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Database: PDB
Entry: 4AUA
LinkDB: 4AUA
Original site: 4AUA 
HEADER    TRANSFERASE                             15-MAY-12   4AUA              
TITLE     LIGANDED X-RAY CRYSTAL STRUCTURE OF CYCLIN DEPENDENT KINASE 6 (CDK6)  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 6;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN, RESIDUES 1-301;                             
COMPND   5 SYNONYM: CELL DIVISION PROTEIN KINASE 6, SERINE/THREONINE-PROTEIN    
COMPND   6 KINASE PLSTIRE;                                                      
COMPND   7 EC: 2.7.11.22;                                                       
COMPND   8 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                                        
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.S.CHO,H.ANGOVE,C.BRAIN,C.H.T.CHEN,R.CHENG,R.CHOPRA,K.CHUNG,         
AUTHOR   2 M.CONGREVE,C.DAGOSTIN,D.DAVIS,R.FELTELL,J.GIRALDES,S.HISCOCK,S.KIM,  
AUTHOR   3 S.KOVATS,B.LAGU,K.LEWRY,A.LOO,Y.LU,M.LUZZIO,W.MANIARA,R.MCMENAMIN,   
AUTHOR   4 P.MORTENSON,R.BENNING,M.O'REILLY,D.REES,J.SHEN,T.SMITH,Y.WANG,       
AUTHOR   5 G.WILLIAMS,A.WOOLFORD,W.WRONA,M.XU,F.YANG,S.HOWARD                   
REVDAT   4   03-APR-19 4AUA    1       REMARK                                   
REVDAT   3   07-FEB-18 4AUA    1       AUTHOR JRNL                              
REVDAT   2   18-JUN-14 4AUA    1       JRNL                                     
REVDAT   1   06-FEB-13 4AUA    0                                                
JRNL        AUTH   Y.S.CHO,H.ANGOVE,C.BRAIN,C.H.CHEN,H.CHENG,R.CHENG,R.CHOPRA,  
JRNL        AUTH 2 K.CHUNG,M.CONGREVE,C.DAGOSTIN,D.J.DAVIS,R.FELTELL,           
JRNL        AUTH 3 J.GIRALDES,S.D.HISCOCK,S.KIM,S.KOVATS,B.LAGU,K.LEWRY,A.LOO,  
JRNL        AUTH 4 Y.LU,M.LUZZIO,W.MANIARA,R.MCMENAMIN,P.N.MORTENSON,R.BENNING, 
JRNL        AUTH 5 M.O'REILLY,D.C.REES,J.SHEN,T.SMITH,Y.WANG,G.WILLIAMS,        
JRNL        AUTH 6 A.J.WOOLFORD,W.WRONA,M.XU,F.YANG,S.HOWARD                    
JRNL        TITL   FRAGMENT-BASED DISCOVERY OF 7-AZABENZIMIDAZOLES AS POTENT,   
JRNL        TITL 2 HIGHLY SELECTIVE, AND ORALLY ACTIVE CDK4/6 INHIBITORS.       
JRNL        REF    ACS MED CHEM LETT             V.   3   445 2012              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   24900493                                                     
JRNL        DOI    10.1021/ML200241A                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.31 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019G                                     
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.31                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 71.23                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 12395                          
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) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 680                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.31                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.37                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 884                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.64                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 60                           
REMARK   3   BIN FREE R VALUE                    : 0.4280                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2048                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 86                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.95                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.42000                                              
REMARK   3    B22 (A**2) : 2.42000                                              
REMARK   3    B33 (A**2) : -4.83000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.369         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.274         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.238         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.961         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.911                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2110 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1466 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2853 ; 1.354 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3557 ; 0.948 ; 2.993       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   251 ; 6.243 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    98 ;34.838 ;23.469       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   366 ;18.916 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;17.102 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2294 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   440 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   485 ; 0.211 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1521 ; 0.201 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1025 ; 0.180 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1085 ; 0.090 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    31 ; 0.152 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.025 ; 0.200       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    11 ; 0.130 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    29 ; 0.249 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.059 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1274 ; 0.037 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   512 ; 0.013 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2060 ; 0.057 ; 6.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   836 ; 0.047 ; 6.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   793 ; 0.063 ; 7.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4AUA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAY-12.                  
REMARK 100 THE DEPOSITION ID IS D_1290052506.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9611                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13277                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 71.230                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5MG/ML 0.1 M MES/NAOH PH 5.7,, 4.5%      
REMARK 280  W/V PEG 3350, 25 MM SODIUM NITRATE, 10% V/V GLYCEROL, 10 DEGREES    
REMARK 280  CELSIUS, TEMPERATURE 287K                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       8555   Y+1/2,-X+1/2,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        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       50.36700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.36700            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       30.15000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       50.36700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.36700            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       30.15000            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       50.36700            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       50.36700            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       30.15000            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       50.36700            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       50.36700            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       30.15000            
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 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     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     CYS A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     ASP A    10                                                      
REMARK 465     TYR A    24                                                      
REMARK 465     VAL A    45                                                      
REMARK 465     ARG A    46                                                      
REMARK 465     VAL A    47                                                      
REMARK 465     GLN A    48                                                      
REMARK 465     THR A    49                                                      
REMARK 465     GLY A    50                                                      
REMARK 465     GLU A    51                                                      
REMARK 465     GLU A    52                                                      
REMARK 465     GLY A    53                                                      
REMARK 465     MET A    54                                                      
REMARK 465     PRO A    55                                                      
REMARK 465     LEU A    56                                                      
REMARK 465     VAL A    85                                                      
REMARK 465     SER A    86                                                      
REMARK 465     ARG A    87                                                      
REMARK 465     THR A    88                                                      
REMARK 465     ASP A    89                                                      
REMARK 465     ARG A    90                                                      
REMARK 465     GLU A    91                                                      
REMARK 465     THR A    92                                                      
REMARK 465     ARG A   168                                                      
REMARK 465     ILE A   169                                                      
REMARK 465     TYR A   170                                                      
REMARK 465     SER A   171                                                      
REMARK 465     PHE A   172                                                      
REMARK 465     GLN A   173                                                      
REMARK 465     MET A   174                                                      
REMARK 465     ALA A   175                                                      
REMARK 465     LEU A   176                                                      
REMARK 465     THR A   177                                                      
REMARK 465     SER A   178                                                      
REMARK 465     VAL A   179                                                      
REMARK 465     VAL A   180                                                      
REMARK 465     VAL A   181                                                      
REMARK 465     HIS A   302                                                      
REMARK 465     HIS A   303                                                      
REMARK 465     HIS A   304                                                      
REMARK 465     HIS A   305                                                      
REMARK 465     HIS A   306                                                      
REMARK 465     HIS A   307                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  2078     O    HOH A  2081              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  16      -35.50   -138.14                                   
REMARK 500    ASN A  35       68.68   -107.38                                   
REMARK 500    GLU A  72       58.68     28.70                                   
REMARK 500    ARG A 140       50.84     37.47                                   
REMARK 500    ARG A 144      -16.23     77.48                                   
REMARK 500    ASP A 145       53.46   -142.00                                   
REMARK 500    ALA A 197     -176.77    -69.50                                   
REMARK 500    LYS A 257      -82.23     -1.31                                   
REMARK 500    VAL A 266       78.88   -115.62                                   
REMARK 500    ASP A 268      -27.12    106.49                                   
REMARK 500    LEU A 281       43.83    -93.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4AU A 1302                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BI7   RELATED DB: PDB                                   
REMARK 900 MECHANISM OF G1 CYCLIN DEPENDENT KINASE INHIBITION FROM THE          
REMARK 900 STRUCTURE OF THE CDK6-P16INK4A TUMOR SUPPRESSOR COMPLEX              
REMARK 900 RELATED ID: 1BI8   RELATED DB: PDB                                   
REMARK 900 MECHANISM OF G1 CYCLIN DEPENDENT KINASE INHIBITION FROM THE          
REMARK 900 STRUCTURES CDK6-P19INK4D INHIBITOR COMPLEX                           
REMARK 900 RELATED ID: 1BLX   RELATED DB: PDB                                   
REMARK 900 P19INK4D/CDK6 COMPLEX                                                
REMARK 900 RELATED ID: 1G3N   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF A P18(INK4C)-CDK6-K-CYCLIN TERNARY COMPLEX              
REMARK 900 RELATED ID: 1JOW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A COMPLEX OF HUMAN CDK6 AND A VIRALCYCLIN       
REMARK 900 RELATED ID: 1XO2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A HUMAN CYCLIN-DEPENDENT KINASE 6COMPLEX WITH   
REMARK 900 A FLAVONOL INHIBITOR, FISETIN                                        
REMARK 900 RELATED ID: 2EUF   RELATED DB: PDB                                   
REMARK 900 X-RAY STRUCTURE OF HUMAN CDK6-VCYCLIN IN COMPLEX WITH THEINHIBITOR   
REMARK 900 PD0332991                                                            
REMARK 900 RELATED ID: 2F2C   RELATED DB: PDB                                   
REMARK 900 X-RAY STRUCTURE OF HUMAN CDK6-VCYCLINWITH THE                        
REMARK 900 INHIBITORAMINOPURVALANOL                                             
DBREF  4AUA A    1   301  UNP    Q00534   CDK6_HUMAN       1    301             
SEQADV 4AUA HIS A  302  UNP  Q00534              EXPRESSION TAG                 
SEQADV 4AUA HIS A  303  UNP  Q00534              EXPRESSION TAG                 
SEQADV 4AUA HIS A  304  UNP  Q00534              EXPRESSION TAG                 
SEQADV 4AUA HIS A  305  UNP  Q00534              EXPRESSION TAG                 
SEQADV 4AUA HIS A  306  UNP  Q00534              EXPRESSION TAG                 
SEQADV 4AUA HIS A  307  UNP  Q00534              EXPRESSION TAG                 
SEQRES   1 A  307  MET GLU LYS ASP GLY LEU CYS ARG ALA ASP GLN GLN TYR          
SEQRES   2 A  307  GLU CYS VAL ALA GLU ILE GLY GLU GLY ALA TYR GLY LYS          
SEQRES   3 A  307  VAL PHE LYS ALA ARG ASP LEU LYS ASN GLY GLY ARG PHE          
SEQRES   4 A  307  VAL ALA LEU LYS ARG VAL ARG VAL GLN THR GLY GLU GLU          
SEQRES   5 A  307  GLY MET PRO LEU SER THR ILE ARG GLU VAL ALA VAL LEU          
SEQRES   6 A  307  ARG HIS LEU GLU THR PHE GLU HIS PRO ASN VAL VAL ARG          
SEQRES   7 A  307  LEU PHE ASP VAL CYS THR VAL SER ARG THR ASP ARG GLU          
SEQRES   8 A  307  THR LYS LEU THR LEU VAL PHE GLU HIS VAL ASP GLN ASP          
SEQRES   9 A  307  LEU THR THR TYR LEU ASP LYS VAL PRO GLU PRO GLY VAL          
SEQRES  10 A  307  PRO THR GLU THR ILE LYS ASP MET MET PHE GLN LEU LEU          
SEQRES  11 A  307  ARG GLY LEU ASP PHE LEU HIS SER HIS ARG VAL VAL HIS          
SEQRES  12 A  307  ARG ASP LEU LYS PRO GLN ASN ILE LEU VAL THR SER SER          
SEQRES  13 A  307  GLY GLN ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ILE          
SEQRES  14 A  307  TYR SER PHE GLN MET ALA LEU THR SER VAL VAL VAL THR          
SEQRES  15 A  307  LEU TRP TYR ARG ALA PRO GLU VAL LEU LEU GLN SER SER          
SEQRES  16 A  307  TYR ALA THR PRO VAL ASP LEU TRP SER VAL GLY CYS ILE          
SEQRES  17 A  307  PHE ALA GLU MET PHE ARG ARG LYS PRO LEU PHE ARG GLY          
SEQRES  18 A  307  SER SER ASP VAL ASP GLN LEU GLY LYS ILE LEU ASP VAL          
SEQRES  19 A  307  ILE GLY LEU PRO GLY GLU GLU ASP TRP PRO ARG ASP VAL          
SEQRES  20 A  307  ALA LEU PRO ARG GLN ALA PHE HIS SER LYS SER ALA GLN          
SEQRES  21 A  307  PRO ILE GLU LYS PHE VAL THR ASP ILE ASP GLU LEU GLY          
SEQRES  22 A  307  LYS ASP LEU LEU LEU LYS CYS LEU THR PHE ASN PRO ALA          
SEQRES  23 A  307  LYS ARG ILE SER ALA TYR SER ALA LEU SER HIS PRO TYR          
SEQRES  24 A  307  PHE GLN HIS HIS HIS HIS HIS HIS                              
HET    4AU  A1302      25                                                       
HETNAM     4AU 1H-BENZIMIDAZOL-2-YL(1H-PYRROL-2-YL)METHANONE                    
FORMUL   2  4AU    C12 H9 N3 O                                                  
FORMUL   3  HOH   *86(H2 O)                                                     
HELIX    1   1 SER A   57  THR A   70  1                                  14    
HELIX    2   2 LEU A  105  VAL A  112  1                                   8    
HELIX    3   3 PRO A  118  HIS A  139  1                                  22    
HELIX    4   4 LYS A  147  GLN A  149  5                                   3    
HELIX    5   5 ALA A  187  LEU A  192  1                                   6    
HELIX    6   6 THR A  198  ARG A  215  1                                  18    
HELIX    7   7 SER A  223  GLY A  236  1                                  14    
HELIX    8   8 GLY A  239  TRP A  243  5                                   5    
HELIX    9   9 PRO A  250  PHE A  254  5                                   5    
HELIX   10  10 PRO A  261  PHE A  265  5                                   5    
HELIX   11  11 ASP A  270  LEU A  281  1                                  12    
HELIX   12  12 SER A  290  HIS A  297  1                                   8    
HELIX   13  13 PRO A  298  GLN A  301  5                                   4    
SHEET    1  AA 5 TYR A  13  GLU A  21  0                                        
SHEET    2  AA 5 LYS A  26  ASP A  32 -1  O  VAL A  27   N  ILE A  19           
SHEET    3  AA 5 ARG A  38  LYS A  43 -1  O  ARG A  38   N  ASP A  32           
SHEET    4  AA 5 THR A  95  GLU A  99 -1  O  LEU A  96   N  LYS A  43           
SHEET    5  AA 5 LEU A  79  CYS A  83 -1  N  PHE A  80   O  VAL A  97           
SHEET    1  AB 3 GLN A 103  ASP A 104  0                                        
SHEET    2  AB 3 ILE A 151  VAL A 153 -1  O  VAL A 153   N  GLN A 103           
SHEET    3  AB 3 ILE A 159  LEU A 161 -1  O  LYS A 160   N  LEU A 152           
CISPEP   1 ILE A   19    GLY A   20          0         2.70                     
CISPEP   2 GLY A   22    ALA A   23          0        -2.75                     
CISPEP   3 GLU A  114    PRO A  115          0         0.03                     
SITE     1 AC1  9 ILE A  19  ALA A  41  GLU A  99  HIS A 100                    
SITE     2 AC1  9 VAL A 101  ASP A 102  ASP A 104  LEU A 152                    
SITE     3 AC1  9 ALA A 162                                                     
CRYST1  100.734  100.734   60.300  90.00  90.00  90.00 I 4           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      0.009927  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009927  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016584        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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