GenomeNet

Database: PDB
Entry: 3B4W
LinkDB: 3B4W
Original site: 3B4W 
HEADER    OXIDOREDUCTASE                          24-OCT-07   3B4W              
TITLE     CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ALDEHYDE DEHYDROGENASE
TITLE    2 COMPLEXED WITH NAD+                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALDEHYDE DEHYDROGENASE;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.2.1.-;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 83332;                                               
SOURCE   4 STRAIN: H37RV;                                                       
SOURCE   5 ATCC: 25618;                                                         
SOURCE   6 GENE: RV0223C, MT0233;                                               
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET28B                           
KEYWDS    RV0223C-NAD COMPLEX, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE    
KEYWDS   2 INITIATIVE, INTEGRATED CENTER FOR STRUCTURE AND FUNCTION INNOVATION, 
KEYWDS   3 ISFI, TB STRUCTURAL GENOMICS CONSORTIUM, TBSGC, OXIDOREDUCTASE       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.H.MOON,A.E.LYON,M.YU,L-W.HUNG,T.TERWILLIGER,C-Y.KIM,INTEGRATED      
AUTHOR   2 CENTER FOR STRUCTURE AND FUNCTION INNOVATION (ISFI),TB STRUCTURAL    
AUTHOR   3 GENOMICS CONSORTIUM (TBSGC)                                          
REVDAT   3   13-JUL-11 3B4W    1       VERSN                                    
REVDAT   2   24-FEB-09 3B4W    1       VERSN                                    
REVDAT   1   27-NOV-07 3B4W    0                                                
JRNL        AUTH   J.H.MOON,A.E.LYON,M.YU,L-W.HUNG,T.TERWILLIGER,C-Y.KIM        
JRNL        TITL   X-RAY CRYSTAL STRUCTURE OF ALDEHYDE DEHYDROGENASE FROM       
JRNL        TITL 2 MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH NAD+.              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.90                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 57064                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5471                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1  1.8200 -  1.8000    0.80        0   144  0.2394 0.2809        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.45180                                              
REMARK   3    B22 (A**2) : 0.45180                                              
REMARK   3    B33 (A**2) : -0.90350                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  : 18.283           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3B4W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB045082.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795, 0.9800, 0.9600             
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62513                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.896                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, 0.8 M AMMONIUM SULFATE, PH    
REMARK 280  6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.27150            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       67.55550            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       67.55550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       54.40725            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       67.55550            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       67.55550            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       18.13575            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       67.55550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       67.55550            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       54.40725            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       67.55550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       67.55550            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       18.13575            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       36.27150            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT OF THIS PROTEIN IS    
REMARK 300 UNKNOWN.                                                             
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5430 ANGSTROM**2                          
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  0.000000 -1.000000  0.000000      135.11100            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000      135.11100            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       36.27150            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1178  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     ALA A   487                                                      
REMARK 465     GLY A   488                                                      
REMARK 465     SER A   489                                                      
REMARK 465     HIS A   490                                                      
REMARK 465     HIS A   491                                                      
REMARK 465     HIS A   492                                                      
REMARK 465     HIS A   493                                                      
REMARK 465     HIS A   494                                                      
REMARK 465     HIS A   495                                                      
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    TRP A 110      -61.66    -99.41                                   
REMARK 500    LEU A 255     -155.81   -119.62                                   
REMARK 500    LYS A 258       57.09   -145.06                                   
REMARK 500    ASP A 399      -72.64    -86.97                                   
REMARK 500    ALA A 416     -158.64   -144.74                                   
REMARK 500    LYS A 456     -134.83     53.29                                   
REMARK 500    ASN A 464      165.42     70.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1231        DISTANCE =  6.00 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 703                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: RV0223C   RELATED DB: TARGETDB                           
REMARK 900 MYCOBACTERIUM TUBERCULOSIS ALDEHYDE DEHYDROGENASE                    
DBREF  3B4W A    1   487  UNP    P96405   P96405_MYCTU     1    487             
SEQADV 3B4W GLY A  488  UNP  P96405              EXPRESSION TAG                 
SEQADV 3B4W SER A  489  UNP  P96405              EXPRESSION TAG                 
SEQADV 3B4W HIS A  490  UNP  P96405              EXPRESSION TAG                 
SEQADV 3B4W HIS A  491  UNP  P96405              EXPRESSION TAG                 
SEQADV 3B4W HIS A  492  UNP  P96405              EXPRESSION TAG                 
SEQADV 3B4W HIS A  493  UNP  P96405              EXPRESSION TAG                 
SEQADV 3B4W HIS A  494  UNP  P96405              EXPRESSION TAG                 
SEQADV 3B4W HIS A  495  UNP  P96405              EXPRESSION TAG                 
SEQRES   1 A  495  MET SER ASP SER ALA THR GLU TYR ASP LYS LEU PHE ILE          
SEQRES   2 A  495  GLY GLY LYS TRP THR LYS PRO SER THR SER ASP VAL ILE          
SEQRES   3 A  495  GLU VAL ARG CYS PRO ALA THR GLY GLU TYR VAL GLY LYS          
SEQRES   4 A  495  VAL PRO MET ALA ALA ALA ALA ASP VAL ASP ALA ALA VAL          
SEQRES   5 A  495  ALA ALA ALA ARG ALA ALA PHE ASP ASN GLY PRO TRP PRO          
SEQRES   6 A  495  SER THR PRO PRO HIS GLU ARG ALA ALA VAL ILE ALA ALA          
SEQRES   7 A  495  ALA VAL LYS MET LEU ALA GLU ARG LYS ASP LEU PHE THR          
SEQRES   8 A  495  LYS LEU LEU ALA ALA GLU THR GLY GLN PRO PRO THR ILE          
SEQRES   9 A  495  ILE GLU THR MET HIS TRP MET GLY SER MET GLY ALA MET          
SEQRES  10 A  495  ASN TYR PHE ALA GLY ALA ALA ASP LYS VAL THR TRP THR          
SEQRES  11 A  495  GLU THR ARG THR GLY SER TYR GLY GLN SER ILE VAL SER          
SEQRES  12 A  495  ARG GLU PRO VAL GLY VAL VAL GLY ALA ILE VAL ALA TRP          
SEQRES  13 A  495  ASN VAL PRO LEU PHE LEU ALA VAL ASN LYS ILE ALA PRO          
SEQRES  14 A  495  ALA LEU LEU ALA GLY CYS THR ILE VAL LEU LYS PRO ALA          
SEQRES  15 A  495  ALA GLU THR PRO LEU THR ALA ASN ALA LEU ALA GLU VAL          
SEQRES  16 A  495  PHE ALA GLU VAL GLY LEU PRO GLU GLY VAL LEU SER VAL          
SEQRES  17 A  495  VAL PRO GLY GLY ILE GLU THR GLY GLN ALA LEU THR SER          
SEQRES  18 A  495  ASN PRO ASP ILE ASP MET PHE THR PHE THR GLY SER SER          
SEQRES  19 A  495  ALA VAL GLY ARG GLU VAL GLY ARG ARG ALA ALA GLU MET          
SEQRES  20 A  495  LEU LYS PRO CYS THR LEU GLU LEU GLY GLY LYS SER ALA          
SEQRES  21 A  495  ALA ILE ILE LEU GLU ASP VAL ASP LEU ALA ALA ALA ILE          
SEQRES  22 A  495  PRO MET MET VAL PHE SER GLY VAL MET ASN ALA GLY GLN          
SEQRES  23 A  495  GLY CYS VAL ASN GLN THR ARG ILE LEU ALA PRO ARG SER          
SEQRES  24 A  495  ARG TYR ASP GLU ILE VAL ALA ALA VAL THR ASN PHE VAL          
SEQRES  25 A  495  THR ALA LEU PRO VAL GLY PRO PRO SER ASP PRO ALA ALA          
SEQRES  26 A  495  GLN ILE GLY PRO LEU ILE SER GLU LYS GLN ARG THR ARG          
SEQRES  27 A  495  VAL GLU GLY TYR ILE ALA LYS GLY ILE GLU GLU GLY ALA          
SEQRES  28 A  495  ARG LEU VAL CYS GLY GLY GLY ARG PRO GLU GLY LEU ASP          
SEQRES  29 A  495  ASN GLY PHE PHE ILE GLN PRO THR VAL PHE ALA ASP VAL          
SEQRES  30 A  495  ASP ASN LYS MET THR ILE ALA GLN GLU GLU ILE PHE GLY          
SEQRES  31 A  495  PRO VAL LEU ALA ILE ILE PRO TYR ASP THR GLU GLU ASP          
SEQRES  32 A  495  ALA ILE ALA ILE ALA ASN ASP SER VAL TYR GLY LEU ALA          
SEQRES  33 A  495  GLY SER VAL TRP THR THR ASP VAL PRO LYS GLY ILE LYS          
SEQRES  34 A  495  ILE SER GLN GLN ILE ARG THR GLY THR TYR GLY ILE ASN          
SEQRES  35 A  495  TRP TYR ALA PHE ASP PRO GLY SER PRO PHE GLY GLY TYR          
SEQRES  36 A  495  LYS ASN SER GLY ILE GLY ARG GLU ASN GLY PRO GLU GLY          
SEQRES  37 A  495  VAL GLU HIS PHE THR GLN GLN LYS SER VAL LEU LEU PRO          
SEQRES  38 A  495  MET GLY TYR THR VAL ALA GLY SER HIS HIS HIS HIS HIS          
SEQRES  39 A  495  HIS                                                          
HET    SO4  A 801       5                                                       
HET    SO4  A 802       5                                                       
HET    NAD  A 500      44                                                       
HET    GOL  A 600       6                                                       
HET    GOL  A 601       6                                                       
HET    GOL  A 602       6                                                       
HET    GOL  A 603      14                                                       
HET    EOH  A 701       3                                                       
HET    EOH  A 702       3                                                       
HET    EOH  A 703       9                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     GOL GLYCEROL                                                         
HETNAM     EOH ETHANOL                                                          
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4  NAD    C21 H27 N7 O14 P2                                            
FORMUL   5  GOL    4(C3 H8 O3)                                                  
FORMUL   9  EOH    3(C2 H6 O)                                                   
FORMUL  12  HOH   *441(H2 O)                                                    
HELIX    1   1 ALA A   44  GLY A   62  1                                  19    
HELIX    2   2 PRO A   68  ARG A   86  1                                  19    
HELIX    3   3 ARG A   86  GLY A   99  1                                  14    
HELIX    4   4 PRO A  101  MET A  108  1                                   8    
HELIX    5   5 TRP A  110  GLY A  122  1                                  13    
HELIX    6   6 ALA A  123  VAL A  127  5                                   5    
HELIX    7   7 VAL A  158  ALA A  173  1                                  16    
HELIX    8   8 PRO A  186  VAL A  199  1                                  14    
HELIX    9   9 GLY A  212  THR A  220  1                                   9    
HELIX   10  10 SER A  233  MET A  247  1                                  15    
HELIX   11  11 ASP A  268  MET A  282  1                                  15    
HELIX   12  12 ASN A  283  GLN A  286  5                                   4    
HELIX   13  13 ARG A  300  LEU A  315  1                                  16    
HELIX   14  14 SER A  332  GLU A  349  1                                  18    
HELIX   15  15 MET A  381  GLU A  386  1                                   6    
HELIX   16  16 THR A  400  ASP A  410  1                                  11    
HELIX   17  17 ASP A  423  ILE A  434  1                                  12    
HELIX   18  18 TYR A  455  ASN A  457  5                                   3    
HELIX   19  19 ASN A  464  HIS A  471  1                                   8    
SHEET    1   A 3 THR A   6  GLU A   7  0                                        
SHEET    2   A 3 TYR A  36  PRO A  41  1  O  VAL A  37   N  THR A   6           
SHEET    3   A 3 VAL A  25  ARG A  29 -1  N  ILE A  26   O  VAL A  40           
SHEET    1   B 2 LEU A  11  ILE A  13  0                                        
SHEET    2   B 2 LYS A  16  THR A  18 -1  O  THR A  18   N  LEU A  11           
SHEET    1   C 3 THR A 130  GLY A 135  0                                        
SHEET    2   C 3 GLY A 138  PRO A 146 -1  O  SER A 140   N  ARG A 133           
SHEET    3   C 3 THR A 473  LEU A 479 -1  O  GLN A 474   N  GLU A 145           
SHEET    1   D 6 LEU A 206  VAL A 208  0                                        
SHEET    2   D 6 THR A 176  LYS A 180  1  N  LEU A 179   O  SER A 207           
SHEET    3   D 6 VAL A 149  ILE A 153  1  N  ALA A 152   O  LYS A 180           
SHEET    4   D 6 MET A 227  THR A 231  1  O  MET A 227   N  GLY A 151           
SHEET    5   D 6 CYS A 251  GLU A 254  1  O  GLU A 254   N  PHE A 230           
SHEET    6   D 6 GLY A 459  ILE A 460 -1  O  ILE A 460   N  LEU A 253           
SHEET    1   E 7 ARG A 352  CYS A 355  0                                        
SHEET    2   E 7 THR A 372  ALA A 375 -1  O  ALA A 375   N  ARG A 352           
SHEET    3   E 7 VAL A 392  TYR A 398  1  O  LEU A 393   N  THR A 372           
SHEET    4   E 7 GLN A 291  PRO A 297  1  N  ILE A 294   O  ALA A 394           
SHEET    5   E 7 SER A 259  ILE A 263  1  N  ALA A 261   O  LEU A 295           
SHEET    6   E 7 SER A 418  TRP A 420  1  O  SER A 418   N  ILE A 262           
SHEET    7   E 7 GLY A 440  ILE A 441  1  O  GLY A 440   N  VAL A 419           
SITE     1 AC1  5 ALA A 235  ARG A 238  HOH A 807  HOH A 925                    
SITE     2 AC1  5 HOH A1105                                                     
SITE     1 AC2  2 ARG A 242  ARG A 243                                          
SITE     1 AC3 28 ILE A 153  VAL A 154  ALA A 155  TRP A 156                    
SITE     2 AC3 28 ASN A 157  LYS A 180  ALA A 182  ILE A 213                    
SITE     3 AC3 28 GLY A 216  PHE A 230  THR A 231  GLY A 232                    
SITE     4 AC3 28 SER A 233  VAL A 236  GLU A 239  GLU A 254                    
SITE     5 AC3 28 LEU A 255  GLY A 256  CYS A 288  GLU A 387                    
SITE     6 AC3 28 PHE A 389  PHE A 452  GOL A 602  HOH A 855                    
SITE     7 AC3 28 HOH A 899  HOH A 947  HOH A1120  HOH A1141                    
SITE     1 AC4  5 ASP A 268  ARG A 298  HOH A1168  HOH A1192                    
SITE     2 AC4  5 HOH A1207                                                     
SITE     1 AC5  7 ASP A 302  VAL A 305  ALA A 306  PRO A 316                    
SITE     2 AC5  7 GLN A 326  ARG A 352  HOH A 870                               
SITE     1 AC6  7 ASN A 157  PHE A 161  GLY A 287  CYS A 288                    
SITE     2 AC6  7 NAD A 500  HOH A 899  HOH A1225                               
SITE     1 AC7  9 MET A 227  PRO A 250  GLY A 461  HIS A 471                    
SITE     2 AC7  9 THR A 473  GLN A 474  HOH A 850  HOH A1062                    
SITE     3 AC7  9 HOH A1125                                                     
SITE     1 AC8  2 CYS A  30  PRO A 320                                          
SITE     1 AC9  5 VAL A 267  ASP A 268  LEU A 269  ALA A 270                    
SITE     2 AC9  5 ARG A 300                                                     
SITE     1 BC1  4 ASN A 379  ILE A 407  ASP A 410  HOH A 934                    
CRYST1  135.111  135.111   72.543  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007401  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007401  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013785        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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