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Database: PDB
Entry: 1JST
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Original site: 1JST 
HEADER    COMPLEX (PROTEIN KINASE/CYCLIN)         03-JUL-96   1JST              
TITLE     PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE-2;                                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CDK2;                                                       
COMPND   5 EC: 2.7.1.-;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: PHOSPHORYLATED;                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CYCLIN A;                                                  
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: RESIDUES 173-432;                                          
COMPND  12 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: SF9;                                                      
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS VECTOR;                        
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PET3A;                                    
SOURCE  13 OTHER_DETAILS: CYCLIN A-BOUND FORM PHOSPHORYLATED ON THR 160 IN      
SOURCE  14 VITRO USING A CDK-ACTIVATING KINASE CONSISTING OF THE CYCLINH-CDK7   
SOURCE  15 COMPLEX;                                                             
SOURCE  16 MOL_ID: 2;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 CELL_LINE: SF9;                                                      
SOURCE  21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  23 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  24 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  25 EXPRESSION_SYSTEM_PLASMID: PET3A;                                    
SOURCE  26 OTHER_DETAILS: THE FRAGMENT USED IN THE CRYSTALLIZATION (RESIDUES    
SOURCE  27 173-432) WAS PRODUCED BY THE CLEAVAGE OF FULL-LENGTH CYCLIN A BY     
SOURCE  28 SUBTILISIN                                                           
KEYWDS    COMPLEX (PROTEIN KINASE-CYCLIN), CYCLIN, CDK, PHOSPHORYLATION,        
KEYWDS   2 COMPLEX (PROTEIN KINASE-CYCLIN) COMPLEX                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.A.RUSSO,P.D.JEFFREY,N.P.PAVLETICH                                   
REVDAT   3   13-JUL-11 1JST    1       VERSN                                    
REVDAT   2   24-FEB-09 1JST    1       VERSN                                    
REVDAT   1   11-JAN-97 1JST    0                                                
JRNL        AUTH   A.A.RUSSO,P.D.JEFFREY,N.P.PAVLETICH                          
JRNL        TITL   STRUCTURAL BASIS OF CYCLIN-DEPENDENT KINASE ACTIVATION BY    
JRNL        TITL 2 PHOSPHORYLATION.                                             
JRNL        REF    NAT.STRUCT.BIOL.              V.   3   696 1996              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   8756328                                                      
JRNL        DOI    10.1038/NSB0896-696                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 39189                          
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8972                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 64                                      
REMARK   3   SOLVENT ATOMS            : 98                                      
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.013 ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : 1.740 ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; 2.700 ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : 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  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : NULL                                             
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1JST COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
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        : 22-DEC-95                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.920                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       69.80000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.10000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       74.55000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.10000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       69.80000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       74.55000            
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                                                 
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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    PRO B 204   C   -  N   -  CA  ANGL. DEV. =  16.8 DEGREES          
REMARK 500    PRO B 204   C   -  N   -  CD  ANGL. DEV. = -13.2 DEGREES          
REMARK 500    ASP B 345   N   -  CA  -  C   ANGL. DEV. = -16.3 DEGREES          
REMARK 500    LEU C  76   CA  -  CB  -  CG  ANGL. DEV. =  20.0 DEGREES          
REMARK 500    PRO D 176   C   -  N   -  CA  ANGL. DEV. =   9.9 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    GLU A   8      176.61    166.40                                   
REMARK 500    ILE A  10     -119.09    -97.20                                   
REMARK 500    THR A  14      -86.75     43.27                                   
REMARK 500    LEU A  37     -145.69     75.47                                   
REMARK 500    ASP A  38       51.80   -156.54                                   
REMARK 500    THR A  39      -51.28    -24.82                                   
REMARK 500    THR A  41     -144.82   -159.98                                   
REMARK 500    LEU A  96      -76.86     67.26                                   
REMARK 500    THR A  97      -72.87    -12.70                                   
REMARK 500    ARG A 122       52.51     31.98                                   
REMARK 500    ASP A 127       40.64   -150.79                                   
REMARK 500    ASP A 145       78.76     48.93                                   
REMARK 500    PHE A 146       30.29    -92.24                                   
REMARK 500    GLU A 162       90.01     47.63                                   
REMARK 500    VAL A 164      135.16     80.72                                   
REMARK 500    SER A 181     -153.79   -161.05                                   
REMARK 500    PRO A 228      105.18    -45.32                                   
REMARK 500    ASP B 177      -16.14    -42.73                                   
REMARK 500    VAL B 197       -9.35    -53.11                                   
REMARK 500    THR B 282       56.74    -92.27                                   
REMARK 500    ASP B 283       97.01    -23.16                                   
REMARK 500    ASP B 284      -14.41     66.93                                   
REMARK 500    VAL C   7      -81.55    -90.04                                   
REMARK 500    GLU C   8     -168.34   -111.12                                   
REMARK 500    ILE C  10     -130.62   -135.85                                   
REMARK 500    THR C  14      -83.28     65.85                                   
REMARK 500    VAL C  18       93.29     11.59                                   
REMARK 500    ASP C  38       77.45   -103.17                                   
REMARK 500    THR C  41      -90.86   -128.69                                   
REMARK 500    LEU C  96      -26.15     98.47                                   
REMARK 500    ASP C 127       41.80   -150.65                                   
REMARK 500    ASP C 145       86.29     53.92                                   
REMARK 500    ARG C 157     -155.24    -93.90                                   
REMARK 500    GLU C 162       96.06     16.17                                   
REMARK 500    VAL C 163     -163.70   -111.31                                   
REMARK 500    VAL C 164      148.27     66.67                                   
REMARK 500    LEU C 166      -64.21    -26.21                                   
REMARK 500    PRO C 204       58.40    -67.45                                   
REMARK 500    SER C 207      168.69    179.25                                   
REMARK 500    PRO C 228      104.52    -53.54                                   
REMARK 500    VAL C 251      -72.08    -55.25                                   
REMARK 500    ILE C 275      156.57    -42.38                                   
REMARK 500    HIS C 283      134.82    -21.35                                   
REMARK 500    GLN C 287      -28.92    -28.88                                   
REMARK 500    THR C 290     -139.29   -128.92                                   
REMARK 500    LYS C 291       68.65   -160.44                                   
REMARK 500    PRO D 176      -24.79    -25.31                                   
REMARK 500    ASP D 177      -67.76   -120.76                                   
REMARK 500    ARG D 250      -36.05    -38.27                                   
REMARK 500    ASP D 283       66.39     39.84                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR D 347         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR A 231        24.5      L          L   OUTSIDE RANGE           
REMARK 500    VAL C  18        24.8      L          L   OUTSIDE RANGE           
REMARK 500    HIS C  84        23.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 299  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 132   OD1                                                    
REMARK 620 2 ATP A 300   O2A 109.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 299  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C 132   OD1                                                    
REMARK 620 2 ATP C 300   O2G 122.0                                              
REMARK 620 3 ATP C 300   O5' 105.3  89.0                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 299                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 299                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C 300                 
DBREF  1JST A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  1JST B  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
DBREF  1JST C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  1JST D  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
SEQADV 1JST TPO A  160  UNP  P24941    THR   160 MODIFIED RESIDUE               
SEQADV 1JST TPO C  160  UNP  P24941    THR   160 MODIFIED RESIDUE               
SEQRES   1 A  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 A  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 A  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 A  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 A  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 A  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 A  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 A  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 A  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 A  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 A  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 A  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 A  298  ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 A  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 A  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 A  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 A  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 A  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 A  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 A  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 A  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 A  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 A  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
SEQRES   1 B  258  VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 B  258  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 B  258  LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 B  258  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 B  258  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 B  258  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 B  258  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 B  258  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 B  258  VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL          
SEQRES  10 B  258  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE          
SEQRES  11 B  258  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 B  258  TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 B  258  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 B  258  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA          
SEQRES  15 B  258  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 B  258  GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR          
SEQRES  17 B  258  THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS          
SEQRES  18 B  258  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 B  258  ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL          
SEQRES  20 B  258  SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU                  
SEQRES   1 C  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 C  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 C  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 C  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 C  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 C  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 C  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 C  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 C  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 C  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 C  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 C  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 C  298  ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 C  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 C  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 C  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 C  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 C  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 C  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 C  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 C  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 C  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 C  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
SEQRES   1 D  258  VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 D  258  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 D  258  LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 D  258  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 D  258  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 D  258  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 D  258  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 D  258  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 D  258  VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL          
SEQRES  10 D  258  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE          
SEQRES  11 D  258  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 D  258  TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 D  258  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 D  258  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA          
SEQRES  15 D  258  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 D  258  GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR          
SEQRES  17 D  258  THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS          
SEQRES  18 D  258  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 D  258  ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL          
SEQRES  20 D  258  SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU                  
MODRES 1JST TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 1JST TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET     MN  A 299       1                                                       
HET     MN  C 299       1                                                       
HET    ATP  A 300      31                                                       
HET    ATP  C 300      31                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5   MN    2(MN 2+)                                                     
FORMUL   7  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL   9  HOH   *98(H2 O)                                                     
HELIX    1   1 SER A   46  LEU A   55  1                                  10    
HELIX    2   2 LEU A   87  ALA A   93  1                                   7    
HELIX    3   3 LEU A  101  HIS A  121  1                                  21    
HELIX    4   4 PRO A  130  ASN A  132  5                                   3    
HELIX    5   5 LEU A  166  TYR A  168  5                                   3    
HELIX    6   6 PRO A  171  LEU A  174  1                                   4    
HELIX    7   7 THR A  182  THR A  198  5                                  17    
HELIX    8   8 GLU A  208  LEU A  219  1                                  12    
HELIX    9   9 VAL A  230  SER A  232  5                                   3    
HELIX   10  10 PHE A  248  VAL A  251  1                                   4    
HELIX   11  11 GLU A  257  MET A  266  1                                  10    
HELIX   12  12 ALA A  277  ALA A  280  1                                   4    
HELIX   13  13 PRO A  284  ASP A  288  5                                   5    
HELIX   14  14 PRO B  176  LYS B  192  5                                  17    
HELIX   15  15 TYR B  199  LYS B  202  1                                   4    
HELIX   16  16 ASN B  208  GLU B  224  1                                  17    
HELIX   17  17 ASN B  229  LEU B  243  1                                  15    
HELIX   18  18 LEU B  253  GLU B  268  1                                  16    
HELIX   19  19 VAL B  275  ILE B  281  1                                   7    
HELIX   20  20 LYS B  288  VAL B  301  1                                  14    
HELIX   21  21 VAL B  311  HIS B  321  1                                  11    
HELIX   22  22 CYS B  327  ILE B  342  1                                  16    
HELIX   23  23 ALA B  344  LYS B  349  1                                   6    
HELIX   24  24 PRO B  352  THR B  368  1                                  17    
HELIX   25  25 GLU B  374  THR B  380  1                                   7    
HELIX   26  26 LEU B  384  GLN B  403  1                                  20    
HELIX   27  27 SER B  408  LYS B  412  1                                   5    
HELIX   28  28 SER B  416  TYR B  418  5                                   3    
HELIX   29  29 VAL B  421  LEU B  423  5                                   3    
HELIX   30  30 SER C   46  GLU C   57  1                                  12    
HELIX   31  31 LEU C   87  ALA C   93  1                                   7    
HELIX   32  32 LEU C  101  HIS C  121  1                                  21    
HELIX   33  33 PRO C  130  ASN C  132  5                                   3    
HELIX   34  34 LEU C  166  TYR C  168  5                                   3    
HELIX   35  35 PRO C  171  LEU C  174  1                                   4    
HELIX   36  36 THR C  182  VAL C  197  5                                  16    
HELIX   37  37 GLU C  208  LEU C  219  1                                  12    
HELIX   38  38 VAL C  230  SER C  232  5                                   3    
HELIX   39  39 PHE C  248  VAL C  251  1                                   4    
HELIX   40  40 GLU C  257  MET C  266  1                                  10    
HELIX   41  41 PRO C  271  LYS C  273  5                                   3    
HELIX   42  42 ALA C  277  ALA C  282  1                                   6    
HELIX   43  43 PRO C  284  ASP C  288  5                                   5    
HELIX   44  44 TYR D  178  GLU D  190  1                                  13    
HELIX   45  45 TYR D  199  LYS D  202  5                                   4    
HELIX   46  46 ASN D  208  TYR D  225  1                                  18    
HELIX   47  47 ASN D  229  SER D  245  1                                  17    
HELIX   48  48 LEU D  253  GLU D  268  1                                  16    
HELIX   49  49 VAL D  275  THR D  282  1                                   8    
HELIX   50  50 LYS D  288  VAL D  301  1                                  14    
HELIX   51  51 VAL D  311  HIS D  321  1                                  11    
HELIX   52  52 CYS D  327  ILE D  342  1                                  16    
HELIX   53  53 ALA D  344  LYS D  349  1                                   6    
HELIX   54  54 PRO D  352  THR D  368  1                                  17    
HELIX   55  55 GLU D  374  THR D  380  1                                   7    
HELIX   56  56 LYS D  388  GLN D  403  1                                  16    
HELIX   57  57 SER D  408  LYS D  414  1                                   7    
HELIX   58  58 VAL D  421  LEU D  423  5                                   3    
SHEET    1   A 5 LEU A  66  HIS A  71  0                                        
SHEET    2   A 5 LEU A  76  GLU A  81 -1  N  VAL A  79   O  LEU A  67           
SHEET    3   A 5 VAL A  29  ILE A  35 -1  N  ILE A  35   O  LEU A  76           
SHEET    4   A 5 VAL A  18  ASN A  23 -1  N  ALA A  21   O  VAL A  30           
SHEET    5   A 5 PHE A   4  LYS A   9 -1  N  GLU A   8   O  LYS A  20           
SHEET    1   B 2 LEU A 133  ILE A 135  0                                        
SHEET    2   B 2 ILE A 141  LEU A 143 -1  N  LYS A 142   O  LEU A 134           
SHEET    1   C 5 LEU C  66  HIS C  71  0                                        
SHEET    2   C 5 LYS C  75  GLU C  81 -1  N  VAL C  79   O  LEU C  67           
SHEET    3   C 5 VAL C  29  ARG C  36 -1  N  ILE C  35   O  LEU C  76           
SHEET    4   C 5 TYR C  19  ASN C  23 -1  N  ALA C  21   O  VAL C  30           
SHEET    5   C 5 PHE C   4  LYS C   9 -1  N  GLU C   8   O  LYS C  20           
SHEET    1   D 2 LEU C 133  ILE C 135  0                                        
SHEET    2   D 2 ILE C 141  LEU C 143 -1  N  LYS C 142   O  LEU C 134           
LINK         N   TPO A 160                 C   TYR A 159     1555   1555  1.32  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
LINK         N   TPO C 160                 C   TYR C 159     1555   1555  1.32  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.34  
LINK        MN    MN A 299                 OD1 ASN A 132     1555   1555  2.28  
LINK        MN    MN C 299                 OD1 ASN C 132     1555   1555  2.23  
LINK        MN    MN A 299                 O2A ATP A 300     1555   1555  2.48  
LINK        MN    MN C 299                 O2G ATP C 300     1555   1555  2.43  
LINK        MN    MN C 299                 O5' ATP C 300     1555   1555  2.52  
CISPEP   1 VAL A  154    PRO A  155          0        -0.81                     
CISPEP   2 GLN B  323    PRO B  324          0        -0.55                     
CISPEP   3 ASP B  345    PRO B  346          0        -0.34                     
CISPEP   4 VAL C  154    PRO C  155          0        -0.07                     
CISPEP   5 GLN D  323    PRO D  324          0         0.10                     
CISPEP   6 ASP D  345    PRO D  346          0         0.56                     
SITE     1 AC1  3 ASN A 132  ASP A 145  ATP A 300                               
SITE     1 AC2  3 ASN C 132  ASP C 145  ATP C 300                               
SITE     1 AC3 18 ILE A  10  GLY A  11  GLU A  12  GLY A  13                    
SITE     2 AC3 18 THR A  14  TYR A  15  VAL A  18  ALA A  31                    
SITE     3 AC3 18 LYS A  33  GLU A  51  PHE A  80  GLU A  81                    
SITE     4 AC3 18 PHE A  82  LEU A  83  ASP A  86  ASP A 145                    
SITE     5 AC3 18  MN A 299  HOH A 329                                          
SITE     1 AC4 18 ILE C  10  GLY C  11  GLY C  13  THR C  14                    
SITE     2 AC4 18 TYR C  15  GLY C  16  VAL C  18  ALA C  31                    
SITE     3 AC4 18 LYS C  33  GLU C  81  PHE C  82  LEU C  83                    
SITE     4 AC4 18 ASP C  86  GLN C 131  LEU C 134  ASP C 145                    
SITE     5 AC4 18  MN C 299  HOH C 316                                          
CRYST1  139.600  149.100   74.200  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      0.007163  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006707  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013477        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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