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Entry: 2PD4
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HEADER    OXIDOREDUCTASE                          31-MAR-07   2PD4              
TITLE     CRYSTAL STRUCTURE OF THE HELICOBACTER PYLORI ENOYL-ACYL               
TITLE    2 CARRIER PROTEIN REDUCTASE IN COMPLEX WITH HYDROXYDIPHENYL            
TITLE    3 ETHER COMPOUNDS, TRICLOSAN AND DICLOSAN                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH];             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: ENOYL-ACYL CARRIER PROTEIN REDUCTASE, NADH-                 
COMPND   5 DEPENDENT ENOYL-ACP REDUCTASE;                                       
COMPND   6 EC: 1.3.1.9;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;                            
SOURCE   3 ORGANISM_TAXID: 210;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET-22B(+)                                
KEYWDS    ANTIBACTERIAL TARGET, HELICOBACTER PYLORI, TYPE II FATTY              
KEYWDS   2 ACID BIOSYNTHESIS, ENOYL-ACP-REDUCTASE, FABI, OXIDOREDUCTASE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.H.LEE,J.H.MOON,S.W.SUH                                              
REVDAT   2   24-JUN-08 2PD4    1       JRNL   VERSN                             
REVDAT   1   17-APR-07 2PD4    0                                                
SPRSDE     17-APR-07 2PD4      1JW7                                             
JRNL        AUTH   H.H.LEE,J.H.MOON,S.W.SUH                                     
JRNL        TITL   CRYSTAL STRUCTURE OF THE HELICOBACTER PYLORI                 
JRNL        TITL 2 ENOYL-ACYL CARRIER PROTEIN REDUCTASE IN COMPLEX              
JRNL        TITL 3 WITH HYDROXYDIPHENYL ETHER COMPOUNDS, TRICLOSAN              
JRNL        TITL 4 AND DICLOSAN                                                 
JRNL        REF    PROTEINS                      V.  69   691 2007              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   17879346                                                     
JRNL        DOI    10.1002/PROT.21586                                           
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 730444.810                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 39424                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3908                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5717                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2820                       
REMARK   3   BIN FREE R VALUE                    : 0.3050                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 597                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8408                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 240                                     
REMARK   3   SOLVENT ATOMS            : 218                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.73000                                              
REMARK   3    B22 (A**2) : -1.87000                                             
REMARK   3    B33 (A**2) : 1.14000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.07000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.30                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.28                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.34                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.32                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 2.54                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.520 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.510 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.140 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.160 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 33.23                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : DCL.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NAD.PARAM                                      
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : DCL.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NAD.PAR                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2PD4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-APR-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB042243.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-DEC-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 6B                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0072                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAC SCIENCE DIP-2030               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39424                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ID CODE 1DFI                                     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM ACETATE BUFFER, PH          
REMARK 280  4.8, 100MM AMMONIUM SULFATE, 23%(W/V) PEG 400, VAPOR                
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 296K                           
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       47.53600            
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: 24960 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -199.0 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     MET A     1                                                      
REMARK 465     MET B     1                                                      
REMARK 465     MET C     1                                                      
REMARK 465     MET D     1                                                      
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    GLU B 274   CB    GLU B 274   CG     -0.269                       
REMARK 500    GLU B 274   C     GLN B 275   N      -0.180                       
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    GLU B 274   CA  -  CB  -  CG  ANGL. DEV. =  23.6 DEGREES          
REMARK 500    GLU B 274   C   -  N   -  CA  ANGL. DEV. =  15.7 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    ASN A  17        1.62    -69.46                                   
REMARK 500    VAL A  65       -6.79    -58.07                                   
REMARK 500    SER A  91       71.74   -119.55                                   
REMARK 500    ALA A  93      143.74   -170.15                                   
REMARK 500    VAL A 120      -60.40   -126.74                                   
REMARK 500    ALA A 153      106.87    -32.42                                   
REMARK 500    HIS A 154       19.07     54.55                                   
REMARK 500    ASN A 156     -122.00     43.98                                   
REMARK 500    ASP A 201       29.14     42.62                                   
REMARK 500    ARG A 216       64.57     38.41                                   
REMARK 500    LYS A 217      162.01    178.58                                   
REMARK 500    VAL A 258      -27.07   -155.24                                   
REMARK 500    GLU A 259      -52.19    -18.89                                   
REMARK 500    ALA A 265      112.30     66.13                                   
REMARK 500    LYS A 273       54.53     36.20                                   
REMARK 500    GLU A 274      133.34    150.85                                   
REMARK 500    ASN B  17        0.24    -64.40                                   
REMARK 500    LEU B  63      104.48   -163.12                                   
REMARK 500    VAL B  65       -6.45    -53.63                                   
REMARK 500    SER B  91       67.23   -117.83                                   
REMARK 500    ALA B 153      110.57    -34.91                                   
REMARK 500    HIS B 154       23.27     49.87                                   
REMARK 500    ASN B 156     -124.03     43.45                                   
REMARK 500    ASP B 201       28.95     42.09                                   
REMARK 500    VAL B 258      -29.30   -154.23                                   
REMARK 500    GLU B 259      -55.19    -17.61                                   
REMARK 500    ALA B 265      112.48     60.18                                   
REMARK 500    LYS B 273       55.54     35.04                                   
REMARK 500    GLU B 274      167.03    154.89                                   
REMARK 500    ASN C  17        2.88    -69.24                                   
REMARK 500    VAL C  65       -9.89    -57.04                                   
REMARK 500    VAL C 120      -57.18   -124.12                                   
REMARK 500    ALA C 153      116.62    -38.48                                   
REMARK 500    HIS C 154       16.51     47.73                                   
REMARK 500    ASN C 156     -124.18     38.02                                   
REMARK 500    LYS C 217      158.09    178.28                                   
REMARK 500    MET C 255     -176.61   -171.70                                   
REMARK 500    VAL C 258      -29.93   -152.74                                   
REMARK 500    GLU C 259      -55.15    -16.45                                   
REMARK 500    ALA C 265      110.24     63.98                                   
REMARK 500    LYS C 273       60.32     39.88                                   
REMARK 500    GLU C 274      141.49    147.76                                   
REMARK 500    ASN D  17        2.28    -66.32                                   
REMARK 500    LEU D  55       31.68    -99.85                                   
REMARK 500    VAL D  65       -8.62    -57.45                                   
REMARK 500    VAL D 120      -57.65   -120.14                                   
REMARK 500    ALA D 153      111.03    -38.51                                   
REMARK 500    ASN D 156     -122.18     47.25                                   
REMARK 500    ASP D 201       28.92     44.45                                   
REMARK 500    VAL D 258      -27.34   -156.56                                   
REMARK 500    GLU D 259      -55.83    -18.35                                   
REMARK 500    ALA D 265      111.03     64.73                                   
REMARK 500    LYS D 273       51.32     39.07                                   
REMARK 500    GLU D 274      123.80    155.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS B  273     GLU B  274                  145.17                    
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 B3450        DISTANCE =  6.40 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 1780                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 2780                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 3780                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 4780                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCN A 2414                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCN B 3414                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCN C 4414                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCN D 5414                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2PD3   RELATED DB: PDB                                   
REMARK 900 TRICLOSAN COMPLEX                                                    
DBREF  2PD4 A    1   275  UNP    O24990   FABI_HELPY       1    275             
DBREF  2PD4 B    1   275  UNP    O24990   FABI_HELPY       1    275             
DBREF  2PD4 C    1   275  UNP    O24990   FABI_HELPY       1    275             
DBREF  2PD4 D    1   275  UNP    O24990   FABI_HELPY       1    275             
SEQRES   1 A  275  MET GLY PHE LEU LYS GLY LYS LYS GLY LEU ILE VAL GLY          
SEQRES   2 A  275  VAL ALA ASN ASN LYS SER ILE ALA TYR GLY ILE ALA GLN          
SEQRES   3 A  275  SER CYS PHE ASN GLN GLY ALA THR LEU ALA PHE THR TYR          
SEQRES   4 A  275  LEU ASN GLU SER LEU GLU LYS ARG VAL ARG PRO ILE ALA          
SEQRES   5 A  275  GLN GLU LEU ASN SER PRO TYR VAL TYR GLU LEU ASP VAL          
SEQRES   6 A  275  SER LYS GLU GLU HIS PHE LYS SER LEU TYR ASN SER VAL          
SEQRES   7 A  275  LYS LYS ASP LEU GLY SER LEU ASP PHE ILE VAL HIS SER          
SEQRES   8 A  275  VAL ALA PHE ALA PRO LYS GLU ALA LEU GLU GLY SER LEU          
SEQRES   9 A  275  LEU GLU THR SER LYS SER ALA PHE ASN THR ALA MET GLU          
SEQRES  10 A  275  ILE SER VAL TYR SER LEU ILE GLU LEU THR ASN THR LEU          
SEQRES  11 A  275  LYS PRO LEU LEU ASN ASN GLY ALA SER VAL LEU THR LEU          
SEQRES  12 A  275  SER TYR LEU GLY SER THR LYS TYR MET ALA HIS TYR ASN          
SEQRES  13 A  275  VAL MET GLY LEU ALA LYS ALA ALA LEU GLU SER ALA VAL          
SEQRES  14 A  275  ARG TYR LEU ALA VAL ASP LEU GLY LYS HIS HIS ILE ARG          
SEQRES  15 A  275  VAL ASN ALA LEU SER ALA GLY PRO ILE ARG THR LEU ALA          
SEQRES  16 A  275  SER SER GLY ILE ALA ASP PHE ARG MET ILE LEU LYS TRP          
SEQRES  17 A  275  ASN GLU ILE ASN ALA PRO LEU ARG LYS ASN VAL SER LEU          
SEQRES  18 A  275  GLU GLU VAL GLY ASN ALA GLY MET TYR LEU LEU SER SER          
SEQRES  19 A  275  LEU SER SER GLY VAL SER GLY GLU VAL HIS PHE VAL ASP          
SEQRES  20 A  275  ALA GLY TYR HIS VAL MET GLY MET GLY ALA VAL GLU GLU          
SEQRES  21 A  275  LYS ASP ASN LYS ALA THR LEU LEU TRP ASP LEU HIS LYS          
SEQRES  22 A  275  GLU GLN                                                      
SEQRES   1 B  275  MET GLY PHE LEU LYS GLY LYS LYS GLY LEU ILE VAL GLY          
SEQRES   2 B  275  VAL ALA ASN ASN LYS SER ILE ALA TYR GLY ILE ALA GLN          
SEQRES   3 B  275  SER CYS PHE ASN GLN GLY ALA THR LEU ALA PHE THR TYR          
SEQRES   4 B  275  LEU ASN GLU SER LEU GLU LYS ARG VAL ARG PRO ILE ALA          
SEQRES   5 B  275  GLN GLU LEU ASN SER PRO TYR VAL TYR GLU LEU ASP VAL          
SEQRES   6 B  275  SER LYS GLU GLU HIS PHE LYS SER LEU TYR ASN SER VAL          
SEQRES   7 B  275  LYS LYS ASP LEU GLY SER LEU ASP PHE ILE VAL HIS SER          
SEQRES   8 B  275  VAL ALA PHE ALA PRO LYS GLU ALA LEU GLU GLY SER LEU          
SEQRES   9 B  275  LEU GLU THR SER LYS SER ALA PHE ASN THR ALA MET GLU          
SEQRES  10 B  275  ILE SER VAL TYR SER LEU ILE GLU LEU THR ASN THR LEU          
SEQRES  11 B  275  LYS PRO LEU LEU ASN ASN GLY ALA SER VAL LEU THR LEU          
SEQRES  12 B  275  SER TYR LEU GLY SER THR LYS TYR MET ALA HIS TYR ASN          
SEQRES  13 B  275  VAL MET GLY LEU ALA LYS ALA ALA LEU GLU SER ALA VAL          
SEQRES  14 B  275  ARG TYR LEU ALA VAL ASP LEU GLY LYS HIS HIS ILE ARG          
SEQRES  15 B  275  VAL ASN ALA LEU SER ALA GLY PRO ILE ARG THR LEU ALA          
SEQRES  16 B  275  SER SER GLY ILE ALA ASP PHE ARG MET ILE LEU LYS TRP          
SEQRES  17 B  275  ASN GLU ILE ASN ALA PRO LEU ARG LYS ASN VAL SER LEU          
SEQRES  18 B  275  GLU GLU VAL GLY ASN ALA GLY MET TYR LEU LEU SER SER          
SEQRES  19 B  275  LEU SER SER GLY VAL SER GLY GLU VAL HIS PHE VAL ASP          
SEQRES  20 B  275  ALA GLY TYR HIS VAL MET GLY MET GLY ALA VAL GLU GLU          
SEQRES  21 B  275  LYS ASP ASN LYS ALA THR LEU LEU TRP ASP LEU HIS LYS          
SEQRES  22 B  275  GLU GLN                                                      
SEQRES   1 C  275  MET GLY PHE LEU LYS GLY LYS LYS GLY LEU ILE VAL GLY          
SEQRES   2 C  275  VAL ALA ASN ASN LYS SER ILE ALA TYR GLY ILE ALA GLN          
SEQRES   3 C  275  SER CYS PHE ASN GLN GLY ALA THR LEU ALA PHE THR TYR          
SEQRES   4 C  275  LEU ASN GLU SER LEU GLU LYS ARG VAL ARG PRO ILE ALA          
SEQRES   5 C  275  GLN GLU LEU ASN SER PRO TYR VAL TYR GLU LEU ASP VAL          
SEQRES   6 C  275  SER LYS GLU GLU HIS PHE LYS SER LEU TYR ASN SER VAL          
SEQRES   7 C  275  LYS LYS ASP LEU GLY SER LEU ASP PHE ILE VAL HIS SER          
SEQRES   8 C  275  VAL ALA PHE ALA PRO LYS GLU ALA LEU GLU GLY SER LEU          
SEQRES   9 C  275  LEU GLU THR SER LYS SER ALA PHE ASN THR ALA MET GLU          
SEQRES  10 C  275  ILE SER VAL TYR SER LEU ILE GLU LEU THR ASN THR LEU          
SEQRES  11 C  275  LYS PRO LEU LEU ASN ASN GLY ALA SER VAL LEU THR LEU          
SEQRES  12 C  275  SER TYR LEU GLY SER THR LYS TYR MET ALA HIS TYR ASN          
SEQRES  13 C  275  VAL MET GLY LEU ALA LYS ALA ALA LEU GLU SER ALA VAL          
SEQRES  14 C  275  ARG TYR LEU ALA VAL ASP LEU GLY LYS HIS HIS ILE ARG          
SEQRES  15 C  275  VAL ASN ALA LEU SER ALA GLY PRO ILE ARG THR LEU ALA          
SEQRES  16 C  275  SER SER GLY ILE ALA ASP PHE ARG MET ILE LEU LYS TRP          
SEQRES  17 C  275  ASN GLU ILE ASN ALA PRO LEU ARG LYS ASN VAL SER LEU          
SEQRES  18 C  275  GLU GLU VAL GLY ASN ALA GLY MET TYR LEU LEU SER SER          
SEQRES  19 C  275  LEU SER SER GLY VAL SER GLY GLU VAL HIS PHE VAL ASP          
SEQRES  20 C  275  ALA GLY TYR HIS VAL MET GLY MET GLY ALA VAL GLU GLU          
SEQRES  21 C  275  LYS ASP ASN LYS ALA THR LEU LEU TRP ASP LEU HIS LYS          
SEQRES  22 C  275  GLU GLN                                                      
SEQRES   1 D  275  MET GLY PHE LEU LYS GLY LYS LYS GLY LEU ILE VAL GLY          
SEQRES   2 D  275  VAL ALA ASN ASN LYS SER ILE ALA TYR GLY ILE ALA GLN          
SEQRES   3 D  275  SER CYS PHE ASN GLN GLY ALA THR LEU ALA PHE THR TYR          
SEQRES   4 D  275  LEU ASN GLU SER LEU GLU LYS ARG VAL ARG PRO ILE ALA          
SEQRES   5 D  275  GLN GLU LEU ASN SER PRO TYR VAL TYR GLU LEU ASP VAL          
SEQRES   6 D  275  SER LYS GLU GLU HIS PHE LYS SER LEU TYR ASN SER VAL          
SEQRES   7 D  275  LYS LYS ASP LEU GLY SER LEU ASP PHE ILE VAL HIS SER          
SEQRES   8 D  275  VAL ALA PHE ALA PRO LYS GLU ALA LEU GLU GLY SER LEU          
SEQRES   9 D  275  LEU GLU THR SER LYS SER ALA PHE ASN THR ALA MET GLU          
SEQRES  10 D  275  ILE SER VAL TYR SER LEU ILE GLU LEU THR ASN THR LEU          
SEQRES  11 D  275  LYS PRO LEU LEU ASN ASN GLY ALA SER VAL LEU THR LEU          
SEQRES  12 D  275  SER TYR LEU GLY SER THR LYS TYR MET ALA HIS TYR ASN          
SEQRES  13 D  275  VAL MET GLY LEU ALA LYS ALA ALA LEU GLU SER ALA VAL          
SEQRES  14 D  275  ARG TYR LEU ALA VAL ASP LEU GLY LYS HIS HIS ILE ARG          
SEQRES  15 D  275  VAL ASN ALA LEU SER ALA GLY PRO ILE ARG THR LEU ALA          
SEQRES  16 D  275  SER SER GLY ILE ALA ASP PHE ARG MET ILE LEU LYS TRP          
SEQRES  17 D  275  ASN GLU ILE ASN ALA PRO LEU ARG LYS ASN VAL SER LEU          
SEQRES  18 D  275  GLU GLU VAL GLY ASN ALA GLY MET TYR LEU LEU SER SER          
SEQRES  19 D  275  LEU SER SER GLY VAL SER GLY GLU VAL HIS PHE VAL ASP          
SEQRES  20 D  275  ALA GLY TYR HIS VAL MET GLY MET GLY ALA VAL GLU GLU          
SEQRES  21 D  275  LYS ASP ASN LYS ALA THR LEU LEU TRP ASP LEU HIS LYS          
SEQRES  22 D  275  GLU GLN                                                      
HET    NAD  A1780      44                                                       
HET    NAD  B2780      44                                                       
HET    NAD  C3780      44                                                       
HET    NAD  D4780      44                                                       
HET    DCN  A2414      16                                                       
HET    DCN  B3414      16                                                       
HET    DCN  C4414      16                                                       
HET    DCN  D5414      16                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     DCN DICLOSAN                                                         
FORMUL   5  NAD    4(C21 H27 N7 O14 P2)                                         
FORMUL   9  DCN    4(C12 H8 CL2 O2)                                             
FORMUL  13  HOH   *218(H2 O)                                                    
HELIX    1   1 SER A   19  ASN A   30  1                                  12    
HELIX    2   2 LEU A   44  LEU A   55  1                                  12    
HELIX    3   3 LYS A   67  LEU A   82  1                                  16    
HELIX    4   4 PRO A   96  GLU A  101  5                                   6    
HELIX    5   5 SER A  103  THR A  107  5                                   5    
HELIX    6   6 SER A  108  VAL A  120  1                                  13    
HELIX    7   7 VAL A  120  LYS A  131  1                                  12    
HELIX    8   8 TYR A  145  THR A  149  5                                   5    
HELIX    9   9 TYR A  155  LYS A  178  1                                  24    
HELIX   10  10 ALA A  195  ILE A  199  5                                   5    
HELIX   11  11 ASP A  201  ALA A  213  1                                  13    
HELIX   12  12 SER A  220  SER A  233  1                                  14    
HELIX   13  13 SER A  234  SER A  237  5                                   4    
HELIX   14  14 GLY A  249  MET A  253  5                                   5    
HELIX   15  15 LEU A  267  HIS A  272  1                                   6    
HELIX   16  16 SER B   19  ASN B   30  1                                  12    
HELIX   17  17 ASN B   41  LEU B   55  1                                  15    
HELIX   18  18 LYS B   67  LEU B   82  1                                  16    
HELIX   19  19 SER B  103  THR B  107  5                                   5    
HELIX   20  20 SER B  108  VAL B  120  1                                  13    
HELIX   21  21 VAL B  120  LYS B  131  1                                  12    
HELIX   22  22 TYR B  145  THR B  149  5                                   5    
HELIX   23  23 TYR B  155  LYS B  178  1                                  24    
HELIX   24  24 ALA B  195  ILE B  199  5                                   5    
HELIX   25  25 ASP B  201  ALA B  213  1                                  13    
HELIX   26  26 SER B  220  SER B  233  1                                  14    
HELIX   27  27 SER B  234  SER B  237  5                                   4    
HELIX   28  28 GLY B  249  MET B  253  5                                   5    
HELIX   29  29 LEU B  267  HIS B  272  1                                   6    
HELIX   30  30 SER C   19  ASN C   30  1                                  12    
HELIX   31  31 ASN C   41  LEU C   55  1                                  15    
HELIX   32  32 LYS C   67  LEU C   82  1                                  16    
HELIX   33  33 PRO C   96  GLU C  101  5                                   6    
HELIX   34  34 SER C  103  THR C  107  5                                   5    
HELIX   35  35 SER C  108  VAL C  120  1                                  13    
HELIX   36  36 VAL C  120  LYS C  131  1                                  12    
HELIX   37  37 TYR C  145  THR C  149  5                                   5    
HELIX   38  38 TYR C  155  LYS C  178  1                                  24    
HELIX   39  39 ALA C  195  ILE C  199  5                                   5    
HELIX   40  40 ASP C  201  ALA C  213  1                                  13    
HELIX   41  41 SER C  220  SER C  233  1                                  14    
HELIX   42  42 SER C  234  SER C  237  5                                   4    
HELIX   43  43 GLY C  249  MET C  253  5                                   5    
HELIX   44  44 LEU C  267  HIS C  272  1                                   6    
HELIX   45  45 SER D   19  ASN D   30  1                                  12    
HELIX   46  46 ASN D   41  LEU D   55  1                                  15    
HELIX   47  47 LYS D   67  LEU D   82  1                                  16    
HELIX   48  48 SER D  103  THR D  107  5                                   5    
HELIX   49  49 SER D  108  VAL D  120  1                                  13    
HELIX   50  50 VAL D  120  LYS D  131  1                                  12    
HELIX   51  51 TYR D  145  THR D  149  5                                   5    
HELIX   52  52 TYR D  155  LYS D  178  1                                  24    
HELIX   53  53 THR D  193  GLY D  198  1                                   6    
HELIX   54  54 ASP D  201  ALA D  213  1                                  13    
HELIX   55  55 SER D  220  SER D  233  1                                  14    
HELIX   56  56 SER D  234  SER D  237  5                                   4    
HELIX   57  57 GLY D  249  MET D  253  5                                   5    
HELIX   58  58 LEU D  267  HIS D  272  1                                   6    
SHEET    1   A 7 VAL A  60  GLU A  62  0                                        
SHEET    2   A 7 THR A  34  TYR A  39  1  N  PHE A  37   O  TYR A  61           
SHEET    3   A 7 LYS A   8  VAL A  12  1  N  ILE A  11   O  ALA A  36           
SHEET    4   A 7 LEU A  85  HIS A  90  1  O  ASP A  86   N  LYS A   8           
SHEET    5   A 7 LEU A 134  SER A 144  1  O  LEU A 141   N  HIS A  90           
SHEET    6   A 7 ARG A 182  ALA A 188  1  O  ARG A 182   N  ALA A 138           
SHEET    7   A 7 VAL A 243  VAL A 246  1  O  HIS A 244   N  SER A 187           
SHEET    1   B 7 VAL B  60  GLU B  62  0                                        
SHEET    2   B 7 THR B  34  TYR B  39  1  N  PHE B  37   O  TYR B  61           
SHEET    3   B 7 LYS B   8  VAL B  12  1  N  ILE B  11   O  ALA B  36           
SHEET    4   B 7 LEU B  85  HIS B  90  1  O  ASP B  86   N  LYS B   8           
SHEET    5   B 7 LEU B 134  SER B 144  1  O  LEU B 141   N  HIS B  90           
SHEET    6   B 7 ARG B 182  ALA B 188  1  O  ARG B 182   N  VAL B 140           
SHEET    7   B 7 VAL B 243  VAL B 246  1  O  HIS B 244   N  SER B 187           
SHEET    1   C 7 VAL C  60  GLU C  62  0                                        
SHEET    2   C 7 THR C  34  TYR C  39  1  N  PHE C  37   O  TYR C  61           
SHEET    3   C 7 LYS C   8  VAL C  12  1  N  ILE C  11   O  ALA C  36           
SHEET    4   C 7 LEU C  85  HIS C  90  1  O  ASP C  86   N  LYS C   8           
SHEET    5   C 7 LEU C 134  SER C 144  1  O  LEU C 141   N  HIS C  90           
SHEET    6   C 7 ARG C 182  ALA C 188  1  O  ARG C 182   N  VAL C 140           
SHEET    7   C 7 VAL C 243  VAL C 246  1  O  HIS C 244   N  SER C 187           
SHEET    1   D 7 VAL D  60  GLU D  62  0                                        
SHEET    2   D 7 THR D  34  TYR D  39  1  N  PHE D  37   O  TYR D  61           
SHEET    3   D 7 LYS D   8  VAL D  12  1  N  ILE D  11   O  ALA D  36           
SHEET    4   D 7 LEU D  85  HIS D  90  1  O  ASP D  86   N  LYS D   8           
SHEET    5   D 7 LEU D 134  SER D 144  1  O  LEU D 141   N  HIS D  90           
SHEET    6   D 7 ARG D 182  ALA D 188  1  O  ARG D 182   N  VAL D 140           
SHEET    7   D 7 VAL D 243  VAL D 246  1  O  HIS D 244   N  SER D 187           
SITE     1 AC1 26 GLY A  13  VAL A  14  ALA A  15  SER A  19                    
SITE     2 AC1 26 ILE A  20  LEU A  40  LEU A  44  LEU A  63                    
SITE     3 AC1 26 ASP A  64  VAL A  65  SER A  91  VAL A  92                    
SITE     4 AC1 26 ALA A  93  ILE A 118  SER A 144  LYS A 162                    
SITE     5 AC1 26 ALA A 188  GLY A 189  PRO A 190  ILE A 191                    
SITE     6 AC1 26 THR A 193  ALA A 195  PHE A 202  DCN A2414                    
SITE     7 AC1 26 HOH A2434  HOH A2444                                          
SITE     1 AC2 27 GLY B  13  VAL B  14  ALA B  15  SER B  19                    
SITE     2 AC2 27 ILE B  20  LEU B  40  LEU B  44  LEU B  63                    
SITE     3 AC2 27 ASP B  64  VAL B  65  SER B  91  VAL B  92                    
SITE     4 AC2 27 ALA B  93  LEU B 143  SER B 144  TYR B 145                    
SITE     5 AC2 27 LYS B 162  GLY B 189  PRO B 190  ILE B 191                    
SITE     6 AC2 27 THR B 193  ALA B 195  DCN B3414  HOH B3415                    
SITE     7 AC2 27 HOH B3417  HOH B3443  HOH B3467                               
SITE     1 AC3 26 GLY C  13  VAL C  14  ALA C  15  SER C  19                    
SITE     2 AC3 26 ILE C  20  LEU C  40  LEU C  44  LEU C  63                    
SITE     3 AC3 26 ASP C  64  VAL C  65  SER C  91  VAL C  92                    
SITE     4 AC3 26 ALA C  93  LEU C 143  SER C 144  TYR C 145                    
SITE     5 AC3 26 LYS C 162  ALA C 188  GLY C 189  PRO C 190                    
SITE     6 AC3 26 ILE C 191  THR C 193  LEU C 194  ALA C 195                    
SITE     7 AC3 26 DCN C4414  HOH C4428                                          
SITE     1 AC4 28 GLY D  13  ALA D  15  SER D  19  ILE D  20                    
SITE     2 AC4 28 LEU D  40  LEU D  44  LEU D  63  ASP D  64                    
SITE     3 AC4 28 VAL D  65  SER D  91  VAL D  92  ALA D  93                    
SITE     4 AC4 28 ILE D 118  LEU D 143  SER D 144  TYR D 145                    
SITE     5 AC4 28 LYS D 162  ALA D 188  GLY D 189  PRO D 190                    
SITE     6 AC4 28 ILE D 191  THR D 193  LEU D 194  ALA D 195                    
SITE     7 AC4 28 PHE D 202  DCN D5414  HOH D5419  HOH D5424                    
SITE     1 AC5 10 ALA A  93  ALA A  95  LEU A 100  TYR A 145                    
SITE     2 AC5 10 TYR A 155  MET A 158  ALA A 195  ILE A 199                    
SITE     3 AC5 10 PHE A 202  NAD A1780                                          
SITE     1 AC6 11 ALA B  93  PHE B  94  ALA B  95  LEU B 100                    
SITE     2 AC6 11 TYR B 145  TYR B 155  MET B 158  ALA B 195                    
SITE     3 AC6 11 ILE B 199  PHE B 202  NAD B2780                               
SITE     1 AC7 11 ALA C  93  PHE C  94  ALA C  95  LEU C 100                    
SITE     2 AC7 11 TYR C 145  TYR C 155  MET C 158  ALA C 195                    
SITE     3 AC7 11 ILE C 199  PHE C 202  NAD C3780                               
SITE     1 AC8 10 ALA D  93  ALA D  95  LEU D 100  TYR D 145                    
SITE     2 AC8 10 TYR D 155  MET D 158  ALA D 195  ILE D 199                    
SITE     3 AC8 10 PHE D 202  NAD D4780                                          
CRYST1   73.253   95.072   75.019  90.00 106.53  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      0.013651  0.000000  0.004051        0.00000                         
SCALE2      0.000000  0.010518  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013905        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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