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Database: PDB
Entry: 2VHV
LinkDB: 2VHV
Original site: 2VHV 
HEADER    OXIDOREDUCTASE                          26-NOV-07   2VHV              
TITLE     CRYSTAL STRUCTURE OF THE D270A MUTANT OF L-ALANINE                    
TITLE    2 DEHYDROGENASE FROM MYCOBACTERIUM TUBERCULOSIS IN                     
TITLE    3 COMPLEX WITH NADH.                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALANINE DEHYDROGENASE;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: 40 KDA ANTIGEN, TB43;                                       
COMPND   5 EC: 1.4.1.1;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET26                                     
KEYWDS    NAD, SECRETED, OXIDOREDUCTASE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.AGREN,G.SCHNEIDER                                                   
REVDAT   3   24-FEB-09 2VHV    1       VERSN                                    
REVDAT   2   11-NOV-08 2VHV    1       JRNL   REMARK HET    HETNAM              
REVDAT   2 2                           FORMUL SCALE1 SCALE2 SCALE3              
REVDAT   2 3                           TER    HETATM CONECT                     
REVDAT   1   11-MAR-08 2VHV    0                                                
JRNL        AUTH   D.AGREN,M.STEHR,C.L.BERTHOLD,S.KAPOOR,W.OEHLMANN,            
JRNL        AUTH 2 M.SINGH,G.SCHNEIDER                                          
JRNL        TITL   THREE-DIMENSIONAL STRUCTURES OF APO- AND HOLO-L-             
JRNL        TITL 2 ALANINE DEHYDROGENASE FROM MYCOBACTERIUM                     
JRNL        TITL 3 TUBERCULOSIS REVEAL CONFORMATIONAL CHANGES UPON              
JRNL        TITL 4 COENZYME BINDING.                                            
JRNL        REF    J.MOL.BIOL.                   V. 377  1161 2008              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   18304579                                                     
JRNL        DOI    10.1016/J.JMB.2008.01.091                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.8  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 21753                          
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1162                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1576                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 79                           
REMARK   3   BIN FREE R VALUE                    : 0.3010                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5438                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 88                                      
REMARK   3   SOLVENT ATOMS            : 17                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.349         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.248         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.753        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.904                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5640 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7702 ; 1.375 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   740 ; 5.640 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   210 ;36.287 ;23.429       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   848 ;17.764 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    38 ;18.954 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   910 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4234 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2766 ; 0.211 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3830 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   202 ; 0.115 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    38 ; 0.202 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.349 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3743 ; 0.487 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5860 ; 0.835 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2105 ; 1.265 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1842 ; 2.079 ; 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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     100      2                      
REMARK   3           1     B      1       B     100      2                      
REMARK   3           2     A    310       A     370      2                      
REMARK   3           2     B    310       B     370      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    644 ;  0.02 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    558 ;  0.21 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):    644 ;  0.28 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    558 ;  0.30 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    130       A     280      2                      
REMARK   3           1     B    130       B     280      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    A    (A):    604 ;  0.02 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    478 ;  0.16 ;  0.50           
REMARK   3   TIGHT THERMAL      2    A (A**2):    604 ;  0.28 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    478 ;  0.38 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 2VHV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-NOV-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-34559.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-SEP-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22947                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.80                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 4.1                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 4.4                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.90                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.5                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.40                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.10                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 58.62                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS TRIS PROPANE PH 8.2,            
REMARK 280  20% PEG 3350 AND 0.2M SODIUM ACETATE. CO CRYSTALLIZED WITH          
REMARK 280  10MM NADH WHICH WAS ADDED TO THE PROTEIN SOLUTION                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3                           
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       70.40100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.40100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       70.40100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.40100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       70.40100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       70.40100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       70.40100            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       70.40100            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       70.40100            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       70.40100            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       70.40100            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       70.40100            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       70.40100            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       70.40100            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       70.40100            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       70.40100            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       70.40100            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       70.40100            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 19880 ANGSTROM**2                         
REMARK 350 TOTAL SURFACE AREA FOR THE COMPLEX:  86410 ANGSTROM**2               
REMARK 350 GAIN IN SOLVENT FREE ENERGY: -97 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 350   BIOMT1   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000       70.40100            
REMARK 350   BIOMT3   2  0.000000 -1.000000  0.000000       70.40100            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000      -70.40100            
REMARK 350   BIOMT2   3  0.000000  0.000000 -1.000000       70.40100            
REMARK 350   BIOMT3   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASP 270 TO ASN                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASP 270 TO ASN                        
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     HIS A   372                                                      
REMARK 465     HIS A   373                                                      
REMARK 465     HIS A   374                                                      
REMARK 465     HIS A   375                                                      
REMARK 465     HIS A   376                                                      
REMARK 465     HIS A   377                                                      
REMARK 465     HIS B   372                                                      
REMARK 465     HIS B   373                                                      
REMARK 465     HIS B   374                                                      
REMARK 465     HIS B   375                                                      
REMARK 465     HIS B   376                                                      
REMARK 465     HIS B   377                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  12       28.70     45.95                                   
REMARK 500    ALA A  98      -19.63    -49.74                                   
REMARK 500    SER A 220       62.87    -67.73                                   
REMARK 500    ALA A 238       46.84   -140.15                                   
REMARK 500    HIS A 291     -131.97     49.27                                   
REMARK 500    CYS A 297       52.99   -141.43                                   
REMARK 500    VAL A 305       53.34   -141.13                                   
REMARK 500    ALA B 238       43.08   -141.54                                   
REMARK 500    HIS B 291     -129.99     44.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI A1372                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI B1372                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VHW   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HOLO L-ALANINE DEHYDROGENASE                   
REMARK 900  FROM MYCOBACTERIUM TUBERCULOSIS IN THE OPEN AND                     
REMARK 900  CLOSED CONFORMATION                                                 
REMARK 900 RELATED ID: 2VHX   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF                         
REMARK 900  L-ALANINE DEHYDROGENASE FROM MYCOBACTERIUM                          
REMARK 900  TUBERCULOSIS WITH NAD+ AND PYRUVATE                                 
REMARK 900 RELATED ID: 2VHY   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF APO L-ALANINE DEHYDROGENASE                    
REMARK 900  FROM MYCOBACTERIUM TUBERCULOSIS                                     
REMARK 900 RELATED ID: 2VHZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HOLO L-ALANINE DEHYDROGENASE                   
REMARK 900  FROM MYCOBACTERIUM TUBERCULOSIS IN THE CLOSED                       
REMARK 900  CONFORMATION                                                        
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 EXPRESSED WITH A C-TERMINAL 6XHIS TAG.                               
DBREF  2VHV A    1   371  UNP    P30234   DHA_MYCTU        1    371             
DBREF  2VHV A  372   377  PDB    2VHV     2VHV           372    377             
DBREF  2VHV B    1   371  UNP    P30234   DHA_MYCTU        1    371             
DBREF  2VHV B  372   377  PDB    2VHV     2VHV           372    377             
SEQADV 2VHV ASN A  270  UNP  P30234    ASP   270 ENGINEERED MUTATION            
SEQADV 2VHV ASN B  270  UNP  P30234    ASP   270 ENGINEERED MUTATION            
SEQRES   1 A  377  MET ARG VAL GLY ILE PRO THR GLU THR LYS ASN ASN GLU          
SEQRES   2 A  377  PHE ARG VAL ALA ILE THR PRO ALA GLY VAL ALA GLU LEU          
SEQRES   3 A  377  THR ARG ARG GLY HIS GLU VAL LEU ILE GLN ALA GLY ALA          
SEQRES   4 A  377  GLY GLU GLY SER ALA ILE THR ASP ALA ASP PHE LYS ALA          
SEQRES   5 A  377  ALA GLY ALA GLN LEU VAL GLY THR ALA ASP GLN VAL TRP          
SEQRES   6 A  377  ALA ASP ALA ASP LEU LEU LEU LYS VAL LYS GLU PRO ILE          
SEQRES   7 A  377  ALA ALA GLU TYR GLY ARG LEU ARG HIS GLY GLN ILE LEU          
SEQRES   8 A  377  PHE THR PHE LEU HIS LEU ALA ALA SER ARG ALA CYS THR          
SEQRES   9 A  377  ASP ALA LEU LEU ASP SER GLY THR THR SER ILE ALA TYR          
SEQRES  10 A  377  GLU THR VAL GLN THR ALA ASP GLY ALA LEU PRO LEU LEU          
SEQRES  11 A  377  ALA PRO MET SER GLU VAL ALA GLY ARG LEU ALA ALA GLN          
SEQRES  12 A  377  VAL GLY ALA TYR HIS LEU MET ARG THR GLN GLY GLY ARG          
SEQRES  13 A  377  GLY VAL LEU MET GLY GLY VAL PRO GLY VAL GLU PRO ALA          
SEQRES  14 A  377  ASP VAL VAL VAL ILE GLY ALA GLY THR ALA GLY TYR ASN          
SEQRES  15 A  377  ALA ALA ARG ILE ALA ASN GLY MET GLY ALA THR VAL THR          
SEQRES  16 A  377  VAL LEU ASP ILE ASN ILE ASP LYS LEU ARG GLN LEU ASP          
SEQRES  17 A  377  ALA GLU PHE CYS GLY ARG ILE HIS THR ARG TYR SER SER          
SEQRES  18 A  377  ALA TYR GLU LEU GLU GLY ALA VAL LYS ARG ALA ASP LEU          
SEQRES  19 A  377  VAL ILE GLY ALA VAL LEU VAL PRO GLY ALA LYS ALA PRO          
SEQRES  20 A  377  LYS LEU VAL SER ASN SER LEU VAL ALA HIS MET LYS PRO          
SEQRES  21 A  377  GLY ALA VAL LEU VAL ASP ILE ALA ILE ASN GLN GLY GLY          
SEQRES  22 A  377  CYS PHE GLU GLY SER ARG PRO THR THR TYR ASP HIS PRO          
SEQRES  23 A  377  THR PHE ALA VAL HIS ASP THR LEU PHE TYR CYS VAL ALA          
SEQRES  24 A  377  ASN MET PRO ALA SER VAL PRO LYS THR SER THR TYR ALA          
SEQRES  25 A  377  LEU THR ASN ALA THR MET PRO TYR VAL LEU GLU LEU ALA          
SEQRES  26 A  377  ASP HIS GLY TRP ARG ALA ALA CYS ARG SER ASN PRO ALA          
SEQRES  27 A  377  LEU ALA LYS GLY LEU SER THR HIS GLU GLY ALA LEU LEU          
SEQRES  28 A  377  SER GLU ARG VAL ALA THR ASP LEU GLY VAL PRO PHE THR          
SEQRES  29 A  377  GLU PRO ALA SER VAL LEU ALA HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  377  MET ARG VAL GLY ILE PRO THR GLU THR LYS ASN ASN GLU          
SEQRES   2 B  377  PHE ARG VAL ALA ILE THR PRO ALA GLY VAL ALA GLU LEU          
SEQRES   3 B  377  THR ARG ARG GLY HIS GLU VAL LEU ILE GLN ALA GLY ALA          
SEQRES   4 B  377  GLY GLU GLY SER ALA ILE THR ASP ALA ASP PHE LYS ALA          
SEQRES   5 B  377  ALA GLY ALA GLN LEU VAL GLY THR ALA ASP GLN VAL TRP          
SEQRES   6 B  377  ALA ASP ALA ASP LEU LEU LEU LYS VAL LYS GLU PRO ILE          
SEQRES   7 B  377  ALA ALA GLU TYR GLY ARG LEU ARG HIS GLY GLN ILE LEU          
SEQRES   8 B  377  PHE THR PHE LEU HIS LEU ALA ALA SER ARG ALA CYS THR          
SEQRES   9 B  377  ASP ALA LEU LEU ASP SER GLY THR THR SER ILE ALA TYR          
SEQRES  10 B  377  GLU THR VAL GLN THR ALA ASP GLY ALA LEU PRO LEU LEU          
SEQRES  11 B  377  ALA PRO MET SER GLU VAL ALA GLY ARG LEU ALA ALA GLN          
SEQRES  12 B  377  VAL GLY ALA TYR HIS LEU MET ARG THR GLN GLY GLY ARG          
SEQRES  13 B  377  GLY VAL LEU MET GLY GLY VAL PRO GLY VAL GLU PRO ALA          
SEQRES  14 B  377  ASP VAL VAL VAL ILE GLY ALA GLY THR ALA GLY TYR ASN          
SEQRES  15 B  377  ALA ALA ARG ILE ALA ASN GLY MET GLY ALA THR VAL THR          
SEQRES  16 B  377  VAL LEU ASP ILE ASN ILE ASP LYS LEU ARG GLN LEU ASP          
SEQRES  17 B  377  ALA GLU PHE CYS GLY ARG ILE HIS THR ARG TYR SER SER          
SEQRES  18 B  377  ALA TYR GLU LEU GLU GLY ALA VAL LYS ARG ALA ASP LEU          
SEQRES  19 B  377  VAL ILE GLY ALA VAL LEU VAL PRO GLY ALA LYS ALA PRO          
SEQRES  20 B  377  LYS LEU VAL SER ASN SER LEU VAL ALA HIS MET LYS PRO          
SEQRES  21 B  377  GLY ALA VAL LEU VAL ASP ILE ALA ILE ASN GLN GLY GLY          
SEQRES  22 B  377  CYS PHE GLU GLY SER ARG PRO THR THR TYR ASP HIS PRO          
SEQRES  23 B  377  THR PHE ALA VAL HIS ASP THR LEU PHE TYR CYS VAL ALA          
SEQRES  24 B  377  ASN MET PRO ALA SER VAL PRO LYS THR SER THR TYR ALA          
SEQRES  25 B  377  LEU THR ASN ALA THR MET PRO TYR VAL LEU GLU LEU ALA          
SEQRES  26 B  377  ASP HIS GLY TRP ARG ALA ALA CYS ARG SER ASN PRO ALA          
SEQRES  27 B  377  LEU ALA LYS GLY LEU SER THR HIS GLU GLY ALA LEU LEU          
SEQRES  28 B  377  SER GLU ARG VAL ALA THR ASP LEU GLY VAL PRO PHE THR          
SEQRES  29 B  377  GLU PRO ALA SER VAL LEU ALA HIS HIS HIS HIS HIS HIS          
HET    NAI  A1372      44                                                       
HET    NAI  B1372      44                                                       
HETNAM     NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE                     
FORMUL   3  NAI    2(C21 H29 N7 O14 P2)                                         
FORMUL   4  HOH   *17(H2 O1)                                                    
HELIX    1   1 THR A   19  ARG A   29  1                                  11    
HELIX    2   2 GLY A   40  ALA A   44  5                                   5    
HELIX    3   3 THR A   46  GLY A   54  1                                   9    
HELIX    4   4 THR A   60  ALA A   68  1                                   9    
HELIX    5   5 ILE A   78  LEU A   85  5                                   8    
HELIX    6   6 HIS A   96  ALA A   99  5                                   4    
HELIX    7   7 SER A  100  GLY A  111  1                                  12    
HELIX    8   8 GLU A  118  VAL A  120  5                                   3    
HELIX    9   9 LEU A  130  LEU A  149  1                                  20    
HELIX   10  10 MET A  150  GLY A  154  5                                   5    
HELIX   11  11 GLY A  177  MET A  190  1                                  14    
HELIX   12  12 ASN A  200  PHE A  211  1                                  12    
HELIX   13  13 SER A  221  ALA A  232  1                                  12    
HELIX   14  14 SER A  251  ALA A  256  1                                   6    
HELIX   15  15 ALA A  268  GLY A  272  5                                   5    
HELIX   16  16 ASN A  300  SER A  304  5                                   5    
HELIX   17  17 VAL A  305  LYS A  341  1                                  37    
HELIX   18  18 SER A  352  GLY A  360  1                                   9    
HELIX   19  19 GLU A  365  VAL A  369  5                                   5    
HELIX   20  20 THR B   19  ARG B   29  1                                  11    
HELIX   21  21 GLY B   40  ALA B   44  5                                   5    
HELIX   22  22 THR B   46  GLY B   54  1                                   9    
HELIX   23  23 THR B   60  ALA B   68  1                                   9    
HELIX   24  24 ILE B   78  LEU B   85  5                                   8    
HELIX   25  25 HIS B   96  ALA B   99  5                                   4    
HELIX   26  26 SER B  100  GLY B  111  1                                  12    
HELIX   27  27 GLU B  118  VAL B  120  5                                   3    
HELIX   28  28 LEU B  130  LEU B  149  1                                  20    
HELIX   29  29 MET B  150  GLY B  154  5                                   5    
HELIX   30  30 GLY B  177  MET B  190  1                                  14    
HELIX   31  31 ASN B  200  PHE B  211  1                                  12    
HELIX   32  32 SER B  221  ALA B  232  1                                  12    
HELIX   33  33 SER B  251  ALA B  256  1                                   6    
HELIX   34  34 ALA B  268  GLY B  272  5                                   5    
HELIX   35  35 ASN B  300  SER B  304  5                                   5    
HELIX   36  36 VAL B  305  LYS B  341  1                                  37    
HELIX   37  37 SER B  352  GLY B  360  1                                   9    
HELIX   38  38 GLU B  365  VAL B  369  5                                   5    
SHEET    1  AA 8 GLN A  56  VAL A  58  0                                        
SHEET    2  AA 8 GLU A  32  GLN A  36  1  O  VAL A  33   N  GLN A  56           
SHEET    3  AA 8 ARG A   2  ILE A   5  1  O  VAL A   3   N  LEU A  34           
SHEET    4  AA 8 LEU A  70  LEU A  72  1  O  LEU A  70   N  GLY A   4           
SHEET    5  AA 8 ILE A  90  THR A  93  1  O  ILE A  90   N  LEU A  71           
SHEET    6  AA 8 THR A 113  ALA A 116  1  O  THR A 113   N  LEU A  91           
SHEET    7  AA 8 LEU A 343  HIS A 346 -1  N  SER A 344   O  SER A 114           
SHEET    8  AA 8 ALA A 349  LEU A 350 -1  O  ALA A 349   N  HIS A 346           
SHEET    1  AB 7 HIS A 216  TYR A 219  0                                        
SHEET    2  AB 7 THR A 193  ASP A 198  1  O  VAL A 194   N  HIS A 216           
SHEET    3  AB 7 ASP A 170  ILE A 174  1  O  VAL A 171   N  THR A 195           
SHEET    4  AB 7 LEU A 234  GLY A 237  1  O  LEU A 234   N  VAL A 172           
SHEET    5  AB 7 VAL A 263  ASP A 266  1  O  VAL A 263   N  VAL A 235           
SHEET    6  AB 7 THR A 293  TYR A 296  1  O  LEU A 294   N  LEU A 264           
SHEET    7  AB 7 THR A 287  VAL A 290 -1  O  PHE A 288   N  PHE A 295           
SHEET    1  BA 8 GLN B  56  VAL B  58  0                                        
SHEET    2  BA 8 GLU B  32  GLN B  36  1  O  VAL B  33   N  GLN B  56           
SHEET    3  BA 8 ARG B   2  ILE B   5  1  O  VAL B   3   N  LEU B  34           
SHEET    4  BA 8 LEU B  70  LEU B  72  1  O  LEU B  70   N  GLY B   4           
SHEET    5  BA 8 ILE B  90  THR B  93  1  O  ILE B  90   N  LEU B  71           
SHEET    6  BA 8 THR B 113  ALA B 116  1  O  THR B 113   N  LEU B  91           
SHEET    7  BA 8 LEU B 343  HIS B 346 -1  N  SER B 344   O  SER B 114           
SHEET    8  BA 8 ALA B 349  LEU B 350 -1  O  ALA B 349   N  HIS B 346           
SHEET    1  BB 7 HIS B 216  TYR B 219  0                                        
SHEET    2  BB 7 THR B 193  ASP B 198  1  O  VAL B 194   N  HIS B 216           
SHEET    3  BB 7 ASP B 170  ILE B 174  1  O  VAL B 171   N  THR B 195           
SHEET    4  BB 7 LEU B 234  GLY B 237  1  O  LEU B 234   N  VAL B 172           
SHEET    5  BB 7 VAL B 263  ASP B 266  1  O  VAL B 263   N  VAL B 235           
SHEET    6  BB 7 THR B 293  TYR B 296  1  O  LEU B 294   N  LEU B 264           
SHEET    7  BB 7 THR B 287  VAL B 290 -1  O  PHE B 288   N  PHE B 295           
SITE     1 AC1 22 LEU A 130  MET A 133  SER A 134  ALA A 137                    
SITE     2 AC1 22 GLY A 177  THR A 178  ALA A 179  ASP A 198                    
SITE     3 AC1 22 LYS A 203  SER A 220  ALA A 238  VAL A 239                    
SITE     4 AC1 22 LEU A 240  LEU A 249  ILE A 267  ASN A 270                    
SITE     5 AC1 22 GLN A 271  VAL A 298  ALA A 299  ASN A 300                    
SITE     6 AC1 22 MET A 301  PRO A 302                                          
SITE     1 AC2 21 MET B 133  SER B 134  ALA B 137  GLY B 177                    
SITE     2 AC2 21 THR B 178  ALA B 179  ASP B 198  ILE B 199                    
SITE     3 AC2 21 LYS B 203  SER B 220  ALA B 238  VAL B 239                    
SITE     4 AC2 21 LEU B 240  LEU B 249  ILE B 267  ASN B 270                    
SITE     5 AC2 21 GLN B 271  VAL B 298  ALA B 299  MET B 301                    
SITE     6 AC2 21 PRO B 302                                                     
CRYST1  140.802  140.802  140.802  90.00  90.00  90.00 P 21 3       24          
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      0.007102  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007102  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007102        0.00000                         
MTRIX1   1 -1.000000  0.000290  0.000640      -35.21101    1                    
MTRIX2   1  0.000640  0.000480  1.000000       35.20195    1                    
MTRIX3   1  0.000290  1.000000 -0.000480      -35.18603    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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