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Database: PDB
Entry: 1LX6
LinkDB: 1LX6
Original site: 1LX6 
HEADER    OXIDOREDUCTASE                          04-JUN-02   1LX6              
TITLE     CRYSTAL STRUCTURE OF E. COLI ENOYL REDUCTASE-NAD+ WITH A BOUND        
TITLE    2 BENZAMIDE INHIBITOR                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH];             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: NADH-DEPENDENT ENOYL-ACP REDUCTASE;                         
COMPND   5 EC: 1.3.1.9;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    FABI, ENOYL REDUCTASE, OXIDOREDUCTASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.W.SMITH,X.QIU,C.A.JANSON                                            
REVDAT   4   13-JUL-11 1LX6    1       VERSN                                    
REVDAT   3   24-FEB-09 1LX6    1       VERSN                                    
REVDAT   2   01-APR-03 1LX6    1       JRNL                                     
REVDAT   1   04-SEP-02 1LX6    0                                                
JRNL        AUTH   W.H.MILLER,M.A.SEEFELD,K.A.NEWLANDER,I.N.UZINSKAS,           
JRNL        AUTH 2 W.J.BURGESS,D.A.HEERDING,C.C.YUAN,M.S.HEAD,D.J.PAYNE,        
JRNL        AUTH 3 S.F.RITTENHOUSE,T.D.MOORE,S.C.PEARSON,V.BERRY,               
JRNL        AUTH 4 W.E.DEWOLF JR.,P.M.KELLER,B.J.POLIZZI,X.QIU,C.A.JANSON,      
JRNL        AUTH 5 W.F.HUFFMAN                                                  
JRNL        TITL   DISCOVERY OF AMINOPYRIDINE-BASED INHIBITORS OF BACTERIAL     
JRNL        TITL 2 ENOYL-ACP REDUCTASE (FABI).                                  
JRNL        REF    J.MED.CHEM.                   V.  45  3246 2002              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   12109908                                                     
JRNL        DOI    10.1021/JM020050+                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 590722.010                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 20345                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 981                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.012                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.50                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1442                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2500                       
REMARK   3   BIN FREE R VALUE                    : 0.3400                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 72                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.120                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3598                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 144                                     
REMARK   3   SOLVENT ATOMS            : 247                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.00                          
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.46                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.44                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.41                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.41                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.94                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.45                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : OVERALL                                   
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1LX6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB016370.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-FEB-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRANDEIS                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20345                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.58                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.19800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: PDB 1C14                                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 2M(NH4)2SO4,5% PEG400, PH    
REMARK 280  7.50, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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      109.02667            
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      218.05333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      163.54000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      272.56667            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       54.51333            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      109.02667            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      218.05333            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      272.56667            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      163.54000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       54.51333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 21840 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 28380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -150.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.500000 -0.866025  0.000000       39.72000            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000       68.79706            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      272.56667            
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     ARG A   193                                                      
REMARK 465     THR A   194                                                      
REMARK 465     LEU A   195                                                      
REMARK 465     ALA A   196                                                      
REMARK 465     ALA A   197                                                      
REMARK 465     SER A   198                                                      
REMARK 465     GLY A   199                                                      
REMARK 465     ILE A   200                                                      
REMARK 465     LYS A   201                                                      
REMARK 465     ASP A   202                                                      
REMARK 465     PHE A   203                                                      
REMARK 465     ARG A   204                                                      
REMARK 465     LYS A   205                                                      
REMARK 465     GLU A   258                                                      
REMARK 465     LEU A   259                                                      
REMARK 465     GLU A   260                                                      
REMARK 465     LEU A   261                                                      
REMARK 465     LYS A   262                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B   193                                                      
REMARK 465     THR B   194                                                      
REMARK 465     LEU B   195                                                      
REMARK 465     ALA B   196                                                      
REMARK 465     ALA B   197                                                      
REMARK 465     SER B   198                                                      
REMARK 465     GLY B   199                                                      
REMARK 465     ILE B   200                                                      
REMARK 465     LYS B   201                                                      
REMARK 465     ASP B   202                                                      
REMARK 465     PHE B   203                                                      
REMARK 465     ARG B   204                                                      
REMARK 465     LYS B   205                                                      
REMARK 465     GLU B   258                                                      
REMARK 465     LEU B   259                                                      
REMARK 465     GLU B   260                                                      
REMARK 465     LEU B   261                                                      
REMARK 465     LYS B   262                                                      
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    CYS A  63      116.97   -161.63                                   
REMARK 500    ASN A 155      -23.30     69.63                                   
REMARK 500    ASN A 157     -126.40     33.84                                   
REMARK 500    VAL A 247       74.51   -113.82                                   
REMARK 500    ASP B  58       27.34   -140.83                                   
REMARK 500    CYS B  63      114.79   -163.15                                   
REMARK 500    SER B  91       60.68   -118.99                                   
REMARK 500    LEU B 100       43.13    -86.50                                   
REMARK 500    ASN B 155      -23.26     75.30                                   
REMARK 500    ASN B 157     -122.15     32.30                                   
REMARK 500    VAL B 247       70.38   -113.53                                   
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 A 519        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH A 575        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH A 583        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH A 586        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH A 587        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH A 609        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH A 611        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH A 622        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH B 599        DISTANCE =  5.35 ANGSTROMS                       
REMARK 525    HOH B 607        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH B 624        DISTANCE =  6.86 ANGSTROMS                       
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C SSEQI                                                      
REMARK 615     HOH B  594                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZAM A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZAM B 504                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1C14   RELATED DB: PDB                                   
REMARK 900 1C14 IS THE CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-             
REMARK 900 NAD+-TRICLOSAN COMPLEX                                               
REMARK 900 RELATED ID: 1I2Z   RELATED DB: PDB                                   
REMARK 900 1I2Z IS E. COLI ENOYL REDUCTASE IN COMPLEX WITH NAD AND BRL          
REMARK 900 -12654                                                               
REMARK 900 RELATED ID: 1I30   RELATED DB: PDB                                   
REMARK 900 1I30 IS E. COLI ENOYL REDUCTASE +NAD+SB385826                        
REMARK 900 RELATED ID: 1QG6   RELATED DB: PDB                                   
REMARK 900 1QG6 IS THE CRYSTAL STRUCTURE OF E. COLI ENOYL ACYL CARRIER          
REMARK 900 PROTEIN REDUCTASE IN COMPLEX WITH NAD AND TRICLOSAN                  
REMARK 900 RELATED ID: 1LXC   RELATED DB: PDB                                   
REMARK 900 1LXC IS THE CRYSTAL STRUCTURE OF E. COLI ENOYL REDUCTASE-            
REMARK 900 NAD+ WITH A BOUND ACRYLAMIDE INHIBITOR                               
DBREF  1LX6 A    1   262  UNP    P29132   FABI_ECOLI       0    261             
DBREF  1LX6 B    1   262  UNP    P29132   FABI_ECOLI       0    261             
SEQRES   1 A  262  MET GLY PHE LEU SER GLY LYS ARG ILE LEU VAL THR GLY          
SEQRES   2 A  262  VAL ALA SER LYS LEU SER ILE ALA TYR GLY ILE ALA GLN          
SEQRES   3 A  262  ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR          
SEQRES   4 A  262  GLN ASN ASP LYS LEU LYS GLY ARG VAL GLU GLU PHE ALA          
SEQRES   5 A  262  ALA GLN LEU GLY SER ASP ILE VAL LEU GLN CYS ASP VAL          
SEQRES   6 A  262  ALA GLU ASP ALA SER ILE ASP THR MET PHE ALA GLU LEU          
SEQRES   7 A  262  GLY LYS VAL TRP PRO LYS PHE ASP GLY PHE VAL HIS SER          
SEQRES   8 A  262  ILE GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY ASP TYR          
SEQRES   9 A  262  VAL ASN ALA VAL THR ARG GLU GLY PHE LYS ILE ALA HIS          
SEQRES  10 A  262  ASP ILE SER SER TYR SER PHE VAL ALA MET ALA LYS ALA          
SEQRES  11 A  262  CYS ARG SER MET LEU ASN PRO GLY SER ALA LEU LEU THR          
SEQRES  12 A  262  LEU SER TYR LEU GLY ALA GLU ARG ALA ILE PRO ASN TYR          
SEQRES  13 A  262  ASN VAL MET GLY LEU ALA LYS ALA SER LEU GLU ALA ASN          
SEQRES  14 A  262  VAL ARG TYR MET ALA ASN ALA MET GLY PRO GLU GLY VAL          
SEQRES  15 A  262  ARG VAL ASN ALA ILE SER ALA GLY PRO ILE ARG THR LEU          
SEQRES  16 A  262  ALA ALA SER GLY ILE LYS ASP PHE ARG LYS MET LEU ALA          
SEQRES  17 A  262  HIS CYS GLU ALA VAL THR PRO ILE ARG ARG THR VAL THR          
SEQRES  18 A  262  ILE GLU ASP VAL GLY ASN SER ALA ALA PHE LEU CYS SER          
SEQRES  19 A  262  ASP LEU SER ALA GLY ILE SER GLY GLU VAL VAL HIS VAL          
SEQRES  20 A  262  ASP GLY GLY PHE SER ILE ALA ALA MET ASN GLU LEU GLU          
SEQRES  21 A  262  LEU LYS                                                      
SEQRES   1 B  262  MET GLY PHE LEU SER GLY LYS ARG ILE LEU VAL THR GLY          
SEQRES   2 B  262  VAL ALA SER LYS LEU SER ILE ALA TYR GLY ILE ALA GLN          
SEQRES   3 B  262  ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR          
SEQRES   4 B  262  GLN ASN ASP LYS LEU LYS GLY ARG VAL GLU GLU PHE ALA          
SEQRES   5 B  262  ALA GLN LEU GLY SER ASP ILE VAL LEU GLN CYS ASP VAL          
SEQRES   6 B  262  ALA GLU ASP ALA SER ILE ASP THR MET PHE ALA GLU LEU          
SEQRES   7 B  262  GLY LYS VAL TRP PRO LYS PHE ASP GLY PHE VAL HIS SER          
SEQRES   8 B  262  ILE GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY ASP TYR          
SEQRES   9 B  262  VAL ASN ALA VAL THR ARG GLU GLY PHE LYS ILE ALA HIS          
SEQRES  10 B  262  ASP ILE SER SER TYR SER PHE VAL ALA MET ALA LYS ALA          
SEQRES  11 B  262  CYS ARG SER MET LEU ASN PRO GLY SER ALA LEU LEU THR          
SEQRES  12 B  262  LEU SER TYR LEU GLY ALA GLU ARG ALA ILE PRO ASN TYR          
SEQRES  13 B  262  ASN VAL MET GLY LEU ALA LYS ALA SER LEU GLU ALA ASN          
SEQRES  14 B  262  VAL ARG TYR MET ALA ASN ALA MET GLY PRO GLU GLY VAL          
SEQRES  15 B  262  ARG VAL ASN ALA ILE SER ALA GLY PRO ILE ARG THR LEU          
SEQRES  16 B  262  ALA ALA SER GLY ILE LYS ASP PHE ARG LYS MET LEU ALA          
SEQRES  17 B  262  HIS CYS GLU ALA VAL THR PRO ILE ARG ARG THR VAL THR          
SEQRES  18 B  262  ILE GLU ASP VAL GLY ASN SER ALA ALA PHE LEU CYS SER          
SEQRES  19 B  262  ASP LEU SER ALA GLY ILE SER GLY GLU VAL VAL HIS VAL          
SEQRES  20 B  262  ASP GLY GLY PHE SER ILE ALA ALA MET ASN GLU LEU GLU          
SEQRES  21 B  262  LEU LYS                                                      
HET    NAD  A 501      44                                                       
HET    ZAM  A 502      28                                                       
HET    NAD  B 503      44                                                       
HET    ZAM  B 504      28                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     ZAM 3-[(ACETYL-METHYL-AMINO)-METHYL]-4-AMINO-N-METHYL-N-(1-          
HETNAM   2 ZAM  METHYL-1H-INDOL-2-YLMETHYL)-BENZAMIDE                           
FORMUL   3  NAD    2(C21 H27 N7 O14 P2)                                         
FORMUL   4  ZAM    2(C22 H26 N4 O2)                                             
FORMUL   7  HOH   *247(H2 O)                                                    
HELIX    1   1 SER A   19  GLU A   31  1                                  13    
HELIX    2   2 ASN A   41  LYS A   43  5                                   3    
HELIX    3   3 LEU A   44  LEU A   55  1                                  12    
HELIX    4   4 GLU A   67  TRP A   82  1                                  16    
HELIX    5   5 PRO A   96  ASP A  101  5                                   6    
HELIX    6   6 ASP A  103  VAL A  108  1                                   6    
HELIX    7   7 THR A  109  SER A  121  1                                  13    
HELIX    8   8 SER A  121  ARG A  132  1                                  12    
HELIX    9   9 TYR A  146  GLU A  150  5                                   5    
HELIX   10  10 VAL A  158  GLY A  178  1                                  21    
HELIX   11  11 MET A  206  THR A  214  1                                   9    
HELIX   12  12 THR A  221  CYS A  233  1                                  13    
HELIX   13  13 SER A  234  ALA A  238  5                                   5    
HELIX   14  14 SER B   19  GLU B   31  1                                  13    
HELIX   15  15 ASN B   41  LEU B   55  1                                  15    
HELIX   16  16 GLU B   67  LYS B   80  1                                  14    
HELIX   17  17 PRO B   96  ASP B  101  5                                   6    
HELIX   18  18 ASP B  103  VAL B  108  1                                   6    
HELIX   19  19 THR B  109  SER B  121  1                                  13    
HELIX   20  20 SER B  121  ARG B  132  1                                  12    
HELIX   21  21 SER B  133  LEU B  135  5                                   3    
HELIX   22  22 TYR B  146  GLU B  150  5                                   5    
HELIX   23  23 ASN B  157  GLY B  178  1                                  22    
HELIX   24  24 MET B  206  THR B  214  1                                   9    
HELIX   25  25 THR B  221  CYS B  233  1                                  13    
HELIX   26  26 SER B  234  ALA B  238  5                                   5    
HELIX   27  27 GLY B  250  ALA B  254  5                                   5    
SHEET    1   A 7 VAL A  60  GLN A  62  0                                        
SHEET    2   A 7 GLU A  34  TYR A  39  1  N  PHE A  37   O  LEU A  61           
SHEET    3   A 7 ARG A   8  VAL A  11  1  N  VAL A  11   O  ALA A  36           
SHEET    4   A 7 PHE A  88  HIS A  90  1  O  VAL A  89   N  LEU A  10           
SHEET    5   A 7 SER A 139  SER A 145  1  O  LEU A 142   N  HIS A  90           
SHEET    6   A 7 VAL A 182  ALA A 189  1  O  ILE A 187   N  SER A 145           
SHEET    7   A 7 VAL A 244  VAL A 247  1  O  VAL A 247   N  SER A 188           
SHEET    1   B 7 VAL B  60  GLN B  62  0                                        
SHEET    2   B 7 GLU B  34  TYR B  39  1  N  PHE B  37   O  LEU B  61           
SHEET    3   B 7 ARG B   8  VAL B  11  1  N  VAL B  11   O  ALA B  36           
SHEET    4   B 7 PHE B  88  HIS B  90  1  O  VAL B  89   N  LEU B  10           
SHEET    5   B 7 SER B 139  SER B 145  1  O  LEU B 142   N  HIS B  90           
SHEET    6   B 7 VAL B 182  ALA B 189  1  O  ILE B 187   N  SER B 145           
SHEET    7   B 7 VAL B 244  VAL B 247  1  O  VAL B 245   N  SER B 188           
SITE     1 AC1 21 GLY A  13  SER A  19  ILE A  20  GLN A  40                    
SITE     2 AC1 21 CYS A  63  ASP A  64  VAL A  65  SER A  91                    
SITE     3 AC1 21 ILE A  92  GLY A  93  ILE A 119  LEU A 144                    
SITE     4 AC1 21 SER A 145  LYS A 163  ALA A 189  GLY A 190                    
SITE     5 AC1 21 PRO A 191  ILE A 192  ZAM A 502  HOH A 534                    
SITE     6 AC1 21 HOH A 546                                                     
SITE     1 AC2  6 GLY A  93  PHE A  94  TYR A 146  ASN A 155                    
SITE     2 AC2  6 TYR A 156  NAD A 501                                          
SITE     1 AC3 22 GLY B  13  ALA B  15  SER B  19  ILE B  20                    
SITE     2 AC3 22 GLN B  40  CYS B  63  ASP B  64  VAL B  65                    
SITE     3 AC3 22 SER B  91  ILE B  92  ILE B 119  SER B 145                    
SITE     4 AC3 22 LYS B 163  ALA B 189  GLY B 190  PRO B 191                    
SITE     5 AC3 22 ILE B 192  ZAM B 504  HOH B 512  HOH B 520                    
SITE     6 AC3 22 HOH B 522  HOH B 579                                          
SITE     1 AC4  9 GLY B  93  PHE B  94  ALA B  95  TYR B 146                    
SITE     2 AC4  9 ASN B 155  TYR B 156  MET B 206  NAD B 503                    
SITE     3 AC4  9 HOH B 520                                                     
CRYST1   79.440   79.440  327.080  90.00  90.00 120.00 P 61 2 2     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      0.012590  0.007270  0.000000        0.00000                         
SCALE2      0.000000  0.014540  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003060        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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