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Database: PDB
Entry: 1YJ6
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Original site: 1YJ6 
HEADER    TRANSFERASE                             13-JAN-05   1YJ6              
TITLE     CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE M1A-1A COMPLEXED 
TITLE    2 WITH GLUTATHIONYL-ZINC-TRIHYDROXIDE                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE MU 1;                            
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: GSTM1-1, GST CLASS-MU 1, GSTM1A-1A, GSTM1B-1B, HB SUBUNIT 4,
COMPND   5 GTH4;                                                                
COMPND   6 EC: 2.5.1.18;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GSTM1, GST1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET3A_HGSTM1A                             
KEYWDS    TRANSFERASE, GLUTATHIONE, CONJUGATION, DETOXIFICATION, CYTOSOLIC,     
KEYWDS   2 DIMER, ACTIVE SITE, ZINC, COORDINATION COMPLEX                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.V.PATSKOVSKY,L.N.PATSKOVSKA,I.LISTOWSKY,S.C.ALMO                    
REVDAT   3   11-OCT-17 1YJ6    1       REMARK                                   
REVDAT   2   24-FEB-09 1YJ6    1       VERSN                                    
REVDAT   1   01-FEB-05 1YJ6    0                                                
JRNL        AUTH   Y.V.PATSKOVSKY,L.N.PATSKOVSKA,I.LISTOWSKY,S.C.ALMO           
JRNL        TITL   HUMAN GLUTATHIONE S-TRANSFERASE M1A-1A CATALYZES FORMATION   
JRNL        TITL 2 OF GSH-METAL COMPLEXES                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   Y.V.PATSKOVSKY,L.N.PATSKOVSKA,I.LISTOWSKY                    
REMARK   1  TITL   FUNCTIONS OF HIS-107 IN THE CATALYTIC MECHANISM OF HUMAN     
REMARK   1  TITL 2 GLUTATHIONE S-TRANSFERASE HGSTM1A-1A                         
REMARK   1  REF    BIOCHEMISTRY                  V.  38  1193 1999              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 137983.260                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 22694                          
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 SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 674                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 68.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2779                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4010                       
REMARK   3   BIN FREE R VALUE                    : 0.3750                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 89                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.040                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5412                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 63                                      
REMARK   3   SOLVENT ATOMS            : 106                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -9.04000                                             
REMARK   3    B22 (A**2) : 13.28000                                             
REMARK   3    B33 (A**2) : -4.24000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.28000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.38                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.73                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.43                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.77                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.110                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.430 ; 2.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.720 ; 3.500                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.940 ; 3.500                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.510 ; 4.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.27                                                 
REMARK   3   BSOL        : 10.00                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN.PARAM                                  
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1YJ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000031574.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23285                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.4                               
REMARK 200  DATA REDUNDANCY                : 11.50                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : 0.04900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 61.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.39000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP (CCP4), CCP4 (MOLREP)                          
REMARK 200 STARTING MODEL: 1GTU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, GSH, ZINC CHLORIDE, PH 6.00,    
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 280K                                   
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       89.32000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.70500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       89.32000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       25.70500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HOMODIMER. THE ASYMMETRIC UNIT  
REMARK 300 CONTAINS ONE FULL HOMODIMER (CHAINS A,B) AND A MONOMER (CHAIN C)     
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: 4160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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 350   BIOMT1   2 -1.000000  0.000000  0.000000       50.36801            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -79.15337            
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     MET A     0                                                      
REMARK 465     MET B     0                                                      
REMARK 465     MET C     0                                                      
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  10      -76.55    -69.33                                   
REMARK 500    GLU A  48       -9.85   -157.67                                   
REMARK 500    PRO A  57      120.03    -39.23                                   
REMARK 500    GLN A  71      108.59     79.06                                   
REMARK 500    GLU A  88      -58.80   -129.20                                   
REMARK 500    ARG B  10      -74.81    -70.47                                   
REMARK 500    GLU B  48       -7.64   -157.06                                   
REMARK 500    PRO B  57      116.64    -39.49                                   
REMARK 500    GLN B  71      105.07     80.14                                   
REMARK 500    GLU B  88      -60.10   -126.67                                   
REMARK 500    GLU B 118       30.78    -94.15                                   
REMARK 500    ARG C  10      -70.30    -72.28                                   
REMARK 500    GLU C  48       -7.55   -155.48                                   
REMARK 500    PRO C  57      115.95    -39.68                                   
REMARK 500    GLN C  71      103.22     77.35                                   
REMARK 500    GLU C  88      -57.07   -129.75                                   
REMARK 500    GLU C 118       33.93    -92.45                                   
REMARK 500    PHE C 208     -169.65   -119.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 219  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 257   O                                                      
REMARK 620 2 HOH A 258   O   117.0                                              
REMARK 620 3 HOH A 259   O   115.8 110.9                                        
REMARK 620 4 GSH A 218   SG2 103.3 101.9 105.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 219  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 253   O                                                      
REMARK 620 2 HOH B 251   O   109.6                                              
REMARK 620 3 HOH B 252   O   110.7  98.2                                        
REMARK 620 4 GSH B 218   SG2 105.4 113.0 119.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 219  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 249   O                                                      
REMARK 620 2 HOH C 251   O   125.3                                              
REMARK 620 3 HOH C 250   O   101.9 104.7                                        
REMARK 620 4 GSH C 218   SG2 108.6 111.4 101.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 219                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 219                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 219                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 218                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 218                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH C 218                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1GTU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF LIGAND-FREE HUMAN GLUTATHIONE-S-TRANSFERASE     
REMARK 900 M1A-1A                                                               
REMARK 900 RELATED ID: 1XW6   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE M1A-1A COMLEXED WITH    
REMARK 900 GLUTATHIONE                                                          
REMARK 900 RELATED ID: 1XWK   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE M1A-1A COMLEXED WITH    
REMARK 900 GLUTATHIONYL-S-DINITROBENZENE                                        
DBREF  1YJ6 A    1   217  UNP    P09488   GSTM1_HUMAN      1    217             
DBREF  1YJ6 B    1   217  UNP    P09488   GSTM1_HUMAN      1    217             
DBREF  1YJ6 C    1   217  UNP    P09488   GSTM1_HUMAN      1    217             
SEQADV 1YJ6 MET A    0  UNP  P09488              INITIATING METHIONINE          
SEQADV 1YJ6 MET B    0  UNP  P09488              INITIATING METHIONINE          
SEQADV 1YJ6 MET C    0  UNP  P09488              INITIATING METHIONINE          
SEQRES   1 A  218  MET PRO MET ILE LEU GLY TYR TRP ASP ILE ARG GLY LEU          
SEQRES   2 A  218  ALA HIS ALA ILE ARG LEU LEU LEU GLU TYR THR ASP SER          
SEQRES   3 A  218  SER TYR GLU GLU LYS LYS TYR THR MET GLY ASP ALA PRO          
SEQRES   4 A  218  ASP TYR ASP ARG SER GLN TRP LEU ASN GLU LYS PHE LYS          
SEQRES   5 A  218  LEU GLY LEU ASP PHE PRO ASN LEU PRO TYR LEU ILE ASP          
SEQRES   6 A  218  GLY ALA HIS LYS ILE THR GLN SER ASN ALA ILE LEU CYS          
SEQRES   7 A  218  TYR ILE ALA ARG LYS HIS ASN LEU CYS GLY GLU THR GLU          
SEQRES   8 A  218  GLU GLU LYS ILE ARG VAL ASP ILE LEU GLU ASN GLN THR          
SEQRES   9 A  218  MET ASP ASN HIS MET GLN LEU GLY MET ILE CYS TYR ASN          
SEQRES  10 A  218  PRO GLU PHE GLU LYS LEU LYS PRO LYS TYR LEU GLU GLU          
SEQRES  11 A  218  LEU PRO GLU LYS LEU LYS LEU TYR SER GLU PHE LEU GLY          
SEQRES  12 A  218  LYS ARG PRO TRP PHE ALA GLY ASN LYS ILE THR PHE VAL          
SEQRES  13 A  218  ASP PHE LEU VAL TYR ASP VAL LEU ASP LEU HIS ARG ILE          
SEQRES  14 A  218  PHE GLU PRO LYS CYS LEU ASP ALA PHE PRO ASN LEU LYS          
SEQRES  15 A  218  ASP PHE ILE SER ARG PHE GLU GLY LEU GLU LYS ILE SER          
SEQRES  16 A  218  ALA TYR MET LYS SER SER ARG PHE LEU PRO ARG PRO VAL          
SEQRES  17 A  218  PHE SER LYS MET ALA VAL TRP GLY ASN LYS                      
SEQRES   1 B  218  MET PRO MET ILE LEU GLY TYR TRP ASP ILE ARG GLY LEU          
SEQRES   2 B  218  ALA HIS ALA ILE ARG LEU LEU LEU GLU TYR THR ASP SER          
SEQRES   3 B  218  SER TYR GLU GLU LYS LYS TYR THR MET GLY ASP ALA PRO          
SEQRES   4 B  218  ASP TYR ASP ARG SER GLN TRP LEU ASN GLU LYS PHE LYS          
SEQRES   5 B  218  LEU GLY LEU ASP PHE PRO ASN LEU PRO TYR LEU ILE ASP          
SEQRES   6 B  218  GLY ALA HIS LYS ILE THR GLN SER ASN ALA ILE LEU CYS          
SEQRES   7 B  218  TYR ILE ALA ARG LYS HIS ASN LEU CYS GLY GLU THR GLU          
SEQRES   8 B  218  GLU GLU LYS ILE ARG VAL ASP ILE LEU GLU ASN GLN THR          
SEQRES   9 B  218  MET ASP ASN HIS MET GLN LEU GLY MET ILE CYS TYR ASN          
SEQRES  10 B  218  PRO GLU PHE GLU LYS LEU LYS PRO LYS TYR LEU GLU GLU          
SEQRES  11 B  218  LEU PRO GLU LYS LEU LYS LEU TYR SER GLU PHE LEU GLY          
SEQRES  12 B  218  LYS ARG PRO TRP PHE ALA GLY ASN LYS ILE THR PHE VAL          
SEQRES  13 B  218  ASP PHE LEU VAL TYR ASP VAL LEU ASP LEU HIS ARG ILE          
SEQRES  14 B  218  PHE GLU PRO LYS CYS LEU ASP ALA PHE PRO ASN LEU LYS          
SEQRES  15 B  218  ASP PHE ILE SER ARG PHE GLU GLY LEU GLU LYS ILE SER          
SEQRES  16 B  218  ALA TYR MET LYS SER SER ARG PHE LEU PRO ARG PRO VAL          
SEQRES  17 B  218  PHE SER LYS MET ALA VAL TRP GLY ASN LYS                      
SEQRES   1 C  218  MET PRO MET ILE LEU GLY TYR TRP ASP ILE ARG GLY LEU          
SEQRES   2 C  218  ALA HIS ALA ILE ARG LEU LEU LEU GLU TYR THR ASP SER          
SEQRES   3 C  218  SER TYR GLU GLU LYS LYS TYR THR MET GLY ASP ALA PRO          
SEQRES   4 C  218  ASP TYR ASP ARG SER GLN TRP LEU ASN GLU LYS PHE LYS          
SEQRES   5 C  218  LEU GLY LEU ASP PHE PRO ASN LEU PRO TYR LEU ILE ASP          
SEQRES   6 C  218  GLY ALA HIS LYS ILE THR GLN SER ASN ALA ILE LEU CYS          
SEQRES   7 C  218  TYR ILE ALA ARG LYS HIS ASN LEU CYS GLY GLU THR GLU          
SEQRES   8 C  218  GLU GLU LYS ILE ARG VAL ASP ILE LEU GLU ASN GLN THR          
SEQRES   9 C  218  MET ASP ASN HIS MET GLN LEU GLY MET ILE CYS TYR ASN          
SEQRES  10 C  218  PRO GLU PHE GLU LYS LEU LYS PRO LYS TYR LEU GLU GLU          
SEQRES  11 C  218  LEU PRO GLU LYS LEU LYS LEU TYR SER GLU PHE LEU GLY          
SEQRES  12 C  218  LYS ARG PRO TRP PHE ALA GLY ASN LYS ILE THR PHE VAL          
SEQRES  13 C  218  ASP PHE LEU VAL TYR ASP VAL LEU ASP LEU HIS ARG ILE          
SEQRES  14 C  218  PHE GLU PRO LYS CYS LEU ASP ALA PHE PRO ASN LEU LYS          
SEQRES  15 C  218  ASP PHE ILE SER ARG PHE GLU GLY LEU GLU LYS ILE SER          
SEQRES  16 C  218  ALA TYR MET LYS SER SER ARG PHE LEU PRO ARG PRO VAL          
SEQRES  17 C  218  PHE SER LYS MET ALA VAL TRP GLY ASN LYS                      
HET     ZN  A 219       1                                                       
HET    GSH  A 218      20                                                       
HET     ZN  B 219       1                                                       
HET    GSH  B 218      20                                                       
HET     ZN  C 219       1                                                       
HET    GSH  C 218      20                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     GSH GLUTATHIONE                                                      
FORMUL   4   ZN    3(ZN 2+)                                                     
FORMUL   5  GSH    3(C10 H17 N3 O6 S)                                           
FORMUL  10  HOH   *106(H2 O)                                                    
HELIX    1   1 LEU A   12  THR A   23  1                                  12    
HELIX    2   2 ARG A   42  ASN A   47  1                                   6    
HELIX    3   3 GLN A   71  LYS A   82  1                                  12    
HELIX    4   4 THR A   89  TYR A  115  1                                  27    
HELIX    5   5 GLU A  118  GLY A  142  1                                  25    
HELIX    6   6 PHE A  154  GLU A  170  1                                  17    
HELIX    7   7 PRO A  171  ASP A  175  5                                   5    
HELIX    8   8 PHE A  177  GLY A  189  1                                  13    
HELIX    9   9 LEU A  190  SER A  199  1                                  10    
HELIX   10  10 ALA B   13  THR B   23  1                                  11    
HELIX   11  11 ARG B   42  ASN B   47  1                                   6    
HELIX   12  12 GLN B   71  LYS B   82  1                                  12    
HELIX   13  13 THR B   89  ASN B  116  1                                  28    
HELIX   14  14 GLU B  118  GLY B  142  1                                  25    
HELIX   15  15 PHE B  154  GLU B  170  1                                  17    
HELIX   16  16 PRO B  171  ASP B  175  5                                   5    
HELIX   17  17 PHE B  177  GLY B  189  1                                  13    
HELIX   18  18 LEU B  190  SER B  199  1                                  10    
HELIX   19  19 ALA C   13  THR C   23  1                                  11    
HELIX   20  20 ARG C   42  ASN C   47  1                                   6    
HELIX   21  21 GLN C   71  LYS C   82  1                                  12    
HELIX   22  22 THR C   89  ASN C  116  1                                  28    
HELIX   23  23 GLU C  118  GLY C  142  1                                  25    
HELIX   24  24 THR C  153  GLU C  170  1                                  18    
HELIX   25  25 PRO C  171  ASP C  175  5                                   5    
HELIX   26  26 PHE C  177  GLY C  189  1                                  13    
HELIX   27  27 LEU C  190  SER C  199  1                                  10    
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  ILE A  63   N  ILE A   3           
SHEET    4   A 4 HIS 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 HIS B  67  THR B  70 -1  O  ILE B  69   N  LEU B  62           
SHEET    1   C 4 TYR C  27  TYR C  32  0                                        
SHEET    2   C 4 MET C   2  TRP C   7  1  N  MET C   2   O  GLU C  28           
SHEET    3   C 4 TYR C  61  ASP C  64 -1  O  ILE C  63   N  ILE C   3           
SHEET    4   C 4 HIS C  67  THR C  70 -1  O  HIS C  67   N  ASP C  64           
LINK        ZN    ZN A 219                 O   HOH A 257     1555   1555  1.87  
LINK        ZN    ZN A 219                 O   HOH A 258     1555   1555  1.94  
LINK        ZN    ZN A 219                 O   HOH A 259     1555   1555  1.86  
LINK        ZN    ZN B 219                 O   HOH B 253     1555   1555  1.83  
LINK        ZN    ZN B 219                 O   HOH B 251     1555   1555  1.98  
LINK        ZN    ZN B 219                 O   HOH B 252     1555   1555  1.93  
LINK        ZN    ZN C 219                 O   HOH C 249     1555   1555  1.87  
LINK        ZN    ZN C 219                 O   HOH C 251     1555   1555  1.88  
LINK        ZN    ZN C 219                 O   HOH C 250     1555   1555  1.93  
LINK        ZN    ZN A 219                 SG2 GSH A 218     1555   1555  2.20  
LINK         SG2 GSH B 218                ZN    ZN B 219     1555   1555  1.96  
LINK         SG2 GSH C 218                ZN    ZN C 219     1555   1555  2.00  
CISPEP   1 ALA A   37    PRO A   38          0         0.29                     
CISPEP   2 LEU A   59    PRO A   60          0         0.80                     
CISPEP   3 ARG A  205    PRO A  206          0        -0.32                     
CISPEP   4 ALA B   37    PRO B   38          0        -0.47                     
CISPEP   5 LEU B   59    PRO B   60          0         0.13                     
CISPEP   6 ARG B  205    PRO B  206          0        -0.12                     
CISPEP   7 ALA C   37    PRO C   38          0        -0.10                     
CISPEP   8 LEU C   59    PRO C   60          0        -0.46                     
CISPEP   9 ARG C  205    PRO C  206          0        -0.48                     
SITE     1 AC1  4 GSH A 218  HOH A 257  HOH A 258  HOH A 259                    
SITE     1 AC2  4 GSH B 218  HOH B 251  HOH B 252  HOH B 253                    
SITE     1 AC3  4 GSH C 218  HOH C 249  HOH C 250  HOH C 251                    
SITE     1 AC4 12 TRP A   7  LEU A  12  ARG A  42  TRP A  45                    
SITE     2 AC4 12 LYS A  49  ASN A  58  LEU A  59  GLN A  71                    
SITE     3 AC4 12 SER A  72   ZN A 219  HOH A 228  ASP B 105                    
SITE     1 AC5 15 ASP A 105  TRP B   7  LEU B  12  ARG B  42                    
SITE     2 AC5 15 TRP B  45  LYS B  49  ASN B  58  LEU B  59                    
SITE     3 AC5 15 GLN B  71  SER B  72  MET B 104   ZN B 219                    
SITE     4 AC5 15 HOH B 232  HOH B 243  HOH B 253                               
SITE     1 AC6 12 TYR C   6  LEU C  12  TRP C  45  LYS C  49                    
SITE     2 AC6 12 ASN C  58  LEU C  59  GLN C  71  SER C  72                    
SITE     3 AC6 12 MET C 104  ASP C 105   ZN C 219  HOH C 250                    
CRYST1  178.640   51.410   93.820  90.00 122.47  90.00 C 1 2 1      12          
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      0.005598  0.000000  0.003562        0.00000                         
SCALE2      0.000000  0.019451  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012634        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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