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Database: PDB
Entry: 1BI8
LinkDB: 1BI8
Original site: 1BI8 
HEADER    COMPLEX (KINASE/INHIBITOR)              22-JUN-98   1BI8              
TITLE     MECHANISM OF G1 CYCLIN DEPENDENT KINASE INHIBITION FROM THE           
TITLE    2 STRUCTURES CDK6-P19INK4D INHIBITOR COMPLEX                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 6;                                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CDK6;                                                       
COMPND   5 EC: 2.7.1.-;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYCLIN-DEPENDENT KINASE INHIBITOR;                         
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 SYNONYM: P19INK4D;                                                   
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, COMPLEX (KINASE/INHIBITOR)           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.A.RUSSO,L.TONG,J.O.LEE,P.D.JEFFREY,N.P.PAVLETICH                    
REVDAT   3   24-FEB-09 1BI8    1       VERSN                                    
REVDAT   2   16-FEB-99 1BI8    1       SOURCE COMPND REMARK DBREF               
REVDAT   2 2                   1       SEQADV KEYWDS HEADER HELIX               
REVDAT   1   13-JAN-99 1BI8    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.    2.80 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) : 2.80                           
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)   (%) : 85.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 27794                          
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) : 0.255                           
REMARK   3   FREE R VALUE                     : 0.308                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1407                            
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            : 3397                                    
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) : -29.00000                                            
REMARK   3    B22 (A**2) : -8.00000                                             
REMARK   3    B33 (A**2) : 37.00000                                             
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : 17.90000                                             
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) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.05                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.800 ; 3.800                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.800 ; 3.800                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : STRICT                                                  
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  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:  REFINED WITH NCS STRICT THROUGHOUT       
REMARK   4                                                                      
REMARK   4 1BI8 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-98                             
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0060                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33400                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
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     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 2.650                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.32000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.8                                            
REMARK 200 STARTING MODEL: BNL-22910                                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       48.43000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.03000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       48.43000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       58.03000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     ALA A     9                                                      
REMARK 465     ASP A    10                                                      
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     THR A    88                                                      
REMARK 465     ASP A    89                                                      
REMARK 465     ARG A    90                                                      
REMARK 465     GLU A    91                                                      
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     LEU B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     HIS B   161                                                      
REMARK 465     MET B   162                                                      
REMARK 465     VAL B   163                                                      
REMARK 465     ALA B   164                                                      
REMARK 465     PRO B   165                                                      
REMARK 465     LEU B   166                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     ASP C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     LEU C     6                                                      
REMARK 465     CYS C     7                                                      
REMARK 465     ARG C     8                                                      
REMARK 465     ALA C     9                                                      
REMARK 465     ASP C    10                                                      
REMARK 465     THR C    49                                                      
REMARK 465     GLY C    50                                                      
REMARK 465     GLU C    51                                                      
REMARK 465     GLU C    52                                                      
REMARK 465     GLY C    53                                                      
REMARK 465     MET C    54                                                      
REMARK 465     PRO C    55                                                      
REMARK 465     LEU C    56                                                      
REMARK 465     SER C    57                                                      
REMARK 465     THR C    58                                                      
REMARK 465     ILE C    59                                                      
REMARK 465     ARG C    60                                                      
REMARK 465     GLU C    61                                                      
REMARK 465     VAL C    62                                                      
REMARK 465     ALA C    63                                                      
REMARK 465     VAL C    64                                                      
REMARK 465     LEU C    65                                                      
REMARK 465     ARG C    66                                                      
REMARK 465     HIS C    67                                                      
REMARK 465     LEU C    68                                                      
REMARK 465     GLU C    69                                                      
REMARK 465     THR C    70                                                      
REMARK 465     PHE C    71                                                      
REMARK 465     THR C    88                                                      
REMARK 465     ASP C    89                                                      
REMARK 465     ARG C    90                                                      
REMARK 465     GLU C    91                                                      
REMARK 465     ASP C   302                                                      
REMARK 465     LEU C   303                                                      
REMARK 465     GLU C   304                                                      
REMARK 465     ARG C   305                                                      
REMARK 465     CYS C   306                                                      
REMARK 465     LYS C   307                                                      
REMARK 465     GLU C   308                                                      
REMARK 465     ASN C   309                                                      
REMARK 465     LEU C   310                                                      
REMARK 465     ASP C   311                                                      
REMARK 465     SER C   312                                                      
REMARK 465     HIS C   313                                                      
REMARK 465     LEU C   314                                                      
REMARK 465     PRO C   315                                                      
REMARK 465     PRO C   316                                                      
REMARK 465     SER C   317                                                      
REMARK 465     GLN C   318                                                      
REMARK 465     ASN C   319                                                      
REMARK 465     THR C   320                                                      
REMARK 465     SER C   321                                                      
REMARK 465     GLU C   322                                                      
REMARK 465     LEU C   323                                                      
REMARK 465     ASN C   324                                                      
REMARK 465     THR C   325                                                      
REMARK 465     ALA C   326                                                      
REMARK 465     MET D     1                                                      
REMARK 465     LEU D     2                                                      
REMARK 465     LEU D     3                                                      
REMARK 465     GLU D     4                                                      
REMARK 465     GLU D     5                                                      
REMARK 465     HIS D   161                                                      
REMARK 465     MET D   162                                                      
REMARK 465     VAL D   163                                                      
REMARK 465     ALA D   164                                                      
REMARK 465     PRO D   165                                                      
REMARK 465     LEU D   166                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CB   ALA C   175     CB   ALA C   175     2755     0.74            
REMARK 500   CB   ALA A   175     N    ALA C   175     1455     1.56            
REMARK 500   NE2  GLN A   301     NE2  GLN C   301     3455     1.58            
REMARK 500   CA   ALA A   175     CG   MET C   174     1455     1.74            
REMARK 500   CA   ALA A   175     SD   MET C   174     1455     1.84            
REMARK 500   CB   ALA A   175     CB   ALA C   175     1455     1.89            
REMARK 500   CB   ALA A   175     SD   MET C   174     1455     2.06            
REMARK 500   CB   ALA A   175     CA   ALA C   175     1455     2.07            
REMARK 500   O    ASP A   246     O    GLY C    22     2655     2.15            
REMARK 500   CA   ALA C   175     CB   ALA C   175     2755     2.17            
REMARK 500   C    ALA A   175     SD   MET C   174     1455     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    GLU A  18   CG    GLU A  18   CD      0.093                       
REMARK 500    GLU C  18   CG    GLU C  18   CD      0.093                       
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    LEU A 176   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    LEU A 202   CA  -  CB  -  CG  ANGL. DEV. = -20.2 DEGREES          
REMARK 500    LEU C 176   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    LEU C 202   CA  -  CB  -  CG  ANGL. DEV. = -20.2 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    ARG A  38      122.62      1.73                                   
REMARK 500    GLN A 103      131.95   -175.42                                   
REMARK 500    GLU A 114      -39.13    -29.34                                   
REMARK 500    THR A 119      -53.30    -29.26                                   
REMARK 500    ARG A 140       63.97     27.10                                   
REMARK 500    ARG A 144      -14.96     64.66                                   
REMARK 500    LEU A 146       42.96    -76.45                                   
REMARK 500    ASP A 163       88.19   -161.05                                   
REMARK 500    MET A 174      140.06     96.36                                   
REMARK 500    ALA A 175      -84.30      1.49                                   
REMARK 500    LEU A 176       57.88    -66.00                                   
REMARK 500    SER A 194      -78.15   -102.48                                   
REMARK 500    TYR A 196       28.03   -155.11                                   
REMARK 500    LEU A 237      108.76    -56.11                                   
REMARK 500    PRO A 238      176.04    -56.68                                   
REMARK 500    ARG A 245      -89.53    -59.17                                   
REMARK 500    ASP A 246      -63.15    -23.85                                   
REMARK 500    VAL A 247      127.48     -4.11                                   
REMARK 500    LYS A 257       99.75      7.99                                   
REMARK 500    SER A 258     -139.43     55.69                                   
REMARK 500    ALA A 259       56.11    162.39                                   
REMARK 500    PHE A 265      -62.02   -127.82                                   
REMARK 500    LEU A 281       43.19    -65.62                                   
REMARK 500    LYS A 287       34.30    -88.49                                   
REMARK 500    PRO A 298        3.06    -62.06                                   
REMARK 500    PHE A 300       65.51   -106.63                                   
REMARK 500    ARG B   7      -89.41    -48.74                                   
REMARK 500    HIS B  29      -84.45    -82.58                                   
REMARK 500    ARG B  30       46.63    -66.63                                   
REMARK 500    GLU B  31      -39.12   -170.81                                   
REMARK 500    ALA B  65      106.00     56.54                                   
REMARK 500    GLU B  95      -17.48    -45.92                                   
REMARK 500    PRO B 110      -65.73    -28.45                                   
REMARK 500    GLN B 152      -73.15    -44.67                                   
REMARK 500    ARG C  38      122.70      1.63                                   
REMARK 500    GLN C 103      132.00   -175.42                                   
REMARK 500    GLU C 114      -39.08    -29.37                                   
REMARK 500    THR C 119      -53.36    -29.18                                   
REMARK 500    ARG C 140       64.03     27.01                                   
REMARK 500    ARG C 144      -14.95     64.63                                   
REMARK 500    LEU C 146       42.94    -76.42                                   
REMARK 500    ASP C 163       88.21   -161.05                                   
REMARK 500    MET C 174      140.01     96.29                                   
REMARK 500    ALA C 175      -84.33      1.55                                   
REMARK 500    LEU C 176       57.96    -66.04                                   
REMARK 500    SER C 194      -78.16   -102.46                                   
REMARK 500    TYR C 196       28.05   -155.12                                   
REMARK 500    LEU C 237      108.85    -56.14                                   
REMARK 500    PRO C 238      176.10    -56.74                                   
REMARK 500    ARG C 245      -89.57    -59.13                                   
REMARK 500    ASP C 246      -63.12    -23.81                                   
REMARK 500    VAL C 247      127.51     -4.21                                   
REMARK 500    LYS C 257       99.75      8.02                                   
REMARK 500    SER C 258     -139.44     55.72                                   
REMARK 500    ALA C 259       56.09    162.34                                   
REMARK 500    PHE C 265      -62.03   -127.85                                   
REMARK 500    LEU C 281       43.21    -65.63                                   
REMARK 500    LYS C 287       34.25    -88.50                                   
REMARK 500    PRO C 298        3.05    -62.04                                   
REMARK 500    PHE C 300       65.55   -106.63                                   
REMARK 500    ARG D   7      -89.38    -48.81                                   
REMARK 500    HIS D  29      -84.46    -82.64                                   
REMARK 500    ARG D  30       46.69    -66.60                                   
REMARK 500    GLU D  31      -39.15   -170.83                                   
REMARK 500    ALA D  65      105.94     56.59                                   
REMARK 500    GLU D  95      -17.48    -45.92                                   
REMARK 500    PRO D 110      -65.68    -28.51                                   
REMARK 500    GLN D 152      -73.17    -44.65                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1BI8 A    1   326  UNP    Q00534   CDK6_HUMAN       1    326             
DBREF  1BI8 B    1   166  UNP    P55273   CDN2D_HUMAN      1    166             
DBREF  1BI8 C    1   326  UNP    Q00534   CDK6_HUMAN       1    326             
DBREF  1BI8 D    1   166  UNP    P55273   CDN2D_HUMAN      1    166             
SEQRES   1 A  326  MET GLU LYS ASP GLY LEU CYS ARG ALA ASP GLN GLN TYR          
SEQRES   2 A  326  GLU CYS VAL ALA GLU ILE GLY GLU GLY ALA TYR GLY LYS          
SEQRES   3 A  326  VAL PHE LYS ALA ARG ASP LEU LYS ASN GLY GLY ARG PHE          
SEQRES   4 A  326  VAL ALA LEU LYS ARG VAL ARG VAL GLN THR GLY GLU GLU          
SEQRES   5 A  326  GLY MET PRO LEU SER THR ILE ARG GLU VAL ALA VAL LEU          
SEQRES   6 A  326  ARG HIS LEU GLU THR PHE GLU HIS PRO ASN VAL VAL ARG          
SEQRES   7 A  326  LEU PHE ASP VAL CYS THR VAL SER ARG THR ASP ARG GLU          
SEQRES   8 A  326  THR LYS LEU THR LEU VAL PHE GLU HIS VAL ASP GLN ASP          
SEQRES   9 A  326  LEU THR THR TYR LEU ASP LYS VAL PRO GLU PRO GLY VAL          
SEQRES  10 A  326  PRO THR GLU THR ILE LYS ASP MET MET PHE GLN LEU LEU          
SEQRES  11 A  326  ARG GLY LEU ASP PHE LEU HIS SER HIS ARG VAL VAL HIS          
SEQRES  12 A  326  ARG ASP LEU LYS PRO GLN ASN ILE LEU VAL THR SER SER          
SEQRES  13 A  326  GLY GLN ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ILE          
SEQRES  14 A  326  TYR SER PHE GLN MET ALA LEU THR SER VAL VAL VAL THR          
SEQRES  15 A  326  LEU TRP TYR ARG ALA PRO GLU VAL LEU LEU GLN SER SER          
SEQRES  16 A  326  TYR ALA THR PRO VAL ASP LEU TRP SER VAL GLY CYS ILE          
SEQRES  17 A  326  PHE ALA GLU MET PHE ARG ARG LYS PRO LEU PHE ARG GLY          
SEQRES  18 A  326  SER SER ASP VAL ASP GLN LEU GLY LYS ILE LEU ASP VAL          
SEQRES  19 A  326  ILE GLY LEU PRO GLY GLU GLU ASP TRP PRO ARG ASP VAL          
SEQRES  20 A  326  ALA LEU PRO ARG GLN ALA PHE HIS SER LYS SER ALA GLN          
SEQRES  21 A  326  PRO ILE GLU LYS PHE VAL THR ASP ILE ASP GLU LEU GLY          
SEQRES  22 A  326  LYS ASP LEU LEU LEU LYS CYS LEU THR PHE ASN PRO ALA          
SEQRES  23 A  326  LYS ARG ILE SER ALA TYR SER ALA LEU SER HIS PRO TYR          
SEQRES  24 A  326  PHE GLN ASP LEU GLU ARG CYS LYS GLU ASN LEU ASP SER          
SEQRES  25 A  326  HIS LEU PRO PRO SER GLN ASN THR SER GLU LEU ASN THR          
SEQRES  26 A  326  ALA                                                          
SEQRES   1 B  166  MET LEU LEU GLU GLU VAL ARG ALA GLY ASP ARG LEU SER          
SEQRES   2 B  166  GLY ALA ALA ALA ARG GLY ASP VAL GLN GLU VAL ARG ARG          
SEQRES   3 B  166  LEU LEU HIS ARG GLU LEU VAL HIS PRO ASP ALA LEU ASN          
SEQRES   4 B  166  ARG PHE GLY LYS THR ALA LEU GLN VAL MET MET PHE GLY          
SEQRES   5 B  166  SER THR ALA ILE ALA LEU GLU LEU LEU LYS GLN GLY ALA          
SEQRES   6 B  166  SER PRO ASN VAL GLN ASP THR SER GLY THR SER PRO VAL          
SEQRES   7 B  166  HIS ASP ALA ALA ARG THR GLY PHE LEU ASP THR LEU LYS          
SEQRES   8 B  166  VAL LEU VAL GLU HIS GLY ALA ASP VAL ASN VAL PRO ASP          
SEQRES   9 B  166  GLY THR GLY ALA LEU PRO ILE HIS LEU ALA VAL GLN GLU          
SEQRES  10 B  166  GLY HIS THR ALA VAL VAL SER PHE LEU ALA ALA GLU SER          
SEQRES  11 B  166  ASP LEU HIS ARG ARG ASP ALA ARG GLY LEU THR PRO LEU          
SEQRES  12 B  166  GLU LEU ALA LEU GLN ARG GLY ALA GLN ASP LEU VAL ASP          
SEQRES  13 B  166  ILE LEU GLN GLY HIS MET VAL ALA PRO LEU                      
SEQRES   1 C  326  MET GLU LYS ASP GLY LEU CYS ARG ALA ASP GLN GLN TYR          
SEQRES   2 C  326  GLU CYS VAL ALA GLU ILE GLY GLU GLY ALA TYR GLY LYS          
SEQRES   3 C  326  VAL PHE LYS ALA ARG ASP LEU LYS ASN GLY GLY ARG PHE          
SEQRES   4 C  326  VAL ALA LEU LYS ARG VAL ARG VAL GLN THR GLY GLU GLU          
SEQRES   5 C  326  GLY MET PRO LEU SER THR ILE ARG GLU VAL ALA VAL LEU          
SEQRES   6 C  326  ARG HIS LEU GLU THR PHE GLU HIS PRO ASN VAL VAL ARG          
SEQRES   7 C  326  LEU PHE ASP VAL CYS THR VAL SER ARG THR ASP ARG GLU          
SEQRES   8 C  326  THR LYS LEU THR LEU VAL PHE GLU HIS VAL ASP GLN ASP          
SEQRES   9 C  326  LEU THR THR TYR LEU ASP LYS VAL PRO GLU PRO GLY VAL          
SEQRES  10 C  326  PRO THR GLU THR ILE LYS ASP MET MET PHE GLN LEU LEU          
SEQRES  11 C  326  ARG GLY LEU ASP PHE LEU HIS SER HIS ARG VAL VAL HIS          
SEQRES  12 C  326  ARG ASP LEU LYS PRO GLN ASN ILE LEU VAL THR SER SER          
SEQRES  13 C  326  GLY GLN ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ILE          
SEQRES  14 C  326  TYR SER PHE GLN MET ALA LEU THR SER VAL VAL VAL THR          
SEQRES  15 C  326  LEU TRP TYR ARG ALA PRO GLU VAL LEU LEU GLN SER SER          
SEQRES  16 C  326  TYR ALA THR PRO VAL ASP LEU TRP SER VAL GLY CYS ILE          
SEQRES  17 C  326  PHE ALA GLU MET PHE ARG ARG LYS PRO LEU PHE ARG GLY          
SEQRES  18 C  326  SER SER ASP VAL ASP GLN LEU GLY LYS ILE LEU ASP VAL          
SEQRES  19 C  326  ILE GLY LEU PRO GLY GLU GLU ASP TRP PRO ARG ASP VAL          
SEQRES  20 C  326  ALA LEU PRO ARG GLN ALA PHE HIS SER LYS SER ALA GLN          
SEQRES  21 C  326  PRO ILE GLU LYS PHE VAL THR ASP ILE ASP GLU LEU GLY          
SEQRES  22 C  326  LYS ASP LEU LEU LEU LYS CYS LEU THR PHE ASN PRO ALA          
SEQRES  23 C  326  LYS ARG ILE SER ALA TYR SER ALA LEU SER HIS PRO TYR          
SEQRES  24 C  326  PHE GLN ASP LEU GLU ARG CYS LYS GLU ASN LEU ASP SER          
SEQRES  25 C  326  HIS LEU PRO PRO SER GLN ASN THR SER GLU LEU ASN THR          
SEQRES  26 C  326  ALA                                                          
SEQRES   1 D  166  MET LEU LEU GLU GLU VAL ARG ALA GLY ASP ARG LEU SER          
SEQRES   2 D  166  GLY ALA ALA ALA ARG GLY ASP VAL GLN GLU VAL ARG ARG          
SEQRES   3 D  166  LEU LEU HIS ARG GLU LEU VAL HIS PRO ASP ALA LEU ASN          
SEQRES   4 D  166  ARG PHE GLY LYS THR ALA LEU GLN VAL MET MET PHE GLY          
SEQRES   5 D  166  SER THR ALA ILE ALA LEU GLU LEU LEU LYS GLN GLY ALA          
SEQRES   6 D  166  SER PRO ASN VAL GLN ASP THR SER GLY THR SER PRO VAL          
SEQRES   7 D  166  HIS ASP ALA ALA ARG THR GLY PHE LEU ASP THR LEU LYS          
SEQRES   8 D  166  VAL LEU VAL GLU HIS GLY ALA ASP VAL ASN VAL PRO ASP          
SEQRES   9 D  166  GLY THR GLY ALA LEU PRO ILE HIS LEU ALA VAL GLN GLU          
SEQRES  10 D  166  GLY HIS THR ALA VAL VAL SER PHE LEU ALA ALA GLU SER          
SEQRES  11 D  166  ASP LEU HIS ARG ARG ASP ALA ARG GLY LEU THR PRO LEU          
SEQRES  12 D  166  GLU LEU ALA LEU GLN ARG GLY ALA GLN ASP LEU VAL ASP          
SEQRES  13 D  166  ILE LEU GLN GLY HIS MET VAL ALA PRO LEU                      
HELIX    1   1 LEU A  105  LEU A  109  1                                   5    
HELIX    2   2 THR A  119  HIS A  137  1                                  19    
HELIX    3   3 PRO A  188  LEU A  191  1                                   4    
HELIX    4   4 THR A  198  ARG A  214  5                                  17    
HELIX    5   5 ASP A  224  ILE A  235  1                                  12    
HELIX    6   6 GLU A  240  ASP A  242  5                                   3    
HELIX    7   7 ARG A  251  ALA A  253  5                                   3    
HELIX    8   8 ILE A  262  LYS A  264  5                                   3    
HELIX    9  19 GLU A  271  CYS A  280  1                                  10    
HELIX   10  10 ALA A  291  SER A  296  1                                   6    
HELIX   11  11 ARG B    7  ARG B   18  1                                  12    
HELIX   12  12 VAL B   21  LEU B   28  1                                   8    
HELIX   13  13 ALA B   45  VAL B   48  1                                   4    
HELIX   14  14 THR B   54  LYS B   62  1                                   9    
HELIX   15  15 PRO B   77  THR B   84  1                                   8    
HELIX   16  16 LEU B   87  HIS B   96  1                                  10    
HELIX   17  17 PRO B  110  GLU B  117  1                                   8    
HELIX   18  17 THR B  120  GLU B  129  1                                  10    
HELIX   19  19 PRO B  142  ARG B  149  1                                   8    
HELIX   20  20 GLN B  152  LEU B  158  1                                   7    
HELIX   21  21 LEU C  105  LEU C  109  1                                   5    
HELIX   22  22 THR C  119  HIS C  137  1                                  19    
HELIX   23  23 PRO C  188  LEU C  191  1                                   4    
HELIX   24  24 THR C  198  ARG C  214  5                                  17    
HELIX   25  25 ASP C  224  ILE C  235  1                                  12    
HELIX   26  26 GLU C  240  ASP C  242  5                                   3    
HELIX   27  27 ARG C  251  ALA C  253  5                                   3    
HELIX   28  28 ILE C  262  LYS C  264  5                                   3    
HELIX   29  29 GLU C  271  CYS C  280  1                                  10    
HELIX   30  30 ALA C  291  SER C  296  1                                   6    
HELIX   31  31 ARG D    7  ARG D   18  1                                  12    
HELIX   32  32 VAL D   21  LEU D   28  1                                   8    
HELIX   33  33 ALA D   45  VAL D   48  1                                   4    
HELIX   34  34 THR D   54  LYS D   62  1                                   9    
HELIX   35  35 PRO D   77  THR D   84  1                                   8    
HELIX   36  36 LEU D   87  HIS D   96  1                                  10    
HELIX   37  37 PRO D  110  GLU D  117  1                                   8    
HELIX   38  37 THR D  120  GLU D  129  1                                  10    
HELIX   39  39 PRO D  142  ARG D  149  1                                   8    
HELIX   40  30 GLN D  152  LEU D  158  1                                   7    
SHEET    1   A 5 LEU A  79  THR A  84  0                                        
SHEET    2   A 5 LYS A  93  PHE A  98 -1  N  VAL A  97   O  PHE A  80           
SHEET    3   A 5 PHE A  39  ARG A  46 -1  N  VAL A  45   O  LEU A  94           
SHEET    4   A 5 VAL A  27  ARG A  31 -1  N  ALA A  30   O  VAL A  40           
SHEET    5   A 5 GLU A  14  GLU A  18 -1  N  ALA A  17   O  LYS A  29           
SHEET    1   B 2 ILE A 151  VAL A 153  0                                        
SHEET    2   B 2 ILE A 159  LEU A 161 -1  N  LYS A 160   O  LEU A 152           
SHEET    1   C 5 LEU C  79  THR C  84  0                                        
SHEET    2   C 5 LYS C  93  PHE C  98 -1  N  VAL C  97   O  PHE C  80           
SHEET    3   C 5 PHE C  39  ARG C  46 -1  N  VAL C  45   O  LEU C  94           
SHEET    4   C 5 VAL C  27  ARG C  31 -1  N  ALA C  30   O  VAL C  40           
SHEET    5   C 5 GLU C  14  GLU C  18 -1  N  ALA C  17   O  LYS C  29           
SHEET    1   D 2 ILE C 151  VAL C 153  0                                        
SHEET    2   D 2 ILE C 159  LEU C 161 -1  N  LYS C 160   O  LEU C 152           
CRYST1   96.860  116.060  131.490  90.00 110.63  90.00 C 1 2 1       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      0.010324  0.000000  0.003887        0.00000                         
SCALE2      0.000000  0.008616  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008126        0.00000                         
MTRIX1   1 -0.965395  0.252602  0.064847       95.66276    1                    
MTRIX2   1 -0.251980 -0.967570  0.017727        7.52021    1                    
MTRIX3   1  0.067222  0.000774  0.997738       -1.44159    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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