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Database: PDB
Entry: 1BI7
LinkDB: 1BI7
Original site: 1BI7 
HEADER    COMPLEX (KINASE/ANTI-ONCOGENE)          22-JUN-98   1BI7              
TITLE     MECHANISM OF G1 CYCLIN DEPENDENT KINASE INHIBITION FROM THE           
TITLE    2 STRUCTURE OF THE CDK6-P16INK4A TUMOR SUPPRESSOR COMPLEX              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 6;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CDK6;                                                       
COMPND   5 EC: 2.7.1.-;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: MULTIPLE TUMOR SUPPRESSOR;                                 
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: P16INK4A, MTS1;                                             
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: SPODOPTERA FRUGIPERDA;                                    
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: HI5;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;                               
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 CELL_LINE: SPODOPTERA FRUGIPERDA;                                    
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: HI5;                                       
SOURCE  19 EXPRESSION_SYSTEM_VECTOR: GLUTATHIONE-S-TRANSFERASE FUSION           
KEYWDS    CYCLIN DEPENDENT KINASE, CYCLIN DEPENDENT KINASE INHIBITORY           
KEYWDS   2 PROTEIN, CDK, INK4, CELL CYCLE, MULTIPLE TUMOR SUPPRESSOR,           
KEYWDS   3 MTS1, COMPLEX (KINASE/ANTI-ONCOGENE)                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.A.RUSSO,L.TONG,J.O.LEE,P.D.JEFFREY,N.P.PAVLETICH                    
REVDAT   3   24-FEB-09 1BI7    1       VERSN                                    
REVDAT   2   16-FEB-99 1BI7    1       SOURCE COMPND REMARK DBREF               
REVDAT   2 2                   1       SEQADV KEYWDS HEADER                     
REVDAT   1   13-JAN-99 1BI7    0                                                
JRNL        AUTH   A.A.RUSSO,L.TONG,J.O.LEE,P.D.JEFFREY,N.P.PAVLETICH           
JRNL        TITL   STRUCTURAL BASIS FOR INHIBITION OF THE                       
JRNL        TITL 2 CYCLIN-DEPENDENT KINASE CDK6 BY THE TUMOUR                   
JRNL        TITL 3 SUPPRESSOR P16INK4A.                                         
JRNL        REF    NATURE                        V. 395   237 1998              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   9751050                                                      
JRNL        DOI    10.1038/26155                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 11109                          
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) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.330                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 562                             
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            : 3311                                    
REMARK   3   NUCLEIC ACID ATOMS       : NULL                                    
REMARK   3   HETEROGEN ATOMS          : NULL                                    
REMARK   3   SOLVENT ATOMS            : NULL                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED 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) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.94                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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  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 1BI7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JAN-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.908                              
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12443                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.33000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR, MAD                     
REMARK 200 SOFTWARE USED: X-PLOR 3.8                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z+1/2                                             
REMARK 290       7555   Y,X,-Z+3/4                                              
REMARK 290       8555   -Y,-X,-Z+1/4                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.25000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       28.12500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       84.37500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       56.25000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       84.37500            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       28.12500            
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: TETRAMERIC                        
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 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      123.10000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      168.75000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     CYS A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     THR A    49                                                      
REMARK 465     GLY A    50                                                      
REMARK 465     GLU A    51                                                      
REMARK 465     GLU A    52                                                      
REMARK 465     GLY A    53                                                      
REMARK 465     MET A    54                                                      
REMARK 465     PRO A    55                                                      
REMARK 465     LEU A    56                                                      
REMARK 465     SER A    57                                                      
REMARK 465     THR A    58                                                      
REMARK 465     ILE A    59                                                      
REMARK 465     ARG A    60                                                      
REMARK 465     GLU A    61                                                      
REMARK 465     VAL A    62                                                      
REMARK 465     ALA A    63                                                      
REMARK 465     VAL A    64                                                      
REMARK 465     LEU A    65                                                      
REMARK 465     ARG A    66                                                      
REMARK 465     HIS A    67                                                      
REMARK 465     LEU A    68                                                      
REMARK 465     GLU A    69                                                      
REMARK 465     THR A    70                                                      
REMARK 465     PHE A    71                                                      
REMARK 465     ASP A   302                                                      
REMARK 465     LEU A   303                                                      
REMARK 465     GLU A   304                                                      
REMARK 465     ARG A   305                                                      
REMARK 465     CYS A   306                                                      
REMARK 465     LYS A   307                                                      
REMARK 465     GLU A   308                                                      
REMARK 465     ASN A   309                                                      
REMARK 465     LEU A   310                                                      
REMARK 465     ASP A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     HIS A   313                                                      
REMARK 465     LEU A   314                                                      
REMARK 465     PRO A   315                                                      
REMARK 465     PRO A   316                                                      
REMARK 465     SER A   317                                                      
REMARK 465     GLN A   318                                                      
REMARK 465     ASN A   319                                                      
REMARK 465     THR A   320                                                      
REMARK 465     SER A   321                                                      
REMARK 465     GLU A   322                                                      
REMARK 465     LEU A   323                                                      
REMARK 465     ASN A   324                                                      
REMARK 465     THR A   325                                                      
REMARK 465     ALA A   326                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     MET B     9                                                      
REMARK 465     GLY B   135                                                      
REMARK 465     GLY B   136                                                      
REMARK 465     THR B   137                                                      
REMARK 465     ARG B   138                                                      
REMARK 465     GLY B   139                                                      
REMARK 465     SER B   140                                                      
REMARK 465     ASN B   141                                                      
REMARK 465     HIS B   142                                                      
REMARK 465     ALA B   143                                                      
REMARK 465     ARG B   144                                                      
REMARK 465     ILE B   145                                                      
REMARK 465     ASP B   146                                                      
REMARK 465     ALA B   147                                                      
REMARK 465     ALA B   148                                                      
REMARK 465     GLU B   149                                                      
REMARK 465     GLY B   150                                                      
REMARK 465     PRO B   151                                                      
REMARK 465     SER B   152                                                      
REMARK 465     ASP B   153                                                      
REMARK 465     ILE B   154                                                      
REMARK 465     PRO B   155                                                      
REMARK 465     ASP B   156                                                      
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     MET A 174    CG   SD   CE                                        
REMARK 470     LEU A 176    CG   CD1  CD2                                       
REMARK 470     TYR A 196    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B  10    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A 114   N   -  CA  -  C   ANGL. DEV. =  17.2 DEGREES          
REMARK 500    LEU A 202   CA  -  CB  -  CG  ANGL. DEV. = -17.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS A  15      106.99    -57.09                                   
REMARK 500    ALA A  17      149.13   -178.75                                   
REMARK 500    ASN A  35     -166.02   -101.24                                   
REMARK 500    VAL A  47     -120.73   -124.37                                   
REMARK 500    HIS A  73      122.32     61.37                                   
REMARK 500    SER A  86      111.49   -169.63                                   
REMARK 500    ARG A  90       94.74     58.96                                   
REMARK 500    GLU A  91      134.33    143.21                                   
REMARK 500    THR A  95       89.36   -164.20                                   
REMARK 500    GLN A 103      118.10    175.31                                   
REMARK 500    GLU A 114      -37.60    -20.64                                   
REMARK 500    ARG A 140       -8.02     58.25                                   
REMARK 500    ARG A 144      -46.96     63.16                                   
REMARK 500    ASP A 145       61.42   -108.23                                   
REMARK 500    GLN A 149       -0.89    -55.33                                   
REMARK 500    ALA A 167       86.11     70.49                                   
REMARK 500    GLN A 173       72.43     -9.83                                   
REMARK 500    MET A 174      -82.89     47.12                                   
REMARK 500    THR A 177       76.98    -49.69                                   
REMARK 500    VAL A 180      155.05    179.73                                   
REMARK 500    VAL A 181       41.81   -105.22                                   
REMARK 500    THR A 182       88.32     41.63                                   
REMARK 500    GLN A 193       92.93     69.09                                   
REMARK 500    SER A 194        8.00   -159.45                                   
REMARK 500    SER A 195      179.60    171.27                                   
REMARK 500    TYR A 196       60.10   -164.55                                   
REMARK 500    SER A 222      -62.35   -103.89                                   
REMARK 500    VAL A 234      -72.33    -81.25                                   
REMARK 500    GLU A 240       79.31    -62.26                                   
REMARK 500    GLU A 241      -55.02   -164.70                                   
REMARK 500    PRO A 244      170.87    -59.49                                   
REMARK 500    VAL A 247      141.07    -30.29                                   
REMARK 500    ALA A 248      -96.66    -21.90                                   
REMARK 500    PHE A 254       49.89   -100.45                                   
REMARK 500    HIS A 255      121.52    -12.78                                   
REMARK 500    SER A 256      -32.08    -16.33                                   
REMARK 500    LYS A 257      122.38    -20.12                                   
REMARK 500    SER A 258      169.56     91.44                                   
REMARK 500    ALA A 259       45.16    173.87                                   
REMARK 500    ASP A 268       23.06     49.48                                   
REMARK 500    ASP A 275      -78.40    -66.33                                   
REMARK 500    LEU A 281       49.88    -89.50                                   
REMARK 500    TYR A 299      -52.43    -20.07                                   
REMARK 500    PRO B  11      -83.98    -90.20                                   
REMARK 500    SER B  12      -51.06     77.58                                   
REMARK 500    ASP B  14      -41.28   -154.62                                   
REMARK 500    ARG B  29      -71.29    -54.18                                   
REMARK 500    GLU B  33       28.51    -71.09                                   
REMARK 500    PRO B  38       40.64    -78.19                                   
REMARK 500    ASN B  39       -2.66   -165.03                                   
REMARK 500    ASN B  42       31.96    -94.89                                   
REMARK 500    SER B  43      -15.15     75.37                                   
REMARK 500    ARG B  46      118.33    168.55                                   
REMARK 500    GLN B  50      -36.34   -147.04                                   
REMARK 500    MET B  54      150.18    -48.85                                   
REMARK 500    SER B  56       62.32   -111.34                                   
REMARK 500    HIS B  66       19.21   -163.25                                   
REMARK 500    GLU B  69      109.32    -49.28                                   
REMARK 500    PRO B  75      -94.62      0.96                                   
REMARK 500    ALA B  76      -78.49    -57.32                                   
REMARK 500    LEU B  78       -8.85     76.94                                   
REMARK 500    VAL B  82      -29.21    -39.96                                   
REMARK 500    ASP B  92      -70.05    -40.78                                   
REMARK 500    LEU B 104       24.14    -65.01                                   
REMARK 500    ASP B 105       73.27   -150.93                                   
REMARK 500    ARG B 131       42.86    -86.12                                   
REMARK 500    ALA B 132      164.28    178.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 170         0.06    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1BI7 A    1   326  UNP    Q00534   CDK6_HUMAN       1    326             
DBREF  1BI7 B    1   156  UNP    P42771   CDN2A_HUMAN      1    156             
SEQADV 1BI7 ASN B   37  UNP  P42771    LEU    37 CONFLICT                       
SEQRES   1 A  326  MET GLU LYS ASP GLY LEU CYS ARG ALA ASP GLN GLN TYR          
SEQRES   2 A  326  GLU CYS VAL ALA GLU ILE GLY GLU GLY ALA TYR GLY LYS          
SEQRES   3 A  326  VAL PHE LYS ALA ARG ASP LEU LYS ASN GLY GLY ARG PHE          
SEQRES   4 A  326  VAL ALA LEU LYS ARG VAL ARG VAL GLN THR GLY GLU GLU          
SEQRES   5 A  326  GLY MET PRO LEU SER THR ILE ARG GLU VAL ALA VAL LEU          
SEQRES   6 A  326  ARG HIS LEU GLU THR PHE GLU HIS PRO ASN VAL VAL ARG          
SEQRES   7 A  326  LEU PHE ASP VAL CYS THR VAL SER ARG THR ASP ARG GLU          
SEQRES   8 A  326  THR LYS LEU THR LEU VAL PHE GLU HIS VAL ASP GLN ASP          
SEQRES   9 A  326  LEU THR THR TYR LEU ASP LYS VAL PRO GLU PRO GLY VAL          
SEQRES  10 A  326  PRO THR GLU THR ILE LYS ASP MET MET PHE GLN LEU LEU          
SEQRES  11 A  326  ARG GLY LEU ASP PHE LEU HIS SER HIS ARG VAL VAL HIS          
SEQRES  12 A  326  ARG ASP LEU LYS PRO GLN ASN ILE LEU VAL THR SER SER          
SEQRES  13 A  326  GLY GLN ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ILE          
SEQRES  14 A  326  TYR SER PHE GLN MET ALA LEU THR SER VAL VAL VAL THR          
SEQRES  15 A  326  LEU TRP TYR ARG ALA PRO GLU VAL LEU LEU GLN SER SER          
SEQRES  16 A  326  TYR ALA THR PRO VAL ASP LEU TRP SER VAL GLY CYS ILE          
SEQRES  17 A  326  PHE ALA GLU MET PHE ARG ARG LYS PRO LEU PHE ARG GLY          
SEQRES  18 A  326  SER SER ASP VAL ASP GLN LEU GLY LYS ILE LEU ASP VAL          
SEQRES  19 A  326  ILE GLY LEU PRO GLY GLU GLU ASP TRP PRO ARG ASP VAL          
SEQRES  20 A  326  ALA LEU PRO ARG GLN ALA PHE HIS SER LYS SER ALA GLN          
SEQRES  21 A  326  PRO ILE GLU LYS PHE VAL THR ASP ILE ASP GLU LEU GLY          
SEQRES  22 A  326  LYS ASP LEU LEU LEU LYS CYS LEU THR PHE ASN PRO ALA          
SEQRES  23 A  326  LYS ARG ILE SER ALA TYR SER ALA LEU SER HIS PRO TYR          
SEQRES  24 A  326  PHE GLN ASP LEU GLU ARG CYS LYS GLU ASN LEU ASP SER          
SEQRES  25 A  326  HIS LEU PRO PRO SER GLN ASN THR SER GLU LEU ASN THR          
SEQRES  26 A  326  ALA                                                          
SEQRES   1 B  156  MET GLU PRO ALA ALA GLY SER SER MET GLU PRO SER ALA          
SEQRES   2 B  156  ASP TRP LEU ALA THR ALA ALA ALA ARG GLY ARG VAL GLU          
SEQRES   3 B  156  GLU VAL ARG ALA LEU LEU GLU ALA GLY ALA ASN PRO ASN          
SEQRES   4 B  156  ALA PRO ASN SER TYR GLY ARG ARG PRO ILE GLN VAL MET          
SEQRES   5 B  156  MET MET GLY SER ALA ARG VAL ALA GLU LEU LEU LEU LEU          
SEQRES   6 B  156  HIS GLY ALA GLU PRO ASN CYS ALA ASP PRO ALA THR LEU          
SEQRES   7 B  156  THR ARG PRO VAL HIS ASP ALA ALA ARG GLU GLY PHE LEU          
SEQRES   8 B  156  ASP THR LEU VAL VAL LEU HIS ARG ALA GLY ALA ARG LEU          
SEQRES   9 B  156  ASP VAL ARG ASP ALA TRP GLY ARG LEU PRO VAL ASP LEU          
SEQRES  10 B  156  ALA GLU GLU LEU GLY HIS ARG ASP VAL ALA ARG TYR LEU          
SEQRES  11 B  156  ARG ALA ALA ALA GLY GLY THR ARG GLY SER ASN HIS ALA          
SEQRES  12 B  156  ARG ILE ASP ALA ALA GLU GLY PRO SER ASP ILE PRO ASP          
HELIX    1   2 LEU A  105  LYS A  111  1                                   7    
HELIX    2   3 THR A  119  HIS A  139  1                                  21    
HELIX    3   4 PRO A  148  ASN A  150  5                                   3    
HELIX    4   5 PRO A  188  LEU A  192  1                                   5    
HELIX    5   6 THR A  198  ARG A  214  5                                  17    
HELIX    6   7 ASP A  224  ILE A  235  1                                  12    
HELIX    7   8 ARG A  251  PHE A  254  5                                   4    
HELIX    8   9 ILE A  262  LYS A  264  5                                   3    
HELIX    9  10 GLU A  271  CYS A  280  1                                  10    
HELIX   10  11 ALA A  291  SER A  296  1                                   6    
HELIX   11  12 TRP B   15  ARG B   22  1                                   8    
HELIX   12  13 VAL B   25  ALA B   34  1                                  10    
HELIX   13  14 ALA B   57  HIS B   66  1                                  10    
HELIX   14  15 PRO B   81  GLU B   88  1                                   8    
HELIX   15  16 LEU B   91  ALA B  100  1                                  10    
HELIX   16  17 PRO B  114  LEU B  121  1                                   8    
HELIX   17  18 ARG B  124  LEU B  130  1                                   7    
SHEET    1   A 5 GLY A  20  GLY A  22  0                                        
SHEET    2   A 5 GLY A  25  ASP A  32 -1  N  VAL A  27   O  GLY A  20           
SHEET    3   A 5 ARG A  38  VAL A  45 -1  N  ARG A  44   O  LYS A  26           
SHEET    4   A 5 LEU A  94  GLU A  99 -1  N  PHE A  98   O  ALA A  41           
SHEET    5   A 5 LEU A  79  THR A  84 -1  N  CYS A  83   O  THR A  95           
SHEET    1   B 2 TYR A  13  GLU A  18  0                                        
SHEET    2   B 2 PHE A  28  ASP A  32 -1  N  ARG A  31   O  GLU A  14           
CRYST1  123.100  123.100  112.500  90.00  90.00  90.00 P 41 2 2      8          
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      0.008123  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008123  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008889        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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