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Database: PDB
Entry: 1XO2
LinkDB: 1XO2
Original site: 1XO2 
HEADER    CELL CYCLE/TRANSFERASE                  05-OCT-04   1XO2              
TITLE     CRYSTAL STRUCTURE OF A HUMAN CYCLIN-DEPENDENT KINASE 6 COMPLEX WITH A 
TITLE    2 FLAVONOL INHIBITOR, FISETIN                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN;                                                    
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 SYNONYM: SERINE/THREONINE-PROTEIN KINASE PLSTIRE;                    
COMPND  10 EC: 2.7.1.37;                                                        
COMPND  11 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 GENE: 72, ECLF2;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF-9;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBACHTA;                              
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: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: SF-9;                                   
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1                                 
KEYWDS    CRYSTAL STRUCTURE,HUMAN CYCLIN-DEPENDENT KINASE 6, FISETIN, CELL      
KEYWDS   2 CYCLE-TRANSFERASE COMPLEX                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.S.LU,D.J.CHANG,B.BARATTE,L.MEIJER,U.SCHULZE-GAHMEN                  
REVDAT   4   13-JUL-11 1XO2    1       VERSN                                    
REVDAT   3   08-DEC-10 1XO2    1       HETSYN                                   
REVDAT   2   24-FEB-09 1XO2    1       VERSN                                    
REVDAT   1   01-MAR-05 1XO2    0                                                
JRNL        AUTH   H.S.LU,D.J.CHANG,B.BARATTE,L.MEIJER,U.SCHULZE-GAHMEN         
JRNL        TITL   CRYSTAL STRUCTURE OF A HUMAN CYCLIN-DEPENDENT KINASE 6       
JRNL        TITL 2 COMPLEX WITH A FLAVONOL INHIBITOR, FISETIN.                  
JRNL        REF    J.MED.CHEM.                   V.  48   737 2005              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   15689157                                                     
JRNL        DOI    10.1021/JM049353P                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 12984                          
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) : 0.260                           
REMARK   3   FREE R VALUE                     : 0.313                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 952                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4151                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 50.00                          
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.38                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : 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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1XO2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-OCT-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030566.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-04                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14353                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.5                               
REMARK 200  DATA REDUNDANCY                : 8.160                              
REMARK 200  R MERGE                    (I) : 0.12200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.73000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
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: PDB ENTRY 1JOW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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      299.06400            
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      149.53200            
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      224.29800            
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       74.76600            
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      373.83000            
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      299.06400            
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      149.53200            
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       74.76600            
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      224.29800            
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      373.83000            
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: 4880 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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     ASP B    10                                                      
REMARK 465     THR B    88                                                      
REMARK 465     ASP B    89                                                      
REMARK 465     ARG B    90                                                      
REMARK 465     SER B   256                                                      
REMARK 465     LYS B   257                                                      
REMARK 465     SER B   258                                                      
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     LYS A  12    CG   CD   CE   NZ                                   
REMARK 470     ILE A  13    CG1  CG2  CD1                                       
REMARK 470     LEU A 130    CG   CD1  CD2                                       
REMARK 470     ASN A 213    CG   OD1                                            
REMARK 470     TYR B  24    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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     ARG B  46    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 245    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 246    CG   OD1  OD2                                       
REMARK 470     VAL B 247    CG1  CG2                                            
REMARK 470     LEU B 249    CG   CD1  CD2                                       
REMARK 470     PRO B 250    CG   CD                                             
REMARK 470     ARG B 251    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 263    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 264    CG   CD   CE   NZ                                   
REMARK 470     GLN B 301    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 302    CG   OD1  OD2                                       
REMARK 470     LEU B 303    CG   CD1  CD2                                       
REMARK 470     GLU B 304    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 305    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A  13     -164.67   -100.19                                   
REMARK 500    ASP A  20      -19.95   -163.59                                   
REMARK 500    PRO A  21      -96.77    -84.55                                   
REMARK 500    ARG A  22       45.32   -145.11                                   
REMARK 500    LEU A  32       32.35    -71.06                                   
REMARK 500    LYS A  36      -73.54    -76.86                                   
REMARK 500    PHE A  37      -30.11     60.90                                   
REMARK 500    TYR A 121      -19.12    -44.20                                   
REMARK 500    ASN A 129       47.41    -71.56                                   
REMARK 500    LEU A 130      -11.27   -157.99                                   
REMARK 500    TRP A 145        4.87     59.20                                   
REMARK 500    GLU A 148      170.73    -53.86                                   
REMARK 500    LEU A 193      155.10    -49.14                                   
REMARK 500    GLU A 208      -83.39    -54.34                                   
REMARK 500    THR A 209       38.81    -58.11                                   
REMARK 500    ASP A 210       90.22    168.17                                   
REMARK 500    THR A 212       49.67   -102.51                                   
REMARK 500    ARG A 215      153.13    -44.61                                   
REMARK 500    PRO A 216      130.88    -33.10                                   
REMARK 500    THR A 218       36.32    -75.89                                   
REMARK 500    ASN A 229       -0.19     74.20                                   
REMARK 500    SER A 231     -159.30    -78.28                                   
REMARK 500    ALA B  17      148.78    177.72                                   
REMARK 500    ARG B  38      136.61    -21.25                                   
REMARK 500    THR B  49       47.16    -68.26                                   
REMARK 500    GLU B  51        2.56    168.67                                   
REMARK 500    GLU B  69      -57.87    -29.68                                   
REMARK 500    THR B  70      -37.36    -36.06                                   
REMARK 500    GLU B  72       45.12     38.99                                   
REMARK 500    LEU B 109       20.67    -69.97                                   
REMARK 500    ASP B 110      -59.10   -133.03                                   
REMARK 500    LYS B 111       11.78    -65.42                                   
REMARK 500    THR B 119      -25.36    -36.87                                   
REMARK 500    ARG B 144       22.20    -67.33                                   
REMARK 500    ASP B 145       48.83   -144.87                                   
REMARK 500    ASP B 163       74.76     59.21                                   
REMARK 500    VAL B 180      150.39    164.80                                   
REMARK 500    VAL B 181       88.21     92.32                                   
REMARK 500    THR B 182      -70.63      8.61                                   
REMARK 500    LEU B 183      -58.48    166.09                                   
REMARK 500    TRP B 184        1.58    -64.29                                   
REMARK 500    GLN B 193       40.45     78.33                                   
REMARK 500    ALA B 197     -140.18   -162.78                                   
REMARK 500    PHE B 213      -77.67    -67.29                                   
REMARK 500    ARG B 215       51.21    -68.86                                   
REMARK 500    PRO B 217      131.37    -37.88                                   
REMARK 500    ASP B 233       -9.78    -47.92                                   
REMARK 500    PRO B 238     -164.90    -57.84                                   
REMARK 500    GLU B 240        4.35    -53.88                                   
REMARK 500    ALA B 248     -146.51     82.22                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      56 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FSE B 309                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JOW   RELATED DB: PDB                                   
DBREF  1XO2 A    1   254  UNP    Q01043   CGH2_SHV21       1    254             
DBREF  1XO2 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                          
HET    FSE  B 309      21                                                       
HETNAM     FSE 3,7,3',4'-TETRAHYDROXYFLAVONE                                    
HETSYN     FSE FISETIN, 2-(3,4-DIHYDROXYPHENYL)-3,7-DIHYDROXY-4H-               
HETSYN   2 FSE  CHROMEN-4-ONE                                                   
FORMUL   3  FSE    C15 H10 O6                                                   
HELIX    1   1 ARG A   22  LEU A   32  1                                  11    
HELIX    2   2 THR A   48  PHE A   66  1                                  19    
HELIX    3   3 VAL A   72  LYS A   87  1                                  16    
HELIX    4   4 THR A   93  THR A  110  1                                  18    
HELIX    5   5 THR A  115  TYR A  121  1                                   7    
HELIX    6   6 LEU A  130  LEU A  143  1                                  14    
HELIX    7   7 LEU A  151  ASP A  154  5                                   4    
HELIX    8   8 PHE A  155  LEU A  163  1                                   9    
HELIX    9   9 LEU A  169  GLN A  187  1                                  19    
HELIX   10  10 PRO A  188  ALA A  191  5                                   4    
HELIX   11  11 SER A  194  THR A  209  1                                  16    
HELIX   12  12 PRO A  216  CYS A  219  5                                   4    
HELIX   13  13 TYR A  220  ASN A  229  1                                  10    
HELIX   14  14 SER A  231  TYR A  249  1                                  19    
HELIX   15  15 ASP A  250  LEU A  254  5                                   5    
HELIX   16  16 PRO B   55  GLU B   69  1                                  15    
HELIX   17  17 THR B   70  GLU B   72  5                                   3    
HELIX   18  18 LEU B  105  LEU B  109  1                                   5    
HELIX   19  19 GLU B  120  HIS B  139  1                                  20    
HELIX   20  20 LYS B  147  GLN B  149  5                                   3    
HELIX   21  21 ALA B  187  LEU B  192  1                                   6    
HELIX   22  22 THR B  198  ARG B  214  1                                  17    
HELIX   23  23 SER B  223  GLY B  236  1                                  14    
HELIX   24  24 PRO B  261  PHE B  265  5                                   5    
HELIX   25  25 LEU B  272  LEU B  281  1                                  10    
HELIX   26  26 ASN B  284  ARG B  288  5                                   5    
HELIX   27  27 SER B  290  LEU B  295  1                                   6    
HELIX   28  28 SER B  296  GLN B  301  5                                   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 5 TYR B  13  GLU B  21  0                                        
SHEET    2   B 5 LYS B  26  ASP B  32 -1  O  VAL B  27   N  ILE B  19           
SHEET    3   B 5 VAL B  40  VAL B  47 -1  O  LEU B  42   N  PHE B  28           
SHEET    4   B 5 THR B  92  GLU B  99 -1  O  PHE B  98   N  ALA B  41           
SHEET    5   B 5 LEU B  79  VAL B  85 -1  N  CYS B  83   O  THR B  95           
SHEET    1   C 3 GLN B 103  ASP B 104  0                                        
SHEET    2   C 3 ILE B 151  VAL B 153 -1  O  VAL B 153   N  GLN B 103           
SHEET    3   C 3 ILE B 159  LEU B 161 -1  O  LYS B 160   N  LEU B 152           
SHEET    1   D 2 VAL B 141  VAL B 142  0                                        
SHEET    2   D 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         0.04                     
SITE     1 AC1 12 ILE B  19  ALA B  41  LYS B  43  GLU B  61                    
SITE     2 AC1 12 PHE B  98  GLU B  99  HIS B 100  VAL B 101                    
SITE     3 AC1 12 ASP B 104  GLN B 149  LEU B 152  ASP B 163                    
CRYST1   66.162   66.162  448.596  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      0.015114  0.008726  0.000000        0.00000                         
SCALE2      0.000000  0.017453  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002229        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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