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Database: PDB
Entry: 3EZR
LinkDB: 3EZR
Original site: 3EZR 
HEADER    TRANSFERASE/TRANSFERASE INHIBITO        23-OCT-08   3EZR              
TITLE     CDK-2 WITH INDAZOLE INHIBITOR 17 BOUND AT ITS ACTIVE SITE             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: 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;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    KINASE, PKC, PROTEIN KINASE, INHIBITOR, ATP-BINDING, CELL CYCLE, CELL 
KEYWDS   2 DIVISION, MITOSIS, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, POLYMORPHISM, 
KEYWDS   3 SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE-TRANSFERASE INHIBITOR   
KEYWDS   4 COMPLEX, TRANSFERASE-TRANSFERASE INHIBITO COMPLEX                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.KIEFER,J.E.DAY,N.L.CASPERS,K.J.MATHIS,K.K.KRETZMER,R.A.WEINBERG,  
AUTHOR   2 B.A.REITZ,R.A.STEGEMAN,J.I.TRUJILLO,W.HUANG,A.THORARENSEN,L.XING,    
AUTHOR   3 A.WRIGHTSTONE,L.CHRISTINE,R.COMPTON,X.LI                             
REVDAT   3   24-JAN-18 3EZR    1       HEADER KEYWDS                            
REVDAT   2   25-OCT-17 3EZR    1       REMARK                                   
REVDAT   1   03-FEB-09 3EZR    0                                                
JRNL        AUTH   J.I.TRUJILLO,J.R.KIEFER,W.HUANG,A.THORARENSEN,L.XING,        
JRNL        AUTH 2 N.L.CASPERS,J.E.DAY,K.J.MATHIS,K.K.KRETZMER,B.A.REITZ,       
JRNL        AUTH 3 R.A.WEINBERG,R.A.STEGEMAN,A.WRIGHTSTONE,L.CHRISTINE,         
JRNL        AUTH 4 R.COMPTON,X.LI                                               
JRNL        TITL   2-(6-PHENYL-1H-INDAZOL-3-YL)-1H-BENZO[D]IMIDAZOLES: DESIGN   
JRNL        TITL 2 AND SYNTHESIS OF A POTENT AND ISOFORM SELECTIVE PKC-ZETA     
JRNL        TITL 3 INHIBITOR                                                    
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  19   908 2009              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   19097791                                                     
JRNL        DOI    10.1016/J.BMCL.2008.11.105                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 22591                          
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) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1159                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1544                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.33                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2240                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 90                           
REMARK   3   BIN FREE R VALUE                    : 0.2280                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2201                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 189                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.30000                                             
REMARK   3    B22 (A**2) : 2.44000                                              
REMARK   3    B33 (A**2) : -1.14000                                             
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): 0.184         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.160         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.114         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.776         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2336 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1568 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3176 ; 1.298 ; 2.015       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3830 ; 0.821 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.618 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    96 ;41.722 ;23.438       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   399 ;13.867 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;15.182 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   345 ; 0.066 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2600 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   453 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   535 ; 0.218 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1654 ; 0.186 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1175 ; 0.196 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1100 ; 0.083 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   133 ; 0.133 ; 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):    37 ; 0.300 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    64 ; 0.279 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    33 ; 0.200 ; 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):  1426 ; 0.737 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   539 ; 0.113 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2224 ; 1.268 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1070 ; 1.407 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   952 ; 2.196 ; 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 : 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   : 1.20                                          
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 3EZR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000049965.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC BLUE MIRRORS                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22591                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 18.790                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 4K, 50MM HEPES PH 7.5, 50MM      
REMARK 280  AMMONIUM ACETATE, 10 MM DTT, VAPOR DIFFUSION, TEMPERATURE 291K      
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       26.88150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.19600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.04050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.19600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.88150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.04050            
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     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
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 465     GLY A   147                                                      
REMARK 465     LEU A   148                                                      
REMARK 465     ALA A   149                                                      
REMARK 465     ARG A   150                                                      
REMARK 465     ALA A   151                                                      
REMARK 465     PHE A   152                                                      
REMARK 465     GLY A   153                                                      
REMARK 465     VAL A   154                                                      
REMARK 465     PRO A   155                                                      
REMARK 465     VAL A   156                                                      
REMARK 465     ARG A   157                                                      
REMARK 465     THR A   158                                                      
REMARK 465     TYR A   159                                                      
REMARK 465     THR A   160                                                      
REMARK 465     HIS A   161                                                      
REMARK 465     GLU A   162                                                      
REMARK 465     VAL A   163                                                      
REMARK 465     VAL A   164                                                      
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    CG   CD   NE   CZ   NH1  NH2                        
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   O    PRO A   253     N32  EZR A   301     2565     2.11            
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    PRO A 254   C   -  N   -  CA  ANGL. DEV. = -17.8 DEGREES          
REMARK 500    PRO A 254   C   -  N   -  CD  ANGL. DEV. =  18.5 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    ARG A 126      -23.52     86.14                                   
REMARK 500    ASP A 127       49.81   -144.93                                   
REMARK 500    PRO A 253      -96.32    -23.51                                   
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 EZR A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EZR A 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3EZV   RELATED DB: PDB                                   
DBREF  3EZR A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
SEQADV 3EZR GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 3EZR SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQRES   1 A  300  GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY          
SEQRES   2 A  300  GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS          
SEQRES   3 A  300  LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU          
SEQRES   4 A  300  ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG          
SEQRES   5 A  300  GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE          
SEQRES   6 A  300  VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU          
SEQRES   7 A  300  TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS          
SEQRES   8 A  300  PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO          
SEQRES   9 A  300  LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU          
SEQRES  10 A  300  ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU          
SEQRES  11 A  300  LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE          
SEQRES  12 A  300  LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL          
SEQRES  13 A  300  PRO VAL ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP          
SEQRES  14 A  300  TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR          
SEQRES  15 A  300  SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE          
SEQRES  16 A  300  ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP          
SEQRES  17 A  300  SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU          
SEQRES  18 A  300  GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER          
SEQRES  19 A  300  MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG          
SEQRES  20 A  300  GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP          
SEQRES  21 A  300  GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO          
SEQRES  22 A  300  ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO          
SEQRES  23 A  300  PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG          
SEQRES  24 A  300  LEU                                                          
HET    EZR  A 300      34                                                       
HET    EZR  A 301      34                                                       
HETNAM     EZR 3-METHOXY-4-{3-[4-(4-METHYLPIPERAZIN-1-YL)-1H-                   
HETNAM   2 EZR  BENZIMIDAZOL-2-YL]-1H-INDAZOL-6-YL}ANILINE                      
FORMUL   2  EZR    2(C26 H27 N7 O)                                              
FORMUL   4  HOH   *189(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 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    
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 LYS A  75  GLU A  81 -1  O  PHE A  80   N  ALA A  31           
SHEET    5   A 5 LEU A  66  THR A  72 -1  N  ILE A  70   O  TYR A  77           
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           
SITE     1 AC1 17 ILE A  10  ALA A  31  LYS A  33  VAL A  64                    
SITE     2 AC1 17 PHE A  80  GLU A  81  PHE A  82  LEU A  83                    
SITE     3 AC1 17 HIS A  84  ASP A  86  LYS A  89  GLN A 131                    
SITE     4 AC1 17 LEU A 134  ALA A 144  ASP A 145  PHE A 146                    
SITE     5 AC1 17 HOH A8079                                                     
SITE     1 AC2 15 LEU A  25  THR A  26  GLU A  28  LYS A 178                    
SITE     2 AC2 15 PHE A 213  ARG A 217  TRP A 243  SER A 249                    
SITE     3 AC2 15 PRO A 253  PRO A 254  LEU A 255  ARG A 260                    
SITE     4 AC2 15 HOH A8135  HOH A8181  HOH A8187                               
CRYST1   53.763   72.081   72.392  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      0.018600  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013873  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013814        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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