GenomeNet

Database: PDB
Entry: 4AOU
LinkDB: 4AOU
Original site: 4AOU 
HEADER    OXIDOREDUCTASE                          30-MAR-12   4AOU              
TITLE     CTIDH BOUND TO NADP. THE COMPLEX STRUCTURES OF ISOCITRATE             
TITLE    2 DEHYDROGENASE FROM CLOSTRIDIUM THERMOCELLUM AND DESULFOTALEA         
TITLE    3 PSYCHROPHILA, SUPPORT A NEW ACTIVE SITE LOCKING MECHANISM            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ISOCITRATE DEHYDROGENASE [NADP];                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.1.1.42;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;                       
SOURCE   3 ORGANISM_TAXID: 1515;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    OXIDOREDUCTASE, TEMPERATURE ADAPTATION, THERMOPHILIC, PSYCHROPHILIC,  
KEYWDS   2 NADP+ SELECTIVITY, DOMAIN MOVEMENTS                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.-K.S.LEIROS,A.-E.FEDOY,I.LEIROS,I.H.STEEN                           
REVDAT   3   22-MAY-13 4AOU    1       JRNL                                     
REVDAT   2   20-MAR-13 4AOU    1       JRNL                                     
REVDAT   1   11-JUL-12 4AOU    0                                                
JRNL        AUTH   H.-K.S.LEIROS,A.-E.FEDOY,I.LEIROS,I.H.STEEN                  
JRNL        TITL   THE COMPLEX STRUCTURES OF ISOCITRATE DEHYDROGENASE FROM      
JRNL        TITL 2 CLOSTRIDIUM THERMOCELLUM AND DESULFOTALEA PSYCHROPHILA       
JRNL        TITL 3 SUGGEST A NEW ACTIVE SITE LOCKING MECHANISM                  
JRNL        REF    FEBS OPEN BIO.                V.   2   159 2012              
JRNL        REFN                   ISSN 2211-5463                               
JRNL        PMID   23650595                                                     
JRNL        DOI    10.1016/J.FOB.2012.06.003                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0069                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.89                          
REMARK   3   NUMBER OF REFLECTIONS             : 19347                          
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) : 0.19197                         
REMARK   3   R VALUE            (WORKING SET) : 0.18931                         
REMARK   3   FREE R VALUE                     : 0.24403                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1043                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.500                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.565                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1385                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.86                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.278                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 89                           
REMARK   3   BIN FREE R VALUE                    : 0.329                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3210                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 62                                      
REMARK   3   SOLVENT ATOMS            : 41                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 56.17                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.485                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.71                                                 
REMARK   3    B22 (A**2) : 0.71                                                 
REMARK   3    B33 (A**2) : -1.07                                                
REMARK   3    B12 (A**2) : 0.36                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.349         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.256         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.173         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.724         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3299 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4465 ; 1.883 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   400 ; 7.143 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   148 ;36.071 ;24.392       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   579 ;19.670 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;20.890 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   491 ; 0.118 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2453 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  1991 ; 0.788 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3216 ; 1.509 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1308 ; 2.406 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1249 ; 3.757 ; 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 4AOU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-MAR-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-51916.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.2                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91840                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20411                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.50                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5                                  
REMARK 200  R MERGE                    (I) : 0.13                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 0.00                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5                                  
REMARK 200  R MERGE FOR SHELL          (I) : 0.61                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.80                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP METHOD. RESERVOIR           
REMARK 280  SOLUTIONS OF 9-11% (W/V) POLYETHYLENE GLYCOL (PEG) PEG3350,         
REMARK 280   AND 0.15 M AMMONIUM DIHYDROGEN CITRATE, 10% (V/V/)                 
REMARK 280  PROPYLENE GLYCOL AT 37 DEG. C.  CTIDH-NADP AT 5 MG/ML, 10           
REMARK 280  MM NADP AND 10 MM DL-ISOCITRATE.                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.39333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       20.19667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       20.19667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       40.39333            
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: 11620 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 29000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.4 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -40.39333            
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 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     GLU A   36   CG   CD   OE1  OE2                                  
REMARK 480     GLU A   84   CD   OE1  OE2                                       
REMARK 480     ASN A  115   OD1                                                 
REMARK 480     LYS A  125   CE   NZ                                             
REMARK 480     LYS A  126   CD   CE   NZ                                        
REMARK 480     GLU A  162   CD   OE1  OE2                                       
REMARK 480     LYS A  185   CE   NZ                                             
REMARK 480     GLN A  243   NE2                                                 
REMARK 480     LYS A  339   CE   NZ                                             
REMARK 480     LYS A  347   CG   CD   CE   NZ                                   
REMARK 480     LYS A  371   CD   CE                                             
REMARK 480     LYS A  392   CD   CE                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A   116     OE1  GLU A   365              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    GLU A  84   CG    GLU A  84   CD     -0.090                       
REMARK 500    GLU A 162   CG    GLU A 162   CD     -0.379                       
REMARK 500    LYS A 185   CD    LYS A 185   CE     -0.205                       
REMARK 500    GLN A 243   CD    GLN A 243   NE2     0.218                       
REMARK 500    LYS A 371   CE    LYS A 371   NZ     -0.652                       
REMARK 500    LYS A 392   CE    LYS A 392   NZ     -0.499                       
REMARK 500    LYS A 392   CG    LYS A 392   CD     -0.435                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  33   C   -  N   -  CA  ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    GLN A 243   OE1 -  CD  -  NE2 ANGL. DEV. = -23.5 DEGREES          
REMARK 500    VAL A 253   CB  -  CA  -  C   ANGL. DEV. = -12.0 DEGREES          
REMARK 500    LYS A 347   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    LYS A 371   CB  -  CG  -  CD  ANGL. DEV. =  46.9 DEGREES          
REMARK 500    LYS A 392   CB  -  CG  -  CD  ANGL. DEV. =  30.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A   7      -95.95    -94.82                                   
REMARK 500    GLU A  17     -128.79     47.77                                   
REMARK 500    LEU A  31      -71.19   -112.92                                   
REMARK 500    ASP A  54       -0.60     66.16                                   
REMARK 500    ASP A 104      166.00     56.87                                   
REMARK 500    ASP A 137     -138.62     53.60                                   
REMARK 500    SER A 148     -167.01   -164.66                                   
REMARK 500    ALA A 149      150.61    -46.23                                   
REMARK 500    ASN A 160     -118.47    -72.79                                   
REMARK 500    ASP A 200      -36.93    -39.05                                   
REMARK 500    LYS A 210       67.94   -118.75                                   
REMARK 500    TYR A 217      -74.06    -46.57                                   
REMARK 500    GLU A 232      -18.96   -163.61                                   
REMARK 500    MET A 288       57.78    -96.20                                   
REMARK 500    LYS A 318        3.14    -67.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    GLN A 243         0.17    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR A 354        24.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C SSEQI                                                      
REMARK 615     NAP A 1520                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1404  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 250   OD2                                                    
REMARK 620 2 ASP A 273   OD1  87.4                                              
REMARK 620 3 ICT A1403   O1  164.0  82.7                                        
REMARK 620 4 ICT A1403   O7   84.1  89.3  83.3                                  
REMARK 620 5 HOH A2029   O   100.6  81.2  90.3 169.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A1520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ICT A1403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1404                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4AOV   RELATED DB: PDB                                   
REMARK 900  DPIDH-NADP. THE COMPLEX STRUCTURES OF ISOCITRATE                    
REMARK 900  DEHYDROGENASE FROM CLOSTRIDIUM THERMOCELLUM AND DESULFOTALEA        
REMARK 900   PSYCHROPHILA, SUPPORT A NEW ACTIVE SITE LOCKING                    
REMARK 900  MECHANISM                                                           
DBREF  4AOU A    1   402  UNP    A3DC45   A3DC45_CLOTH     1    402             
SEQRES   1 A  402  MET SER LYS ILE LYS MET LYS VAL PRO LEU VAL GLU MET          
SEQRES   2 A  402  ASP GLY ASP GLU MET THR ARG ILE ILE TRP ARG LEU ILE          
SEQRES   3 A  402  LYS GLU ASN LEU LEU GLU PRO TYR ILE GLU LEU ASN THR          
SEQRES   4 A  402  GLU TYR TYR ASP LEU GLY LEU GLU ASN ARG ASP LYS THR          
SEQRES   5 A  402  GLU ASP GLN VAL THR ILE ASP ALA ALA ARG ALA ILE GLN          
SEQRES   6 A  402  LYS TYR GLY VAL GLY VAL LYS CYS ALA THR ILE THR PRO          
SEQRES   7 A  402  ASN ALA GLN ARG VAL GLU GLU TYR ASN LEU LYS LYS MET          
SEQRES   8 A  402  TRP LYS SER PRO ASN GLY THR ILE ARG ALA ILE LEU ASP          
SEQRES   9 A  402  GLY THR VAL PHE ARG ALA PRO ILE VAL VAL ASN SER ILE          
SEQRES  10 A  402  LYS PRO PHE VAL LYS GLY TRP LYS LYS PRO ILE SER ILE          
SEQRES  11 A  402  ALA ARG HIS ALA TYR GLY ASP VAL TYR LYS ASN VAL GLU          
SEQRES  12 A  402  TYR TYR VAL PRO SER ALA GLY LYS ALA GLU LEU VAL PHE          
SEQRES  13 A  402  THR SER GLU ASN GLY GLU VAL SER ARG GLN THR ILE HIS          
SEQRES  14 A  402  GLU PHE ASP GLY PRO GLY VAL ILE MET GLY MET HIS ASN          
SEQRES  15 A  402  THR ASP LYS SER ILE ARG SER PHE ALA ARG ALA CYS PHE          
SEQRES  16 A  402  ASN TYR ALA LEU ASP MET ASN GLN ASP LEU TRP PHE SER          
SEQRES  17 A  402  THR LYS ASP THR ILE SER LYS THR TYR ASP HIS ARG PHE          
SEQRES  18 A  402  LYS ASP ILE PHE GLN GLU ILE TYR GLU ASN GLU TYR LYS          
SEQRES  19 A  402  GLU LYS PHE GLU ALA LYS ASN LEU GLN TYR PHE TYR THR          
SEQRES  20 A  402  LEU ILE ASP ASP ALA VAL ALA ARG ILE ILE ARG SER GLU          
SEQRES  21 A  402  GLY GLY MET VAL TRP ALA CYS LYS ASN TYR ASP GLY ASP          
SEQRES  22 A  402  VAL MET SER ASP MET VAL ALA SER ALA PHE GLY SER LEU          
SEQRES  23 A  402  ALA MET MET THR SER VAL LEU VAL SER PRO ASP GLY LYS          
SEQRES  24 A  402  TYR GLU PHE GLU ALA ALA HIS GLY THR VAL THR ARG HIS          
SEQRES  25 A  402  TYR TYR LYS HIS LEU LYS GLY GLU GLU THR SER THR ASN          
SEQRES  26 A  402  SER MET ALA THR ILE PHE ALA TRP THR GLY ALA LEU LYS          
SEQRES  27 A  402  LYS ARG GLY GLU LEU ASP GLY ILE LYS GLU LEU VAL ASP          
SEQRES  28 A  402  PHE ALA THR LYS LEU GLU GLN ALA SER VAL GLN THR ILE          
SEQRES  29 A  402  GLU ASN GLY VAL MET THR LYS ASP LEU ALA SER LEU SER          
SEQRES  30 A  402  GLU VAL PRO GLU LYS LYS ILE VAL ASN THR GLU ASP PHE          
SEQRES  31 A  402  LEU LYS GLU ILE ARG LYS THR PHE GLU GLY MET ALA              
HET    ICT  A1403      13                                                       
HET     MG  A1404       1                                                       
HET    NAP  A1520      48                                                       
HETNAM     ICT ISOCITRIC ACID                                                   
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
FORMUL   2  ICT    C6 H8 O7                                                     
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  NAP    C21 H28 N7 O17 P3                                            
FORMUL   5  HOH   *41(H2 O)                                                     
HELIX    1   1 ASP A   16  LEU A   31  1                                  16    
HELIX    2   2 GLY A   45  THR A   52  1                                   8    
HELIX    3   3 ASP A   54  GLY A   68  1                                  15    
HELIX    4   4 ASN A   79  ASN A   87  1                                   9    
HELIX    5   5 SER A   94  ASP A  104  1                                  11    
HELIX    6   6 GLY A  136  ASN A  141  5                                   6    
HELIX    7   7 THR A  183  ASN A  202  1                                  20    
HELIX    8   8 THR A  216  ASN A  231  1                                  16    
HELIX    9   9 TYR A  233  LYS A  240  1                                   8    
HELIX   10  10 ILE A  249  SER A  259  1                                  11    
HELIX   11  11 LYS A  268  GLY A  284  1                                  17    
HELIX   12  12 VAL A  309  LYS A  318  1                                  10    
HELIX   13  13 SER A  326  GLY A  345  1                                  20    
HELIX   14  14 ILE A  346  ASN A  366  1                                  21    
HELIX   15  15 THR A  370  SER A  375  1                                   6    
HELIX   16  16 ASN A  386  GLY A  400  1                                  15    
SHEET    1  AA10 THR A  39  ASP A  43  0                                        
SHEET    2  AA10 LEU A  10  ASP A  14  1  O  LEU A  10   N  GLU A  40           
SHEET    3  AA10 VAL A  69  LYS A  72  1  O  VAL A  69   N  VAL A  11           
SHEET    4  AA10 TYR A 300  ALA A 304  1  O  TYR A 300   N  GLY A  70           
SHEET    5  AA10 MET A 289  VAL A 294 -1  O  SER A 291   N  GLU A 303           
SHEET    6  AA10 THR A 106  PRO A 111 -1  O  THR A 106   N  VAL A 294           
SHEET    7  AA10 SER A 129  HIS A 133 -1  O  ILE A 130   N  ARG A 109           
SHEET    8  AA10 VAL A 264  CYS A 267  1  O  TRP A 265   N  ALA A 131           
SHEET    9  AA10 LEU A 205  THR A 209  1  O  TRP A 206   N  ALA A 266           
SHEET   10  AA10 TYR A 244  LEU A 248  1  O  PHE A 245   N  PHE A 207           
SHEET    1  AB 2 VAL A 142  VAL A 146  0                                        
SHEET    2  AB 2 GLY A 175  GLY A 179 -1  O  GLY A 175   N  VAL A 146           
SHEET    1  AC 2 GLY A 150  THR A 157  0                                        
SHEET    2  AC 2 VAL A 163  PHE A 171 -1  O  SER A 164   N  PHE A 156           
SHEET    1  AD 2 VAL A 368  MET A 369  0                                        
SHEET    2  AD 2 LYS A 383  ILE A 384  1  O  LYS A 383   N  MET A 369           
LINK        MG    MG A1404                 OD2 ASP A 250     1555   5554  2.15  
LINK        MG    MG A1404                 OD1 ASP A 273     1555   1555  2.04  
LINK        MG    MG A1404                 O1  ICT A1403     1555   1555  2.12  
LINK        MG    MG A1404                 O7  ICT A1403     1555   1555  2.19  
LINK        MG    MG A1404                 O   HOH A2029     1555   1555  1.95  
SITE     1 AC1 18 THR A  75  THR A  77  ARG A  82  ASP A 251                    
SITE     2 AC1 18 ARG A 255  LEU A 286  ALA A 287  HIS A 306                    
SITE     3 AC1 18 GLY A 307  THR A 308  VAL A 309  THR A 310                    
SITE     4 AC1 18 ARG A 311  HIS A 312  ASN A 325  ICT A1403                    
SITE     5 AC1 18 HOH A2032  HOH A2040                                          
SITE     1 AC2 15 THR A  77  SER A  94  ASN A  96  ARG A 100                    
SITE     2 AC2 15 ARG A 109  ARG A 132  TYR A 139  LYS A 210                    
SITE     3 AC2 15 ILE A 213  ASP A 250  ASP A 273  ALA A 305                    
SITE     4 AC2 15  MG A1404  NAP A1520  HOH A2029                               
SITE     1 AC3  4 ASP A 250  ASP A 273  ICT A1403  HOH A2029                    
CRYST1  129.200  129.200   60.590  90.00  90.00 120.00 P 32 2 1      6          
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      0.007740  0.004469  0.000000        0.00000                         
SCALE2      0.000000  0.008937  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016504        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system