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Database: PDB
Entry: 3FYG
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HEADER    TRANSFERASE                             07-AUG-97   3FYG              
TITLE     CRYSTAL STRUCTURE OF TETRADECA-(3-FLUOROTYROSYL)-                     
TITLE    2 GLUTATHIONE S-TRANSFERASE                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MU CLASS TETRADECA-(3-FLUOROTYROSYL)-GLUTATHIONE           
COMPND   3 S-TRANSFERASE OF ISOENZYME;                                          
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: RAT 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 CLONE PGT33M;                                   
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: T7;                                   
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PSW1GST33;                                
SOURCE  13 EXPRESSION_SYSTEM_GENE: CDNA INSERT OF CLONE PGT33M                  
KEYWDS    TRANSFERASE, 3-FLUOROTYROSINE, UNNATURAL AMINO ACID, THREE-           
KEYWDS   2 DIMENSIONAL STRUCTURE, DETOXIFICATION ENZYME                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.XIAO,J.F.PARSONS,R.N.ARMSTRONG,G.L.GILLILAND                        
REVDAT   2   24-FEB-09 3FYG    1       VERSN                                    
REVDAT   1   01-JUN-99 3FYG    0                                                
JRNL        AUTH   G.XIAO,J.F.PARSONS,K.TESH,R.N.ARMSTRONG,                     
JRNL        AUTH 2 G.L.GILLILAND                                                
JRNL        TITL   CONFORMATIONAL CHANGES IN THE CRYSTAL STRUCTURE OF           
JRNL        TITL 2 RAT GLUTATHIONE TRANSFERASE M1-1 WITH GLOBAL                 
JRNL        TITL 3 SUBSTITUTION OF 3-FLUOROTYROSINE FOR TYROSINE.               
JRNL        REF    J.MOL.BIOL.                   V. 281   323 1998              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   9698551                                                      
JRNL        DOI    10.1006/JMBI.1998.1935                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.F.PARSONS,R.N.ARMSTRONG                                    
REMARK   1  TITL   PROTON CONFIGURATION IN THE GROUND STATE AND                 
REMARK   1  TITL 2 TRANSITION STATE OF A GLUTATHIONE                            
REMARK   1  TITL 3 TRANSFERASE-CATALYZED REACTION INFERRED FROM THE             
REMARK   1  TITL 4 PROPERTIES OF                                                
REMARK   1  TITL 5 TETRADECA(3-FLUOROTYROSYL)GLUTATHIONE TRANSFERASE            
REMARK   1  REF    J.AM.CHEM.SOC.                V. 118  2295 1996              
REMARK   1  REFN                   ISSN 0002-7863                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   X.JI,W.W.JOHNSON,M.A.SESAY,L.DICKERT,S.M.PRASAD,             
REMARK   1  AUTH 2 H.L.AMMON,R.N.ARMSTRONG,G.L.GILLILAND                        
REMARK   1  TITL   STRUCTURE AND FUNCTION OF THE XENOBIOTIC SUBSTRATE           
REMARK   1  TITL 2 BINDING SITE OF A GLUTATHIONE S-TRANSFERASE AS               
REMARK   1  TITL 3 REVEALED BY X-RAY CRYSTALLOGRAPHIC ANALYSIS OF               
REMARK   1  TITL 4 PRODUCT COMPLEXES WITH THE DIASTEREOMERS OF                  
REMARK   1  TITL 5 9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-                          
REMARK   1  TITL 6 DIHYDROPHENANTHRENE                                          
REMARK   1  REF    BIOCHEMISTRY                  V.  33  1043 1994              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   X.JI,R.N.ARMSTRONG,G.L.GILLILAND                             
REMARK   1  TITL   SNAPSHOTS ALONG THE REACTION COORDINATE OF AN SNAR           
REMARK   1  TITL 2 REACTION CATALYZED BY GLUTATHIONE TRANSFERASE                
REMARK   1  REF    BIOCHEMISTRY                  V.  32 12949 1993              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   S.LIU,X.JI,G.L.GILLILAND,W.J.STEVENS,R.N.ARMSTRONG           
REMARK   1  TITL   SECOND-SPHERE ELECTROSTATIC EFFECTS IN THE ACTIVE            
REMARK   1  TITL 2 SITE OF GLUTATHIONE S-TRANSFERASE. OBSERVATION OF            
REMARK   1  TITL 3 AN ON-FACET HYDROGEN BOND BETWEEN THE SIDE CHAIN             
REMARK   1  TITL 4 OF THREONINE 13 AND THE PI-CLOUD OF TYROSINE 6 AND           
REMARK   1  TITL 5 ITS INFLUENCE ON CATALYSIS                                   
REMARK   1  REF    J.AM.CHEM.SOC.                V. 115  7910 1993              
REMARK   1  REFN                   ISSN 0002-7863                               
REMARK   1 REFERENCE 5                                                          
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   1 REFERENCE 6                                                          
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   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT V. 5-E                                           
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.200                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 243942                         
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) : 0.170                           
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            : 3654                                    
REMARK   3   NUCLEIC ACID ATOMS       : NULL                                    
REMARK   3   HETEROGEN ATOMS          : NULL                                    
REMARK   3   SOLVENT ATOMS            : NULL                                    
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : 39.800                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.015 ; 0.800 ; 3852            
REMARK   3   BOND ANGLES            (DEGREES) : 2.360 ; 1.300 ; 5172            
REMARK   3   TORSION ANGLES         (DEGREES) : 20.000; 0.000 ; 2290            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : 0.010 ; 2.000 ; 108             
REMARK   3   GENERAL PLANES               (A) : 0.011 ; 5.000 ; 532             
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : 5.810 ; 1.000 ; 3540            
REMARK   3   NON-BONDED CONTACTS          (A) : 0.090 ; 10.000; 143             
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        : 220.00                                               
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 3FYG 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        : 01-OCT-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 103                                
REMARK 200  PH                             : 6.8                                
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                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
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   : 22702                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 65.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 10.750                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.35000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 3GST: CLASS MU GST                                   
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.8                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       42.71500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.21000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.71500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.21000            
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: 4750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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 IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   815     O    HOH A   851              2.00            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 A   649     O    HOH A   649     2655     1.90            
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  48   CD    GLU A  48   OE1     0.070                       
REMARK 500    GLU A  88   CD    GLU A  88   OE2     0.067                       
REMARK 500    GLU A 125   CD    GLU A 125   OE2     0.069                       
REMARK 500    GLU A 132   CD    GLU A 132   OE2     0.104                       
REMARK 500    GLU A 188   CD    GLU A 188   OE2     0.069                       
REMARK 500    GLU B  28   CD    GLU B  28   OE1     0.073                       
REMARK 500    GLU B  91   CD    GLU B  91   OE2     0.076                       
REMARK 500    GLU B 120   CD    GLU B 120   OE2     0.089                       
REMARK 500    GLU B 132   CD    GLU B 132   OE2     0.089                       
REMARK 500    GLU B 139   CD    GLU B 139   OE1     0.073                       
REMARK 500    LYS B 198   CD    LYS B 198   CE      0.235                       
REMARK 500    LYS B 198   CE    LYS B 198   NZ      0.171                       
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    ASP A  24   CB  -  CG  -  OD1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP A  36   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A  36   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    PRO A  57   N   -  CA  -  CB  ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ASP A  64   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ASP A  64   CB  -  CG  -  OD2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ARG A  77   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    ARG A  77   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG A  95   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A  95   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP A 150   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP A 182   CB  -  CG  -  OD2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    ASP B  24   CB  -  CG  -  OD1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ASP B  24   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ASP B  36   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ASP B  39   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    ARG B  42   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ASP B  64   CB  -  CG  -  OD1 ANGL. DEV. =   8.6 DEGREES          
REMARK 500    ASP B  64   CB  -  CG  -  OD2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    ARG B  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG B  81   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG B  81   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B  93   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG B  93   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ASP B 118   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    ASP B 150   CB  -  CG  -  OD2 ANGL. DEV. =  -8.2 DEGREES          
REMARK 500    ASP B 164   CB  -  CG  -  OD2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    ASP B 175   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP B 182   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP B 182   CB  -  CG  -  OD2 ANGL. DEV. =  -7.1 DEGREES          
REMARK 500    ARG B 201   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 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   8      -15.46    -29.77                                   
REMARK 500    PRO A  38      -86.08    -75.15                                   
REMARK 500    SER A  43      -82.31    -28.95                                   
REMARK 500    GLN A  44      -69.89    -25.18                                   
REMARK 500    LYS A  49      -34.08    -31.67                                   
REMARK 500    PRO A  57      116.51    -32.60                                   
REMARK 500    GLN A  71      111.19     73.19                                   
REMARK 500    ASP A 118       34.45    -97.50                                   
REMARK 500    LYS A 123      -74.64    -27.81                                   
REMARK 500    PRO A 171      -14.96    -38.58                                   
REMARK 500    LEU A 190      116.54    -17.75                                   
REMARK 500    SER A 199      160.85    -45.60                                   
REMARK 500    SER A 209     -138.18   -102.56                                   
REMARK 500    LYS A 210     -107.02    -29.76                                   
REMARK 500    LEU A 211      -59.59    -11.41                                   
REMARK 500    ALA A 212      125.76    -20.06                                   
REMARK 500    SER A 215       69.12     83.18                                   
REMARK 500    ASN B   8       25.70    -72.77                                   
REMARK 500    ASP B  55      -73.42    -51.36                                   
REMARK 500    PRO B  57      131.48    -35.02                                   
REMARK 500    GLN B  71       99.40     78.52                                   
REMARK 500    ASP B 118       23.58    -74.35                                   
REMARK 500    PHE B 119      -92.39    -36.60                                   
REMARK 500    GLU B 120      -40.44    -18.36                                   
REMARK 500    LYS B 123      -10.67    -48.49                                   
REMARK 500    PRO B 171      -26.86    -38.34                                   
REMARK 500    CYS B 173      -17.36    -42.70                                   
REMARK 500    SER B 209     -145.50   -100.06                                   
REMARK 500    SER B 215       72.82     82.44                                   
REMARK 500    ASN B 216       31.85    -95.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AVA                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE FOR BINDING BOTH THE SUBSTRATE         
REMARK 800  GLUTATHIONE AND XENOBIOTIC SUBSTRATE.                               
REMARK 800 SITE_IDENTIFIER: AVB                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE FOR BINDING BOTH THE SUBSTRATE         
REMARK 800  GLUTATHIONE AND XENOBIOTIC SUBSTRATE.                               
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  3FYG A    1   217  UNP    P04905   GSTM1_RAT        1    217             
DBREF  3FYG B    1   217  UNP    P04905   GSTM1_RAT        1    217             
SEQADV 3FYG YOF A    6  UNP  P04905    TYR     6 ENGINEERED                     
SEQADV 3FYG YOF A   22  UNP  P04905    TYR    22 ENGINEERED                     
SEQADV 3FYG YOF A   27  UNP  P04905    TYR    27 ENGINEERED                     
SEQADV 3FYG YOF A   32  UNP  P04905    TYR    32 ENGINEERED                     
SEQADV 3FYG YOF A   40  UNP  P04905    TYR    40 ENGINEERED                     
SEQADV 3FYG YOF A   61  UNP  P04905    TYR    61 ENGINEERED                     
SEQADV 3FYG YOF A   78  UNP  P04905    TYR    78 ENGINEERED                     
SEQADV 3FYG YOF A  137  UNP  P04905    TYR   137 ENGINEERED                     
SEQADV 3FYG YOF A  154  UNP  P04905    TYR   154 ENGINEERED                     
SEQADV 3FYG YOF A  160  UNP  P04905    TYR   160 ENGINEERED                     
SEQADV 3FYG YOF A  166  UNP  P04905    TYR   166 ENGINEERED                     
SEQADV 3FYG YOF A  196  UNP  P04905    TYR   196 ENGINEERED                     
SEQADV 3FYG YOF A  202  UNP  P04905    TYR   202 ENGINEERED                     
SEQADV 3FYG YOF B    6  UNP  P04905    TYR     6 ENGINEERED                     
SEQADV 3FYG YOF B   22  UNP  P04905    TYR    22 ENGINEERED                     
SEQADV 3FYG YOF B   27  UNP  P04905    TYR    27 ENGINEERED                     
SEQADV 3FYG YOF B   32  UNP  P04905    TYR    32 ENGINEERED                     
SEQADV 3FYG YOF B   40  UNP  P04905    TYR    40 ENGINEERED                     
SEQADV 3FYG YOF B   61  UNP  P04905    TYR    61 ENGINEERED                     
SEQADV 3FYG YOF B   78  UNP  P04905    TYR    78 ENGINEERED                     
SEQADV 3FYG YOF B  137  UNP  P04905    TYR   137 ENGINEERED                     
SEQADV 3FYG YOF B  154  UNP  P04905    TYR   154 ENGINEERED                     
SEQADV 3FYG YOF B  160  UNP  P04905    TYR   160 ENGINEERED                     
SEQADV 3FYG YOF B  166  UNP  P04905    TYR   166 ENGINEERED                     
SEQADV 3FYG YOF B  196  UNP  P04905    TYR   196 ENGINEERED                     
SEQADV 3FYG YOF B  202  UNP  P04905    TYR   202 ENGINEERED                     
SEQRES   1 A  217  PRO MET ILE LEU GLY YOF TRP ASN VAL ARG GLY LEU THR          
SEQRES   2 A  217  HIS PRO ILE ARG LEU LEU LEU GLU YOF THR ASP SER SER          
SEQRES   3 A  217  YOF GLU GLU LYS ARG YOF ALA MET GLY ASP ALA PRO ASP          
SEQRES   4 A  217  YOF ASP ARG SER GLN TRP LEU ASN GLU LYS PHE LYS LEU          
SEQRES   5 A  217  GLY LEU ASP PHE PRO ASN LEU PRO YOF LEU ILE ASP GLY          
SEQRES   6 A  217  SER ARG LYS ILE THR GLN SER ASN ALA ILE MET ARG YOF          
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 YOF SER GLU PHE LEU GLY LYS          
SEQRES  12 A  217  ARG PRO TRP PHE ALA GLY ASP LYS VAL THR YOF VAL ASP          
SEQRES  13 A  217  PHE LEU ALA YOF ASP ILE LEU ASP GLN YOF 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  YOF MET LYS SER SER ARG YOF LEU SER THR PRO ILE PHE          
SEQRES  17 A  217  SER LYS LEU ALA GLN TRP SER ASN LYS                          
SEQRES   1 B  217  PRO MET ILE LEU GLY YOF TRP ASN VAL ARG GLY LEU THR          
SEQRES   2 B  217  HIS PRO ILE ARG LEU LEU LEU GLU YOF THR ASP SER SER          
SEQRES   3 B  217  YOF GLU GLU LYS ARG YOF ALA MET GLY ASP ALA PRO ASP          
SEQRES   4 B  217  YOF ASP ARG SER GLN TRP LEU ASN GLU LYS PHE LYS LEU          
SEQRES   5 B  217  GLY LEU ASP PHE PRO ASN LEU PRO YOF LEU ILE ASP GLY          
SEQRES   6 B  217  SER ARG LYS ILE THR GLN SER ASN ALA ILE MET ARG YOF          
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 YOF SER GLU PHE LEU GLY LYS          
SEQRES  12 B  217  ARG PRO TRP PHE ALA GLY ASP LYS VAL THR YOF VAL ASP          
SEQRES  13 B  217  PHE LEU ALA YOF ASP ILE LEU ASP GLN YOF 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  YOF MET LYS SER SER ARG YOF LEU SER THR PRO ILE PHE          
SEQRES  17 B  217  SER LYS LEU ALA GLN TRP SER ASN LYS                          
MODRES 3FYG YOF A    6  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF A   22  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF A   27  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF A   32  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF A   40  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF A   61  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF A   78  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF A  137  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF A  154  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF A  160  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF A  166  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF A  196  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF A  202  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF B    6  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF B   22  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF B   27  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF B   32  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF B   40  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF B   61  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF B   78  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF B  137  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF B  154  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF B  160  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF B  166  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF B  196  TYR  3-FLUOROTYROSINE                                   
MODRES 3FYG YOF B  202  TYR  3-FLUOROTYROSINE                                   
HET    YOF  A   6      13                                                       
HET    YOF  A  22      13                                                       
HET    YOF  A  27      13                                                       
HET    YOF  A  32      13                                                       
HET    YOF  A  40      13                                                       
HET    YOF  A  61      13                                                       
HET    YOF  A  78      13                                                       
HET    YOF  A 137      13                                                       
HET    YOF  A 154      18                                                       
HET    YOF  A 160      13                                                       
HET    YOF  A 166      13                                                       
HET    YOF  A 196      13                                                       
HET    YOF  A 202      13                                                       
HET    YOF  B   6      13                                                       
HET    YOF  B  22      13                                                       
HET    YOF  B  27      13                                                       
HET    YOF  B  32      13                                                       
HET    YOF  B  40      13                                                       
HET    YOF  B  61      13                                                       
HET    YOF  B  78      13                                                       
HET    YOF  B 137      13                                                       
HET    YOF  B 154      18                                                       
HET    YOF  B 160      13                                                       
HET    YOF  B 166      13                                                       
HET    YOF  B 196      13                                                       
HET    YOF  B 202      13                                                       
HET    GPR  A 218      35                                                       
HET    GPR  B 218      35                                                       
HETNAM     YOF 3-FLUOROTYROSINE                                                 
HETNAM     GPR (9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-                     
HETNAM   2 GPR  DIHYDROPHENANTHRENE                                             
FORMUL   1  YOF    26(C9 H10 F N O3)                                            
FORMUL   3  GPR    2(C24 H27 N3 O7 S)                                           
FORMUL   5  HOH   *431(H2 O)                                                    
HELIX    1   1 GLY A   11  LEU A   20  5                                  10    
HELIX    2   2 SER A   43  GLU A   48  1                                   6    
HELIX    3   3 SER A   72  ALA A   80  1                                   9    
HELIX    4   4 GLU A   90  CYS A  114  1                                  25    
HELIX    5   5 PHE A  119  GLU A  139  1                                  21    
HELIX    6   6 LEU A  158  ILE A  162  5                                   5    
HELIX    7   7 ASP A  164  ILE A  168  5                                   5    
HELIX    8   8 PRO A  178  GLY A  189  1                                  12    
HELIX    9   9 LYS A  191  LYS A  198  1                                   8    
HELIX   10  10 GLY B   11  LEU B   20  5                                  10    
HELIX   11  11 SER B   43  LEU B   46  1                                   4    
HELIX   12  12 SER B   72  HIS B   83  1                                  12    
HELIX   13  13 GLU B   90  CYS B  114  1                                  25    
HELIX   14  14 PHE B  119  GLU B  125  1                                   7    
HELIX   15  15 ILE B  130  GLU B  139  1                                  10    
HELIX   16  16 LEU B  158  ILE B  162  5                                   5    
HELIX   17  17 ASP B  164  ILE B  168  5                                   5    
HELIX   18  18 PRO B  178  GLY B  189  1                                  12    
HELIX   19  19 LYS B  191  LYS B  198  1                                   8    
SHEET    1   A 2 ILE A  63  ASP A  64  0                                        
SHEET    2   A 2 ARG A  67  LYS A  68 -1  O  ARG A  67   N  ASP A  64           
SHEET    1   B 2 ILE B  63  ASP B  64  0                                        
SHEET    2   B 2 ARG B  67  LYS B  68 -1  O  ARG B  67   N  ASP B  64           
LINK         N   YOF A   6                 C   GLY A   5     1555   1555  1.31  
LINK         C   YOF A   6                 N   TRP A   7     1555   1555  1.35  
LINK         N   YOF A  22                 C   GLU A  21     1555   1555  1.31  
LINK         C   YOF A  22                 N   THR A  23     1555   1555  1.28  
LINK         N   YOF A  27                 C   SER A  26     1555   1555  1.29  
LINK         C   YOF A  27                 N   GLU A  28     1555   1555  1.33  
LINK         N   YOF A  32                 C   ARG A  31     1555   1555  1.34  
LINK         C   YOF A  32                 N   ALA A  33     1555   1555  1.32  
LINK         N   YOF A  40                 C   ASP A  39     1555   1555  1.34  
LINK         C   YOF A  40                 N   ASP A  41     1555   1555  1.37  
LINK         N   YOF A  61                 C   PRO A  60     1555   1555  1.32  
LINK         C   YOF A  61                 N   LEU A  62     1555   1555  1.33  
LINK         N   YOF A  78                 C   ARG A  77     1555   1555  1.31  
LINK         C   YOF A  78                 N   LEU A  79     1555   1555  1.35  
LINK         N   YOF A 137                 C   LEU A 136     1555   1555  1.35  
LINK         C   YOF A 137                 N   SER A 138     1555   1555  1.35  
LINK         N   YOF A 154                 C   THR A 153     1555   1555  1.34  
LINK         C   YOF A 154                 N   VAL A 155     1555   1555  1.33  
LINK         N   YOF A 160                 C   ALA A 159     1555   1555  1.33  
LINK         C   YOF A 160                 N   ASP A 161     1555   1555  1.31  
LINK         N   YOF A 166                 C   GLN A 165     1555   1555  1.33  
LINK         C   YOF A 166                 N   HIS A 167     1555   1555  1.33  
LINK         N   YOF A 196                 C   ALA A 195     1555   1555  1.31  
LINK         C   YOF A 196                 N   MET A 197     1555   1555  1.35  
LINK         N   YOF A 202                 C   ARG A 201     1555   1555  1.35  
LINK         C   YOF A 202                 N   LEU A 203     1555   1555  1.36  
LINK         N   YOF B   6                 C   GLY B   5     1555   1555  1.32  
LINK         C   YOF B   6                 N   TRP B   7     1555   1555  1.30  
LINK         N   YOF B  22                 C   GLU B  21     1555   1555  1.32  
LINK         C   YOF B  22                 N   THR B  23     1555   1555  1.32  
LINK         N   YOF B  27                 C   SER B  26     1555   1555  1.33  
LINK         C   YOF B  27                 N   GLU B  28     1555   1555  1.31  
LINK         N   YOF B  32                 C   ARG B  31     1555   1555  1.33  
LINK         C   YOF B  32                 N   ALA B  33     1555   1555  1.31  
LINK         N   YOF B  40                 C   ASP B  39     1555   1555  1.32  
LINK         C   YOF B  40                 N   ASP B  41     1555   1555  1.33  
LINK         N   YOF B  61                 C   PRO B  60     1555   1555  1.35  
LINK         C   YOF B  61                 N   LEU B  62     1555   1555  1.30  
LINK         N   YOF B  78                 C   ARG B  77     1555   1555  1.32  
LINK         C   YOF B  78                 N   LEU B  79     1555   1555  1.33  
LINK         N   YOF B 137                 C   LEU B 136     1555   1555  1.33  
LINK         C   YOF B 137                 N   SER B 138     1555   1555  1.33  
LINK         N   YOF B 154                 C   THR B 153     1555   1555  1.31  
LINK         C   YOF B 154                 N   VAL B 155     1555   1555  1.34  
LINK         N   YOF B 160                 C   ALA B 159     1555   1555  1.33  
LINK         C   YOF B 160                 N   ASP B 161     1555   1555  1.32  
LINK         N   YOF B 166                 C   GLN B 165     1555   1555  1.34  
LINK         C   YOF B 166                 N   HIS B 167     1555   1555  1.30  
LINK         N   YOF B 196                 C   ALA B 195     1555   1555  1.30  
LINK         C   YOF B 196                 N   MET B 197     1555   1555  1.31  
LINK         N   YOF B 202                 C   ARG B 201     1555   1555  1.33  
LINK         C   YOF B 202                 N   LEU B 203     1555   1555  1.33  
CISPEP   1 ALA A   37    PRO A   38          0        -1.34                     
CISPEP   2 LEU A   59    PRO A   60          0         4.34                     
CISPEP   3 THR A  205    PRO A  206          0        -2.64                     
CISPEP   4 ALA B   37    PRO B   38          0         0.64                     
CISPEP   5 LEU B   59    PRO B   60          0         1.07                     
CISPEP   6 THR B  205    PRO B  206          0         0.08                     
SITE     1 AVA  8 YOF A   6  TRP A   7  VAL A   9  LEU A  12                    
SITE     2 AVA  8 ILE A 111  TYR A 115  PHE A 208  SER A 209                    
SITE     1 AVB  8 YOF B   6  TRP B   7  VAL B   9  LEU B  12                    
SITE     2 AVB  8 ILE B 111  TYR B 115  PHE B 208  SER B 209                    
SITE     1 AC1 18 YOF A   6  TRP A   7  GLY A  11  LEU A  12                    
SITE     2 AC1 18 ARG A  42  TRP A  45  LYS A  49  ASN A  58                    
SITE     3 AC1 18 LEU A  59  GLN A  71  SER A  72  MET A 104                    
SITE     4 AC1 18 ILE A 207  HOH A 540  HOH A 704  HOH A 743                    
SITE     5 AC1 18 HOH A 945  ASP B 105                                          
SITE     1 AC2 21 ASP A 105  YOF B   6  TRP B   7  GLY B  11                    
SITE     2 AC2 21 LEU B  12  ARG B  42  TRP B  45  LYS B  49                    
SITE     3 AC2 21 ASN B  58  LEU B  59  PRO B  60  GLN B  71                    
SITE     4 AC2 21 SER B  72  ILE B 111  ILE B 207  SER B 209                    
SITE     5 AC2 21 HOH B 522  HOH B 525  HOH B 694  HOH B 804                    
SITE     6 AC2 21 HOH B 816                                                     
CRYST1   85.430   88.420   57.260  90.00  90.00  90.00 P 21 21 2     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      0.011705  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011310  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017464        0.00000                         
MTRIX1   1 -0.282070 -0.747740 -0.601100       49.75153    1                    
MTRIX2   1 -0.754600 -0.214000  0.620310       29.32965    1                    
MTRIX3   1 -0.592470  0.628560 -0.503880       22.56671    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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