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Database: PDB
Entry: 2A0C
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Original site: 2A0C 
HEADER    TRANSFERASE                             16-JUN-05   2A0C              
TITLE     HUMAN CDK2 IN COMPLEX WITH OLOMOUCINE II, A NOVEL 2,6,9-              
TITLE    2 TRISUBSTITUTED PURINE CYCLIN-DEPENDENT KINASE INHIBITOR              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: X;                                                            
COMPND   4 SYNONYM: CYCLIN DEPENDANT KINASE 2, CDK2, P33 PROTEIN                
COMPND   5 KINASE;                                                              
COMPND   6 EC: 2.7.1.37;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK2;                                                          
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    PROTEIN KINASE, CELL CYCLE, PHOSPHORYLATION, CELL DIVISION,           
KEYWDS   2 MITOSIS, INHIBITION, TRANSFERASE, SERINE/THREONINE-PROTEIN           
KEYWDS   3 KINASE, ATP-BINDING, 3D-STRUCTURE                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.KRYSTOF,I.W.MCNAE,M.D.WALKINSHAW,P.M.FISCHER,P.MULLER,              
AUTHOR   2 B.VOJTESEK,M.ORSAG,L.HAVLICEK,M.STRNAD                               
REVDAT   2   24-FEB-09 2A0C    1       VERSN                                    
REVDAT   1   24-JAN-06 2A0C    0                                                
JRNL        AUTH   V.KRYSTOF,I.W.MCNAE,M.D.WALKINSHAW,P.M.FISCHER,              
JRNL        AUTH 2 P.MULLER,B.VOJTESEK,M.ORSAG,L.HAVLICEK,M.STRNAD              
JRNL        TITL   ANTIPROLIFERATIVE ACTIVITY OF OLOMOUCINE II, A               
JRNL        TITL 2 NOVEL 2,6,9-TRISUBSTITUTED PURINE CYCLIN-DEPENDENT           
JRNL        TITL 3 KINASE INHIBITOR                                             
JRNL        REF    CELL.MOL.LIFE SCI.            V.  62  1763 2005              
JRNL        REFN                   ISSN 1420-682X                               
JRNL        PMID   16003486                                                     
JRNL        DOI    10.1007/S00018-005-5185-1                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 19008                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1027                            
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) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1400                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 72                           
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2370                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 27                                      
REMARK   3   SOLVENT ATOMS            : 134                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.22000                                             
REMARK   3    B22 (A**2) : 1.25000                                              
REMARK   3    B33 (A**2) : -1.03000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.204         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.178         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.112         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.862         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2460 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2294 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3337 ; 1.703 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5338 ; 1.361 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   292 ; 6.234 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   373 ; 0.125 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2657 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   506 ; 0.005 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   542 ; 0.225 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2669 ; 0.240 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1453 ; 0.093 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   114 ; 0.179 ; 0.200       
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):    27 ; 0.194 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    71 ; 0.266 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    16 ; 0.156 ; 0.200       
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):  1470 ; 1.266 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2393 ; 2.320 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   990 ; 2.841 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   944 ; 4.646 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2A0C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-SEP-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB033332.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-OCT-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93400                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20070                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.640                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.28100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, NA-HEPES,, PH 7.8, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.62100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.93450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.47250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       35.93450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.62100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.47250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU X    37                                                      
REMARK 465     ASP X    38                                                      
REMARK 465     THR X    39                                                      
REMARK 465     GLU X    40                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU X 298    O                                                   
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    ASP X 145   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP X 210   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL X  44      110.19     53.97                                   
REMARK 500    ARG X 126      -22.41     83.44                                   
REMARK 500    ASP X 127       49.66   -141.46                                   
REMARK 500    THR X 158     -152.67    -94.74                                   
REMARK 500    TYR X 179       56.67   -108.43                                   
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 CK9 X 500                 
DBREF  2A0C X    1   298  UNP    P24941   CDK2_HUMAN       1    298             
SEQRES   1 X  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 X  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 X  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 X  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 X  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 X  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 X  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 X  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 X  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 X  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 X  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 X  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 X  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 X  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 X  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 X  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 X  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 X  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 X  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 X  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 X  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 X  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 X  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
HET    CK9  X 500      27                                                       
HETNAM     CK9 2-{[(2-{[(1R)-1-(HYDROXYMETHYL)PROPYL]AMINO}-9-                  
HETNAM   2 CK9  ISOPROPYL-9H-PURIN-6-YL)AMINO]METHYL}PHENOL                     
HETSYN     CK9 OLOMOUCINE II                                                    
FORMUL   2  CK9    C19 H26 N6 O2                                                
FORMUL   3  HOH   *134(H2 O)                                                    
HELIX    1   1 PRO X   45  LEU X   54  1                                  10    
HELIX    2   2 LEU X   55  LEU X   58  5                                   4    
HELIX    3   3 LEU X   87  SER X   94  1                                   8    
HELIX    4   4 PRO X  100  HIS X  121  1                                  22    
HELIX    5   5 LYS X  129  GLN X  131  5                                   3    
HELIX    6   6 GLY X  147  PHE X  152  1                                   6    
HELIX    7   7 ALA X  170  LEU X  175  1                                   6    
HELIX    8   8 THR X  182  ARG X  199  1                                  18    
HELIX    9   9 SER X  207  GLY X  220  1                                  14    
HELIX   10  10 GLY X  229  MET X  233  5                                   5    
HELIX   11  11 ASP X  256  LEU X  267  1                                  12    
HELIX   12  12 SER X  276  ALA X  282  1                                   7    
HELIX   13  13 HIS X  283  GLN X  287  5                                   5    
SHEET    1   A 5 PHE X   4  GLU X  12  0                                        
SHEET    2   A 5 GLY X  16  ASN X  23 -1  O  LYS X  20   N  VAL X   7           
SHEET    3   A 5 VAL X  29  ILE X  35 -1  O  LEU X  32   N  TYR X  19           
SHEET    4   A 5 LYS X  75  GLU X  81 -1  O  LEU X  76   N  ILE X  35           
SHEET    5   A 5 LEU X  66  THR X  72 -1  N  ILE X  70   O  TYR X  77           
SHEET    1   B 3 GLN X  85  ASP X  86  0                                        
SHEET    2   B 3 LEU X 133  ILE X 135 -1  O  ILE X 135   N  GLN X  85           
SHEET    3   B 3 ILE X 141  LEU X 143 -1  O  LYS X 142   N  LEU X 134           
CISPEP   1 PRO X  253    PRO X  254          0         6.24                     
SITE     1 AC1 15 ILE X  10  GLY X  11  GLU X  12  VAL X  18                    
SITE     2 AC1 15 ALA X  31  PHE X  80  GLU X  81  LEU X  83                    
SITE     3 AC1 15 HIS X  84  LYS X  89  GLN X 131  ASN X 132                    
SITE     4 AC1 15 LEU X 134  ALA X 144  HOH X 517                               
CRYST1   53.242   70.945   71.869  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018782  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014095  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013914        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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