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Database: PDB
Entry: 5L2I
LinkDB: 5L2I
Original site: 5L2I 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       01-AUG-16   5L2I              
TITLE     THE X-RAY CO-CRYSTAL STRUCTURE OF HUMAN CDK6 AND PALBOCICLIB.         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 6;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP 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 GENE: CDK6, CDKN6;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    CYCLIN-DEPENDENT KINASE, KINASE INHIBITOR, KINASE SELECTIVITY,        
KEYWDS   2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.CHEN,R.A.FERRE,W.DEIHL,X.YU,Y.-A.HE                                 
REVDAT   2   19-OCT-16 5L2I    1       JRNL                                     
REVDAT   1   24-AUG-16 5L2I    0                                                
JRNL        AUTH   P.CHEN,N.V.LEE,W.HU,M.XU,R.A.FERRE,H.LAM,S.BERGQVIST,        
JRNL        AUTH 2 J.SOLOWIEJ,W.DIEHL,Y.A.HE,X.YU,A.NAGATA,T.VANARSDALE,        
JRNL        AUTH 3 B.W.MURRAY                                                   
JRNL        TITL   SPECTRUM AND DEGREE OF CDK DRUG INTERACTIONS PREDICTS        
JRNL        TITL 2 CLINICAL PERFORMANCE.                                        
JRNL        REF    MOL.CANCER THER.              V.  15  2273 2016              
JRNL        REFN                   ESSN 1538-8514                               
JRNL        PMID   27496135                                                     
JRNL        DOI    10.1158/1535-7163.MCT-16-0300                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.4                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 8187                           
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)  : 0.235                          
REMARK   3   R VALUE            (WORKING SET)  : 0.226                          
REMARK   3   FREE R VALUE                      : 0.304                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 10.170                         
REMARK   3   FREE R VALUE TEST SET COUNT       : 833                            
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               : 5                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.75                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.07                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.96                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2303                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2721                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2083                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2657                   
REMARK   3   BIN FREE R VALUE                        : 0.3369                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 9.55                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 220                      
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            : 2084                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 100.7                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 92.38                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -8.00070                                             
REMARK   3    B22 (A**2) : -8.00070                                             
REMARK   3    B33 (A**2) : 16.00150                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.489               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 3.599               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.408               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
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      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.876                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2197   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3004   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 759    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 50     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 338    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2197   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 269    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 2514   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.16                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.59                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.01                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5L2I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000223022.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-AUG-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 98.15                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.21                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8324                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: BUSTER                                                
REMARK 200 STARTING MODEL: 3NUX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:1 (PROTEIN TO WELL BUFFER) WITH WELL   
REMARK 280  BUFFER CONTAINING: 0.1 M MES PH 6.0, 70 - 80 MM NH4NO3, 10 - 15%    
REMARK 280  POLYETHYLENEGLYCOL 3350., VAPOR DIFFUSION, SITTING DROP,            
REMARK 280  TEMPERATURE 286.15K                                                 
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       50.87450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.87450            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       30.38900            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       50.87450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.87450            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       30.38900            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       50.87450            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       50.87450            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       30.38900            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       50.87450            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       50.87450            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       30.38900            
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     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     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     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     ALA A   167                                                      
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     HIS A   255                                                      
REMARK 465     SER A   256                                                      
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 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     LEU A 166    CG   CD1  CD2                                       
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    ASN A  35       59.14   -102.72                                   
REMARK 500    GLU A  72       62.34     27.36                                   
REMARK 500    PRO A 115       47.12    -89.56                                   
REMARK 500    ARG A 144      -27.68     80.46                                   
REMARK 500    GLN A 193       35.30     74.38                                   
REMARK 500    SER A 194      -96.77    -94.79                                   
REMARK 500    TYR A 196       28.75   -141.58                                   
REMARK 500    PHE A 213      -77.34    -75.36                                   
REMARK 500    ARG A 220       71.60   -110.18                                   
REMARK 500    ASP A 246       88.18     66.19                                   
REMARK 500    THR A 267      -88.74    -47.26                                   
REMARK 500    HIS A 297      135.76    -22.45                                   
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 LQQ A 900                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5L2S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5L2T   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5L2W   RELATED DB: PDB                                   
DBREF  5L2I A    1   301  UNP    Q00534   CDK6_HUMAN       1    301             
SEQADV 5L2I HIS A  302  UNP  Q00534              EXPRESSION TAG                 
SEQADV 5L2I HIS A  303  UNP  Q00534              EXPRESSION TAG                 
SEQADV 5L2I HIS A  304  UNP  Q00534              EXPRESSION TAG                 
SEQADV 5L2I HIS A  305  UNP  Q00534              EXPRESSION TAG                 
SEQADV 5L2I HIS A  306  UNP  Q00534              EXPRESSION TAG                 
SEQADV 5L2I 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    LQQ  A 900      62                                                       
HETNAM     LQQ 6-ACETYL-8-CYCLOPENTYL-5-METHYL-2-[(5-PIPERAZIN-1-               
HETNAM   2 LQQ  YLPYRIDIN-2-YL)AMINO]PYRIDO[2,3-D]PYRIMIDIN-7(8H)-ONE           
HETSYN     LQQ PALBOCICLIB                                                      
FORMUL   2  LQQ    C24 H29 N7 O2                                                
HELIX    1 AA1 THR A   58  GLU A   69  1                                  12    
HELIX    2 AA2 THR A   70  GLU A   72  5                                   3    
HELIX    3 AA3 LEU A  105  ASP A  110  1                                   6    
HELIX    4 AA4 PRO A  118  HIS A  139  1                                  22    
HELIX    5 AA5 ALA A  187  GLN A  193  1                                   7    
HELIX    6 AA6 PRO A  199  ARG A  215  1                                  17    
HELIX    7 AA7 SER A  223  GLY A  236  1                                  14    
HELIX    8 AA8 GLY A  239  TRP A  243  5                                   5    
HELIX    9 AA9 PRO A  250  PHE A  254  5                                   5    
HELIX   10 AB1 ASP A  270  LEU A  281  1                                  12    
HELIX   11 AB2 SER A  290  LEU A  295  1                                   6    
HELIX   12 AB3 HIS A  297  GLN A  301  5                                   5    
SHEET    1 AA1 5 GLU A  14  GLY A  20  0                                        
SHEET    2 AA1 5 VAL A  27  ASP A  32 -1  O  ARG A  31   N  GLU A  14           
SHEET    3 AA1 5 ARG A  38  VAL A  45 -1  O  VAL A  40   N  ALA A  30           
SHEET    4 AA1 5 LEU A  94  GLU A  99 -1  O  PHE A  98   N  ALA A  41           
SHEET    5 AA1 5 LEU A  79  CYS A  83 -1  N  PHE A  80   O  VAL A  97           
SHEET    1 AA2 3 GLN A 103  ASP A 104  0                                        
SHEET    2 AA2 3 ILE A 151  VAL A 153 -1  O  VAL A 153   N  GLN A 103           
SHEET    3 AA2 3 ILE A 159  LEU A 161 -1  O  LYS A 160   N  LEU A 152           
CISPEP   1 GLU A  114    PRO A  115          0         0.26                     
SITE     1 AC1 12 ILE A  19  TYR A  24  VAL A  27  ALA A  41                    
SITE     2 AC1 12 PHE A  98  GLU A  99  VAL A 101  THR A 107                    
SITE     3 AC1 12 GLN A 149  LEU A 152  ALA A 162  ASP A 163                    
CRYST1  101.749  101.749   60.778  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      0.009828  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009828  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016453        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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