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Database: PDB
Entry: 2J9H
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Original site: 2J9H 
HEADER    TRANSFERASE                             08-NOV-06   2J9H              
TITLE     CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE-S-TRANSFERASE P1-1 CYS-FREE    
TITLE    2 MUTANT IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.4 A RESOLUTION        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE P;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GLUTATHIONE-S-TRANSFERASE P1-1, GST CLASS-PI, GSTP1-1;      
COMPND   5 EC: 2.5.1.18;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: XL-1 BLUE                                  
KEYWDS    P1-1, TRANSFERASE, GLUTATHIONE, POLYMORPHISM, GLUTATHIONE TRANSFERASE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.TARS,U.M.HEGAZY,U.HELLMAN,B.MANNERVIK                               
REVDAT   8   08-MAY-19 2J9H    1       REMARK                                   
REVDAT   7   17-JAN-18 2J9H    1       REMARK                                   
REVDAT   6   23-SEP-15 2J9H    1       REMARK VERSN  FORMUL                     
REVDAT   5   24-FEB-09 2J9H    1       VERSN                                    
REVDAT   4   19-FEB-08 2J9H    1       JRNL                                     
REVDAT   3   15-JAN-08 2J9H    1       AUTHOR JRNL   REMARK                     
REVDAT   2   26-JUN-07 2J9H    1       REMARK                                   
REVDAT   1   14-NOV-06 2J9H    0                                                
JRNL        AUTH   U.M.HEGAZY,K.TARS,U.HELLMAN,B.MANNERVIK                      
JRNL        TITL   MODULATING CATALYTIC ACTIVITY BY UNNATURAL AMINO ACID        
JRNL        TITL 2 RESIDUES IN A GSH-BINDING LOOP OF GST P1-1.                  
JRNL        REF    J.MOL.BIOL.                   V. 376   811 2008              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   18177897                                                     
JRNL        DOI    10.1016/J.JMB.2007.12.013                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 15269                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.253                           
REMARK   3   R VALUE            (WORKING SET) : 0.250                           
REMARK   3   FREE R VALUE                     : 0.310                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 808                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1175                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.28                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3130                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.4810                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3272                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 45                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.77000                                              
REMARK   3    B22 (A**2) : 0.77000                                              
REMARK   3    B33 (A**2) : -1.54000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.868         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.367         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.288         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.479        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.923                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.888                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3392 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4598 ; 1.507 ; 2.000       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   416 ; 6.000 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   150 ;31.890 ;24.800       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   562 ;18.971 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;23.192 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   506 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2570 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1609 ; 0.211 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2272 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   147 ; 0.183 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    48 ; 0.236 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.175 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2146 ; 0.541 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3324 ; 0.954 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1433 ; 1.407 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1274 ; 2.106 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2J9H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-NOV-06.                  
REMARK 100 THE DEPOSITION ID IS D_1290030454.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-APR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.40                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.042                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16119                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.400                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 9GSS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP VAPOUR TECHNIQUE, 1         
REMARK 280  MICROLITRE OF PROTEIN AT 10 MG/ML IN 20 MM TRIS-HCL, PH 8.0         
REMARK 280  CONTAINING 5MM S-HEXYLGLUTATHIONE WAS MIXED WITH 1 MICROLITRE OF    
REMARK 280  RESERVOIR SOLUTION, COMPOSED OF 1.5M AMMONIUM SULFATE AND 100MM     
REMARK 280  SODIUM CITRATE, PH 7.40, VAPOR DIFFUSION, SITTING DROP              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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      119.17500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       29.78300            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       29.78300            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      178.76250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       29.78300            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       29.78300            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       59.58750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       29.78300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       29.78300            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      178.76250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       29.78300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       29.78300            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       59.58750            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      119.17500            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4060 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.3 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 15 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 48 TO ALA                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 102 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 170 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 15 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 48 TO ALA                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 102 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 170 TO SER                        
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    LEU B  61   CA  -  CB  -  CG  ANGL. DEV. =  14.1 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  65      117.57     74.26                                   
REMARK 500    ASN A 111       68.90   -158.01                                   
REMARK 500    THR A 132      -71.41    -56.21                                   
REMARK 500    GLN A 136       15.36    -66.22                                   
REMARK 500    THR A 142      -76.86   -122.19                                   
REMARK 500    LEU A 194        3.36    -67.79                                   
REMARK 500    GLU A 198       -4.50    -59.42                                   
REMARK 500    PRO B  10       62.21    -68.48                                   
REMARK 500    GLN B  65      113.74     80.17                                   
REMARK 500    LEU B  79       52.88   -112.92                                   
REMARK 500    ASN B 111       72.02   -170.19                                   
REMARK 500    GLN B 138       15.02     58.90                                   
REMARK 500    THR B 142     -102.52   -120.51                                   
REMARK 500    TYR B 199      -66.54    -95.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX B 300                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 10GS   RELATED DB: PDB                                   
REMARK 900 HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH TER117            
REMARK 900 RELATED ID: 11GS   RELATED DB: PDB                                   
REMARK 900 GLUTATHIONE S-TRANSFERASE COMPLEXED WITH ETHACRYNIC ACID-            
REMARK 900 GLUTATHIONE CONJUGATE (FORM II)                                      
REMARK 900 RELATED ID: 12GS   RELATED DB: PDB                                   
REMARK 900 GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S- NONYL-GLUTATHIONE        
REMARK 900 RELATED ID: 13GS   RELATED DB: PDB                                   
REMARK 900 GLUTATHIONE S-TRANSFERASE COMPLEXED WITH SULFASALAZINE               
REMARK 900 RELATED ID: 14GS   RELATED DB: PDB                                   
REMARK 900 GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1                            
REMARK 900 RELATED ID: 16GS   RELATED DB: PDB                                   
REMARK 900 GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3                            
REMARK 900 RELATED ID: 17GS   RELATED DB: PDB                                   
REMARK 900 GLUTATHIONE S-TRANSFERASE P1-1                                       
REMARK 900 RELATED ID: 18GS   RELATED DB: PDB                                   
REMARK 900 GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH 1-(S-GLUTATHIONYL)-2,  
REMARK 900 4-DINITROBENZENE                                                     
REMARK 900 RELATED ID: 19GS   RELATED DB: PDB                                   
REMARK 900 GLUTATHIONE S-TRANSFERASE P1-1                                       
REMARK 900 RELATED ID: 1AQV   RELATED DB: PDB                                   
REMARK 900 GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH P -BROMOBENZYLGLUTATHIONE  
REMARK 900 RELATED ID: 1AQW   RELATED DB: PDB                                   
REMARK 900 GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH GLUTATHIONE                
REMARK 900 RELATED ID: 1AQX   RELATED DB: PDB                                   
REMARK 900 GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH MEISENHEIMER COMPLEX       
REMARK 900 RELATED ID: 1EOG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE                
REMARK 900 RELATED ID: 1EOH   RELATED DB: PDB                                   
REMARK 900 GLUTATHIONE TRANSFERASE P1-1                                         
REMARK 900 RELATED ID: 1GSS   RELATED DB: PDB                                   
REMARK 900 GLUTATHIONE S-TRANSFERASE (CLASS PI)                                 
REMARK 900 RELATED ID: 1KBN   RELATED DB: PDB                                   
REMARK 900 GLUTATHIONE TRANSFERASE MUTANT                                       
REMARK 900 RELATED ID: 1LBK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A RECOMBINANT GLUTATHIONE TRANSFERASE,CREATED   
REMARK 900 BY REPLACING THE LAST SEVEN RESIDUES OF EACHSUBUNIT OF THE HUMAN     
REMARK 900 CLASS PI ISOENZYME WITH THEADDITIONAL C- TERMINAL HELIX OF HUMAN     
REMARK 900 CLASS ALPHA ISOENZYME                                                
REMARK 900 RELATED ID: 1MD3   RELATED DB: PDB                                   
REMARK 900 A FOLDING MUTANT OF HUMAN CLASS PI GLUTATHIONE TRANSFERASE,CREATED   
REMARK 900 BY MUTATING GLYCINE 146 OF THE WILD-TYPE PROTEINTO ALANINE           
REMARK 900 RELATED ID: 1MD4   RELATED DB: PDB                                   
REMARK 900 A FOLDING MUTANT OF HUMAN CLASS PI GLUTATHIONE TRANSFERASE,CREATED   
REMARK 900 BY MUTATING GLYCINE 146 OF THE WILD-TYPE PROTEINTO VALINE            
REMARK 900 RELATED ID: 1PGT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S- TRANSFERASE P1-1[V104]     
REMARK 900 COMPLEXED WITH S- HEXYLGLUTATHIONE                                   
REMARK 900 RELATED ID: 1PX6   RELATED DB: PDB                                   
REMARK 900 A FOLDING MUTANT OF HUMAN CLASS PI GLUTATHIONE TRANSFERASE,CREATED   
REMARK 900 BY MUTATING ASPARTATE 153 OF THE WILD-TYPE PROTEINTO ASPARAGINE      
REMARK 900 RELATED ID: 1PX7   RELATED DB: PDB                                   
REMARK 900 A FOLDING MUTANT OF HUMAN CLASS PI GLUTATHIONE TRANSFERASE,CREATED   
REMARK 900 BY MUTATING ASPARTATE 153 OF THE WILD-TYPE PROTEINTO GLUTAMATE       
REMARK 900 RELATED ID: 1ZGN   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE GLUTATHIONE TRANSFERASE PI INCOMPLEX WITH   
REMARK 900 DINITROSYL- DIGLUTATHIONYL IRON COMPLEX                              
REMARK 900 RELATED ID: 20GS   RELATED DB: PDB                                   
REMARK 900 GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH CIBACRON BLUE          
REMARK 900 RELATED ID: 21GS   RELATED DB: PDB                                   
REMARK 900 HUMAN GLUTATHIONE S-TRANSFERASE P1-1 IN COMPLEX WITH CHLORAMBUCIL    
REMARK 900 RELATED ID: 22GS   RELATED DB: PDB                                   
REMARK 900 HUMAN GLUTATHIONE S-TRANSFERASE P1-1 Y49F MUTANT                     
REMARK 900 RELATED ID: 2A2R   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GLUTATHIONE TRANSFERASE PI IN COMPLEXWITH S-    
REMARK 900 NITROSOGLUTATHIONE                                                   
REMARK 900 RELATED ID: 2A2S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE TRANSFERASE INCOMPLEX WITH S- 
REMARK 900 NITROSOGLUTATHIONE IN THE ABSENCE OFREDUCING AGENT                   
REMARK 900 RELATED ID: 2GSS   RELATED DB: PDB                                   
REMARK 900 HUMAN GLUTATHIONE S-TRANSFERASE P1-1 IN COMPLEX WITH ETHACRYNIC ACID 
REMARK 900 RELATED ID: 2PGT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S- TRANSFERASE P1-1[V104]     
REMARK 900 COMPLEXED WITH (9R, 10R)-9-(S-GLUTATHIONYL)-10- HYDROXY-9,10-        
REMARK 900 DIHYDROPHENANTHRENE                                                  
REMARK 900 RELATED ID: 3GSS   RELATED DB: PDB                                   
REMARK 900 HUMAN GLUTATHIONE S-TRANSFERASE P1-1 IN COMPLEX WITH ETHACRYNIC      
REMARK 900 ACID-GLUTATHIONE CONJUGATE                                           
REMARK 900 RELATED ID: 3PGT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HGSTP1-1[I104] COMPLEXED WITH THE GSH           
REMARK 900 CONJUGATE OF (+)-ANTI -BPDE                                          
REMARK 900 RELATED ID: 4GSS   RELATED DB: PDB                                   
REMARK 900 HUMAN GLUTATHIONE S-TRANSFERASE P1-1 Y108F MUTANT                    
REMARK 900 RELATED ID: 4PGT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HGSTP1-1[V104] COMPLEXED WITH THE GSH           
REMARK 900 CONJUGATE OF (+)-ANTI -BPDE                                          
REMARK 900 RELATED ID: 5GSS   RELATED DB: PDB                                   
REMARK 900 HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE       
REMARK 900 RELATED ID: 6GSS   RELATED DB: PDB                                   
REMARK 900 HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE       
REMARK 900 RELATED ID: 7GSS   RELATED DB: PDB                                   
REMARK 900 HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE       
REMARK 900 RELATED ID: 8GSS   RELATED DB: PDB                                   
REMARK 900 HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE       
REMARK 900 RELATED ID: 9GSS   RELATED DB: PDB                                   
REMARK 900 HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH S-HEXYL           
REMARK 900 GLUTATHIONE                                                          
DBREF  2J9H A    2   210  UNP    P09211   GSTP1_HUMAN      2    210             
DBREF  2J9H B    2   210  UNP    P09211   GSTP1_HUMAN      2    210             
SEQADV 2J9H SER A   15  UNP  P09211    CYS    15 ENGINEERED MUTATION            
SEQADV 2J9H ALA A   48  UNP  P09211    CYS    48 ENGINEERED MUTATION            
SEQADV 2J9H ALA A  102  UNP  P09211    CYS   102 ENGINEERED MUTATION            
SEQADV 2J9H SER A  170  UNP  P09211    CYS   170 ENGINEERED MUTATION            
SEQADV 2J9H SER B   15  UNP  P09211    CYS    15 ENGINEERED MUTATION            
SEQADV 2J9H ALA B   48  UNP  P09211    CYS    48 ENGINEERED MUTATION            
SEQADV 2J9H ALA B  102  UNP  P09211    CYS   102 ENGINEERED MUTATION            
SEQADV 2J9H SER B  170  UNP  P09211    CYS   170 ENGINEERED MUTATION            
SEQRES   1 A  209  PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG          
SEQRES   2 A  209  SER ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN          
SEQRES   3 A  209  SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN          
SEQRES   4 A  209  GLU GLY SER LEU LYS ALA SER ALA LEU TYR GLY GLN LEU          
SEQRES   5 A  209  PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER          
SEQRES   6 A  209  ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU          
SEQRES   7 A  209  TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET          
SEQRES   8 A  209  VAL ASN ASP GLY VAL GLU ASP LEU ARG ALA LYS TYR ILE          
SEQRES   9 A  209  SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP ASP          
SEQRES  10 A  209  TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU          
SEQRES  11 A  209  THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE          
SEQRES  12 A  209  VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU          
SEQRES  13 A  209  ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY SER          
SEQRES  14 A  209  LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG          
SEQRES  15 A  209  LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER          
SEQRES  16 A  209  PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS          
SEQRES  17 A  209  GLN                                                          
SEQRES   1 B  209  PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG          
SEQRES   2 B  209  SER ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN          
SEQRES   3 B  209  SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN          
SEQRES   4 B  209  GLU GLY SER LEU LYS ALA SER ALA LEU TYR GLY GLN LEU          
SEQRES   5 B  209  PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER          
SEQRES   6 B  209  ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU          
SEQRES   7 B  209  TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET          
SEQRES   8 B  209  VAL ASN ASP GLY VAL GLU ASP LEU ARG ALA LYS TYR ILE          
SEQRES   9 B  209  SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP ASP          
SEQRES  10 B  209  TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU          
SEQRES  11 B  209  THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE          
SEQRES  12 B  209  VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU          
SEQRES  13 B  209  ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY SER          
SEQRES  14 B  209  LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG          
SEQRES  15 B  209  LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER          
SEQRES  16 B  209  PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS          
SEQRES  17 B  209  GLN                                                          
HET    GTX  A 300      26                                                       
HET    GTX  B 300      26                                                       
HETNAM     GTX S-HEXYLGLUTATHIONE                                               
FORMUL   3  GTX    2(C16 H30 N3 O6 S 1+)                                        
FORMUL   5  HOH   *45(H2 O)                                                     
HELIX    1   1 SER A   15  GLN A   25  1                                  11    
HELIX    2   2 THR A   35  GLY A   42  1                                   8    
HELIX    3   3 GLY A   42  ALA A   48  1                                   7    
HELIX    4   4 GLN A   65  GLY A   78  1                                  14    
HELIX    5   5 ASP A   83  ASN A  111  1                                  29    
HELIX    6   6 ASN A  111  LEU A  134  1                                  24    
HELIX    7   7 ASN A  137  LYS A  141  5                                   5    
HELIX    8   8 SER A  150  ALA A  167  1                                  18    
HELIX    9   9 PHE A  174  ARG A  187  1                                  14    
HELIX   10  10 ARG A  187  LEU A  194  1                                   8    
HELIX   11  11 SER A  196  ASN A  201  1                                   6    
HELIX   12  12 ARG B   12  ARG B   14  5                                   3    
HELIX   13  13 SER B   15  GLN B   25  1                                  11    
HELIX   14  14 THR B   35  GLY B   42  1                                   8    
HELIX   15  15 GLY B   42  ALA B   48  1                                   7    
HELIX   16  16 GLN B   65  GLY B   78  1                                  14    
HELIX   17  17 ASP B   83  GLN B  136  1                                  54    
HELIX   18  18 SER B  150  ALA B  167  1                                  18    
HELIX   19  19 PHE B  174  SER B  185  1                                  12    
HELIX   20  20 ARG B  187  SER B  196  1                                  10    
HELIX   21  21 SER B  196  ASN B  201  1                                   6    
SHEET    1  AA 4 TRP A  29  VAL A  33  0                                        
SHEET    2  AA 4 TYR A   4  TYR A   8  1  O  TYR A   4   N  LYS A  30           
SHEET    3  AA 4 LYS A  55  ASP A  58 -1  O  LYS A  55   N  VAL A   7           
SHEET    4  AA 4 LEU A  61  TYR A  64 -1  O  LEU A  61   N  ASP A  58           
SHEET    1  BA 4 TRP B  29  VAL B  33  0                                        
SHEET    2  BA 4 TYR B   4  TYR B   8  1  O  TYR B   4   N  LYS B  30           
SHEET    3  BA 4 LYS B  55  ASP B  58 -1  O  LYS B  55   N  VAL B   7           
SHEET    4  BA 4 LEU B  61  TYR B  64 -1  O  LEU B  61   N  ASP B  58           
CISPEP   1 PRO A    2    PRO A    3          0         8.61                     
CISPEP   2 LEU A   53    PRO A   54          0         7.63                     
CISPEP   3 PRO B    2    PRO B    3          0         7.69                     
CISPEP   4 LEU B   53    PRO B   54          0        13.15                     
SITE     1 AC1 13 PHE A   9  ARG A  14  VAL A  36  TRP A  39                    
SITE     2 AC1 13 GLN A  40  LYS A  45  GLN A  52  LEU A  53                    
SITE     3 AC1 13 GLN A  65  SER A  66  TYR A 109  HOH A2011                    
SITE     4 AC1 13 ASP B  99                                                     
SITE     1 AC2 14 ASP A  99  VAL A 200  PHE B   9  ARG B  14                    
SITE     2 AC2 14 TRP B  39  LYS B  45  GLY B  51  GLN B  52                    
SITE     3 AC2 14 LEU B  53  PRO B  54  GLN B  65  SER B  66                    
SITE     4 AC2 14 TYR B 109  HOH B2008                                          
CRYST1   59.566   59.566  238.350  90.00  90.00  90.00 P 43 21 2    16          
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      0.016788  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016788  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004196        0.00000                         
MTRIX1   1 -0.999457  0.002414  0.032846       43.88900    1                    
MTRIX2   1 -0.029422 -0.513625 -0.857509        3.51600    1                    
MTRIX3   1  0.014800 -0.858011  0.513418        1.63700    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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