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Database: PDB
Entry: 1G3N
LinkDB: 1G3N
Original site: 1G3N 
HEADER    CELL CYCLE, SIGNALING PROTEIN           24-OCT-00   1G3N              
TITLE     STRUCTURE OF A P18(INK4C)-CDK6-K-CYCLIN TERNARY COMPLEX               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 6;                                 
COMPND   3 CHAIN: A, E;                                                         
COMPND   4 SYNONYM: CELL DIVISION PROTEIN KINASE 6, PROTEIN KINASE CDK6;        
COMPND   5 EC: 2.7.1.37;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYCLIN-DEPENDENT KINASE 6 INHIBITOR;                       
COMPND   9 CHAIN: B, F;                                                         
COMPND  10 SYNONYM: P18(INK4C), CYCLIN-DEPENDENT KINASE INHIBITOR 2C, P18,      
COMPND  11 INHIBITS CDK4, CYCLIN-DEPENDENT KINASE 4 INHIBITOR C, P18-INK4C;     
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: V-CYCLIN;                                                  
COMPND  15 CHAIN: C, G;                                                         
COMPND  16 SYNONYM: K-CYCLIN, FUNCTIONAL CYCLIN D HOMOLOG;                      
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CYCLIN-DEPENDENT KINASE 6;                                     
SOURCE   6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HI5;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: P18(INK4C);                                                    
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 MOL_ID: 3;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 8;                            
SOURCE  18 ORGANISM_TAXID: 37296;                                               
SOURCE  19 GENE: K-CYCLIN (VIRAL CYCLIND HOMOLOG);                              
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CYCLIN-DEPENDENT KINASE, INK4 INHIBITOR, VIRAL CYCLIN, CELL CYCLE,    
KEYWDS   2 SIGNALING PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.D.JEFFREY,L.TONG,N.P.PAVLETICH                                      
REVDAT   5   04-APR-18 1G3N    1       REMARK                                   
REVDAT   4   04-OCT-17 1G3N    1       REMARK                                   
REVDAT   3   24-FEB-09 1G3N    1       VERSN                                    
REVDAT   2   01-APR-03 1G3N    1       JRNL                                     
REVDAT   1   10-JAN-01 1G3N    0                                                
JRNL        AUTH   P.D.JEFFREY,L.TONG,N.P.PAVLETICH                             
JRNL        TITL   STRUCTURAL BASIS OF INHIBITION OF CDK-CYCLIN COMPLEXES BY    
JRNL        TITL 2 INK4 INHIBITORS.                                             
JRNL        REF    GENES DEV.                    V.  14  3115 2000              
JRNL        REFN                   ISSN 0890-9369                               
JRNL        PMID   11124804                                                     
JRNL        DOI    10.1101/GAD.851100                                           
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 : CNS                                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
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)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 33824                          
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) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1905                            
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            : 10644                                   
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) : 55.00                          
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) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.760                           
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 1G3N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000012192.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAR-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 113                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRROR, YALE DESIGN                
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40272                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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   (%): 56.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: (NH4)2SO4, DIOXANE, TRIS-HCL, PH 7.6,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       38.89000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.41000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       73.47500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       82.41000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.89000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       73.47500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G                               
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E, G                            
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                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     CYS A     7                                                      
REMARK 465     ARG A     8                                                      
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     ALA B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     TRP B     5                                                      
REMARK 465     ALA B   161                                                      
REMARK 465     GLY B   162                                                      
REMARK 465     GLY B   163                                                      
REMARK 465     ALA B   164                                                      
REMARK 465     THR B   165                                                      
REMARK 465     ASN B   166                                                      
REMARK 465     LEU B   167                                                      
REMARK 465     GLN B   168                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     ALA C     4                                                      
REMARK 465     ASN C     5                                                      
REMARK 465     ASN C     6                                                      
REMARK 465     PRO C     7                                                      
REMARK 465     PRO C     8                                                      
REMARK 465     SER C     9                                                      
REMARK 465     GLY C    10                                                      
REMARK 465     LEU C    11                                                      
REMARK 465     LEU C    12                                                      
REMARK 465     ASP C    13                                                      
REMARK 465     PRO C    14                                                      
REMARK 465     THR C    15                                                      
REMARK 465     ASP C   214                                                      
REMARK 465     THR C   215                                                      
REMARK 465     HIS C   216                                                      
REMARK 465     SER C   217                                                      
REMARK 465     GLY C   218                                                      
REMARK 465     LEU C   254                                                      
REMARK 465     ASP C   255                                                      
REMARK 465     SER C   256                                                      
REMARK 465     TYR C   257                                                      
REMARK 465     MET E     1                                                      
REMARK 465     GLU E     2                                                      
REMARK 465     LYS E     3                                                      
REMARK 465     ASP E     4                                                      
REMARK 465     GLY E     5                                                      
REMARK 465     LEU E     6                                                      
REMARK 465     CYS E     7                                                      
REMARK 465     ARG E     8                                                      
REMARK 465     ASP E   302                                                      
REMARK 465     LEU E   303                                                      
REMARK 465     GLU E   304                                                      
REMARK 465     ARG E   305                                                      
REMARK 465     CYS E   306                                                      
REMARK 465     LYS E   307                                                      
REMARK 465     GLU E   308                                                      
REMARK 465     ASN E   309                                                      
REMARK 465     LEU E   310                                                      
REMARK 465     ASP E   311                                                      
REMARK 465     SER E   312                                                      
REMARK 465     HIS E   313                                                      
REMARK 465     LEU E   314                                                      
REMARK 465     PRO E   315                                                      
REMARK 465     PRO E   316                                                      
REMARK 465     SER E   317                                                      
REMARK 465     GLN E   318                                                      
REMARK 465     ASN E   319                                                      
REMARK 465     THR E   320                                                      
REMARK 465     SER E   321                                                      
REMARK 465     GLU E   322                                                      
REMARK 465     LEU E   323                                                      
REMARK 465     ASN E   324                                                      
REMARK 465     THR E   325                                                      
REMARK 465     ALA E   326                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ALA F     2                                                      
REMARK 465     GLU F     3                                                      
REMARK 465     PRO F     4                                                      
REMARK 465     TRP F     5                                                      
REMARK 465     ALA F   161                                                      
REMARK 465     GLY F   162                                                      
REMARK 465     GLY F   163                                                      
REMARK 465     ALA F   164                                                      
REMARK 465     THR F   165                                                      
REMARK 465     ASN F   166                                                      
REMARK 465     LEU F   167                                                      
REMARK 465     GLN F   168                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ALA G     2                                                      
REMARK 465     THR G     3                                                      
REMARK 465     ALA G     4                                                      
REMARK 465     ASN G     5                                                      
REMARK 465     ASN G     6                                                      
REMARK 465     PRO G     7                                                      
REMARK 465     PRO G     8                                                      
REMARK 465     SER G     9                                                      
REMARK 465     GLY G    10                                                      
REMARK 465     LEU G    11                                                      
REMARK 465     LEU G    12                                                      
REMARK 465     ASP G    13                                                      
REMARK 465     PRO G    14                                                      
REMARK 465     THR G    15                                                      
REMARK 465     ASP G   214                                                      
REMARK 465     THR G   215                                                      
REMARK 465     HIS G   216                                                      
REMARK 465     SER G   217                                                      
REMARK 465     GLY G   218                                                      
REMARK 465     LEU G   254                                                      
REMARK 465     ASP G   255                                                      
REMARK 465     SER G   256                                                      
REMARK 465     TYR G   257                                                      
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    LEU B    25     NH1  ARG B    59              2.09            
REMARK 500   O    LEU F    25     NH1  ARG F    59              2.14            
REMARK 500   NE2  GLN A   252     OE2  GLU E    21              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS A 147   CD    LYS A 147   CE      0.153                       
REMARK 500    LYS A 147   CE    LYS A 147   NZ      0.151                       
REMARK 500    LYS E 147   CD    LYS E 147   CE      0.172                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS A 147   CD  -  CE  -  NZ  ANGL. DEV. =  18.6 DEGREES          
REMARK 500    LYS E 147   CD  -  CE  -  NZ  ANGL. DEV. =  16.5 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    GLN A  11       -7.07   -176.21                                   
REMARK 500    ASN A  35       44.42   -144.08                                   
REMARK 500    ARG A  87      -80.35    -70.24                                   
REMARK 500    THR A  88     -155.98   -125.91                                   
REMARK 500    ARG A  90      -15.99    -48.96                                   
REMARK 500    ASP A 102       39.89    -77.45                                   
REMARK 500    ASP A 110       38.27    -77.33                                   
REMARK 500    PRO A 113      175.71    -52.09                                   
REMARK 500    ARG A 144       -4.18     66.22                                   
REMARK 500    ASP A 145       46.15   -146.21                                   
REMARK 500    ASP A 163       74.07   -168.57                                   
REMARK 500    GLN A 173      -80.70    -44.76                                   
REMARK 500    SER A 194     -121.65   -114.87                                   
REMARK 500    HIS A 255      172.64    -57.54                                   
REMARK 500    SER A 258      -97.68    -64.20                                   
REMARK 500    ALA A 259       80.04    153.83                                   
REMARK 500    LEU A 281       44.53    -75.49                                   
REMARK 500    PRO A 298       -2.32    -57.76                                   
REMARK 500    LYS B  46       92.60    -66.49                                   
REMARK 500    ASP B 100     -157.03    -81.54                                   
REMARK 500    ASN B 129       89.59    -66.77                                   
REMARK 500    ARG B 149       48.81    -67.09                                   
REMARK 500    SER B 154      -72.98    -47.75                                   
REMARK 500    GLU C  29      -67.63    -12.81                                   
REMARK 500    PHE C  39      -91.94    -37.33                                   
REMARK 500    THR C  41      -81.62   -125.05                                   
REMARK 500    GLN C  44      -63.17     76.01                                   
REMARK 500    SER C  60      -74.48    -58.07                                   
REMARK 500    CYS C  62      -80.99    -70.96                                   
REMARK 500    GLU C  64      -70.15    -82.34                                   
REMARK 500    TYR C  65       21.27    -58.63                                   
REMARK 500    THR C 111       60.22   -108.09                                   
REMARK 500    TRP C 144       12.58     55.68                                   
REMARK 500    LEU C 162      -67.88    -93.86                                   
REMARK 500    HIS C 168      -33.00     86.25                                   
REMARK 500    PRO C 212      177.49    -45.14                                   
REMARK 500    ASP C 250      107.15   -163.55                                   
REMARK 500    LEU C 251       12.59    -61.83                                   
REMARK 500    GLN E  11       -5.76   -178.23                                   
REMARK 500    ASN E  35       45.07   -144.30                                   
REMARK 500    GLU E  72       56.86     39.63                                   
REMARK 500    ARG E  87      -76.43    -71.18                                   
REMARK 500    THR E  88     -157.40   -130.43                                   
REMARK 500    ASP E 102       33.35    -75.62                                   
REMARK 500    ASP E 110       33.91    -85.96                                   
REMARK 500    SER E 138      -16.70    -49.19                                   
REMARK 500    ARG E 144       -5.97     72.24                                   
REMARK 500    ASP E 145       49.28   -145.32                                   
REMARK 500    ASP E 163       69.19   -172.45                                   
REMARK 500    GLN E 173      -83.81    -44.02                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      81 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BI7   RELATED DB: PDB                                   
REMARK 900 P16(INK4A)-CDK6 BINARY COMPLEX                                       
REMARK 900 RELATED ID: 1BI8   RELATED DB: PDB                                   
REMARK 900 P19(INK4D)-CDK6 BINARY COMPLEX                                       
DBREF  1G3N A    1   326  UNP    Q00534   CDK6_HUMAN       1    326             
DBREF  1G3N E    1   326  UNP    Q00534   CDK6_HUMAN       1    326             
DBREF  1G3N B    1   168  UNP    P42773   CDN2C_HUMAN      1    168             
DBREF  1G3N F    1   168  UNP    P42773   CDN2C_HUMAN      1    168             
DBREF  1G3N C    1   257  UNP    O40946   O40946_HHV8      1    257             
DBREF  1G3N G    1   257  UNP    O40946   O40946_HHV8      1    257             
SEQADV 1G3N VAL C  163  UNP  O40946    LEU   163 CONFLICT                       
SEQADV 1G3N LEU C  188  UNP  O40946    LYS   188 CONFLICT                       
SEQADV 1G3N VAL G  163  UNP  O40946    LEU   163 CONFLICT                       
SEQADV 1G3N LEU G  188  UNP  O40946    LYS   188 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  168  MET ALA GLU PRO TRP GLY ASN GLU LEU ALA SER ALA ALA          
SEQRES   2 B  168  ALA ARG GLY ASP LEU GLU GLN LEU THR SER LEU LEU GLN          
SEQRES   3 B  168  ASN ASN VAL ASN VAL ASN ALA GLN ASN GLY PHE GLY ARG          
SEQRES   4 B  168  THR ALA LEU GLN VAL MET LYS LEU GLY ASN PRO GLU ILE          
SEQRES   5 B  168  ALA ARG ARG LEU LEU LEU ARG GLY ALA ASN PRO ASP LEU          
SEQRES   6 B  168  LYS ASP ARG THR GLY PHE ALA VAL ILE HIS ASP ALA ALA          
SEQRES   7 B  168  ARG ALA GLY PHE LEU ASP THR LEU GLN THR LEU LEU GLU          
SEQRES   8 B  168  PHE GLN ALA ASP VAL ASN ILE GLU ASP ASN GLU GLY ASN          
SEQRES   9 B  168  LEU PRO LEU HIS LEU ALA ALA LYS GLU GLY HIS LEU ARG          
SEQRES  10 B  168  VAL VAL GLU PHE LEU VAL LYS HIS THR ALA SER ASN VAL          
SEQRES  11 B  168  GLY HIS ARG ASN HIS LYS GLY ASP THR ALA CYS ASP LEU          
SEQRES  12 B  168  ALA ARG LEU TYR GLY ARG ASN GLU VAL VAL SER LEU MET          
SEQRES  13 B  168  GLN ALA ASN GLY ALA GLY GLY ALA THR ASN LEU GLN              
SEQRES   1 C  257  MET ALA THR ALA ASN ASN PRO PRO SER GLY LEU LEU ASP          
SEQRES   2 C  257  PRO THR LEU CYS GLU ASP ARG ILE PHE TYR ASN ILE LEU          
SEQRES   3 C  257  GLU ILE GLU PRO ARG PHE LEU THR SER ASP SER VAL PHE          
SEQRES   4 C  257  GLY THR PHE GLN GLN SER LEU THR SER HIS MET ARG LYS          
SEQRES   5 C  257  LEU LEU GLY THR TRP MET PHE SER VAL CYS GLN GLU TYR          
SEQRES   6 C  257  ASN LEU GLU PRO ASN VAL VAL ALA LEU ALA LEU ASN LEU          
SEQRES   7 C  257  LEU ASP ARG LEU LEU LEU ILE LYS GLN VAL SER LYS GLU          
SEQRES   8 C  257  HIS PHE GLN LYS THR GLY SER ALA CYS LEU LEU VAL ALA          
SEQRES   9 C  257  SER LYS LEU ARG SER LEU THR PRO ILE SER THR SER SER          
SEQRES  10 C  257  LEU CYS TYR ALA ALA ALA ASP SER PHE SER ARG GLN GLU          
SEQRES  11 C  257  LEU ILE ASP GLN GLU LYS GLU LEU LEU GLU LYS LEU ALA          
SEQRES  12 C  257  TRP ARG THR GLU ALA VAL LEU ALA THR ASP VAL THR SER          
SEQRES  13 C  257  PHE LEU LEU LEU LYS LEU VAL GLY GLY SER GLN HIS LEU          
SEQRES  14 C  257  ASP PHE TRP HIS HIS GLU VAL ASN THR LEU ILE THR LYS          
SEQRES  15 C  257  ALA LEU VAL ASP PRO LEU THR GLY SER LEU PRO ALA SER          
SEQRES  16 C  257  ILE ILE SER ALA ALA GLY CYS ALA LEU LEU VAL PRO ALA          
SEQRES  17 C  257  ASN VAL ILE PRO GLN ASP THR HIS SER GLY GLY VAL VAL          
SEQRES  18 C  257  PRO GLN LEU ALA SER ILE LEU GLY CYS ASP VAL SER VAL          
SEQRES  19 C  257  LEU GLN ALA ALA VAL GLU GLN ILE LEU THR SER VAL SER          
SEQRES  20 C  257  ASP PHE ASP LEU ARG ILE LEU ASP SER TYR                      
SEQRES   1 E  326  MET GLU LYS ASP GLY LEU CYS ARG ALA ASP GLN GLN TYR          
SEQRES   2 E  326  GLU CYS VAL ALA GLU ILE GLY GLU GLY ALA TYR GLY LYS          
SEQRES   3 E  326  VAL PHE LYS ALA ARG ASP LEU LYS ASN GLY GLY ARG PHE          
SEQRES   4 E  326  VAL ALA LEU LYS ARG VAL ARG VAL GLN THR GLY GLU GLU          
SEQRES   5 E  326  GLY MET PRO LEU SER THR ILE ARG GLU VAL ALA VAL LEU          
SEQRES   6 E  326  ARG HIS LEU GLU THR PHE GLU HIS PRO ASN VAL VAL ARG          
SEQRES   7 E  326  LEU PHE ASP VAL CYS THR VAL SER ARG THR ASP ARG GLU          
SEQRES   8 E  326  THR LYS LEU THR LEU VAL PHE GLU HIS VAL ASP GLN ASP          
SEQRES   9 E  326  LEU THR THR TYR LEU ASP LYS VAL PRO GLU PRO GLY VAL          
SEQRES  10 E  326  PRO THR GLU THR ILE LYS ASP MET MET PHE GLN LEU LEU          
SEQRES  11 E  326  ARG GLY LEU ASP PHE LEU HIS SER HIS ARG VAL VAL HIS          
SEQRES  12 E  326  ARG ASP LEU LYS PRO GLN ASN ILE LEU VAL THR SER SER          
SEQRES  13 E  326  GLY GLN ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ILE          
SEQRES  14 E  326  TYR SER PHE GLN MET ALA LEU THR SER VAL VAL VAL THR          
SEQRES  15 E  326  LEU TRP TYR ARG ALA PRO GLU VAL LEU LEU GLN SER SER          
SEQRES  16 E  326  TYR ALA THR PRO VAL ASP LEU TRP SER VAL GLY CYS ILE          
SEQRES  17 E  326  PHE ALA GLU MET PHE ARG ARG LYS PRO LEU PHE ARG GLY          
SEQRES  18 E  326  SER SER ASP VAL ASP GLN LEU GLY LYS ILE LEU ASP VAL          
SEQRES  19 E  326  ILE GLY LEU PRO GLY GLU GLU ASP TRP PRO ARG ASP VAL          
SEQRES  20 E  326  ALA LEU PRO ARG GLN ALA PHE HIS SER LYS SER ALA GLN          
SEQRES  21 E  326  PRO ILE GLU LYS PHE VAL THR ASP ILE ASP GLU LEU GLY          
SEQRES  22 E  326  LYS ASP LEU LEU LEU LYS CYS LEU THR PHE ASN PRO ALA          
SEQRES  23 E  326  LYS ARG ILE SER ALA TYR SER ALA LEU SER HIS PRO TYR          
SEQRES  24 E  326  PHE GLN ASP LEU GLU ARG CYS LYS GLU ASN LEU ASP SER          
SEQRES  25 E  326  HIS LEU PRO PRO SER GLN ASN THR SER GLU LEU ASN THR          
SEQRES  26 E  326  ALA                                                          
SEQRES   1 F  168  MET ALA GLU PRO TRP GLY ASN GLU LEU ALA SER ALA ALA          
SEQRES   2 F  168  ALA ARG GLY ASP LEU GLU GLN LEU THR SER LEU LEU GLN          
SEQRES   3 F  168  ASN ASN VAL ASN VAL ASN ALA GLN ASN GLY PHE GLY ARG          
SEQRES   4 F  168  THR ALA LEU GLN VAL MET LYS LEU GLY ASN PRO GLU ILE          
SEQRES   5 F  168  ALA ARG ARG LEU LEU LEU ARG GLY ALA ASN PRO ASP LEU          
SEQRES   6 F  168  LYS ASP ARG THR GLY PHE ALA VAL ILE HIS ASP ALA ALA          
SEQRES   7 F  168  ARG ALA GLY PHE LEU ASP THR LEU GLN THR LEU LEU GLU          
SEQRES   8 F  168  PHE GLN ALA ASP VAL ASN ILE GLU ASP ASN GLU GLY ASN          
SEQRES   9 F  168  LEU PRO LEU HIS LEU ALA ALA LYS GLU GLY HIS LEU ARG          
SEQRES  10 F  168  VAL VAL GLU PHE LEU VAL LYS HIS THR ALA SER ASN VAL          
SEQRES  11 F  168  GLY HIS ARG ASN HIS LYS GLY ASP THR ALA CYS ASP LEU          
SEQRES  12 F  168  ALA ARG LEU TYR GLY ARG ASN GLU VAL VAL SER LEU MET          
SEQRES  13 F  168  GLN ALA ASN GLY ALA GLY GLY ALA THR ASN LEU GLN              
SEQRES   1 G  257  MET ALA THR ALA ASN ASN PRO PRO SER GLY LEU LEU ASP          
SEQRES   2 G  257  PRO THR LEU CYS GLU ASP ARG ILE PHE TYR ASN ILE LEU          
SEQRES   3 G  257  GLU ILE GLU PRO ARG PHE LEU THR SER ASP SER VAL PHE          
SEQRES   4 G  257  GLY THR PHE GLN GLN SER LEU THR SER HIS MET ARG LYS          
SEQRES   5 G  257  LEU LEU GLY THR TRP MET PHE SER VAL CYS GLN GLU TYR          
SEQRES   6 G  257  ASN LEU GLU PRO ASN VAL VAL ALA LEU ALA LEU ASN LEU          
SEQRES   7 G  257  LEU ASP ARG LEU LEU LEU ILE LYS GLN VAL SER LYS GLU          
SEQRES   8 G  257  HIS PHE GLN LYS THR GLY SER ALA CYS LEU LEU VAL ALA          
SEQRES   9 G  257  SER LYS LEU ARG SER LEU THR PRO ILE SER THR SER SER          
SEQRES  10 G  257  LEU CYS TYR ALA ALA ALA ASP SER PHE SER ARG GLN GLU          
SEQRES  11 G  257  LEU ILE ASP GLN GLU LYS GLU LEU LEU GLU LYS LEU ALA          
SEQRES  12 G  257  TRP ARG THR GLU ALA VAL LEU ALA THR ASP VAL THR SER          
SEQRES  13 G  257  PHE LEU LEU LEU LYS LEU VAL GLY GLY SER GLN HIS LEU          
SEQRES  14 G  257  ASP PHE TRP HIS HIS GLU VAL ASN THR LEU ILE THR LYS          
SEQRES  15 G  257  ALA LEU VAL ASP PRO LEU THR GLY SER LEU PRO ALA SER          
SEQRES  16 G  257  ILE ILE SER ALA ALA GLY CYS ALA LEU LEU VAL PRO ALA          
SEQRES  17 G  257  ASN VAL ILE PRO GLN ASP THR HIS SER GLY GLY VAL VAL          
SEQRES  18 G  257  PRO GLN LEU ALA SER ILE LEU GLY CYS ASP VAL SER VAL          
SEQRES  19 G  257  LEU GLN ALA ALA VAL GLU GLN ILE LEU THR SER VAL SER          
SEQRES  20 G  257  ASP PHE ASP LEU ARG ILE LEU ASP SER TYR                      
HELIX    1   1 PRO A   55  PHE A   71  1                                  17    
HELIX    2   2 ASP A  104  ASP A  110  1                                   7    
HELIX    3   3 PRO A  118  HIS A  139  1                                  22    
HELIX    4   4 LYS A  147  GLN A  149  5                                   3    
HELIX    5   5 THR A  182  ARG A  186  5                                   5    
HELIX    6   6 ALA A  187  LEU A  192  1                                   6    
HELIX    7   7 THR A  198  ARG A  215  1                                  18    
HELIX    8   8 SER A  223  GLY A  236  1                                  14    
HELIX    9   9 GLY A  239  TRP A  243  5                                   5    
HELIX   10  10 PRO A  250  PHE A  254  5                                   5    
HELIX   11  11 PRO A  261  PHE A  265  5                                   5    
HELIX   12  12 ASP A  270  LEU A  281  1                                  12    
HELIX   13  13 ASN A  284  ARG A  288  5                                   5    
HELIX   14  14 SER A  290  SER A  296  1                                   7    
HELIX   15  15 HIS A  297  GLN A  301  5                                   5    
HELIX   16  16 GLY B    6  GLY B   16  1                                  11    
HELIX   17  17 ASP B   17  LEU B   25  1                                   9    
HELIX   18  18 THR B   40  MET B   45  1                                   6    
HELIX   19  19 ASN B   49  ARG B   59  1                                  11    
HELIX   20  20 ALA B   72  GLY B   81  1                                  10    
HELIX   21  21 PHE B   82  PHE B   92  1                                  11    
HELIX   22  22 LEU B  105  GLY B  114  1                                  10    
HELIX   23  23 HIS B  115  THR B  126  1                                  12    
HELIX   24  24 THR B  139  GLY B  148  1                                  10    
HELIX   25  25 ARG B  149  GLY B  160  1                                  12    
HELIX   26  26 LEU C   16  GLU C   29  1                                  14    
HELIX   27  27 PRO C   30  LEU C   33  5                                   4    
HELIX   28  28 SER C   35  PHE C   39  5                                   5    
HELIX   29  29 THR C   47  TYR C   65  1                                  19    
HELIX   30  30 GLU C   68  LEU C   83  1                                  16    
HELIX   31  31 SER C   89  SER C  109  1                                  21    
HELIX   32  32 SER C  114  ALA C  122  1                                   9    
HELIX   33  33 SER C  127  LEU C  142  1                                  16    
HELIX   34  34 LEU C  150  VAL C  163  1                                  14    
HELIX   35  35 HIS C  168  VAL C  185  1                                  18    
HELIX   36  36 LEU C  188  LEU C  192  5                                   5    
HELIX   37  37 PRO C  193  VAL C  206  1                                  14    
HELIX   38  38 PRO C  207  ILE C  211  5                                   5    
HELIX   39  39 GLY C  219  GLY C  229  1                                  11    
HELIX   40  40 ASP C  231  PHE C  249  1                                  19    
HELIX   41  41 PRO E   55  PHE E   71  1                                  17    
HELIX   42  42 ASP E  104  ASP E  110  1                                   7    
HELIX   43  43 PRO E  118  HIS E  139  1                                  22    
HELIX   44  44 LYS E  147  GLN E  149  5                                   3    
HELIX   45  45 THR E  182  ARG E  186  5                                   5    
HELIX   46  46 ALA E  187  LEU E  192  1                                   6    
HELIX   47  47 THR E  198  ARG E  215  1                                  18    
HELIX   48  48 SER E  223  GLY E  236  1                                  14    
HELIX   49  49 PRO E  250  PHE E  254  5                                   5    
HELIX   50  50 PRO E  261  PHE E  265  5                                   5    
HELIX   51  51 ASP E  270  LEU E  281  1                                  12    
HELIX   52  52 ASN E  284  ARG E  288  5                                   5    
HELIX   53  53 SER E  290  SER E  296  1                                   7    
HELIX   54  54 HIS E  297  GLN E  301  5                                   5    
HELIX   55  55 GLY F    6  GLY F   16  1                                  11    
HELIX   56  56 ASP F   17  LEU F   25  1                                   9    
HELIX   57  57 THR F   40  MET F   45  1                                   6    
HELIX   58  58 ASN F   49  ARG F   59  1                                  11    
HELIX   59  59 ALA F   72  GLY F   81  1                                  10    
HELIX   60  60 PHE F   82  PHE F   92  1                                  11    
HELIX   61  61 LEU F  105  GLY F  114  1                                  10    
HELIX   62  62 HIS F  115  THR F  126  1                                  12    
HELIX   63  63 THR F  139  GLY F  148  1                                  10    
HELIX   64  64 ARG F  149  ALA F  158  1                                  10    
HELIX   65  65 LEU G   16  GLU G   29  1                                  14    
HELIX   66  66 PRO G   30  LEU G   33  5                                   4    
HELIX   67  67 SER G   35  PHE G   39  5                                   5    
HELIX   68  68 THR G   47  TYR G   65  1                                  19    
HELIX   69  69 GLU G   68  LEU G   83  1                                  16    
HELIX   70  70 SER G   89  SER G  109  1                                  21    
HELIX   71  71 SER G  114  ALA G  122  1                                   9    
HELIX   72  72 SER G  127  LEU G  142  1                                  16    
HELIX   73  73 ALA G  151  VAL G  163  1                                  13    
HELIX   74  74 HIS G  168  ASP G  186  1                                  19    
HELIX   75  75 LEU G  188  LEU G  192  5                                   5    
HELIX   76  76 PRO G  193  VAL G  206  1                                  14    
HELIX   77  77 PRO G  207  ILE G  211  5                                   5    
HELIX   78  78 GLY G  219  GLY G  229  1                                  11    
HELIX   79  79 ASP G  231  PHE G  249  1                                  19    
SHEET    1   A 5 TYR A  13  GLY A  22  0                                        
SHEET    2   A 5 GLY A  25  ASP A  32 -1  N  GLY A  25   O  GLY A  22           
SHEET    3   A 5 PHE A  39  GLN A  48 -1  N  VAL A  40   O  ALA A  30           
SHEET    4   A 5 GLU A  91  GLU A  99 -1  O  THR A  92   N  VAL A  47           
SHEET    5   A 5 LEU A  79  SER A  86 -1  N  PHE A  80   O  VAL A  97           
SHEET    1   B 2 ILE A 151  VAL A 153  0                                        
SHEET    2   B 2 ILE A 159  LEU A 161 -1  O  LYS A 160   N  LEU A 152           
SHEET    1   C 2 ILE A 169  PHE A 172  0                                        
SHEET    2   C 2 THR A 177  VAL A 180 -1  O  THR A 177   N  PHE A 172           
SHEET    1   D 5 TYR E  13  GLY E  22  0                                        
SHEET    2   D 5 GLY E  25  ASP E  32 -1  N  GLY E  25   O  GLY E  22           
SHEET    3   D 5 PHE E  39  GLN E  48 -1  O  VAL E  40   N  ALA E  30           
SHEET    4   D 5 GLU E  91  GLU E  99 -1  O  THR E  92   N  VAL E  47           
SHEET    5   D 5 LEU E  79  SER E  86 -1  N  PHE E  80   O  VAL E  97           
SHEET    1   E 2 ILE E 151  VAL E 153  0                                        
SHEET    2   E 2 ILE E 159  LEU E 161 -1  O  LYS E 160   N  LEU E 152           
SHEET    1   F 2 ILE E 169  PHE E 172  0                                        
SHEET    2   F 2 THR E 177  VAL E 180 -1  O  THR E 177   N  PHE E 172           
CRYST1   77.780  146.950  164.820  90.00  90.00  90.00 P 21 21 21    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      0.012860  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006810  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006070        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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