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Database: PDB
Entry: 1DFH
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HEADER    OXIDOREDUCTASE                          16-JAN-97   1DFH              
TITLE     X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD AND
TITLE    2 THIENO-DIAZABORINE                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENOYL ACYL CARRIER PROTEIN REDUCTASE;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ENR;                                                        
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 BL21;                            
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PENVM5                                    
KEYWDS    OXIDOREDUCTASE, LIPID BIOSYNTHESIS, DIAZABORINE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.BALDOCK,J.B.RAFFERTY,D.W.RICE                                       
REVDAT   3   13-JUL-11 1DFH    1       VERSN                                    
REVDAT   2   24-FEB-09 1DFH    1       VERSN                                    
REVDAT   1   28-JAN-98 1DFH    0                                                
JRNL        AUTH   C.BALDOCK,J.B.RAFFERTY,S.E.SEDELNIKOVA,P.J.BAKER,            
JRNL        AUTH 2 A.R.STUITJE,A.R.SLABAS,T.R.HAWKES,D.W.RICE                   
JRNL        TITL   A MECHANISM OF DRUG ACTION REVEALED BY STRUCTURAL STUDIES OF 
JRNL        TITL 2 ENOYL REDUCTASE.                                             
JRNL        REF    SCIENCE                       V. 274  2107 1996              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   8953047                                                      
JRNL        DOI    10.1126/SCIENCE.274.5295.2107                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.BALDOCK,J.B.RAFFERTY,S.E.SEDELNIKOVA,S.BITHELL,            
REMARK   1  AUTH 2 A.R.STUITJE,A.R.SLABAS,D.W.RICE                              
REMARK   1  TITL   CRYSTALLIZATION OF ESCHERICHIA COLI ENOYL REDUCTASE AND ITS  
REMARK   1  TITL 2 COMPLEX WITH DIAZABORINE                                     
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  52  1181 1996              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 30825                          
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.1940                 
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 30825                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3814                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 122                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : 27.000                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.012 ; 2.000 ; 4010            
REMARK   3   BOND ANGLES            (DEGREES) : 1.608 ; 3.000 ; 5411            
REMARK   3   TORSION ANGLES         (DEGREES) : 16.086; 0.000 ; 2363            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : 0.010 ; 4.000 ; 86              
REMARK   3   GENERAL PLANES               (A) : 0.016 ; 9.000 ; 591             
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : 0.365 ; 0.000 ; 26              
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : 0.85                                                 
REMARK   3   BSOL        : 182.90                                               
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : ENGH AND HUBER                                   
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  INITIALLY THE NAD AND THIENO-DIAZABORINE WERE REFINED INDEPENDENTLY 
REMARK   3  AND NOT RESTRAINED BY THE COVALENT BOND BETWEEN THEM. AFTER TWO     
REMARK   3  CYCLES OF REFINEMENT IT WAS CLEAR THAT THEY WERE BOUND COVALENTLY   
REMARK   3  AND THIS RESTRAINT WAS ADDED.                                       
REMARK   3                                                                      
REMARK   3  ASN A 155, ASN A 157, ASN B 155, ASN B 157 ARE THE RESIDUES         
REMARK   3  EITHER SIDE OF THE CATALYTIC TYROSINE AND HAVE DIHEDRAL             
REMARK   3  ANGLES WHICH LIE OUTSIDE THEIR EXPECTED RANGE.  THIS IS             
REMARK   3  THOUGHT TO ALLOW THE TYROSINE SIDE-CHAIN TO OCCUPY THE              
REMARK   3  CORRECT POSITION WITH RESPECT TO THE POSITION OF THE                
REMARK   3  NICOTINAMIDE RING.                                                  
REMARK   4                                                                      
REMARK   4 1DFH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-FEB-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AGROVATA                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31179                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9800                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 56.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.13900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CCP4                                                  
REMARK 200 STARTING MODEL: E. COLI ENR                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 400, PH5.0 100MM ACETATE, 5MM    
REMARK 280  NAD, 5MM 1,2-DIHYDRO-1-HYDROXY-2-(PROP-1-YLSULPHONYL)(5-            
REMARK 280  METHYLTHIENO)[3,2-E][1,2,3]DIAZABORINE                              
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      109.43333            
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      218.86667            
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      164.15000            
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      273.58333            
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       54.71667            
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      109.43333            
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      218.86667            
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      273.58333            
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      164.15000            
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       54.71667            
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: 21670 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 31160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -126.0 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       40.45000            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000       70.06146            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      273.58333            
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     LEU A   259                                                      
REMARK 465     GLU A   260                                                      
REMARK 465     LEU A   261                                                      
REMARK 465     LYS A   262                                                      
REMARK 465     LEU B   259                                                      
REMARK 465     GLU B   260                                                      
REMARK 465     LEU B   261                                                      
REMARK 465     LYS B   262                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 204    CG   CD   NE   CZ   NH1  NH2                        
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   NH2  ARG B   218     OD2  ASP B   224              2.04            
REMARK 500   NH2  ARG A   132     OE2  GLU A   180              2.14            
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    GLY A  13   O   -  C   -  N   ANGL. DEV. = -18.3 DEGREES          
REMARK 500    GLY B  13   O   -  C   -  N   ANGL. DEV. = -17.0 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      119.89   -161.67                                   
REMARK 500    PHE A  94      148.48   -174.31                                   
REMARK 500    LEU A 100       32.65    -98.24                                   
REMARK 500    SER A 121      -54.71   -123.72                                   
REMARK 500    SER A 145     -167.60   -108.62                                   
REMARK 500    ASN A 155      -27.58     68.23                                   
REMARK 500    ASN A 157     -119.38     45.84                                   
REMARK 500    VAL A 247       71.07   -116.22                                   
REMARK 500    ASN A 257       11.60    -67.13                                   
REMARK 500    SER B 145     -167.89   -115.57                                   
REMARK 500    ASN B 155      -26.09     71.81                                   
REMARK 500    ASN B 157     -128.23     39.45                                   
REMARK 500    ALA B 196     -177.02    -54.29                                   
REMARK 500    VAL B 247       76.32   -116.48                                   
REMARK 500    ASP B 248       21.04   -140.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLY A  13        -23.90                                           
REMARK 500    GLY B  13        -22.17                                           
REMARK 500    ASN B 257        -15.38                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PHE B   3        24.9      L          L   OUTSIDE RANGE           
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 NAD A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TDB A 0                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TDB B 0                   
DBREF  1DFH A    2   262  UNP    P29132   FABI_ECOLI       1    261             
DBREF  1DFH B    2   262  UNP    P29132   FABI_ECOLI       1    261             
SEQRES   1 A  261  GLY PHE LEU SER GLY LYS ARG ILE LEU VAL THR GLY VAL          
SEQRES   2 A  261  ALA SER LYS LEU SER ILE ALA TYR GLY ILE ALA GLN ALA          
SEQRES   3 A  261  MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR GLN          
SEQRES   4 A  261  ASN ASP LYS LEU LYS GLY ARG VAL GLU GLU PHE ALA ALA          
SEQRES   5 A  261  GLN LEU GLY SER ASP ILE VAL LEU GLN CYS ASP VAL ALA          
SEQRES   6 A  261  GLU ASP ALA SER ILE ASP THR MET PHE ALA GLU LEU GLY          
SEQRES   7 A  261  LYS VAL TRP PRO LYS PHE ASP GLY PHE VAL HIS SER ILE          
SEQRES   8 A  261  GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY ASP TYR VAL          
SEQRES   9 A  261  ASN ALA VAL THR ARG GLU GLY PHE LYS ILE ALA HIS ASP          
SEQRES  10 A  261  ILE SER SER TYR SER PHE VAL ALA MET ALA LYS ALA CYS          
SEQRES  11 A  261  ARG SER MET LEU ASN PRO GLY SER ALA LEU LEU THR LEU          
SEQRES  12 A  261  SER TYR LEU GLY ALA GLU ARG ALA ILE PRO ASN TYR ASN          
SEQRES  13 A  261  VAL MET GLY LEU ALA LYS ALA SER LEU GLU ALA ASN VAL          
SEQRES  14 A  261  ARG TYR MET ALA ASN ALA MET GLY PRO GLU GLY VAL ARG          
SEQRES  15 A  261  VAL ASN ALA ILE SER ALA GLY PRO ILE ARG THR LEU ALA          
SEQRES  16 A  261  ALA SER GLY ILE LYS ASP PHE ARG LYS MET LEU ALA HIS          
SEQRES  17 A  261  CYS GLU ALA VAL THR PRO ILE ARG ARG THR VAL THR ILE          
SEQRES  18 A  261  GLU ASP VAL GLY ASN SER ALA ALA PHE LEU CYS SER ASP          
SEQRES  19 A  261  LEU SER ALA GLY ILE SER GLY GLU VAL VAL HIS VAL ASP          
SEQRES  20 A  261  GLY GLY PHE SER ILE ALA ALA MET ASN GLU LEU GLU LEU          
SEQRES  21 A  261  LYS                                                          
SEQRES   1 B  261  GLY PHE LEU SER GLY LYS ARG ILE LEU VAL THR GLY VAL          
SEQRES   2 B  261  ALA SER LYS LEU SER ILE ALA TYR GLY ILE ALA GLN ALA          
SEQRES   3 B  261  MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR GLN          
SEQRES   4 B  261  ASN ASP LYS LEU LYS GLY ARG VAL GLU GLU PHE ALA ALA          
SEQRES   5 B  261  GLN LEU GLY SER ASP ILE VAL LEU GLN CYS ASP VAL ALA          
SEQRES   6 B  261  GLU ASP ALA SER ILE ASP THR MET PHE ALA GLU LEU GLY          
SEQRES   7 B  261  LYS VAL TRP PRO LYS PHE ASP GLY PHE VAL HIS SER ILE          
SEQRES   8 B  261  GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY ASP TYR VAL          
SEQRES   9 B  261  ASN ALA VAL THR ARG GLU GLY PHE LYS ILE ALA HIS ASP          
SEQRES  10 B  261  ILE SER SER TYR SER PHE VAL ALA MET ALA LYS ALA CYS          
SEQRES  11 B  261  ARG SER MET LEU ASN PRO GLY SER ALA LEU LEU THR LEU          
SEQRES  12 B  261  SER TYR LEU GLY ALA GLU ARG ALA ILE PRO ASN TYR ASN          
SEQRES  13 B  261  VAL MET GLY LEU ALA LYS ALA SER LEU GLU ALA ASN VAL          
SEQRES  14 B  261  ARG TYR MET ALA ASN ALA MET GLY PRO GLU GLY VAL ARG          
SEQRES  15 B  261  VAL ASN ALA ILE SER ALA GLY PRO ILE ARG THR LEU ALA          
SEQRES  16 B  261  ALA SER GLY ILE LYS ASP PHE ARG LYS MET LEU ALA HIS          
SEQRES  17 B  261  CYS GLU ALA VAL THR PRO ILE ARG ARG THR VAL THR ILE          
SEQRES  18 B  261  GLU ASP VAL GLY ASN SER ALA ALA PHE LEU CYS SER ASP          
SEQRES  19 B  261  LEU SER ALA GLY ILE SER GLY GLU VAL VAL HIS VAL ASP          
SEQRES  20 B  261  GLY GLY PHE SER ILE ALA ALA MET ASN GLU LEU GLU LEU          
SEQRES  21 B  261  LYS                                                          
HET    NAD  A 501      44                                                       
HET    TDB  A   0      17                                                       
HET    NAD  B 501      44                                                       
HET    TDB  B   0      17                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     TDB 6-METHYL-2(PROPANE-1-SULFONYL)-2H-THIENO[3,2-D][1,2,             
HETNAM   2 TDB  3]DIAZABORININ-1-OL                                             
FORMUL   3  NAD    2(C21 H27 N7 O14 P2)                                         
FORMUL   4  TDB    2(C9 H13 B N2 O3 S2)                                         
HELIX    1   1 ILE A   20  ARG A   30  1                                  11    
HELIX    2   2 ASP A   42  LEU A   55  1                                  14    
HELIX    3   3 ASP A   68  LYS A   80  1                                  13    
HELIX    4   4 GLY A   97  LEU A  100  5                                   4    
HELIX    5   5 TYR A  104  ALA A  107  1                                   4    
HELIX    6   6 ARG A  110  SER A  120  1                                  11    
HELIX    7   7 TYR A  122  MET A  134  1                                  13    
HELIX    8   8 LEU A  147  ALA A  149  5                                   3    
HELIX    9   9 ASN A  157  GLU A  180  5                                  24    
HELIX   10  10 PHE A  203  VAL A  213  1                                  11    
HELIX   11  11 ILE A  222  CYS A  233  1                                  12    
HELIX   12  12 ASP A  235  SER A  237  5                                   3    
HELIX   13  13 PHE A  251  ILE A  253  5                                   3    
HELIX   14  14 ILE B   20  ARG B   30  1                                  11    
HELIX   15  15 ASP B   42  GLN B   54  1                                  13    
HELIX   16  16 ASP B   68  VAL B   81  1                                  14    
HELIX   17  17 GLY B   97  LEU B  100  5                                   4    
HELIX   18  18 TYR B  104  ALA B  107  1                                   4    
HELIX   19  19 ARG B  110  SER B  120  1                                  11    
HELIX   20  20 TYR B  122  MET B  134  1                                  13    
HELIX   21  21 LEU B  147  ALA B  149  5                                   3    
HELIX   22  22 ASN B  157  GLU B  180  5                                  24    
HELIX   23  23 PHE B  203  VAL B  213  1                                  11    
HELIX   24  24 ILE B  222  LEU B  232  1                                  11    
HELIX   25  25 ASP B  235  SER B  237  5                                   3    
HELIX   26  26 PHE B  251  ILE B  253  5                                   3    
SHEET    1   A 3 ARG A   8  VAL A  11  0                                        
SHEET    2   A 3 GLU A  34  TYR A  39  1  N  GLU A  34   O  ILE A   9           
SHEET    3   A 3 VAL A  60  GLN A  62  1  N  LEU A  61   O  PHE A  37           
SHEET    1   B 4 GLY A  87  HIS A  90  0                                        
SHEET    2   B 4 SER A 139  SER A 145  1  N  ALA A 140   O  PHE A  88           
SHEET    3   B 4 VAL A 182  ALA A 189  1  N  ARG A 183   O  SER A 139           
SHEET    4   B 4 VAL A 244  VAL A 247  1  N  VAL A 245   O  ALA A 186           
SHEET    1   C 3 ARG B   8  VAL B  11  0                                        
SHEET    2   C 3 GLU B  34  TYR B  39  1  N  GLU B  34   O  ILE B   9           
SHEET    3   C 3 VAL B  60  GLN B  62  1  N  LEU B  61   O  PHE B  37           
SHEET    1   D 4 GLY B  87  HIS B  90  0                                        
SHEET    2   D 4 SER B 139  SER B 145  1  N  ALA B 140   O  PHE B  88           
SHEET    3   D 4 VAL B 182  ALA B 189  1  N  ARG B 183   O  SER B 139           
SHEET    4   D 4 VAL B 244  VAL B 247  1  N  VAL B 245   O  ALA B 186           
LINK         O2D NAD A 501                 B1  TDB A   0     1555   1555  1.53  
LINK         O2D NAD B 501                 B1  TDB B   0     1555   1555  1.50  
SITE     1 AC1 19 TDB A   0  GLY A  13  ALA A  15  SER A  19                    
SITE     2 AC1 19 ILE A  20  GLN A  40  CYS A  63  ASP A  64                    
SITE     3 AC1 19 VAL A  65  SER A  91  ILE A  92  GLY A  93                    
SITE     4 AC1 19 LEU A 144  SER A 145  LYS A 163  ALA A 189                    
SITE     5 AC1 19 GLY A 190  PRO A 191  ILE A 192                               
SITE     1 AC2  5 GLY A  93  TYR A 156  MET A 159  LYS A 163                    
SITE     2 AC2  5 NAD A 501                                                     
SITE     1 AC3 20 TDB B   0  GLY B  13  ALA B  15  SER B  19                    
SITE     2 AC3 20 ILE B  20  GLN B  40  LEU B  44  CYS B  63                    
SITE     3 AC3 20 ASP B  64  VAL B  65  SER B  91  ILE B  92                    
SITE     4 AC3 20 GLY B  93  LEU B 144  SER B 145  LYS B 163                    
SITE     5 AC3 20 ALA B 189  GLY B 190  PRO B 191  ILE B 192                    
SITE     1 AC4  5 GLY B  93  TYR B 156  MET B 159  LYS B 163                    
SITE     2 AC4  5 NAD B 501                                                     
CRYST1   80.900   80.900  328.300  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      0.012361  0.007137  0.000000        0.00000                         
SCALE2      0.000000  0.014273  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003046        0.00000                         
MTRIX1   1 -0.650000  0.605000 -0.459000       42.52000    1                    
MTRIX2   1  0.606000  0.049000 -0.794000      148.48000    1                    
MTRIX3   1 -0.458000 -0.794000 -0.399000      228.46001    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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