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Database: PDB
Entry: 1MTC
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Original site: 1MTC 
HEADER    TRANSFERASE                             20-SEP-02   1MTC              
TITLE     GLUTATHIONE TRANSFERASE MUTANT Y115F                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE YB1;                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CHAIN 3; GST M1-1; GST CLASS-MU 1; GLUTATHIONE S-           
COMPND   5 TRANSFERASE YB-1 SUBUNIT;                                            
COMPND   6 EC: 2.5.1.18;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 OTHER_DETAILS: COMPLEX WITH (9R,10R)-9-(S-GLUTATHIONYL)-10-          
COMPND  10 HYDROXY-9,10-DIHROPHENANTHRENE                                       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 ORGAN: LIVER;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGT33MX                                   
KEYWDS    GLUTATHIONE TRANSFERASE, PROTEIN DYNAMICS, PROTEIN CATALYSIS          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.LADNER,G.XIAO,R.N.ARMSTRONG,G.L.GILLILAND                         
REVDAT   2   24-FEB-09 1MTC    1       VERSN                                    
REVDAT   1   25-MAR-03 1MTC    0                                                
JRNL        AUTH   S.G.CODREANU,J.E.LADNER,G.XIAO,N.V.STOURMAN,                 
JRNL        AUTH 2 D.L.HACHEY,G.L.GILLILAND,R.N.ARMSTRONG                       
JRNL        TITL   LOCAL PROTEIN DYNAMICS AND CATALYSIS: DETECTION OF           
JRNL        TITL 2 SEGMENTAL MOTION ASSOCIATED WITH RATE-LIMITING               
JRNL        TITL 3 PRODUCT RELEASE BY A GLUTATHIONE TRANSFERASE                 
JRNL        REF    BIOCHEMISTRY                  V.  41 15161 2002              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   12484753                                                     
JRNL        DOI    10.1021/BI026776P                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.203                  
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) : 21775                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.187                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 18747                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 3632                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 70                                            
REMARK   3   SOLVENT ATOMS      : 185                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 3889.00                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 0                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 15571                   
REMARK   3   NUMBER OF RESTRAINTS                     : 15303                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.011                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.039                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.015                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.016                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.022                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.015                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.044                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE        
REMARK   3  METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56         
REMARK   4                                                                      
REMARK   4 1MTC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB017169.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-MAR-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 143                                
REMARK 200  PH                             : 8.0                                
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          : SIEMENS                            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : BRUKER                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN                             
REMARK 200  DATA SCALING SOFTWARE          : XENGEN                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21775                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 33.0000                            
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) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: SHELXS                                                
REMARK 200 STARTING MODEL: 3GST                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONOIUM SULFATE AT PH 8.0, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP                                             
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       43.37500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.29000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       43.37500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.29000            
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: 4650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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: 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. =  -3.9 DEGREES          
REMARK 500    TYR A  22   CB  -  CG  -  CD2 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    SER A  26   N   -  CA  -  CB  ANGL. DEV. =  11.3 DEGREES          
REMARK 500    ARG A  31   CD  -  NE  -  CZ  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    ARG A  31   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A  42   CD  -  NE  -  CZ  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ARG A  42   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    TYR A  61   CB  -  CG  -  CD1 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    TYR A  61   CG  -  CD1 -  CE1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A  64   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG A  67   CD  -  NE  -  CZ  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    ARG A  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A  77   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    TYR A  78   CB  -  CG  -  CD1 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ARG A  81   CD  -  NE  -  CZ  ANGL. DEV. = -12.4 DEGREES          
REMARK 500    HIS A  84   CA  -  CB  -  CG  ANGL. DEV. = -10.9 DEGREES          
REMARK 500    ARG A 107   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG A 144   CD  -  NE  -  CZ  ANGL. DEV. =  10.8 DEGREES          
REMARK 500    ARG A 144   NE  -  CZ  -  NH1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG A 144   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    TYR A 154   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    TYR A 154   CB  -  CG  -  CD1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    TYR A 160   CB  -  CG  -  CD1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    TYR A 196   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    TYR A 196   CB  -  CG  -  CD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG B  10   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG B  10   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B  42   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B  42   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    TYR B  61   CB  -  CG  -  CD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG B  67   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG B  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    GLU B  92   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    ARG B  95   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ASP B  97   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    GLU B 100   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.3 DEGREES          
REMARK 500    PHE B 115   CB  -  CG  -  CD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG B 144   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG B 186   CD  -  NE  -  CZ  ANGL. DEV. =  15.6 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    GLN A  71      111.01     80.81                                   
REMARK 500    HIS A  84       55.34     39.88                                   
REMARK 500    ASP A 118       29.36    -79.72                                   
REMARK 500    LEU A 203       87.95   -153.72                                   
REMARK 500    LYS A 210        1.21    -68.23                                   
REMARK 500    ASN B   8       54.13    -96.00                                   
REMARK 500    TYR B  40       43.60     71.57                                   
REMARK 500    PHE B  56       79.35   -118.40                                   
REMARK 500    GLN B  71      110.25     81.50                                   
REMARK 500    PHE B 177       69.82   -119.00                                   
REMARK 500    SER B 209     -138.73    -59.75                                   
REMARK 500    LEU B 211       20.44    -59.41                                   
REMARK 500    GLN B 213       33.91    -96.66                                   
REMARK 500    TRP B 214      139.75   -174.18                                   
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 A 443        DISTANCE =  5.88 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GPR A 5218                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GPR B 6218                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3GST   RELATED DB: PDB                                   
DBREF  1MTC A    1   217  UNP    P04905   GSTM1_RAT        1    217             
DBREF  1MTC B    1   217  UNP    P04905   GSTM1_RAT        1    217             
SEQADV 1MTC PHE A  115  UNP  P04905    TYR   115 ENGINEERED                     
SEQADV 1MTC PHE B  115  UNP  P04905    TYR   115 ENGINEERED                     
SEQRES   1 A  217  PRO MET ILE LEU GLY TYR TRP 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 TRP 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 PHE 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 TRP 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 TRP SER ASN LYS                          
SEQRES   1 B  217  PRO MET ILE LEU GLY TYR TRP 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 TRP 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 PHE 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 TRP 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 TRP SER ASN LYS                          
HET    GPR  A5218      35                                                       
HET    GPR  B6218      35                                                       
HETNAM     GPR (9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-                     
HETNAM   2 GPR  DIHYDROPHENANTHRENE                                             
FORMUL   3  GPR    2(C24 H27 N3 O7 S)                                           
FORMUL   5  HOH   *185(H2 O)                                                    
HELIX    1   1 THR A   13  THR A   23  1                                  11    
HELIX    2   2 ARG A   42  ASN A   47  1                                   6    
HELIX    3   3 GLU A   48  LEU A   52  5                                   5    
HELIX    4   4 GLN A   71  HIS A   83  1                                  13    
HELIX    5   5 THR A   89  PHE A  115  1                                  27    
HELIX    6   6 ASP A  118  GLY A  142  1                                  25    
HELIX    7   7 THR A  153  GLU A  170  1                                  18    
HELIX    8   8 PRO A  171  ASP A  175  5                                   5    
HELIX    9   9 PHE A  177  LEU A  190  1                                  14    
HELIX   10  10 LEU A  190  LYS A  198  1                                   9    
HELIX   11  11 THR B   13  THR B   23  1                                  11    
HELIX   12  12 ARG B   42  PHE B   50  1                                   9    
HELIX   13  13 GLN B   71  HIS B   83  1                                  13    
HELIX   14  14 THR B   89  PHE B  115  1                                  27    
HELIX   15  15 ASP B  118  GLY B  142  1                                  25    
HELIX   16  16 THR B  153  GLU B  170  1                                  18    
HELIX   17  17 PHE B  177  LEU B  190  1                                  14    
HELIX   18  18 LEU B  190  LYS B  198  1                                   9    
SHEET    1   A 4 TYR A  27  TYR A  32  0                                        
SHEET    2   A 4 MET A   2  TRP A   7  1  N  MET A   2   O  GLU A  28           
SHEET    3   A 4 TYR A  61  ASP A  64 -1  O  TYR A  61   N  GLY A   5           
SHEET    4   A 4 ARG A  67  THR A  70 -1  O  ILE A  69   N  LEU A  62           
SHEET    1   B 4 TYR B  27  TYR B  32  0                                        
SHEET    2   B 4 MET B   2  TRP B   7  1  N  MET B   2   O  GLU B  28           
SHEET    3   B 4 TYR B  61  ASP B  64 -1  O  ILE B  63   N  ILE B   3           
SHEET    4   B 4 ARG B  67  THR B  70 -1  O  ARG B  67   N  ASP B  64           
CISPEP   1 ALA A   37    PRO A   38          0        -1.34                     
CISPEP   2 LEU A   59    PRO A   60          0        -0.35                     
CISPEP   3 THR A  205    PRO A  206          0        -4.86                     
CISPEP   4 ALA B   37    PRO B   38          0        -1.06                     
CISPEP   5 LEU B   59    PRO B   60          0         0.01                     
CISPEP   6 THR B  205    PRO B  206          0        -2.06                     
SITE     1 AC1 22 TYR A   6  TRP A   7  LEU A  12  ARG A  42                    
SITE     2 AC1 22 TRP A  45  LYS A  49  ASN A  58  LEU A  59                    
SITE     3 AC1 22 PRO A  60  GLN A  71  SER A  72  MET A 104                    
SITE     4 AC1 22 MET A 108  ILE A 111  PHE A 208  SER A 209                    
SITE     5 AC1 22 HOH A 306  HOH A 313  HOH A 315  HOH A 380                    
SITE     6 AC1 22 HOH A 415  ASP B 105                                          
SITE     1 AC2 18 ASP A 105  TYR B   6  TRP B   7  GLY B  11                    
SITE     2 AC2 18 LEU B  12  TRP B  45  LYS B  49  ASN B  58                    
SITE     3 AC2 18 LEU B  59  GLN B  71  SER B  72  MET B 104                    
SITE     4 AC2 18 ILE B 111  PHE B 115  SER B 209  HOH B 329                    
SITE     5 AC2 18 HOH B 333  HOH B 367                                          
CRYST1   86.750   68.580   80.460  90.00 105.12  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      0.011527  0.000000  0.003115        0.00000                         
SCALE2      0.000000  0.014582  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012874        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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