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Database: PDB
Entry: 1DFI
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HEADER    OXIDOREDUCTASE                          16-JAN-97   1DFI              
TITLE     X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH              
TITLE    2 BOUND NAD                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENOYL ACYL CARRIER PROTEIN REDUCTASE;                      
COMPND   3 CHAIN: A, B, C, D;                                                   
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                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.BALDOCK,J.B.RAFFERTY,D.W.RICE                                       
REVDAT   2   24-FEB-09 1DFI    1       VERSN                                    
REVDAT   1   28-JAN-98 1DFI    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            
JRNL        TITL 2 STUDIES OF 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                    
REMARK   1  TITL 2 REDUCTASE AND ITS 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.    2.09 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) : 2.09                           
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             : 52346                          
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) : 0.162                           
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) : 0.1620                 
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) : 52346                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7336                                    
REMARK   3   NUCLEIC ACID ATOMS       : NULL                                    
REMARK   3   HETEROGEN ATOMS          : NULL                                    
REMARK   3   SOLVENT ATOMS            : NULL                                    
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : 33.000                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.013 ; 2.000 ; 7648            
REMARK   3   BOND ANGLES            (DEGREES) : 1.503 ; 3.000 ; 10336           
REMARK   3   TORSION ANGLES         (DEGREES) : 16.461; 0.000 ; 4504            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : 0.012 ; 4.000 ; 168             
REMARK   3   GENERAL PLANES               (A) : 0.018 ; 9.000 ; 1128            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : 0.188 ; 0.000 ; 77              
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        : 275.10                                               
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:  ASN A 155, ASN A 157, ASN B 155,         
REMARK   3  ASN B 157 ARE THE RESIDUES EITHER SIDE OF THE CATALYTIC             
REMARK   3  TYROSINE AND HAVE DIHEDRAL ANGLES WHICH LIE OUTSIDE THEIR           
REMARK   3  EXPECTED RANGE. THIS IS THOUGHT TO ALLOW THE TYROSINE SIDE-         
REMARK   3  CHAIN TO OCCUPY THE CORRECT POSITION WITH RESPECT TO THE            
REMARK   3  POSITION OF THE NICOTINAMIDE RING.                                  
REMARK   4                                                                      
REMARK   4 1DFI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
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        : 22-JUL-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX7.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488                              
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   : 51902                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.080                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.350                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.1                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.10400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200  AND ISOMORPHOUS REPLACEMENT                                         
REMARK 200 SOFTWARE USED: CCP4                                                  
REMARK 200 STARTING MODEL: BRASSICA NAPUS ENR (PDB ENTRY 1ENO)                  
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 400, PH 5.0 ACETATE, 10MM        
REMARK 280  NAD                                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       40.60000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19060 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 30540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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     LEU A   259                                                      
REMARK 465     GLU A   260                                                      
REMARK 465     LEU A   261                                                      
REMARK 465     LYS A   262                                                      
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     LEU B   259                                                      
REMARK 465     GLU B   260                                                      
REMARK 465     LEU B   261                                                      
REMARK 465     LYS B   262                                                      
REMARK 465     ALA C   196                                                      
REMARK 465     ALA C   197                                                      
REMARK 465     SER C   198                                                      
REMARK 465     GLY C   199                                                      
REMARK 465     ILE C   200                                                      
REMARK 465     LYS C   201                                                      
REMARK 465     ASP C   202                                                      
REMARK 465     PHE C   203                                                      
REMARK 465     ARG C   204                                                      
REMARK 465     LYS C   205                                                      
REMARK 465     LEU C   259                                                      
REMARK 465     GLU C   260                                                      
REMARK 465     LEU C   261                                                      
REMARK 465     LYS C   262                                                      
REMARK 465     ALA D   196                                                      
REMARK 465     ALA D   197                                                      
REMARK 465     SER D   198                                                      
REMARK 465     GLY D   199                                                      
REMARK 465     ILE D   200                                                      
REMARK 465     LYS D   201                                                      
REMARK 465     ASP D   202                                                      
REMARK 465     PHE D   203                                                      
REMARK 465     ARG D   204                                                      
REMARK 465     LYS D   205                                                      
REMARK 465     LEU D   259                                                      
REMARK 465     GLU D   260                                                      
REMARK 465     LEU D   261                                                      
REMARK 465     LYS D   262                                                      
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   N    TYR A   156     O    HOH A   581              1.69            
REMARK 500   OH   TYR C    22     OE1  GLN C    54              1.88            
REMARK 500   NH2  ARG B     8     O    HOH B   524              1.89            
REMARK 500   O    PRO A   154     O    HOH A   581              2.02            
REMARK 500   ND1  HIS C    29     O    HOH C   553              2.03            
REMARK 500   CD2  LEU D    61     OE2  GLU D    77              2.07            
REMARK 500   NZ   LYS B   163     O2D  NAD B   501              2.09            
REMARK 500   O3D  NAD A   501     O    HOH A   591              2.15            
REMARK 500   NH2  ARG D   193     OE2  GLU D   211              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LEU C  10   C     VAL C  11   N       0.146                       
REMARK 500    VAL D  11   C     THR D  12   N      -0.259                       
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    ARG A 151   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    GLY B  13   O   -  C   -  N   ANGL. DEV. = -19.0 DEGREES          
REMARK 500    GLY C  13   O   -  C   -  N   ANGL. DEV. = -16.8 DEGREES          
REMARK 500    ARG C 218   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    THR D  12   C   -  N   -  CA  ANGL. DEV. =  16.5 DEGREES          
REMARK 500    ARG D 193   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG D 218   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG D 218   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 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    LYS A  45      -61.94    -29.96                                   
REMARK 500    SER A 121      -52.23   -124.09                                   
REMARK 500    ASN A 155      -20.07     65.24                                   
REMARK 500    ASN A 157     -113.99     40.11                                   
REMARK 500    VAL A 247       73.15   -119.90                                   
REMARK 500    SER B 121      -50.82   -121.55                                   
REMARK 500    ASN B 155      -13.30     71.68                                   
REMARK 500    ASN B 157     -130.88     38.17                                   
REMARK 500    VAL B 247       77.29   -115.68                                   
REMARK 500    ASP B 248       21.90   -140.85                                   
REMARK 500    LYS C  45      -48.57    -25.36                                   
REMARK 500    ASN C 155      -11.30     65.56                                   
REMARK 500    ASN C 157     -128.34     42.57                                   
REMARK 500    ARG C 193      -73.84    -42.79                                   
REMARK 500    THR C 194      -77.41    -30.05                                   
REMARK 500    ASN C 257       15.67    -65.31                                   
REMARK 500    ASN D 155      -23.39     73.93                                   
REMARK 500    ASN D 157     -121.18     41.71                                   
REMARK 500    VAL D 247       76.59   -119.94                                   
REMARK 500    ASN D 257       45.14    -86.07                                   
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, 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 B  13        -24.96                                           
REMARK 500    GLY C  13        -18.53                                           
REMARK 500    GLU D 167        -10.21                                           
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 C 571        DISTANCE =  5.62 ANGSTROMS                       
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 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 501                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 501                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 501                 
DBREF  1DFI A    2   262  UNP    P29132   FABI_ECOLI       1    261             
DBREF  1DFI B    2   262  UNP    P29132   FABI_ECOLI       1    261             
DBREF  1DFI C    2   262  UNP    P29132   FABI_ECOLI       1    261             
DBREF  1DFI D    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                                                          
SEQRES   1 C  261  GLY PHE LEU SER GLY LYS ARG ILE LEU VAL THR GLY VAL          
SEQRES   2 C  261  ALA SER LYS LEU SER ILE ALA TYR GLY ILE ALA GLN ALA          
SEQRES   3 C  261  MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR GLN          
SEQRES   4 C  261  ASN ASP LYS LEU LYS GLY ARG VAL GLU GLU PHE ALA ALA          
SEQRES   5 C  261  GLN LEU GLY SER ASP ILE VAL LEU GLN CYS ASP VAL ALA          
SEQRES   6 C  261  GLU ASP ALA SER ILE ASP THR MET PHE ALA GLU LEU GLY          
SEQRES   7 C  261  LYS VAL TRP PRO LYS PHE ASP GLY PHE VAL HIS SER ILE          
SEQRES   8 C  261  GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY ASP TYR VAL          
SEQRES   9 C  261  ASN ALA VAL THR ARG GLU GLY PHE LYS ILE ALA HIS ASP          
SEQRES  10 C  261  ILE SER SER TYR SER PHE VAL ALA MET ALA LYS ALA CYS          
SEQRES  11 C  261  ARG SER MET LEU ASN PRO GLY SER ALA LEU LEU THR LEU          
SEQRES  12 C  261  SER TYR LEU GLY ALA GLU ARG ALA ILE PRO ASN TYR ASN          
SEQRES  13 C  261  VAL MET GLY LEU ALA LYS ALA SER LEU GLU ALA ASN VAL          
SEQRES  14 C  261  ARG TYR MET ALA ASN ALA MET GLY PRO GLU GLY VAL ARG          
SEQRES  15 C  261  VAL ASN ALA ILE SER ALA GLY PRO ILE ARG THR LEU ALA          
SEQRES  16 C  261  ALA SER GLY ILE LYS ASP PHE ARG LYS MET LEU ALA HIS          
SEQRES  17 C  261  CYS GLU ALA VAL THR PRO ILE ARG ARG THR VAL THR ILE          
SEQRES  18 C  261  GLU ASP VAL GLY ASN SER ALA ALA PHE LEU CYS SER ASP          
SEQRES  19 C  261  LEU SER ALA GLY ILE SER GLY GLU VAL VAL HIS VAL ASP          
SEQRES  20 C  261  GLY GLY PHE SER ILE ALA ALA MET ASN GLU LEU GLU LEU          
SEQRES  21 C  261  LYS                                                          
SEQRES   1 D  261  GLY PHE LEU SER GLY LYS ARG ILE LEU VAL THR GLY VAL          
SEQRES   2 D  261  ALA SER LYS LEU SER ILE ALA TYR GLY ILE ALA GLN ALA          
SEQRES   3 D  261  MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR GLN          
SEQRES   4 D  261  ASN ASP LYS LEU LYS GLY ARG VAL GLU GLU PHE ALA ALA          
SEQRES   5 D  261  GLN LEU GLY SER ASP ILE VAL LEU GLN CYS ASP VAL ALA          
SEQRES   6 D  261  GLU ASP ALA SER ILE ASP THR MET PHE ALA GLU LEU GLY          
SEQRES   7 D  261  LYS VAL TRP PRO LYS PHE ASP GLY PHE VAL HIS SER ILE          
SEQRES   8 D  261  GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY ASP TYR VAL          
SEQRES   9 D  261  ASN ALA VAL THR ARG GLU GLY PHE LYS ILE ALA HIS ASP          
SEQRES  10 D  261  ILE SER SER TYR SER PHE VAL ALA MET ALA LYS ALA CYS          
SEQRES  11 D  261  ARG SER MET LEU ASN PRO GLY SER ALA LEU LEU THR LEU          
SEQRES  12 D  261  SER TYR LEU GLY ALA GLU ARG ALA ILE PRO ASN TYR ASN          
SEQRES  13 D  261  VAL MET GLY LEU ALA LYS ALA SER LEU GLU ALA ASN VAL          
SEQRES  14 D  261  ARG TYR MET ALA ASN ALA MET GLY PRO GLU GLY VAL ARG          
SEQRES  15 D  261  VAL ASN ALA ILE SER ALA GLY PRO ILE ARG THR LEU ALA          
SEQRES  16 D  261  ALA SER GLY ILE LYS ASP PHE ARG LYS MET LEU ALA HIS          
SEQRES  17 D  261  CYS GLU ALA VAL THR PRO ILE ARG ARG THR VAL THR ILE          
SEQRES  18 D  261  GLU ASP VAL GLY ASN SER ALA ALA PHE LEU CYS SER ASP          
SEQRES  19 D  261  LEU SER ALA GLY ILE SER GLY GLU VAL VAL HIS VAL ASP          
SEQRES  20 D  261  GLY GLY PHE SER ILE ALA ALA MET ASN GLU LEU GLU LEU          
SEQRES  21 D  261  LYS                                                          
HET    NAD  A 501      44                                                       
HET    NAD  B 501      44                                                       
HET    NAD  C 501      44                                                       
HET    NAD  D 501      44                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
FORMUL   5  NAD    4(C21 H27 N7 O14 P2)                                         
FORMUL   9  HOH   *327(H2 O)                                                    
HELIX    1   1 ILE A   20  ARG A   30  1                                  11    
HELIX    2   2 LYS A   45  LEU A   55  1                                  11    
HELIX    3   3 ASP A   68  VAL A   81  1                                  14    
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 LEU A  207  VAL A  213  1                                   7    
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 LYS B   45  LEU B   55  1                                  11    
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  1                                  24    
HELIX   23  23 LEU B  207  VAL B  213  1                                   7    
HELIX   24  24 ILE B  222  CYS B  233  1                                  12    
HELIX   25  25 ASP B  235  SER B  237  5                                   3    
HELIX   26  26 PHE B  251  ILE B  253  5                                   3    
HELIX   27  27 ILE C   20  ARG C   30  1                                  11    
HELIX   28  28 ASP C   42  LEU C   55  1                                  14    
HELIX   29  29 ASP C   68  VAL C   81  1                                  14    
HELIX   30  30 ASP C   98  LEU C  100  5                                   3    
HELIX   31  31 TYR C  104  ALA C  107  1                                   4    
HELIX   32  32 ARG C  110  SER C  120  1                                  11    
HELIX   33  33 TYR C  122  MET C  134  1                                  13    
HELIX   34  34 LEU C  147  ALA C  149  5                                   3    
HELIX   35  35 ASN C  157  GLU C  180  5                                  24    
HELIX   36  36 LEU C  207  VAL C  213  1                                   7    
HELIX   37  37 ILE C  222  CYS C  233  1                                  12    
HELIX   38  38 ASP C  235  SER C  237  5                                   3    
HELIX   39  39 PHE C  251  ILE C  253  5                                   3    
HELIX   40  40 ILE D   20  ARG D   30  1                                  11    
HELIX   41  41 ASP D   42  GLN D   54  1                                  13    
HELIX   42  42 ASP D   68  VAL D   81  1                                  14    
HELIX   43  43 GLY D   97  LEU D  100  5                                   4    
HELIX   44  44 TYR D  104  ALA D  107  1                                   4    
HELIX   45  45 ARG D  110  SER D  120  1                                  11    
HELIX   46  46 TYR D  122  MET D  134  1                                  13    
HELIX   47  47 LEU D  147  ALA D  149  5                                   3    
HELIX   48  48 ASN D  157  GLU D  180  1                                  24    
HELIX   49  49 LEU D  207  VAL D  213  1                                   7    
HELIX   50  50 ILE D  222  CYS D  233  1                                  12    
HELIX   51  51 ASP D  235  SER D  237  5                                   3    
HELIX   52  52 PHE D  251  ILE D  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 ALA A 140  SER A 145  1  N  ALA A 140   O  PHE A  88           
SHEET    3   B 4 ARG A 183  ALA A 189  1  N  ARG A 183   O  LEU A 141           
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 ALA B 140  SER B 145  1  N  ALA B 140   O  PHE B  88           
SHEET    3   D 4 ARG B 183  ALA B 189  1  N  ARG B 183   O  LEU B 141           
SHEET    4   D 4 VAL B 244  VAL B 247  1  N  VAL B 245   O  ALA B 186           
SHEET    1   E 3 ARG C   8  VAL C  11  0                                        
SHEET    2   E 3 GLU C  34  TYR C  39  1  N  GLU C  34   O  ILE C   9           
SHEET    3   E 3 VAL C  60  GLN C  62  1  N  LEU C  61   O  PHE C  37           
SHEET    1   F 4 GLY C  87  HIS C  90  0                                        
SHEET    2   F 4 ALA C 140  SER C 145  1  N  ALA C 140   O  PHE C  88           
SHEET    3   F 4 ARG C 183  ALA C 189  1  N  ARG C 183   O  LEU C 141           
SHEET    4   F 4 VAL C 244  VAL C 247  1  N  VAL C 245   O  ALA C 186           
SHEET    1   G 3 ARG D   8  VAL D  11  0                                        
SHEET    2   G 3 GLU D  34  TYR D  39  1  N  GLU D  34   O  ILE D   9           
SHEET    3   G 3 VAL D  60  GLN D  62  1  N  LEU D  61   O  PHE D  37           
SHEET    1   H 4 GLY D  87  HIS D  90  0                                        
SHEET    2   H 4 ALA D 140  SER D 145  1  N  ALA D 140   O  PHE D  88           
SHEET    3   H 4 ARG D 183  ALA D 189  1  N  ARG D 183   O  LEU D 141           
SHEET    4   H 4 VAL D 244  VAL D 247  1  N  VAL D 245   O  ALA D 186           
SITE     1 AC1 20 GLY A  13  VAL A  14  ALA A  15  SER A  19                    
SITE     2 AC1 20 ILE A  20  GLN A  40  CYS A  63  ASP A  64                    
SITE     3 AC1 20 VAL A  65  SER A  91  ILE A  92  LEU A 144                    
SITE     4 AC1 20 SER A 145  LYS A 163  ALA A 189  ILE A 192                    
SITE     5 AC1 20 LEU A 195  HOH A 539  HOH A 541  HOH A 591                    
SITE     1 AC2 17 GLY B  13  ALA B  15  SER B  19  ILE B  20                    
SITE     2 AC2 17 ALA B  21  GLN B  40  CYS B  63  ASP B  64                    
SITE     3 AC2 17 VAL B  65  SER B  91  ILE B  92  LEU B 144                    
SITE     4 AC2 17 SER B 145  LYS B 163  ALA B 189  GLY B 190                    
SITE     5 AC2 17 HOH B 528                                                     
SITE     1 AC3 20 GLY C  13  ALA C  15  ILE C  20  GLN C  40                    
SITE     2 AC3 20 CYS C  63  ASP C  64  VAL C  65  SER C  91                    
SITE     3 AC3 20 ILE C  92  GLY C  93  LEU C 144  SER C 145                    
SITE     4 AC3 20 LYS C 163  ALA C 189  GLY C 190  ILE C 192                    
SITE     5 AC3 20 LEU C 195  HOH C 512  HOH C 551  HOH C 580                    
SITE     1 AC4 21 GLY D  13  ALA D  15  SER D  19  ILE D  20                    
SITE     2 AC4 21 GLN D  40  CYS D  63  ASP D  64  VAL D  65                    
SITE     3 AC4 21 SER D  91  LEU D 144  SER D 145  LYS D 163                    
SITE     4 AC4 21 ALA D 189  GLY D 190  PRO D 191  ILE D 192                    
SITE     5 AC4 21 LEU D 195  HOH D 526  HOH D 535  HOH D 561                    
SITE     6 AC4 21 HOH D 564                                                     
CRYST1   74.000   81.200   79.000  90.00  92.90  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013514  0.000000  0.000685        0.00000                         
SCALE2      0.000000  0.012315  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012674        0.00000                         
MTRIX1   1  0.795000  0.159000 -0.585000       14.51000    1                    
MTRIX2   1  0.158000 -0.986000 -0.053000       -0.98000    1                    
MTRIX3   1 -0.585000 -0.050000 -0.809000       44.24000    1                    
MTRIX1   2 -0.812000  0.025000  0.583000       19.05000    1                    
MTRIX2   2  0.018000 -0.997000  0.068000       -1.09000    1                    
MTRIX3   2  0.583000  0.066000  0.810000       -6.12000    1                    
MTRIX1   3 -0.984000 -0.175000 -0.001000       33.13000    1                    
MTRIX2   3 -0.175000  0.984000 -0.009000        3.10000    1                    
MTRIX3   3  0.002000 -0.008000 -1.000000       38.10000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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