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Database: PDB
Entry: 5FWG
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HEADER    TRANSFERASE                             08-NOV-97   5FWG              
TITLE     TETRA-(5-FLUOROTRYPTOPHANYL)-GLUTATHIONE TRANSFERASE                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TETRA-(5-FLUOROTRYPTOPHANYL)-GLUTATHIONE                   
COMPND   3 TRANSFERASE MU CLASS;                                                
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: RAT MU CLASS GST, RAT M1-1 GST;                             
COMPND   6 EC: 2.5.1.18;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 CELL_LINE: BL21;                                                     
SOURCE   6 ORGAN: LIVER;                                                        
SOURCE   7 GENE: CDNA INSERT OF 3-3 (M1-1) ENZY;                                
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PSW1GST33;                                
SOURCE  13 EXPRESSION_SYSTEM_GENE: CDNA INSERT OF 3-3 (M1-1) ENZYME             
KEYWDS    GLUTATHIONE TRANSFERASE, UNNATURAL AMINO ACID, 5-                     
KEYWDS   2 FLUOROTRYPTOPHAN, THREE-DIMENSIONAL STRUCTURE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.F.PARSONS,G.XIAO,R.N.ARMSTRONG,G.L.GILLILAND                        
REVDAT   3   24-FEB-09 5FWG    1       VERSN                                    
REVDAT   2   02-SEP-08 5FWG    1       JRNL                                     
REVDAT   1   27-JAN-99 5FWG    0                                                
JRNL        AUTH   J.F.PARSONS,G.XIAO,G.L.GILLILAND,R.N.ARMSTRONG               
JRNL        TITL   ENZYMES HARBORING UNNATURAL AMINO ACIDS:                     
JRNL        TITL 2 MECHANISTIC AND STRUCTURAL ANALYSIS OF THE                   
JRNL        TITL 3 ENHANCED CATALYTIC ACTIVITY OF A GLUTATHIONE                 
JRNL        TITL 4 TRANSFERASE CONTAINING 5-FLUOROTRYPTOPHAN.                   
JRNL        REF    BIOCHEMISTRY                  V.  37  6286 1998              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   9572843                                                      
JRNL        DOI    10.1021/BI980219E                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.W.JOHNSON,S.LIU,X.JI,G.L.GILLILAND,R.N.ARMSTRONG           
REMARK   1  TITL   TYROSINE 115 PARTICIPATES BOTH IN CHEMICAL AND               
REMARK   1  TITL 2 PHYSICAL STEPS OF THE CATALYTIC MECHANISM OF A               
REMARK   1  TITL 3 GLUTATHIONE S-TRANSFERASE                                    
REMARK   1  REF    J.BIOL.CHEM.                  V. 268 11508 1993              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   S.LIU,P.ZHANG,X.JI,W.W.JOHNSON,G.L.GILLILAND,                
REMARK   1  AUTH 2 R.N.ARMSTRONG                                                
REMARK   1  TITL   CONTRIBUTION OF TYROSINE 6 TO THE CATALYTIC                  
REMARK   1  TITL 2 MECHANISM OF ISOENZYME 3-3 OF GLUTATHIONE                    
REMARK   1  TITL 3 S-TRANSFERASE                                                
REMARK   1  REF    J.BIOL.CHEM.                  V. 267  4296 1992              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   X.JI,P.ZHANG,R.N.ARMSTRONG,G.L.GILLILAND                     
REMARK   1  TITL   THE THREE-DIMENSIONAL STRUCTURE OF A GLUTATHIONE             
REMARK   1  TITL 2 S-TRANSFERASE FROM THE MU GENE CLASS. STRUCTURAL             
REMARK   1  TITL 3 ANALYSIS OF THE BINARY COMPLEX OF ISOENZYME 3-3              
REMARK   1  TITL 4 AND GLUTATHIONE AT 2.2-A RESOLUTION                          
REMARK   1  REF    BIOCHEMISTRY                  V.  31 10169 1992              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT V. 5-E, X-PLOR                                   
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 65.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 28281                          
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3644                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 371                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : 27.800                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.017 ; 0.800 ; 3856            
REMARK   3   BOND ANGLES            (DEGREES) : 3.000 ; 1.200 ; 5154            
REMARK   3   TORSION ANGLES         (DEGREES) : 19.530; 0.000 ; 2296            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : 0.013 ; 1.500 ; 112             
REMARK   3   GENERAL PLANES               (A) : 0.016 ; 4.000 ; 534             
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : 7.089 ; 1.000 ; 3702            
REMARK   3   NON-BONDED CONTACTS          (A) : 0.023 ; 10.000; 154             
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : BABINET SCALING                                      
REMARK   3   KSOL        : 0.81                                                 
REMARK   3   BSOL        : 71.40                                                
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : TNT PROTGEO                                      
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : TNT BCORREL V1.0             
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5FWG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-APR-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 103                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : YALE MIRRORS                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 184888                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 65.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 5.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY                : 6.240                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 68.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.13700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 15.000                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR MODIFICATION       
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3GST                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.6                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       43.46950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.37350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       43.46950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.37350            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   828     O    HOH B   828     2655     1.95            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  28   CD    GLU A  28   OE2     0.068                       
REMARK 500    GLU A  29   CD    GLU A  29   OE2     0.077                       
REMARK 500    GLU A  48   CD    GLU A  48   OE2     0.069                       
REMARK 500    GLU A  88   CD    GLU A  88   OE2     0.072                       
REMARK 500    GLU A 120   CD    GLU A 120   OE2     0.084                       
REMARK 500    GLU A 125   CD    GLU A 125   OE2     0.076                       
REMARK 500    GLU A 132   CD    GLU A 132   OE2     0.079                       
REMARK 500    GLU A 139   CD    GLU A 139   OE2     0.086                       
REMARK 500    GLU A 170   CD    GLU A 170   OE2     0.083                       
REMARK 500    GLU B  21   CD    GLU B  21   OE2     0.125                       
REMARK 500    GLU B  28   CD    GLU B  28   OE2     0.067                       
REMARK 500    GLU B  48   CD    GLU B  48   OE2     0.067                       
REMARK 500    GLU B  91   CD    GLU B  91   OE2     0.069                       
REMARK 500    GLU B 125   CD    GLU B 125   OE2     0.066                       
REMARK 500    GLU B 132   CD    GLU B 132   OE2     0.077                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  10   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ASP A  24   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A  24   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ASP A  36   CB  -  CG  -  OD1 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ASP A  36   CB  -  CG  -  OD2 ANGL. DEV. =  -8.7 DEGREES          
REMARK 500    ASP A  39   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP A  39   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    ASN A  47   N   -  CA  -  CB  ANGL. DEV. =  10.8 DEGREES          
REMARK 500    ASP A  55   CB  -  CG  -  OD1 ANGL. DEV. =  11.3 DEGREES          
REMARK 500    ASP A  55   CB  -  CG  -  OD2 ANGL. DEV. = -15.0 DEGREES          
REMARK 500    ARG A  67   CD  -  NE  -  CZ  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    ARG A  67   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG A  81   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG A  93   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A  95   CD  -  NE  -  CZ  ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ARG A  95   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG A  95   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ASP A  97   CB  -  CG  -  OD1 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ASP A  97   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    ASP A 105   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP A 105   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG A 144   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A 144   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    ASP A 150   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP A 156   CB  -  CG  -  OD1 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ASP A 156   CB  -  CG  -  OD2 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ASP A 175   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A 182   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP A 182   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG A 201   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ASN B   8   N   -  CA  -  CB  ANGL. DEV. = -15.5 DEGREES          
REMARK 500    ARG B  10   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG B  17   NE  -  CZ  -  NH1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG B  17   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    GLU B  21   CB  -  CG  -  CD  ANGL. DEV. =  17.0 DEGREES          
REMARK 500    ASP B  24   CB  -  CG  -  OD1 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ASP B  24   CB  -  CG  -  OD2 ANGL. DEV. =  -8.3 DEGREES          
REMARK 500    SER B  25   N   -  CA  -  CB  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    PRO B  38   C   -  N   -  CD  ANGL. DEV. = -14.3 DEGREES          
REMARK 500    ASP B  39   CB  -  CG  -  OD2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ASP B  41   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    THR B  70   N   -  CA  -  CB  ANGL. DEV. =  12.3 DEGREES          
REMARK 500    ASP B  97   CB  -  CG  -  OD1 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG B 107   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP B 118   CB  -  CG  -  OD1 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ASP B 118   CB  -  CG  -  OD2 ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    ASP B 150   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    CYS B 173   CB  -  CA  -  C   ANGL. DEV. =   8.3 DEGREES          
REMARK 500    ASP B 182   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B 182   CB  -  CG  -  OD2 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  41      133.68    -37.24                                   
REMARK 500    PRO A  57      130.35    -37.61                                   
REMARK 500    ASN A  58     -178.46   -174.74                                   
REMARK 500    GLN A  71      113.36     69.97                                   
REMARK 500    CYS A 173       -8.80    -52.00                                   
REMARK 500    LYS A 191      -53.37    -27.05                                   
REMARK 500    ASP B  36     -146.90    -79.28                                   
REMARK 500    TYR B  40       57.35     74.13                                   
REMARK 500    ASP B  41      145.68    -30.63                                   
REMARK 500    GLN B  71      108.56     82.93                                   
REMARK 500    LYS B 123      -58.07    167.69                                   
REMARK 500    CYS B 173      -34.88    -32.45                                   
REMARK 500    LYS B 191      -80.54    -14.79                                   
REMARK 500    ALA B 212     -140.99    -14.64                                   
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 B 609        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH B 716        DISTANCE =  6.49 ANGSTROMS                       
REMARK 525    HOH B 718        DISTANCE =  7.30 ANGSTROMS                       
REMARK 525    HOH A 827        DISTANCE =  7.19 ANGSTROMS                       
REMARK 525    HOH A 837        DISTANCE =  7.52 ANGSTROMS                       
REMARK 525    HOH B 802        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH B 803        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH B 810        DISTANCE =  7.25 ANGSTROMS                       
REMARK 525    HOH B 821        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH B 854        DISTANCE =  6.42 ANGSTROMS                       
REMARK 525    HOH B 857        DISTANCE =  5.66 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: GPS                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE DEFINED LARGELY BY THESE RESIDUES.     
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GPR A 218                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GPR B 218                 
DBREF  5FWG A    1   217  UNP    P04905   GSTM1_RAT        1    217             
DBREF  5FWG B    1   217  UNP    P04905   GSTM1_RAT        1    217             
SEQADV 5FWG FTR A    7  UNP  P04905    TRP     7 CONFLICT                       
SEQADV 5FWG FTR A   45  UNP  P04905    TRP    45 CONFLICT                       
SEQADV 5FWG FTR A  146  UNP  P04905    TRP   146 CONFLICT                       
SEQADV 5FWG FTR A  214  UNP  P04905    TRP   214 CONFLICT                       
SEQADV 5FWG FTR B    7  UNP  P04905    TRP     7 CONFLICT                       
SEQADV 5FWG FTR B   45  UNP  P04905    TRP    45 CONFLICT                       
SEQADV 5FWG FTR B  146  UNP  P04905    TRP   146 CONFLICT                       
SEQADV 5FWG FTR B  214  UNP  P04905    TRP   214 CONFLICT                       
SEQRES   1 A  217  PRO MET ILE LEU GLY TYR FTR ASN VAL ARG GLY LEU THR          
SEQRES   2 A  217  HIS PRO ILE ARG LEU LEU LEU GLU TYR THR ASP SER SER          
SEQRES   3 A  217  TYR GLU GLU LYS ARG TYR ALA MET GLY ASP ALA PRO ASP          
SEQRES   4 A  217  TYR ASP ARG SER GLN FTR LEU ASN GLU LYS PHE LYS LEU          
SEQRES   5 A  217  GLY LEU ASP PHE PRO ASN LEU PRO TYR LEU ILE ASP GLY          
SEQRES   6 A  217  SER ARG LYS ILE THR GLN SER ASN ALA ILE MET ARG TYR          
SEQRES   7 A  217  LEU ALA ARG LYS HIS HIS LEU CYS GLY GLU THR GLU GLU          
SEQRES   8 A  217  GLU ARG ILE ARG ALA ASP ILE VAL GLU ASN GLN VAL MET          
SEQRES   9 A  217  ASP ASN ARG MET GLN LEU ILE MET LEU CYS TYR ASN PRO          
SEQRES  10 A  217  ASP PHE GLU LYS GLN LYS PRO GLU PHE LEU LYS THR ILE          
SEQRES  11 A  217  PRO GLU LYS MET LYS LEU TYR SER GLU PHE LEU GLY LYS          
SEQRES  12 A  217  ARG PRO FTR PHE ALA GLY ASP LYS VAL THR TYR VAL ASP          
SEQRES  13 A  217  PHE LEU ALA TYR ASP ILE LEU ASP GLN TYR HIS ILE PHE          
SEQRES  14 A  217  GLU PRO LYS CYS LEU ASP ALA PHE PRO ASN LEU LYS ASP          
SEQRES  15 A  217  PHE LEU ALA ARG PHE GLU GLY LEU LYS LYS ILE SER ALA          
SEQRES  16 A  217  TYR MET LYS SER SER ARG TYR LEU SER THR PRO ILE PHE          
SEQRES  17 A  217  SER LYS LEU ALA GLN FTR SER ASN LYS                          
SEQRES   1 B  217  PRO MET ILE LEU GLY TYR FTR ASN VAL ARG GLY LEU THR          
SEQRES   2 B  217  HIS PRO ILE ARG LEU LEU LEU GLU TYR THR ASP SER SER          
SEQRES   3 B  217  TYR GLU GLU LYS ARG TYR ALA MET GLY ASP ALA PRO ASP          
SEQRES   4 B  217  TYR ASP ARG SER GLN FTR LEU ASN GLU LYS PHE LYS LEU          
SEQRES   5 B  217  GLY LEU ASP PHE PRO ASN LEU PRO TYR LEU ILE ASP GLY          
SEQRES   6 B  217  SER ARG LYS ILE THR GLN SER ASN ALA ILE MET ARG TYR          
SEQRES   7 B  217  LEU ALA ARG LYS HIS HIS LEU CYS GLY GLU THR GLU GLU          
SEQRES   8 B  217  GLU ARG ILE ARG ALA ASP ILE VAL GLU ASN GLN VAL MET          
SEQRES   9 B  217  ASP ASN ARG MET GLN LEU ILE MET LEU CYS TYR ASN PRO          
SEQRES  10 B  217  ASP PHE GLU LYS GLN LYS PRO GLU PHE LEU LYS THR ILE          
SEQRES  11 B  217  PRO GLU LYS MET LYS LEU TYR SER GLU PHE LEU GLY LYS          
SEQRES  12 B  217  ARG PRO FTR PHE ALA GLY ASP LYS VAL THR TYR VAL ASP          
SEQRES  13 B  217  PHE LEU ALA TYR ASP ILE LEU ASP GLN TYR HIS ILE PHE          
SEQRES  14 B  217  GLU PRO LYS CYS LEU ASP ALA PHE PRO ASN LEU LYS ASP          
SEQRES  15 B  217  PHE LEU ALA ARG PHE GLU GLY LEU LYS LYS ILE SER ALA          
SEQRES  16 B  217  TYR MET LYS SER SER ARG TYR LEU SER THR PRO ILE PHE          
SEQRES  17 B  217  SER LYS LEU ALA GLN FTR SER ASN LYS                          
MODRES 5FWG FTR A    7  TRP  FLUOROTRYPTOPHANE                                  
MODRES 5FWG FTR A   45  TRP  FLUOROTRYPTOPHANE                                  
MODRES 5FWG FTR A  146  TRP  FLUOROTRYPTOPHANE                                  
MODRES 5FWG FTR A  214  TRP  FLUOROTRYPTOPHANE                                  
MODRES 5FWG FTR B    7  TRP  FLUOROTRYPTOPHANE                                  
MODRES 5FWG FTR B   45  TRP  FLUOROTRYPTOPHANE                                  
MODRES 5FWG FTR B  146  TRP  FLUOROTRYPTOPHANE                                  
MODRES 5FWG FTR B  214  TRP  FLUOROTRYPTOPHANE                                  
HET    FTR  A   7      15                                                       
HET    FTR  A  45      15                                                       
HET    FTR  A 146      15                                                       
HET    FTR  A 214      15                                                       
HET    FTR  B   7      15                                                       
HET    FTR  B  45      15                                                       
HET    FTR  B 146      15                                                       
HET    FTR  B 214      15                                                       
HET    GPR  A 218      35                                                       
HET    GPR  B 218      35                                                       
HETNAM     FTR FLUOROTRYPTOPHANE                                                
HETNAM     GPR (9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-                     
HETNAM   2 GPR  DIHYDROPHENANTHRENE                                             
FORMUL   1  FTR    8(C11 H11 F N2 O2)                                           
FORMUL   3  GPR    2(C24 H27 N3 O7 S)                                           
FORMUL   5  HOH   *371(H2 O)                                                    
HELIX    1 H1A HIS A   14  TYR A   22  1                                   9    
HELIX    2 H2A SER A   43  LEU A   46  1                                   4    
HELIX    3 H3A SER A   72  LYS A   82  1                                  11    
HELIX    4 H4A GLU A   90  CYS A  114  1                                  25    
HELIX    5 H5A PHE A  119  LYS A  128  1                                  10    
HELIX    6 H6A ILE A  130  LEU A  141  1                                  12    
HELIX    7 H7A VAL A  155  PHE A  169  1                                  15    
HELIX    8 H8A PRO A  178  GLU A  188  1                                  11    
HELIX    9 H9A LYS A  191  TYR A  196  1                                   6    
HELIX   10 H1B HIS B   14  TYR B   22  1                                   9    
HELIX   11 H2B SER B   43  LEU B   46  1                                   4    
HELIX   12  HA LYS B   49  LYS B   51  5                                   3    
HELIX   13 H3B SER B   72  HIS B   83  1                                  12    
HELIX   14 H4B GLU B   90  CYS B  114  1                                  25    
HELIX   15 H5B PHE B  119  LYS B  128  1                                  10    
HELIX   16 H6B ILE B  130  LEU B  141  1                                  12    
HELIX   17 H7B TYR B  154  PHE B  169  1                                  16    
HELIX   18 H8B PRO B  178  GLU B  188  1                                  11    
HELIX   19 H9B LYS B  191  MET B  197  1                                   7    
SHEET    1 S1A 4 TYR A  27  TYR A  32  0                                        
SHEET    2 S1A 4 MET A   2  FTR A   7  1  O  MET A   2   N  GLU A  28           
SHEET    3 S1A 4 TYR A  61  ASP A  64 -1  O  ILE A  63   N  ILE A   3           
SHEET    4 S1A 4 ARG A  67  THR A  70 -1  O  ARG A  67   N  ASP A  64           
SHEET    1 S1B 4 TYR B  27  TYR B  32  0                                        
SHEET    2 S1B 4 MET B   2  FTR B   7  1  O  MET B   2   N  GLU B  28           
SHEET    3 S1B 4 TYR B  61  ASP B  64 -1  O  ILE B  63   N  ILE B   3           
SHEET    4 S1B 4 ARG B  67  THR B  70 -1  O  ARG B  67   N  ASP B  64           
LINK         N   FTR A   7                 C   TYR A   6     1555   1555  1.31  
LINK         C   FTR A   7                 N   ASN A   8     1555   1555  1.30  
LINK         N   FTR A  45                 C   GLN A  44     1555   1555  1.30  
LINK         C   FTR A  45                 N   LEU A  46     1555   1555  1.31  
LINK         N   FTR A 146                 C   PRO A 145     1555   1555  1.36  
LINK         C   FTR A 146                 N   PHE A 147     1555   1555  1.33  
LINK         N   FTR A 214                 C   GLN A 213     1555   1555  1.34  
LINK         C   FTR A 214                 N   SER A 215     1555   1555  1.33  
LINK         N   FTR B   7                 C   TYR B   6     1555   1555  1.32  
LINK         C   FTR B   7                 N   ASN B   8     1555   1555  1.32  
LINK         N   FTR B  45                 C   GLN B  44     1555   1555  1.36  
LINK         C   FTR B  45                 N   LEU B  46     1555   1555  1.34  
LINK         N   FTR B 146                 C   PRO B 145     1555   1555  1.32  
LINK         C   FTR B 146                 N   PHE B 147     1555   1555  1.33  
LINK         N   FTR B 214                 C   GLN B 213     1555   1555  1.33  
LINK         C   FTR B 214                 N   SER B 215     1555   1555  1.35  
CISPEP   1 ALA A   37    PRO A   38          0         0.59                     
CISPEP   2 LEU A   59    PRO A   60          0         2.35                     
CISPEP   3 THR A  205    PRO A  206          0         1.82                     
CISPEP   4 ALA B   37    PRO B   38          0        -0.24                     
CISPEP   5 LEU B   59    PRO B   60          0        10.64                     
CISPEP   6 THR B  205    PRO B  206          0        -2.99                     
SITE     1 GPS  7 TYR A   6  FTR A   7  VAL A   9  LEU A  12                    
SITE     2 GPS  7 ILE A 111  TYR A 115  SER A 209                               
SITE     1 AC1 21 TYR A   6  FTR A   7  GLY A  11  LEU A  12                    
SITE     2 AC1 21 FTR A  45  LYS A  49  ASN A  58  LEU A  59                    
SITE     3 AC1 21 PRO A  60  GLN A  71  SER A  72  MET A 104                    
SITE     4 AC1 21 ILE A 111  SER A 209  HOH A 530  HOH A 627                    
SITE     5 AC1 21 HOH A 745  HOH A 759  HOH A 777  HOH A 779                    
SITE     6 AC1 21 ASP B 105                                                     
SITE     1 AC2 18 ASP A 105  TYR B   6  FTR B   7  LEU B  12                    
SITE     2 AC2 18 ARG B  42  FTR B  45  LYS B  49  ASN B  58                    
SITE     3 AC2 18 LEU B  59  PRO B  60  GLN B  71  SER B  72                    
SITE     4 AC2 18 ILE B 111  HOH B 526  HOH B 598  HOH B 637                    
SITE     5 AC2 18 HOH B 682  HOH B 813                                          
CRYST1   86.939   68.747   80.539  90.00 105.08  90.00 C 1 2 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      0.011502  0.000000  0.003099        0.00000                         
SCALE2      0.000000  0.014546  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012859        0.00000                         
MTRIX1   1  0.841869 -0.090312  0.532071       -6.46100    1                    
MTRIX2   1 -0.089096 -0.995629 -0.028023       31.39400    1                    
MTRIX3   1  0.532277 -0.023813 -0.846236       27.26000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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