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Database: PDB
Entry: 1JOW
LinkDB: 1JOW
Original site: 1JOW 
HEADER    CELL CYCLE/TRANSFERASE                  31-JUL-01   1JOW              
TITLE     CRYSTAL STRUCTURE OF A COMPLEX OF HUMAN CDK6 AND A VIRAL              
TITLE    2 CYCLIN                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN HOMOLOG;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: V-CYCLIN;                                                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CELL DIVISION PROTEIN KINASE 6;                            
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: RESIDUES 1-308;                                            
COMPND  10 SYNONYM: CDK6, SERINE/THREONINE-PROTEIN KINASE PLSTIRE;              
COMPND  11 EC: 2.7.1.-;                                                         
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SAIMIRIINE HERPESVIRUS 2;                       
SOURCE   3 ORGANISM_COMMON: HERPESVIRUS SAIMIRI;                                
SOURCE   4 ORGANISM_TAXID: 10381;                                               
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC HTA DONOR PLASMID;               
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: CDK6;                                                          
SOURCE  16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  17 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  19 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1 DONOR PLASMID                   
KEYWDS    CDK-CYCLIN COMPLEX, CYCLIN FOLD, CELL CYCLE/TRANSFERASE               
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.SCHULZE-GAHMEN,S.H.KIM                                              
REVDAT   2   24-FEB-09 1JOW    1       VERSN                                    
REVDAT   1   27-FEB-02 1JOW    0                                                
JRNL        AUTH   U.SCHULZE-GAHMEN,S.H.KIM                                     
JRNL        TITL   STRUCTURAL BASIS FOR CDK6 ACTIVATION BY A                    
JRNL        TITL 2 VIRUS-ENCODED CYCLIN.                                        
JRNL        REF    NAT.STRUCT.BIOL.              V.   9   177 2002              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   11828325                                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   U.SCHULZE-GAHMEN,S.H.KIM                                     
REMARK   1  TITL   CRYSTALLIZATION OF A COMPLEX BETWEEN HUMAN CDK6              
REMARK   1  TITL 2 AND A VIRUS-ENCODED CYCLIN IS CRITICALLY DEPENDENT           
REMARK   1  TITL 3 ON THE ADDITION OF SMALL CHARGED ORGANIC MOLECULES           
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2293632.740                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 12629                          
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 SET) : 0.266                           
REMARK   3   FREE R VALUE                     : 0.323                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 959                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.29                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1675                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3850                       
REMARK   3   BIN FREE R VALUE                    : 0.4510                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 141                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.038                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3986                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 73.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 10.00000                                             
REMARK   3    B22 (A**2) : 10.00000                                             
REMARK   3    B33 (A**2) : -19.99000                                            
REMARK   3    B12 (A**2) : 16.11000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.47                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.61                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.65                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.78                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.93                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : GROUP                                     
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.27                                                 
REMARK   3   BSOL        : 29.99                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1JOW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB014015.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-DEC-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99999                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12783                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 1.0                                
REMARK 200  DATA REDUNDANCY                : 7.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.19                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 0.8                                
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.29000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS/HCL, SODIUM CHLORIDE, PEG           
REMARK 280  3350, CALCIUM ACETATE, PH 8.0, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 295.0K                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      299.18000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      149.59000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      224.38500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       74.79500            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      373.97500            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      299.18000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      149.59000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       74.79500            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      224.38500            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      373.97500            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS THE HETERODIMER IN THE            
REMARK 300 ASYMMETRIC UNIT                                                      
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: 4000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     ASN A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     CYS A   124                                                      
REMARK 465     ASP A   125                                                      
REMARK 465     CYS A   126                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     CYS B     7                                                      
REMARK 465     ARG B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     GLU B    18                                                      
REMARK 465     ILE B    19                                                      
REMARK 465     GLY B    20                                                      
REMARK 465     GLU B    21                                                      
REMARK 465     GLY B    22                                                      
REMARK 465     ALA B    23                                                      
REMARK 465     ARG B   245                                                      
REMARK 465     ASP B   246                                                      
REMARK 465     VAL B   247                                                      
REMARK 465     ALA B   248                                                      
REMARK 465     LEU B   249                                                      
REMARK 465     PRO B   250                                                      
REMARK 465     ARG B   251                                                      
REMARK 465     GLN B   301                                                      
REMARK 465     ASP B   302                                                      
REMARK 465     LEU B   303                                                      
REMARK 465     GLU B   304                                                      
REMARK 465     ARG B   305                                                      
REMARK 465     CYS B   306                                                      
REMARK 465     LYS B   307                                                      
REMARK 465     GLU B   308                                                      
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     ASN A   9    CG   OD1  ND2                                       
REMARK 470     ARG A  10    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  12    CG   CD   CE   NZ                                   
REMARK 470     THR A  17    OG1  CG2                                            
REMARK 470     MET A  18    CG   SD   CE                                        
REMARK 470     GLU A  42    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  92    CG   CD   CE   NZ                                   
REMARK 470     SER A 123    OG                                                  
REMARK 470     ASP A 210    CG   OD1  OD2                                       
REMARK 470     ASN A 211    CG   OD1  ND2                                       
REMARK 470     THR A 212    OG1  CG2                                            
REMARK 470     ASN A 213    CG   OD1  ND2                                       
REMARK 470     ARG A 215    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 221    CG   CD1  CD2                                       
REMARK 470     ASP B  10    CG   OD1  OD2                                       
REMARK 470     GLN B  11    CG   CD   OE1  NE2                                  
REMARK 470     GLN B  12    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  14    CG   CD   OE1  OE2                                  
REMARK 470     CYS B  15    SG                                                  
REMARK 470     VAL B  16    CG1  CG2                                            
REMARK 470     LYS B  26    CG   CD   CE   NZ                                   
REMARK 470     LYS B  29    CG   CD   CE   NZ                                   
REMARK 470     ARG B  31    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B  32    CG   OD1  OD2                                       
REMARK 470     LEU B  33    CG   CD1  CD2                                       
REMARK 470     ASN B  35    CG   OD1  ND2                                       
REMARK 470     ARG B  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B  40    CG1  CG2                                            
REMARK 470     ARG B  44    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  46    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  51    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     CYS B  83    SG                                                  
REMARK 470     ARG B  87    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B  88    OG1  CG2                                            
REMARK 470     ARG B  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B  92    OG1  CG2                                            
REMARK 470     LYS B  93    CG   CD   CE   NZ                                   
REMARK 470     THR B  95    OG1  CG2                                            
REMARK 470     GLN B 103    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 111    CG   CD   CE   NZ                                   
REMARK 470     LEU B 183    CG   CD1  CD2                                       
REMARK 470     GLU B 189    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 252    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 260    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ARG B   214     N    LYS B   216              2.12            
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    LYS A  12      122.84    -39.73                                   
REMARK 500    SER A  15       66.21   -173.78                                   
REMARK 500    THR A  16      -38.48    -25.88                                   
REMARK 500    THR A  17       35.26    -76.91                                   
REMARK 500    MET A  18       -1.94   -172.98                                   
REMARK 500    ARG A  22       78.84    -51.49                                   
REMARK 500    LEU A  32       18.42    -63.06                                   
REMARK 500    GLU A  46      -45.31   -132.75                                   
REMARK 500    LEU A  84       35.86    -80.98                                   
REMARK 500    LYS A  86      -70.55    -66.64                                   
REMARK 500    ILE A  97      -78.56    -45.82                                   
REMARK 500    ILE A 108      -77.41    -72.73                                   
REMARK 500    ASN A 129        2.64    -63.17                                   
REMARK 500    TRP A 145        4.10     50.55                                   
REMARK 500    THR A 147      -64.55    -97.05                                   
REMARK 500    GLU A 148      152.59    -35.20                                   
REMARK 500    GLU A 167      -39.27    -32.35                                   
REMARK 500    LEU A 185      -19.41    -46.56                                   
REMARK 500    GLU A 208       58.38    -93.75                                   
REMARK 500    THR A 209       91.15   -161.35                                   
REMARK 500    ASP A 210       95.30     65.48                                   
REMARK 500    ASN A 211      -36.38    -31.76                                   
REMARK 500    ASN A 213        7.38     86.16                                   
REMARK 500    TRP A 217      -35.71    -34.44                                   
REMARK 500    ASN A 229       72.98     70.69                                   
REMARK 500    LEU A 248        0.97    -54.16                                   
REMARK 500    GLN B  12       65.58   -103.74                                   
REMARK 500    LYS B  34      -83.00    -54.70                                   
REMARK 500    ASN B  35      163.02    -47.20                                   
REMARK 500    ARG B  38      160.41    -43.33                                   
REMARK 500    THR B  49       60.04    -64.69                                   
REMARK 500    GLU B  51       58.98   -165.49                                   
REMARK 500    GLU B  52        0.51   -150.02                                   
REMARK 500    THR B  58       -2.72    -55.72                                   
REMARK 500    ILE B  59      -64.45    -98.49                                   
REMARK 500    CYS B  83      -71.43    -39.53                                   
REMARK 500    THR B  84      105.15     57.94                                   
REMARK 500    ASP B  89      -88.60    -69.09                                   
REMARK 500    PHE B  98     -162.39   -112.16                                   
REMARK 500    LEU B 105      -17.14    -45.24                                   
REMARK 500    PRO B 113      162.92    -46.78                                   
REMARK 500    THR B 119      -14.46    -49.97                                   
REMARK 500    ASP B 163       74.32     45.68                                   
REMARK 500    LEU B 166      -18.02   -145.66                                   
REMARK 500    GLN B 173       15.47     56.03                                   
REMARK 500    VAL B 181      143.48     72.23                                   
REMARK 500    LEU B 183      -62.69     -5.31                                   
REMARK 500    GLN B 193       15.69     54.24                                   
REMARK 500    ALA B 197     -134.72   -166.47                                   
REMARK 500    PRO B 199       -8.65    -53.28                                   
REMARK 500    SER B 204      -11.48    -49.90                                   
REMARK 500    GLU B 211        8.88    -65.73                                   
REMARK 500    ARG B 215       55.54    -38.05                                   
REMARK 500    PRO B 217       93.48    -39.74                                   
REMARK 500    PHE B 219       72.18   -117.08                                   
REMARK 500    VAL B 234      -71.99    -87.10                                   
REMARK 500    SER B 256       57.20   -105.54                                   
REMARK 500    ALA B 259      114.10    -37.32                                   
REMARK 500    PRO B 261      126.36    -28.96                                   
REMARK 500    ASP B 268       82.66     62.10                                   
REMARK 500    LEU B 281       53.36    -99.08                                   
REMARK 500    ARG B 288      113.64    -34.75                                   
REMARK 500    TYR B 292      -70.84    -58.89                                   
REMARK 500    TYR B 299      -16.39    -46.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JST   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1F5Q   RELATED DB: PDB                                   
DBREF  1JOW A    1   254  UNP    Q01043   CGH2_SHV21       1    254             
DBREF  1JOW B    1   308  UNP    Q00534   CDK6_HUMAN       1    308             
SEQRES   1 A  254  MET ALA ASP SER PRO ASN ARG LEU ASN ARG ALA LYS ILE          
SEQRES   2 A  254  ASP SER THR THR MET LYS ASP PRO ARG VAL LEU ASN ASN          
SEQRES   3 A  254  LEU LYS LEU ARG GLU LEU LEU LEU PRO LYS PHE THR SER          
SEQRES   4 A  254  LEU TRP GLU ILE GLN THR GLU VAL THR VAL ASP ASN ARG          
SEQRES   5 A  254  THR ILE LEU LEU THR TRP MET HIS LEU LEU CYS GLU SER          
SEQRES   6 A  254  PHE GLU LEU ASP LYS SER VAL PHE PRO LEU SER VAL SER          
SEQRES   7 A  254  ILE LEU ASP ARG TYR LEU CYS LYS LYS GLN GLY THR LYS          
SEQRES   8 A  254  LYS THR LEU GLN LYS ILE GLY ALA ALA CYS VAL LEU ILE          
SEQRES   9 A  254  GLY SER LYS ILE ARG THR VAL LYS PRO MET THR VAL SER          
SEQRES  10 A  254  LYS LEU THR TYR LEU SER CYS ASP CYS PHE THR ASN LEU          
SEQRES  11 A  254  GLU LEU ILE ASN GLN GLU LYS ASP ILE LEU GLU ALA LEU          
SEQRES  12 A  254  LYS TRP ASP THR GLU ALA VAL LEU ALA THR ASP PHE LEU          
SEQRES  13 A  254  ILE PRO LEU CYS ASN ALA LEU LYS ILE PRO GLU ASP LEU          
SEQRES  14 A  254  TRP PRO GLN LEU TYR GLU ALA ALA SER THR THR ILE CYS          
SEQRES  15 A  254  LYS ALA LEU ILE GLN PRO ASN ILE ALA LEU LEU SER PRO          
SEQRES  16 A  254  GLY LEU ILE CYS ALA GLY GLY LEU LEU THR THR ILE GLU          
SEQRES  17 A  254  THR ASP ASN THR ASN CYS ARG PRO TRP THR CYS TYR LEU          
SEQRES  18 A  254  GLU ASP LEU SER SER ILE LEU ASN PHE SER THR ASN THR          
SEQRES  19 A  254  VAL ARG THR VAL LYS ASP GLN VAL SER GLU ALA PHE SER          
SEQRES  20 A  254  LEU TYR ASP LEU GLU ILE LEU                                  
SEQRES   1 B  308  MET GLU LYS ASP GLY LEU CYS ARG ALA ASP GLN GLN TYR          
SEQRES   2 B  308  GLU CYS VAL ALA GLU ILE GLY GLU GLY ALA TYR GLY LYS          
SEQRES   3 B  308  VAL PHE LYS ALA ARG ASP LEU LYS ASN GLY GLY ARG PHE          
SEQRES   4 B  308  VAL ALA LEU LYS ARG VAL ARG VAL GLN THR GLY GLU GLU          
SEQRES   5 B  308  GLY MET PRO LEU SER THR ILE ARG GLU VAL ALA VAL LEU          
SEQRES   6 B  308  ARG HIS LEU GLU THR PHE GLU HIS PRO ASN VAL VAL ARG          
SEQRES   7 B  308  LEU PHE ASP VAL CYS THR VAL SER ARG THR ASP ARG GLU          
SEQRES   8 B  308  THR LYS LEU THR LEU VAL PHE GLU HIS VAL ASP GLN ASP          
SEQRES   9 B  308  LEU THR THR TYR LEU ASP LYS VAL PRO GLU PRO GLY VAL          
SEQRES  10 B  308  PRO THR GLU THR ILE LYS ASP MET MET PHE GLN LEU LEU          
SEQRES  11 B  308  ARG GLY LEU ASP PHE LEU HIS SER HIS ARG VAL VAL HIS          
SEQRES  12 B  308  ARG ASP LEU LYS PRO GLN ASN ILE LEU VAL THR SER SER          
SEQRES  13 B  308  GLY GLN ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ILE          
SEQRES  14 B  308  TYR SER PHE GLN MET ALA LEU THR SER VAL VAL VAL THR          
SEQRES  15 B  308  LEU TRP TYR ARG ALA PRO GLU VAL LEU LEU GLN SER SER          
SEQRES  16 B  308  TYR ALA THR PRO VAL ASP LEU TRP SER VAL GLY CYS ILE          
SEQRES  17 B  308  PHE ALA GLU MET PHE ARG ARG LYS PRO LEU PHE ARG GLY          
SEQRES  18 B  308  SER SER ASP VAL ASP GLN LEU GLY LYS ILE LEU ASP VAL          
SEQRES  19 B  308  ILE GLY LEU PRO GLY GLU GLU ASP TRP PRO ARG ASP VAL          
SEQRES  20 B  308  ALA LEU PRO ARG GLN ALA PHE HIS SER LYS SER ALA GLN          
SEQRES  21 B  308  PRO ILE GLU LYS PHE VAL THR ASP ILE ASP GLU LEU GLY          
SEQRES  22 B  308  LYS ASP LEU LEU LEU LYS CYS LEU THR PHE ASN PRO ALA          
SEQRES  23 B  308  LYS ARG ILE SER ALA TYR SER ALA LEU SER HIS PRO TYR          
SEQRES  24 B  308  PHE GLN ASP LEU GLU ARG CYS LYS GLU                          
HELIX    1   1 SER A   15  ASP A   20  1                                   6    
HELIX    2   2 VAL A   23  LEU A   32  1                                  10    
HELIX    3   3 THR A   48  PHE A   66  1                                  19    
HELIX    4   4 VAL A   72  LYS A   87  1                                  16    
HELIX    5   5 THR A   90  THR A  110  1                                  21    
HELIX    6   6 VAL A  116  TYR A  121  1                                   6    
HELIX    7   7 LEU A  130  LYS A  144  1                                  15    
HELIX    8   8 LEU A  151  ASP A  154  5                                   4    
HELIX    9   9 PHE A  155  LEU A  163  1                                   9    
HELIX   10  10 PRO A  166  ASP A  168  5                                   3    
HELIX   11  11 LEU A  169  LEU A  185  1                                  17    
HELIX   12  12 ASN A  189  LEU A  193  5                                   5    
HELIX   13  13 SER A  194  GLU A  208  1                                  15    
HELIX   14  14 TRP A  217  ASN A  229  1                                  13    
HELIX   15  15 SER A  231  LEU A  248  1                                  18    
HELIX   16  16 ASP A  250  LEU A  254  5                                   5    
HELIX   17  17 LEU B   56  GLU B   69  1                                  14    
HELIX   18  18 THR B   70  GLU B   72  5                                   3    
HELIX   19  19 LEU B  105  LYS B  111  1                                   7    
HELIX   20  20 PRO B  118  HIS B  139  1                                  22    
HELIX   21  21 LYS B  147  GLN B  149  5                                   3    
HELIX   22  22 THR B  182  ARG B  186  5                                   5    
HELIX   23  23 ALA B  187  LEU B  192  1                                   6    
HELIX   24  24 THR B  198  ARG B  214  1                                  17    
HELIX   25  25 SER B  223  GLY B  236  1                                  14    
HELIX   26  26 PRO B  261  PHE B  265  5                                   5    
HELIX   27  27 ASP B  270  LEU B  281  1                                  12    
HELIX   28  28 SER B  290  LEU B  295  1                                   6    
SHEET    1   A 2 ARG A  10  ALA A  11  0                                        
SHEET    2   A 2 ALA B 175  LEU B 176 -1  O  LEU B 176   N  ARG A  10           
SHEET    1   B 2 TYR B  13  GLU B  14  0                                        
SHEET    2   B 2 ARG B  31  ASP B  32 -1  O  ARG B  31   N  GLU B  14           
SHEET    1   C 4 VAL B  27  PHE B  28  0                                        
SHEET    2   C 4 LEU B  42  LYS B  43 -1  O  LEU B  42   N  PHE B  28           
SHEET    3   C 4 LEU B  96  PHE B  98 -1  O  LEU B  96   N  LYS B  43           
SHEET    4   C 4 LEU B  79  VAL B  82 -1  N  ASP B  81   O  VAL B  97           
SHEET    1   D 3 GLN B 103  ASP B 104  0                                        
SHEET    2   D 3 ILE B 151  VAL B 153 -1  O  VAL B 153   N  GLN B 103           
SHEET    3   D 3 ILE B 159  LEU B 161 -1  O  LYS B 160   N  LEU B 152           
SHEET    1   E 2 VAL B 141  VAL B 142  0                                        
SHEET    2   E 2 ARG B 168  ILE B 169 -1  O  ARG B 168   N  VAL B 142           
CISPEP   1 GLU B  114    PRO B  115          0        -0.21                     
CRYST1   70.140   70.140  448.770  90.00  90.00 120.00 P 65 2 2     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014257  0.008231  0.000000        0.00000                         
SCALE2      0.000000  0.016463  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002228        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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