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Database: PDB
Entry: 5FP6
LinkDB: 5FP6
Original site: 5FP6 
HEADER    TRANSFERASE                             27-NOV-15   5FP6              
TITLE     STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 WITH SMALL-MOLECULE            
TITLE    2 LIGAND 3-(4,7-DICHLORO-1H-INDOL-3-YL)PROP-2-YN-1-OL (AT17833)        
TITLE    3 IN AN ALTERNATE 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   2   13-JAN-16 5FP6    1       JRNL                                     
REVDAT   1   23-DEC-15 5FP6    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 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         
REMARK   1  TITL 5 DESIGN.                                                      
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.    1.85 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,WOMACK;       
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.29                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.28                          
REMARK   3   NUMBER OF REFLECTIONS             : 23282                          
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)  : 0.2086                         
REMARK   3   R VALUE            (WORKING SET)  : 0.2070                         
REMARK   3   FREE R VALUE                      : 0.2403                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.91                           
REMARK   3   FREE R VALUE TEST SET COUNT       : 1142                           
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               : 12                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.85                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.93                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 65.51                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 1936                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2568                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 1850                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2540                   
REMARK   3   BIN FREE R VALUE                        : 0.3147                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.44                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 86                       
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            : 2177                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 337                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.83                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.9128                                               
REMARK   3    B22 (A**2) : -4.6795                                              
REMARK   3    B33 (A**2) : 2.7667                                               
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) : 0.264               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.195               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.159               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.172               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.150               
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      : 0.9397                        
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.9269                        
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              :   2279 ;   2.00 ;  HARMONIC           
REMARK   3    BOND ANGLES               :   3109 ;   2.00 ;  HARMONIC           
REMARK   3    TORSION ANGLES            :    747 ;   2.00 ;  SINUSOIDAL         
REMARK   3    TRIGONAL CARBON PLANES    :     44 ;   2.00 ;  HARMONIC           
REMARK   3    GENERAL PLANES            :    342 ;  16.00 ;  HARMONIC           
REMARK   3    ISOTROPIC THERMAL FACTORS :   2279 ;  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   :    294 ;   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   :   2965 ;   4.00 ;  SEMIHARMONIC       
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.012                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.65                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 5.72                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.51                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS.                                                        
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|1  - A|83  }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   17.6028    2.1880   64.7304           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0765 T22:    0.0627                                    
REMARK   3     T33:   -0.0007 T12:    0.0129                                    
REMARK   3     T13:   -0.0040 T23:    0.0479                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.5958 L22:    0.0291                                    
REMARK   3     L33:    0.3914 L12:    0.1152                                    
REMARK   3     L13:   -0.2220 L23:    0.3593                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0037 S12:   -0.0229 S13:    0.0090                     
REMARK   3     S21:   -0.0103 S22:   -0.0099 S23:    0.0406                     
REMARK   3     S31:   -0.0024 S32:   -0.0254 S33:    0.0136                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|130  - A|164  }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   31.9230    2.5875   57.7899           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0071 T22:    0.0198                                    
REMARK   3     T33:   -0.0271 T12:    0.0294                                    
REMARK   3     T13:    0.0037 T23:    0.0546                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3218 L22:    0.0000                                    
REMARK   3     L33:    0.6546 L12:    0.2024                                    
REMARK   3     L13:   -0.7171 L23:   -0.1970                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0033 S12:   -0.0201 S13:    0.0047                     
REMARK   3     S21:    0.0133 S22:   -0.0049 S23:    0.0074                     
REMARK   3     S31:   -0.0084 S32:    0.0068 S33:    0.0016                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { A|84  - A|129  A|165  - A|294  }                     
REMARK   3    ORIGIN FOR THE GROUP (A):   33.4831    6.6684   41.8204           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0484 T22:   -0.0213                                    
REMARK   3     T33:   -0.0371 T12:    0.0063                                    
REMARK   3     T13:    0.0047 T23:    0.0061                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0165 L22:    0.4794                                    
REMARK   3     L33:    1.2655 L12:   -0.1503                                    
REMARK   3     L13:    0.3251 L23:   -0.0809                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0078 S12:    0.0180 S13:    0.0202                     
REMARK   3     S21:    0.0039 S22:   -0.0137 S23:    0.0096                     
REMARK   3     S31:   -0.0522 S32:    0.0531 S33:    0.0058                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.    
REMARK   3    ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY                        
REMARK   4                                                                      
REMARK   4 5FP6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-DEC-15.                  
REMARK 100 THE PDBE ID CODE IS EBI-65636.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DSTARTREK 9.7                      
REMARK 200  DATA SCALING SOFTWARE          : DTSCALE                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24694                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.85                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.30                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.7                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY                : 0                                  
REMARK 200  R MERGE                    (I) : 0.04                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.20                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 63.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.00                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CSEARCH                                               
REMARK 200 STARTING MODEL: PDB ENTRY 5FP5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN CONCENTRATION: 13.6              
REMARK 280  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       26.95850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.09900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.10700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.09900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.95850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.10700            
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     LEU A   148                                                      
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     HIS A   295                                                      
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     MET A   1    CE                                                  
REMARK 470     LYS A   6    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     ARG A  36    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A  40    CD   OE1  OE2                                       
REMARK 470     ARG A  50    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASN A  59    CG   OD1  ND2                                       
REMARK 470     LYS A  65    CE   NZ                                             
REMARK 470     LYS A  88    CD   CE   NZ                                        
REMARK 470     LYS A  89    CD   CE   NZ                                        
REMARK 470     LEU A  96    CD1  CD2                                            
REMARK 470     ARG A 122    CD   NE   CZ   NH1  NH2                             
REMARK 470     VAL A 164    CG1  CG2                                            
REMARK 470     LYS A 178    CD   CE   NZ                                        
REMARK 470     LYS A 242    NZ                                                  
REMARK 470     ASP A 247    CG   OD1  OD2                                       
REMARK 470     LYS A 278    CD   CE   NZ                                        
REMARK 470     GLN A 287    CD   OE1  NE2                                       
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    ARG A 122       47.15     38.71                                   
REMARK 500    ARG A 126      -20.61     83.61                                   
REMARK 500    ASP A 127       47.24   -142.94                                   
REMARK 500    TYR A 179       53.72   -114.27                                   
REMARK 500    PRO A 254       35.91    -99.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 3-(4,7-DICHLORO-1H-INDOL-3-YL)PROP-2-YN-1-OL (MFZ): ASTEX            
REMARK 600  COMPOUND REGISTRY AT17833                                           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MFZ A1295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MFZ A1296                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5FP5   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 WITH SMALL-                  
REMARK 900  MOLECULE LIGAND 4-FLUOROBENZOIC ACID (AT222) IN AN                  
REMARK 900  ALTERNATE BINDING SITE.                                             
REMARK 900 RELATED ID: 5FPD   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HEAT SHOCK-RELATED 70KDA PROTEIN 2 WITH                
REMARK 900  SMALL-MOLECULE LIGAND PYRAZINE-2-CARBOXAMIDE (AT513) IN             
REMARK 900   AN ALTERNATE BINDING SITE.                                         
REMARK 900 RELATED ID: 5FPE   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HEAT SHOCK-RELATED 70KDA PROTEIN 2 WITH                
REMARK 900  SMALL-MOLECULE LIGAND 1H-1,2,4-TRIAZOL-3-AMINE (                    
REMARK 900  AT485) IN AN ALTERNATE BINDING SITE.                                
REMARK 900 RELATED ID: 5FPM   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HEAT SHOCK-RELATED 70KDA PROTEIN 2 WITH                
REMARK 900  SMALL-MOLECULE LIGAND 5-PHENYL-1,3,4-OXADIAZOLE-2-                  
REMARK 900  THIOL (AT809) IN AN ALTERNATE BINDING SITE.                         
REMARK 900 RELATED ID: 5FPN   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HEAT SHOCK-RELATED 70KDA PROTEIN 2 WITH                
REMARK 900  SMALL-MOLECULE LIGAND 3,5-DIMETHYL-1H-PYRAZOLE-4-                   
REMARK 900  CARBOXYLIC ACID (AT9084) IN AN ALTERNATE BINDING SITE.              
REMARK 900 RELATED ID: 5FPO   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF BACTERIAL DNA LIGASE WITH SMALL-MOLECULE               
REMARK 900  LIGAND 1H-INDAZOL-7-AMINE (AT4213) IN AN ALTERNATE                  
REMARK 900  BINDING SITE.                                                       
REMARK 900 RELATED ID: 5FPR   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF BACTERIAL DNA LIGASE WITH SMALL-MOLECULE               
REMARK 900  LIGAND PYRIMIDIN-2-AMINE (AT371) IN AN ALTERNATE                    
REMARK 900  BINDING SITE.                                                       
REMARK 900 RELATED ID: 5FPS   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HEPATITIS C VIRUS (HCV) FULL-LENGTH NS3                
REMARK 900  COMPLEX WITH SMALL-MOLECULE LIGAND 3-AMINOBENZENE-1,2               
REMARK 900  -DICARBOXYLIC ACID (AT1246) IN AN ALTERNATE BINDING                 
REMARK 900  SITE.                                                               
REMARK 900 RELATED ID: 5FPT   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HEPATITIS C VIRUS (HCV) FULL-LENGTH NS3                
REMARK 900  COMPLEX WITH SMALL-MOLECULE LIGAND 2-(1-METHYL-1H-                  
REMARK 900  INDOL-3-YL)ACETIC ACID (AT3437) IN AN ALTERNATE                     
REMARK 900  BINDING SITE.                                                       
REMARK 900 RELATED ID: 5FPY   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HEPATITIS C VIRUS (HCV) FULL-LENGTH NS3                
REMARK 900  COMPLEX WITH SMALL-MOLECULE LIGAND 5-BROMO-1-METHYL-                
REMARK 900  1H-INDOLE-2-CARBOXYLIC ACID (AT21457) IN AN ALTERNATE               
REMARK 900   BINDING SITE.                                                      
DBREF  5FP6 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    MFZ  A1295      22                                                       
HET    MFZ  A1296      22                                                       
HETNAM     MFZ 3-(4,7-DICHLORO-1H-INDOL-3-YL)PROP-2-YN-1-OL                     
FORMUL   3  MFZ    2(C11 H7 CL2 N O)                                            
FORMUL   4  HOH   *337(H2 O)                                                    
HELIX    1   1 ASP A   38  VAL A   44  1                                   7    
HELIX    2   2 PRO A   45  LEU A   58  1                                  14    
HELIX    3   3 LEU A   87  SER A   94  1                                   8    
HELIX    4   4 PRO A  100  HIS A  121  1                                  22    
HELIX    5   5 LYS A  129  GLN A  131  5                                   3    
HELIX    6   6 ALA A  170  LEU A  175  1                                   6    
HELIX    7   7 THR A  182  ARG A  199  1                                  18    
HELIX    8   8 SER A  207  GLY A  220  1                                  14    
HELIX    9   9 GLY A  229  MET A  233  5                                   5    
HELIX   10  10 ASP A  247  VAL A  252  1                                   6    
HELIX   11  11 ASP A  256  LEU A  267  1                                  12    
HELIX   12  12 SER A  276  ALA A  282  1                                   7    
HELIX   13  13 HIS A  283  GLN A  287  5                                   5    
SHEET    1  AA 5 PHE A   4  GLU A  12  0                                        
SHEET    2  AA 5 GLY A  16  ASN A  23 -1  O  VAL A  18   N  ILE A  10           
SHEET    3  AA 5 VAL A  29  ARG A  36 -1  O  VAL A  30   N  ALA A  21           
SHEET    4  AA 5 LYS A  75  GLU A  81 -1  O  LEU A  76   N  ILE A  35           
SHEET    5  AA 5 LEU A  66  THR A  72 -1  N  LEU A  67   O  VAL A  79           
SHEET    1  AB 3 GLN A  85  ASP A  86  0                                        
SHEET    2  AB 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3  AB 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
CISPEP   1 PRO A  253    PRO A  254          0        -1.58                     
SITE     1 AC1 11 ILE A  10  GLY A  13  VAL A  18  ALA A  31                    
SITE     2 AC1 11 GLU A  81  PHE A  82  LEU A  83  LEU A 134                    
SITE     3 AC1 11 ASP A 145  HOH A2021  HOH A2123                               
SITE     1 AC2  7 PRO A  45  ILE A  49  HIS A  71  LEU A  76                    
SITE     2 AC2  7 PRO A 228  GLY A 229  HOH A2085                               
CRYST1   53.917   72.214   72.198  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      0.018547  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013848  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013851        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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