  -  CG  ANGL. DEV. = -16.4 DEGREES          
REMARK 500    PRO D 346   C   -  N   -  CA  ANGL. DEV. =  13.5 DEGREES          
REMARK 500    LEU D 362   CB  -  CG  -  CD2 ANGL. DEV. = -11.2 DEGREES          
REMARK 500    ASP D 393   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 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    THR A  14      143.68    171.74                                   
REMARK 500    TYR A  15       55.97      0.63                                   
REMARK 500    ARG A  36       89.71    -34.65                                   
REMARK 500    THR A  39       30.72    -82.93                                   
REMARK 500    GLU A  40      -37.25   -133.97                                   
REMARK 500    HIS A  60      150.78    164.14                                   
REMARK 500    ASP A  68      142.29    176.16                                   
REMARK 500    THR A  72     -159.31    -78.49                                   
REMARK 500    LYS A  88      -72.54    -48.73                                   
REMARK 500    ALA A  93        2.40    -69.12                                   
REMARK 500    LEU A  96      -63.08     88.37                                   
REMARK 500    PRO A 100      117.35    -35.89                                   
REMARK 500    LEU A 101      -59.55    -17.16                                   
REMARK 500    ARG A 122       37.46     74.85                                   
REMARK 500    ARG A 126      -15.18     63.25                                   
REMARK 500    LYS A 129      146.67   -174.29                                   
REMARK 500    ASP A 145       81.13     64.88                                   
REMARK 500    PHE A 146       31.90    -99.82                                   
REMARK 500    HIS A 161       59.02   -110.78                                   
REMARK 500    GLU A 162      103.37    -34.04                                   
REMARK 500    THR A 165      156.35    122.49                                   
REMARK 500    LEU A 166     -115.33    -96.74                                   
REMARK 500    TRP A 167      -47.85     57.50                                   
REMARK 500    THR A 182      -52.55    -28.72                                   
REMARK 500    MET A 196      -48.08    -23.79                                   
REMARK 500    ALA A 201      116.81    -14.85                                   
REMARK 500    PHE A 203       56.04   -140.64                                   
REMARK 500    THR A 218      -71.27   -107.72                                   
REMARK 500    ASP A 223     -158.12   -123.54                                   
REMARK 500    TRP A 227       84.78   -152.36                                   
REMARK 500    VAL A 230      -69.17    -19.71                                   
REMARK 500    THR A 231      -19.57    -46.98                                   
REMARK 500    ARG A 245      129.35    -39.33                                   
REMARK 500    LYS A 278      -70.27    -23.90                                   
REMARK 500    PRO A 284      -37.66    -35.29                                   
REMARK 500    THR A 290     -115.83   -128.92                                   
REMARK 500    LYS A 291       46.76    175.22                                   
REMARK 500    PRO B 176       27.37    -18.75                                   
REMARK 500    CYS B 193       30.81    -82.10                                   
REMARK 500    LYS B 226       64.29     37.24                                   
REMARK 500    ARG B 250      -27.32    -39.49                                   
REMARK 500    ASP B 284       74.35     17.93                                   
REMARK 500    THR B 303       67.31     27.50                                   
REMARK 500    PHE B 304       17.71     35.77                                   
REMARK 500    THR B 316      -50.58    -29.53                                   
REMARK 500    HIS B 321       51.96   -102.64                                   
REMARK 500    ASN B 326      116.40    173.71                                   
REMARK 500    LEU B 336      -74.75    -52.30                                   
REMARK 500    GLU B 338      -53.44    -29.53                                   
REMARK 500    LEU B 339      -32.26    -33.70                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     134 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A   11     GLU A   12                  145.07                    
REMARK 500 GLY A   13     THR A   14                 -145.08                    
REMARK 500 TYR A   19     LYS A   20                  145.17                    
REMARK 500 ASN A   59     HIS A   60                 -149.92                    
REMARK 500 ASN A   62     ILE A   63                  147.41                    
REMARK 500 MET A   91     ASP A   92                  140.81                    
REMARK 500 LEU A  166     TRP A  167                  121.28                    
REMARK 500 HIS A  295     LEU A  296                 -146.17                    
REMARK 500 ILE B  270     TYR B  271                  137.19                    
REMARK 500 PRO B  272     PRO B  273                  149.06                    
REMARK 500 LEU B  336     GLY B  337                  125.80                    
REMARK 500 SER B  340     LEU B  341                  149.61                    
REMARK 500 ALA B  344     ASP B  345                  133.74                    
REMARK 500 ASP B  345     PRO B  346                  145.85                    
REMARK 500 LEU B  423     LEU B  424                  127.75                    
REMARK 500 PRO B  427     GLU B  428                 -146.68                    
REMARK 500 THR B  429     LEU B  430                 -148.94                    
REMARK 500 GLU C    8     LYS C    9                  147.35                    
REMARK 500 GLY C   11     GLU C   12                  147.84                    
REMARK 500 TYR C   15     GLY C   16                 -135.75                    
REMARK 500 ILE C   70     HIS C   71                 -139.79                    
REMARK 500 HIS C  161     GLU C  162                  141.31                    
REMARK 500 VAL C  164     THR C  165                  147.89                    
REMARK 500 THR C  165     LEU C  166                 -141.34                    
REMARK 500 ASP C  206     SER C  207                 -141.84                    
REMARK 500 GLY D  198     TYR D  199                 -135.16                    
REMARK 500 ASP D  283     ASP D  284                 -145.45                    
REMARK 500 PRO D  324     ALA D  325                  149.71                    
REMARK 500 ALA D  344     ASP D  345                 -148.18                    
REMARK 500 ASP D  345     PRO D  346                  141.23                    
REMARK 500 PRO D  346     TYR D  347                 -141.74                    
REMARK 500 GLY D  369     GLN D  370                  137.32                    
REMARK 500 LEU D  423     LEU D  424                  142.62                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    VAL C  64        -10.41                                           
REMARK 500    MET C 233        -19.97                                           
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 MTW A1297                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTW C1297                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AQ1   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 STAUROSPORINE                                                        
REMARK 900 RELATED ID: 1B38   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1B39   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 PHOSPHORYLATED ON THR 160            
REMARK 900 RELATED ID: 1BUH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CDK2 KINASE COMPLEX WITHCELL CYCLE-   
REMARK 900 REGULATORY PROTEIN CKSHS1                                            
REMARK 900 RELATED ID: 1CKP   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 PURVALANOL B                                                         
REMARK 900 RELATED ID: 1DI8   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN COMPLEX WITH 4- 
REMARK 900 [3- HYDROXYANILINO]-6,7-DIMETHOXYQUINAZOLINE                         
REMARK 900 RELATED ID: 1DM2   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 HYMENIALDISINE                                                       
REMARK 900 RELATED ID: 1E1V   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR NU2058  
REMARK 900 RELATED ID: 1E1X   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR NU6027  
REMARK 900 RELATED ID: 1E9H   RELATED DB: PDB                                   
REMARK 900 THR 160 PHOSPHORYLATED CDK2 - HUMAN CYCLIN A3 COMPLEX WITH THE       
REMARK 900 INHIBITOR INDIRUBIN-5- SULPHONATE BOUND                              
REMARK 900 RELATED ID: 1F5Q   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MURINE GAMMA HERPESVIRUS CYCLIN COMPLEXED TO    
REMARK 900 HUMAN CYCLIN DEPENDANT KINASE 2                                      
REMARK 900 RELATED ID: 1FIN   RELATED DB: PDB                                   
REMARK 900 CYCLIN A - CYCLIN-DEPENDENT KINASE 2 COMPLEX                         
REMARK 900 RELATED ID: 1FQ1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) INCOMPLEX   
REMARK 900 WITH PHOSPHO-CDK2                                                    
REMARK 900 RELATED ID: 1FVT   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) INCOMPLEX WITH AN  
REMARK 900 OXINDOLE INHIBITOR                                                   
REMARK 900 RELATED ID: 1FVV   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CDK2/CYCLIN A IN COMPLEX WITH AN OXINDOLEINHIBITOR  
REMARK 900 RELATED ID: 1G5S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2)IN        
REMARK 900 COMPLEX WITH THE INHIBITOR H717                                      
REMARK 900 RELATED ID: 1GIH   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4INHIBITOR     
REMARK 900 RELATED ID: 1GII   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4INHIBITOR     
REMARK 900 RELATED ID: 1GIJ   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4INHIBITOR     
REMARK 900 RELATED ID: 1GY3   RELATED DB: PDB                                   
REMARK 900 PCDK2/CYCLIN A IN COMPLEX WITH MGADP, NITRATE AND PEPTIDE SUBSTRATE  
REMARK 900 RELATED ID: 1GZ8   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 2-      
REMARK 900 AMINO-6-(3'-METHYL- 2'-OXO)BUTOXYPURINE                              
REMARK 900 RELATED ID: 1H00   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1H01   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 2, 4 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1H07   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1H08   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 2, 4 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1H0V   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE          
REMARK 900 INHIBITOR 2-AMINO-6-[(R )-PYRROLIDINO-5'-YL]METHOXYPURINE            
REMARK 900 RELATED ID: 1H0W   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE          
REMARK 900 INHIBITOR 2-AMINO-6-[ CYCLOHEX-3-ENYL]METHOXYPURINE                  
REMARK 900 RELATED ID: 1H1P   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH THE  
REMARK 900 INHIBITOR NU2058                                                     
REMARK 900 RELATED ID: 1H1Q   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH THE  
REMARK 900 INHIBITOR NU6094                                                     
REMARK 900 RELATED ID: 1H1R   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH THE  
REMARK 900 INHIBITOR NU6086                                                     
REMARK 900 RELATED ID: 1H1S   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH THE  
REMARK 900 INHIBITOR NU6102                                                     
REMARK 900 RELATED ID: 1H24   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH A 9 RESIDUE RECRUITMENT PEPTIDE FROM    
REMARK 900 E2F                                                                  
REMARK 900 RELATED ID: 1H25   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM  
REMARK 900 E2F                                                                  
REMARK 900 RELATED ID: 1H26   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM  
REMARK 900 P53                                                                  
REMARK 900 RELATED ID: 1H27   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM  
REMARK 900 P27                                                                  
REMARK 900 RELATED ID: 1H28   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM  
REMARK 900 P107                                                                 
REMARK 900 RELATED ID: 1HCK   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1HCL   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1JST   RELATED DB: PDB                                   
REMARK 900 PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A           
REMARK 900 RELATED ID: 1JSU   RELATED DB: PDB                                   
REMARK 900 P27(KIP1)/CYCLIN A/CDK2 COMPLEX                                      
REMARK 900 RELATED ID: 1JSV   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) INCOMPLEX WITH 4-  
REMARK 900 [(6-AMINO-4- PYRIMIDINYL)AMINO]BENZENESULFONAMIDE                    
REMARK 900 RELATED ID: 1JVP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 ( UNPHOSPHORYLATED) INCOMPLEX WITH   
REMARK 900 PKF049-365                                                           
REMARK 900 RELATED ID: 1KE5   RELATED DB: PDB                                   
REMARK 900 CDK2 COMPLEXED WITH N-METHYL-4-{[(2-OXO- 1,2-DIHYDRO-3H-INDOL-3-     
REMARK 900 YLIDENE)METHYL] AMINO}BENZENESULFONAMIDE                             
REMARK 900 RELATED ID: 1KE6   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH N-METHYL-{4-[2-(7-   
REMARK 900 OXO-6,7-DIHYDRO -8H-[1,3]THIAZOLO[5,4-E]INDOL-8- YLIDENE)HYDRAZINO]  
REMARK 900 PHENYL}METHANESULFONAMIDE                                            
REMARK 900 RELATED ID: 1KE7   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[(2,2-DIOXIDO-1,  
REMARK 900 3-DIHYDRO-2- BENZOTHIEN-5-YL)AMINO]METHYLENE}-5-(1,3- OXAZOL-5-YL)-  
REMARK 900 1,3-DIHYDRO-2H-INDOL-2- ONE                                          
REMARK 900 RELATED ID: 1KE8   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 4-{[(2-OXO-1,2-      
REMARK 900 DIHYDRO-3H-INDOL-3 -YLIDENE)METHYL]AMINO}-N-(1,3-THIAZOL-2- YL)      
REMARK 900 BENZENESULFONAMIDE                                                   
REMARK 900 RELATED ID: 1KE9   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[4-({             
REMARK 900 [AMINO(IMINO)METHYL] AMINOSULFONYL)ANILINO]METHYLENE}-2-OXO-2,3-     
REMARK 900 DIHYDRO-1H-INDOLE                                                    
REMARK 900 RELATED ID: 1OGU   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH A 2- 
REMARK 900 ARYLAMINO-4- CYCLOHEXYLMETHYL-5-NITROSO-6-AMINOPYRIMIDINE INHIBITOR  
REMARK 900 RELATED ID: 1OI9   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH A 6- 
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR                       
REMARK 900 RELATED ID: 1OIQ   RELATED DB: PDB                                   
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-DEPENDENT   
REMARK 900 KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION   
REMARK 900 RELATED ID: 1OIR   RELATED DB: PDB                                   
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-DEPENDENT   
REMARK 900 KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION   
REMARK 900 RELATED ID: 1OIT   RELATED DB: PDB                                   
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-DEPENDENT   
REMARK 900 KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION   
REMARK 900 RELATED ID: 1OIU   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH A 6- 
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR                       
REMARK 900 RELATED ID: 1OIY   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH A 6- 
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR                       
REMARK 900 RELATED ID: 1OKU   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ALA- ALA-ABU-ARG-ER-LEU-ILE-(P-  
REMARK 900 F-PHE)-NH2                                                           
REMARK 900 RELATED ID: 1OKV   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG- ARG-LEU-ILE-PHE-NH2         
REMARK 900 RELATED ID: 1OKW   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR AC-ARG- ARG-LEU-ASN-(M-CL-PHE)-NH2 
REMARK 900 RELATED ID: 1OL1   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-CIT- CIT-LEU-ILE-(P-F-PHE)-NH2   
REMARK 900 RELATED ID: 1OL2   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG- ARG-LEU-ASN-(P-F-PHE)-NH2   
REMARK 900 RELATED ID: 1P2A   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN DEPENDENT KINASE 2 (CKD2) WITH               
REMARK 900 ATRISUBSTITUTED NAPHTHOSTYRIL INHIBITOR                              
REMARK 900 RELATED ID: 1P5E   RELATED DB: PDB                                   
REMARK 900 THE STRUCURE OF PHOSPHO-CDK2/CYCLIN A IN COMPLEX WITH THEINHIBITOR   
REMARK 900 4,5,6,7- TETRABROMOBENZOTRIAZOLE (TBS)                               
REMARK 900 RELATED ID: 1PF8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLIN-DEPENDENT KINASE 2COMPLEXED WITH   
REMARK 900 A NUCLEOSIDE INHIBITOR                                               
REMARK 900 RELATED ID: 1PKD   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF UCN-01 IN COMPLEX WITH PHOSPHO-CDK2/CYCLIN  
REMARK 900 A                                                                    
REMARK 900 RELATED ID: 1PW2   RELATED DB: PDB                                   
REMARK 900 APO STRUCTURE OF HUMAN CYCLIN-DEPENDENT KINASE 2                     
REMARK 900 RELATED ID: 1PXI   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR 4-(2,5-  
REMARK 900 DICHLORO-THIOPHEN- 3-YL)-PYRIMIDIN-2-YLAMINE                         
REMARK 900 RELATED ID: 1PXJ   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR 4-(2,4-  
REMARK 900 DIMETHYL-THIAZOL- 5-YL)-PYRIMIDIN-2-YLAMINE                          
REMARK 900 RELATED ID: 1PXK   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR N-[4-(2, 
REMARK 900 4-DIMETHYL- THIAZOL-5-YL)PYRIMIDIN-2-YL]-N'- HYDROXYIMINOFORMAMIDE   
REMARK 900 RELATED ID: 1PXL   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR [4-(2,4- 
REMARK 900 DIMETHYL-THIAZOL- 5-YL)-PYRIMIDIN-2-YL]-(4-TRIFLUOROMETHYL- PHENYL)- 
REMARK 900 AMINE                                                                
REMARK 900 RELATED ID: 1PXM   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR 3-[4-(2, 
REMARK 900 4-DIMETHYL- THIAZOL-5-YL)-PYRIMIDIN-2-YLAMINO]-PHENOL                
REMARK 900 RELATED ID: 1PXN   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR 4-[4-(4- 
REMARK 900 METHYL-2- METHYLAMINO-THIAZOL-5-YL)-PYRIMIDIN-2- YLAMINO]-PHENOL     
REMARK 900 RELATED ID: 1PXO   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR [4-(2-   
REMARK 900 AMINO-4-METHYL- THIAZOL-5-YL)-PYRIMIDIN-2-YL]-(3-NITRO- PHENYL)-     
REMARK 900 AMINE                                                                
REMARK 900 RELATED ID: 1PXP   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR N-[4-(2, 
REMARK 900 4-DIMETHYL- THIAZOL-5-YL)-PYRIMIDIN-2-YL]-N',N'- DIMETHYL-BENZENE-1, 
REMARK 900 4-DIAMINE                                                            
REMARK 900 RELATED ID: 1PYE   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CDK2 WITH INHIBITOR                             
REMARK 900 RELATED ID: 1QMZ   RELATED DB: PDB                                   
REMARK 900 PHOSPHORYLATED CDK2-CYCLYIN A-SUBSTRATE PEPTIDE COMPLEX              
REMARK 900 RELATED ID: 1R78   RELATED DB: PDB                                   
REMARK 900 CDK2 COMPLEX WITH A 4-ALKYNYL OXINDOLE INHIBITOR                     
REMARK 900 RELATED ID: 1URC   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG- ARG-LEU-ASN-(P-F-PHE)-NH2   
REMARK 900 RELATED ID: 1URW   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH AN IMIDAZO[1,2-B] PYRIDAZINE                    
REMARK 900 RELATED ID: 1V1K   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1VYW   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2/CYCLIN A WITH PNU-292137                           
REMARK 900 RELATED ID: 1VYZ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2 COMPLEXED WITH PNU-181227                          
REMARK 900 RELATED ID: 1W0X   RELATED DB: PDB                                   
REMARK 900 CRYSTALS STRUCTURE OF HUMAN CDK2 IN COMPLEX WITH THE INHIBITOR       
REMARK 900 OLOMOUCINE.                                                          
REMARK 900 RELATED ID: 1W8C   RELATED DB: PDB                                   
REMARK 900 CO-CRYSTAL STRUCTURE OF 6-CYCLOHEXYLMETHOXY- 8-ISOPROPYL-9H-PURIN-2- 
REMARK 900 YLAMINE AND MONOMERIC CDK2                                           
REMARK 900 RELATED ID: 1W98   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURAL BASIS OF CDK2 ACTIVATION BY CYCLIN E                  
REMARK 900 RELATED ID: 1WCC   RELATED DB: PDB                                   
REMARK 900 SCREENING FOR FRAGMENT BINDING BY X-RAY CRYSTALLOGRAPHY              
REMARK 900 RELATED ID: 1Y8Y   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 COMPLEXED WITH A PYRAZOLO[1,5-A]     
REMARK 900 PYRIMIDINE INHIBITOR                                                 
REMARK 900 RELATED ID: 1Y91   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 COMPLEXED WITH A PYRAZOLO[1,5-A]     
REMARK 900 PYRIMIDINE INHIBITOR                                                 
REMARK 900 RELATED ID: 2B52   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH DPH-042562     
REMARK 900 RELATED ID: 2B53   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH DIN-234325     
REMARK 900 RELATED ID: 2B54   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 (CKD2) COMPLEXED WITH DIN-232305     
REMARK 900 RELATED ID: 2B55   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2) COMPLEXED WITHINDENOPYRAXOLE  
REMARK 900 DIN-101312                                                           
REMARK 900 RELATED ID: 2BHE   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE          
REMARK 900 INHIBITOR 5-BROMO- INDIRUBINE                                        
REMARK 900 RELATED ID: 2BHH   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE          
REMARK 900 INHIBITOR 4- HYDROXYPIPERINDINESULFONYL-INDIRUBINE                   
REMARK 900 RELATED ID: 2BKZ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2-CYCLIN A WITH PHA-404611                           
REMARK 900 RELATED ID: 2BPM   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2-CYCLIN A WITH PHA-630529                           
REMARK 900 RELATED ID: 2BTR   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2 COMPLEXED WITH PNU-198873                          
REMARK 900 RELATED ID: 2BTS   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2 COMPLEXED WITH PNU-230032                          
REMARK 900 RELATED ID: 2C4G   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2-CYCLIN A WITH PHA-533514                           
REMARK 900 RELATED ID: 2C5N   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
REMARK 900 RELATED ID: 2C5O   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
REMARK 900 RELATED ID: 2C5P   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
REMARK 900 RELATED ID: 2C5T   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
REMARK 900 RELATED ID: 2C5V   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
REMARK 900 RELATED ID: 2C5Y   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE DESIGN                  
DBREF  2C5X A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  2C5X C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  2C5X B  174   432  UNP    P20248   CCNA2_HUMAN    174    432             
DBREF  2C5X D  174   432  UNP    P20248   CCNA2_HUMAN    174    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  259  GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU          
SEQRES   2 B  259  ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR          
SEQRES   3 B  259  MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA          
SEQRES   4 B  259  ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR          
SEQRES   5 B  259  LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR          
SEQRES   6 B  259  ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY          
SEQRES   7 B  259  LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA          
SEQRES   8 B  259  SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU          
SEQRES   9 B  259  PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN          
SEQRES  10 B  259  VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR          
SEQRES  11 B  259  PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR          
SEQRES  12 B  259  GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL          
SEQRES  13 B  259  GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE          
SEQRES  14 B  259  ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE          
SEQRES  15 B  259  ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR          
SEQRES  16 B  259  GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY          
SEQRES  17 B  259  TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU          
SEQRES  18 B  259  HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN          
SEQRES  19 B  259  SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY          
SEQRES  20 B  259  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  259  GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU          
SEQRES   2 D  259  ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR          
SEQRES   3 D  259  MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA          
SEQRES   4 D  259  ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR          
SEQRES   5 D  259  LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR          
SEQRES   6 D  259  ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY          
SEQRES   7 D  259  LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA          
SEQRES   8 D  259  SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU          
SEQRES   9 D  259  PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN          
SEQRES  10 D  259  VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR          
SEQRES  11 D  259  PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR          
SEQRES  12 D  259  GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL          
SEQRES  13 D  259  GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE          
SEQRES  14 D  259  ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE          
SEQRES  15 D  259  ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR          
SEQRES  16 D  259  GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY          
SEQRES  17 D  259  TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU          
SEQRES  18 D  259  HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN          
SEQRES  19 D  259  SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY          
SEQRES  20 D  259  VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU              
HET    MTW  A1297      28                                                       
HET    MTW  C1297      28                                                       
HETNAM     MTW HYDROXY(OXO)(3-{[(2Z)-4-[3-(1H-1,2,4-TRIAZOL-1-                  
HETNAM   2 MTW  YLMETHYL)PHENYL]PYRIMIDIN-2(5H)-YLIDENE]AMINO}PHENYL)           
HETNAM   3 MTW  AMMONIUM                                                        
FORMUL   5  MTW    2(C19 H15 N7 O2)                                             
FORMUL   7  HOH   *88(H2 O)                                                     
HELIX    1   1 PRO A   45  LYS A   56  1                                  12    
HELIX    2   2 LEU A   87  ALA A   93  1                                   7    
HELIX    3   3 PRO A  100  HIS A  121  1                                  22    
HELIX    4   4 LYS A  129  GLN A  131  5                                   3    
HELIX    5   5 ALA A  170  LEU A  175  1                                   6    
HELIX    6   6 THR A  182  ARG A  199  1                                  18    
HELIX    7   7 SER A  207  GLY A  220  1                                  14    
HELIX    8   8 GLY A  229  MET A  233  5                                   5    
HELIX    9   9 ASP A  247  VAL A  252  1                                   6    
HELIX   10  10 ASP A  256  LEU A  267  1                                  12    
HELIX   11  11 SER A  276  ALA A  282  1                                   7    
HELIX   12  12 HIS A  283  GLN A  287  5                                   5    
HELIX   13  13 TYR B  178  CYS B  193  1                                  16    
HELIX   14  14 THR B  207  LYS B  226  1                                  20    
HELIX   15  15 GLN B  228  SER B  244  1                                  17    
HELIX   16  16 LEU B  249  GLU B  269  1                                  21    
HELIX   17  17 GLU B  274  ILE B  281  1                                   8    
HELIX   18  18 THR B  287  LEU B  302  1                                  16    
HELIX   19  19 THR B  310  LEU B  320  1                                  11    
HELIX   20  20 ASN B  326  ILE B  342  1                                  17    
HELIX   21  21 ASP B  343  LEU B  348  1                                   6    
HELIX   22  22 LEU B  351  GLY B  369  1                                  19    
HELIX   23  23 PRO B  373  GLY B  381  1                                   9    
HELIX   24  24 LEU B  387  ALA B  401  1                                  15    
HELIX   25  25 PRO B  402  HIS B  404  5                                   3    
HELIX   26  26 GLN B  407  LYS B  414  1                                   8    
HELIX   27  27 ASN B  415  HIS B  419  5                                   5    
HELIX   28  28 PRO C   45  LYS C   56  1                                  12    
HELIX   29  29 LEU C   87  ALA C   93  1                                   7    
HELIX   30  30 PRO C  100  HIS C  121  1                                  22    
HELIX   31  31 LYS C  129  GLN C  131  5                                   3    
HELIX   32  32 ALA C  170  LEU C  175  1                                   6    
HELIX   33  33 SER C  181  ARG C  199  1                                  19    
HELIX   34  34 SER C  207  GLY C  220  1                                  14    
HELIX   35  35 GLY C  229  MET C  233  5                                   5    
HELIX   36  36 ASP C  247  VAL C  251  5                                   5    
HELIX   37  37 ASP C  256  LEU C  267  1                                  12    
HELIX   38  38 SER C  276  ALA C  282  1                                   7    
HELIX   39  39 HIS C  283  VAL C  289  5                                   7    
HELIX   40  40 TYR D  178  CYS D  193  1                                  16    
HELIX   41  41 GLY D  198  GLN D  203  5                                   6    
HELIX   42  42 THR D  207  TYR D  225  1                                  19    
HELIX   43  43 GLN D  228  LEU D  243  1                                  16    
HELIX   44  44 LEU D  249  GLU D  269  1                                  21    
HELIX   45  45 GLU D  274  ILE D  281  1                                   8    
HELIX   46  46 THR D  287  LEU D  302  1                                  16    
HELIX   47  47 THR D  310  LEU D  320  1                                  11    
HELIX   48  48 ASN D  326  SER D  340  1                                  15    
HELIX   49  49 ASP D  343  LEU D  348  1                                   6    
HELIX   50  50 LEU D  351  THR D  368  1                                  18    
HELIX   51  51 PRO D  373  GLY D  381  1                                   9    
HELIX   52  52 THR D  383  ALA D  401  1                                  19    
HELIX   53  53 PRO D  402  HIS D  404  5                                   3    
HELIX   54  54 GLN D  407  TYR D  413  1                                   7    
HELIX   55  55 ASN D  415  HIS D  419  5                                   5    
SHEET    1  AA 5 PHE A   4  GLU A  12  0                                        
SHEET    2  AA 5 VAL A  17  ASN A  23 -1  O  VAL A  18   N  ILE A  10           
SHEET    3  AA 5 VAL A  29  ARG A  36 -1  O  VAL A  30   N  ALA A  21           
SHEET    4  AA 5 LYS A  75  PHE A  80 -1  O  LEU A  76   N  ILE A  35           
SHEET    5  AA 5 LEU A  66  HIS A  71 -1  N  LEU A  67   O  VAL A  79           
SHEET    1  AB 3 GLN A  85  ASP A  86  0                                        
SHEET    2  AB 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3  AB 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1  AC 2 VAL A 123  LEU A 124  0                                        
SHEET    2  AC 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1  CA 5 PHE C   4  LYS C   9  0                                        
SHEET    2  CA 5 VAL C  18  ASN C  23 -1  O  LYS C  20   N  VAL C   7           
SHEET    3  CA 5 VAL C  29  ARG C  36 -1  O  VAL C  30   N  ALA C  21           
SHEET    4  CA 5 LYS C  75  GLU C  81 -1  O  LEU C  76   N  ILE C  35           
SHEET    5  CA 5 LEU C  66  HIS C  71 -1  N  LEU C  67   O  VAL C  79           
SHEET    1  CB 3 GLN C  85  ASP C  86  0                                        
SHEET    2  CB 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3  CB 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1  CC 2 VAL C 123  LEU C 124  0                                        
SHEET    2  CC 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
CISPEP   1 GLN B  323    PRO B  324          0       -12.78                     
CISPEP   2 GLN D  323    PRO D  324          0        -9.82                     
SITE     1 AC1 14 ILE A  10  GLY A  13  VAL A  18  ALA A  31                    
SITE     2 AC1 14 LYS A  33  PHE A  80  GLU A  81  PHE A  82                    
SITE     3 AC1 14 LEU A  83  HIS A  84  GLN A 131  ASN A 132                    
SITE     4 AC1 14 LEU A 134  ASP A 145                                          
SITE     1 AC2 12 ILE C  10  ALA C  31  LYS C  33  PHE C  80                    
SITE     2 AC2 12 GLU C  81  LEU C  83  HIS C  84  GLN C  85                    
SITE     3 AC2 12 ASP C  86  GLN C 131  LEU C 134  ASP C 145                    
CRYST1   74.334  112.352  154.911  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      0.013453  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008901  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006455        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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