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Database: PDB
Entry: 5FP5
LinkDB: 5FP5
Original site: 5FP5 
HEADER    TRANSFERASE                             27-NOV-15   5FP5              
TITLE     STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 WITH SMALL-MOLECULE            
TITLE    2 LIGAND 4-FLUOROBENZOIC ACID (AT222) IN AN ALTERNATE                  
TITLE    3 BINDING SITE.                                                        
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                                                      
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_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1                                 
KEYWDS    TRANSFERASE, KINASE, MITOSIS, CELL CYCLE, FRAGMENT SCREENING,         
KEYWDS   2 ALTERNATE BINDING SITE.                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.JHOTI,R.F.LUDLOW,M.O'REILLY,H.K.SAINI,I.J.TICKLE, M.VERDONK         
REVDAT   3   13-JAN-16 5FP5    1       JRNL   REMARK                            
REVDAT   2   23-DEC-15 5FP5    1       JRNL                                     
REVDAT   1   09-DEC-15 5FP5    0                                                
JRNL        AUTH   R.F.LUDLOW,M.L.VERDONK,H.K.SAINI,I.J.TICKLE,H.JHOTI          
JRNL        TITL   DETECTION OF SECONDARY BINDING SITES IN PROTEINS USING       
JRNL        TITL 2 FRAGMENT SCREENING.                                          
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 112 15910 2015              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   26655740                                                     
JRNL        DOI    10.1073/PNAS.1518946112                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.G.WYATT,A.J.WOODHEAD,V.BERDINI,J.A.BOULSTRIDGE,M.G.CARR,   
REMARK   1  AUTH 2 D.M.CROSS,D.J.DAVIS,L.A.DEVINE,T.R.EARLY,R.E.FELTELL,        
REMARK   1  AUTH 3 E.J.LEWIS,R.L.MCMENAMIN,E.F.NAVARRO,M.A.O'BRIEN,M.O'REILLY,  
REMARK   1  AUTH 4 M.REULE,G.SAXTY,L.C.A.SEAVERS,D.SMITH,M.S.SQUIRES,           
REMARK   1  AUTH 5 G.TREWARTHA,M.T.WALKER,A.J.WOOLFORD                          
REMARK   1  TITL   IDENTIFICATION OF N-(4-PIPERIDINYL)-4-(2,6-                  
REMARK   1  TITL 2 DICHLOROBENZOYLAMINO)-1H-PYRAZOLE-3-CARBOXAMIDE (AT7519), A  
REMARK   1  TITL 3 NOVEL CYCLIN DEPENDENT KINASE INHIBITOR USING FRAGMENT-      
REMARK   1  TITL 4 BASED X-RAY CRYSTALLOGRAPHY AND STRUCTURE BASED DRUG DESIGN. 
REMARK   1  TITL 5                                                              
REMARK   1  REF    J.MED.CHEM.                   V.  51  4986 2008              
REMARK   1  REFN                   ISSN 0022-2623                               
REMARK   1  PMID   18656911                                                     
REMARK   1  DOI    10.1021/JM800382H                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.16 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.6                                        
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) : 2.16                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.12                          
REMARK   3   NUMBER OF REFLECTIONS             : 14466                          
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)  : 0.1898                         
REMARK   3   R VALUE            (WORKING SET)  : 0.1866                         
REMARK   3   FREE R VALUE                      : 0.253                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.05                           
REMARK   3   FREE R VALUE TEST SET COUNT       : 731                            
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               : 7                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.16                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.33                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 88.89                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2798                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2011                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2660                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1966                   
REMARK   3   BIN FREE R VALUE                        : 0.2883                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.93                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 138                      
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            : 2076                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 321                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.8404                                              
REMARK   3    B22 (A**2) : 2.6526                                               
REMARK   3    B33 (A**2) : -0.8121                                              
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : 0.0000                                               
REMARK   3    B23 (A**2) : 0.0000                                               
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.242               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.392               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.244               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.294               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.229               
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      : 0.9405                        
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.9067                        
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2160   ; 2.00   ; HARMONIC            
REMARK   3    BOND ANGLES               : 2934   ; 2.00   ; HARMONIC            
REMARK   3    TORSION ANGLES            : 708    ; 2.00   ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 40     ; 2.00   ; HARMONIC            
REMARK   3    GENERAL PLANES            : 328    ; 16.00  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2160   ; 20.00  ; 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   : 273    ; 5.00   ; 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   : 2776   ; 4.00   ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.011                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.04                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 5.87                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.01                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):   20.1137    1.4260   66.3227           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0667 T22:    0.0407                                    
REMARK   3     T33:    0.0060 T12:   -0.0111                                    
REMARK   3     T13:    0.0135 T23:    0.0927                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1178 L22:    0.0748                                    
REMARK   3     L33:    0.4592 L12:   -1.1947                                    
REMARK   3     L13:   -0.4848 L23:    0.6036                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0073 S12:    0.0007 S13:   -0.0082                     
REMARK   3     S21:   -0.0506 S22:    0.0338 S23:    0.0699                     
REMARK   3     S31:    0.0131 S32:   -0.0561 S33:   -0.0265                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):   31.6335    2.1913   58.0783           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0123 T22:    0.0392                                    
REMARK   3     T33:   -0.0403 T12:    0.0092                                    
REMARK   3     T13:   -0.0025 T23:    0.0764                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3762 L22:    0.0000                                    
REMARK   3     L33:    0.7724 L12:    0.2176                                    
REMARK   3     L13:   -1.2358 L23:    0.1674                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0006 S12:   -0.0309 S13:   -0.0031                     
REMARK   3     S21:    0.0079 S22:   -0.0138 S23:    0.0123                     
REMARK   3     S31:   -0.0004 S32:    0.0059 S33:    0.0132                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   33.4641    6.5356   42.2810           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0364 T22:   -0.0192                                    
REMARK   3     T33:   -0.0645 T12:    0.0078                                    
REMARK   3     T13:    0.0020 T23:   -0.0013                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1992 L22:    0.7243                                    
REMARK   3     L33:    1.3373 L12:   -0.4218                                    
REMARK   3     L13:    0.3386 L23:   -0.3421                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0050 S12:    0.0026 S13:    0.0081                     
REMARK   3     S21:    0.0255 S22:   -0.0095 S23:    0.0056                     
REMARK   3     S31:   -0.0080 S32:    0.0476 S33:    0.0046                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5FP5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-NOV-15.                  
REMARK 100 THE PDBE ID CODE IS EBI-65633.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-MAY-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
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                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
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 : DSTARTREK                          
REMARK 200  DATA SCALING SOFTWARE          : DTSCALE                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14466                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.16                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.7                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.1                               
REMARK 200  DATA REDUNDANCY                : 0                                  
REMARK 200  R MERGE                    (I) : 0.00                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1HCK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10MM HEPES/NAOH PH7.4 15MM NACL          
REMARK 280  PROTEIN CONCENTRATION: 8.6 MG/ML                                    
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       26.83850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.19100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.84900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.19100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.83850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.84900            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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     THR A    14                                                      
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 465     VAL A    44                                                      
REMARK 465     PRO A    45                                                      
REMARK 465     SER A    46                                                      
REMARK 465     GLU A    73                                                      
REMARK 465     ASN A    74                                                      
REMARK 465     LYS A    75                                                      
REMARK 465     ALA A   149                                                      
REMARK 465     ARG A   150                                                      
REMARK 465     ALA A   151                                                      
REMARK 465     PHE A   152                                                      
REMARK 465     GLY A   153                                                      
REMARK 465     VAL A   154                                                      
REMARK 465     PRO A   155                                                      
REMARK 465     VAL A   156                                                      
REMARK 465     ARG A   157                                                      
REMARK 465     THR A   158                                                      
REMARK 465     TYR A   159                                                      
REMARK 465     THR A   160                                                      
REMARK 465     HIS A   161                                                      
REMARK 465     GLU A   162                                                      
REMARK 465     VAL A   163                                                      
REMARK 465     VAL A   164                                                      
REMARK 465     LEU A   296                                                      
REMARK 465     ARG A   297                                                      
REMARK 465     LEU A   298                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A   5    CD   OE1  NE2                                       
REMARK 470     LYS A   6    CD   CE   NZ                                        
REMARK 470     LYS A   9    CE   NZ                                             
REMARK 470     GLU A  12    CD   OE1  OE2                                       
REMARK 470     LEU A  25    CG   CD1  CD2                                       
REMARK 470     LYS A  33    NZ                                                  
REMARK 470     LYS A  34    CE   NZ                                             
REMARK 470     THR A  47    CG2                                                 
REMARK 470     ILE A  49    CG2                                                 
REMARK 470     ARG A  50    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  51    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  52    CD1                                                 
REMARK 470     LYS A  88    NZ                                                  
REMARK 470     THR A  97    CG2                                                 
REMARK 470     ARG A 122    CD   NE   CZ   NH1  NH2                             
REMARK 470     LEU A 148    CB   CG   CD1  CD2                                  
REMARK 470     LYS A 178    CD   CE   NZ                                        
REMARK 470     LYS A 242    NZ                                                  
REMARK 470     GLN A 246    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 278    CE   NZ                                             
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    LEU A  58       96.77    -54.52                                   
REMARK 500    ARG A 126      -21.84     80.13                                   
REMARK 500    TYR A 179       53.43   -112.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 4-FLUOROBENZOIC ACID (L02): ASTEX COMPOUND REGISTRY AT222            
REMARK 600 4-FLUOROBENZOIC ACID (L01): ASTEX COMPOUND REGISTRY AT222            
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE A1296                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1Y6 A1297                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1Y6 A1298                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5FP6   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 WITH SMALL-                  
REMARK 900  MOLECULE LIGAND 3-(4,7-DICHLORO-1H-INDOL-3-YL)PROP                  
REMARK 900  -2-YN-1-OL (AT17833) IN AN ALTERNATE BINDING SITE.                  
DBREF  5FP5 A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
SEQRES   1 A  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 A  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 A  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 A  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 A  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 A  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 A  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 A  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 A  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 A  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 A  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 A  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 A  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 A  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 A  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 A  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 A  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 A  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 A  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 A  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 A  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 A  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 A  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
HET    ACE  A1296       3                                                       
HET    1Y6  A1297       3                                                       
HET    1Y6  A1298       3                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     1Y6 4-FLUOROBENZOIC ACID                                             
FORMUL   2  ACE    C2 H4 O                                                      
FORMUL   3  1Y6    2(C7 H5 F O2)                                                
FORMUL   5  HOH   *321(H2 O)                                                    
HELIX    1   1 THR A   47  LEU A   58  1                                  12    
HELIX    2   2 LEU A   87  SER A   94  1                                   8    
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 ALA A  170  LEU A  175  1                                   6    
HELIX    6   6 THR A  182  ARG A  199  1                                  18    
HELIX    7   7 SER A  207  GLY A  220  1                                  14    
HELIX    8   8 GLY A  229  MET A  233  5                                   5    
HELIX    9   9 ASP A  247  VAL A  252  1                                   6    
HELIX   10  10 ASP A  256  LEU A  267  1                                  12    
HELIX   11  11 SER A  276  ALA A  282  1                                   7    
HELIX   12  12 HIS A  283  GLN A  287  5                                   5    
SHEET    1  AA 5 PHE A   4  GLU A  12  0                                        
SHEET    2  AA 5 VAL A  17  ASN A  23 -1  O  VAL A  18   N  ILE A  10           
SHEET    3  AA 5 VAL A  29  LYS A  34 -1  O  VAL A  30   N  ALA A  21           
SHEET    4  AA 5 TYR A  77  GLU A  81 -1  O  LEU A  78   N  LYS A  33           
SHEET    5  AA 5 LEU A  66  ILE A  70 -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           
LINK         N   MET A   1                 C   ACE A1296     1555   1555  1.34  
CISPEP   1 PRO A  253    PRO A  254          0        -2.01                     
SITE     1 AC1  3 MET A   1  LEU A  32  TYR A  77                               
SITE     1 AC2  8 ALA A  31  LYS A  33  PHE A  80  GLU A  81                    
SITE     2 AC2  8 LEU A  83  LEU A 134  ALA A 144  ASP A 145                    
SITE     1 AC3  9 GLU A 138  VAL A 226  ARG A 245  HIS A 268                    
SITE     2 AC3  9 TYR A 269  LYS A 291  HOH A2243  HOH A2267                    
SITE     3 AC3  9 HOH A2268                                                     
CRYST1   53.677   71.698   72.382  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      0.018630  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013947  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013816        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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