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Database: PDB
Entry: 2D1C
LinkDB: 2D1C
Original site: 2D1C 
HEADER    OXIDOREDUCTASE                          15-AUG-05   2D1C              
TITLE     CRYSTAL STRUCTURE OF TT0538 PROTEIN FROM THERMUS THERMOPHILUS HB8     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ISOCITRATE DEHYDROGENASE;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: OXALOSUCCINATE DECARBOXYLASE, IDH, NADP+, -SPECIFIC ICDH,   
COMPND   5 IDP;                                                                 
COMPND   6 EC: 1.1.1.42;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE   3 ORGANISM_TAXID: 300852;                                              
SOURCE   4 STRAIN: HB8;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET11A                                    
KEYWDS    DEHYDROGENASE, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON       
KEYWDS   2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL         
KEYWDS   3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, OXIDOREDUCTASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.K.LOKANATH,N.KUNISHIMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS         
AUTHOR   2 INITIATIVE (RSGI)                                                    
REVDAT   3   13-JUL-11 2D1C    1       VERSN                                    
REVDAT   2   24-FEB-09 2D1C    1       VERSN                                    
REVDAT   1   10-OCT-06 2D1C    0                                                
JRNL        AUTH   N.K.LOKANATH,N.KUNISHIMA                                     
JRNL        TITL   CRYSTAL STRUCTURE OF TT0538 PROTEIN FROM THERMUS             
JRNL        TITL 2 THERMOPHILUS HB8                                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.49                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1792149.520                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 92029                          
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) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4617                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 14562                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740                       
REMARK   3   BIN FREE R VALUE                    : 0.3200                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 753                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7652                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 122                                     
REMARK   3   SOLVENT ATOMS            : 870                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.84000                                              
REMARK   3    B22 (A**2) : -1.70000                                             
REMARK   3    B33 (A**2) : -0.15000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.13000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.22                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.21                            
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) : 0.26                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.28                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.86                            
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) : 1.170 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.730 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.780 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.550 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.32                                                 
REMARK   3   BSOL        : 45.33                                                
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  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : LIG.PAR                                        
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : LIG.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2D1C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-AUG-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB024865.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-05; 10-JUL-05               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0; NULL                        
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : SPRING-8; SPRING-8                 
REMARK 200  BEAMLINE                       : BL26B1; BL26B1                     
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0; 0.978954, 0.979321, 1.0       
REMARK 200  MONOCHROMATOR                  : GRAPHITE; GRAPHITE                 
REMARK 200  OPTICS                         : GRAPHITE; GRAPHITE                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE; IMAGE PLATE           
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS V; RIGAKU RAXIS V     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 92029                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NH2SO4, PEG 4000, PH 5.6, MICROBATCH,    
REMARK 280  TEMPERATURE 295.0K                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       47.59200            
REMARK 290   SMTRY3   2  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: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14880 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 31940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     MET B     1                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLN B  363   CB   CG   CD   OE1  NE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TRP B 474   NE1   TRP B 474   CE2     0.111                       
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    ASP A 132       88.01   -152.93                                   
REMARK 500    GLU A 141     -148.59   -135.29                                   
REMARK 500    ASP A 142     -155.75     73.07                                   
REMARK 500    TYR A 144        0.57    -59.35                                   
REMARK 500    MET A 195       75.74   -106.26                                   
REMARK 500    GLU A 238      -66.08   -122.63                                   
REMARK 500    GLU A 310       58.05   -100.83                                   
REMARK 500    LYS A 361      -93.40    -95.91                                   
REMARK 500    ARG A 365       57.09   -109.66                                   
REMARK 500    PRO A 417       33.60    -82.35                                   
REMARK 500    ASP A 442       33.49    -83.33                                   
REMARK 500    ARG A 471      -30.92   -132.63                                   
REMARK 500    MET A 475      -10.17   -142.37                                   
REMARK 500    ASN B 121       19.39     57.79                                   
REMARK 500    VAL B 122       79.78   -112.14                                   
REMARK 500    ASP B 132       86.95   -151.67                                   
REMARK 500    GLU B 141     -149.56   -133.63                                   
REMARK 500    ASP B 142     -154.20     73.06                                   
REMARK 500    TYR B 144        0.03    -60.29                                   
REMARK 500    MET B 195       76.48   -105.52                                   
REMARK 500    GLU B 238      -67.06   -124.24                                   
REMARK 500    ALA B 283       73.46     38.78                                   
REMARK 500    GLU B 310       61.03   -101.22                                   
REMARK 500    THR B 362       73.79    -61.42                                   
REMARK 500    GLN B 363       43.94    -93.76                                   
REMARK 500    PRO B 417       34.33    -84.54                                   
REMARK 500    ASP B 442       33.34    -84.96                                   
REMARK 500    ARG B 471      -31.51   -131.71                                   
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 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1904        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH A1981        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH B2011        DISTANCE =  5.04 ANGSTROMS                       
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 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 1585                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 1586                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: TTK003000538.1   RELATED DB: TARGETDB                    
DBREF  2D1C A    1   496  UNP    P33197   IDH_THET8        1    496             
DBREF  2D1C B    1   496  UNP    P33197   IDH_THET8        1    496             
SEQRES   1 A  496  MET PRO LEU ILE THR THR GLU THR GLY LYS LYS MET HIS          
SEQRES   2 A  496  VAL LEU GLU ASP GLY ARG LYS LEU ILE THR VAL ILE PRO          
SEQRES   3 A  496  GLY ASP GLY ILE GLY PRO GLU CYS VAL GLU ALA THR LEU          
SEQRES   4 A  496  LYS VAL LEU GLU ALA ALA LYS ALA PRO LEU ALA TYR GLU          
SEQRES   5 A  496  VAL ARG GLU ALA GLY ALA SER VAL PHE ARG ARG GLY ILE          
SEQRES   6 A  496  ALA SER GLY VAL PRO GLN GLU THR ILE GLU SER ILE ARG          
SEQRES   7 A  496  LYS THR ARG VAL VAL LEU LYS GLY PRO LEU GLU THR PRO          
SEQRES   8 A  496  VAL GLY TYR GLY GLU LYS SER ALA ASN VAL THR LEU ARG          
SEQRES   9 A  496  LYS LEU PHE GLU THR TYR ALA ASN VAL ARG PRO VAL ARG          
SEQRES  10 A  496  GLU PHE PRO ASN VAL PRO THR PRO TYR ALA GLY ARG GLY          
SEQRES  11 A  496  ILE ASP LEU VAL VAL VAL ARG GLU ASN VAL GLU ASP LEU          
SEQRES  12 A  496  TYR ALA GLY ILE GLU HIS MET GLN THR PRO SER VAL ALA          
SEQRES  13 A  496  GLN THR LEU LYS LEU ILE SER TRP LYS GLY SER GLU LYS          
SEQRES  14 A  496  ILE VAL ARG PHE ALA PHE GLU LEU ALA ARG ALA GLU GLY          
SEQRES  15 A  496  ARG LYS LYS VAL HIS CYS ALA THR LYS SER ASN ILE MET          
SEQRES  16 A  496  LYS LEU ALA GLU GLY THR LEU LYS ARG ALA PHE GLU GLN          
SEQRES  17 A  496  VAL ALA GLN GLU TYR PRO ASP ILE GLU ALA VAL HIS ILE          
SEQRES  18 A  496  ILE VAL ASP ASN ALA ALA HIS GLN LEU VAL LYS ARG PRO          
SEQRES  19 A  496  GLU GLN PHE GLU VAL ILE VAL THR THR ASN MET ASN GLY          
SEQRES  20 A  496  ASP ILE LEU SER ASP LEU THR SER GLY LEU ILE GLY GLY          
SEQRES  21 A  496  LEU GLY PHE ALA PRO SER ALA ASN ILE GLY ASN GLU VAL          
SEQRES  22 A  496  ALA ILE PHE GLU ALA VAL HIS GLY SER ALA PRO LYS TYR          
SEQRES  23 A  496  ALA GLY LYS ASN VAL ILE ASN PRO THR ALA VAL LEU LEU          
SEQRES  24 A  496  SER ALA VAL MET MET LEU ARG TYR LEU GLU GLU PHE ALA          
SEQRES  25 A  496  THR ALA ASP LEU ILE GLU ASN ALA LEU LEU TYR THR LEU          
SEQRES  26 A  496  GLU GLU GLY ARG VAL LEU THR GLY ASP VAL VAL GLY TYR          
SEQRES  27 A  496  ASP ARG GLY ALA LYS THR THR GLU TYR THR GLU ALA ILE          
SEQRES  28 A  496  ILE GLN ASN LEU GLY LYS THR PRO ARG LYS THR GLN VAL          
SEQRES  29 A  496  ARG GLY TYR LYS PRO PHE ARG LEU PRO GLN VAL ASP GLY          
SEQRES  30 A  496  ALA ILE ALA PRO ILE VAL PRO ARG SER ARG ARG VAL VAL          
SEQRES  31 A  496  GLY VAL ASP VAL PHE VAL GLU THR ASN LEU LEU PRO GLU          
SEQRES  32 A  496  ALA LEU GLY LYS ALA LEU GLU ASP LEU ALA ALA GLY THR          
SEQRES  33 A  496  PRO PHE ARG LEU LYS MET ILE SER ASN ARG GLY THR GLN          
SEQRES  34 A  496  VAL TYR PRO PRO THR GLY GLY LEU THR ASP LEU VAL ASP          
SEQRES  35 A  496  HIS TYR ARG CYS ARG PHE LEU TYR THR GLY GLU GLY GLU          
SEQRES  36 A  496  ALA LYS ASP PRO GLU ILE LEU ASP LEU VAL SER ARG VAL          
SEQRES  37 A  496  ALA SER ARG PHE ARG TRP MET HIS LEU GLU LYS LEU GLN          
SEQRES  38 A  496  GLU PHE ASP GLY GLU PRO GLY PHE THR LYS ALA GLN GLY          
SEQRES  39 A  496  GLU ASP                                                      
SEQRES   1 B  496  MET PRO LEU ILE THR THR GLU THR GLY LYS LYS MET HIS          
SEQRES   2 B  496  VAL LEU GLU ASP GLY ARG LYS LEU ILE THR VAL ILE PRO          
SEQRES   3 B  496  GLY ASP GLY ILE GLY PRO GLU CYS VAL GLU ALA THR LEU          
SEQRES   4 B  496  LYS VAL LEU GLU ALA ALA LYS ALA PRO LEU ALA TYR GLU          
SEQRES   5 B  496  VAL ARG GLU ALA GLY ALA SER VAL PHE ARG ARG GLY ILE          
SEQRES   6 B  496  ALA SER GLY VAL PRO GLN GLU THR ILE GLU SER ILE ARG          
SEQRES   7 B  496  LYS THR ARG VAL VAL LEU LYS GLY PRO LEU GLU THR PRO          
SEQRES   8 B  496  VAL GLY TYR GLY GLU LYS SER ALA ASN VAL THR LEU ARG          
SEQRES   9 B  496  LYS LEU PHE GLU THR TYR ALA ASN VAL ARG PRO VAL ARG          
SEQRES  10 B  496  GLU PHE PRO ASN VAL PRO THR PRO TYR ALA GLY ARG GLY          
SEQRES  11 B  496  ILE ASP LEU VAL VAL VAL ARG GLU ASN VAL GLU ASP LEU          
SEQRES  12 B  496  TYR ALA GLY ILE GLU HIS MET GLN THR PRO SER VAL ALA          
SEQRES  13 B  496  GLN THR LEU LYS LEU ILE SER TRP LYS GLY SER GLU LYS          
SEQRES  14 B  496  ILE VAL ARG PHE ALA PHE GLU LEU ALA ARG ALA GLU GLY          
SEQRES  15 B  496  ARG LYS LYS VAL HIS CYS ALA THR LYS SER ASN ILE MET          
SEQRES  16 B  496  LYS LEU ALA GLU GLY THR LEU LYS ARG ALA PHE GLU GLN          
SEQRES  17 B  496  VAL ALA GLN GLU TYR PRO ASP ILE GLU ALA VAL HIS ILE          
SEQRES  18 B  496  ILE VAL ASP ASN ALA ALA HIS GLN LEU VAL LYS ARG PRO          
SEQRES  19 B  496  GLU GLN PHE GLU VAL ILE VAL THR THR ASN MET ASN GLY          
SEQRES  20 B  496  ASP ILE LEU SER ASP LEU THR SER GLY LEU ILE GLY GLY          
SEQRES  21 B  496  LEU GLY PHE ALA PRO SER ALA ASN ILE GLY ASN GLU VAL          
SEQRES  22 B  496  ALA ILE PHE GLU ALA VAL HIS GLY SER ALA PRO LYS TYR          
SEQRES  23 B  496  ALA GLY LYS ASN VAL ILE ASN PRO THR ALA VAL LEU LEU          
SEQRES  24 B  496  SER ALA VAL MET MET LEU ARG TYR LEU GLU GLU PHE ALA          
SEQRES  25 B  496  THR ALA ASP LEU ILE GLU ASN ALA LEU LEU TYR THR LEU          
SEQRES  26 B  496  GLU GLU GLY ARG VAL LEU THR GLY ASP VAL VAL GLY TYR          
SEQRES  27 B  496  ASP ARG GLY ALA LYS THR THR GLU TYR THR GLU ALA ILE          
SEQRES  28 B  496  ILE GLN ASN LEU GLY LYS THR PRO ARG LYS THR GLN VAL          
SEQRES  29 B  496  ARG GLY TYR LYS PRO PHE ARG LEU PRO GLN VAL ASP GLY          
SEQRES  30 B  496  ALA ILE ALA PRO ILE VAL PRO ARG SER ARG ARG VAL VAL          
SEQRES  31 B  496  GLY VAL ASP VAL PHE VAL GLU THR ASN LEU LEU PRO GLU          
SEQRES  32 B  496  ALA LEU GLY LYS ALA LEU GLU ASP LEU ALA ALA GLY THR          
SEQRES  33 B  496  PRO PHE ARG LEU LYS MET ILE SER ASN ARG GLY THR GLN          
SEQRES  34 B  496  VAL TYR PRO PRO THR GLY GLY LEU THR ASP LEU VAL ASP          
SEQRES  35 B  496  HIS TYR ARG CYS ARG PHE LEU TYR THR GLY GLU GLY GLU          
SEQRES  36 B  496  ALA LYS ASP PRO GLU ILE LEU ASP LEU VAL SER ARG VAL          
SEQRES  37 B  496  ALA SER ARG PHE ARG TRP MET HIS LEU GLU LYS LEU GLN          
SEQRES  38 B  496  GLU PHE ASP GLY GLU PRO GLY PHE THR LYS ALA GLN GLY          
SEQRES  39 B  496  GLU ASP                                                      
HET    NAP  A1002      48                                                       
HET    NAP  B1003      48                                                       
HET    CIT  A1585      13                                                       
HET    CIT  B1586      13                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETNAM     CIT CITRIC ACID                                                      
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
FORMUL   3  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   5  CIT    2(C6 H8 O7)                                                  
FORMUL   7  HOH   *870(H2 O)                                                    
HELIX    1   1 ILE A   30  ALA A   45  1                                  16    
HELIX    2   2 GLY A   57  ARG A   62  1                                   6    
HELIX    3   3 PRO A   70  ARG A   81  1                                  12    
HELIX    4   4 SER A   98  PHE A  107  1                                  10    
HELIX    5   5 ASP A  142  GLY A  146  5                                   5    
HELIX    6   6 TRP A  164  GLU A  181  1                                  18    
HELIX    7   7 LEU A  197  GLN A  211  1                                  15    
HELIX    8   8 VAL A  223  ARG A  233  1                                  11    
HELIX    9   9 PRO A  234  PHE A  237  5                                   4    
HELIX   10  10 THR A  243  GLY A  256  1                                  14    
HELIX   11  11 GLY A  260  PHE A  263  5                                   4    
HELIX   12  12 PRO A  294  LEU A  308  1                                  15    
HELIX   13  13 GLU A  310  GLY A  328  1                                  19    
HELIX   14  14 THR A  332  GLY A  337  1                                   6    
HELIX   15  15 LYS A  343  ASN A  354  1                                  12    
HELIX   16  16 GLN A  374  ALA A  378  5                                   5    
HELIX   17  17 LEU A  401  ALA A  414  1                                  14    
HELIX   18  18 LYS A  457  SER A  470  1                                  14    
HELIX   19  19 ILE B   30  ALA B   45  1                                  16    
HELIX   20  20 GLY B   57  ARG B   62  1                                   6    
HELIX   21  21 PRO B   70  ARG B   81  1                                  12    
HELIX   22  22 SER B   98  PHE B  107  1                                  10    
HELIX   23  23 ASP B  142  GLY B  146  5                                   5    
HELIX   24  24 TRP B  164  GLU B  181  1                                  18    
HELIX   25  25 LEU B  197  GLN B  211  1                                  15    
HELIX   26  26 VAL B  223  ARG B  233  1                                  11    
HELIX   27  27 PRO B  234  PHE B  237  5                                   4    
HELIX   28  28 THR B  243  GLY B  256  1                                  14    
HELIX   29  29 GLY B  260  PHE B  263  5                                   4    
HELIX   30  30 ALA B  283  ALA B  287  5                                   5    
HELIX   31  31 PRO B  294  LEU B  308  1                                  15    
HELIX   32  32 GLU B  310  GLY B  328  1                                  19    
HELIX   33  33 THR B  332  GLY B  337  1                                   6    
HELIX   34  34 LYS B  343  ASN B  354  1                                  12    
HELIX   35  35 GLN B  374  ALA B  378  5                                   5    
HELIX   36  36 LEU B  401  ALA B  414  1                                  14    
HELIX   37  37 LYS B  457  SER B  470  1                                  14    
SHEET    1   A 4 LEU A   3  THR A   5  0                                        
SHEET    2   A 4 LYS A  11  VAL A  14 -1  O  MET A  12   N  ILE A   4           
SHEET    3   A 4 LYS A  20  ILE A  25 -1  O  LEU A  21   N  HIS A  13           
SHEET    4   A 4 LEU A  49  VAL A  53  1  O  GLU A  52   N  VAL A  24           
SHEET    1   B11 LEU A   3  THR A   5  0                                        
SHEET    2   B11 LYS A  11  VAL A  14 -1  O  MET A  12   N  ILE A   4           
SHEET    3   B11 LYS A  20  ILE A  25 -1  O  LEU A  21   N  HIS A  13           
SHEET    4   B11 VAL A  82  LYS A  85  1  O  VAL A  82   N  THR A  23           
SHEET    5   B11 ALA A 274  ALA A 278  1  O  PHE A 276   N  VAL A  83           
SHEET    6   B11 PRO A 265  ILE A 269 -1  N  ASN A 268   O  ILE A 275           
SHEET    7   B11 ALA A 111  ARG A 117 -1  N  ALA A 111   O  ILE A 269           
SHEET    8   B11 ASP A 132  GLU A 138 -1  O  ARG A 137   N  ASN A 112           
SHEET    9   B11 VAL A 239  THR A 242  1  O  ILE A 240   N  VAL A 136           
SHEET   10   B11 LYS A 185  THR A 190  1  N  HIS A 187   O  VAL A 239           
SHEET   11   B11 GLU A 217  ILE A 222  1  O  ILE A 221   N  CYS A 188           
SHEET    1   C 4 GLU A 148  THR A 152  0                                        
SHEET    2   C 4 VAL A 155  SER A 163 -1  O  GLN A 157   N  HIS A 149           
SHEET    3   C 4 VAL B 155  SER B 163 -1  O  ALA B 156   N  ILE A 162           
SHEET    4   C 4 GLU B 148  THR B 152 -1  N  HIS B 149   O  GLN B 157           
SHEET    1   D10 THR A 428  TYR A 431  0                                        
SHEET    2   D10 PHE A 418  ASN A 425 -1  N  ILE A 423   O  VAL A 430           
SHEET    3   D10 HIS A 443  TYR A 450 -1  O  ARG A 447   N  LYS A 421           
SHEET    4   D10 ARG A 387  GLU A 397 -1  N  VAL A 390   O  TYR A 450           
SHEET    5   D10 ARG A 473  PHE A 483 -1  O  GLU A 478   N  ASP A 393           
SHEET    6   D10 ARG B 473  PHE B 483 -1  O  MET B 475   N  LYS A 479           
SHEET    7   D10 ARG B 387  GLU B 397 -1  N  ASP B 393   O  GLU B 478           
SHEET    8   D10 HIS B 443  TYR B 450 -1  O  TYR B 450   N  VAL B 390           
SHEET    9   D10 PHE B 418  ASN B 425 -1  N  LYS B 421   O  ARG B 447           
SHEET   10   D10 THR B 428  TYR B 431 -1  O  VAL B 430   N  ILE B 423           
SHEET    1   E 4 GLU A 486  PRO A 487  0                                        
SHEET    2   E 4 ARG A 473  PHE A 483 -1  N  PHE A 483   O  GLU A 486           
SHEET    3   E 4 ARG B 473  PHE B 483 -1  O  MET B 475   N  LYS A 479           
SHEET    4   E 4 GLU B 486  PRO B 487 -1  O  GLU B 486   N  PHE B 483           
SHEET    1   F 4 LEU B   3  THR B   5  0                                        
SHEET    2   F 4 LYS B  11  VAL B  14 -1  O  MET B  12   N  ILE B   4           
SHEET    3   F 4 LYS B  20  ILE B  25 -1  O  LEU B  21   N  HIS B  13           
SHEET    4   F 4 LEU B  49  VAL B  53  1  O  ALA B  50   N  ILE B  22           
SHEET    1   G11 LEU B   3  THR B   5  0                                        
SHEET    2   G11 LYS B  11  VAL B  14 -1  O  MET B  12   N  ILE B   4           
SHEET    3   G11 LYS B  20  ILE B  25 -1  O  LEU B  21   N  HIS B  13           
SHEET    4   G11 VAL B  82  LYS B  85  1  O  VAL B  82   N  THR B  23           
SHEET    5   G11 ALA B 274  ALA B 278  1  O  PHE B 276   N  VAL B  83           
SHEET    6   G11 PRO B 265  ILE B 269 -1  N  ASN B 268   O  ILE B 275           
SHEET    7   G11 ALA B 111  ARG B 117 -1  N  ALA B 111   O  ILE B 269           
SHEET    8   G11 ASP B 132  GLU B 138 -1  O  LEU B 133   N  VAL B 116           
SHEET    9   G11 VAL B 239  THR B 242  1  O  ILE B 240   N  VAL B 136           
SHEET   10   G11 LYS B 185  THR B 190  1  N  HIS B 187   O  VAL B 239           
SHEET   11   G11 GLU B 217  ILE B 222  1  O  VAL B 219   N  CYS B 188           
CISPEP   1 TYR A  431    PRO A  432          0        -0.14                     
CISPEP   2 TYR B  431    PRO B  432          0        -0.28                     
SITE     1 AC1 33 LYS A  85  PRO A  87  LEU A  88  GLU A  89                    
SITE     2 AC1 33 THR A  90  ASN A 100  LEU A 261  GLU A 277                    
SITE     3 AC1 33 VAL A 279  HIS A 280  GLY A 281  SER A 282                    
SITE     4 AC1 33 ALA A 283  LYS A 285  TYR A 286  ILE A 292                    
SITE     5 AC1 33 ASN A 293  ASP A 334  CIT A1585  HOH A1618                    
SITE     6 AC1 33 HOH A1717  HOH A1800  HOH A1810  HOH A1839                    
SITE     7 AC1 33 HOH A1975  ASN B 193  ILE B 222  ASN B 225                    
SITE     8 AC1 33 HIS B 228  GLN B 229  LYS B 232  HOH B1669                    
SITE     9 AC1 33 HOH B1975                                                     
SITE     1 AC2 32 ASN A 193  ILE A 222  ASN A 225  GLN A 229                    
SITE     2 AC2 32 LYS A 232  HOH A1625  HOH A1759  LYS B  85                    
SITE     3 AC2 32 PRO B  87  LEU B  88  GLU B  89  THR B  90                    
SITE     4 AC2 32 ASN B 100  LEU B 261  GLU B 277  VAL B 279                    
SITE     5 AC2 32 HIS B 280  GLY B 281  SER B 282  ALA B 283                    
SITE     6 AC2 32 LYS B 285  TYR B 286  ILE B 292  ASN B 293                    
SITE     7 AC2 32 ASP B 334  CIT B1586  HOH B1612  HOH B1687                    
SITE     8 AC2 32 HOH B1711  HOH B1745  HOH B1816  HOH B1840                    
SITE     1 AC3 14 THR A  90  SER A  98  ASN A 100  ARG A 104                    
SITE     2 AC3 14 ARG A 114  ARG A 137  TYR A 144  ASP A 248                    
SITE     3 AC3 14 NAP A1002  LYS B 191  ASN B 193  ASP B 224                    
SITE     4 AC3 14 HOH B1693  HOH B1854                                          
SITE     1 AC4 14 LYS A 191  ASN A 193  ASP A 224  THR B  90                    
SITE     2 AC4 14 SER B  98  ASN B 100  ARG B 104  ARG B 114                    
SITE     3 AC4 14 ARG B 137  TYR B 144  ASP B 248  NAP B1003                    
SITE     4 AC4 14 HOH B1688  HOH B1698                                          
CRYST1   73.022   95.184   72.989  90.00  92.07  90.00 P 1 21 1      4          
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      0.013695  0.000000  0.000495        0.00000                         
SCALE2      0.000000  0.010506  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013710        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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