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Database: PDB
Entry: 2CMV
LinkDB: 2CMV
Original site: 2CMV 
HEADER    OXIDOREDUCTASE                          15-MAY-06   2CMV              
TITLE     CRYSTAL STRUCTURE OF MOUSE CYTOSOLIC ISOCITRATE                       
TITLE    2 DEHYDROGENASE COMPLEXED WITH CADMIUM AND CITRATE                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ISOCITRATE DEHYDROGENASE [NADP] CYTOPLASMIC;               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 4-413;                                            
COMPND   5 SYNONYM: OXALOSUCCINATE DECARBOXYLASE, IDH, NADP, +-SPECIFIC ICDH),  
COMPND   6  IDP;                                                                
COMPND   7 EC: 1.1.1.42;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: DE3                                       
KEYWDS    TRICARBOXYLIC ACID CYCLE, ISOCITRATE DEHYDROGENASE, NADP, CADMIUM,    
KEYWDS   2 OXIDOREDUCTASE, GLYOXYLATE BYPASS                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.J.CHO,K.J.KIM,T.L.HUH,B.S.KANG                                      
REVDAT   3   13-JUL-11 2CMV    1       VERSN                                    
REVDAT   2   24-FEB-09 2CMV    1       VERSN                                    
REVDAT   1   29-MAY-07 2CMV    0                                                
JRNL        AUTH   H.J.CHO,K.J.KIM,T.L.HUH,B.S.KANG                             
JRNL        TITL   CRYSTAL STRUCTURE OF MOUSE CYTOSOLIC ISOCITRATE              
JRNL        TITL 2 DEHYDROGENASE COMPLEXED WITH CADMIUM AND CITRATE             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.52 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.52                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.87                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 27771                          
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 + TEST SET) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1476                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.52                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.58                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1798                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 98                           
REMARK   3   BIN FREE R VALUE                    : 0.3370                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6435                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 124                                     
REMARK   3   SOLVENT ATOMS            : 116                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.22000                                              
REMARK   3    B22 (A**2) : -0.33000                                             
REMARK   3    B33 (A**2) : 0.54000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.53000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.128         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.305         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.231         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.105        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6693 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9054 ; 1.340 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   817 ; 6.096 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   301 ;36.513 ;24.817       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1172 ;16.445 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;22.043 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   981 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5008 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3103 ; 0.207 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4597 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   326 ; 0.160 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    28 ; 0.193 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.077 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4169 ; 0.487 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6522 ; 0.776 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2900 ; 1.265 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2532 ; 1.988 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     4        A   413                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2700  -0.0250  31.8030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0498 T22:  -0.1148                                     
REMARK   3      T33:  -0.2425 T12:   0.0350                                     
REMARK   3      T13:  -0.0781 T23:   0.0384                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7343 L22:   0.7657                                     
REMARK   3      L33:   2.5156 L12:   0.4643                                     
REMARK   3      L13:  -0.2430 L23:   0.3091                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0008 S12:  -0.0824 S13:   0.0032                       
REMARK   3      S21:   0.0581 S22:  -0.0373 S23:   0.0766                       
REMARK   3      S31:   0.2117 S32:  -0.1398 S33:   0.0365                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     4        B   413                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.5230  -3.1440  16.8870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0942 T22:   0.2778                                     
REMARK   3      T33:  -0.2667 T12:   0.1348                                     
REMARK   3      T13:  -0.0807 T23:  -0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1673 L22:   0.6970                                     
REMARK   3      L33:   2.9676 L12:  -0.2803                                     
REMARK   3      L13:  -0.3286 L23:   0.5850                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0317 S12:   0.0313 S13:  -0.0265                       
REMARK   3      S21:  -0.0442 S22:   0.1287 S23:  -0.0578                       
REMARK   3      S31:   0.2298 S32:   1.0913 S33:  -0.0970                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2CMV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAY-06.                  
REMARK 100 THE PDBE ID CODE IS EBI-28733.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-JUN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 4A                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29260                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 4.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.03000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 2CMJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.8                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4                      
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       49.12300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.71400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       49.12300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       45.71400            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS B   413                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  87    CG   CD   CE   NZ                                   
REMARK 470     LYS A 233    CD   CE   NZ                                        
REMARK 470     LYS B  58    CD   CE   NZ                                        
REMARK 470     LYS B  65    CG   CD   CE   NZ                                   
REMARK 470     LYS B  66    CG   CD   CE   NZ                                   
REMARK 470     GLU B  80    CD   OE1  OE2                                       
REMARK 470     LYS B  81    CD   CE   NZ                                        
REMARK 470     GLU B  84    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 233    CD   CE   NZ                                        
REMARK 470     LYS B 301    CD   CE   NZ                                        
REMARK 470     GLN B 323    CD   OE1  NE2                                       
REMARK 470     LYS B 381    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A    94     OG1  FLC A  1416              2.13            
REMARK 500   NH1  ARG B    49     O    HOH B  2004              2.09            
REMARK 500   OG   SER B    94     OG2  FLC B  1416              2.17            
REMARK 500   O    ILE B    99     O    HOH B  2010              1.73            
REMARK 500   N    LEU B   103     O    HOH B  2010              2.03            
REMARK 500   OB1  FLC B  1416     O    HOH B  2048              1.87            
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  17     -127.10     36.00                                   
REMARK 500    ILE A  31      -66.09   -121.32                                   
REMARK 500    ASN A  68      -11.01     77.90                                   
REMARK 500    ASP A  79     -161.99   -104.83                                   
REMARK 500    ASP A 137     -139.12     47.87                                   
REMARK 500    ARG A 140       49.02   -148.33                                   
REMARK 500    ASP A 160       26.54    -74.21                                   
REMARK 500    THR A 162     -167.53    -58.01                                   
REMARK 500    LYS A 212       56.24   -116.33                                   
REMARK 500    LEU A 216       73.01   -108.87                                   
REMARK 500    ASN A 243       57.00     79.40                                   
REMARK 500    VAL A 312       44.35     79.94                                   
REMARK 500    ASN A 348       38.77     32.73                                   
REMARK 500    ALA A 412       30.29    -71.78                                   
REMARK 500    GLU B  17     -140.82     44.04                                   
REMARK 500    ILE B  21      -70.24    -62.75                                   
REMARK 500    ASN B  68       -6.58     77.46                                   
REMARK 500    LYS B  89      -76.81    -58.75                                   
REMARK 500    ASP B 137     -138.13     51.78                                   
REMARK 500    ASP B 252      -71.93    -41.08                                   
REMARK 500    MET B 290       67.36   -110.47                                   
REMARK 500    LYS B 301      -38.25   -140.31                                   
REMARK 500    ALA B 308      -47.21     62.79                                   
REMARK 500    SER B 326       96.28   -165.30                                   
REMARK 500    ASN B 348       14.90     46.27                                   
REMARK 500    GLN B 411        9.51    -54.66                                   
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                              CD A1414  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 279   OD2                                                    
REMARK 620 2 FLC A1416   OA1 142.1                                              
REMARK 620 3 HOH A2022   O    60.0  82.3                                        
REMARK 620 4 HOH A2051   O    70.5  97.2  73.0                                  
REMARK 620 5 ASP A 275   OD2 117.5  77.9 112.8 171.5                            
REMARK 620 6 ASP B 252   OD2 117.4  96.7 159.4  86.8  86.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD B1414  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 252   OD1                                                    
REMARK 620 2 ASP B 275   OD2  69.2                                              
REMARK 620 3 FLC B1416   OA2 102.5  88.8                                        
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  CD A1414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A1416                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CD B1414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC B1416                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A1415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B1415                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2CMJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE CYTOSOLIC                                
REMARK 900  ISOCITRATE DEHYDROGENASE                                            
DBREF  2CMV A    4   413  UNP    O88844   IDHC_MOUSE       4    413             
DBREF  2CMV B    4   413  UNP    O88844   IDHC_MOUSE       4    413             
SEQRES   1 A  410  LYS ILE GLN GLY GLY SER VAL VAL GLU MET GLN GLY ASP          
SEQRES   2 A  410  GLU MET THR ARG ILE ILE TRP GLU LEU ILE LYS GLU LYS          
SEQRES   3 A  410  LEU ILE LEU PRO TYR VAL GLU LEU ASP LEU HIS SER TYR          
SEQRES   4 A  410  ASP LEU GLY ILE GLU ASN ARG ASP ALA THR ASN ASP GLN          
SEQRES   5 A  410  VAL THR LYS ASP ALA ALA GLU ALA ILE LYS LYS TYR ASN          
SEQRES   6 A  410  VAL GLY VAL LYS CYS ALA THR ILE THR PRO ASP GLU LYS          
SEQRES   7 A  410  ARG VAL GLU GLU PHE LYS LEU LYS GLN MET TRP LYS SER          
SEQRES   8 A  410  PRO ASN GLY THR ILE ARG ASN ILE LEU GLY GLY THR VAL          
SEQRES   9 A  410  PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE PRO ARG LEU          
SEQRES  10 A  410  VAL THR GLY TRP VAL LYS PRO ILE ILE ILE GLY ARG HIS          
SEQRES  11 A  410  ALA TYR GLY ASP GLN TYR ARG ALA THR ASP PHE VAL VAL          
SEQRES  12 A  410  PRO GLY PRO GLY LYS VAL GLU ILE THR TYR THR PRO LYS          
SEQRES  13 A  410  ASP GLY THR GLN LYS VAL THR TYR MET VAL HIS ASP PHE          
SEQRES  14 A  410  GLU GLU GLY GLY GLY VAL ALA MET GLY MET TYR ASN GLN          
SEQRES  15 A  410  ASP LYS SER ILE GLU ASP PHE ALA HIS SER SER PHE GLN          
SEQRES  16 A  410  MET ALA LEU SER LYS GLY TRP PRO LEU TYR LEU SER THR          
SEQRES  17 A  410  LYS ASN THR ILE LEU LYS LYS TYR ASP GLY ARG PHE LYS          
SEQRES  18 A  410  ASP ILE PHE GLN GLU ILE TYR ASP LYS LYS TYR LYS SER          
SEQRES  19 A  410  GLN PHE GLU ALA GLN ASN ILE CYS TYR GLU HIS ARG LEU          
SEQRES  20 A  410  ILE ASP ASP MET VAL ALA GLN ALA MET LYS SER GLU GLY          
SEQRES  21 A  410  GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP GLY ASP VAL          
SEQRES  22 A  410  GLN SER ASP SER VAL ALA GLN GLY TYR GLY SER LEU GLY          
SEQRES  23 A  410  MET MET THR SER VAL LEU ILE CYS PRO ASP GLY LYS THR          
SEQRES  24 A  410  VAL GLU ALA GLU ALA ALA HIS GLY THR VAL THR ARG HIS          
SEQRES  25 A  410  TYR ARG MET TYR GLN LYS GLY GLN GLU THR SER THR ASN          
SEQRES  26 A  410  PRO ILE ALA SER ILE PHE ALA TRP SER ARG GLY LEU ALA          
SEQRES  27 A  410  HIS ARG ALA LYS LEU ASP ASN ASN THR GLU LEU SER PHE          
SEQRES  28 A  410  PHE ALA LYS ALA LEU GLU ASP VAL CYS ILE GLU THR ILE          
SEQRES  29 A  410  GLU ALA GLY PHE MET THR LYS ASP LEU ALA ALA CYS ILE          
SEQRES  30 A  410  LYS GLY LEU PRO ASN VAL GLN ARG SER ASP TYR LEU ASN          
SEQRES  31 A  410  THR PHE GLU PHE MET ASP LYS LEU GLY GLU ASN LEU LYS          
SEQRES  32 A  410  ALA LYS LEU ALA GLN ALA LYS                                  
SEQRES   1 B  410  LYS ILE GLN GLY GLY SER VAL VAL GLU MET GLN GLY ASP          
SEQRES   2 B  410  GLU MET THR ARG ILE ILE TRP GLU LEU ILE LYS GLU LYS          
SEQRES   3 B  410  LEU ILE LEU PRO TYR VAL GLU LEU ASP LEU HIS SER TYR          
SEQRES   4 B  410  ASP LEU GLY ILE GLU ASN ARG ASP ALA THR ASN ASP GLN          
SEQRES   5 B  410  VAL THR LYS ASP ALA ALA GLU ALA ILE LYS LYS TYR ASN          
SEQRES   6 B  410  VAL GLY VAL LYS CYS ALA THR ILE THR PRO ASP GLU LYS          
SEQRES   7 B  410  ARG VAL GLU GLU PHE LYS LEU LYS GLN MET TRP LYS SER          
SEQRES   8 B  410  PRO ASN GLY THR ILE ARG ASN ILE LEU GLY GLY THR VAL          
SEQRES   9 B  410  PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE PRO ARG LEU          
SEQRES  10 B  410  VAL THR GLY TRP VAL LYS PRO ILE ILE ILE GLY ARG HIS          
SEQRES  11 B  410  ALA TYR GLY ASP GLN TYR ARG ALA THR ASP PHE VAL VAL          
SEQRES  12 B  410  PRO GLY PRO GLY LYS VAL GLU ILE THR TYR THR PRO LYS          
SEQRES  13 B  410  ASP GLY THR GLN LYS VAL THR TYR MET VAL HIS ASP PHE          
SEQRES  14 B  410  GLU GLU GLY GLY GLY VAL ALA MET GLY MET TYR ASN GLN          
SEQRES  15 B  410  ASP LYS SER ILE GLU ASP PHE ALA HIS SER SER PHE GLN          
SEQRES  16 B  410  MET ALA LEU SER LYS GLY TRP PRO LEU TYR LEU SER THR          
SEQRES  17 B  410  LYS ASN THR ILE LEU LYS LYS TYR ASP GLY ARG PHE LYS          
SEQRES  18 B  410  ASP ILE PHE GLN GLU ILE TYR ASP LYS LYS TYR LYS SER          
SEQRES  19 B  410  GLN PHE GLU ALA GLN ASN ILE CYS TYR GLU HIS ARG LEU          
SEQRES  20 B  410  ILE ASP ASP MET VAL ALA GLN ALA MET LYS SER GLU GLY          
SEQRES  21 B  410  GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP GLY ASP VAL          
SEQRES  22 B  410  GLN SER ASP SER VAL ALA GLN GLY TYR GLY SER LEU GLY          
SEQRES  23 B  410  MET MET THR SER VAL LEU ILE CYS PRO ASP GLY LYS THR          
SEQRES  24 B  410  VAL GLU ALA GLU ALA ALA HIS GLY THR VAL THR ARG HIS          
SEQRES  25 B  410  TYR ARG MET TYR GLN LYS GLY GLN GLU THR SER THR ASN          
SEQRES  26 B  410  PRO ILE ALA SER ILE PHE ALA TRP SER ARG GLY LEU ALA          
SEQRES  27 B  410  HIS ARG ALA LYS LEU ASP ASN ASN THR GLU LEU SER PHE          
SEQRES  28 B  410  PHE ALA LYS ALA LEU GLU ASP VAL CYS ILE GLU THR ILE          
SEQRES  29 B  410  GLU ALA GLY PHE MET THR LYS ASP LEU ALA ALA CYS ILE          
SEQRES  30 B  410  LYS GLY LEU PRO ASN VAL GLN ARG SER ASP TYR LEU ASN          
SEQRES  31 B  410  THR PHE GLU PHE MET ASP LYS LEU GLY GLU ASN LEU LYS          
SEQRES  32 B  410  ALA LYS LEU ALA GLN ALA LYS                                  
HET     CD  A1414       1                                                       
HET    FLC  A1416      13                                                       
HET     CD  B1414       1                                                       
HET    FLC  B1416      13                                                       
HET    NAP  A1415      48                                                       
HET    NAP  B1415      48                                                       
HETNAM      CD CADMIUM ION                                                      
HETNAM     FLC CITRATE ANION                                                    
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE                           
HETNAM   2 NAP  PHOSPHATE                                                       
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
FORMUL   3   CD    2(CD 2+)                                                     
FORMUL   4  FLC    2(C6 H5 O7 3-)                                               
FORMUL   7  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   9  HOH   *116(H2 O)                                                    
HELIX    1   1 ASP A   16  ILE A   31  1                                  16    
HELIX    2   2 GLY A   45  THR A   52  1                                   8    
HELIX    3   3 ASP A   54  ASN A   68  1                                  15    
HELIX    4   4 ASP A   79  LYS A   87  1                                   9    
HELIX    5   5 SER A   94  GLY A  104  1                                  11    
HELIX    6   6 GLY A  136  ALA A  141  5                                   6    
HELIX    7   7 ASP A  186  GLY A  204  1                                  19    
HELIX    8   8 LYS A  218  TYR A  235  1                                  18    
HELIX    9   9 TYR A  235  ASN A  243  1                                   9    
HELIX   10  10 ILE A  251  SER A  261  1                                  11    
HELIX   11  11 LYS A  270  GLY A  286  1                                  17    
HELIX   12  12 VAL A  312  LYS A  321  1                                  10    
HELIX   13  13 PRO A  329  ASP A  347  1                                  19    
HELIX   14  14 ASN A  349  ALA A  369  1                                  21    
HELIX   15  15 THR A  373  GLY A  382  1                                  10    
HELIX   16  16 GLN A  387  TYR A  391  5                                   5    
HELIX   17  17 ASN A  393  ALA A  412  1                                  20    
HELIX   18  18 ASP B   16  ILE B   31  1                                  16    
HELIX   19  19 GLY B   45  THR B   52  1                                   8    
HELIX   20  20 ASP B   54  ASN B   68  1                                  15    
HELIX   21  21 ASP B   79  LYS B   87  1                                   9    
HELIX   22  22 SER B   94  GLY B  104  1                                  11    
HELIX   23  23 GLY B  136  ALA B  141  5                                   6    
HELIX   24  24 ASP B  186  GLY B  204  1                                  19    
HELIX   25  25 LYS B  218  TYR B  235  1                                  18    
HELIX   26  26 TYR B  235  GLN B  242  1                                   8    
HELIX   27  27 ILE B  251  LYS B  260  1                                  10    
HELIX   28  28 LYS B  270  GLY B  286  1                                  17    
HELIX   29  29 VAL B  312  LYS B  321  1                                  10    
HELIX   30  30 PRO B  329  ASN B  348  1                                  20    
HELIX   31  31 ASN B  349  ALA B  369  1                                  21    
HELIX   32  32 THR B  373  GLY B  382  1                                  10    
HELIX   33  33 LEU B  383  VAL B  386  5                                   4    
HELIX   34  34 GLN B  387  TYR B  391  5                                   5    
HELIX   35  35 ASN B  393  GLN B  411  1                                  19    
SHEET    1  AA10 VAL A  35  ASP A  43  0                                        
SHEET    2  AA10 ILE A   5  GLN A  14  1  O  ILE A   5   N  GLU A  36           
SHEET    3  AA10 VAL A  69  LYS A  72  1  O  VAL A  69   N  VAL A  11           
SHEET    4  AA10 VAL A 303  GLU A 306  1  O  VAL A 303   N  GLY A  70           
SHEET    5  AA10 MET A 291  ILE A 296 -1  O  SER A 293   N  GLU A 306           
SHEET    6  AA10 THR A 106  ALA A 111 -1  O  THR A 106   N  ILE A 296           
SHEET    7  AA10 ILE A 128  HIS A 133 -1  O  ILE A 130   N  ARG A 109           
SHEET    8  AA10 PHE A 265  CYS A 269  1  O  PHE A 265   N  ILE A 129           
SHEET    9  AA10 LEU A 207  THR A 211  1  O  TYR A 208   N  ALA A 268           
SHEET   10  AA10 TYR A 246  LEU A 250  1  O  GLU A 247   N  LEU A 209           
SHEET    1  AB 4 THR A 142  VAL A 146  0                                        
SHEET    2  AB 4 GLY A 177  GLN A 185 -1  O  GLY A 177   N  VAL A 146           
SHEET    3  AB 4 GLY B 177  GLN B 185 -1  O  VAL B 178   N  ASN A 184           
SHEET    4  AB 4 THR B 142  VAL B 146 -1  O  THR B 142   N  GLY B 181           
SHEET    1  AC 4 VAL A 165  PHE A 172  0                                        
SHEET    2  AC 4 GLY A 150  PRO A 158 -1  O  GLY A 150   N  PHE A 172           
SHEET    3  AC 4 GLY B 150  PRO B 158 -1  O  LYS B 151   N  THR A 157           
SHEET    4  AC 4 VAL B 165  PHE B 172 -1  O  VAL B 165   N  TYR B 156           
SHEET    1  BA10 VAL B  35  HIS B  40  0                                        
SHEET    2  BA10 ILE B   5  MET B  13  1  O  ILE B   5   N  GLU B  36           
SHEET    3  BA10 VAL B  69  LYS B  72  1  O  VAL B  69   N  VAL B  11           
SHEET    4  BA10 VAL B 303  ALA B 305  1  O  VAL B 303   N  GLY B  70           
SHEET    5  BA10 MET B 291  ILE B 296 -1  O  LEU B 295   N  GLU B 304           
SHEET    6  BA10 THR B 106  ALA B 111 -1  O  THR B 106   N  ILE B 296           
SHEET    7  BA10 ILE B 128  HIS B 133 -1  O  ILE B 128   N  ALA B 111           
SHEET    8  BA10 PHE B 265  CYS B 269  1  O  PHE B 265   N  ILE B 129           
SHEET    9  BA10 LEU B 207  THR B 211  1  O  TYR B 208   N  ALA B 268           
SHEET   10  BA10 TYR B 246  LEU B 250  1  O  GLU B 247   N  LEU B 209           
LINK        CD    CD A1414                 OD2 ASP A 279     1555   1555  3.11  
LINK        CD    CD A1414                 OA1 FLC A1416     1555   1555  2.22  
LINK        CD    CD A1414                 O   HOH A2022     1555   1555  2.30  
LINK        CD    CD A1414                 O   HOH A2051     1555   1555  2.29  
LINK        CD    CD A1414                 OD2 ASP A 275     1555   1555  1.97  
LINK        CD    CD A1414                 OD2 ASP B 252     1555   1555  2.08  
LINK        CD    CD B1414                 OD2 ASP B 275     1555   1555  2.46  
LINK        CD    CD B1414                 OA2 FLC B1416     1555   1555  1.94  
LINK        CD    CD B1414                 OD1 ASP A 252     1555   1555  2.57  
SITE     1 AC1  6 ASP A 275  ASP A 279  FLC A1416  HOH A2022                    
SITE     2 AC1  6 HOH A2051  ASP B 252                                          
SITE     1 AC2 14 THR A  77  SER A  94  ASN A  96  ARG A 100                    
SITE     2 AC2 14 ARG A 109  ARG A 132  TYR A 139  ASP A 275                    
SITE     3 AC2 14  CD A1414  NAP A1415  HOH A2022  LYS B 212                    
SITE     4 AC2 14 ILE B 215  ASP B 252                                          
SITE     1 AC3  4 ASP A 252  ASP B 275  ASP B 279  FLC B1416                    
SITE     1 AC4 15 LYS A 212  ILE A 215  ASP A 252  THR B  77                    
SITE     2 AC4 15 SER B  94  ASN B  96  ARG B 100  ARG B 109                    
SITE     3 AC4 15 ARG B 132  TYR B 139  ASP B 275  ALA B 308                    
SITE     4 AC4 15  CD B1414  NAP B1415  HOH B2048                               
SITE     1 AC5 24 LYS A  72  ALA A  74  THR A  75  THR A  77                    
SITE     2 AC5 24 ARG A  82  ASN A  96  HIS A 309  GLY A 310                    
SITE     3 AC5 24 THR A 311  VAL A 312  THR A 313  ARG A 314                    
SITE     4 AC5 24 HIS A 315  ASN A 328  FLC A1416  HOH A2064                    
SITE     5 AC5 24 HOH A2065  HOH A2066  HOH A2067  HOH A2068                    
SITE     6 AC5 24 ASP B 253  GLN B 257  LYS B 260  HOH B2032                    
SITE     1 AC6 17 LYS A 260  LYS B  72  ALA B  74  THR B  75                    
SITE     2 AC6 17 THR B  77  ASN B  96  LEU B 288  GLU B 306                    
SITE     3 AC6 17 HIS B 309  GLY B 310  THR B 311  VAL B 312                    
SITE     4 AC6 17 THR B 313  ARG B 314  ASN B 328  FLC B1416                    
SITE     5 AC6 17 HOH B2047                                                     
CRYST1   98.246   91.428  109.724  90.00 113.65  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      0.010179  0.000000  0.004457        0.00000                         
SCALE2      0.000000  0.010938  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009949        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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