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Database: PDB
Entry: 1F5Q
LinkDB: 1F5Q
Original site: 1F5Q 
HEADER    TRANSFERASE                             15-JUN-00   1F5Q              
TITLE     CRYSTAL STRUCTURE OF MURINE GAMMA HERPESVIRUS CYCLIN                  
TITLE    2 COMPLEXED TO HUMAN CYCLIN DEPENDENT KINASE 2                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 EC: 2.7.1.-;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: GAMMA HERPESVIRUS CYCLIN;                                  
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9 INSECT CELLS;                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;                               
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MURID HERPESVIRUS 4;                            
SOURCE  12 ORGANISM_COMMON: MURINE HERPESVIRUS 68;                              
SOURCE  13 ORGANISM_TAXID: 33708;                                               
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: DH5;                                       
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PGEX-KG                                   
KEYWDS    HERPESVIRAL CYCLIN, CYCLIN DEPENDENT KINASE.                          
KEYWDS   2 PROTEIN/PROTEIN COMPLEX, TRANSFERASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.L.CARD,P.KNOWLES,H.LAMAN,N.JONES,N.Q.MCDONALD                       
REVDAT   2   24-FEB-09 1F5Q    1       VERSN                                    
REVDAT   1   27-DEC-00 1F5Q    0                                                
JRNL        AUTH   G.L.CARD,P.KNOWLES,H.LAMAN,N.JONES,N.Q.MCDONALD              
JRNL        TITL   CRYSTAL STRUCTURE OF A GAMMA-HERPESVIRUS                     
JRNL        TITL 2 CYCLIN-CDK COMPLEX.                                          
JRNL        REF    EMBO J.                       V.  19  2877 2000              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   10856233                                                     
JRNL        DOI    10.1093/EMBOJ/19.12.2877                                     
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 45056                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 841                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8556                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 166                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 48.48                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.41                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1F5Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011275.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-NOV-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID13                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.78170                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 140317                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 30.00                    
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37900                            
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: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 12% PROPAN-2-OL, 5% PEG      
REMARK 280  4K, 10MM DTT, PH 7.5, VAPOR DIFFUSION, SITTING DROP,                
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       36.72500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 2460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ILE A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     ILE C    10                                                      
REMARK 465     GLY C    11                                                      
REMARK 465     LYS C    24                                                      
REMARK 465     LEU C    25                                                      
REMARK 465     THR C    26                                                      
REMARK 465     SER C   249                                                      
REMARK 465     LYS C   250                                                      
REMARK 465     VAL C   251                                                      
REMARK 465     VAL C   252                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     GLN D     4                                                      
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     GLN A   5    CG   CD   OE1  NE2                                  
REMARK 470     GLU A   8    CG   CD   OE1  OE2                                  
REMARK 470     LYS A   9    CG   CD   CE   NZ                                   
REMARK 470     ARG A  22    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  24    CG   CD   CE   NZ                                   
REMARK 470     LEU A  25    CG   CD1  CD2                                       
REMARK 470     GLU A 138    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 199    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 257    CG   CD   OE1  OE2                                  
REMARK 470     PHE B   6    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN B   7    CG   CD   OE1  NE2                                  
REMARK 470     GLN C   5    CG   CD   OE1  NE2                                  
REMARK 470     VAL C   7    CG1  CG2                                            
REMARK 470     LYS C   9    CG   CD   CE   NZ                                   
REMARK 470     GLU C  12    CG   CD   OE1  OE2                                  
REMARK 470     TYR C  15    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL C  17    CG1  CG2                                            
REMARK 470     ARG C  22    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN C  23    CG   OD1  ND2                                       
REMARK 470     GLU C  28    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  57    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 199    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 245    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE C 248    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN C 287    CG   CD   OE1  NE2                                  
REMARK 470     HIS C 295    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU C 296    CG   CD1  CD2                                       
REMARK 470     ARG C 297    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D   5    CG   CD   OE1  OE2                                  
REMARK 470     PHE D   6    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN D   7    CG   CD   OE1  NE2                                  
REMARK 470     PHE D   9    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU D  10    CG   CD1  CD2                                       
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    ASN A   3       37.92    167.12                                   
REMARK 500    LYS A   6      151.37    -35.34                                   
REMARK 500    THR A  14      -88.36    -98.77                                   
REMARK 500    TYR A  15       42.24    -85.45                                   
REMARK 500    VAL A  18       90.66   -160.09                                   
REMARK 500    GLU A  73     -127.64     55.97                                   
REMARK 500    ALA A  93       40.02   -102.44                                   
REMARK 500    SER A  94       15.16    172.93                                   
REMARK 500    ARG A 126      -10.81     70.11                                   
REMARK 500    ASP A 127       49.48   -146.70                                   
REMARK 500    ASN A 136     -168.50   -113.69                                   
REMARK 500    ASP A 145       74.60     53.27                                   
REMARK 500    PHE A 146       38.32    -86.39                                   
REMARK 500    THR A 160      -38.65    -19.53                                   
REMARK 500    VAL A 164     -116.00    -78.65                                   
REMARK 500    SER A 181     -140.24   -151.44                                   
REMARK 500    ARG A 199       -2.95     77.85                                   
REMARK 500    PHE A 203       67.44   -118.94                                   
REMARK 500    PRO A 204       48.93    -57.46                                   
REMARK 500    ASP A 206     -121.80    -75.14                                   
REMARK 500    GLU A 208      -73.05     38.49                                   
REMARK 500    THR A 231       -5.83    -56.61                                   
REMARK 500    ASP A 247       97.03    -69.84                                   
REMARK 500    PRO A 254       10.40    -55.79                                   
REMARK 500    ASP A 288       71.16   -117.72                                   
REMARK 500    THR A 290     -158.35   -105.69                                   
REMARK 500    GLN B   7       42.45   -100.42                                   
REMARK 500    GLU B  17      -49.75    -28.27                                   
REMARK 500    VAL B  36       37.28    -74.33                                   
REMARK 500    LEU B  63        0.17    -64.43                                   
REMARK 500    HIS B 161       54.85     33.15                                   
REMARK 500    GLU C   2       46.92    -81.46                                   
REMARK 500    GLN C   5      141.18    176.32                                   
REMARK 500    LYS C   6     -159.61    140.07                                   
REMARK 500    VAL C   7     -155.16   -145.80                                   
REMARK 500    GLU C   8      164.76    -26.97                                   
REMARK 500    THR C  14      -71.06    -37.60                                   
REMARK 500    VAL C  64      108.36    -52.03                                   
REMARK 500    GLU C  73      -87.38     65.71                                   
REMARK 500    ASN C  74       20.58   -142.68                                   
REMARK 500    PHE C  90      -34.50    -39.28                                   
REMARK 500    ASP C  92      -71.64    -51.54                                   
REMARK 500    SER C  94        5.44    176.94                                   
REMARK 500    LEU C  96      -71.39    -38.57                                   
REMARK 500    PRO C 102      -19.09    -42.43                                   
REMARK 500    SER C 106      -73.07    -47.73                                   
REMARK 500    TYR C 107      -38.67    -36.15                                   
REMARK 500    LEU C 112       -6.96    -59.76                                   
REMARK 500    ASP C 127       37.64   -150.09                                   
REMARK 500    ASP C 145       73.44     64.20                                   
REMARK 500    PHE C 146       33.24    -87.93                                   
REMARK 500    THR C 160      -43.40    -27.24                                   
REMARK 500    VAL C 163       81.59    -24.69                                   
REMARK 500    LEU C 166       -8.76    -56.76                                   
REMARK 500    SER C 181     -139.08   -128.81                                   
REMARK 500    PHE C 193      -85.99    -77.41                                   
REMARK 500    ALA C 194      -48.21    -24.27                                   
REMARK 500    ARG C 199      -28.53     73.32                                   
REMARK 500    ALA C 201      159.99    -34.14                                   
REMARK 500    PHE C 203       72.95   -150.42                                   
REMARK 500    PRO C 204       55.24    -66.53                                   
REMARK 500    ASP C 206      -76.18    -67.09                                   
REMARK 500    ARG C 217      -78.43    -53.53                                   
REMARK 500    PRO C 228      107.55    -55.42                                   
REMARK 500    TRP C 243     -153.82    -96.77                                   
REMARK 500    ARG C 245      164.60    -46.89                                   
REMARK 500    GLN C 246     -129.95   -127.34                                   
REMARK 500    PRO C 254       92.70    -54.34                                   
REMARK 500    GLU C 257       -1.46    -58.44                                   
REMARK 500    PRO C 271       -8.75    -57.84                                   
REMARK 500    ARG C 274      150.80    -47.38                                   
REMARK 500    LEU C 281      -19.74    -48.45                                   
REMARK 500    PHE C 285        5.01    -58.47                                   
REMARK 500    GLN C 287      -19.50    -44.17                                   
REMARK 500    THR C 290     -137.42   -109.69                                   
REMARK 500    LYS C 291       54.94   -166.88                                   
REMARK 500    LEU C 296     -164.48    166.38                                   
REMARK 500    SER D  13       47.89    -77.10                                   
REMARK 500    LEU D  14        3.33   -156.14                                   
REMARK 500    ASN D  39       96.26     34.17                                   
REMARK 500    ARG D  64       56.22     31.76                                   
REMARK 500    TYR D 108      -62.22    -93.29                                   
REMARK 500    HIS D 161       60.78     26.27                                   
REMARK 500    ASN D 251       30.61    -98.58                                   
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 CL A 299                  
DBREF  1F5Q A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  1F5Q B    1   252  UNP    P89883   P89883_MHV68     1    252             
DBREF  1F5Q C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  1F5Q D    1   252  UNP    P89883   P89883_MHV68     1    252             
SEQRES   1 A  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 A  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 A  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 A  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 A  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 A  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 A  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 A  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 A  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 A  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 A  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 A  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 A  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 A  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 A  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 A  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 A  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 A  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 A  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 A  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 A  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 A  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 A  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
SEQRES   1 B  252  MET ALA SER GLN GLU PHE GLN GLY PHE LEU ASP SER SER          
SEQRES   2 B  252  LEU LEU ASN GLU GLU ASP CYS ARG GLN MET ILE TYR ARG          
SEQRES   3 B  252  SER GLU ARG GLU HIS ASP ALA ARG MET VAL GLY VAL ASN          
SEQRES   4 B  252  VAL ASP GLN HIS PHE THR SER GLN TYR ARG LYS VAL LEU          
SEQRES   5 B  252  THR THR TRP MET PHE CYS VAL CYS LYS ASP LEU ARG GLN          
SEQRES   6 B  252  ASP ASN ASN VAL PHE PRO LEU ALA VAL ALA LEU LEU ASP          
SEQRES   7 B  252  GLU LEU PHE LEU SER THR ARG ILE ASP ARG GLU ASN TYR          
SEQRES   8 B  252  GLN SER THR ALA ALA VAL ALA LEU HIS ILE ALA GLY LYS          
SEQRES   9 B  252  VAL ARG ALA TYR MET PRO ILE LYS ALA THR GLN LEU ALA          
SEQRES  10 B  252  TYR LEU CYS GLY GLY ALA THR THR ALA ASP LYS LEU LEU          
SEQRES  11 B  252  THR LEU GLU VAL LYS SER LEU ASP THR LEU SER TRP VAL          
SEQRES  12 B  252  ALA ASP ARG CYS LEU SER THR ASP LEU ILE CYS TYR ILE          
SEQRES  13 B  252  LEU HIS ILE MET HIS ALA PRO ARG GLU ASP TYR LEU ASN          
SEQRES  14 B  252  ILE TYR ASN LEU CYS ARG PRO LYS ILE PHE CYS ALA LEU          
SEQRES  15 B  252  CYS ASP GLY ARG SER ALA MET LYS ARG PRO VAL LEU ILE          
SEQRES  16 B  252  THR LEU ALA CYS MET HIS LEU THR MET ASN GLN LYS TYR          
SEQRES  17 B  252  ASP TYR TYR GLU ASN ARG ILE ASP GLY VAL CYS LYS SER          
SEQRES  18 B  252  LEU TYR ILE THR LYS GLU GLU LEU HIS GLN CYS CYS ASP          
SEQRES  19 B  252  LEU VAL ASP ILE ALA ILE VAL SER PHE ASP GLU ASN TYR          
SEQRES  20 B  252  PHE LYS ILE ASN ALA                                          
SEQRES   1 C  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 C  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 C  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 C  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 C  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 C  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 C  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 C  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 C  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 C  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 C  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 C  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 C  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 C  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 C  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 C  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 C  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 C  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 C  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 C  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 C  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 C  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 C  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
SEQRES   1 D  252  MET ALA SER GLN GLU PHE GLN GLY PHE LEU ASP SER SER          
SEQRES   2 D  252  LEU LEU ASN GLU GLU ASP CYS ARG GLN MET ILE TYR ARG          
SEQRES   3 D  252  SER GLU ARG GLU HIS ASP ALA ARG MET VAL GLY VAL ASN          
SEQRES   4 D  252  VAL ASP GLN HIS PHE THR SER GLN TYR ARG LYS VAL LEU          
SEQRES   5 D  252  THR THR TRP MET PHE CYS VAL CYS LYS ASP LEU ARG GLN          
SEQRES   6 D  252  ASP ASN ASN VAL PHE PRO LEU ALA VAL ALA LEU LEU ASP          
SEQRES   7 D  252  GLU LEU PHE LEU SER THR ARG ILE ASP ARG GLU ASN TYR          
SEQRES   8 D  252  GLN SER THR ALA ALA VAL ALA LEU HIS ILE ALA GLY LYS          
SEQRES   9 D  252  VAL ARG ALA TYR MET PRO ILE LYS ALA THR GLN LEU ALA          
SEQRES  10 D  252  TYR LEU CYS GLY GLY ALA THR THR ALA ASP LYS LEU LEU          
SEQRES  11 D  252  THR LEU GLU VAL LYS SER LEU ASP THR LEU SER TRP VAL          
SEQRES  12 D  252  ALA ASP ARG CYS LEU SER THR ASP LEU ILE CYS TYR ILE          
SEQRES  13 D  252  LEU HIS ILE MET HIS ALA PRO ARG GLU ASP TYR LEU ASN          
SEQRES  14 D  252  ILE TYR ASN LEU CYS ARG PRO LYS ILE PHE CYS ALA LEU          
SEQRES  15 D  252  CYS ASP GLY ARG SER ALA MET LYS ARG PRO VAL LEU ILE          
SEQRES  16 D  252  THR LEU ALA CYS MET HIS LEU THR MET ASN GLN LYS TYR          
SEQRES  17 D  252  ASP TYR TYR GLU ASN ARG ILE ASP GLY VAL CYS LYS SER          
SEQRES  18 D  252  LEU TYR ILE THR LYS GLU GLU LEU HIS GLN CYS CYS ASP          
SEQRES  19 D  252  LEU VAL ASP ILE ALA ILE VAL SER PHE ASP GLU ASN TYR          
SEQRES  20 D  252  PHE LYS ILE ASN ALA                                          
HET     CL  A 299       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   5   CL    CL 1-                                                        
FORMUL   6  HOH   *166(H2 O)                                                    
HELIX    1   1 PRO A   45  LEU A   58  1                                  14    
HELIX    2   2 LEU A   87  ALA A   93  1                                   7    
HELIX    3   3 PRO A  100  SER A  120  1                                  21    
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 GLU A  208  GLY A  220  1                                  13    
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  258  LEU A  267  1                                  10    
HELIX   11  11 SER A  276  ALA A  282  1                                   7    
HELIX   12  12 HIS A  283  GLN A  287  5                                   5    
HELIX   13  13 ASN B   16  VAL B   36  1                                  21    
HELIX   14  14 ASN B   39  SER B   46  1                                   8    
HELIX   15  15 GLN B   47  LEU B   63  1                                  17    
HELIX   16  16 ASN B   68  THR B   84  1                                  17    
HELIX   17  17 ASP B   87  GLU B   89  5                                   3    
HELIX   18  18 ASN B   90  ALA B  107  1                                  18    
HELIX   19  19 LYS B  112  GLY B  121  1                                  10    
HELIX   20  20 THR B  125  LEU B  140  1                                  16    
HELIX   21  21 LEU B  148  MET B  160  1                                  13    
HELIX   22  22 GLU B  165  ASP B  184  1                                  20    
HELIX   23  23 ASP B  184  MET B  189  1                                   6    
HELIX   24  24 ARG B  191  ASN B  205  1                                  15    
HELIX   25  25 TYR B  208  LEU B  222  1                                  15    
HELIX   26  26 THR B  225  PHE B  243  1                                  19    
HELIX   27  27 ASN B  246  ASN B  251  1                                   6    
HELIX   28  28 PRO C   45  LYS C   56  1                                  12    
HELIX   29  29 LYS C   88  ALA C   93  1                                   6    
HELIX   30  30 PRO C  100  SER C  120  1                                  21    
HELIX   31  31 LYS C  129  GLN C  131  5                                   3    
HELIX   32  32 THR C  158  GLU C  162  5                                   5    
HELIX   33  33 THR C  165  ARG C  169  5                                   5    
HELIX   34  34 ALA C  170  LEU C  175  1                                   6    
HELIX   35  35 THR C  182  THR C  198  1                                  17    
HELIX   36  36 SER C  207  GLY C  220  1                                  14    
HELIX   37  37 GLY C  229  MET C  233  5                                   5    
HELIX   38  38 ASP C  256  LEU C  267  1                                  12    
HELIX   39  39 SER C  276  LEU C  281  1                                   6    
HELIX   40  40 ALA C  282  GLN C  287  5                                   6    
HELIX   41  42 ASN D   16  VAL D   36  1                                  21    
HELIX   42  43 VAL D   40  SER D   46  1                                   7    
HELIX   43  44 SER D   46  LEU D   63  1                                  18    
HELIX   44  45 ASN D   68  THR D   84  1                                  17    
HELIX   45  46 ASP D   87  GLU D   89  5                                   3    
HELIX   46  47 ASN D   90  ALA D  107  1                                  18    
HELIX   47  48 LYS D  112  GLY D  121  1                                  10    
HELIX   48  49 THR D  125  LEU D  140  1                                  16    
HELIX   49  50 LEU D  148  MET D  160  1                                  13    
HELIX   50  51 PRO D  163  GLU D  165  5                                   3    
HELIX   51  52 ASP D  166  ASP D  184  1                                  19    
HELIX   52  53 ASP D  184  MET D  189  1                                   6    
HELIX   53  54 ARG D  191  ASN D  205  1                                  15    
HELIX   54  55 TYR D  208  LEU D  222  1                                  15    
HELIX   55  56 THR D  225  PHE D  243  1                                  19    
HELIX   56  57 ASN D  246  ASN D  251  1                                   6    
SHEET    1   A 4 VAL A  18  ALA A  21  0                                        
SHEET    2   A 4 VAL A  30  ARG A  36 -1  O  VAL A  30   N  ALA A  21           
SHEET    3   A 4 LYS A  75  GLU A  81 -1  N  LEU A  76   O  ILE A  35           
SHEET    4   A 4 LEU A  66  THR A  72 -1  N  LEU A  67   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  N  ILE A 135   O  GLN A  85           
SHEET    3   B 3 ILE A 141  LEU A 143 -1  N  LYS A 142   O  LEU A 134           
SHEET    1   C 3 VAL A 123  LEU A 124  0                                        
SHEET    2   C 3 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    3   C 3 VAL A 154  PRO A 155 -1  O  VAL A 154   N  ALA A 151           
SHEET    1   D 4 VAL C  29  ARG C  36  0                                        
SHEET    2   D 4 LYS C  75  GLU C  81 -1  N  LEU C  76   O  ILE C  35           
SHEET    3   D 4 LEU C  66  THR C  72 -1  N  LEU C  67   O  VAL C  79           
SHEET    1   E 3 GLN C  85  ASP C  86  0                                        
SHEET    2   E 3 LEU C 133  ILE C 135 -1  N  ILE C 135   O  GLN C  85           
SHEET    3   E 3 ILE C 141  LEU C 143 -1  N  LYS C 142   O  LEU C 134           
SHEET    1   F 3 VAL C 123  LEU C 124  0                                        
SHEET    2   F 3 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
SHEET    3   F 3 VAL C 154  PRO C 155 -1  N  VAL C 154   O  ALA C 151           
SITE     1 AC1  2 ARG A 217  TRP A 243                                          
CRYST1   87.590   73.450  107.670  90.00 102.18  90.00 P 1 21 1      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      0.011417  0.000000  0.002464        0.00000                         
SCALE2      0.000000  0.013615  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009502        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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