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Database: PDB
Entry: 2CMJ
LinkDB: 2CMJ
Original site: 2CMJ 
HEADER    OXIDOREDUCTASE                          10-MAY-06   2CMJ              
TITLE     CRYSTAL STRUCTURE OF MOUSE CYTOSOLIC ISOCITRATE                       
TITLE    2 DEHYDROGENASE                                                        
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,                          
COMPND   6  NADP(+)-SPECIFIC ICDH, IDP;                                         
COMPND   7 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: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: DE3                                       
KEYWDS    OXIDOREDUCTASE, TRICARBOXYLIC ACID CYCLE, ISOCITRATE                  
KEYWDS   2 DEHYDROGENASE, NADP, GLYOXYLATE BYPASS                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.J.CHO,K.J.KIM,T.L.HUH,B.S.KANG                                      
REVDAT   2   24-FEB-09 2CMJ    1       VERSN                                    
REVDAT   1   29-MAY-07 2CMJ    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                                                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.99 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) : 1.99                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.81                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 54264                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2883                            
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) : 1.99                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.04                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3420                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3310                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 187                          
REMARK   3   BIN FREE R VALUE                    : 0.3850                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6493                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 96                                      
REMARK   3   SOLVENT ATOMS            : 599                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.12000                                             
REMARK   3    B22 (A**2) : 0.20000                                              
REMARK   3    B33 (A**2) : -0.14000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.07000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.211         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.184         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6729 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9094 ; 1.260 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   821 ; 6.199 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   308 ;35.807 ;24.935       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1211 ;14.764 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;21.729 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   982 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5020 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3474 ; 0.195 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4613 ; 0.300 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   669 ; 0.153 ; 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):    35 ; 0.227 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    16 ; 0.206 ; 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):  4058 ; 0.579 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6532 ; 1.041 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2671 ; 1.572 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2560 ; 2.448 ; 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  : NULL                                       
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 2CMJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-MAY-06.                  
REMARK 100 THE PDBE ID CODE IS EBI-28545.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-NOV-04                          
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                       : 6B                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1271                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRUKER                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57456                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 6.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 44.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.200                              
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 1T0L                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       48.68600            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.64450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       48.68600            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       45.64450            
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 GENERATING THE BIOMOLECULE                                           
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375      HOH A2159  LIES ON A SPECIAL POSITION.                          
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 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 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     -128.27     51.80                                   
REMARK 500    ILE A  31      -65.69   -106.69                                   
REMARK 500    ASN A  68       -2.40     71.89                                   
REMARK 500    ASP A  79     -166.49   -111.40                                   
REMARK 500    ASP A 137     -135.49     56.47                                   
REMARK 500    ARG A 140       43.87   -142.41                                   
REMARK 500    THR A 162     -177.53    -67.68                                   
REMARK 500    LYS A 212       51.58   -118.66                                   
REMARK 500    LYS A 301      -32.72   -134.40                                   
REMARK 500    ILE B   5      112.54     52.36                                   
REMARK 500    GLU B  17     -129.69     49.58                                   
REMARK 500    ILE B  31      -66.50   -109.05                                   
REMARK 500    ASN B  68       -8.96     75.53                                   
REMARK 500    ASP B  79     -164.98   -115.58                                   
REMARK 500    ASP B 137     -139.09     53.86                                   
REMARK 500    LYS B 212       52.19   -117.17                                   
REMARK 500    MET B 290       66.68   -117.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A1414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B1413                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2CMV   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE CYTOSOLIC                                
REMARK 900  ISOCITRATE DEHYDROGENASE COMPLEXED WITH CADMIUM                     
REMARK 900   AND CITRATE                                                        
DBREF  2CMJ A    4   413  UNP    O88844   IDHC_MOUSE       4    413             
DBREF  2CMJ 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    NAP  A1414      48                                                       
HET    NAP  B1413      48                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE                           
HETNAM   2 NAP  PHOSPHATE                                                       
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
FORMUL   3  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   5  HOH   *599(H2 O1)                                                   
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  GLN A  242  1                                   8    
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  ASN A  348  1                                  20    
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 LEU A  383  VAL A  386  5                                   4    
HELIX   17  17 GLN A  387  TYR A  391  5                                   5    
HELIX   18  18 ASN A  393  LYS A  413  1                                  21    
HELIX   19  19 ASP B   16  ILE B   31  1                                  16    
HELIX   20  20 GLY B   45  THR B   52  1                                   8    
HELIX   21  21 ASP B   54  ASN B   68  1                                  15    
HELIX   22  22 ASP B   79  LYS B   87  1                                   9    
HELIX   23  23 SER B   94  GLY B  104  1                                  11    
HELIX   24  24 GLY B  136  ALA B  141  5                                   6    
HELIX   25  25 ASP B  186  GLY B  204  1                                  19    
HELIX   26  26 LYS B  218  TYR B  235  1                                  18    
HELIX   27  27 TYR B  235  GLN B  242  1                                   8    
HELIX   28  28 ILE B  251  SER B  261  1                                  11    
HELIX   29  29 LYS B  270  GLY B  286  1                                  17    
HELIX   30  30 VAL B  312  LYS B  321  1                                  10    
HELIX   31  31 PRO B  329  ASN B  348  1                                  20    
HELIX   32  32 ASN B  349  ALA B  369  1                                  21    
HELIX   33  33 THR B  373  GLY B  382  1                                  10    
HELIX   34  34 LEU B  383  VAL B  386  5                                   4    
HELIX   35  35 GLN B  387  TYR B  391  5                                   5    
HELIX   36  36 ASN B  393  ALA B  412  1                                  20    
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 GLU B  36  ASP B  43  0                                        
SHEET    2  BA10 GLN B   6  GLN B  14  1  N  GLY B   7   O  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  GLU B 306  1  O  VAL B 303   N  GLY B  70           
SHEET    5  BA10 MET B 291  ILE B 296 -1  O  SER B 293   N  GLU B 306           
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 130   N  ARG B 109           
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           
SITE     1 AC1 32 LYS A  72  ALA A  74  THR A  75  THR A  77                    
SITE     2 AC1 32 ARG A  82  ASN A  96  HIS A 309  GLY A 310                    
SITE     3 AC1 32 THR A 311  VAL A 312  THR A 313  ARG A 314                    
SITE     4 AC1 32 HIS A 315  ASN A 328  HOH A2064  HOH A2253                    
SITE     5 AC1 32 HOH A2330  HOH A2331  HOH A2332  HOH A2333                    
SITE     6 AC1 32 HOH A2334  HOH A2335  HOH A2336  HOH A2337                    
SITE     7 AC1 32 HOH A2338  HOH A2339  LEU B 250  ASP B 253                    
SITE     8 AC1 32 GLN B 257  LYS B 260  HOH B2167  HOH B2170                    
SITE     1 AC2 35 ASP A 253  GLN A 257  LYS A 260  HOH A2216                    
SITE     2 AC2 35 HOH A2218  LYS B  72  ALA B  74  THR B  75                    
SITE     3 AC2 35 ILE B  76  THR B  77  ARG B  82  ASN B  96                    
SITE     4 AC2 35 ALA B 307  ALA B 308  HIS B 309  GLY B 310                    
SITE     5 AC2 35 THR B 311  VAL B 312  THR B 313  ARG B 314                    
SITE     6 AC2 35 HIS B 315  THR B 327  ASN B 328  HOH B2027                    
SITE     7 AC2 35 HOH B2180  HOH B2194  HOH B2197  HOH B2252                    
SITE     8 AC2 35 HOH B2253  HOH B2254  HOH B2255  HOH B2257                    
SITE     9 AC2 35 HOH B2258  HOH B2259  HOH B2260                               
CRYST1   97.372   91.289  109.381  90.00 113.34  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      0.010270  0.000000  0.004431        0.00000                         
SCALE2      0.000000  0.010954  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009957        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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