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Database: PDB
Entry: 2W9F
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HEADER    CELL CYCLE                              23-JAN-09   2W9F              
TITLE     CRYSTAL STRUCTURE OF CDK4 IN COMPLEX WITH A D-TYPE CYCLIN             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: G1/S-SPECIFIC CYCLIN-D1;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: D-TYPE CYCLIN, PRAD1 ONCOGENE;                              
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CELL DIVISION PROTEIN KINASE 4;                            
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: KINASE DOMAIN, RESIDUES 1-44,48-303;                       
COMPND  10 SYNONYM: CDK4, CYCLIN-DEPENDENT KINASE 4, PSK-J3;                    
COMPND  11 EC: 2.7.11.22;                                                       
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: 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_TAXID: 7108;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  15 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    SERINE/THREONINE-PROTEIN KINASE, CHROMOSOMAL REARRANGEMENT, ATP-      
KEYWDS   2 BINDING, TRANSFERASE, POLYMORPHISM, CELL DIVISION, PROTO-ONCOGENE,   
KEYWDS   3 PHOSPHOPROTEIN, DISEASE MUTATION, NUCLEOTIDE-BINDING, CYCLIN         
KEYWDS   4 DEPENDENT KINASE, KINASE, CYCLIN, ONCOLOGY, CELL CYCLE, DRUG DESGN   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.J.DAY,A.CLEASBY,I.J.TICKLE,M.O.REILLY,J.E.COYLE,F.P.HOLDING,        
AUTHOR   2 R.L.MCMENAMIN,J.YON,R.CHOPRA,C.LENGAUER,H.JHOTI                      
REVDAT   3   24-APR-19 2W9F    1       SOURCE                                   
REVDAT   2   31-MAR-09 2W9F    1       JRNL                                     
REVDAT   1   10-MAR-09 2W9F    0                                                
JRNL        AUTH   P.J.DAY,A.CLEASBY,I.J.TICKLE,M.O'REILLY,J.E.COYLE,           
JRNL        AUTH 2 F.P.HOLDING,R.L.MCMENAMIN,J.YON,R.CHOPRA,C.LENGAUER,H.JHOTI  
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN CDK4 IN COMPLEX WITH A D-TYPE     
JRNL        TITL 2 CYCLIN.                                                      
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 106  4166 2009              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   19237565                                                     
JRNL        DOI    10.1073/PNAS.0809645106                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT                                           
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,              
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 93.66                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 16778                          
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)  : 0.229                          
REMARK   3   R VALUE            (WORKING SET)  : 0.225                          
REMARK   3   FREE R VALUE                      : 0.300                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.800                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 801                            
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               : 9                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.85                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.02                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 97.97                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2673                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2111                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2539                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2093                   
REMARK   3   BIN FREE R VALUE                        : 0.2439                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.01                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 134                      
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            : 3966                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 70                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 82.07                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 84.35                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.34606                                             
REMARK   3    B22 (A**2) : 14.77175                                             
REMARK   3    B33 (A**2) : -9.42569                                             
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) : NULL                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
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      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : NULL   ; NULL   ; NULL                
REMARK   3    BOND ANGLES               : NULL   ; NULL   ; NULL                
REMARK   3    TORSION ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : NULL   ; NULL   ; NULL                
REMARK   3    ISOTROPIC THERMAL FACTORS : NULL   ; NULL   ; NULL                
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   : NULL   ; NULL   ; NULL                
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   : NULL   ; NULL   ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : NULL                     
REMARK   3    BOND ANGLES                  (DEGREES) : NULL                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : NULL                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. DISORDERED RESIDUES WERE MODELLED STEREOCHEMICALLY       
REMARK   3  WHEN POSSIBLE                                                       
REMARK   4                                                                      
REMARK   4 2W9F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JAN-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290038621.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
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) : 0.931                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16778                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1BLX                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       29.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       93.80850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.13850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       93.80850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.13850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 2250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.7 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLY 43 TO GLU                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLY 44 TO GLU                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, THR 172 TO PHE                        
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     HIS A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     CYS A     7                                                      
REMARK 465     CYS A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     VAL A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     THR A    12                                                      
REMARK 465     ILE A    13                                                      
REMARK 465     ARG A    14                                                      
REMARK 465     ARG A    15                                                      
REMARK 465     ALA A    16                                                      
REMARK 465     TYR A    17                                                      
REMARK 465     PRO A    18                                                      
REMARK 465     ASP A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     ASN A    21                                                      
REMARK 465     LEU A    22                                                      
REMARK 465     LEU A    23                                                      
REMARK 465     ASN A    24                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     GLN A   263                                                      
REMARK 465     GLN A   264                                                      
REMARK 465     ASN A   265                                                      
REMARK 465     MET A   266                                                      
REMARK 465     ASP A   267                                                      
REMARK 465     PRO A   268                                                      
REMARK 465     LYS A   269                                                      
REMARK 465     ALA A   270                                                      
REMARK 465     ALA A   271                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     LEU B   171                                                      
REMARK 465     PHE B   172                                                      
REMARK 465     PRO B   173                                                      
REMARK 465     VAL B   174                                                      
REMARK 465     VAL B   175                                                      
REMARK 465     VAL B   176                                                      
REMARK 465     LEU B   232                                                      
REMARK 465     PRO B   233                                                      
REMARK 465     PRO B   234                                                      
REMARK 465     GLU B   235                                                      
REMARK 465     ASP B   236                                                      
REMARK 465     ASP B   237                                                      
REMARK 465     LEU B   244                                                      
REMARK 465     PRO B   245                                                      
REMARK 465     ARG B   246                                                      
REMARK 465     GLY B   247                                                      
REMARK 465     ALA B   248                                                      
REMARK 465     PHE B   249                                                      
REMARK 465     PRO B   250                                                      
REMARK 465     PRO B   251                                                      
REMARK 465     ARG B   252                                                      
REMARK 465     GLY B   253                                                      
REMARK 465     PRO B   254                                                      
REMARK 465     ARG B   255                                                      
REMARK 465     PRO B   256                                                      
REMARK 465     VAL B   257                                                      
REMARK 465     GLN B   258                                                      
REMARK 465     HIS B   296                                                      
REMARK 465     LYS B   297                                                      
REMARK 465     ASP B   298                                                      
REMARK 465     GLU B   299                                                      
REMARK 465     GLY B   300                                                      
REMARK 465     ASN B   301                                                      
REMARK 465     PRO B   302                                                      
REMARK 465     GLU B   303                                                      
REMARK 465     HIS B   304                                                      
REMARK 465     HIS B   305                                                      
REMARK 465     HIS B   306                                                      
REMARK 465     HIS B   307                                                      
REMARK 465     HIS B   308                                                      
REMARK 465     HIS B   309                                                      
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 B 108   C   -  N   -  CA  ANGL. DEV. =  12.2 DEGREES          
REMARK 500    PRO B 108   C   -  N   -  CD  ANGL. DEV. = -16.1 DEGREES          
REMARK 500    PRO B 113   C   -  N   -  CA  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    PRO B 113   C   -  N   -  CD  ANGL. DEV. = -14.8 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    ARG A  26      -54.30   -134.18                                   
REMARK 500    LEU A  91       -4.95   -145.38                                   
REMARK 500    LYS A  96      -15.47    -48.25                                   
REMARK 500    PRO A 134      -35.52    -37.71                                   
REMARK 500    PRO A 169       82.36    -68.26                                   
REMARK 500    GLN A 213      -72.23    -59.37                                   
REMARK 500    LYS A 238       77.78     63.80                                   
REMARK 500    ARG A 260      -32.53    -39.73                                   
REMARK 500    VAL B   9       42.56   -167.87                                   
REMARK 500    ALA B  10     -178.46    166.38                                   
REMARK 500    TYR B  21     -161.37    -71.96                                   
REMARK 500    PRO B  26      -60.28    -29.42                                   
REMARK 500    HIS B  30      159.34    -44.69                                   
REMARK 500    ILE B  51      -60.80    -28.97                                   
REMARK 500    ASN B  70       40.27    -91.27                                   
REMARK 500    THR B  80      -78.26   -136.33                                   
REMARK 500    ASP B  84       -5.29    -53.10                                   
REMARK 500    ASP B 105      -74.22    -49.11                                   
REMARK 500    LYS B 106      -71.27    -12.73                                   
REMARK 500    ALA B 107      108.21    -23.12                                   
REMARK 500    PRO B 108      113.19    -14.85                                   
REMARK 500    LEU B 112     -138.58   -142.58                                   
REMARK 500    ALA B 114      -42.71    171.88                                   
REMARK 500    GLU B 115       18.24    -69.30                                   
REMARK 500    ARG B 139      -31.56     71.27                                   
REMARK 500    ILE B 146       67.14    -43.41                                   
REMARK 500    SER B 150       65.23    -66.22                                   
REMARK 500    LEU B 156      156.98    -48.37                                   
REMARK 500    TYR B 167      -70.35    -70.23                                   
REMARK 500    GLN B 188      -88.67   -131.49                                   
REMARK 500    SER B 189        4.71    167.67                                   
REMARK 500    THR B 190      -51.82    -15.37                                   
REMARK 500    ALA B 192     -173.14    -69.53                                   
REMARK 500    PHE B 208      -83.86    -75.10                                   
REMARK 500    ARG B 209      -18.09    -46.94                                   
REMARK 500    LYS B 211      164.68    168.27                                   
REMARK 500    ASN B 217      176.60     72.80                                   
REMARK 500    ARG B 240     -121.98   -167.49                                   
REMARK 500    ASP B 241       64.74   -173.88                                   
REMARK 500    MET B 264      -35.40    172.21                                   
REMARK 500    LEU B 276       47.34    -79.59                                   
REMARK 500    TYR B 294        2.84    -66.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU B  156     ALA B  157                 -143.23                    
REMARK 500 LYS B  211     PRO B  212                 -147.76                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B2004        DISTANCE =  7.99 ANGSTROMS                       
REMARK 525    HOH B2006        DISTANCE =  6.23 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2W99   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CDK4 IN COMPLEX WITH A D-TYPE CYCLIN            
REMARK 900 RELATED ID: 2W96   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CDK4 IN COMPLEX WITH A D-TYPE CYCLIN            
REMARK 900 RELATED ID: 1LD2   RELATED DB: PDB                                   
REMARK 900 THEORETICAL STRUCTURE OF HUMAN CYCLIN- DEPENDENT KINASE 4(CDK4)      
DBREF  2W9F A    1   271  UNP    P24385   CCND1_HUMAN      1    271             
DBREF  2W9F B    1    44  UNP    P11802   CDK4_HUMAN       1     44             
DBREF  2W9F B   48   303  UNP    P11802   CDK4_HUMAN      48    303             
DBREF  2W9F B  304   309  PDB    2W9F     2W9F           304    309             
SEQADV 2W9F GLU B   43  UNP  P11802    GLY    43 ENGINEERED MUTATION            
SEQADV 2W9F GLU B   44  UNP  P11802    GLY    44 ENGINEERED MUTATION            
SEQADV 2W9F PHE B  172  UNP  P11802    THR   172 ENGINEERED MUTATION            
SEQRES   1 A  271  MET GLU HIS GLN LEU LEU CYS CYS GLU VAL GLU THR ILE          
SEQRES   2 A  271  ARG ARG ALA TYR PRO ASP ALA ASN LEU LEU ASN ASP ARG          
SEQRES   3 A  271  VAL LEU ARG ALA MET LEU LYS ALA GLU GLU THR CYS ALA          
SEQRES   4 A  271  PRO SER VAL SER TYR PHE LYS CYS VAL GLN LYS GLU VAL          
SEQRES   5 A  271  LEU PRO SER MET ARG LYS ILE VAL ALA THR TRP MET LEU          
SEQRES   6 A  271  GLU VAL CYS GLU GLU GLN LYS CYS GLU GLU GLU VAL PHE          
SEQRES   7 A  271  PRO LEU ALA MET ASN TYR LEU ASP ARG PHE LEU SER LEU          
SEQRES   8 A  271  GLU PRO VAL LYS LYS SER ARG LEU GLN LEU LEU GLY ALA          
SEQRES   9 A  271  THR CYS MET PHE VAL ALA SER LYS MET LYS GLU THR ILE          
SEQRES  10 A  271  PRO LEU THR ALA GLU LYS LEU CYS ILE TYR THR ASP ASN          
SEQRES  11 A  271  SER ILE ARG PRO GLU GLU LEU LEU GLN MET GLU LEU LEU          
SEQRES  12 A  271  LEU VAL ASN LYS LEU LYS TRP ASN LEU ALA ALA MET THR          
SEQRES  13 A  271  PRO HIS ASP PHE ILE GLU HIS PHE LEU SER LYS MET PRO          
SEQRES  14 A  271  GLU ALA GLU GLU ASN LYS GLN ILE ILE ARG LYS HIS ALA          
SEQRES  15 A  271  GLN THR PHE VAL ALA LEU CYS ALA THR ASP VAL LYS PHE          
SEQRES  16 A  271  ILE SER ASN PRO PRO SER MET VAL ALA ALA GLY SER VAL          
SEQRES  17 A  271  VAL ALA ALA VAL GLN GLY LEU ASN LEU ARG SER PRO ASN          
SEQRES  18 A  271  ASN PHE LEU SER TYR TYR ARG LEU THR ARG PHE LEU SER          
SEQRES  19 A  271  ARG VAL ILE LYS CYS ASP PRO ASP CYS LEU ARG ALA CYS          
SEQRES  20 A  271  GLN GLU GLN ILE GLU ALA LEU LEU GLU SER SER LEU ARG          
SEQRES  21 A  271  GLN ALA GLN GLN ASN MET ASP PRO LYS ALA ALA                  
SEQRES   1 B  306  MET ALA THR SER ARG TYR GLU PRO VAL ALA GLU ILE GLY          
SEQRES   2 B  306  VAL GLY ALA TYR GLY THR VAL TYR LYS ALA ARG ASP PRO          
SEQRES   3 B  306  HIS SER GLY HIS PHE VAL ALA LEU LYS SER VAL ARG VAL          
SEQRES   4 B  306  PRO ASN GLY GLU GLU GLY LEU PRO ILE SER THR VAL ARG          
SEQRES   5 B  306  GLU VAL ALA LEU LEU ARG ARG LEU GLU ALA PHE GLU HIS          
SEQRES   6 B  306  PRO ASN VAL VAL ARG LEU MET ASP VAL CYS ALA THR SER          
SEQRES   7 B  306  ARG THR ASP ARG GLU ILE LYS VAL THR LEU VAL PHE GLU          
SEQRES   8 B  306  HIS VAL ASP GLN ASP LEU ARG THR TYR LEU ASP LYS ALA          
SEQRES   9 B  306  PRO PRO PRO GLY LEU PRO ALA GLU THR ILE LYS ASP LEU          
SEQRES  10 B  306  MET ARG GLN PHE LEU ARG GLY LEU ASP PHE LEU HIS ALA          
SEQRES  11 B  306  ASN CYS ILE VAL HIS ARG ASP LEU LYS PRO GLU ASN ILE          
SEQRES  12 B  306  LEU VAL THR SER GLY GLY THR VAL LYS LEU ALA ASP PHE          
SEQRES  13 B  306  GLY LEU ALA ARG ILE TYR SER TYR GLN MET ALA LEU PHE          
SEQRES  14 B  306  PRO VAL VAL VAL THR LEU TRP TYR ARG ALA PRO GLU VAL          
SEQRES  15 B  306  LEU LEU GLN SER THR TYR ALA THR PRO VAL ASP MET TRP          
SEQRES  16 B  306  SER VAL GLY CYS ILE PHE ALA GLU MET PHE ARG ARG LYS          
SEQRES  17 B  306  PRO LEU PHE CYS GLY ASN SER GLU ALA ASP GLN LEU GLY          
SEQRES  18 B  306  LYS ILE PHE ASP LEU ILE GLY LEU PRO PRO GLU ASP ASP          
SEQRES  19 B  306  TRP PRO ARG ASP VAL SER LEU PRO ARG GLY ALA PHE PRO          
SEQRES  20 B  306  PRO ARG GLY PRO ARG PRO VAL GLN SER VAL VAL PRO GLU          
SEQRES  21 B  306  MET GLU GLU SER GLY ALA GLN LEU LEU LEU GLU MET LEU          
SEQRES  22 B  306  THR PHE ASN PRO HIS LYS ARG ILE SER ALA PHE ARG ALA          
SEQRES  23 B  306  LEU GLN HIS SER TYR LEU HIS LYS ASP GLU GLY ASN PRO          
SEQRES  24 B  306  GLU HIS HIS HIS HIS HIS HIS                                  
FORMUL   3  HOH   *70(H2 O)                                                     
HELIX    1   1 VAL A   27  CYS A   38  1                                  12    
HELIX    2   2 SER A   43  VAL A   48  1                                   6    
HELIX    3   3 LEU A   53  GLN A   71  1                                  19    
HELIX    4   4 GLU A   76  LEU A   89  1                                  14    
HELIX    5   5 ARG A   98  GLU A  115  1                                  18    
HELIX    6   6 THR A  120  TYR A  127  1                                   8    
HELIX    7   7 ARG A  133  LEU A  148  1                                  16    
HELIX    8   8 THR A  156  SER A  166  1                                  11    
HELIX    9   9 ALA A  171  THR A  191  1                                  21    
HELIX   10  10 VAL A  193  ASN A  198  1                                   6    
HELIX   11  11 PRO A  199  SER A  219  1                                  21    
HELIX   12  12 PHE A  223  TYR A  227  5                                   5    
HELIX   13  13 ARG A  228  LYS A  238  1                                  11    
HELIX   14  14 ASP A  240  SER A  257  1                                  18    
HELIX   15  15 PRO B   50  LEU B   63  1                                  14    
HELIX   16  16 GLU B   64  GLU B   67  5                                   4    
HELIX   17  17 ASP B   99  ALA B  107  1                                   9    
HELIX   18  18 THR B  116  ASN B  134  1                                  19    
HELIX   19  19 GLY B  160  ILE B  164  5                                   5    
HELIX   20  20 PRO B  194  MET B  207  1                                  14    
HELIX   21  21 SER B  218  ILE B  230  1                                  13    
HELIX   22  22 GLU B  266  LEU B  276  1                                  11    
HELIX   23  23 SER B  285  GLN B  291  1                                   7    
SHEET    1  BA 5 GLU B   7  GLY B  15  0                                        
SHEET    2  BA 5 GLY B  18  ARG B  24 -1  O  GLY B  18   N  GLY B  15           
SHEET    3  BA 5 PHE B  31  VAL B  39 -1  O  VAL B  32   N  ALA B  23           
SHEET    4  BA 5 ILE B  87  GLU B  94 -1  O  ILE B  87   N  VAL B  39           
SHEET    5  BA 5 ASP B  76  ALA B  79 -1  O  ASP B  76   N  VAL B  92           
SHEET    1  BB 2 LEU B 147  VAL B 148  0                                        
SHEET    2  BB 2 VAL B 154  LYS B 155 -1  O  LYS B 155   N  LEU B 147           
CISPEP   1 PRO B  109    PRO B  110          0         4.04                     
CISPEP   2 LEU B  112    PRO B  113          0         0.82                     
CISPEP   3 VAL B  185    LEU B  186          0       -21.66                     
CRYST1   58.000   64.277  187.617  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017241  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015558  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005330        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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