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Database: PDB
Entry: 2WZM
LinkDB: 2WZM
Original site: 2WZM 
HEADER    OXIDOREDUCTASE                          30-NOV-09   2WZM              
TITLE     CRYSTAL STRUCTURE OF A MYCOBACTERIUM ALDO-KETO REDUCTASE IN           
TITLE    2 ITS APO AND LIGANDED FORM                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALDO-KETO REDUCTASE;                                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: UNCHARACTERIZED OXIDOREDUCTASE MSMEG_2407;                  
COMPND   5 EC: 1.1.1.218;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;                        
SOURCE   3 ORGANISM_TAXID: 246196;                                              
SOURCE   4 STRAIN: MC2 155;                                                     
SOURCE   5 ATCC: 700084;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST17                                   
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.SCOBLE,A.D.MCALISTER,Z.FULTON,S.TROY,E.BYRES,J.P.VIVIAN,            
AUTHOR   2 R.BRAMMANANTH,M.C.J.WILCE,J.LE NOURS,L.ZAKER-TABRIZI,                
AUTHOR   3 R.L.COPPEL,P.K.CRELLIN,J.ROSSJOHN,T.BEDDOE                           
REVDAT   4   14-APR-10 2WZM    1       JRNL                                     
REVDAT   3   16-MAR-10 2WZM    1       JRNL                                     
REVDAT   2   02-MAR-10 2WZM    1       REMARK                                   
REVDAT   1   16-FEB-10 2WZM    0                                                
JRNL        AUTH   J.SCOBLE,A.D.MCALISTER,Z.FULTON,S.TROY,E.BYRES,              
JRNL        AUTH 2 J.P.VIVIAN,R.BRAMMANANTH,M.C.J.WILCE,J.LE NOURS,             
JRNL        AUTH 3 L.ZAKER-TABRIZI,R.L.COPPEL,P.K.CRELLIN,J.ROSSJOHN,           
JRNL        AUTH 4 T.BEDDOE                                                     
JRNL        TITL   CRYSTAL STRUCTURE AND COMPARATIVE FUNCTIONAL                 
JRNL        TITL 2 ANALYSES OF A MYCOBACTERIUM ALDO-KETO REDUCTASE.             
JRNL        REF    J.MOL.BIOL.                   V. 398    26 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20188740                                                     
JRNL        DOI    10.1016/J.JMB.2010.02.021                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.64 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) : 1.64                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.49                          
REMARK   3   NUMBER OF REFLECTIONS             : 54193                          
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) : 0.18029                         
REMARK   3   R VALUE            (WORKING SET) : 0.17808                         
REMARK   3   FREE R VALUE                     : 0.22134                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2895                            
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) : 1.635                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.678                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3859                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.274                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 191                          
REMARK   3   BIN FREE R VALUE                    : 0.302                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4119                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 78                                      
REMARK   3   SOLVENT ATOMS            : 523                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.810                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.49                                                 
REMARK   3    B22 (A**2) : 0.49                                                 
REMARK   3    B33 (A**2) : -0.73                                                
REMARK   3    B12 (A**2) : 0.24                                                 
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): 0.109         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.109         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.073         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.082         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4280 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5864 ; 1.405 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   552 ; 5.331 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   187 ;35.013 ;24.332       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   635 ;12.613 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;13.579 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   683 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3260 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2026 ; 0.201 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2961 ; 0.302 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   346 ; 0.132 ; 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):    61 ; 0.167 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    39 ; 0.129 ; 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):  2783 ; 0.769 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4356 ; 1.287 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1700 ; 2.016 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1505 ; 2.843 ; 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. THE FIRST 9 RESIDUES WERE NOT MODELLED IN         
REMARK   3  STRUCTURE.                                                          
REMARK   4                                                                      
REMARK   4 2WZM COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-DEC-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-41866.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 277                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95367                            
REMARK 200  MONOCHROMATOR                  : NULL                               
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   : 57130                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.64                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.80                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 5.6                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.30                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.0                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.48                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.50                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.4                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2                        
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH 7.6, 1.85               
REMARK 280  (NH4)2HPO4                                                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
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                                                                      
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       64.56267            
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       32.28133            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     GLN B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  19       -4.60     80.56                                   
REMARK 500    ASP B  19       -1.96     79.09                                   
REMARK 500    GLU B  31       32.45    -91.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 THE SHEETS PRESENTED AS "BB" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA7 A1284                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA7 B1284                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WZT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A MYCOBACTERIUM ALDO- KETO REDUCTASE            
REMARK 900 IN ITS APO AND LIGANDED FORM                                         
DBREF  2WZM A    1   283  UNP    A0QV09   Y2407_MYCS2      1    283             
DBREF  2WZM B    1   283  UNP    A0QV09   Y2407_MYCS2      1    283             
SEQRES   1 A  283  MET THR ALA SER HIS GLY GLN ALA ALA ALA ILE PRO THR          
SEQRES   2 A  283  VAL THR LEU ASN ASP ASP ASN THR LEU PRO VAL VAL GLY          
SEQRES   3 A  283  ILE GLY VAL GLY GLU LEU SER ASP SER GLU ALA GLU ARG          
SEQRES   4 A  283  SER VAL SER ALA ALA LEU GLU ALA GLY TYR ARG LEU ILE          
SEQRES   5 A  283  ASP THR ALA ALA ALA TYR GLY ASN GLU ALA ALA VAL GLY          
SEQRES   6 A  283  ARG ALA ILE ALA ALA SER GLY ILE PRO ARG ASP GLU ILE          
SEQRES   7 A  283  TYR VAL THR THR LYS LEU ALA THR PRO ASP GLN GLY PHE          
SEQRES   8 A  283  THR SER SER GLN ALA ALA ALA ARG ALA SER LEU GLU ARG          
SEQRES   9 A  283  LEU GLY LEU ASP TYR VAL ASP LEU TYR LEU ILE HIS TRP          
SEQRES  10 A  283  PRO GLY GLY ASP THR SER LYS TYR VAL ASP SER TRP GLY          
SEQRES  11 A  283  GLY LEU MET LYS VAL LYS GLU ASP GLY ILE ALA ARG SER          
SEQRES  12 A  283  ILE GLY VAL CYS ASN PHE GLY ALA GLU ASP LEU GLU THR          
SEQRES  13 A  283  ILE VAL SER LEU THR TYR PHE THR PRO ALA VAL ASN GLN          
SEQRES  14 A  283  ILE GLU LEU HIS PRO LEU LEU ASN GLN ALA ALA LEU ARG          
SEQRES  15 A  283  GLU VAL ASN ALA GLY TYR ASN ILE VAL THR GLU ALA TYR          
SEQRES  16 A  283  GLY PRO LEU GLY VAL GLY ARG LEU LEU ASP HIS PRO ALA          
SEQRES  17 A  283  VAL THR ALA ILE ALA GLU ALA HIS GLY ARG THR ALA ALA          
SEQRES  18 A  283  GLN VAL LEU LEU ARG TRP SER ILE GLN LEU GLY ASN VAL          
SEQRES  19 A  283  VAL ILE SER ARG SER ALA ASN PRO GLU ARG ILE ALA SER          
SEQRES  20 A  283  ASN LEU ASP VAL PHE GLY PHE GLU LEU THR ALA ASP GLU          
SEQRES  21 A  283  MET GLU THR LEU ASN GLY LEU ASP ASP GLY THR ARG PHE          
SEQRES  22 A  283  ARG PRO ASP PRO ALA THR TYR THR GLY SER                      
SEQRES   1 B  283  MET THR ALA SER HIS GLY GLN ALA ALA ALA ILE PRO THR          
SEQRES   2 B  283  VAL THR LEU ASN ASP ASP ASN THR LEU PRO VAL VAL GLY          
SEQRES   3 B  283  ILE GLY VAL GLY GLU LEU SER ASP SER GLU ALA GLU ARG          
SEQRES   4 B  283  SER VAL SER ALA ALA LEU GLU ALA GLY TYR ARG LEU ILE          
SEQRES   5 B  283  ASP THR ALA ALA ALA TYR GLY ASN GLU ALA ALA VAL GLY          
SEQRES   6 B  283  ARG ALA ILE ALA ALA SER GLY ILE PRO ARG ASP GLU ILE          
SEQRES   7 B  283  TYR VAL THR THR LYS LEU ALA THR PRO ASP GLN GLY PHE          
SEQRES   8 B  283  THR SER SER GLN ALA ALA ALA ARG ALA SER LEU GLU ARG          
SEQRES   9 B  283  LEU GLY LEU ASP TYR VAL ASP LEU TYR LEU ILE HIS TRP          
SEQRES  10 B  283  PRO GLY GLY ASP THR SER LYS TYR VAL ASP SER TRP GLY          
SEQRES  11 B  283  GLY LEU MET LYS VAL LYS GLU ASP GLY ILE ALA ARG SER          
SEQRES  12 B  283  ILE GLY VAL CYS ASN PHE GLY ALA GLU ASP LEU GLU THR          
SEQRES  13 B  283  ILE VAL SER LEU THR TYR PHE THR PRO ALA VAL ASN GLN          
SEQRES  14 B  283  ILE GLU LEU HIS PRO LEU LEU ASN GLN ALA ALA LEU ARG          
SEQRES  15 B  283  GLU VAL ASN ALA GLY TYR ASN ILE VAL THR GLU ALA TYR          
SEQRES  16 B  283  GLY PRO LEU GLY VAL GLY ARG LEU LEU ASP HIS PRO ALA          
SEQRES  17 B  283  VAL THR ALA ILE ALA GLU ALA HIS GLY ARG THR ALA ALA          
SEQRES  18 B  283  GLN VAL LEU LEU ARG TRP SER ILE GLN LEU GLY ASN VAL          
SEQRES  19 B  283  VAL ILE SER ARG SER ALA ASN PRO GLU ARG ILE ALA SER          
SEQRES  20 B  283  ASN LEU ASP VAL PHE GLY PHE GLU LEU THR ALA ASP GLU          
SEQRES  21 B  283  MET GLU THR LEU ASN GLY LEU ASP ASP GLY THR ARG PHE          
SEQRES  22 B  283  ARG PRO ASP PRO ALA THR TYR THR GLY SER                      
HET    NA7  A1284      39                                                       
HET    NA7  B1284      39                                                       
HETNAM     NA7 [(2R,3R,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3-                      
HETNAM   2 NA7  HYDROXY-4-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]                   
HETNAM   3 NA7  METHYL [(2R,3S,4S)-3,4-                                         
HETNAM   4 NA7  DIHYDROXYTETRAHYDROFURAN-2-YL]METHYL DIHYDROGEN                 
HETNAM   5 NA7  DIPHOSPHATE                                                     
FORMUL   3  NA7    2(C15 H24 N5 O16 P3)                                         
FORMUL   4  HOH   *523(H2 O)                                                    
HELIX    1   1 SER A   33  GLY A   48  1                                  16    
HELIX    2   2 ALA A   55  GLY A   59  5                                   5    
HELIX    3   3 ASN A   60  SER A   71  1                                  12    
HELIX    4   4 PRO A   74  ILE A   78  5                                   5    
HELIX    5   5 ALA A   85  GLN A   89  5                                   5    
HELIX    6   6 GLY A   90  GLY A  106  1                                  17    
HELIX    7   7 ASP A  121  ASP A  138  1                                  18    
HELIX    8   8 GLY A  150  TYR A  162  1                                  13    
HELIX    9   9 GLN A  178  TYR A  188  1                                  11    
HELIX   10  10 GLY A  201  ASP A  205  5                                   5    
HELIX   11  11 HIS A  206  GLY A  217  1                                  12    
HELIX   12  12 THR A  219  LEU A  231  1                                  13    
HELIX   13  13 ASN A  241  ASP A  250  1                                  10    
HELIX   14  14 THR A  257  GLY A  266  1                                  10    
HELIX   15  15 SER B   33  GLY B   48  1                                  16    
HELIX   16  16 ALA B   55  GLY B   59  5                                   5    
HELIX   17  17 ASN B   60  SER B   71  1                                  12    
HELIX   18  18 PRO B   74  ILE B   78  5                                   5    
HELIX   19  19 ALA B   85  GLN B   89  5                                   5    
HELIX   20  20 GLY B   90  GLY B  106  1                                  17    
HELIX   21  21 ASP B  121  ASP B  138  1                                  18    
HELIX   22  22 GLY B  150  TYR B  162  1                                  13    
HELIX   23  23 GLN B  178  TYR B  188  1                                  11    
HELIX   24  24 LEU B  198  ASP B  205  5                                   8    
HELIX   25  25 HIS B  206  GLY B  217  1                                  12    
HELIX   26  26 THR B  219  LEU B  231  1                                  13    
HELIX   27  27 ASN B  241  ASP B  250  1                                  10    
HELIX   28  28 THR B  257  GLY B  266  1                                  10    
SHEET    1  AA 2 THR A  13  THR A  15  0                                        
SHEET    2  AA 2 THR A  21  PRO A  23 -1  O  LEU A  22   N  VAL A  14           
SHEET    1  AB 9 VAL A  25  GLY A  28  0                                        
SHEET    2  AB 9 VAL A 234  SER A 237  1  O  VAL A 235   N  GLY A  26           
SHEET    3  AB 9 VAL A 191  TYR A 195  1  O  THR A 192   N  VAL A 234           
SHEET    4  AB 9 VAL A 167  GLU A 171  1  O  ASN A 168   N  GLU A 193           
SHEET    5  AB 9 ALA A 141  CYS A 147  1  O  VAL A 146   N  GLN A 169           
SHEET    6  AB 9 VAL A 110  ILE A 115  1  O  VAL A 110   N  ARG A 142           
SHEET    7  AB 9 TYR A  79  LEU A  84  1  O  VAL A  80   N  LEU A 112           
SHEET    8  AB 9 LEU A  51  ASP A  53  1  O  ILE A  52   N  THR A  81           
SHEET    9  AB 9 VAL A  25  GLY A  28  1  O  VAL A  25   N  LEU A  51           
SHEET    1  BA 2 THR B  13  THR B  15  0                                        
SHEET    2  BA 2 THR B  21  PRO B  23 -1  O  LEU B  22   N  VAL B  14           
SHEET    1  BB 9 VAL B  25  GLY B  28  0                                        
SHEET    2  BB 9 VAL B 234  SER B 237  1  O  VAL B 235   N  GLY B  26           
SHEET    3  BB 9 VAL B 191  TYR B 195  1  O  THR B 192   N  VAL B 234           
SHEET    4  BB 9 VAL B 167  GLU B 171  1  O  ASN B 168   N  GLU B 193           
SHEET    5  BB 9 ALA B 141  CYS B 147  1  O  VAL B 146   N  GLN B 169           
SHEET    6  BB 9 VAL B 110  ILE B 115  1  O  VAL B 110   N  ARG B 142           
SHEET    7  BB 9 TYR B  79  LEU B  84  1  O  VAL B  80   N  LEU B 112           
SHEET    8  BB 9 LEU B  51  ASP B  53  1  O  ILE B  52   N  THR B  81           
SHEET    9  BB 9 VAL B  25  GLY B  28  1  O  VAL B  25   N  LEU B  51           
SITE     1 AC1 23 TYR A 195  GLY A 196  PRO A 197  LEU A 198                    
SITE     2 AC1 23 GLY A 199  VAL A 200  GLY A 201  LEU A 204                    
SITE     3 AC1 23 ALA A 221  ILE A 236  ARG A 238  SER A 239                    
SITE     4 AC1 23 ALA A 240  ARG A 244  SER A 247  ASN A 248                    
SITE     5 AC1 23 ARG A 274  HOH A2252  HOH A2253  HOH A2254                    
SITE     6 AC1 23 HOH A2255  HOH A2257  HOH A2258                               
SITE     1 AC2 23 TYR B 195  GLY B 196  PRO B 197  LEU B 198                    
SITE     2 AC2 23 GLY B 199  VAL B 200  GLY B 201  LEU B 204                    
SITE     3 AC2 23 ALA B 221  ILE B 236  ARG B 238  SER B 239                    
SITE     4 AC2 23 ALA B 240  ARG B 244  SER B 247  ASN B 248                    
SITE     5 AC2 23 ARG B 274  HOH B2205  HOH B2260  HOH B2261                    
SITE     6 AC2 23 HOH B2262  HOH B2263  HOH B2264                               
CRYST1   65.456   65.456   96.844  90.00  90.00 120.00 P 32          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      0.015277  0.008820  0.000000        0.00000                         
SCALE2      0.000000  0.017641  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010326        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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