GenomeNet

Database: PDB
Entry: 6GVA
LinkDB: 6GVA
Original site: 6GVA 
HEADER    CELL CYCLE                              20-JUN-18   6GVA              
TITLE     CDK2/CYCLIN A2 IN COMPLEX WITH PYRAZOLO[4,3-D]PYRIMIDINE INHIBITOR    
TITLE    2 LGR4455                                                              
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;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYCLIN-A2;                                                 
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: CYCLIN-A,CYCLIN A;                                          
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK2, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: CCNA2, CCN1, CCNA;                                             
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CYCLIN-DEPENDENT KINASE, PYRAZOLO[4, 3-D]PYRIMIDINE, CELL CYCLE       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.SKERLOVA,P.REZACOVA                                                 
REVDAT   2   22-MAY-19 6GVA    1       JRNL                                     
REVDAT   1   01-MAY-19 6GVA    0                                                
JRNL        AUTH   R.JORDA,L.HAVLICEK,A.STURC,D.TUSKOVA,L.DAUMOVA,M.ALAM,       
JRNL        AUTH 2 J.SKERLOVA,M.NEKARDOVA,M.PERINA,T.POSPISIL,J.SIROKA,         
JRNL        AUTH 3 L.URBANEK,P.PACHL,P.REZACOVA,M.STRNAD,P.KLENER,V.KRYSTOF     
JRNL        TITL   3,5,7-SUBSTITUTED PYRAZOLO[4,3- D]PYRIMIDINE INHIBITORS OF   
JRNL        TITL 2 CYCLIN-DEPENDENT KINASES AND THEIR EVALUATION IN LYMPHOMA    
JRNL        TITL 3 MODELS.                                                      
JRNL        REF    J.MED.CHEM.                   V.  62  4606 2019              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   30943029                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.9B00189                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 33033                          
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) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1739                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.20                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2066                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.33                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3700                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 109                          
REMARK   3   BIN FREE R VALUE                    : 0.3640                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4402                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 73                                      
REMARK   3   SOLVENT ATOMS            : 160                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.41                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.03000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 0.10000                                              
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): 0.241         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.198         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.185         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.018         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
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):  4583 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4363 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6202 ; 1.619 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10126 ; 1.020 ; 2.993       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   545 ; 6.104 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   195 ;41.098 ;23.949       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   797 ;15.444 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;16.021 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   697 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4914 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   906 ; 0.002 ; 0.020       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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 : 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 U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 6GVA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-JUN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200010282.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-JAN-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : SAGITALLY BENDED SI111-CRYSTAL     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JUN 1, 2017            
REMARK 200                                   BUILT=20170720                     
REMARK 200  DATA SCALING SOFTWARE          : XDS VERSION JUN 1, 2017            
REMARK 200                                   BUILT=20170720                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34773                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 6.247                              
REMARK 200  R MERGE                    (I) : 0.19500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.9600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.45600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.860                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP VERS 11.4.06; 24.05.2016                       
REMARK 200 STARTING MODEL: 5LMK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THIN DIAMOND-SHAPED PLATES                                   
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% W/V PEG 20000, 20% V/V PEG MME       
REMARK 280  550, 0.03 M SODIUM FLUORIDE, 0.03 M SODIUM BROMIDE, 0.03 M          
REMARK 280  SODIUM IODIDE, AND 0.1 M BICINE/TRIZMA BASE, PH 8.5, VAPOR          
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       79.84500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       79.84500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       35.50750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.32100            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       35.50750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.32100            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       79.84500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       35.50750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       56.32100            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       79.84500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       35.50750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       56.32100            
REMARK 290   SMTRY3   8  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A     0                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     LYS A   291                                                      
REMARK 465     PRO A   292                                                      
REMARK 465     VAL A   293                                                      
REMARK 465     PRO A   294                                                      
REMARK 465     HIS A   295                                                      
REMARK 465     LEU A   296                                                      
REMARK 465     ARG A   297                                                      
REMARK 465     LEU A   298                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  12      -72.90   -118.32                                   
REMARK 500    LEU A  37       40.03   -102.31                                   
REMARK 500    ASP A 127       42.52   -154.68                                   
REMARK 500    ASP A 145       78.81     61.57                                   
REMARK 500    VAL A 164      127.56     78.29                                   
REMARK 500    SER A 181     -151.14   -156.25                                   
REMARK 500    PHE B 304       17.73     59.87                                   
REMARK 500    TRP B 372      111.16    -34.62                                   
REMARK 500    ASN B 415      151.56    -48.54                                   
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 FCQ A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SGM B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 504                 
DBREF  6GVA A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  6GVA B  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
SEQADV 6GVA SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQRES   1 A  299  SER 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 TPO 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          
SEQRES   1 B  258  VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 B  258  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 B  258  LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 B  258  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 B  258  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 B  258  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 B  258  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 B  258  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 B  258  VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL          
SEQRES  10 B  258  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE          
SEQRES  11 B  258  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 B  258  TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 B  258  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 B  258  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA          
SEQRES  15 B  258  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 B  258  GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR          
SEQRES  17 B  258  THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS          
SEQRES  18 B  258  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 B  258  ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL          
SEQRES  20 B  258  SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU                  
MODRES 6GVA TPO A  160  THR  MODIFIED RESIDUE                                   
HET    TPO  A 160      11                                                       
HET    FCQ  A 301      30                                                       
HET    EDO  A 302       4                                                       
HET    EDO  A 303       4                                                       
HET     CL  A 304       1                                                       
HET     BR  A 305       1                                                       
HET    PG4  B 501      13                                                       
HET    EDO  B 502       4                                                       
HET    SGM  B 503       6                                                       
HET    PGE  B 504      10                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     FCQ 5-(2-AZANYLETHYLSULFANYL)-3-PROPAN-2-YL-~{N}-[(4-                
HETNAM   2 FCQ  PYRIDIN-2-YLPHENYL)METHYL]-2~{H}-PYRAZOLO[4,3-                  
HETNAM   3 FCQ  D]PYRIMIDIN-7-AMINE                                             
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      CL CHLORIDE ION                                                     
HETNAM      BR BROMIDE ION                                                      
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     SGM MONOTHIOGLYCEROL                                                 
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   3  FCQ    C22 H25 N7 S                                                 
FORMUL   4  EDO    3(C2 H6 O2)                                                  
FORMUL   6   CL    CL 1-                                                        
FORMUL   7   BR    BR 1-                                                        
FORMUL   8  PG4    C8 H18 O5                                                    
FORMUL  10  SGM    C3 H8 O2 S                                                   
FORMUL  11  PGE    C6 H14 O4                                                    
FORMUL  12  HOH   *160(H2 O)                                                    
HELIX    1 AA1 PRO A   45  LEU A   58  1                                  14    
HELIX    2 AA2 LEU A   87  ALA A   93  1                                   7    
HELIX    3 AA3 PRO A  100  HIS A  121  1                                  22    
HELIX    4 AA4 LYS A  129  GLN A  131  5                                   3    
HELIX    5 AA5 ASP A  145  ALA A  149  5                                   5    
HELIX    6 AA6 THR A  165  ARG A  169  5                                   5    
HELIX    7 AA7 ALA A  170  LEU A  175  1                                   6    
HELIX    8 AA8 THR A  182  ARG A  199  1                                  18    
HELIX    9 AA9 SER A  207  GLY A  220  1                                  14    
HELIX   10 AB1 GLY A  229  MET A  233  5                                   5    
HELIX   11 AB2 ASP A  247  VAL A  252  1                                   6    
HELIX   12 AB3 ASP A  256  LEU A  267  1                                  12    
HELIX   13 AB4 SER A  276  ALA A  282  1                                   7    
HELIX   14 AB5 HIS A  283  GLN A  287  5                                   5    
HELIX   15 AB6 TYR B  178  CYS B  193  1                                  16    
HELIX   16 AB7 GLY B  198  GLN B  203  5                                   6    
HELIX   17 AB8 THR B  207  TYR B  225  1                                  19    
HELIX   18 AB9 GLN B  228  MET B  246  1                                  19    
HELIX   19 AC1 LEU B  249  GLU B  269  1                                  21    
HELIX   20 AC2 GLU B  274  ILE B  281  1                                   8    
HELIX   21 AC3 THR B  287  LEU B  302  1                                  16    
HELIX   22 AC4 THR B  310  LEU B  320  1                                  11    
HELIX   23 AC5 ASN B  326  SER B  340  1                                  15    
HELIX   24 AC6 ASP B  343  LEU B  348  1                                   6    
HELIX   25 AC7 LEU B  351  GLY B  369  1                                  19    
HELIX   26 AC8 PRO B  373  GLY B  381  1                                   9    
HELIX   27 AC9 THR B  383  LYS B  400  1                                  18    
HELIX   28 AD1 ALA B  401  HIS B  404  5                                   4    
HELIX   29 AD2 GLN B  407  TYR B  413  1                                   7    
HELIX   30 AD3 LYS B  414  HIS B  419  5                                   6    
HELIX   31 AD4 GLY B  420  LEU B  424  5                                   5    
SHEET    1 AA1 5 PHE A   4  GLY A  11  0                                        
SHEET    2 AA1 5 VAL A  17  ASN A  23 -1  O  VAL A  18   N  ILE A  10           
SHEET    3 AA1 5 VAL A  29  ARG A  36 -1  O  LYS A  34   N  VAL A  17           
SHEET    4 AA1 5 LYS A  75  GLU A  81 -1  O  LEU A  78   N  LYS A  33           
SHEET    5 AA1 5 LEU A  66  THR A  72 -1  N  ASP A  68   O  VAL A  79           
SHEET    1 AA2 3 GLN A  85  ASP A  86  0                                        
SHEET    2 AA2 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3 AA2 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1 AA3 2 VAL A 123  LEU A 124  0                                        
SHEET    2 AA3 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SSBOND   1 CYS B  327    CYS B  327                          1555   4555  2.20  
LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.33  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.34  
LINK         SG  CYS B 193                 S1  SGM B 503     1555   1555  2.02  
CISPEP   1 VAL A  154    PRO A  155          0        -7.07                     
CISPEP   2 GLN B  323    PRO B  324          0        -6.87                     
CISPEP   3 ASP B  345    PRO B  346          0        13.41                     
SITE     1 AC1 13 GLU A   8  ILE A  10  VAL A  18  ALA A  31                    
SITE     2 AC1 13 PHE A  80  GLU A  81  LEU A  83  HIS A  84                    
SITE     3 AC1 13 ASP A  86  GLN A 131  LEU A 134  HOH A 409                    
SITE     4 AC1 13 HOH A 436                                                     
SITE     1 AC2  1 LYS A  56                                                     
SITE     1 AC3  3 GLU A 162  THR A 165  ARG A 169                               
SITE     1 AC4  1 GLN B 254                                                     
SITE     1 AC5  1 LYS B 379                                                     
SITE     1 AC6  4 MET B 189  LYS B 192  CYS B 193  ASP B 305                    
SITE     1 AC7  2 ASP B 345  HIS B 404                                          
CRYST1   71.015  112.642  159.690  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014082  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008878  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006262        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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