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Database: PDB
Entry: 1H28
LinkDB: 1H28
Original site: 1H28 
HEADER    CELL CYCLE/TRANSFERASE SUBSTRATE        31-JUL-02   1H28              
TITLE     CDK2/CYCLIN A IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM  
TITLE    2 P107                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CYCLIN-DEPENDENT KINASE 2, P33 PROTEIN KINASE, CDK2;        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CYCLIN A2;                                                 
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 FRAGMENT: CYCLIN FOLD, RESIDUES 175-432;                             
COMPND  10 SYNONYM: CYCLIN A;                                                   
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: RETINOBLASTOMA-LIKE PROTEIN 1;                             
COMPND  14 CHAIN: E, F;                                                         
COMPND  15 FRAGMENT: RB PEPTIDE, RESIDUES 653-663;                              
COMPND  16 SYNONYM: 107 KDA RETINOBLASTOMA-ASSOCIATED PROTEIN, PRB1, P107,      
COMPND  17  P107 RECRUITMENT PEPTIDE 11MER;                                     
COMPND  18 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: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PGEX;                                     
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PET21D;                                   
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 SYNTHETIC: YES;                                                      
SOURCE  19 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  20 ORGANISM_COMMON: HUMAN;                                              
SOURCE  21 ORGANISM_TAXID: 9606                                                 
KEYWDS    CELL CYCLE, PROTEIN KINASE, CYCLIN, CDK2, RECRUITMENT, PEPTIDE        
KEYWDS   2 SPECIFICITY, SERINE/THREONINE-PROTEIN KINASE, ATP-BINDING, CELL      
KEYWDS   3 DIVISION, MITOSIS, PHOSPHORYLATION, CELL CYCLE-TRANSFERASE           
KEYWDS   4 SUBSTRATE, CELL CYCLE-TRANSFERASE SUBSTRATE COMPLEX                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.TEWS,K.Y.CHENG,E.D.LOWE,M.E.M.NOBLE,N.R.BROWN,S.GUL,S.GAMBLIN,      
AUTHOR   2 L.N.JOHNSON                                                          
REVDAT   3   13-JUL-11 1H28    1       VERSN                                    
REVDAT   2   24-FEB-09 1H28    1       VERSN                                    
REVDAT   1   01-FEB-03 1H28    0                                                
JRNL        AUTH   E.D.LOWE,I.TEWS,K.Y.CHENG,N.R.BROWN,S.GUL,M.E.M.NOBLE,       
JRNL        AUTH 2 S.GAMBLIN,L.N.JOHNSON                                        
JRNL        TITL   SPECIFICITY DETERMINANTS OF RECRUITMENT PEPTIDES BOUND TO    
JRNL        TITL 2 PHOSPHO-CDK2/CYCLIN A                                        
JRNL        REF    BIOCHEMISTRY                  V.  41 15625 2002              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   12501191                                                     
JRNL        DOI    10.1021/BI0268910                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   N.R.BROWN,M.E.M.NOBLE,J.A.ENDICOTT,L.N.JOHNSON               
REMARK   1  TITL   THE STRUCTURAL BASIS FOR SPECIFICITY OF SUBSTRATE AND        
REMARK   1  TITL 2 RECRUITMENT PEPTIDES FOR CYCLIN-DEPENDANT KINASES            
REMARK   1  REF    NAT.CELL BIOL.                V.   1   438 1999              
REMARK   1  REFN                   ISSN 1465-7392                               
REMARK   1  PMID   10559988                                                     
REMARK   1  DOI    10.1038/15674                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.62                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 39408                          
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) : 0.247                           
REMARK   3   R VALUE            (WORKING SET) : 0.243                           
REMARK   3   FREE R VALUE                     : 0.323                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2095                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9088                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 37                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.76                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.07000                                             
REMARK   3    B22 (A**2) : 0.06000                                              
REMARK   3    B33 (A**2) : 0.01000                                              
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): 1.245         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.450         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.260         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.287        
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1H28 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-AUG-02.                  
REMARK 100 THE PDBE ID CODE IS EBI-11187.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41507                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.990                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : 0.16600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 2.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1QMZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M KCL, 1.2M (NH4)2SO4, 40MM HEPES     
REMARK 280  PH 7.0. PROTEIN CONCENTRATION = 10MG/ML                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       74.75150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       81.25700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       74.75150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       81.25700            
REMARK 290   SMTRY3   4  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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E                               
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F                               
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  CDK2: CONTROL OF THE CELL CYCLE DURING S PHASE AND G2.              
REMARK 400  BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES.                   
REMARK 400                                                                      
REMARK 400  CYCLIN A2: CONTROL OF THE CELL CYCLE. INTERACTS WITH THE CDK2       
REMARK 400  AND CDC2 PROTEIN KINASES.                                           
REMARK 400                                                                      
REMARK 400  P107: INVOLVED IN G1 ARREST.                                        
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    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ARG A   297                                                      
REMARK 465     LEU A   298                                                      
REMARK 465     GLU B   175                                                      
REMARK 465     GLY C    -4                                                      
REMARK 465     PRO C    -3                                                      
REMARK 465     LEU C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     GLU D   175                                                      
REMARK 465     ALA E   653                                                      
REMARK 465     ALA F   653                                                      
REMARK 465     GLY F   654                                                      
REMARK 465     SER F   655                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ALA A   277     N    ALA A   279              1.76            
REMARK 500   ND1  HIS D   321     OG   SER D   375              1.87            
REMARK 500   OD1  ASN D   415     N    LYS D   417              1.89            
REMARK 500   O    VAL D   175     N    ASP D   177              2.00            
REMARK 500   O    ILE C    49     OG   SER C    53              2.03            
REMARK 500   OD2  ASP A   247     OG   SER A   249              2.06            
REMARK 500   OE2  GLU A   224     OG1  THR A   231              2.07            
REMARK 500   O    MET A     1     O    HOH A  2002              2.07            
REMARK 500   O    THR A    72     N    ASN A    74              2.07            
REMARK 500   O    LEU C   296     O    HOH C  2010              2.08            
REMARK 500   OE1  GLU A    81     NZ   LYS A   142              2.10            
REMARK 500   NZ   LYS B   266     OE1  GLU B   295              2.11            
REMARK 500   NZ   LYS A   129     OG1  THR A   165              2.11            
REMARK 500   O    LEU D   376     OG1  THR D   380              2.16            
REMARK 500   O    GLU A    40     NZ   LYS B   288              2.18            
REMARK 500   O    LEU D   306     N    ALA D   308              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    LYS B   379     NH2  ARG D   378     2665     1.84            
REMARK 500   NH1  ARG B   378     O    LEU D   320     2665     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MET D 261   CG    MET D 261   SD      0.159                       
REMARK 500    PHE D 267   CE2   PHE D 267   CD2    -0.156                       
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    ASP A  86   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ASP A 185   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 206   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP A 210   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP A 247   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP A 270   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ASP B 181   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP B 205   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP B 283   CB  -  CG  -  OD2 ANGL. DEV. =   7.8 DEGREES          
REMARK 500    ASP B 305   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP B 345   CB  -  CG  -  OD2 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    ASP B 393   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    LEU C  76   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    ASP C  86   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP C  92   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP C 127   CB  -  CG  -  OD2 ANGL. DEV. =   8.3 DEGREES          
REMARK 500    ARG C 169   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ASP C 206   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP C 210   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ASP C 247   CB  -  CG  -  OD2 ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ASP C 256   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP D 177   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP D 216   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    LEU D 243   CA  -  CB  -  CG  ANGL. DEV. =  13.9 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    GLU A   2      -14.38    -49.69                                   
REMARK 500    THR A  14      -83.42     23.81                                   
REMARK 500    LEU A  37      -97.42   -103.12                                   
REMARK 500    ASP A  38      122.76     93.82                                   
REMARK 500    GLU A  40      -35.22     83.20                                   
REMARK 500    THR A  41     -169.71    -67.83                                   
REMARK 500    PRO A  61      -34.12    -37.45                                   
REMARK 500    GLU A  73      -49.47     49.62                                   
REMARK 500    HIS A  84      -60.09    -28.22                                   
REMARK 500    CYS A 118      -71.69    -40.32                                   
REMARK 500    ASP A 127       59.19   -162.82                                   
REMARK 500    THR A 137      -42.56    -18.18                                   
REMARK 500    LEU A 143      143.50    -31.57                                   
REMARK 500    ALA A 144     -159.87   -153.46                                   
REMARK 500    ASP A 145       88.57     20.57                                   
REMARK 500    TYR A 159     -162.22   -112.11                                   
REMARK 500    VAL A 164      137.31     70.46                                   
REMARK 500    LEU A 175       25.74    -64.17                                   
REMARK 500    SER A 181     -138.60   -148.06                                   
REMARK 500    PHE A 193      -76.16    -45.92                                   
REMARK 500    ALA A 201      132.86    -33.94                                   
REMARK 500    LEU A 202      -71.42    -67.48                                   
REMARK 500    PHE A 203       76.34   -109.43                                   
REMARK 500    TRP A 227       68.98   -166.35                                   
REMARK 500    THR A 231       12.57    -69.68                                   
REMARK 500    PHE A 240      152.15    -34.50                                   
REMARK 500    TRP A 243      175.45    -59.47                                   
REMARK 500    ASP A 256     -157.83    -70.09                                   
REMARK 500    LEU A 267       46.34    -78.79                                   
REMARK 500    ALA A 277     -137.23    -68.86                                   
REMARK 500    LYS A 278      -42.61      4.60                                   
REMARK 500    PRO B 176       -9.01    -55.45                                   
REMARK 500    HIS B 179      -73.61    -51.54                                   
REMARK 500    ARG B 187       -8.84    -53.43                                   
REMARK 500    GLU B 190      -71.53    -42.16                                   
REMARK 500    VAL B 191      -38.79    -30.63                                   
REMARK 500    VAL B 197      -82.98    -40.41                                   
REMARK 500    SER B 245      -26.05   -149.05                                   
REMARK 500    SER B 265      -74.61    -59.62                                   
REMARK 500    TYR B 271       73.97   -114.05                                   
REMARK 500    PRO B 273      152.85    -48.72                                   
REMARK 500    ASP B 284       17.08     57.43                                   
REMARK 500    PHE B 304       17.69     56.69                                   
REMARK 500    ALA B 307       57.32    -92.69                                   
REMARK 500    LEU B 320      -34.73    -29.91                                   
REMARK 500    ALA B 325      151.87    -47.34                                   
REMARK 500    ASN B 326       93.60   -160.39                                   
REMARK 500    LEU B 336      -74.12    -45.46                                   
REMARK 500    TYR B 347      -18.36    -39.84                                   
REMARK 500    HIS B 361      -73.60    -59.35                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     121 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    TYR A 159        -24.57                                           
REMARK 500    TPO C 160        -41.19                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A 163        24.7      L          L   OUTSIDE RANGE           
REMARK 500    GLU B 268        24.7      L          L   OUTSIDE RANGE           
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 CHAIN E OF RETINOBLASTOMA-LIKE    
REMARK 800  PROTEIN 1                                                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN F OF RETINOBLASTOMA-LIKE    
REMARK 800  PROTEIN 1                                                           
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AQ1   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 INHIBITOR STAUROSPORINE                                              
REMARK 900 RELATED ID: 1B38   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1B39   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 PHOSPHORYLATED ON THR 160            
REMARK 900 RELATED ID: 1BUH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CDK2 KINASE COMPLEX WITHCELL          
REMARK 900 CYCLE-REGULATORY PROTEIN CKSHS1                                      
REMARK 900 RELATED ID: 1CKP   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 INHIBITOR PURVALANOL B                                               
REMARK 900 RELATED ID: 1DI8   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN                 
REMARK 900 COMPLEX WITH 4-[3- HYDROXYANILINO]-6,7-DIMETHOXYQUINAZOLINE          
REMARK 900 RELATED ID: 1DM2   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 INHIBITOR HYMENIALDISINE                                             
REMARK 900 RELATED ID: 1E1V   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 INHIBITOR NU2058                                                     
REMARK 900 RELATED ID: 1E1X   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 INHIBITOR NU6027                                                     
REMARK 900 RELATED ID: 1E9H   RELATED DB: PDB                                   
REMARK 900 THR 160 PHOSPHORYLATED CDK2 - HUMAN CYCLIN A3 COMPLEX WITH           
REMARK 900 THE INHIBITOR INDIRUBIN-5- SULPHONATE BOUND                          
REMARK 900 RELATED ID: 1F5Q   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MURINE GAMMA HERPESVIRUS CYCLIN                 
REMARK 900 COMPLEXED TO HUMAN CYCLIN DEPENDANT KINASE 2                         
REMARK 900 RELATED ID: 1FIN   RELATED DB: PDB                                   
REMARK 900 CYCLIN A - CYCLIN-DEPENDENT KINASE 2 COMPLEX                         
REMARK 900 RELATED ID: 1FQ1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP)             
REMARK 900 INCOMPLEX WITH PHOSPHO-CDK2                                          
REMARK 900 RELATED ID: 1FVT   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) INCOMPLEX          
REMARK 900 WITH AN OXINDOLE INHIBITOR                                           
REMARK 900 RELATED ID: 1FVV   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CDK2/CYCLIN A IN COMPLEX WITH AN                    
REMARK 900 OXINDOLEINHIBITOR                                                    
REMARK 900 RELATED ID: 1G5S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2)          
REMARK 900 IN COMPLEX WITH THE INHIBITOR H717                                   
REMARK 900 RELATED ID: 1GIH   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 CDK4INHIBITOR                                                        
REMARK 900 RELATED ID: 1GII   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 CDK4INHIBITOR                                                        
REMARK 900 RELATED ID: 1GIJ   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 CDK4INHIBITOR                                                        
REMARK 900 RELATED ID: 1GY3   RELATED DB: PDB                                   
REMARK 900 PCDK2/CYCLIN A IN COMPLEX WITH MGADP, NITRATE AND PEPTIDE            
REMARK 900 SUBSTRATE                                                            
REMARK 900 RELATED ID: 1GZ8   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 INHIBITOR 2-AMINO-6-(3'-METHYL- 2'-OXO)BUTOXYPURINE                  
REMARK 900 RELATED ID: 1H00   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6 -BIS ANILINO               
REMARK 900 PYRIMIDINE CDK4 INHIBITOR                                            
REMARK 900 RELATED ID: 1H01   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 2, 4 -BIS ANILINO               
REMARK 900 PYRIMIDINE CDK4 INHIBITOR                                            
REMARK 900 RELATED ID: 1H06   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6 -BIS ANILINO               
REMARK 900 PYRIMIDINE CDK4 INHIBITOR                                            
REMARK 900 RELATED ID: 1H07   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6 -BIS ANILINO               
REMARK 900 PYRIMIDINE CDK4 INHIBITOR                                            
REMARK 900 RELATED ID: 1H08   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 2, 4 -BIS ANILINO               
REMARK 900 PYRIMIDINE CDK4 INHIBITOR                                            
REMARK 900 RELATED ID: 1H0U   RELATED DB: PDB                                   
REMARK 900 M. SMEGMATIS ARYLAMINE N-ACETYL TRANSFERASE                          
REMARK 900 RELATED ID: 1H0V   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE          
REMARK 900 INHIBITOR 2-AMINO-6-[(R )-PYRROLIDINO-5'-YL]METHOXYPURINE            
REMARK 900 RELATED ID: 1H0W   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE          
REMARK 900 INHIBITOR 2-AMINO-6-[ CYCLOHEX-3-ENYL]METHOXYPURINE                  
REMARK 900 RELATED ID: 1H1P   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED           
REMARK 900 WITH THE INHIBITOR NU2058                                            
REMARK 900 RELATED ID: 1H1Q   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED           
REMARK 900 WITH THE INHIBITOR NU6094                                            
REMARK 900 RELATED ID: 1H1R   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED           
REMARK 900 WITH THE INHIBITOR NU6086                                            
REMARK 900 RELATED ID: 1H1S   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED           
REMARK 900 WITH THE INHIBITOR NU6102                                            
REMARK 900 RELATED ID: 1H24   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH A 9 RESIDUE RECRUITMENT                 
REMARK 900 PEPTIDE FROM E2F                                                     
REMARK 900 RELATED ID: 1H25   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH A 11 RESIDUE RECRUITMENT                
REMARK 900 PEPTIDE FROM E2F                                                     
REMARK 900 RELATED ID: 1H26   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH A 11 RESIDUE RECRUITMENT                
REMARK 900 PEPTIDE FROM P53                                                     
REMARK 900 RELATED ID: 1H27   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH A 11 RESIDUE RECRUITMENT                
REMARK 900 PEPTIDE FROM P27                                                     
REMARK 900 RELATED ID: 1HCK   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1HCL   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1JST   RELATED DB: PDB                                   
REMARK 900 PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A           
REMARK 900 RELATED ID: 1JSU   RELATED DB: PDB                                   
REMARK 900 P27(KIP1)/CYCLIN A/CDK2 COMPLEX                                      
REMARK 900 RELATED ID: 1JSV   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) INCOMPLEX          
REMARK 900 WITH 4-[(6-AMINO-4- PYRIMIDINYL)AMINO]BENZENESULFONAMIDE             
REMARK 900 RELATED ID: 1JVP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 (UNPHOSPHORYLATED)                   
REMARK 900 INCOMPLEX WITH PKF049-365                                            
REMARK 900 RELATED ID: 1KE5   RELATED DB: PDB                                   
REMARK 900 CDK2 COMPLEXED WITH N-METHYL-4-{[(2-OXO- 1,2-DIHYDRO-3H-             
REMARK 900 INDOL-3-YLIDENE)METHYL] AMINO}BENZENESULFONAMIDE                     
REMARK 900 RELATED ID: 1KE6   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH N-METHYL-{           
REMARK 900 4-[2-(7-OXO-6,7-DIHYDRO -8H-[1,3]THIAZOLO[5,4-E]INDOL-8-             
REMARK 900 YLIDENE)HYDRAZINO]PHENYL}METHANESULFONAMIDE                          
REMARK 900 RELATED ID: 1KE7   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[(2,2-            
REMARK 900 DIOXIDO-1,3-DIHYDRO-2- BENZOTHIEN-5-YL)AMINO]METHYLENE}-5-           
REMARK 900 (1,3- OXAZOL-5-YL)-1,3-DIHYDRO-2H-INDOL-2-ONE                        
REMARK 900 RELATED ID: 1KE8   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 4-{[(2-OXO-          
REMARK 900 1,2-DIHYDRO-3H-INDOL-3 -YLIDENE)METHYL]AMINO}-N-(1,3-                
REMARK 900 THIAZOL-2- YL)BENZENESULFONAMIDE                                     
REMARK 900 RELATED ID: 1KE9   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[4-({             
REMARK 900 [AMINO(IMINO)METHYL] AMINOSULFONYL)ANILINO]METHYLENE}-2-OXO          
REMARK 900 -2,3- DIHYDRO-1H-INDOLE                                              
REMARK 900 RELATED ID: 1QMZ   RELATED DB: PDB                                   
REMARK 900 PHOSPHORYLATED CDK2-CYCLYIN A-SUBSTRATE PEPTIDE COMPLEX              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 MOLECULE IS A TRUNCATED FRAGMENT OF CYCLIN A3 CONSISTING OF          
REMARK 999 RESIDUES 175-432                                                     
DBREF  1H28 A   -4     0  PDB    1H28     1H28            -4      0             
DBREF  1H28 A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  1H28 B  175   432  UNP    P20248   CGA2_HUMAN     175    432             
DBREF  1H28 C   -4     0  PDB    1H28     1H28            -4      0             
DBREF  1H28 C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  1H28 D  175   432  UNP    P20248   CGA2_HUMAN     175    432             
DBREF  1H28 E  653   663  UNP    P28749   RBL1_HUMAN     653    663             
DBREF  1H28 F  653   663  UNP    P28749   RBL1_HUMAN     653    663             
SEQRES   1 A  303  GLY PRO LEU GLY SER MET GLU ASN PHE GLN LYS VAL GLU          
SEQRES   2 A  303  LYS ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA          
SEQRES   3 A  303  ARG ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS          
SEQRES   4 A  303  ILE ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR          
SEQRES   5 A  303  ALA ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS          
SEQRES   6 A  303  PRO ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU          
SEQRES   7 A  303  ASN LYS LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP          
SEQRES   8 A  303  LEU LYS LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE          
SEQRES   9 A  303  PRO LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU          
SEQRES  10 A  303  GLN GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS          
SEQRES  11 A  303  ARG ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU          
SEQRES  12 A  303  GLY ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA          
SEQRES  13 A  303  PHE GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL          
SEQRES  14 A  303  THR LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS          
SEQRES  15 A  303  LYS TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY          
SEQRES  16 A  303  CYS ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE          
SEQRES  17 A  303  PRO GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE          
SEQRES  18 A  303  ARG THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY          
SEQRES  19 A  303  VAL THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS          
SEQRES  20 A  303  TRP ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU          
SEQRES  21 A  303  ASP GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS          
SEQRES  22 A  303  TYR ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU          
SEQRES  23 A  303  ALA HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO          
SEQRES  24 A  303  HIS LEU ARG LEU                                              
SEQRES   1 B  259  GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU          
SEQRES   2 B  259  ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR          
SEQRES   3 B  259  MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA          
SEQRES   4 B  259  ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR          
SEQRES   5 B  259  LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR          
SEQRES   6 B  259  ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY          
SEQRES   7 B  259  LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA          
SEQRES   8 B  259  SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU          
SEQRES   9 B  259  PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN          
SEQRES  10 B  259  VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR          
SEQRES  11 B  259  PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR          
SEQRES  12 B  259  GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL          
SEQRES  13 B  259  GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE          
SEQRES  14 B  259  ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE          
SEQRES  15 B  259  ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR          
SEQRES  16 B  259  GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY          
SEQRES  17 B  259  TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU          
SEQRES  18 B  259  HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN          
SEQRES  19 B  259  SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY          
SEQRES  20 B  259  VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU              
SEQRES   1 C  303  GLY PRO LEU GLY SER MET GLU ASN PHE GLN LYS VAL GLU          
SEQRES   2 C  303  LYS ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA          
SEQRES   3 C  303  ARG ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS          
SEQRES   4 C  303  ILE ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR          
SEQRES   5 C  303  ALA ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS          
SEQRES   6 C  303  PRO ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU          
SEQRES   7 C  303  ASN LYS LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP          
SEQRES   8 C  303  LEU LYS LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE          
SEQRES   9 C  303  PRO LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU          
SEQRES  10 C  303  GLN GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS          
SEQRES  11 C  303  ARG ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU          
SEQRES  12 C  303  GLY ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA          
SEQRES  13 C  303  PHE GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL          
SEQRES  14 C  303  THR LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS          
SEQRES  15 C  303  LYS TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY          
SEQRES  16 C  303  CYS ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE          
SEQRES  17 C  303  PRO GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE          
SEQRES  18 C  303  ARG THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY          
SEQRES  19 C  303  VAL THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS          
SEQRES  20 C  303  TRP ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU          
SEQRES  21 C  303  ASP GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS          
SEQRES  22 C  303  TYR ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU          
SEQRES  23 C  303  ALA HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO          
SEQRES  24 C  303  HIS LEU ARG LEU                                              
SEQRES   1 D  259  GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU          
SEQRES   2 D  259  ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR          
SEQRES   3 D  259  MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA          
SEQRES   4 D  259  ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR          
SEQRES   5 D  259  LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR          
SEQRES   6 D  259  ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY          
SEQRES   7 D  259  LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA          
SEQRES   8 D  259  SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU          
SEQRES   9 D  259  PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN          
SEQRES  10 D  259  VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR          
SEQRES  11 D  259  PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR          
SEQRES  12 D  259  GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL          
SEQRES  13 D  259  GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE          
SEQRES  14 D  259  ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE          
SEQRES  15 D  259  ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR          
SEQRES  16 D  259  GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY          
SEQRES  17 D  259  TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU          
SEQRES  18 D  259  HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN          
SEQRES  19 D  259  SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY          
SEQRES  20 D  259  VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU              
SEQRES   1 E   11  ALA GLY SER ALA LYS ARG ARG LEU PHE GLY GLU                  
SEQRES   1 F   11  ALA GLY SER ALA LYS ARG ARG LEU PHE GLY GLU                  
MODRES 1H28 TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 1H28 TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   7  HOH   *37(H2 O)                                                     
HELIX    1   1 PRO A   45  LYS A   56  1                                  12    
HELIX    2   2 LEU A   87  ALA A   93  1                                   7    
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 THR A  165  ARG A  169  5                                   5    
HELIX    6   6 ALA A  170  LEU A  175  1                                   6    
HELIX    7   7 THR A  182  ARG A  199  1                                  18    
HELIX    8   8 SER A  207  GLY A  220  1                                  14    
HELIX    9   9 GLY A  229  MET A  233  5                                   5    
HELIX   10  10 ASP A  247  VAL A  252  1                                   6    
HELIX   11  11 ASP A  256  LEU A  267  1                                  12    
HELIX   12  12 HIS A  283  VAL A  289  5                                   7    
HELIX   13  13 VAL B  175  ASP B  177  5                                   3    
HELIX   14  14 TYR B  178  LYS B  194  1                                  17    
HELIX   15  15 GLY B  198  GLN B  203  1                                   6    
HELIX   16  16 THR B  207  TYR B  225  1                                  19    
HELIX   17  17 GLN B  228  LEU B  243  1                                  16    
HELIX   18  18 LEU B  249  GLU B  269  1                                  21    
HELIX   19  19 GLU B  274  THR B  282  1                                   9    
HELIX   20  20 THR B  287  LEU B  302  1                                  16    
HELIX   21  21 THR B  310  LEU B  320  1                                  11    
HELIX   22  22 ASN B  326  ASP B  343  1                                  18    
HELIX   23  23 LEU B  351  GLY B  369  1                                  19    
HELIX   24  24 PRO B  373  GLY B  381  1                                   9    
HELIX   25  25 THR B  383  LYS B  400  1                                  18    
HELIX   26  26 ALA B  401  HIS B  404  5                                   4    
HELIX   27  27 GLN B  407  TYR B  413  1                                   7    
HELIX   28  28 GLY B  420  LEU B  424  5                                   5    
HELIX   29  29 SER C    0  GLU C    2  5                                   3    
HELIX   30  30 PRO C   45  LYS C   56  1                                  12    
HELIX   31  31 LEU C   87  SER C   94  1                                   8    
HELIX   32  32 PRO C  100  HIS C  121  1                                  22    
HELIX   33  33 LYS C  129  GLN C  131  5                                   3    
HELIX   34  34 ALA C  170  LEU C  175  1                                   6    
HELIX   35  35 SER C  181  ARG C  199  1                                  19    
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  247  VAL C  252  1                                   6    
HELIX   39  39 ASP C  256  LEU C  267  1                                  12    
HELIX   40  40 SER C  276  LEU C  281  1                                   6    
HELIX   41  41 HIS C  283  GLN C  287  5                                   5    
HELIX   42  42 TYR D  178  CYS D  193  1                                  16    
HELIX   43  43 GLY D  198  GLN D  203  5                                   6    
HELIX   44  44 THR D  207  TYR D  225  1                                  19    
HELIX   45  45 GLN D  228  LEU D  243  1                                  16    
HELIX   46  46 LEU D  249  GLU D  269  1                                  21    
HELIX   47  47 GLU D  274  THR D  282  1                                   9    
HELIX   48  48 THR D  287  THR D  303  1                                  17    
HELIX   49  49 THR D  310  PHE D  319  1                                  10    
HELIX   50  50 LEU D  320  GLN D  322  5                                   3    
HELIX   51  51 ASN D  326  ASP D  343  1                                  18    
HELIX   52  52 ASP D  343  LEU D  348  1                                   6    
HELIX   53  53 LEU D  351  GLY D  369  1                                  19    
HELIX   54  54 PRO D  373  GLY D  381  1                                   9    
HELIX   55  55 LEU D  387  ALA D  401  1                                  15    
HELIX   56  56 GLN D  407  TYR D  413  1                                   7    
HELIX   57  57 GLY D  420  LEU D  424  5                                   5    
SHEET    1  AA 5 PHE A   4  GLY A  13  0                                        
SHEET    2  AA 5 GLY A  16  ASN A  23 -1  O  GLY A  16   N  GLY A  13           
SHEET    3  AA 5 VAL A  29  ARG A  36 -1  O  VAL A  30   N  ALA A  21           
SHEET    4  AA 5 LYS A  75  GLU A  81 -1  O  LEU A  76   N  ILE A  35           
SHEET    5  AA 5 LEU A  66  THR A  72 -1  N  LEU A  67   O  VAL A  79           
SHEET    1  AB 3 GLN A  85  ASP A  86  0                                        
SHEET    2  AB 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3  AB 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1  AC 2 VAL A 123  LEU A 124  0                                        
SHEET    2  AC 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1  CA 5 PHE C   4  GLU C  12  0                                        
SHEET    2  CA 5 VAL C  17  ASN C  23 -1  O  VAL C  18   N  ILE C  10           
SHEET    3  CA 5 VAL C  29  ILE C  35 -1  O  VAL C  30   N  ALA C  21           
SHEET    4  CA 5 LEU C  76  GLU C  81 -1  O  LEU C  76   N  ILE C  35           
SHEET    5  CA 5 LEU C  66  HIS C  71 -1  N  LEU C  67   O  VAL C  79           
SHEET    1  CB 3 GLN C  85  ASP C  86  0                                        
SHEET    2  CB 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3  CB 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1  CC 2 VAL C 123  LEU C 124  0                                        
SHEET    2  CC 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.35  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.58  
LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.66  
LINK         O   TPO C 160                 N   HIS C 161     1555   1555  1.82  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.46  
CISPEP   1 VAL A  154    PRO A  155          0         3.47                     
CISPEP   2 GLN B  323    PRO B  324          0       -13.65                     
CISPEP   3 ASP B  345    PRO B  346          0        -9.96                     
CISPEP   4 VAL C  154    PRO C  155          0         4.04                     
CISPEP   5 GLN D  323    PRO D  324          0       -21.86                     
CISPEP   6 ASP D  345    PRO D  346          0        19.81                     
SITE     1 AC1 15 LEU A  96  HIS A 295  MET B 210  TRP B 217                    
SITE     2 AC1 15 GLU B 220  GLU B 224  GLY B 251  LYS B 252                    
SITE     3 AC1 15 GLN B 254  TYR B 280  ILE B 281  THR B 282                    
SITE     4 AC1 15 THR B 285  TYR B 286  SER C 239                               
SITE     1 AC2 18 LYS A 237  SER A 239  HIS C 295  MET D 210                    
SITE     2 AC2 18 TRP D 217  GLU D 220  GLU D 224  ARG D 250                    
SITE     3 AC2 18 GLY D 251  LYS D 252  GLN D 254  TYR D 280                    
SITE     4 AC2 18 ILE D 281  THR D 282  ASP D 283  THR D 285                    
SITE     5 AC2 18 TYR D 286  HOH F2001                                          
CRYST1  149.503  162.514   71.375  90.00  90.00  90.00 P 21 21 2     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      0.006689  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006153  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014010        0.00000                         
MTRIX1   1  0.999990 -0.000490  0.003600       -0.03242    1                    
MTRIX2   1 -0.000480 -1.000000 -0.001210        0.00121    1                    
MTRIX3   1  0.003600  0.001210 -0.999990       -0.99999    1                    
MTRIX1   2  0.999990  0.000630  0.003450       -0.05151    1                    
MTRIX2   2  0.000620 -0.999990  0.004140      154.78839    1                    
MTRIX3   2  0.003450 -0.004140 -0.999990       35.96083    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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