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Database: PDB
Entry: 1MFP
LinkDB: 1MFP
Original site: 1MFP 
HEADER    OXIDOREDUCTASE                          13-AUG-02   1MFP              
TITLE     E. COLI ENOYL REDUCTASE IN COMPLEX WITH NAD AND SB611113              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH];             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ENOYL REDUCTASE, 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, ENOYL-ACP REDUCTASE, OXIDOREDUCTASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.SEEFELD,W.H.MILLER,K.A.NEWLANDER,W.J.BURGESS,W.E.DEWOLF JR.,      
AUTHOR   2 P.A.ELKINS,M.S.HEAD,D.R.JAKAS,C.A.JANSON,P.M.KELLER,P.J.MANLEY,      
AUTHOR   3 T.D.MOORE,D.J.PAYNE,S.PEARSON,B.J.POLIZZI,X.QIU,S.F.RITTENHOUSE,     
AUTHOR   4 I.N.UZINSKAS,N.G.WALLIS,W.F.HUFFMAN                                  
REVDAT   3   13-JUL-11 1MFP    1       VERSN                                    
REVDAT   2   24-FEB-09 1MFP    1       VERSN                                    
REVDAT   1   06-MAY-03 1MFP    0                                                
JRNL        AUTH   M.A.SEEFELD,W.H.MILLER,K.A.NEWLANDER,W.J.BURGESS,            
JRNL        AUTH 2 W.E.DEWOLF JR.,P.A.ELKINS,M.S.HEAD,D.R.JAKAS,C.A.JANSON,     
JRNL        AUTH 3 P.M.KELLER,P.J.MANLEY,T.D.MOORE,D.J.PAYNE,S.PEARSON,         
JRNL        AUTH 4 B.J.POLIZZI,X.QIU,S.F.RITTENHOUSE,I.N.UZINSKAS,N.G.WALLIS,   
JRNL        AUTH 5 W.F.HUFFMAN                                                  
JRNL        TITL   INDOLE NAPHTHYRIDINONES AS INHIBITORS OF BACTERIAL ENOYL-ACP 
JRNL        TITL 2 REDUCTASES FABI AND FABK                                     
JRNL        REF    J.MED.CHEM.                   V.  46  1627 2003              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   12699381                                                     
JRNL        DOI    10.1021/JM0204035                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.33 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.33                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 18869                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 923                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.33                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2370                       
REMARK   3   BIN FREE R VALUE                    : 0.4290                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 48                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3836                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 149                                     
REMARK   3   SOLVENT ATOMS            : 195                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 37.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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 1MFP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-AUG-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB016876.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19201                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.330                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 69.6                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.04400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.33                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 28.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.07700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NAD+, HEPES, AMMONIUM SULFATE, PEG       
REMARK 280  400, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294.0K      
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      108.49333            
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      216.98667            
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      162.74000            
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      271.23333            
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       54.24667            
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      108.49333            
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      216.98667            
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      271.23333            
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      162.74000            
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       54.24667            
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: 23780 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 29830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -164.0 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       39.80000            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000       68.93562            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      271.23333            
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     GLU A   260                                                      
REMARK 465     LEU A   261                                                      
REMARK 465     LYS A   262                                                      
REMARK 465     MET B  1001                                                      
REMARK 465     GLU B  1260                                                      
REMARK 465     LEU B  1261                                                      
REMARK 465     LYS B  1262                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A   180     O    HOH A   382              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 144   CA  -  CB  -  CG  ANGL. DEV. = -14.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS A  63      112.35   -162.70                                   
REMARK 500    LEU A 100       49.16    -99.30                                   
REMARK 500    ASN A 155      -25.32     74.82                                   
REMARK 500    ASN A 157     -122.25     39.14                                   
REMARK 500    LYS A 201     -144.18   -177.23                                   
REMARK 500    VAL A 247       72.63   -113.76                                   
REMARK 500    LEU B1100       52.58   -110.76                                   
REMARK 500    SER B1121      -55.84   -121.71                                   
REMARK 500    ASN B1155      -25.79     79.39                                   
REMARK 500    ASN B1157     -116.21     31.46                                   
REMARK 500    ARG B1193       99.62    -68.41                                   
REMARK 500    ALA B1196       -0.42    -48.67                                   
REMARK 500    SER B1198      -18.02    -41.90                                   
REMARK 500    LYS B1201     -154.28     46.43                                   
REMARK 500    ASP B1202       43.73    -93.52                                   
REMARK 500    VAL B1247       71.92   -113.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR B1022         0.07    SIDE CHAIN                              
REMARK 500    TYR B1122         0.09    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1303                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 1301                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IDN A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IDN B 1302                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1C14   RELATED DB: PDB                                   
REMARK 900 1C14 IS THE SAME PROTEIN COMPLEXED WITH TRICLOSAN.                   
REMARK 900 RELATED ID: 1I2Z   RELATED DB: PDB                                   
REMARK 900 1I2Z IS THE SAME PROTEIN COMPLEXED WITH BRL-12654.                   
REMARK 900 RELATED ID: 1I30   RELATED DB: PDB                                   
REMARK 900 1I30 IS THE SAME PROTEIN COMPLEXED WITH SB385826.                    
DBREF  1MFP A    1   262  UNP    P29132   FABI_ECOLI       0    261             
DBREF  1MFP B 1001  1262  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    SO4  B1303       5                                                       
HET    NAD  A 301      44                                                       
HET    NAD  B1301      44                                                       
HET    IDN  A 302      28                                                       
HET    IDN  B1302      28                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     IDN (E)-N-METHYL-N-(1-METHYL-1H-INDOL-3-YLMETHYL)-3-(7-OXO-          
HETNAM   2 IDN  5,6,7,8-TETRAHYDRO-[1,8]NAPHTHYRIDIN-3-YL)-ACRYLAMIDE           
HETSYN     IDN INDOLE NAPHTHYRIDINONE                                           
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  NAD    2(C21 H27 N7 O14 P2)                                         
FORMUL   6  IDN    2(C22 H22 N4 O2)                                             
FORMUL   8  HOH   *195(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  GLN A   54  1                                  11    
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 SER A  133  LEU A  135  5                                   3    
HELIX   10  10 TYR A  146  GLU A  150  5                                   5    
HELIX   11  11 ASN A  157  GLY A  178  1                                  22    
HELIX   12  12 PRO A  179  GLY A  181  5                                   3    
HELIX   13  13 THR A  194  SER A  198  5                                   5    
HELIX   14  14 ASP A  202  THR A  214  1                                  13    
HELIX   15  15 THR A  221  CYS A  233  1                                  13    
HELIX   16  16 SER A  234  ALA A  238  5                                   5    
HELIX   17  17 GLY A  250  ALA A  254  5                                   5    
HELIX   18  18 SER B 1019  GLU B 1031  1                                  13    
HELIX   19  19 ASN B 1041  LEU B 1055  1                                  15    
HELIX   20  20 GLU B 1067  TRP B 1082  1                                  16    
HELIX   21  21 PRO B 1096  ASP B 1101  5                                   6    
HELIX   22  22 ASP B 1103  VAL B 1108  1                                   6    
HELIX   23  23 THR B 1109  SER B 1121  1                                  13    
HELIX   24  24 SER B 1121  ARG B 1132  1                                  12    
HELIX   25  25 SER B 1133  LEU B 1135  5                                   3    
HELIX   26  26 TYR B 1146  GLU B 1150  5                                   5    
HELIX   27  27 TYR B 1156  GLY B 1178  1                                  23    
HELIX   28  28 THR B 1194  GLY B 1199  1                                   6    
HELIX   29  29 ASP B 1202  THR B 1214  1                                  13    
HELIX   30  30 THR B 1221  CYS B 1233  1                                  13    
HELIX   31  31 SER B 1234  ALA B 1238  5                                   5    
HELIX   32  32 GLY B 1250  ALA B 1254  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 ALA A 140  SER A 145  1  O  LEU A 142   N  HIS A  90           
SHEET    6   A 7 ARG A 183  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 245   N  ALA A 186           
SHEET    1   B 7 VAL B1060  GLN B1062  0                                        
SHEET    2   B 7 GLU B1034  TYR B1039  1  N  PHE B1037   O  LEU B1061           
SHEET    3   B 7 ARG B1008  VAL B1011  1  N  VAL B1011   O  ALA B1036           
SHEET    4   B 7 PHE B1088  HIS B1090  1  O  VAL B1089   N  LEU B1010           
SHEET    5   B 7 SER B1139  SER B1145  1  O  LEU B1142   N  HIS B1090           
SHEET    6   B 7 VAL B1182  ALA B1189  1  O  ILE B1187   N  SER B1145           
SHEET    7   B 7 VAL B1244  VAL B1247  1  O  VAL B1245   N  SER B1188           
SITE     1 AC1  7 HOH B  27  HOH B  84  HOH B 168  LYS B1045                    
SITE     2 AC1  7 ASP B1101  GLY B1102  ASP B1103                               
SITE     1 AC2 23 GLY A  13  ALA A  15  SER A  19  ILE A  20                    
SITE     2 AC2 23 GLN A  40  CYS A  63  ASP A  64  VAL A  65                    
SITE     3 AC2 23 SER A  91  ILE A  92  GLY A  93  LEU A 144                    
SITE     4 AC2 23 SER A 145  LYS A 163  ALA A 189  GLY A 190                    
SITE     5 AC2 23 ILE A 192  THR A 194  ALA A 196  IDN A 302                    
SITE     6 AC2 23 HOH A 309  HOH A 368  HOH A 385                               
SITE     1 AC3 27 HOH B   2  HOH B  10  HOH B  35  HOH B 181                    
SITE     2 AC3 27 GLY B1013  ALA B1015  SER B1019  ILE B1020                    
SITE     3 AC3 27 GLN B1040  LEU B1044  CYS B1063  ASP B1064                    
SITE     4 AC3 27 VAL B1065  SER B1091  ILE B1092  GLY B1093                    
SITE     5 AC3 27 LEU B1144  SER B1145  TYR B1146  LYS B1163                    
SITE     6 AC3 27 ALA B1189  GLY B1190  PRO B1191  ILE B1192                    
SITE     7 AC3 27 THR B1194  ALA B1196  IDN B1302                               
SITE     1 AC4 10 PHE A  94  ALA A  95  TYR A 146  TYR A 156                    
SITE     2 AC4 10 MET A 159  ALA A 196  ILE A 200  LYS A 201                    
SITE     3 AC4 10 MET A 206  NAD A 301                                          
SITE     1 AC5 10 PHE B1094  ALA B1095  TYR B1146  TYR B1156                    
SITE     2 AC5 10 MET B1159  ALA B1196  ILE B1200  LYS B1201                    
SITE     3 AC5 10 MET B1206  NAD B1301                                          
CRYST1   79.600   79.600  325.480  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      0.012563  0.007253  0.000000        0.00000                         
SCALE2      0.000000  0.014506  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003072        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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