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Database: PDB
Entry: 3Q74
LinkDB: 3Q74
Original site: 3Q74 
HEADER    TRANSFERASE                             04-JAN-11   3Q74              
TITLE     CRYSTAL STRUCTURE ANALYSIS OF THE L7A MUTANT OF THE APO FORM OF HUMAN 
TITLE    2 ALPHA CLASS GLUTATHIONE TRANSFERASE                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE A1;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GST HA SUBUNIT 1, GST CLASS-ALPHA MEMBER 1, GST-EPSILON,    
COMPND   5 GSTA1-1, GTH1;                                                       
COMPND   6 EC: 2.5.1.18;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GSTA1;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PKHA1                                     
KEYWDS    GLUTATHIONE TRANSFERASE, THIOREDOXIN, CONSERVED RESIDUES, HYDROPHOBIC 
KEYWDS   2 CORE, TRANSFERASE                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.FANUCCHI,I.A.ACHILONU,T.N.KHOZA,M.A.FERNANDES,S.GILDENHUYS,H.W.DIRR 
REVDAT   1   12-JAN-11 3Q74    0                                                
JRNL        AUTH   T.N.KHOZA,S.FANUCCHI,I.A.ACHILONU,M.A.FERNANDES,H.W.DIRR     
JRNL        TITL   CRYSTAL STRUCTURE ANALYSIS OF THE L7A MUTANT OF THE APO FORM 
JRNL        TITL 2 OF HUMAN ALPHA CLASS GLUTATHIONE TRANSFERASE                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 51.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 42602                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2152                            
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) : 1.79                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.84                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2824                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.27                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3650                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 155                          
REMARK   3   BIN FREE R VALUE                    : 0.3890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3352                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 509                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.05000                                              
REMARK   3    B22 (A**2) : 0.04000                                              
REMARK   3    B33 (A**2) : -0.10000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.12000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.153         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.115         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.579         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.885                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3408 ; 0.024 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4590 ; 1.902 ; 2.005       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   414 ; 6.168 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   145 ;35.377 ;24.207       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   659 ;14.083 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;16.940 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   507 ; 0.134 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2504 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  2081 ; 1.011 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3354 ; 1.716 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1327 ; 3.014 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1236 ; 4.673 ; 4.500       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   -10        A  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.2780 -16.5370  16.3740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0826 T22:   0.0582                                     
REMARK   3      T33:   0.1063 T12:  -0.0004                                     
REMARK   3      T13:   0.0336 T23:   0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5754 L22:   0.3212                                     
REMARK   3      L33:   0.6467 L12:  -0.0952                                     
REMARK   3      L13:  -0.4519 L23:  -0.0556                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0617 S12:   0.0335 S13:  -0.0381                       
REMARK   3      S21:   0.0726 S22:   0.0145 S23:   0.0615                       
REMARK   3      S31:   0.0408 S32:  -0.0399 S33:   0.0472                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   -10        B  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7700 -15.8640   5.8110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0705 T22:   0.0604                                     
REMARK   3      T33:   0.1081 T12:   0.0004                                     
REMARK   3      T13:   0.0110 T23:  -0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5981 L22:   0.8622                                     
REMARK   3      L33:   0.4295 L12:  -0.2093                                     
REMARK   3      L13:  -0.4012 L23:   0.2536                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0050 S12:  -0.0175 S13:   0.0550                       
REMARK   3      S21:   0.0436 S22:   0.0539 S23:  -0.1103                       
REMARK   3      S31:   0.0287 S32:   0.0151 S33:  -0.0488                       
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. U VALUES WITH TLS ADDED.                                 
REMARK   4                                                                      
REMARK   4 3Q74 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063277.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 113                                
REMARK 200  PH                             : 7.5                                
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          : BRUKER AXS MICROSTAR               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRUKER PLATINUM 135                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT                              
REMARK 200  DATA SCALING SOFTWARE          : SAINT                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42718                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 51.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 8.440                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.40700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 84.8800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.73600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, 20% PEG 3350, 2 MM DTT,      
REMARK 280  0.02% AZIDE, PH 7.5, HANGING DROP, TEMPERATURE 293K                 
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       49.67250            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.65850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       49.67250            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       45.65850            
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: 3000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 240  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A   210                                                      
REMARK 465     LYS A   211                                                      
REMARK 465     SER A   212                                                      
REMARK 465     LEU A   213                                                      
REMARK 465     GLU A   214                                                      
REMARK 465     GLU A   215                                                      
REMARK 465     ALA A   216                                                      
REMARK 465     ARG A   217                                                      
REMARK 465     LYS A   218                                                      
REMARK 465     ILE A   219                                                      
REMARK 465     PHE A   220                                                      
REMARK 465     ARG A   221                                                      
REMARK 465     PHE A   222                                                      
REMARK 465     GLU B   210                                                      
REMARK 465     LYS B   211                                                      
REMARK 465     SER B   212                                                      
REMARK 465     LEU B   213                                                      
REMARK 465     GLU B   214                                                      
REMARK 465     GLU B   215                                                      
REMARK 465     ALA B   216                                                      
REMARK 465     ARG B   217                                                      
REMARK 465     LYS B   218                                                      
REMARK 465     ILE B   219                                                      
REMARK 465     PHE B   220                                                      
REMARK 465     ARG B   221                                                      
REMARK 465     PHE B   222                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A  141   CE   NZ                                             
REMARK 480     LYS B   36   NZ                                                  
REMARK 480     GLU B  116   CB   CG   CD   OE1  OE2                             
REMARK 480     LYS B  120   CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B 116   CA    GLU B 116   CB     -0.133                       
REMARK 500    LYS B 120   CB    LYS B 120   CG     -0.215                       
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    ARG A  13      -72.29    -60.08                                   
REMARK 500    GLN A  67      113.79     72.27                                   
REMARK 500    ASP A 171      112.19   -163.30                                   
REMARK 500    GLN B  67      113.72     74.34                                   
REMARK 500    GLU B 116       45.96    -90.57                                   
REMARK 500    LYS B 117      -46.82   -130.22                                   
REMARK 500    ASP B 171      108.13   -166.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3Q74 A    2   222  UNP    P08263   GSTA1_HUMAN      2    222             
DBREF  3Q74 B    2   222  UNP    P08263   GSTA1_HUMAN      2    222             
SEQADV 3Q74 ALA A    7  UNP  P08263    LEU     7 ENGINEERED MUTATION            
SEQADV 3Q74 ALA B    7  UNP  P08263    LEU     7 ENGINEERED MUTATION            
SEQRES   1 A  221  ALA GLU LYS PRO LYS ALA HIS TYR PHE ASN ALA ARG GLY          
SEQRES   2 A  221  ARG MET GLU SER THR ARG TRP LEU LEU ALA ALA ALA GLY          
SEQRES   3 A  221  VAL GLU PHE GLU GLU LYS PHE ILE LYS SER ALA GLU ASP          
SEQRES   4 A  221  LEU ASP LYS LEU ARG ASN ASP GLY TYR LEU MET PHE GLN          
SEQRES   5 A  221  GLN VAL PRO MET VAL GLU ILE ASP GLY MET LYS LEU VAL          
SEQRES   6 A  221  GLN THR ARG ALA ILE LEU ASN TYR ILE ALA SER LYS TYR          
SEQRES   7 A  221  ASN LEU TYR GLY LYS ASP ILE LYS GLU ARG ALA LEU ILE          
SEQRES   8 A  221  ASP MET TYR ILE GLU GLY ILE ALA ASP LEU GLY GLU MET          
SEQRES   9 A  221  ILE LEU LEU LEU PRO VAL CYS PRO PRO GLU GLU LYS ASP          
SEQRES  10 A  221  ALA LYS LEU ALA LEU ILE LYS GLU LYS ILE LYS ASN ARG          
SEQRES  11 A  221  TYR PHE PRO ALA PHE GLU LYS VAL LEU LYS SER HIS GLY          
SEQRES  12 A  221  GLN ASP TYR LEU VAL GLY ASN LYS LEU SER ARG ALA ASP          
SEQRES  13 A  221  ILE HIS LEU VAL GLU LEU LEU TYR TYR VAL GLU GLU LEU          
SEQRES  14 A  221  ASP SER SER LEU ILE SER SER PHE PRO LEU LEU LYS ALA          
SEQRES  15 A  221  LEU LYS THR ARG ILE SER ASN LEU PRO THR VAL LYS LYS          
SEQRES  16 A  221  PHE LEU GLN PRO GLY SER PRO ARG LYS PRO PRO MET ASP          
SEQRES  17 A  221  GLU LYS SER LEU GLU GLU ALA ARG LYS ILE PHE ARG PHE          
SEQRES   1 B  221  ALA GLU LYS PRO LYS ALA HIS TYR PHE ASN ALA ARG GLY          
SEQRES   2 B  221  ARG MET GLU SER THR ARG TRP LEU LEU ALA ALA ALA GLY          
SEQRES   3 B  221  VAL GLU PHE GLU GLU LYS PHE ILE LYS SER ALA GLU ASP          
SEQRES   4 B  221  LEU ASP LYS LEU ARG ASN ASP GLY TYR LEU MET PHE GLN          
SEQRES   5 B  221  GLN VAL PRO MET VAL GLU ILE ASP GLY MET LYS LEU VAL          
SEQRES   6 B  221  GLN THR ARG ALA ILE LEU ASN TYR ILE ALA SER LYS TYR          
SEQRES   7 B  221  ASN LEU TYR GLY LYS ASP ILE LYS GLU ARG ALA LEU ILE          
SEQRES   8 B  221  ASP MET TYR ILE GLU GLY ILE ALA ASP LEU GLY GLU MET          
SEQRES   9 B  221  ILE LEU LEU LEU PRO VAL CYS PRO PRO GLU GLU LYS ASP          
SEQRES  10 B  221  ALA LYS LEU ALA LEU ILE LYS GLU LYS ILE LYS ASN ARG          
SEQRES  11 B  221  TYR PHE PRO ALA PHE GLU LYS VAL LEU LYS SER HIS GLY          
SEQRES  12 B  221  GLN ASP TYR LEU VAL GLY ASN LYS LEU SER ARG ALA ASP          
SEQRES  13 B  221  ILE HIS LEU VAL GLU LEU LEU TYR TYR VAL GLU GLU LEU          
SEQRES  14 B  221  ASP SER SER LEU ILE SER SER PHE PRO LEU LEU LYS ALA          
SEQRES  15 B  221  LEU LYS THR ARG ILE SER ASN LEU PRO THR VAL LYS LYS          
SEQRES  16 B  221  PHE LEU GLN PRO GLY SER PRO ARG LYS PRO PRO MET ASP          
SEQRES  17 B  221  GLU LYS SER LEU GLU GLU ALA ARG LYS ILE PHE ARG PHE          
FORMUL   3  HOH   *509(H2 O)                                                    
HELIX    1   1 MET A   16  ALA A   26  1                                  11    
HELIX    2   2 SER A   37  ASP A   47  1                                  11    
HELIX    3   3 GLN A   67  TYR A   79  1                                  13    
HELIX    4   4 ASP A   85  LEU A  109  1                                  25    
HELIX    5   5 PRO A  110  CYS A  112  5                                   3    
HELIX    6   6 GLU A  116  ARG A  131  1                                  16    
HELIX    7   7 ARG A  131  GLY A  144  1                                  14    
HELIX    8   8 SER A  154  ASP A  171  1                                  18    
HELIX    9   9 PHE A  178  ASN A  190  1                                  13    
HELIX   10  10 LEU A  191  GLN A  199  1                                   9    
HELIX   11  11 MET B   16  ALA B   26  1                                  11    
HELIX   12  12 SER B   37  ASP B   47  1                                  11    
HELIX   13  13 GLN B   67  TYR B   79  1                                  13    
HELIX   14  14 ASP B   85  LEU B  109  1                                  25    
HELIX   15  15 PRO B  110  CYS B  112  5                                   3    
HELIX   16  16 LYS B  117  ARG B  131  1                                  15    
HELIX   17  17 ARG B  131  GLY B  144  1                                  14    
HELIX   18  18 SER B  154  ASP B  171  1                                  18    
HELIX   19  19 PHE B  178  LEU B  191  1                                  14    
HELIX   20  20 LEU B  191  GLN B  199  1                                   9    
SHEET    1   A 4 GLU A  31  ILE A  35  0                                        
SHEET    2   A 4 LYS A   6  PHE A  10  1  N  ALA A   7   O  GLU A  31           
SHEET    3   A 4 MET A  57  ILE A  60 -1  O  MET A  57   N  HIS A   8           
SHEET    4   A 4 MET A  63  VAL A  66 -1  O  LEU A  65   N  VAL A  58           
SHEET    1   B 4 GLU B  31  ILE B  35  0                                        
SHEET    2   B 4 LYS B   6  PHE B  10  1  N  ALA B   7   O  LYS B  33           
SHEET    3   B 4 MET B  57  ILE B  60 -1  O  MET B  57   N  HIS B   8           
SHEET    4   B 4 MET B  63  VAL B  66 -1  O  LEU B  65   N  VAL B  58           
CISPEP   1 VAL A   55    PRO A   56          0         5.00                     
CISPEP   2 VAL B   55    PRO B   56          0         9.24                     
CRYST1   99.345   91.317   51.374  90.00  93.01  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      0.010066  0.000000  0.000530        0.00000                         
SCALE2      0.000000  0.010951  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019492        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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