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Database: PDB
Entry: 5L2W
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Original site: 5L2W 
HEADER    TRANSFERASE/CELL CYCLE/INHIBITOR        02-AUG-16   5L2W              
TITLE     THE X-RAY CO-CRYSTAL STRUCTURE OF HUMAN CDK2/CYCLINE AND DINACICLIB.  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CELL DIVISION PROTEIN KINASE 2,P33 PROTEIN KINASE;          
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: G1/S-SPECIFIC CYCLIN-E1;                                   
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: UNP RESIDUES 81-363;                                       
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK2, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: CCNE1, CCNE;                                                   
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CYCLIN-DEPENDENT KINASE, KINASE INHIBITOR, KINASE SELECTIVITY,        
KEYWDS   2 TRANSFERASE-CELL CYCLE-INHIBITOR COMPLEX                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.CHEN,R.A.FERRE,W.DEIHL,X.YU,Y.-A.HE                                 
REVDAT   2   19-OCT-16 5L2W    1       JRNL                                     
REVDAT   1   24-AUG-16 5L2W    0                                                
JRNL        AUTH   P.CHEN,N.V.LEE,W.HU,M.XU,R.A.FERRE,H.LAM,S.BERGQVIST,        
JRNL        AUTH 2 J.SOLOWIEJ,W.DIEHL,Y.A.HE,X.YU,A.NAGATA,T.VANARSDALE,        
JRNL        AUTH 3 B.W.MURRAY                                                   
JRNL        TITL   SPECTRUM AND DEGREE OF CDK DRUG INTERACTIONS PREDICTS        
JRNL        TITL 2 CLINICAL PERFORMANCE.                                        
JRNL        REF    MOL.CANCER THER.              V.  15  2273 2016              
JRNL        REFN                   ESSN 1538-8514                               
JRNL        PMID   27496135                                                     
JRNL        DOI    10.1158/1535-7163.MCT-16-0300                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.4                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 19741                          
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)  : 0.202                          
REMARK   3   R VALUE            (WORKING SET)  : 0.200                          
REMARK   3   FREE R VALUE                      : 0.246                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.870                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 962                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 10                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.80                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.95                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.99                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2828                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2501                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2699                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2450                   
REMARK   3   BIN FREE R VALUE                        : 0.3483                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.56                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 129                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4617                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 75                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 100.2                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 84.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.10780                                             
REMARK   3    B22 (A**2) : -6.10780                                             
REMARK   3    B33 (A**2) : 12.21560                                             
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.378               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 2.166               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.335               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 1.334               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.337               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4774   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 6482   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1661   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 109    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 693    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4774   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 604    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 5661   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.15                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.72                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.34                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5L2W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000223112.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-NOV-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 98.15                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19770                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 12.76                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: BUSTER                                                
REMARK 200 STARTING MODEL: 1W98                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG20K, 180MM MG(HCO2)2, 0.1M MES PH     
REMARK 280  6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 286.15K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       75.92850            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       50.15350            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       50.15350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       37.96425            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       50.15350            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       50.15350            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      113.89275            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       50.15350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.15350            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       37.96425            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       50.15350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.15350            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      113.89275            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       75.92850            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU A   298                                                      
REMARK 465     MET B    57                                                      
REMARK 465     ALA B    58                                                      
REMARK 465     SER B    59                                                      
REMARK 465     HIS B    60                                                      
REMARK 465     HIS B    61                                                      
REMARK 465     HIS B    62                                                      
REMARK 465     HIS B    63                                                      
REMARK 465     HIS B    64                                                      
REMARK 465     HIS B    65                                                      
REMARK 465     ASP B    66                                                      
REMARK 465     TYR B    67                                                      
REMARK 465     ASP B    68                                                      
REMARK 465     GLY B    69                                                      
REMARK 465     ALA B    70                                                      
REMARK 465     THR B    71                                                      
REMARK 465     THR B    72                                                      
REMARK 465     GLU B    73                                                      
REMARK 465     ASN B    74                                                      
REMARK 465     LEU B    75                                                      
REMARK 465     TYR B    76                                                      
REMARK 465     PHE B    77                                                      
REMARK 465     GLN B    78                                                      
REMARK 465     GLY B    79                                                      
REMARK 465     SER B    80                                                      
REMARK 465     ILE B    81                                                      
REMARK 465     ILE B    82                                                      
REMARK 465     ALA B    83                                                      
REMARK 465     PRO B    84                                                      
REMARK 465     SER B    85                                                      
REMARK 465     ARG B    86                                                      
REMARK 465     GLY B    87                                                      
REMARK 465     ALA B   358                                                      
REMARK 465     ARG B   359                                                      
REMARK 465     ALA B   360                                                      
REMARK 465     LYS B   361                                                      
REMARK 465     LYS B   362                                                      
REMARK 465     ALA B   363                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  12      -64.47   -108.67                                   
REMARK 500    THR A  72       53.30   -113.36                                   
REMARK 500    GLU A  73       33.91     34.86                                   
REMARK 500    ASN A  74      -30.62   -171.45                                   
REMARK 500    ARG A 126       15.83     59.18                                   
REMARK 500    ASP A 127       52.89   -158.99                                   
REMARK 500    ASP A 145       87.67     50.27                                   
REMARK 500    GLU A 162       70.75    -69.45                                   
REMARK 500    SER A 181     -147.78   -152.57                                   
REMARK 500    ASP A 288      -60.23    -91.90                                   
REMARK 500    HIS B 117       45.96   -106.64                                   
REMARK 500    GLU B 166      -68.88   -106.16                                   
REMARK 500    SER B 227       59.98   -115.04                                   
REMARK 500    TYR B 243       74.00   -109.30                                   
REMARK 500    HIS B 248       69.55    -66.19                                   
REMARK 500    VAL B 274        1.32    -60.23                                   
REMARK 500    SER B 293     -114.20   -121.58                                   
REMARK 500    ASP B 350       37.04    -71.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1042        DISTANCE =  6.91 ANGSTROMS                       
REMARK 525    HOH B 431        DISTANCE =  7.26 ANGSTROMS                       
REMARK 525    HOH B 432        DISTANCE = 10.47 ANGSTROMS                       
REMARK 525    HOH B 433        DISTANCE = 13.83 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1QK A 900                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 901                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5L2T   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5L2S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5L2I   RELATED DB: PDB                                   
DBREF  5L2W A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  5L2W B   81   363  UNP    P24864   CCNE1_HUMAN     81    363             
SEQADV 5L2W SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 5L2W MET B   57  UNP  P24864              INITIATING METHIONINE          
SEQADV 5L2W ALA B   58  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W SER B   59  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W HIS B   60  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W HIS B   61  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W HIS B   62  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W HIS B   63  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W HIS B   64  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W HIS B   65  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W ASP B   66  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W TYR B   67  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W ASP B   68  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W GLY B   69  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W ALA B   70  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W THR B   71  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W THR B   72  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W GLU B   73  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W ASN B   74  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W LEU B   75  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W TYR B   76  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W PHE B   77  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W GLN B   78  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W GLY B   79  UNP  P24864              EXPRESSION TAG                 
SEQADV 5L2W SER B   80  UNP  P24864              EXPRESSION TAG                 
SEQRES   1 A  299  SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU          
SEQRES   2 A  299  GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU          
SEQRES   3 A  299  THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP          
SEQRES   4 A  299  THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU          
SEQRES   5 A  299  ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL          
SEQRES   6 A  299  LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR          
SEQRES   7 A  299  LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE          
SEQRES   8 A  299  MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU          
SEQRES   9 A  299  ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA          
SEQRES  10 A  299  PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS          
SEQRES  11 A  299  PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS          
SEQRES  12 A  299  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO          
SEQRES  13 A  299  VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR          
SEQRES  14 A  299  ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER          
SEQRES  15 A  299  THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA          
SEQRES  16 A  299  GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER          
SEQRES  17 A  299  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY          
SEQRES  18 A  299  THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET          
SEQRES  19 A  299  PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN          
SEQRES  20 A  299  ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY          
SEQRES  21 A  299  ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN          
SEQRES  22 A  299  LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE          
SEQRES  23 A  299  PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU          
SEQRES   1 B  307  MET ALA SER HIS HIS HIS HIS HIS HIS ASP TYR ASP GLY          
SEQRES   2 B  307  ALA THR THR GLU ASN LEU TYR PHE GLN GLY SER ILE ILE          
SEQRES   3 B  307  ALA PRO SER ARG GLY SER PRO LEU PRO VAL LEU SER TRP          
SEQRES   4 B  307  ALA ASN ARG GLU GLU VAL TRP LYS ILE MET LEU ASN LYS          
SEQRES   5 B  307  GLU LYS THR TYR LEU ARG ASP GLN HIS PHE LEU GLU GLN          
SEQRES   6 B  307  HIS PRO LEU LEU GLN PRO LYS MET ARG ALA ILE LEU LEU          
SEQRES   7 B  307  ASP TRP LEU MET GLU VAL CYS GLU VAL TYR LYS LEU HIS          
SEQRES   8 B  307  ARG GLU THR PHE TYR LEU ALA GLN ASP PHE PHE ASP ARG          
SEQRES   9 B  307  TYR MET ALA THR GLN GLU ASN VAL VAL LYS THR LEU LEU          
SEQRES  10 B  307  GLN LEU ILE GLY ILE SER SER LEU PHE ILE ALA ALA LYS          
SEQRES  11 B  307  LEU GLU GLU ILE TYR PRO PRO LYS LEU HIS GLN PHE ALA          
SEQRES  12 B  307  TYR VAL THR ASP GLY ALA CYS SER GLY ASP GLU ILE LEU          
SEQRES  13 B  307  THR MET GLU LEU MET ILE MET LYS ALA LEU LYS TRP ARG          
SEQRES  14 B  307  LEU SER PRO LEU THR ILE VAL SER TRP LEU ASN VAL TYR          
SEQRES  15 B  307  MET GLN VAL ALA TYR LEU ASN ASP LEU HIS GLU VAL LEU          
SEQRES  16 B  307  LEU PRO GLN TYR PRO GLN GLN ILE PHE ILE GLN ILE ALA          
SEQRES  17 B  307  GLU LEU LEU ASP LEU CYS VAL LEU ASP VAL ASP CYS LEU          
SEQRES  18 B  307  GLU PHE PRO TYR GLY ILE LEU ALA ALA SER ALA LEU TYR          
SEQRES  19 B  307  HIS PHE SER SER SER GLU LEU MET GLN LYS VAL SER GLY          
SEQRES  20 B  307  TYR GLN TRP CYS ASP ILE GLU ASN CYS VAL LYS TRP MET          
SEQRES  21 B  307  VAL PRO PHE ALA MET VAL ILE ARG GLU THR GLY SER SER          
SEQRES  22 B  307  LYS LEU LYS HIS PHE ARG GLY VAL ALA ASP GLU ASP ALA          
SEQRES  23 B  307  HIS ASN ILE GLN THR HIS ARG ASP SER LEU ASP LEU LEU          
SEQRES  24 B  307  ASP LYS ALA ARG ALA LYS LYS ALA                              
MODRES 5L2W TPO A  160  THR  MODIFIED RESIDUE                                   
HET    TPO  A 160      11                                                       
HET    1QK  A 900      29                                                       
HET    GOL  A 901       6                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     1QK 3-[({3-ETHYL-5-[(2S)-2-(2-HYDROXYETHYL)PIPERIDIN-1-              
HETNAM   2 1QK  YL]PYRAZOLO[1,5-A]PYRIMIDIN-7-YL}AMINO)METHYL]-1-               
HETNAM   3 1QK  HYDROXYPYRIDINIUM                                               
HETNAM     GOL GLYCEROL                                                         
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     1QK DINACICLIB                                                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   3  1QK    C21 H29 N6 O2 1+                                             
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   5  HOH   *75(H2 O)                                                     
HELIX    1 AA1 PRO A   45  LYS A   56  1                                  12    
HELIX    2 AA2 LEU A   87  SER A   94  1                                   8    
HELIX    3 AA3 PRO A  100  HIS A  121  1                                  22    
HELIX    4 AA4 LYS A  129  GLN A  131  5                                   3    
HELIX    5 AA5 THR A  165  ARG A  169  5                                   5    
HELIX    6 AA6 ALA A  170  LEU A  175  1                                   6    
HELIX    7 AA7 THR A  182  ARG A  199  1                                  18    
HELIX    8 AA8 SER A  207  GLY A  220  1                                  14    
HELIX    9 AA9 GLY A  229  MET A  233  5                                   5    
HELIX   10 AB1 ASP A  247  VAL A  252  1                                   6    
HELIX   11 AB2 ASP A  256  LEU A  267  1                                  12    
HELIX   12 AB3 SER A  276  ALA A  282  1                                   7    
HELIX   13 AB4 HIS A  283  GLN A  287  5                                   5    
HELIX   14 AB5 ASN B   97  TYR B  112  1                                  16    
HELIX   15 AB6 GLN B  126  TYR B  144  1                                  19    
HELIX   16 AB7 HIS B  147  ALA B  163  1                                  17    
HELIX   17 AB8 THR B  171  GLU B  189  1                                  19    
HELIX   18 AB9 LYS B  194  VAL B  201  1                                   8    
HELIX   19 AC1 SER B  207  LEU B  222  1                                  16    
HELIX   20 AC2 THR B  230  TYR B  243  1                                  14    
HELIX   21 AC3 PRO B  256  LEU B  272  1                                  17    
HELIX   22 AC4 ASP B  275  PHE B  279  5                                   5    
HELIX   23 AC5 PRO B  280  SER B  293  1                                  14    
HELIX   24 AC6 SER B  294  GLY B  303  1                                  10    
HELIX   25 AC7 GLN B  305  GLY B  327  1                                  23    
HELIX   26 AC8 ALA B  338  ILE B  345  5                                   8    
HELIX   27 AC9 ASP B  350  ASP B  356  1                                   7    
SHEET    1 AA1 5 PHE A   4  GLY A  11  0                                        
SHEET    2 AA1 5 VAL A  17  ASN A  23 -1  O  LYS A  20   N  VAL A   7           
SHEET    3 AA1 5 VAL A  29  ARG A  36 -1  O  LEU A  32   N  TYR A  19           
SHEET    4 AA1 5 LYS A  75  GLU A  81 -1  O  PHE A  80   N  ALA A  31           
SHEET    5 AA1 5 LEU A  66  HIS A  71 -1  N  ILE A  70   O  TYR A  77           
SHEET    1 AA2 3 GLN A  85  ASP A  86  0                                        
SHEET    2 AA2 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3 AA2 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1 AA3 2 VAL A 123  LEU A 124  0                                        
SHEET    2 AA3 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.36  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.35  
CISPEP   1 VAL A  154    PRO A  155          0         5.85                     
SITE     1 AC1 11 ILE A  10  ALA A  31  PHE A  80  GLU A  81                    
SITE     2 AC1 11 PHE A  82  LEU A  83  HIS A  84  GLN A  85                    
SITE     3 AC1 11 LYS A  89  LEU A 134  ALA A 144                               
SITE     1 AC2  4 HIS A  84  TYR A 107  ASN A 136  GLY A 139                    
CRYST1  100.307  100.307  151.857  90.00  90.00  90.00 P 41 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      0.009969  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009969  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006585        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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