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Database: PDB
Entry: 4FKL
LinkDB: 4FKL
Original site: 4FKL 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       13-JUN-12   4FKL              
TITLE     CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH THIAZOLYLPYRIMIDINE     
TITLE    2 INHIBITOR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CELL DIVISION PROTEIN KINASE 2, P33 PROTEIN KINASE;         
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK2, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HIGH-FIVE;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFB1                                      
KEYWDS    ALPHA AND BETA PROTEIN (A+B), TRANSFERASE-TRANSFERASE INHIBITOR       
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.N.KANG,J.A.STUCKEY                                                  
REVDAT   2   22-MAY-13 4FKL    1       SOURCE                                   
REVDAT   1   08-MAY-13 4FKL    0                                                
JRNL        AUTH   Y.N.KANG,J.A.STUCKEY                                         
JRNL        TITL   CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH                
JRNL        TITL 2 THIAZOLYLPYRIMIDINE INHIBITOR                                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.26 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 1.26                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 75492                          
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) : 0.153                           
REMARK   3   R VALUE            (WORKING SET) : 0.151                           
REMARK   3   FREE R VALUE                     : 0.183                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3805                            
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) : 1.26                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.29                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5219                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1670                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 301                          
REMARK   3   BIN FREE R VALUE                    : 0.2020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2339                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 14                                      
REMARK   3   SOLVENT ATOMS            : 247                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.04000                                             
REMARK   3    B22 (A**2) : 0.04000                                              
REMARK   3    B33 (A**2) : -0.00000                                             
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): 0.047         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.022         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.072         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2685 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3695 ; 1.736 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   358 ; 5.259 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   123 ;37.468 ;23.171       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   504 ;13.275 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;19.069 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   412 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2062 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1580 ; 2.045 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2613 ; 3.162 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1105 ; 3.814 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1045 ; 5.423 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2685 ; 1.900 ; 3.000       
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 : 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 RIDING   
REMARK   4                                                                      
REMARK   4 4FKL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073015.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-OCT-09                          
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               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97856                            
REMARK 200  MONOCHROMATOR                  : DIAMOND [111]                      
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 75574                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.260                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 13.900                             
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.26                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.70                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.25900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2R3I                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-20% PEG3350, 0.2M AMMONIUM ACETATE,   
REMARK 280  0.1M HEPES, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K,     
REMARK 280  PH 7.8                                                              
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       26.66650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.24300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.76600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.24300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.66650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.76600            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 A    37                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     THR A    41                                                      
REMARK 465     GLU A    42                                                      
REMARK 465     GLY A    43                                                      
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     ARG A  36    CA   C    O    CB   CG   CD   NE                    
REMARK 470     ARG A  36    CZ   NH1  NH2                                       
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    ARG A 126       -8.39     78.56                                   
REMARK 500    TYR A 179       61.99   -119.92                                   
REMARK 500    PRO A 254       31.41    -97.77                                   
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 CK2 A 300                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4EK3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF APO CDK2                                        
REMARK 900 RELATED ID: 4EK4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE          
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 4EK5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE          
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 4EK6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE          
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 4EK8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH                        
REMARK 900 THIAZOLYLPYRIMIDINE INHIBITOR                                        
REMARK 900 RELATED ID: 4FKG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE          
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 4FKI   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE          
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 4FKJ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE          
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 4FKO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FKP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FKQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FKR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FKS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FKT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FKU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FKV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FKW   RELATED DB: PDB                                   
DBREF  4FKL A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
SEQADV 4FKL ACE A    0  UNP  P24941              ACETYLATION                    
SEQRES   1 A  299  ACE MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU          
SEQRES   2 A  299  GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU          
SEQRES   3 A  299  THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP          
SEQRES   4 A  299  THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU          
SEQRES   5 A  299  ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL          
SEQRES   6 A  299  LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR          
SEQRES   7 A  299  LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE          
SEQRES   8 A  299  MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU          
SEQRES   9 A  299  ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA          
SEQRES  10 A  299  PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS          
SEQRES  11 A  299  PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS          
SEQRES  12 A  299  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO          
SEQRES  13 A  299  VAL ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR          
SEQRES  14 A  299  ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER          
SEQRES  15 A  299  THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA          
SEQRES  16 A  299  GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER          
SEQRES  17 A  299  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY          
SEQRES  18 A  299  THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET          
SEQRES  19 A  299  PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN          
SEQRES  20 A  299  ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY          
SEQRES  21 A  299  ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN          
SEQRES  22 A  299  LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE          
SEQRES  23 A  299  PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU          
HET    ACE  A   0       3                                                       
HET    CK2  A 300      14                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     CK2 4-(2,4-DIMETHYL-1,3-THIAZOL-5-YL)PYRIMIDIN-2-AMINE               
HETSYN     CK2 4-(2,4-DIMETHYL-THIAZOL-5-YL)-PYRIMIDIN-2-YLAMINE                
FORMUL   1  ACE    C2 H4 O                                                      
FORMUL   2  CK2    C9 H10 N4 S                                                  
FORMUL   3  HOH   *247(H2 O)                                                    
HELIX    1   1 PRO A   45  LYS A   56  1                                  12    
HELIX    2   2 LEU A   87  SER A   94  1                                   8    
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 GLY A  147  GLY A  153  1                                   7    
HELIX    6   6 ALA A  170  LEU A  175  1                                   6    
HELIX    7   7 THR A  182  ARG A  199  1                                  18    
HELIX    8   8 SER A  207  GLY A  220  1                                  14    
HELIX    9   9 GLY A  229  MET A  233  5                                   5    
HELIX   10  10 ASP A  247  VAL A  252  1                                   6    
HELIX   11  11 ASP A  256  LEU A  267  1                                  12    
HELIX   12  12 SER A  276  ALA A  282  1                                   7    
HELIX   13  13 HIS A  283  GLN A  287  5                                   5    
SHEET    1   A 5 PHE A   4  GLU A  12  0                                        
SHEET    2   A 5 VAL A  17  ASN A  23 -1  O  LYS A  20   N  VAL A   7           
SHEET    3   A 5 VAL A  29  ILE A  35 -1  O  LEU A  32   N  TYR A  19           
SHEET    4   A 5 LEU A  76  GLU A  81 -1  O  PHE A  80   N  ALA A  31           
SHEET    5   A 5 LEU A  66  HIS A  71 -1  N  ASP A  68   O  VAL A  79           
SHEET    1   B 3 GLN A  85  ASP A  86  0                                        
SHEET    2   B 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3   B 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
LINK         C   ACE A   0                 N   MET A   1     1555   1555  1.34  
CISPEP   1 PRO A  253    PRO A  254          0         2.64                     
SITE     1 AC1  9 ILE A  10  GLU A  12  ALA A  31  LYS A  33                    
SITE     2 AC1  9 GLU A  81  LEU A  83  GLN A 131  LEU A 134                    
SITE     3 AC1  9 HOH A 557                                                     
CRYST1   53.333   71.532   72.486  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      0.018750  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013980  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013796        0.00000                         
HETATM    1  C   ACE A   0     -14.250   2.325  39.685  1.00 25.52           C  
ANISOU    1  C   ACE A   0     2512   3545   3638   -125    242   -224       C  
HETATM    2  O   ACE A   0     -13.301   1.770  40.267  1.00 24.73           O  
ANISOU    2  O   ACE A   0     2482   3410   3501    -77    323   -366       O  
HETATM    3  CH3 ACE A   0     -15.522   1.607  39.333  1.00 26.10           C  
ANISOU    3  CH3 ACE A   0     2719   3548   3649    -91    101   -388       C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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