GenomeNet

Database: PDB
Entry: 4TTH
LinkDB: 4TTH
Original site: 4TTH 
HEADER    TRANSFERASE/CELL CYCLE/INHIBITOR        20-JUN-14   4TTH              
TITLE     CRYSTAL STRUCTURE OF A CDK6/VCYCLIN COMPLEX WITH INHIBITOR BOUND      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN HOMOLOG;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: V-CYCLIN;                                                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CYCLIN-DEPENDENT KINASE 6;                                 
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: CELL DIVISION PROTEIN KINASE 6,SERINE/THREONINE-PROTEIN     
COMPND  10 KINASE PLSTIRE;                                                      
COMPND  11 EC: 2.7.11.22;                                                       
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SAIMIRIINE HERPESVIRUS 2;                       
SOURCE   3 ORGANISM_COMMON: SAHV-2;                                             
SOURCE   4 ORGANISM_TAXID: 10383;                                               
SOURCE   5 STRAIN: 11;                                                          
SOURCE   6 GENE: 72, ECLF2;                                                     
SOURCE   7 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: CDK6, CDKN6;                                                   
SOURCE  14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 7111                                        
KEYWDS    KINASE, TRANSFERASE-CELL CYCLE-INHIBITOR COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.E.PIPER,N.WALKER,Z.WANG                                             
REVDAT   3   22-NOV-17 4TTH    1       SOURCE JRNL   REMARK                     
REVDAT   2   01-OCT-14 4TTH    1       JRNL                                     
REVDAT   1   06-AUG-14 4TTH    0                                                
SPRSDE     06-AUG-14 4TTH      4P41                                             
JRNL        AUTH   Z.LI,X.WANG,J.EKSTEROWICZ,M.W.GRIBBLE,G.Q.ALBA,M.AYRES,      
JRNL        AUTH 2 T.J.CARLSON,A.CHEN,X.CHEN,R.CHO,R.V.CONNORS,M.DEGRAFFENREID, 
JRNL        AUTH 3 J.T.DEIGNAN,J.DUQUETTE,P.FAN,B.FISHER,J.FU,J.N.HUARD,        
JRNL        AUTH 4 J.KAIZERMAN,K.S.KEEGAN,C.LI,K.LI,Y.LI,L.LIANG,W.LIU,         
JRNL        AUTH 5 S.E.LIVELY,M.C.LO,J.MA,D.L.MCMINN,J.T.MIHALIC,K.MODI,R.NGO,  
JRNL        AUTH 6 K.PATTABIRAMAN,D.E.PIPER,C.QUEVA,M.L.RAGAINS,J.SUCHOMEL,     
JRNL        AUTH 7 S.THIBAULT,N.WALKER,X.WANG,Z.WANG,M.WANSKA,P.M.WEHN,         
JRNL        AUTH 8 M.F.WEIDNER,A.J.ZHANG,X.ZHAO,A.KAMB,D.WICKRAMASINGHE,K.DAI,  
JRNL        AUTH 9 L.R.MCGEE,J.C.MEDINA                                         
JRNL        TITL   DISCOVERY OF AMG 925, A FLT3 AND CDK4 DUAL KINASE INHIBITOR  
JRNL        TITL 2 WITH PREFERENTIAL AFFINITY FOR THE ACTIVATED STATE OF FLT3.  
JRNL        REF    J.MED.CHEM.                   V.  57  3430 2014              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   24641103                                                     
JRNL        DOI    10.1021/JM500118J                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.68                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 16018                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.240                           
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.337                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 805                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 19.6804 -  5.2420    1.00     2781   123  0.2266 0.3297        
REMARK   3     2  5.2420 -  4.1738    1.00     2563   131  0.2288 0.3119        
REMARK   3     3  4.1738 -  3.6500    1.00     2509   148  0.2198 0.3225        
REMARK   3     4  3.6500 -  3.3180    1.00     2481   131  0.2465 0.3488        
REMARK   3     5  3.3180 -  3.0812    1.00     2417   136  0.2786 0.4093        
REMARK   3     6  3.0812 -  2.9000    1.00     2462   136  0.2786 0.4059        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.500            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.030           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           3972                                  
REMARK   3   ANGLE     :  1.316           5405                                  
REMARK   3   CHIRALITY :  0.081            657                                  
REMARK   3   PLANARITY :  0.005            666                                  
REMARK   3   DIHEDRAL  : 17.223           1441                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4TTH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000202177.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JUL-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XDS, AIMLESS                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16125                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.680                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 11.80                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.20                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.41000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.200                              
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: 2EUF                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MM TRIS PH 7.9, 100 MM CALCIUM        
REMARK 280  ACETATE, 10 MM DTT, 8-12% PEG 3350, 100 MM NDSB-201, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      299.33000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      149.66500            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      224.49750            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       74.83250            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      374.16250            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      299.33000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      149.66500            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       74.83250            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      224.49750            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      374.16250            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     ASN A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     CYS A   124                                                      
REMARK 465     ASP A   125                                                      
REMARK 465     CYS A   126                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     CYS B     7                                                      
REMARK 465     ARG B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     ASP B    10                                                      
REMARK 465     GLN B    11                                                      
REMARK 465     GLN B    12                                                      
REMARK 465     TYR B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     GLY B    22                                                      
REMARK 465     ALA B    23                                                      
REMARK 465     TYR B    24                                                      
REMARK 465     GLY B    25                                                      
REMARK 465     GLY B    36                                                      
REMARK 465     GLN B    48                                                      
REMARK 465     THR B    49                                                      
REMARK 465     GLY B    50                                                      
REMARK 465     GLU B    51                                                      
REMARK 465     VAL B    85                                                      
REMARK 465     SER B    86                                                      
REMARK 465     ARG B    87                                                      
REMARK 465     THR B    88                                                      
REMARK 465     ASP B    89                                                      
REMARK 465     ARG B    90                                                      
REMARK 465     GLU B    91                                                      
REMARK 465     ARG B   245                                                      
REMARK 465     ASP B   246                                                      
REMARK 465     VAL B   247                                                      
REMARK 465     ALA B   248                                                      
REMARK 465     LEU B   249                                                      
REMARK 465     PRO B   250                                                      
REMARK 465     ARG B   251                                                      
REMARK 465     GLN B   252                                                      
REMARK 465     ALA B   253                                                      
REMARK 465     PHE B   254                                                      
REMARK 465     HIS B   255                                                      
REMARK 465     SER B   256                                                      
REMARK 465     LYS B   257                                                      
REMARK 465     SER B   258                                                      
REMARK 465     ALA B   259                                                      
REMARK 465     GLN B   260                                                      
REMARK 465     VAL B   266                                                      
REMARK 465     THR B   267                                                      
REMARK 465     ARG B   305                                                      
REMARK 465     CYS B   306                                                      
REMARK 465     LYS B   307                                                      
REMARK 465     GLU B   308                                                      
REMARK 465     ASN B   309                                                      
REMARK 465     LEU B   310                                                      
REMARK 465     ASP B   311                                                      
REMARK 465     SER B   312                                                      
REMARK 465     HIS B   313                                                      
REMARK 465     LEU B   314                                                      
REMARK 465     PRO B   315                                                      
REMARK 465     PRO B   316                                                      
REMARK 465     SER B   317                                                      
REMARK 465     GLN B   318                                                      
REMARK 465     ASN B   319                                                      
REMARK 465     THR B   320                                                      
REMARK 465     SER B   321                                                      
REMARK 465     GLU B   322                                                      
REMARK 465     LEU B   323                                                      
REMARK 465     ASN B   324                                                      
REMARK 465     THR B   325                                                      
REMARK 465     ALA B   326                                                      
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     LYS A  36    CG   CD   CE   NZ                                   
REMARK 470     GLU A  42    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  92    CG   CD   CE   NZ                                   
REMARK 470     TYR A 121    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN A 129    CG   OD1  ND2                                       
REMARK 470     LEU A 130    CG   CD1  CD2                                       
REMARK 470     ASN A 213    CG   OD1  ND2                                       
REMARK 470     ARG A 215    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 252    CG   CD   OE1  OE2                                  
REMARK 470     CYS B  15    SG                                                  
REMARK 470     GLU B  18    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  21    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  26    CG   CD   CE   NZ                                   
REMARK 470     LYS B  29    CG   CD   CE   NZ                                   
REMARK 470     ARG B  31    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B  33    CG   CD1  CD2                                       
REMARK 470     LYS B  34    CG   CD   CE   NZ                                   
REMARK 470     ARG B  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  44    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  46    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B  81    CG   OD1  OD2                                       
REMARK 470     ASP B 110    CG   OD1  OD2                                       
REMARK 470     VAL B 117    CG1  CG2                                            
REMARK 470     LYS B 216    CG   CD   CE   NZ                                   
REMARK 470     LEU B 232    CG   CD1  CD2                                       
REMARK 470     ASP B 233    CG   OD1  OD2                                       
REMARK 470     ILE B 235    CG1  CG2  CD1                                       
REMARK 470     LEU B 237    CG   CD1  CD2                                       
REMARK 470     ASP B 268    CG   OD1  OD2                                       
REMARK 470     LYS B 274    CG   CD   CE   NZ                                   
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    ILE A    43     NE2  GLN A    88              2.12            
REMARK 500   O    PHE B   135     OG   SER B   138              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 188   C   -  N   -  CA  ANGL. DEV. =  10.3 DEGREES          
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    ILE A  43        4.51    -47.68                                   
REMARK 500    GLU A  46      -83.23    -96.79                                   
REMARK 500    GLU A 141      -73.49    -57.37                                   
REMARK 500    ALA A 142      -37.39    -32.09                                   
REMARK 500    LYS A 164       58.33     39.22                                   
REMARK 500    LEU A 185      -14.19    -45.32                                   
REMARK 500    ASN A 213       47.71    -57.77                                   
REMARK 500    CYS A 214     -157.67    -97.98                                   
REMARK 500    ASN A 229       53.02     76.88                                   
REMARK 500    THR A 232        0.13    -55.68                                   
REMARK 500    VAL B  16      -81.06   -127.01                                   
REMARK 500    PHE B  28     -158.12    -82.30                                   
REMARK 500    LYS B  34      -77.32    -68.22                                   
REMARK 500    GLU B  72       64.88     33.54                                   
REMARK 500    LYS B 111       -2.04   -150.43                                   
REMARK 500    THR B 119      -73.25      8.71                                   
REMARK 500    PHE B 135      -82.66    -52.42                                   
REMARK 500    LEU B 136      -72.39    -24.08                                   
REMARK 500    ARG B 144       68.83   -104.34                                   
REMARK 500    ASP B 145       40.69   -171.60                                   
REMARK 500    SER B 156        8.38    -68.14                                   
REMARK 500    ASP B 163       95.63     52.47                                   
REMARK 500    THR B 177     -178.33    -65.44                                   
REMARK 500    VAL B 181      140.58     67.44                                   
REMARK 500    PRO B 188      -88.18    -39.59                                   
REMARK 500    GLU B 189      -32.08    -27.56                                   
REMARK 500    LEU B 192        5.69    -61.66                                   
REMARK 500    ALA B 197     -143.91   -176.38                                   
REMARK 500    ARG B 215       49.03    -39.24                                   
REMARK 500    SER B 222      -14.48   -140.14                                   
REMARK 500    ASP B 233       32.56    -93.15                                   
REMARK 500    VAL B 234      -66.39   -139.59                                   
REMARK 500    LYS B 264      -49.15    -28.19                                   
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 24V B 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4P41   RELATED DB: PDB                                   
REMARK 900 THIS IS USING THE SAME DATA SET AS WAS USED FOR 4P41, BUT PROCESSED  
REMARK 900 WITH XDS. THE COMPOUND ELECTRON DENSITY IS SIGNIFICANTLY BETTER.     
DBREF  4TTH A    1   254  UNP    Q01043   CGH2_SHV21       1    254             
DBREF  4TTH B    1   326  UNP    Q00534   CDK6_HUMAN       1    326             
SEQRES   1 A  254  MET ALA ASP SER PRO ASN ARG LEU ASN ARG ALA LYS ILE          
SEQRES   2 A  254  ASP SER THR THR MET LYS ASP PRO ARG VAL LEU ASN ASN          
SEQRES   3 A  254  LEU LYS LEU ARG GLU LEU LEU LEU PRO LYS PHE THR SER          
SEQRES   4 A  254  LEU TRP GLU ILE GLN THR GLU VAL THR VAL ASP ASN ARG          
SEQRES   5 A  254  THR ILE LEU LEU THR TRP MET HIS LEU LEU CYS GLU SER          
SEQRES   6 A  254  PHE GLU LEU ASP LYS SER VAL PHE PRO LEU SER VAL SER          
SEQRES   7 A  254  ILE LEU ASP ARG TYR LEU CYS LYS LYS GLN GLY THR LYS          
SEQRES   8 A  254  LYS THR LEU GLN LYS ILE GLY ALA ALA CYS VAL LEU ILE          
SEQRES   9 A  254  GLY SER LYS ILE ARG THR VAL LYS PRO MET THR VAL SER          
SEQRES  10 A  254  LYS LEU THR TYR LEU SER CYS ASP CYS PHE THR ASN LEU          
SEQRES  11 A  254  GLU LEU ILE ASN GLN GLU LYS ASP ILE LEU GLU ALA LEU          
SEQRES  12 A  254  LYS TRP ASP THR GLU ALA VAL LEU ALA THR ASP PHE LEU          
SEQRES  13 A  254  ILE PRO LEU CYS ASN ALA LEU LYS ILE PRO GLU ASP LEU          
SEQRES  14 A  254  TRP PRO GLN LEU TYR GLU ALA ALA SER THR THR ILE CYS          
SEQRES  15 A  254  LYS ALA LEU ILE GLN PRO ASN ILE ALA LEU LEU SER PRO          
SEQRES  16 A  254  GLY LEU ILE CYS ALA GLY GLY LEU LEU THR THR ILE GLU          
SEQRES  17 A  254  THR ASP ASN THR ASN CYS ARG PRO TRP THR CYS TYR LEU          
SEQRES  18 A  254  GLU ASP LEU SER SER ILE LEU ASN PHE SER THR ASN THR          
SEQRES  19 A  254  VAL ARG THR VAL LYS ASP GLN VAL SER GLU ALA PHE SER          
SEQRES  20 A  254  LEU TYR ASP LEU GLU ILE LEU                                  
SEQRES   1 B  326  MET GLU LYS ASP GLY LEU CYS ARG ALA ASP GLN GLN TYR          
SEQRES   2 B  326  GLU CYS VAL ALA GLU ILE GLY GLU GLY ALA TYR GLY LYS          
SEQRES   3 B  326  VAL PHE LYS ALA ARG ASP LEU LYS ASN GLY GLY ARG PHE          
SEQRES   4 B  326  VAL ALA LEU LYS ARG VAL ARG VAL GLN THR GLY GLU GLU          
SEQRES   5 B  326  GLY MET PRO LEU SER THR ILE ARG GLU VAL ALA VAL LEU          
SEQRES   6 B  326  ARG HIS LEU GLU THR PHE GLU HIS PRO ASN VAL VAL ARG          
SEQRES   7 B  326  LEU PHE ASP VAL CYS THR VAL SER ARG THR ASP ARG GLU          
SEQRES   8 B  326  THR LYS LEU THR LEU VAL PHE GLU HIS VAL ASP GLN ASP          
SEQRES   9 B  326  LEU THR THR TYR LEU ASP LYS VAL PRO GLU PRO GLY VAL          
SEQRES  10 B  326  PRO THR GLU THR ILE LYS ASP MET MET PHE GLN LEU LEU          
SEQRES  11 B  326  ARG GLY LEU ASP PHE LEU HIS SER HIS ARG VAL VAL HIS          
SEQRES  12 B  326  ARG ASP LEU LYS PRO GLN ASN ILE LEU VAL THR SER SER          
SEQRES  13 B  326  GLY GLN ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ILE          
SEQRES  14 B  326  TYR SER PHE GLN MET ALA LEU THR SER VAL VAL VAL THR          
SEQRES  15 B  326  LEU TRP TYR ARG ALA PRO GLU VAL LEU LEU GLN SER SER          
SEQRES  16 B  326  TYR ALA THR PRO VAL ASP LEU TRP SER VAL GLY CYS ILE          
SEQRES  17 B  326  PHE ALA GLU MET PHE ARG ARG LYS PRO LEU PHE ARG GLY          
SEQRES  18 B  326  SER SER ASP VAL ASP GLN LEU GLY LYS ILE LEU ASP VAL          
SEQRES  19 B  326  ILE GLY LEU PRO GLY GLU GLU ASP TRP PRO ARG ASP VAL          
SEQRES  20 B  326  ALA LEU PRO ARG GLN ALA PHE HIS SER LYS SER ALA GLN          
SEQRES  21 B  326  PRO ILE GLU LYS PHE VAL THR ASP ILE ASP GLU LEU GLY          
SEQRES  22 B  326  LYS ASP LEU LEU LEU LYS CYS LEU THR PHE ASN PRO ALA          
SEQRES  23 B  326  LYS ARG ILE SER ALA TYR SER ALA LEU SER HIS PRO TYR          
SEQRES  24 B  326  PHE GLN ASP LEU GLU ARG CYS LYS GLU ASN LEU ASP SER          
SEQRES  25 B  326  HIS LEU PRO PRO SER GLN ASN THR SER GLU LEU ASN THR          
SEQRES  26 B  326  ALA                                                          
HET    24V  B 401      31                                                       
HETNAM     24V 9-CYCLOPENTYL-N-(5-PIPERAZIN-1-YLPYRIDIN-2-YL)PYRIDO[4,          
HETNAM   2 24V  5]PYRROLO[1,2-D]PYRIMIDIN-2-AMINE                               
FORMUL   3  24V    C23 H26 N8                                                   
FORMUL   4  HOH   *10(H2 O)                                                     
HELIX    1 AA1 ASP A   14  LYS A   19  1                                   6    
HELIX    2 AA2 ASP A   20  GLU A   31  1                                  12    
HELIX    3 AA3 LEU A   32  LEU A   34  5                                   3    
HELIX    4 AA4 THR A   48  PHE A   66  1                                  19    
HELIX    5 AA5 SER A   71  LYS A   87  1                                  17    
HELIX    6 AA6 THR A   93  THR A  110  1                                  18    
HELIX    7 AA7 THR A  115  LEU A  122  1                                   8    
HELIX    8 AA8 THR A  128  LEU A  143  1                                  16    
HELIX    9 AA9 LEU A  151  ASP A  154  5                                   4    
HELIX   10 AB1 PHE A  155  LEU A  163  1                                   9    
HELIX   11 AB2 PRO A  166  ASP A  168  5                                   3    
HELIX   12 AB3 LEU A  169  LEU A  185  1                                  17    
HELIX   13 AB4 ILE A  186  ALA A  191  5                                   6    
HELIX   14 AB5 SER A  194  ASN A  211  1                                  18    
HELIX   15 AB6 PRO A  216  CYS A  219  5                                   4    
HELIX   16 AB7 TYR A  220  ASN A  229  1                                  10    
HELIX   17 AB8 SER A  231  LEU A  248  1                                  18    
HELIX   18 AB9 ASP A  250  LEU A  254  5                                   5    
HELIX   19 AC1 PRO B   55  GLU B   69  1                                  15    
HELIX   20 AC2 THR B   70  GLU B   72  5                                   3    
HELIX   21 AC3 LEU B  105  ASP B  110  1                                   6    
HELIX   22 AC4 PRO B  118  HIS B  139  1                                  22    
HELIX   23 AC5 ALA B  187  LEU B  192  1                                   6    
HELIX   24 AC6 THR B  198  ARG B  214  1                                  17    
HELIX   25 AC7 SER B  223  GLY B  236  1                                  14    
HELIX   26 AC8 LEU B  272  CYS B  280  1                                   9    
HELIX   27 AC9 SER B  290  SER B  296  1                                   7    
SHEET    1 AA1 3 VAL B  40  LYS B  43  0                                        
SHEET    2 AA1 3 THR B  95  GLU B  99 -1  O  PHE B  98   N  ALA B  41           
SHEET    3 AA1 3 LEU B  79  CYS B  83 -1  N  PHE B  80   O  VAL B  97           
SHEET    1 AA2 3 GLN B 103  ASP B 104  0                                        
SHEET    2 AA2 3 ILE B 151  VAL B 153 -1  O  VAL B 153   N  GLN B 103           
SHEET    3 AA2 3 ILE B 159  LEU B 161 -1  O  LYS B 160   N  LEU B 152           
SHEET    1 AA3 2 VAL B 141  VAL B 142  0                                        
SHEET    2 AA3 2 ARG B 168  ILE B 169 -1  O  ARG B 168   N  VAL B 142           
CISPEP   1 GLU B  114    PRO B  115          0         4.42                     
SITE     1 AC1 11 ILE B  19  VAL B  27  ALA B  41  PHE B  98                    
SITE     2 AC1 11 GLU B  99  VAL B 101  ASP B 102  ASP B 104                    
SITE     3 AC1 11 THR B 107  GLN B 149  LEU B 152                               
CRYST1   71.100   71.100  448.995  90.00  90.00 120.00 P 65 2 2     12          
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      0.014065  0.008120  0.000000        0.00000                         
SCALE2      0.000000  0.016241  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002227        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system