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Database: PDB
Entry: 1QSG
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HEADER    OXIDOREDUCTASE                          21-JUN-99   1QSG              
TITLE     CRYSTAL STRUCTURE OF ENOYL REDUCTASE INHIBITION BY TRICLOSAN          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE;                    
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: NADH-DEPENDENT ENOYL-ACP REDUCTASE;                         
COMPND   5 EC: 1.3.1.9;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    ENOYL REDUCTASE, OXIDOREDUCTASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.J.STEWART,S.PARIKH,G.XIAO,P.J.TONGE,C.KISKER                        
REVDAT   7   13-JUL-11 1QSG    1       VERSN                                    
REVDAT   6   24-FEB-09 1QSG    1       VERSN                                    
REVDAT   5   29-APR-03 1QSG    1       REMARK HET    FORMUL HETATM              
REVDAT   5 2                   1       CONECT MASTER                            
REVDAT   4   26-SEP-01 1QSG    3       ATOM   CONECT                            
REVDAT   3   23-JUN-00 1QSG    3       HETATM HETNAM COMPND SOURCE              
REVDAT   3 2                   3       DBREF  SEQADV                            
REVDAT   2   22-DEC-99 1QSG    1       REMARK                                   
REVDAT   1   21-JUL-99 1QSG    0                                                
JRNL        AUTH   M.J.STEWART,S.PARIKH,G.XIAO,P.J.TONGE,C.KISKER               
JRNL        TITL   STRUCTURAL BASIS AND MECHANISM OF ENOYL REDUCTASE INHIBITION 
JRNL        TITL 2 BY TRICLOSAN.                                                
JRNL        REF    J.MOL.BIOL.                   V. 290   859 1999              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   10398587                                                     
JRNL        DOI    10.1006/JMBI.1999.2907                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 182903                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3664                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15353                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 584                                     
REMARK   3   SOLVENT ATOMS            : 1350                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.120         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.120         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.100         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.260         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.012 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.030 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.035 ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.022 ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.109 ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.166 ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : 0.258 ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : 0.157 ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 4.000 ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : 13.800; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : 27.300; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.456 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.040 ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.038 ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.308 ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1QSG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB009210.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-FEB-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 95.0                               
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X26C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4R                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 183224                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : 1.850                              
REMARK 200  R MERGE                    (I) : 0.04400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.64                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1DFI                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, AMMONIUM ACETATE, SODIUM       
REMARK 280  ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  295.15K                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 22690 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -201.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 22820 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -201.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
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     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLU A   260                                                      
REMARK 465     LEU A   261                                                      
REMARK 465     LYS A   262                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B   260                                                      
REMARK 465     LEU B   261                                                      
REMARK 465     LYS B   262                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C   260                                                      
REMARK 465     LEU C   261                                                      
REMARK 465     LYS C   262                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLU D   260                                                      
REMARK 465     LEU D   261                                                      
REMARK 465     LYS D   262                                                      
REMARK 465     GLY E    -2                                                      
REMARK 465     SER E    -1                                                      
REMARK 465     HIS E     0                                                      
REMARK 465     MET E     1                                                      
REMARK 465     GLU E   260                                                      
REMARK 465     LEU E   261                                                      
REMARK 465     LYS E   262                                                      
REMARK 465     GLY F    -2                                                      
REMARK 465     SER F    -1                                                      
REMARK 465     HIS F     0                                                      
REMARK 465     MET F     1                                                      
REMARK 465     GLU F   260                                                      
REMARK 465     LEU F   261                                                      
REMARK 465     LYS F   262                                                      
REMARK 465     GLY G    -2                                                      
REMARK 465     SER G    -1                                                      
REMARK 465     HIS G     0                                                      
REMARK 465     MET G     1                                                      
REMARK 465     LEU G   261                                                      
REMARK 465     LYS G   262                                                      
REMARK 465     GLY H    -2                                                      
REMARK 465     SER H    -1                                                      
REMARK 465     HIS H     0                                                      
REMARK 465     MET H     1                                                      
REMARK 465     GLU H   260                                                      
REMARK 465     LEU H   261                                                      
REMARK 465     LYS H   262                                                      
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   8   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    ASP A  42   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A  98   CB  -  CG  -  OD1 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ASP A 101   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ASP A 103   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A 110   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG A 151   CD  -  NE  -  CZ  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ARG A 151   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    GLU A 167   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    ARG B  30   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP B  98   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ARG B 151   CD  -  NE  -  CZ  ANGL. DEV. =  11.8 DEGREES          
REMARK 500    ARG B 151   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG C   8   CD  -  NE  -  CZ  ANGL. DEV. =  13.8 DEGREES          
REMARK 500    ARG C   8   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG C   8   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG C  30   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ASP C  64   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG C 110   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG C 151   CD  -  NE  -  CZ  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    ARG C 218   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ASP D  98   OD1 -  CG  -  OD2 ANGL. DEV. = -12.0 DEGREES          
REMARK 500    ASP D  98   CB  -  CG  -  OD1 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ARG D 132   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG E  30   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG E 110   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG F   8   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG F  30   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG F  47   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ASP F  98   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP F 101   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG F 110   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG F 151   CD  -  NE  -  CZ  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ARG F 151   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG F 193   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG F 193   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG F 218   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG G   8   CD  -  NE  -  CZ  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    ARG G   8   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG G  30   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP G  98   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG G 110   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG G 151   CD  -  NE  -  CZ  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ARG G 151   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG H  30   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG H 151   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 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      117.59   -160.35                                   
REMARK 500    SER A 121      -54.33   -123.23                                   
REMARK 500    ASN A 155      -33.14     72.01                                   
REMARK 500    ASN A 157     -124.50     43.68                                   
REMARK 500    VAL A 247       63.10   -119.40                                   
REMARK 500    LEU B 100       30.39    -98.12                                   
REMARK 500    SER B 121      -58.35   -123.83                                   
REMARK 500    ASN B 155      -21.74     71.98                                   
REMARK 500    ASN B 157     -123.21     43.02                                   
REMARK 500    VAL B 247       65.09   -119.70                                   
REMARK 500    SER C 121      -55.73   -120.10                                   
REMARK 500    ASN C 155      -24.03     65.93                                   
REMARK 500    ASN C 157     -130.41     48.83                                   
REMARK 500    ARG C 193       99.27    -69.06                                   
REMARK 500    VAL C 247       66.05   -117.43                                   
REMARK 500    CYS D  63      118.71   -162.27                                   
REMARK 500    SER D 121      -55.33   -123.32                                   
REMARK 500    ASN D 155      -24.17     74.64                                   
REMARK 500    ASN D 157     -125.57     43.72                                   
REMARK 500    SER D 237       32.20    -98.76                                   
REMARK 500    VAL D 247       64.77   -116.88                                   
REMARK 500    CYS E  63      114.51   -165.87                                   
REMARK 500    SER E 121      -57.20   -121.26                                   
REMARK 500    ASN E 155      -27.80     73.87                                   
REMARK 500    ASN E 157     -129.63     42.37                                   
REMARK 500    VAL E 247       73.16   -112.63                                   
REMARK 500    GLU E 258       -8.50    -45.63                                   
REMARK 500    SER F 121      -58.95   -120.33                                   
REMARK 500    ASN F 155      -25.15     71.53                                   
REMARK 500    ASN F 157     -123.67     41.71                                   
REMARK 500    VAL F 247       66.38   -119.71                                   
REMARK 500    SER G 121      -56.30   -121.22                                   
REMARK 500    ASN G 155      -21.45     65.82                                   
REMARK 500    ASN G 157     -130.23     49.21                                   
REMARK 500    VAL G 247       63.16   -117.88                                   
REMARK 500    LEU H 100       30.87    -99.12                                   
REMARK 500    ASP H 103      125.97    -39.71                                   
REMARK 500    SER H 121      -59.71   -121.53                                   
REMARK 500    ASN H 155      -17.37     70.86                                   
REMARK 500    ASN H 157     -127.69     44.46                                   
REMARK 500    VAL H 247       68.22   -116.09                                   
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 A1433        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH A1494        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH B1471        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH C1411        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH D1482        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH D1483        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH E1414        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH G1486        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH H1448        DISTANCE =  5.41 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1303                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 1306                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC C 1309                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC D 1312                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC E 1315                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC F 1318                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC G 1321                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC H 1324                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 1301                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCL A 1302                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 1304                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCL B 1305                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 1307                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCL C 1308                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 1310                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCL D 1311                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD E 1313                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCL E 1314                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD F 1316                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCL F 1317                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD G 1319                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCL G 1320                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD H 1322                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCL H 1323                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DFI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1DFG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1DFH   RELATED DB: PDB                                   
DBREF  1QSG A    1   262  UNP    P29132   FABI_ECOLI       1    262             
DBREF  1QSG B    1   262  UNP    P29132   FABI_ECOLI       1    262             
DBREF  1QSG C    1   262  UNP    P29132   FABI_ECOLI       1    262             
DBREF  1QSG D    1   262  UNP    P29132   FABI_ECOLI       1    262             
DBREF  1QSG E    1   262  UNP    P29132   FABI_ECOLI       1    262             
DBREF  1QSG F    1   262  UNP    P29132   FABI_ECOLI       1    262             
DBREF  1QSG G    1   262  UNP    P29132   FABI_ECOLI       1    262             
DBREF  1QSG H    1   262  UNP    P29132   FABI_ECOLI       1    262             
SEQADV 1QSG GLY A   -2  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG SER A   -1  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG HIS A    0  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG GLY B   -2  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG SER B   -1  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG HIS B    0  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG GLY C   -2  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG SER C   -1  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG HIS C    0  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG GLY D   -2  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG SER D   -1  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG HIS D    0  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG GLY E   -2  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG SER E   -1  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG HIS E    0  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG GLY F   -2  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG SER F   -1  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG HIS F    0  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG GLY G   -2  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG SER G   -1  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG HIS G    0  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG GLY H   -2  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG SER H   -1  UNP  P29132              EXPRESSION TAG                 
SEQADV 1QSG HIS H    0  UNP  P29132              EXPRESSION TAG                 
SEQRES   1 A  265  GLY SER HIS MET GLY PHE LEU SER GLY LYS ARG ILE LEU          
SEQRES   2 A  265  VAL THR GLY VAL ALA SER LYS LEU SER ILE ALA TYR GLY          
SEQRES   3 A  265  ILE ALA GLN ALA MET HIS ARG GLU GLY ALA GLU LEU ALA          
SEQRES   4 A  265  PHE THR TYR GLN ASN ASP LYS LEU LYS GLY ARG VAL GLU          
SEQRES   5 A  265  GLU PHE ALA ALA GLN LEU GLY SER ASP ILE VAL LEU GLN          
SEQRES   6 A  265  CYS ASP VAL ALA GLU ASP ALA SER ILE ASP THR MET PHE          
SEQRES   7 A  265  ALA GLU LEU GLY LYS VAL TRP PRO LYS PHE ASP GLY PHE          
SEQRES   8 A  265  VAL HIS SER ILE GLY PHE ALA PRO GLY ASP GLN LEU ASP          
SEQRES   9 A  265  GLY ASP TYR VAL ASN ALA VAL THR ARG GLU GLY PHE LYS          
SEQRES  10 A  265  ILE ALA HIS ASP ILE SER SER TYR SER PHE VAL ALA MET          
SEQRES  11 A  265  ALA LYS ALA CYS ARG SER MET LEU ASN PRO GLY SER ALA          
SEQRES  12 A  265  LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG ALA ILE          
SEQRES  13 A  265  PRO ASN TYR ASN VAL MET GLY LEU ALA LYS ALA SER LEU          
SEQRES  14 A  265  GLU ALA ASN VAL ARG TYR MET ALA ASN ALA MET GLY PRO          
SEQRES  15 A  265  GLU GLY VAL ARG VAL ASN ALA ILE SER ALA GLY PRO ILE          
SEQRES  16 A  265  ARG THR LEU ALA ALA SER GLY ILE LYS ASP PHE ARG LYS          
SEQRES  17 A  265  MET LEU ALA HIS CYS GLU ALA VAL THR PRO ILE ARG ARG          
SEQRES  18 A  265  THR VAL THR ILE GLU ASP VAL GLY ASN SER ALA ALA PHE          
SEQRES  19 A  265  LEU CYS SER ASP LEU SER ALA GLY ILE SER GLY GLU VAL          
SEQRES  20 A  265  VAL HIS VAL ASP GLY GLY PHE SER ILE ALA ALA MET ASN          
SEQRES  21 A  265  GLU LEU GLU LEU LYS                                          
SEQRES   1 B  265  GLY SER HIS MET GLY PHE LEU SER GLY LYS ARG ILE LEU          
SEQRES   2 B  265  VAL THR GLY VAL ALA SER LYS LEU SER ILE ALA TYR GLY          
SEQRES   3 B  265  ILE ALA GLN ALA MET HIS ARG GLU GLY ALA GLU LEU ALA          
SEQRES   4 B  265  PHE THR TYR GLN ASN ASP LYS LEU LYS GLY ARG VAL GLU          
SEQRES   5 B  265  GLU PHE ALA ALA GLN LEU GLY SER ASP ILE VAL LEU GLN          
SEQRES   6 B  265  CYS ASP VAL ALA GLU ASP ALA SER ILE ASP THR MET PHE          
SEQRES   7 B  265  ALA GLU LEU GLY LYS VAL TRP PRO LYS PHE ASP GLY PHE          
SEQRES   8 B  265  VAL HIS SER ILE GLY PHE ALA PRO GLY ASP GLN LEU ASP          
SEQRES   9 B  265  GLY ASP TYR VAL ASN ALA VAL THR ARG GLU GLY PHE LYS          
SEQRES  10 B  265  ILE ALA HIS ASP ILE SER SER TYR SER PHE VAL ALA MET          
SEQRES  11 B  265  ALA LYS ALA CYS ARG SER MET LEU ASN PRO GLY SER ALA          
SEQRES  12 B  265  LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG ALA ILE          
SEQRES  13 B  265  PRO ASN TYR ASN VAL MET GLY LEU ALA LYS ALA SER LEU          
SEQRES  14 B  265  GLU ALA ASN VAL ARG TYR MET ALA ASN ALA MET GLY PRO          
SEQRES  15 B  265  GLU GLY VAL ARG VAL ASN ALA ILE SER ALA GLY PRO ILE          
SEQRES  16 B  265  ARG THR LEU ALA ALA SER GLY ILE LYS ASP PHE ARG LYS          
SEQRES  17 B  265  MET LEU ALA HIS CYS GLU ALA VAL THR PRO ILE ARG ARG          
SEQRES  18 B  265  THR VAL THR ILE GLU ASP VAL GLY ASN SER ALA ALA PHE          
SEQRES  19 B  265  LEU CYS SER ASP LEU SER ALA GLY ILE SER GLY GLU VAL          
SEQRES  20 B  265  VAL HIS VAL ASP GLY GLY PHE SER ILE ALA ALA MET ASN          
SEQRES  21 B  265  GLU LEU GLU LEU LYS                                          
SEQRES   1 C  265  GLY SER HIS MET GLY PHE LEU SER GLY LYS ARG ILE LEU          
SEQRES   2 C  265  VAL THR GLY VAL ALA SER LYS LEU SER ILE ALA TYR GLY          
SEQRES   3 C  265  ILE ALA GLN ALA MET HIS ARG GLU GLY ALA GLU LEU ALA          
SEQRES   4 C  265  PHE THR TYR GLN ASN ASP LYS LEU LYS GLY ARG VAL GLU          
SEQRES   5 C  265  GLU PHE ALA ALA GLN LEU GLY SER ASP ILE VAL LEU GLN          
SEQRES   6 C  265  CYS ASP VAL ALA GLU ASP ALA SER ILE ASP THR MET PHE          
SEQRES   7 C  265  ALA GLU LEU GLY LYS VAL TRP PRO LYS PHE ASP GLY PHE          
SEQRES   8 C  265  VAL HIS SER ILE GLY PHE ALA PRO GLY ASP GLN LEU ASP          
SEQRES   9 C  265  GLY ASP TYR VAL ASN ALA VAL THR ARG GLU GLY PHE LYS          
SEQRES  10 C  265  ILE ALA HIS ASP ILE SER SER TYR SER PHE VAL ALA MET          
SEQRES  11 C  265  ALA LYS ALA CYS ARG SER MET LEU ASN PRO GLY SER ALA          
SEQRES  12 C  265  LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG ALA ILE          
SEQRES  13 C  265  PRO ASN TYR ASN VAL MET GLY LEU ALA LYS ALA SER LEU          
SEQRES  14 C  265  GLU ALA ASN VAL ARG TYR MET ALA ASN ALA MET GLY PRO          
SEQRES  15 C  265  GLU GLY VAL ARG VAL ASN ALA ILE SER ALA GLY PRO ILE          
SEQRES  16 C  265  ARG THR LEU ALA ALA SER GLY ILE LYS ASP PHE ARG LYS          
SEQRES  17 C  265  MET LEU ALA HIS CYS GLU ALA VAL THR PRO ILE ARG ARG          
SEQRES  18 C  265  THR VAL THR ILE GLU ASP VAL GLY ASN SER ALA ALA PHE          
SEQRES  19 C  265  LEU CYS SER ASP LEU SER ALA GLY ILE SER GLY GLU VAL          
SEQRES  20 C  265  VAL HIS VAL ASP GLY GLY PHE SER ILE ALA ALA MET ASN          
SEQRES  21 C  265  GLU LEU GLU LEU LYS                                          
SEQRES   1 D  265  GLY SER HIS MET GLY PHE LEU SER GLY LYS ARG ILE LEU          
SEQRES   2 D  265  VAL THR GLY VAL ALA SER LYS LEU SER ILE ALA TYR GLY          
SEQRES   3 D  265  ILE ALA GLN ALA MET HIS ARG GLU GLY ALA GLU LEU ALA          
SEQRES   4 D  265  PHE THR TYR GLN ASN ASP LYS LEU LYS GLY ARG VAL GLU          
SEQRES   5 D  265  GLU PHE ALA ALA GLN LEU GLY SER ASP ILE VAL LEU GLN          
SEQRES   6 D  265  CYS ASP VAL ALA GLU ASP ALA SER ILE ASP THR MET PHE          
SEQRES   7 D  265  ALA GLU LEU GLY LYS VAL TRP PRO LYS PHE ASP GLY PHE          
SEQRES   8 D  265  VAL HIS SER ILE GLY PHE ALA PRO GLY ASP GLN LEU ASP          
SEQRES   9 D  265  GLY ASP TYR VAL ASN ALA VAL THR ARG GLU GLY PHE LYS          
SEQRES  10 D  265  ILE ALA HIS ASP ILE SER SER TYR SER PHE VAL ALA MET          
SEQRES  11 D  265  ALA LYS ALA CYS ARG SER MET LEU ASN PRO GLY SER ALA          
SEQRES  12 D  265  LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG ALA ILE          
SEQRES  13 D  265  PRO ASN TYR ASN VAL MET GLY LEU ALA LYS ALA SER LEU          
SEQRES  14 D  265  GLU ALA ASN VAL ARG TYR MET ALA ASN ALA MET GLY PRO          
SEQRES  15 D  265  GLU GLY VAL ARG VAL ASN ALA ILE SER ALA GLY PRO ILE          
SEQRES  16 D  265  ARG THR LEU ALA ALA SER GLY ILE LYS ASP PHE ARG LYS          
SEQRES  17 D  265  MET LEU ALA HIS CYS GLU ALA VAL THR PRO ILE ARG ARG          
SEQRES  18 D  265  THR VAL THR ILE GLU ASP VAL GLY ASN SER ALA ALA PHE          
SEQRES  19 D  265  LEU CYS SER ASP LEU SER ALA GLY ILE SER GLY GLU VAL          
SEQRES  20 D  265  VAL HIS VAL ASP GLY GLY PHE SER ILE ALA ALA MET ASN          
SEQRES  21 D  265  GLU LEU GLU LEU LYS                                          
SEQRES   1 E  265  GLY SER HIS MET GLY PHE LEU SER GLY LYS ARG ILE LEU          
SEQRES   2 E  265  VAL THR GLY VAL ALA SER LYS LEU SER ILE ALA TYR GLY          
SEQRES   3 E  265  ILE ALA GLN ALA MET HIS ARG GLU GLY ALA GLU LEU ALA          
SEQRES   4 E  265  PHE THR TYR GLN ASN ASP LYS LEU LYS GLY ARG VAL GLU          
SEQRES   5 E  265  GLU PHE ALA ALA GLN LEU GLY SER ASP ILE VAL LEU GLN          
SEQRES   6 E  265  CYS ASP VAL ALA GLU ASP ALA SER ILE ASP THR MET PHE          
SEQRES   7 E  265  ALA GLU LEU GLY LYS VAL TRP PRO LYS PHE ASP GLY PHE          
SEQRES   8 E  265  VAL HIS SER ILE GLY PHE ALA PRO GLY ASP GLN LEU ASP          
SEQRES   9 E  265  GLY ASP TYR VAL ASN ALA VAL THR ARG GLU GLY PHE LYS          
SEQRES  10 E  265  ILE ALA HIS ASP ILE SER SER TYR SER PHE VAL ALA MET          
SEQRES  11 E  265  ALA LYS ALA CYS ARG SER MET LEU ASN PRO GLY SER ALA          
SEQRES  12 E  265  LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG ALA ILE          
SEQRES  13 E  265  PRO ASN TYR ASN VAL MET GLY LEU ALA LYS ALA SER LEU          
SEQRES  14 E  265  GLU ALA ASN VAL ARG TYR MET ALA ASN ALA MET GLY PRO          
SEQRES  15 E  265  GLU GLY VAL ARG VAL ASN ALA ILE SER ALA GLY PRO ILE          
SEQRES  16 E  265  ARG THR LEU ALA ALA SER GLY ILE LYS ASP PHE ARG LYS          
SEQRES  17 E  265  MET LEU ALA HIS CYS GLU ALA VAL THR PRO ILE ARG ARG          
SEQRES  18 E  265  THR VAL THR ILE GLU ASP VAL GLY ASN SER ALA ALA PHE          
SEQRES  19 E  265  LEU CYS SER ASP LEU SER ALA GLY ILE SER GLY GLU VAL          
SEQRES  20 E  265  VAL HIS VAL ASP GLY GLY PHE SER ILE ALA ALA MET ASN          
SEQRES  21 E  265  GLU LEU GLU LEU LYS                                          
SEQRES   1 F  265  GLY SER HIS MET GLY PHE LEU SER GLY LYS ARG ILE LEU          
SEQRES   2 F  265  VAL THR GLY VAL ALA SER LYS LEU SER ILE ALA TYR GLY          
SEQRES   3 F  265  ILE ALA GLN ALA MET HIS ARG GLU GLY ALA GLU LEU ALA          
SEQRES   4 F  265  PHE THR TYR GLN ASN ASP LYS LEU LYS GLY ARG VAL GLU          
SEQRES   5 F  265  GLU PHE ALA ALA GLN LEU GLY SER ASP ILE VAL LEU GLN          
SEQRES   6 F  265  CYS ASP VAL ALA GLU ASP ALA SER ILE ASP THR MET PHE          
SEQRES   7 F  265  ALA GLU LEU GLY LYS VAL TRP PRO LYS PHE ASP GLY PHE          
SEQRES   8 F  265  VAL HIS SER ILE GLY PHE ALA PRO GLY ASP GLN LEU ASP          
SEQRES   9 F  265  GLY ASP TYR VAL ASN ALA VAL THR ARG GLU GLY PHE LYS          
SEQRES  10 F  265  ILE ALA HIS ASP ILE SER SER TYR SER PHE VAL ALA MET          
SEQRES  11 F  265  ALA LYS ALA CYS ARG SER MET LEU ASN PRO GLY SER ALA          
SEQRES  12 F  265  LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG ALA ILE          
SEQRES  13 F  265  PRO ASN TYR ASN VAL MET GLY LEU ALA LYS ALA SER LEU          
SEQRES  14 F  265  GLU ALA ASN VAL ARG TYR MET ALA ASN ALA MET GLY PRO          
SEQRES  15 F  265  GLU GLY VAL ARG VAL ASN ALA ILE SER ALA GLY PRO ILE          
SEQRES  16 F  265  ARG THR LEU ALA ALA SER GLY ILE LYS ASP PHE ARG LYS          
SEQRES  17 F  265  MET LEU ALA HIS CYS GLU ALA VAL THR PRO ILE ARG ARG          
SEQRES  18 F  265  THR VAL THR ILE GLU ASP VAL GLY ASN SER ALA ALA PHE          
SEQRES  19 F  265  LEU CYS SER ASP LEU SER ALA GLY ILE SER GLY GLU VAL          
SEQRES  20 F  265  VAL HIS VAL ASP GLY GLY PHE SER ILE ALA ALA MET ASN          
SEQRES  21 F  265  GLU LEU GLU LEU LYS                                          
SEQRES   1 G  265  GLY SER HIS MET GLY PHE LEU SER GLY LYS ARG ILE LEU          
SEQRES   2 G  265  VAL THR GLY VAL ALA SER LYS LEU SER ILE ALA TYR GLY          
SEQRES   3 G  265  ILE ALA GLN ALA MET HIS ARG GLU GLY ALA GLU LEU ALA          
SEQRES   4 G  265  PHE THR TYR GLN ASN ASP LYS LEU LYS GLY ARG VAL GLU          
SEQRES   5 G  265  GLU PHE ALA ALA GLN LEU GLY SER ASP ILE VAL LEU GLN          
SEQRES   6 G  265  CYS ASP VAL ALA GLU ASP ALA SER ILE ASP THR MET PHE          
SEQRES   7 G  265  ALA GLU LEU GLY LYS VAL TRP PRO LYS PHE ASP GLY PHE          
SEQRES   8 G  265  VAL HIS SER ILE GLY PHE ALA PRO GLY ASP GLN LEU ASP          
SEQRES   9 G  265  GLY ASP TYR VAL ASN ALA VAL THR ARG GLU GLY PHE LYS          
SEQRES  10 G  265  ILE ALA HIS ASP ILE SER SER TYR SER PHE VAL ALA MET          
SEQRES  11 G  265  ALA LYS ALA CYS ARG SER MET LEU ASN PRO GLY SER ALA          
SEQRES  12 G  265  LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG ALA ILE          
SEQRES  13 G  265  PRO ASN TYR ASN VAL MET GLY LEU ALA LYS ALA SER LEU          
SEQRES  14 G  265  GLU ALA ASN VAL ARG TYR MET ALA ASN ALA MET GLY PRO          
SEQRES  15 G  265  GLU GLY VAL ARG VAL ASN ALA ILE SER ALA GLY PRO ILE          
SEQRES  16 G  265  ARG THR LEU ALA ALA SER GLY ILE LYS ASP PHE ARG LYS          
SEQRES  17 G  265  MET LEU ALA HIS CYS GLU ALA VAL THR PRO ILE ARG ARG          
SEQRES  18 G  265  THR VAL THR ILE GLU ASP VAL GLY ASN SER ALA ALA PHE          
SEQRES  19 G  265  LEU CYS SER ASP LEU SER ALA GLY ILE SER GLY GLU VAL          
SEQRES  20 G  265  VAL HIS VAL ASP GLY GLY PHE SER ILE ALA ALA MET ASN          
SEQRES  21 G  265  GLU LEU GLU LEU LYS                                          
SEQRES   1 H  265  GLY SER HIS MET GLY PHE LEU SER GLY LYS ARG ILE LEU          
SEQRES   2 H  265  VAL THR GLY VAL ALA SER LYS LEU SER ILE ALA TYR GLY          
SEQRES   3 H  265  ILE ALA GLN ALA MET HIS ARG GLU GLY ALA GLU LEU ALA          
SEQRES   4 H  265  PHE THR TYR GLN ASN ASP LYS LEU LYS GLY ARG VAL GLU          
SEQRES   5 H  265  GLU PHE ALA ALA GLN LEU GLY SER ASP ILE VAL LEU GLN          
SEQRES   6 H  265  CYS ASP VAL ALA GLU ASP ALA SER ILE ASP THR MET PHE          
SEQRES   7 H  265  ALA GLU LEU GLY LYS VAL TRP PRO LYS PHE ASP GLY PHE          
SEQRES   8 H  265  VAL HIS SER ILE GLY PHE ALA PRO GLY ASP GLN LEU ASP          
SEQRES   9 H  265  GLY ASP TYR VAL ASN ALA VAL THR ARG GLU GLY PHE LYS          
SEQRES  10 H  265  ILE ALA HIS ASP ILE SER SER TYR SER PHE VAL ALA MET          
SEQRES  11 H  265  ALA LYS ALA CYS ARG SER MET LEU ASN PRO GLY SER ALA          
SEQRES  12 H  265  LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG ALA ILE          
SEQRES  13 H  265  PRO ASN TYR ASN VAL MET GLY LEU ALA LYS ALA SER LEU          
SEQRES  14 H  265  GLU ALA ASN VAL ARG TYR MET ALA ASN ALA MET GLY PRO          
SEQRES  15 H  265  GLU GLY VAL ARG VAL ASN ALA ILE SER ALA GLY PRO ILE          
SEQRES  16 H  265  ARG THR LEU ALA ALA SER GLY ILE LYS ASP PHE ARG LYS          
SEQRES  17 H  265  MET LEU ALA HIS CYS GLU ALA VAL THR PRO ILE ARG ARG          
SEQRES  18 H  265  THR VAL THR ILE GLU ASP VAL GLY ASN SER ALA ALA PHE          
SEQRES  19 H  265  LEU CYS SER ASP LEU SER ALA GLY ILE SER GLY GLU VAL          
SEQRES  20 H  265  VAL HIS VAL ASP GLY GLY PHE SER ILE ALA ALA MET ASN          
SEQRES  21 H  265  GLU LEU GLU LEU LYS                                          
HET    GLC  A1303      12                                                       
HET    GLC  B1306      12                                                       
HET    GLC  C1309      12                                                       
HET    GLC  D1312      12                                                       
HET    GLC  E1315      12                                                       
HET    GLC  F1318      12                                                       
HET    GLC  G1321      12                                                       
HET    GLC  H1324      12                                                       
HET    NAD  A1301      44                                                       
HET    TCL  A1302      17                                                       
HET    NAD  B1304      44                                                       
HET    TCL  B1305      17                                                       
HET    NAD  C1307      44                                                       
HET    TCL  C1308      17                                                       
HET    NAD  D1310      44                                                       
HET    TCL  D1311      17                                                       
HET    NAD  E1313      44                                                       
HET    TCL  E1314      17                                                       
HET    NAD  F1316      44                                                       
HET    TCL  F1317      17                                                       
HET    NAD  G1319      44                                                       
HET    TCL  G1320      17                                                       
HET    NAD  H1322      44                                                       
HET    TCL  H1323      17                                                       
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     TCL TRICLOSAN                                                        
FORMUL   9  GLC    8(C6 H12 O6)                                                 
FORMUL  17  NAD    8(C21 H27 N7 O14 P2)                                         
FORMUL  18  TCL    8(C12 H7 CL3 O2)                                             
FORMUL  33  HOH   *1350(H2 O)                                                   
HELIX    1   1 SER A   19  GLU A   31  1                                  13    
HELIX    2   2 LEU A   44  LEU A   55  1                                  12    
HELIX    3   3 GLU A   67  LYS A   80  1                                  14    
HELIX    4   4 PRO A   96  ASP A  101  5                                   6    
HELIX    5   5 ASP A  103  VAL A  108  1                                   6    
HELIX    6   6 THR A  109  SER A  121  1                                  13    
HELIX    7   7 SER A  121  ARG A  132  1                                  12    
HELIX    8   8 TYR A  146  GLU A  150  5                                   5    
HELIX    9   9 ASN A  157  GLY A  178  1                                  22    
HELIX   10  10 ALA A  196  ILE A  200  5                                   5    
HELIX   11  11 ASP A  202  THR A  214  1                                  13    
HELIX   12  12 THR A  221  CYS A  233  1                                  13    
HELIX   13  13 SER A  234  ALA A  238  5                                   5    
HELIX   14  14 GLY A  250  ILE A  253  5                                   4    
HELIX   15  15 SER B   19  GLU B   31  1                                  13    
HELIX   16  16 ASN B   41  LEU B   55  1                                  15    
HELIX   17  17 GLU B   67  GLY B   79  1                                  13    
HELIX   18  18 PRO B   96  ASP B  101  5                                   6    
HELIX   19  19 ASP B  103  VAL B  108  1                                   6    
HELIX   20  20 THR B  109  SER B  121  1                                  13    
HELIX   21  21 SER B  121  ARG B  132  1                                  12    
HELIX   22  22 TYR B  146  GLU B  150  5                                   5    
HELIX   23  23 ASN B  157  GLY B  178  1                                  22    
HELIX   24  24 LEU B  195  ILE B  200  5                                   6    
HELIX   25  25 ASP B  202  THR B  214  1                                  13    
HELIX   26  26 THR B  221  CYS B  233  1                                  13    
HELIX   27  27 SER B  234  ALA B  238  5                                   5    
HELIX   28  28 GLY B  250  ILE B  253  5                                   4    
HELIX   29  29 SER C   19  GLU C   31  1                                  13    
HELIX   30  30 ASN C   41  LYS C   43  5                                   3    
HELIX   31  31 LEU C   44  LEU C   55  1                                  12    
HELIX   32  32 GLU C   67  LYS C   80  1                                  14    
HELIX   33  33 PRO C   96  ASP C  101  5                                   6    
HELIX   34  34 ASP C  103  VAL C  108  1                                   6    
HELIX   35  35 THR C  109  SER C  121  1                                  13    
HELIX   36  36 SER C  121  ARG C  132  1                                  12    
HELIX   37  37 TYR C  146  GLU C  150  5                                   5    
HELIX   38  38 ASN C  157  GLY C  178  1                                  22    
HELIX   39  39 PRO C  179  GLY C  181  5                                   3    
HELIX   40  40 LEU C  195  ILE C  200  5                                   6    
HELIX   41  41 ASP C  202  THR C  214  1                                  13    
HELIX   42  42 THR C  221  CYS C  233  1                                  13    
HELIX   43  43 SER C  234  ALA C  238  5                                   5    
HELIX   44  44 GLY C  250  ILE C  253  5                                   4    
HELIX   45  45 SER D   19  GLU D   31  1                                  13    
HELIX   46  46 ASN D   41  LEU D   55  1                                  15    
HELIX   47  47 GLU D   67  TRP D   82  1                                  16    
HELIX   48  48 PRO D   96  ASP D  101  5                                   6    
HELIX   49  49 ASP D  103  VAL D  108  1                                   6    
HELIX   50  50 THR D  109  SER D  121  1                                  13    
HELIX   51  51 SER D  121  ARG D  132  1                                  12    
HELIX   52  52 TYR D  146  GLU D  150  5                                   5    
HELIX   53  53 ASN D  157  GLY D  178  1                                  22    
HELIX   54  54 LEU D  195  ILE D  200  5                                   6    
HELIX   55  55 ASP D  202  THR D  214  1                                  13    
HELIX   56  56 THR D  221  CYS D  233  1                                  13    
HELIX   57  57 SER D  234  ALA D  238  5                                   5    
HELIX   58  58 GLY D  250  ILE D  253  5                                   4    
HELIX   59  59 SER E   19  GLU E   31  1                                  13    
HELIX   60  60 ASN E   41  LEU E   55  1                                  15    
HELIX   61  61 GLU E   67  LYS E   80  1                                  14    
HELIX   62  62 PRO E   96  LEU E  100  5                                   5    
HELIX   63  63 ASP E  103  VAL E  108  1                                   6    
HELIX   64  64 THR E  109  SER E  121  1                                  13    
HELIX   65  65 SER E  121  ARG E  132  1                                  12    
HELIX   66  66 TYR E  146  GLU E  150  5                                   5    
HELIX   67  67 ASN E  157  GLY E  178  1                                  22    
HELIX   68  68 ALA E  196  ILE E  200  5                                   5    
HELIX   69  69 ASP E  202  THR E  214  1                                  13    
HELIX   70  70 THR E  221  CYS E  233  1                                  13    
HELIX   71  71 SER E  234  ALA E  238  5                                   5    
HELIX   72  72 GLY E  250  ILE E  253  5                                   4    
HELIX   73  73 SER F   19  GLU F   31  1                                  13    
HELIX   74  74 ASN F   41  LEU F   55  1                                  15    
HELIX   75  75 GLU F   67  TRP F   82  1                                  16    
HELIX   76  76 PRO F   96  ASP F  101  5                                   6    
HELIX   77  77 ASP F  103  VAL F  108  1                                   6    
HELIX   78  78 THR F  109  SER F  121  1                                  13    
HELIX   79  79 SER F  121  ARG F  132  1                                  12    
HELIX   80  80 TYR F  146  GLU F  150  5                                   5    
HELIX   81  81 ASN F  157  GLY F  178  1                                  22    
HELIX   82  82 LEU F  195  ILE F  200  5                                   6    
HELIX   83  83 ASP F  202  THR F  214  1                                  13    
HELIX   84  84 THR F  221  SER F  234  1                                  14    
HELIX   85  85 ASP F  235  ALA F  238  5                                   4    
HELIX   86  86 GLY F  250  ILE F  253  5                                   4    
HELIX   87  87 SER G   19  GLU G   31  1                                  13    
HELIX   88  88 LEU G   44  LEU G   55  1                                  12    
HELIX   89  89 GLU G   67  LYS G   80  1                                  14    
HELIX   90  90 PRO G   96  ASP G  101  5                                   6    
HELIX   91  91 ASP G  103  VAL G  108  1                                   6    
HELIX   92  92 THR G  109  SER G  121  1                                  13    
HELIX   93  93 SER G  121  ARG G  132  1                                  12    
HELIX   94  94 TYR G  146  GLU G  150  5                                   5    
HELIX   95  95 ASN G  157  GLY G  178  1                                  22    
HELIX   96  96 ALA G  196  ILE G  200  5                                   5    
HELIX   97  97 ASP G  202  THR G  214  1                                  13    
HELIX   98  98 THR G  221  CYS G  233  1                                  13    
HELIX   99  99 SER G  234  ALA G  238  5                                   5    
HELIX  100 100 GLY G  250  ILE G  253  5                                   4    
HELIX  101 101 MET G  256  GLU G  260  5                                   5    
HELIX  102 102 SER H   19  GLU H   31  1                                  13    
HELIX  103 103 ASN H   41  LYS H   43  5                                   3    
HELIX  104 104 LEU H   44  LEU H   55  1                                  12    
HELIX  105 105 GLU H   67  GLY H   79  1                                  13    
HELIX  106 106 PRO H   96  ASP H  101  5                                   6    
HELIX  107 107 ASP H  103  VAL H  108  1                                   6    
HELIX  108 108 THR H  109  SER H  121  1                                  13    
HELIX  109 109 SER H  121  ARG H  132  1                                  12    
HELIX  110 110 TYR H  146  GLU H  150  5                                   5    
HELIX  111 111 ASN H  157  GLY H  178  1                                  22    
HELIX  112 112 ALA H  196  ILE H  200  5                                   5    
HELIX  113 113 ASP H  202  THR H  214  1                                  13    
HELIX  114 114 THR H  221  CYS H  233  1                                  13    
HELIX  115 115 SER H  234  ALA H  238  5                                   5    
HELIX  116 116 GLY H  250  ILE H  253  5                                   4    
SHEET    1   A 7 VAL A  60  GLN A  62  0                                        
SHEET    2   A 7 GLU A  34  TYR A  39  1  O  PHE A  37   N  LEU A  61           
SHEET    3   A 7 ARG A   8  VAL A  11  1  N  ILE A   9   O  GLU A  34           
SHEET    4   A 7 PHE A  85  HIS A  90  1  N  ASP A  86   O  ARG A   8           
SHEET    5   A 7 LEU A 135  SER A 145  1  N  ASN A 136   O  PHE A  85           
SHEET    6   A 7 VAL A 182  ALA A 189  1  O  ARG A 183   N  LEU A 141           
SHEET    7   A 7 VAL A 244  VAL A 247  1  N  VAL A 245   O  ALA A 186           
SHEET    1   B 7 VAL B  60  GLN B  62  0                                        
SHEET    2   B 7 GLU B  34  TYR B  39  1  O  PHE B  37   N  LEU B  61           
SHEET    3   B 7 ARG B   8  VAL B  11  1  N  ILE B   9   O  GLU B  34           
SHEET    4   B 7 PHE B  85  HIS B  90  1  N  ASP B  86   O  ARG B   8           
SHEET    5   B 7 LEU B 135  SER B 145  1  N  ASN B 136   O  PHE B  85           
SHEET    6   B 7 VAL B 182  ALA B 189  1  O  ARG B 183   N  LEU B 141           
SHEET    7   B 7 VAL B 244  VAL B 247  1  N  VAL B 245   O  ALA B 186           
SHEET    1   C 7 VAL C  60  GLN C  62  0                                        
SHEET    2   C 7 GLU C  34  TYR C  39  1  O  PHE C  37   N  LEU C  61           
SHEET    3   C 7 ARG C   8  VAL C  11  1  N  ILE C   9   O  GLU C  34           
SHEET    4   C 7 PHE C  85  HIS C  90  1  N  ASP C  86   O  ARG C   8           
SHEET    5   C 7 LEU C 135  SER C 145  1  N  ASN C 136   O  PHE C  85           
SHEET    6   C 7 ARG C 183  ALA C 189  1  O  ARG C 183   N  LEU C 141           
SHEET    7   C 7 VAL C 244  VAL C 247  1  N  VAL C 245   O  ALA C 186           
SHEET    1   D 7 VAL D  60  GLN D  62  0                                        
SHEET    2   D 7 GLU D  34  TYR D  39  1  O  PHE D  37   N  LEU D  61           
SHEET    3   D 7 ARG D   8  VAL D  11  1  N  ILE D   9   O  GLU D  34           
SHEET    4   D 7 PHE D  85  HIS D  90  1  N  ASP D  86   O  ARG D   8           
SHEET    5   D 7 LEU D 135  SER D 145  1  N  ASN D 136   O  PHE D  85           
SHEET    6   D 7 VAL D 182  ALA D 189  1  N  ARG D 183   O  SER D 139           
SHEET    7   D 7 VAL D 244  VAL D 247  1  N  VAL D 245   O  ALA D 186           
SHEET    1   E 7 VAL E  60  GLN E  62  0                                        
SHEET    2   E 7 GLU E  34  TYR E  39  1  O  PHE E  37   N  LEU E  61           
SHEET    3   E 7 ARG E   8  VAL E  11  1  N  ILE E   9   O  GLU E  34           
SHEET    4   E 7 PHE E  85  HIS E  90  1  N  ASP E  86   O  ARG E   8           
SHEET    5   E 7 LEU E 135  SER E 145  1  N  ASN E 136   O  PHE E  85           
SHEET    6   E 7 VAL E 182  ALA E 189  1  O  ARG E 183   N  LEU E 141           
SHEET    7   E 7 VAL E 244  VAL E 247  1  N  VAL E 245   O  ALA E 186           
SHEET    1   F 7 VAL F  60  GLN F  62  0                                        
SHEET    2   F 7 GLU F  34  TYR F  39  1  O  PHE F  37   N  LEU F  61           
SHEET    3   F 7 ARG F   8  VAL F  11  1  N  ILE F   9   O  GLU F  34           
SHEET    4   F 7 PHE F  85  HIS F  90  1  N  ASP F  86   O  ARG F   8           
SHEET    5   F 7 LEU F 135  SER F 145  1  N  ASN F 136   O  PHE F  85           
SHEET    6   F 7 VAL F 182  ALA F 189  1  N  ARG F 183   O  SER F 139           
SHEET    7   F 7 VAL F 244  VAL F 247  1  O  VAL F 245   N  SER F 188           
SHEET    1   G 7 VAL G  60  GLN G  62  0                                        
SHEET    2   G 7 GLU G  34  TYR G  39  1  O  PHE G  37   N  LEU G  61           
SHEET    3   G 7 ARG G   8  VAL G  11  1  N  ILE G   9   O  GLU G  34           
SHEET    4   G 7 PHE G  85  HIS G  90  1  N  ASP G  86   O  ARG G   8           
SHEET    5   G 7 LEU G 135  SER G 145  1  N  ASN G 136   O  PHE G  85           
SHEET    6   G 7 VAL G 182  ALA G 189  1  O  ARG G 183   N  LEU G 141           
SHEET    7   G 7 VAL G 244  VAL G 247  1  N  VAL G 245   O  ALA G 186           
SHEET    1   H 7 VAL H  60  GLN H  62  0                                        
SHEET    2   H 7 GLU H  34  TYR H  39  1  O  PHE H  37   N  LEU H  61           
SHEET    3   H 7 ARG H   8  VAL H  11  1  N  ILE H   9   O  GLU H  34           
SHEET    4   H 7 PHE H  85  HIS H  90  1  N  ASP H  86   O  ARG H   8           
SHEET    5   H 7 LEU H 135  SER H 145  1  N  ASN H 136   O  PHE H  85           
SHEET    6   H 7 VAL H 182  ALA H 189  1  O  ARG H 183   N  LEU H 141           
SHEET    7   H 7 VAL H 244  VAL H 247  1  N  VAL H 245   O  ALA H 186           
SITE     1 AC1 10 GLN A  40  PHE A  94  ILE A 119  NAD A1301                    
SITE     2 AC1 10 HOH A1366  HOH A1378  HOH A1441  HOH A1446                    
SITE     3 AC1 10 HOH A1485  HOH A1487                                          
SITE     1 AC2  6 GLN B  40  PHE B  94  NAD B1304  HOH B1355                    
SITE     2 AC2  6 HOH B1437  HOH B1459                                          
SITE     1 AC3  5 GLN C  40  NAD C1307  HOH C1378  HOH C1393                    
SITE     2 AC3  5 HOH C1482                                                     
SITE     1 AC4  7 GLN D  40  PHE D  94  ILE D 119  NAD D1310                    
SITE     2 AC4  7 HOH D1389  HOH D1408  HOH D1480                               
SITE     1 AC5  6 GLN E  40  NAD E1313  HOH E1392  HOH E1412                    
SITE     2 AC5  6 HOH E1415  HOH E1459                                          
SITE     1 AC6  2 GLN F  40  NAD F1316                                          
SITE     1 AC7  9 GLN G  40  PHE G  94  ILE G 119  NAD G1319                    
SITE     2 AC7  9 HOH G1363  HOH G1405  HOH G1435  HOH G1485                    
SITE     3 AC7  9 HOH G1505                                                     
SITE     1 AC8  4 GLN H  40  PHE H  94  NAD H1322  HOH H1415                    
SITE     1 AC9 28 GLY A  13  ALA A  15  SER A  19  ILE A  20                    
SITE     2 AC9 28 GLN A  40  CYS A  63  ASP A  64  VAL A  65                    
SITE     3 AC9 28 SER A  91  ILE A  92  GLY A  93  LEU A 144                    
SITE     4 AC9 28 SER A 145  LYS A 163  ALA A 189  GLY A 190                    
SITE     5 AC9 28 PRO A 191  ILE A 192  THR A 194  ALA A 196                    
SITE     6 AC9 28 TCL A1302  GLC A1303  HOH A1308  HOH A1309                    
SITE     7 AC9 28 HOH A1321  HOH A1324  HOH A1336  HOH A1371                    
SITE     1 BC1  8 GLY A  93  ALA A  95  LEU A 100  TYR A 146                    
SITE     2 BC1  8 TYR A 156  ALA A 196  ALA A 197  NAD A1301                    
SITE     1 BC2 28 GLY B  13  ALA B  15  SER B  19  ILE B  20                    
SITE     2 BC2 28 GLN B  40  CYS B  63  ASP B  64  VAL B  65                    
SITE     3 BC2 28 SER B  91  ILE B  92  LEU B 144  SER B 145                    
SITE     4 BC2 28 LYS B 163  ALA B 189  GLY B 190  PRO B 191                    
SITE     5 BC2 28 ILE B 192  THR B 194  LEU B 195  ALA B 196                    
SITE     6 BC2 28 TCL B1305  GLC B1306  HOH B1328  HOH B1331                    
SITE     7 BC2 28 HOH B1337  HOH B1344  HOH B1414  HOH B1415                    
SITE     1 BC3  7 GLY B  93  ALA B  95  TYR B 146  TYR B 156                    
SITE     2 BC3  7 ALA B 196  ILE B 200  NAD B1304                               
SITE     1 BC4 26 GLY C  13  ALA C  15  SER C  19  ILE C  20                    
SITE     2 BC4 26 GLN C  40  CYS C  63  ASP C  64  VAL C  65                    
SITE     3 BC4 26 SER C  91  ILE C  92  LEU C 144  SER C 145                    
SITE     4 BC4 26 LYS C 163  ALA C 189  PRO C 191  ILE C 192                    
SITE     5 BC4 26 THR C 194  ALA C 196  TCL C1308  GLC C1309                    
SITE     6 BC4 26 HOH C1317  HOH C1348  HOH C1349  HOH C1353                    
SITE     7 BC4 26 HOH C1383  HOH C1483                                          
SITE     1 BC5  6 GLY C  93  ALA C  95  TYR C 146  TYR C 156                    
SITE     2 BC5  6 ALA C 196  NAD C1307                                          
SITE     1 BC6 27 GLY D  13  ALA D  15  SER D  19  ILE D  20                    
SITE     2 BC6 27 GLN D  40  CYS D  63  ASP D  64  VAL D  65                    
SITE     3 BC6 27 SER D  91  ILE D  92  GLY D  93  LEU D 144                    
SITE     4 BC6 27 SER D 145  LYS D 163  ALA D 189  GLY D 190                    
SITE     5 BC6 27 PRO D 191  ILE D 192  THR D 194  ALA D 196                    
SITE     6 BC6 27 TCL D1311  GLC D1312  HOH D1315  HOH D1322                    
SITE     7 BC6 27 HOH D1329  HOH D1332  HOH D1369                               
SITE     1 BC7  7 GLY D  93  ALA D  95  TYR D 146  TYR D 156                    
SITE     2 BC7  7 ALA D 196  ILE D 200  NAD D1310                               
SITE     1 BC8 30 GLY E  13  ALA E  15  SER E  19  ILE E  20                    
SITE     2 BC8 30 GLN E  40  LEU E  44  CYS E  63  ASP E  64                    
SITE     3 BC8 30 VAL E  65  SER E  91  ILE E  92  LEU E 144                    
SITE     4 BC8 30 SER E 145  TYR E 146  LYS E 163  ALA E 189                    
SITE     5 BC8 30 GLY E 190  PRO E 191  ILE E 192  THR E 194                    
SITE     6 BC8 30 LEU E 195  ALA E 196  TCL E1314  GLC E1315                    
SITE     7 BC8 30 HOH E1330  HOH E1332  HOH E1338  HOH E1341                    
SITE     8 BC8 30 HOH E1343  HOH E1358                                          
SITE     1 BC9  7 GLY E  93  ALA E  95  TYR E 146  TYR E 156                    
SITE     2 BC9  7 ALA E 196  ILE E 200  NAD E1313                               
SITE     1 CC1 27 GLY F  13  ALA F  15  SER F  19  ILE F  20                    
SITE     2 CC1 27 GLN F  40  CYS F  63  ASP F  64  VAL F  65                    
SITE     3 CC1 27 SER F  91  ILE F  92  LEU F 144  SER F 145                    
SITE     4 CC1 27 LYS F 163  ALA F 189  GLY F 190  PRO F 191                    
SITE     5 CC1 27 ILE F 192  THR F 194  ALA F 196  TCL F1317                    
SITE     6 CC1 27 GLC F1318  HOH F1321  HOH F1324  HOH F1344                    
SITE     7 CC1 27 HOH F1357  HOH F1361  HOH F1393                               
SITE     1 CC2  8 GLY F  93  ALA F  95  TYR F 146  TYR F 156                    
SITE     2 CC2  8 ALA F 196  ALA F 197  ILE F 200  NAD F1316                    
SITE     1 CC3 28 GLY G  13  ALA G  15  SER G  19  ILE G  20                    
SITE     2 CC3 28 GLN G  40  CYS G  63  ASP G  64  VAL G  65                    
SITE     3 CC3 28 SER G  91  ILE G  92  GLY G  93  LEU G 144                    
SITE     4 CC3 28 SER G 145  LYS G 163  ALA G 189  GLY G 190                    
SITE     5 CC3 28 PRO G 191  ILE G 192  THR G 194  ALA G 196                    
SITE     6 CC3 28 TCL G1320  GLC G1321  HOH G1330  HOH G1343                    
SITE     7 CC3 28 HOH G1351  HOH G1364  HOH G1366  HOH G1369                    
SITE     1 CC4  9 GLY G  93  ALA G  95  LEU G 100  TYR G 146                    
SITE     2 CC4  9 TYR G 156  ALA G 196  ALA G 197  ILE G 200                    
SITE     3 CC4  9 NAD G1319                                                     
SITE     1 CC5 28 GLY H  13  ALA H  15  SER H  19  ILE H  20                    
SITE     2 CC5 28 GLN H  40  CYS H  63  ASP H  64  VAL H  65                    
SITE     3 CC5 28 SER H  91  ILE H  92  GLY H  93  LEU H 144                    
SITE     4 CC5 28 SER H 145  TYR H 146  LYS H 163  ALA H 189                    
SITE     5 CC5 28 PRO H 191  ILE H 192  THR H 194  ALA H 196                    
SITE     6 CC5 28 TCL H1323  GLC H1324  HOH H1339  HOH H1348                    
SITE     7 CC5 28 HOH H1355  HOH H1385  HOH H1436  HOH H1439                    
SITE     1 CC6  8 GLY H  93  ALA H  95  LEU H 100  TYR H 146                    
SITE     2 CC6  8 TYR H 156  ALA H 196  ALA H 197  NAD H1322                    
CRYST1   73.733   82.077   84.177  89.54  87.43  77.77 P 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      0.013560 -0.002940 -0.000610        0.00000                         
SCALE2      0.000000  0.012470  0.000020        0.00000                         
SCALE3      0.000000  0.000000  0.011890        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system