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Database: PDB
Entry: 1T09
LinkDB: 1T09
Original site: 1T09 
HEADER    OXIDOREDUCTASE                          08-APR-04   1T09              
TITLE     CRYSTAL STRUCTURE OF HUMAN CYTOSOLIC NADP(+)-DEPENDENT                
TITLE    2 ISOCITRATE DEHYDROGENASE IN COMPLEX NADP                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ISOCITRATE DEHYDROGENASE [NADP] CYTOPLASMIC;               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CYTOSOLIC NADP(+)-DEPENDENT ISOCITRATE                      
COMPND   5 DEHYDROGENASE, OXALOSUCCINATE DECARBOXYLASE, IDH, NADP+-             
COMPND   6 SPECIFIC ICDH, IDP;                                                  
COMPND   7 EC: 1.1.1.42;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: IDH;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-22B(+)                                
KEYWDS    ROSSMANN FOLD, PROTEIN-COFACTOR COMPLEX, NADP,                        
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.XU,J.ZHAO,B.PENG,Q.HUANG,E.ARNOLD,J.DING                            
REVDAT   3   24-FEB-09 1T09    1       VERSN                                    
REVDAT   2   07-SEP-04 1T09    1       JRNL                                     
REVDAT   1   15-JUN-04 1T09    0                                                
JRNL        AUTH   X.XU,J.ZHAO,Z.XU,B.PENG,Q.HUANG,E.ARNOLD,J.DING              
JRNL        TITL   STRUCTURES OF HUMAN CYTOSOLIC NADP-DEPENDENT                 
JRNL        TITL 2 ISOCITRATE DEHYDROGENASE REVEAL A NOVEL                      
JRNL        TITL 3 SELF-REGULATORY MECHANISM OF ACTIVITY                        
JRNL        REF    J.BIOL.CHEM.                  V. 279 33946 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15173171                                                     
JRNL        DOI    10.1074/JBC.M404298200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2335794.040                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 30393                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1529                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4649                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2731                       
REMARK   3   BIN FREE R VALUE                    : 0.3107                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 236                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6556                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 96                                      
REMARK   3   SOLVENT ATOMS            : 155                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.00000                                              
REMARK   3    B22 (A**2) : 2.62000                                              
REMARK   3    B33 (A**2) : -5.62000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.32                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.32                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.42                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.40                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.77                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.32                                                 
REMARK   3   BSOL        : 20.25                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NDP.PARAM                                      
REMARK   3  PARAMETER FILE  5  : ICT.PARAM                                      
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NDP.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : ICT.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1T09 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-APR-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022150.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-MAR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F2                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30445                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 9.100                              
REMARK 200  R MERGE                    (I) : 0.10300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1LWD                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, MES, PH 6.5, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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      154.01500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       41.35500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       41.35500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      231.02250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       41.35500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       41.35500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       77.00750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       41.35500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       41.35500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      231.02250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       41.35500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       41.35500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       77.00750            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      154.01500            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS AN ASYMMETRIC HOMODIMER.          
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: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 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 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     MET A   1    CG   SD   CE                                        
REMARK 470     MET B   1    CG   SD   CE                                        
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    SER A   2     -104.40    -87.66                                   
REMARK 500    GLU A  17     -129.30     36.40                                   
REMARK 500    ASN A  68      -24.68     67.97                                   
REMARK 500    GLN A  90      146.42    166.13                                   
REMARK 500    SER A 122      -38.82    -37.22                                   
REMARK 500    THR A 142       68.14   -118.52                                   
REMARK 500    VAL A 146       97.69     72.14                                   
REMARK 500    PRO A 149      159.52    -36.94                                   
REMARK 500    GLN A 163      122.87    -39.01                                   
REMARK 500    LEU A 168       96.82     64.72                                   
REMARK 500    HIS A 170      141.96   -176.31                                   
REMARK 500    TYR A 235      -62.12     72.01                                   
REMARK 500    GLU A 247      138.03   -177.16                                   
REMARK 500    ILE A 251      -37.18    -34.31                                   
REMARK 500    VAL A 281      -66.18   -108.04                                   
REMARK 500    ALA A 282      111.42    145.12                                   
REMARK 500    GLN A 283      -70.84    -33.60                                   
REMARK 500    SER B   2     -104.07   -105.42                                   
REMARK 500    GLU B  17     -131.97     36.19                                   
REMARK 500    ASN B  68       -2.21     60.64                                   
REMARK 500    GLN B  90      146.89   -176.05                                   
REMARK 500    ASP B 137     -141.12     45.87                                   
REMARK 500    ARG B 140      148.97   -171.28                                   
REMARK 500    PRO B 158      154.18    -49.93                                   
REMARK 500    ASP B 160       37.00    -82.24                                   
REMARK 500    HIS B 170      149.29   -178.01                                   
REMARK 500    ASN B 213        3.87    -61.13                                   
REMARK 500    LEU B 216       73.64   -109.04                                   
REMARK 500    GLN B 234       -6.47   -141.65                                   
REMARK 500    LYS B 260       42.35    -86.97                                   
REMARK 500    ASP B 273     -160.72     55.31                                   
REMARK 500    ASP B 275     -142.56   -166.55                                   
REMARK 500    GLN B 277     -179.93   -173.93                                   
REMARK 500    ASP B 279      -79.18    -83.31                                   
REMARK 500    ASP B 299       -1.14    -56.20                                   
REMARK 500    HIS B 309     -173.41    -69.81                                   
REMARK 500    ASN B 349       79.80   -109.66                                   
REMARK 500    ALA B 377      -50.04     75.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 415                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 1003                
DBREF  1T09 A    1   414  UNP    O75874   IDHC_HUMAN       1    414             
DBREF  1T09 B    1   414  UNP    O75874   IDHC_HUMAN       1    414             
SEQRES   1 A  414  MET SER LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET          
SEQRES   2 A  414  GLN GLY ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE          
SEQRES   3 A  414  LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU          
SEQRES   4 A  414  HIS SER TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR          
SEQRES   5 A  414  ASN ASP GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS          
SEQRES   6 A  414  LYS HIS ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO          
SEQRES   7 A  414  ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET          
SEQRES   8 A  414  TRP LYS SER PRO ASN GLY THR ILE ARG ASN ILE LEU GLY          
SEQRES   9 A  414  GLY THR VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE          
SEQRES  10 A  414  PRO ARG LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE          
SEQRES  11 A  414  GLY ARG HIS ALA TYR GLY ASP GLN TYR ARG ALA THR ASP          
SEQRES  12 A  414  PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR          
SEQRES  13 A  414  THR PRO SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL          
SEQRES  14 A  414  HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET          
SEQRES  15 A  414  TYR ASN GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER          
SEQRES  16 A  414  SER PHE GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR          
SEQRES  17 A  414  LEU SER THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY          
SEQRES  18 A  414  ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN          
SEQRES  19 A  414  TYR LYS SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU          
SEQRES  20 A  414  HIS ARG LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS          
SEQRES  21 A  414  SER GLU GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP          
SEQRES  22 A  414  GLY ASP VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY          
SEQRES  23 A  414  SER LEU GLY MET MET THR SER VAL LEU VAL CYS PRO ASP          
SEQRES  24 A  414  GLY LYS THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL          
SEQRES  25 A  414  THR ARG HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR          
SEQRES  26 A  414  SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG          
SEQRES  27 A  414  GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU          
SEQRES  28 A  414  LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE          
SEQRES  29 A  414  GLU THR ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA          
SEQRES  30 A  414  ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP          
SEQRES  31 A  414  TYR LEU ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU          
SEQRES  32 A  414  ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS LEU                  
SEQRES   1 B  414  MET SER LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET          
SEQRES   2 B  414  GLN GLY ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE          
SEQRES   3 B  414  LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU          
SEQRES   4 B  414  HIS SER TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR          
SEQRES   5 B  414  ASN ASP GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS          
SEQRES   6 B  414  LYS HIS ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO          
SEQRES   7 B  414  ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET          
SEQRES   8 B  414  TRP LYS SER PRO ASN GLY THR ILE ARG ASN ILE LEU GLY          
SEQRES   9 B  414  GLY THR VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE          
SEQRES  10 B  414  PRO ARG LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE          
SEQRES  11 B  414  GLY ARG HIS ALA TYR GLY ASP GLN TYR ARG ALA THR ASP          
SEQRES  12 B  414  PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR          
SEQRES  13 B  414  THR PRO SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL          
SEQRES  14 B  414  HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET          
SEQRES  15 B  414  TYR ASN GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER          
SEQRES  16 B  414  SER PHE GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR          
SEQRES  17 B  414  LEU SER THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY          
SEQRES  18 B  414  ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN          
SEQRES  19 B  414  TYR LYS SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU          
SEQRES  20 B  414  HIS ARG LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS          
SEQRES  21 B  414  SER GLU GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP          
SEQRES  22 B  414  GLY ASP VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY          
SEQRES  23 B  414  SER LEU GLY MET MET THR SER VAL LEU VAL CYS PRO ASP          
SEQRES  24 B  414  GLY LYS THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL          
SEQRES  25 B  414  THR ARG HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR          
SEQRES  26 B  414  SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG          
SEQRES  27 B  414  GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU          
SEQRES  28 B  414  LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE          
SEQRES  29 B  414  GLU THR ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA          
SEQRES  30 B  414  ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP          
SEQRES  31 B  414  TYR LEU ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU          
SEQRES  32 B  414  ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS LEU                  
HET    NAP  A 415      48                                                       
HET    NAP  B1003      48                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
FORMUL   3  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   5  HOH   *155(H2 O)                                                    
HELIX    1   1 ASP A   16  LEU A   30  1                                  15    
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  PHE A   86  1                                   8    
HELIX    5   5 SER A   94  GLY A  104  1                                  11    
HELIX    6   6 ASP A  186  GLY A  204  1                                  19    
HELIX    7   7 LYS A  218  GLN A  234  1                                  17    
HELIX    8   8 TYR A  235  GLN A  242  1                                   8    
HELIX    9   9 ILE A  251  LYS A  260  1                                  10    
HELIX   10  10 SER A  287  GLY A  289  5                                   3    
HELIX   11  11 VAL A  312  LYS A  321  1                                  10    
HELIX   12  12 PRO A  329  ASN A  348  1                                  20    
HELIX   13  13 ASN A  349  ALA A  369  1                                  21    
HELIX   14  14 THR A  373  GLY A  382  1                                  10    
HELIX   15  15 LEU A  383  VAL A  386  5                                   4    
HELIX   16  16 GLN A  387  TYR A  391  5                                   5    
HELIX   17  17 ASN A  393  LYS A  413  1                                  21    
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  PHE B   86  1                                   8    
HELIX   22  22 SER B   94  GLY B  104  1                                  11    
HELIX   23  23 ASP B  186  LYS B  203  1                                  18    
HELIX   24  24 LYS B  218  TYR B  235  1                                  18    
HELIX   25  25 TYR B  235  GLN B  242  1                                   8    
HELIX   26  26 LEU B  250  LYS B  260  1                                  11    
HELIX   27  27 ASP B  279  GLY B  284  1                                   6    
HELIX   28  28 SER B  287  GLY B  289  5                                   3    
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 LYS B  374  GLY B  382  1                                   9    
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  LEU B  414  1                                  22    
SHEET    1   A10 VAL A  35  ASP A  43  0                                        
SHEET    2   A10 ILE A   5  GLN A  14  1  N  GLY A   8   O  ASP A  38           
SHEET    3   A10 VAL A  69  LYS A  72  1  O  VAL A  71   N  VAL A  11           
SHEET    4   A10 VAL A 303  ALA A 307  1  O  ALA A 305   N  LYS A  72           
SHEET    5   A10 MET A 291  VAL A 296 -1  N  LEU A 295   O  GLU A 304           
SHEET    6   A10 THR A 106  ALA A 111 -1  N  GLU A 110   O  THR A 292           
SHEET    7   A10 LYS A 126  ARG A 132 -1  O  ILE A 130   N  ARG A 109           
SHEET    8   A10 GLY A 263  CYS A 269  1  O  TRP A 267   N  ILE A 129           
SHEET    9   A10 LEU A 207  THR A 211  1  N  TYR A 208   O  ALA A 268           
SHEET   10   A10 HIS A 248  LEU A 250  1  O  ARG A 249   N  LEU A 209           
SHEET    1   B 2 ALA A 134  TYR A 135  0                                        
SHEET    2   B 2 ASP A 275  VAL A 276  1  O  ASP A 275   N  TYR A 135           
SHEET    1   C 4 THR A 142  PHE A 144  0                                        
SHEET    2   C 4 GLY A 177  GLN A 185 -1  O  ALA A 179   N  PHE A 144           
SHEET    3   C 4 GLY B 177  GLN B 185 -1  O  VAL B 178   N  ASN A 184           
SHEET    4   C 4 THR B 142  VAL B 146 -1  N  THR B 142   O  GLY B 181           
SHEET    1   D 3 VAL A 165  THR A 166  0                                        
SHEET    2   D 3 GLY A 150  PRO A 158 -1  N  TYR A 156   O  VAL A 165           
SHEET    3   D 3 HIS A 170  PHE A 172 -1  O  HIS A 170   N  VAL A 152           
SHEET    1   E 4 VAL A 165  THR A 166  0                                        
SHEET    2   E 4 GLY A 150  PRO A 158 -1  N  TYR A 156   O  VAL A 165           
SHEET    3   E 4 GLY B 150  PRO B 158 -1  O  THR B 157   N  LYS A 151           
SHEET    4   E 4 VAL B 165  PHE B 172 -1  O  VAL B 165   N  TYR B 156           
SHEET    1   F10 VAL B  35  ASP B  43  0                                        
SHEET    2   F10 ILE B   5  GLN B  14  1  N  GLY B   8   O  ASP B  38           
SHEET    3   F10 VAL B  69  LYS B  72  1  O  VAL B  71   N  VAL B  11           
SHEET    4   F10 VAL B 303  ALA B 307  1  O  ALA B 305   N  GLY B  70           
SHEET    5   F10 MET B 291  VAL B 296 -1  N  LEU B 295   O  GLU B 304           
SHEET    6   F10 THR B 106  ALA B 111 -1  N  GLU B 110   O  THR B 292           
SHEET    7   F10 LYS B 126  ARG B 132 -1  O  ILE B 130   N  ARG B 109           
SHEET    8   F10 GLY B 263  CYS B 269  1  O  CYS B 269   N  GLY B 131           
SHEET    9   F10 LEU B 207  SER B 210  1  N  TYR B 208   O  ILE B 266           
SHEET   10   F10 TYR B 246  HIS B 248  1  O  GLU B 247   N  LEU B 207           
SITE     1 AC1 19 LYS A  72  ALA A  74  THR A  75  ILE A  76                    
SITE     2 AC1 19 THR A  77  ARG A  82  ASN A  96  ASP A 279                    
SITE     3 AC1 19 SER A 280  LEU A 288  HIS A 309  GLY A 310                    
SITE     4 AC1 19 THR A 311  VAL A 312  ARG A 314  HIS A 315                    
SITE     5 AC1 19 THR A 327  ASN A 328  HOH A 501                               
SITE     1 AC2 17 LYS B  72  ALA B  74  THR B  75  ILE B  76                    
SITE     2 AC2 17 THR B  77  ARG B  82  ASN B  96  LEU B 288                    
SITE     3 AC2 17 HIS B 309  GLY B 310  THR B 311  VAL B 312                    
SITE     4 AC2 17 ARG B 314  HIS B 315  ASN B 328  HOH B1024                    
SITE     5 AC2 17 HOH B1025                                                     
CRYST1   82.710   82.710  308.030  90.00  90.00  90.00 P 43 21 2    16          
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      0.012090  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012090  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003246        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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