GenomeNet

Database: PDB
Entry: 1BLX
LinkDB: 1BLX
Original site: 1BLX 
HEADER    COMPLEX (INHIBITOR PROTEIN/KINASE)      21-JUL-98   1BLX              
TITLE     P19INK4D/CDK6 COMPLEX                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 6;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: P19INK4D;                                                  
COMPND   7 CHAIN: B;                                                            
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: SF9;                                                      
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  10 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: GST FUSION;                           
SOURCE  12 EXPRESSION_SYSTEM_VECTOR: GST-CDK6 BACULOVIRUS;                      
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: GST FUSION PLASMID;                       
SOURCE  14 MOL_ID: 2;                                                           
SOURCE  15 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  16 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  17 ORGANISM_TAXID: 10090;                                               
SOURCE  18 CELL_LINE: SF9;                                                      
SOURCE  19 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  21 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  22 EXPRESSION_SYSTEM_VECTOR_TYPE: GST FUSION;                           
SOURCE  23 EXPRESSION_SYSTEM_PLASMID: GST FUSION PLASMID                        
KEYWDS    INHIBITOR PROTEIN, CYCLIN-DEPENDENT KINASE, CELL CYCLE                
KEYWDS   2 CONTROL, ALPHA/BETA, COMPLEX (INHIBITOR PROTEIN/KINASE)              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.H.BROTHERTON,V.DHANARAJ,S.WICK,L.BRIZUELA,P.J.DOMAILLE,             
AUTHOR   2 E.VOLYANIK,X.XU,E.PARISINI,B.O.SMITH,S.J.ARCHER,M.SERRANO,           
AUTHOR   3 S.L.BRENNER,T.L.BLUNDELL,E.D.LAUE                                    
REVDAT   4   24-FEB-09 1BLX    1       VERSN                                    
REVDAT   3   04-AUG-99 1BLX    1       COMPND                                   
REVDAT   2   08-JUN-99 1BLX    1       COMPND                                   
REVDAT   1   01-JUN-99 1BLX    0                                                
JRNL        AUTH   D.H.BROTHERTON,V.DHANARAJ,S.WICK,L.BRIZUELA,                 
JRNL        AUTH 2 P.J.DOMAILLE,E.VOLYANIK,X.XU,E.PARISINI,B.O.SMITH,           
JRNL        AUTH 3 S.J.ARCHER,M.SERRANO,S.L.BRENNER,T.L.BLUNDELL,               
JRNL        AUTH 4 E.D.LAUE                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF THE COMPLEX OF THE CYCLIN               
JRNL        TITL 2 D-DEPENDENT KINASE CDK6 BOUND TO THE CELL-CYCLE              
JRNL        TITL 3 INHIBITOR P19INK4D.                                          
JRNL        REF    NATURE                        V. 395   244 1998              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   9751051                                                      
JRNL        DOI    10.1038/26164                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   D.H.BROTHERTON,V.DHANARAJ,S.WICK,L.BRIZUELA,                 
REMARK   1  AUTH 2 P.J.DOMAILLE,E.VOLYANIK,X.XU,E.PARISINI,B.O.SMITH,           
REMARK   1  AUTH 3 S.J.ARCHER,M.SERRANO,S.L.BRENNER,T.L.BLUNDELL,               
REMARK   1  AUTH 4 E.D.LAUE                                                     
REMARK   1  TITL   ERRATUM. CRYSTAL STRUCTURE OF THE COMPLEX OF THE             
REMARK   1  TITL 2 CYCLIN D-DEPENDENT KINASE CDK6 BOUND TO THE                  
REMARK   1  TITL 3 CELL-CYCLE INHIBITOR P19INK4D                                
REMARK   1  REF    NATURE                        V. 396   390 1998              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 41965                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R                          
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3565                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 294                                     
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1BLX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : FEB-98                             
REMARK 200  TEMPERATURE           (KELVIN) : 279                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9475                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41965                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 18.540                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : 0.05400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.32700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRIES 1HCK AND 1AP7                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5                                   
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       37.10500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.90000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.20500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       46.90000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.10500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.20500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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     GLU A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     LEU A   310                                                      
REMARK 465     ASP A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     HIS A   313                                                      
REMARK 465     LEU A   314                                                      
REMARK 465     PRO A   315                                                      
REMARK 465     PRO A   316                                                      
REMARK 465     SER A   317                                                      
REMARK 465     GLN A   318                                                      
REMARK 465     ASN A   319                                                      
REMARK 465     THR A   320                                                      
REMARK 465     SER A   321                                                      
REMARK 465     GLU A   322                                                      
REMARK 465     LEU A   323                                                      
REMARK 465     ASN A   324                                                      
REMARK 465     THR A   325                                                      
REMARK 465     ALA A   326                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LEU B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     MET B   166                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU A   6    CG   CD1  CD2                                       
REMARK 470     ARG A   8    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A  48    CG   CD   OE1  NE2                                  
REMARK 470     THR A  49    OG1  CG2                                            
REMARK 470     GLU A  51    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  52    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 168    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 172    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A 173    CG   CD   OE1  NE2                                  
REMARK 470     MET A 174    CG   SD   CE                                        
REMARK 470     LEU A 176    CG   CD1  CD2                                       
REMARK 470     GLU A 240    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 241    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 251    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 308    CG   CD   OE1  OE2                                  
REMARK 470     VAL B   6    CG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   510     O    HOH B   188     3556     1.80            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PRO B 165   CD    PRO B 165   N       0.107                       
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    ARG A  31   CD  -  NE  -  CZ  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    ARG A  31   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    ARG A  60   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG A  60   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG A  60   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    GLU A  69   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    VAL A  77   N   -  CA  -  CB  ANGL. DEV. = -15.5 DEGREES          
REMARK 500    VAL A  77   CG1 -  CB  -  CG2 ANGL. DEV. =  18.0 DEGREES          
REMARK 500    ARG A  78   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ASP A  81   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A  81   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    ASP A 102   CB  -  CG  -  OD2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    ASP A 110   CB  -  CG  -  OD2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ARG A 131   CD  -  NE  -  CZ  ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ARG A 131   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    THR A 154   N   -  CA  -  CB  ANGL. DEV. = -15.1 DEGREES          
REMARK 500    THR A 154   OG1 -  CB  -  CG2 ANGL. DEV. =  20.8 DEGREES          
REMARK 500    VAL A 200   CA  -  CB  -  CG1 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ARG A 214   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP A 246   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A 246   CB  -  CG  -  OD2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    ASP A 275   CB  -  CG  -  OD2 ANGL. DEV. =   9.0 DEGREES          
REMARK 500    ILE A 289   CB  -  CA  -  C   ANGL. DEV. = -14.3 DEGREES          
REMARK 500    ILE A 289   CA  -  CB  -  CG2 ANGL. DEV. =  12.8 DEGREES          
REMARK 500    TYR A 299   CB  -  CG  -  CD2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    TYR A 299   CB  -  CG  -  CD1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ASP B  20   CB  -  CG  -  OD2 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    GLU B  23   OE1 -  CD  -  OE2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ARG B  25   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG B  26   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B  40   CD  -  NE  -  CZ  ANGL. DEV. =  42.0 DEGREES          
REMARK 500    ARG B  40   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    LEU B  60   CA  -  CB  -  CG  ANGL. DEV. =  17.9 DEGREES          
REMARK 500    ARG B  83   CD  -  NE  -  CZ  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    ARG B  83   NH1 -  CZ  -  NH2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ARG B  83   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    THR B  84   N   -  CA  -  CB  ANGL. DEV. = -18.7 DEGREES          
REMARK 500    THR B  84   OG1 -  CB  -  CG2 ANGL. DEV. =  18.0 DEGREES          
REMARK 500    ASP B  88   CB  -  CG  -  OD1 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    ARG B 116   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    HIS B 133   CA  -  CB  -  CG  ANGL. DEV. = -10.5 DEGREES          
REMARK 500    ARG B 147   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    PRO B 165   CA  -  N   -  CD  ANGL. DEV. =  -8.4 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    LEU A   6      -20.25   -169.83                                   
REMARK 500    ASN A  35       50.17   -118.87                                   
REMARK 500    ASP A 102       42.33    -85.66                                   
REMARK 500    ARG A 144      -18.06     83.55                                   
REMARK 500    ASP A 145       47.47   -140.27                                   
REMARK 500    PHE A 172       97.26    -45.56                                   
REMARK 500    GLN A 173       69.65      0.12                                   
REMARK 500    ALA A 175        8.79     85.04                                   
REMARK 500    LEU A 176       -2.81     88.37                                   
REMARK 500    SER A 178       99.15     63.54                                   
REMARK 500    ALA A 197     -149.35   -143.45                                   
REMARK 500    ARG A 220       77.96   -108.47                                   
REMARK 500    ASP A 268      -10.29     88.20                                   
REMARK 500    LEU A 281       49.04    -88.02                                   
REMARK 500    ASP A 302       40.77    -93.10                                   
REMARK 500    CYS A 306       92.40     66.73                                   
REMARK 500    LYS A 307     -141.09    -88.22                                   
REMARK 500    MET B  50      104.20    -59.44                                   
REMARK 500    ALA B  72      -73.91    -44.06                                   
REMARK 500    MET B 163       61.55   -113.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ILE B 164        -10.02                                           
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 B 254        DISTANCE =  5.23 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A   0  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  69   OE2                                                    
REMARK 620 2 GLU A  72   OE2  98.6                                              
REMARK 620 3 HOH A 477   O    86.9  92.0                                        
REMARK 620 4 HOH A 327   O   101.3  82.1 170.5                                  
REMARK 620 5 HOH A 392   O   166.0  93.9  86.5  86.4                            
REMARK 620 6 HOH A 349   O    78.3 167.8  99.6  86.9  90.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CAB                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE                               
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 0                    
DBREF  1BLX A    1   326  UNP    Q00534   CDK6_HUMAN       1    326             
DBREF  1BLX B    1   166  UNP    Q60773   CDN2D_MOUSE      1    166             
SEQADV 1BLX ALA B   16  UNP  Q60773    ARG    16 VARIANT                        
SEQRES   1 A  326  MET GLU LYS ASP GLY LEU CYS ARG ALA ASP GLN GLN TYR          
SEQRES   2 A  326  GLU CYS VAL ALA GLU ILE GLY GLU GLY ALA TYR GLY LYS          
SEQRES   3 A  326  VAL PHE LYS ALA ARG ASP LEU LYS ASN GLY GLY ARG PHE          
SEQRES   4 A  326  VAL ALA LEU LYS ARG VAL ARG VAL GLN THR GLY GLU GLU          
SEQRES   5 A  326  GLY MET PRO LEU SER THR ILE ARG GLU VAL ALA VAL LEU          
SEQRES   6 A  326  ARG HIS LEU GLU THR PHE GLU HIS PRO ASN VAL VAL ARG          
SEQRES   7 A  326  LEU PHE ASP VAL CYS THR VAL SER ARG THR ASP ARG GLU          
SEQRES   8 A  326  THR LYS LEU THR LEU VAL PHE GLU HIS VAL ASP GLN ASP          
SEQRES   9 A  326  LEU THR THR TYR LEU ASP LYS VAL PRO GLU PRO GLY VAL          
SEQRES  10 A  326  PRO THR GLU THR ILE LYS ASP MET MET PHE GLN LEU LEU          
SEQRES  11 A  326  ARG GLY LEU ASP PHE LEU HIS SER HIS ARG VAL VAL HIS          
SEQRES  12 A  326  ARG ASP LEU LYS PRO GLN ASN ILE LEU VAL THR SER SER          
SEQRES  13 A  326  GLY GLN ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ILE          
SEQRES  14 A  326  TYR SER PHE GLN MET ALA LEU THR SER VAL VAL VAL THR          
SEQRES  15 A  326  LEU TRP TYR ARG ALA PRO GLU VAL LEU LEU GLN SER SER          
SEQRES  16 A  326  TYR ALA THR PRO VAL ASP LEU TRP SER VAL GLY CYS ILE          
SEQRES  17 A  326  PHE ALA GLU MET PHE ARG ARG LYS PRO LEU PHE ARG GLY          
SEQRES  18 A  326  SER SER ASP VAL ASP GLN LEU GLY LYS ILE LEU ASP VAL          
SEQRES  19 A  326  ILE GLY LEU PRO GLY GLU GLU ASP TRP PRO ARG ASP VAL          
SEQRES  20 A  326  ALA LEU PRO ARG GLN ALA PHE HIS SER LYS SER ALA GLN          
SEQRES  21 A  326  PRO ILE GLU LYS PHE VAL THR ASP ILE ASP GLU LEU GLY          
SEQRES  22 A  326  LYS ASP LEU LEU LEU LYS CYS LEU THR PHE ASN PRO ALA          
SEQRES  23 A  326  LYS ARG ILE SER ALA TYR SER ALA LEU SER HIS PRO TYR          
SEQRES  24 A  326  PHE GLN ASP LEU GLU ARG CYS LYS GLU ASN LEU ASP SER          
SEQRES  25 A  326  HIS LEU PRO PRO SER GLN ASN THR SER GLU LEU ASN THR          
SEQRES  26 A  326  ALA                                                          
SEQRES   1 B  166  MET LEU LEU GLU GLU VAL CYS VAL GLY ASP ARG LEU SER          
SEQRES   2 B  166  GLY ALA ALA ALA ARG GLY ASP VAL GLN GLU VAL ARG ARG          
SEQRES   3 B  166  LEU LEU HIS ARG GLU LEU VAL HIS PRO ASP ALA LEU ASN          
SEQRES   4 B  166  ARG PHE GLY LYS THR ALA LEU GLN VAL MET MET PHE GLY          
SEQRES   5 B  166  SER PRO ALA VAL ALA LEU GLU LEU LEU LYS GLN GLY ALA          
SEQRES   6 B  166  SER PRO ASN VAL GLN ASP ALA SER GLY THR SER PRO VAL          
SEQRES   7 B  166  HIS ASP ALA ALA ARG THR GLY PHE LEU ASP THR LEU LYS          
SEQRES   8 B  166  VAL LEU VAL GLU HIS GLY ALA ASP VAL ASN ALA LEU ASP          
SEQRES   9 B  166  SER THR GLY SER LEU PRO ILE HIS LEU ALA ILE ARG GLU          
SEQRES  10 B  166  GLY HIS SER SER VAL VAL SER PHE LEU ALA PRO GLU SER          
SEQRES  11 B  166  ASP LEU HIS HIS ARG ASP ALA SER GLY LEU THR PRO LEU          
SEQRES  12 B  166  GLU LEU ALA ARG GLN ARG GLY ALA GLN ASN LEU MET ASP          
SEQRES  13 B  166  ILE LEU GLN GLY HIS MET MET ILE PRO MET                      
HET     CA  A   0       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  HOH   *294(H2 O)                                                    
HELIX    1   1 ALA A    9  GLN A   11  5                                   3    
HELIX    2   2 SER A   57  PHE A   71  5                                  15    
HELIX    3   3 LEU A  105  LYS A  111  1                                   7    
HELIX    4   4 THR A  119  HIS A  139  1                                  21    
HELIX    5   5 PRO A  148  ASN A  150  5                                   3    
HELIX    6   6 PHE A  172  LEU A  176  5                                   5    
HELIX    7   7 PRO A  188  LEU A  191  1                                   4    
HELIX    8   8 THR A  198  ARG A  214  5                                  17    
HELIX    9   9 ASP A  224  ILE A  235  1                                  12    
HELIX   10  10 GLU A  240  ASP A  242  5                                   3    
HELIX   11  11 ARG A  251  ALA A  253  5                                   3    
HELIX   12  12 ILE A  262  LYS A  264  5                                   3    
HELIX   13  13 GLU A  271  CYS A  280  1                                  10    
HELIX   14  14 ALA A  291  LEU A  295  1                                   5    
HELIX   15  15 PRO A  298  PHE A  300  5                                   3    
HELIX   16  16 CYS B    7  ALA B   17  1                                  11    
HELIX   17  17 VAL B   21  HIS B   29  1                                   9    
HELIX   18  18 ALA B   45  VAL B   48  1                                   4    
HELIX   19  19 PRO B   54  LYS B   62  1                                   9    
HELIX   20  20 PRO B   77  THR B   84  1                                   8    
HELIX   21  21 LEU B   87  GLU B   95  1                                   9    
HELIX   22  22 PRO B  110  GLU B  117  1                                   8    
HELIX   23  23 SER B  120  GLU B  129  1                                  10    
HELIX   24  24 PRO B  142  ARG B  149  1                                   8    
HELIX   25  25 GLN B  152  HIS B  161  1                                  10    
SHEET    1   A 5 GLY A  20  GLY A  22  0                                        
SHEET    2   A 5 GLY A  25  ASP A  32 -1  N  VAL A  27   O  GLY A  20           
SHEET    3   A 5 ARG A  38  GLN A  48 -1  N  LEU A  42   O  PHE A  28           
SHEET    4   A 5 GLU A  91  GLU A  99 -1  N  PHE A  98   O  ALA A  41           
SHEET    5   A 5 LEU A  79  THR A  84 -1  N  CYS A  83   O  THR A  95           
SHEET    1   B 2 ILE A 151  VAL A 153  0                                        
SHEET    2   B 2 ILE A 159  LEU A 161 -1  N  LYS A 160   O  LEU A 152           
SHEET    1   C 2 TYR A  13  GLU A  18  0                                        
SHEET    2   C 2 PHE A  28  ASP A  32 -1  N  ARG A  31   O  GLU A  14           
LINK        CA    CA A   0                 OE2 GLU A  69     1555   1555  2.39  
LINK        CA    CA A   0                 OE2 GLU A  72     1555   1555  2.30  
LINK        CA    CA A   0                 O   HOH A 477     1555   1555  2.35  
LINK        CA    CA A   0                 O   HOH A 327     1555   1555  2.47  
LINK        CA    CA A   0                 O   HOH A 392     1555   1555  2.45  
LINK        CA    CA A   0                 O   HOH A 349     1555   1555  2.67  
CISPEP   1 GLU A  114    PRO A  115          0         1.95                     
SITE     1 CAB  2 GLU A  69  GLU A  72                                          
SITE     1 AC1  6 GLU A  69  GLU A  72  HOH A 327  HOH A 349                    
SITE     2 AC1  6 HOH A 392  HOH A 477                                          
CRYST1   74.210   76.410   93.800  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      0.013475  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013087  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010661        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system