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Database: PDB
Entry: 1B38
LinkDB: 1B38
Original site: 1B38 
HEADER    TRANSFERASE                             17-DEC-98   1B38              
TITLE     HUMAN CYCLIN-DEPENDENT KINASE 2                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (CELL DIVISION PROTEIN KINASE 2);                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: INTACT;                                                    
COMPND   5 SYNONYM: P33 PROTEIN KINASE;                                         
COMPND   6 EC: 2.7.1.37;                                                        
COMPND   7 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;                                    
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: BACULOVIRUS                               
KEYWDS    PROTEIN KINASE, TRANSFERASE, SERINE/THREONINE PROTEIN                 
KEYWDS   2 KINASE, ATP-BINDING, CELL CYCLE, CELL DIVISION, MITOSIS,             
KEYWDS   3 PHOSPHORYLATION                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.R.BROWN,M.E.M.NOBLE,A.M.LAWRIE,M.C.MORRIS,P.TUNNAH,                 
AUTHOR   2 G.DIVITA,L.N.JOHNSON,J.A.ENDICOTT                                    
REVDAT   4   24-FEB-09 1B38    1       VERSN                                    
REVDAT   3   01-APR-03 1B38    1       JRNL                                     
REVDAT   2   22-DEC-99 1B38    4       HEADER COMPND REMARK JRNL                
REVDAT   2 2                   4       ATOM   SOURCE SEQRES                     
REVDAT   1   23-DEC-98 1B38    0                                                
JRNL        AUTH   N.R.BROWN,M.E.NOBLE,A.M.LAWRIE,M.C.MORRIS,P.TUNNAH,          
JRNL        AUTH 2 G.DIVITA,L.N.JOHNSON,J.A.ENDICOTT                            
JRNL        TITL   EFFECTS OF PHOSPHORYLATION OF THREONINE 160 ON               
JRNL        TITL 2 CYCLIN-DEPENDENT KINASE 2 STRUCTURE AND ACTIVITY.            
JRNL        REF    J.BIOL.CHEM.                  V. 274  8746 1999              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   10085115                                                     
JRNL        DOI    10.1074/JBC.274.13.8746                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   U.SCHULZE-GAHMEN,J.BRANDSEN,H.D.JONES,D.O.MORGAN,            
REMARK   1  AUTH 2 L.MEIJER,J.VESELY,S.H.KIM                                    
REMARK   1  TITL   MULTIPLE MODES OF LIGAND RECOGNITION: CRYSTAL                
REMARK   1  TITL 2 STRUCTURES OF CYCLIN-DEPENDENT PROTEIN KINASE 2 IN           
REMARK   1  TITL 3 COMPLEX WITH ATP AND TWO INHIBITORS, OLOMOUCINE              
REMARK   1  TITL 4 AND ISOPENTENYLADENINE                                       
REMARK   1  REF    PROTEINS                      V.  22   378 1995              
REMARK   1  REFN                   ISSN 0887-3585                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 19547                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE-R                          
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM 10%                      
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2338                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 206                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.016 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.042 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.046 ; 0.050               
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) : 0.144 ; 0.150               
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 1B38 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB008203.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAY-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.5                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18076                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.09200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.260                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: UNPUBLISHED                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 10 MG/ML IN 10MM HEPES/       
REMARK 280  HCL PH7.4, 15MM NACL WELL BUFFER CONTAINING 50MM AMMONIUM           
REMARK 280  ACETATE, 12% PEG 3350, 100MM HEPES/HCL PH 7.4                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.66650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.09500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.56100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.09500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.66650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.56100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A    36                                                      
REMARK 465     LEU A    37                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     THR A    41                                                      
REMARK 465     GLU A    42                                                      
REMARK 465     GLY A    43                                                      
REMARK 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   OH   TYR A    15     O    GLY A   153              2.18            
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    HOH A   431     O    HOH A   489     2564     2.13            
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    ARG A  22   NH1 -  CZ  -  NH2 ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ARG A  22   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A  22   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ILE A  35   CA  -  C   -  O   ANGL. DEV. = -13.1 DEGREES          
REMARK 500    ASP A  86   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    TYR A 168   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    GLU A 172   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    TYR A 179   CB  -  CG  -  CD2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 199   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG A 199   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.7 DEGREES          
REMARK 500    GLU A 208   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ARG A 214   NE  -  CZ  -  NH1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG A 214   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG A 217   CD  -  NE  -  CZ  ANGL. DEV. =  27.8 DEGREES          
REMARK 500    ARG A 217   NE  -  CZ  -  NH1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    MET A 233   CA  -  CB  -  CG  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    TYR A 236   CB  -  CG  -  CD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    TYR A 236   CB  -  CG  -  CD1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG A 245   CD  -  NE  -  CZ  ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ASP A 256   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    SER A 264   N   -  CA  -  CB  ANGL. DEV. =  11.1 DEGREES          
REMARK 500    ASN A 272   OD1 -  CG  -  ND2 ANGL. DEV. =  15.2 DEGREES          
REMARK 500    HIS A 295   CA  -  CB  -  CG  ANGL. DEV. =  12.8 DEGREES          
REMARK 500    ARG A 297   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 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    LYS A  24        9.33    -62.27                                   
REMARK 500    LEU A  25      -43.27   -143.99                                   
REMARK 500    GLU A  73       53.28     29.35                                   
REMARK 500    ARG A 126      -20.78     89.85                                   
REMARK 500    HIS A 161       -4.68     62.34                                   
REMARK 500    SER A 181     -169.37   -102.31                                   
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, 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    GLU A 138         11.09                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 382  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 132   OD1                                                    
REMARK 620 2 ASP A 145   OD2 100.5                                              
REMARK 620 3 ATP A 381   O2G  96.2  91.5                                        
REMARK 620 4 ATP A 381   O2A 172.9  84.4  88.7                                  
REMARK 620 5 HOH A 412   O    86.0  92.9 174.6  88.6                            
REMARK 620 6 ATP A 381   O1B  89.1 169.6  83.5  86.3  91.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 382                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 381                 
DBREF  1B38 A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
SEQRES   1 A  299  ACE MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU          
SEQRES   2 A  299  GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU          
SEQRES   3 A  299  THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP          
SEQRES   4 A  299  THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU          
SEQRES   5 A  299  ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL          
SEQRES   6 A  299  LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR          
SEQRES   7 A  299  LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE          
SEQRES   8 A  299  MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU          
SEQRES   9 A  299  ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA          
SEQRES  10 A  299  PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS          
SEQRES  11 A  299  PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS          
SEQRES  12 A  299  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO          
SEQRES  13 A  299  VAL ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR          
SEQRES  14 A  299  ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER          
SEQRES  15 A  299  THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA          
SEQRES  16 A  299  GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER          
SEQRES  17 A  299  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY          
SEQRES  18 A  299  THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET          
SEQRES  19 A  299  PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN          
SEQRES  20 A  299  ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY          
SEQRES  21 A  299  ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN          
SEQRES  22 A  299  LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE          
SEQRES  23 A  299  PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU          
HET    ACE  A   0       3                                                       
HET     MG  A 382       1                                                       
HET    ATP  A 381      31                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   1  ACE    C2 H4 O                                                      
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  ATP    C10 H16 N5 O13 P3                                            
FORMUL   4  HOH   *206(H2 O)                                                    
HELIX    1   1 SER A   46  GLU A   57  1                                  12    
HELIX    2   2 LEU A   87  ALA A   93  1                                   7    
HELIX    3   3 LEU A  101  SER A  120  1                                  20    
HELIX    4   4 PRO A  130  ASN A  132  5                                   3    
HELIX    5   5 LEU A  148  PHE A  152  1                                   5    
HELIX    6   6 PRO A  171  LEU A  174  1                                   4    
HELIX    7   7 THR A  182  THR A  198  5                                  17    
HELIX    8   8 GLU A  208  LEU A  219  1                                  12    
HELIX    9   9 VAL A  230  SER A  232  5                                   3    
HELIX   10  10 PHE A  248  VAL A  251  1                                   4    
HELIX   11  11 GLU A  257  MET A  266  1                                  10    
HELIX   12  12 ALA A  277  ALA A  282  1                                   6    
HELIX   13  13 PRO A  284  PHE A  286  5                                   3    
SHEET    1   A 5 LEU A  66  THR A  72  0                                        
SHEET    2   A 5 LYS A  75  GLU A  81 -1  N  VAL A  79   O  LEU A  67           
SHEET    3   A 5 VAL A  29  ILE A  35 -1  N  ILE A  35   O  LEU A  76           
SHEET    4   A 5 VAL A  17  ASN A  23 -1  N  ALA A  21   O  VAL A  30           
SHEET    5   A 5 PHE A   4  LYS A   9 -1  N  GLU A   8   O  LYS A  20           
SHEET    1   B 2 LEU A 133  ILE A 135  0                                        
SHEET    2   B 2 ILE A 141  LEU A 143 -1  N  LYS A 142   O  LEU A 134           
LINK         C   ACE A   0                 N   MET A   1     1555   1555  1.33  
LINK        MG    MG A 382                 OD1 ASN A 132     1555   1555  2.12  
LINK        MG    MG A 382                 OD2 ASP A 145     1555   1555  2.02  
LINK        MG    MG A 382                 O2G ATP A 381     1555   1555  2.16  
LINK        MG    MG A 382                 O2A ATP A 381     1555   1555  2.12  
LINK        MG    MG A 382                 O   HOH A 412     1555   1555  2.09  
LINK        MG    MG A 382                 O1B ATP A 381     1555   1555  2.13  
SITE     1 AC1  4 ASN A 132  ASP A 145  ATP A 381  HOH A 412                    
SITE     1 AC2 25 ILE A  10  GLU A  12  GLY A  13  THR A  14                    
SITE     2 AC2 25 GLY A  16  VAL A  18  ALA A  31  LYS A  33                    
SITE     3 AC2 25 VAL A  64  PHE A  80  GLU A  81  PHE A  82                    
SITE     4 AC2 25 LEU A  83  ASP A  86  ASP A 127  LYS A 129                    
SITE     5 AC2 25 GLN A 131  ASN A 132  LEU A 134  ASP A 145                    
SITE     6 AC2 25  MG A 382  HOH A 412  HOH A 414  HOH A 580                    
SITE     7 AC2 25 HOH A 585                                                     
CRYST1   53.333   71.122   72.190  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018750  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014060  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013852        0.00000                         
HETATM    1  C   ACE A   0     -13.948  32.824  -3.419  1.00 48.44           C  
HETATM    2  O   ACE A   0     -12.734  33.456  -3.978  1.00 46.48           O  
HETATM    3  CH3 ACE A   0     -15.034  33.432  -3.317  1.00 51.81           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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