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Entry: 1A0F
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HEADER    TRANSFERASE                             29-NOV-97   1A0F              
TITLE     CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM                   
TITLE    2 ESCHERICHIA COLI COMPLEXED WITH GLUTATHIONESULFONIC ACID             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: GLUTATHIONE-BINDING DOMAIN;                                
COMPND   5 SYNONYM: GST, GLUTATHIONE TRANSFERASE;                               
COMPND   6 EC: 2.5.1.18;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K12;                           
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K-12;                                                        
SOURCE   5 GENE: GST;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K12;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: K-12;                                      
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PUC18;                                    
SOURCE  10 EXPRESSION_SYSTEM_GENE: GST                                          
KEYWDS    TRANSFERASE, GLUTAHIONE CONJUGATION, DETOXIFICATION,                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.NISHIDA,S.HARADA,S.NOGUCHI,H.INOUE,K.TAKAHASHI,Y.SATOW              
REVDAT   2   24-FEB-09 1A0F    1       VERSN                                    
REVDAT   1   13-JAN-99 1A0F    0                                                
JRNL        AUTH   M.NISHIDA,S.HARADA,S.NOGUCHI,Y.SATOW,H.INOUE,                
JRNL        AUTH 2 K.TAKAHASHI                                                  
JRNL        TITL   THREE-DIMENSIONAL STRUCTURE OF ESCHERICHIA COLI              
JRNL        TITL 2 GLUTATHIONE S-TRANSFERASE COMPLEXED WITH                     
JRNL        TITL 3 GLUTATHIONE SULFONATE: CATALYTIC ROLES OF CYS10              
JRNL        TITL 4 AND HIS106.                                                  
JRNL        REF    J.MOL.BIOL.                   V. 281   135 1998              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   9680481                                                      
JRNL        DOI    10.1006/JMBI.1998.1927                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 24071                          
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) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1221                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.19                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1757                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460                       
REMARK   3   BIN FREE R VALUE                    : 0.2600                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 97                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.026                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3224                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 46                                      
REMARK   3   SOLVENT ATOMS            : 174                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.17                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.17                            
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) : 0.18                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.18                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.64                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.96                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.44                            
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) : NULL  ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; 2.500                
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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : GTS.PAR                                        
REMARK   3  PARAMETER FILE  3  : WAT.PAR                                        
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : GTS.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WAT.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1A0F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JUN-96                             
REMARK 200  TEMPERATURE           (KELVIN) : 277                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 11                                 
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 RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : BENT MIRRORS, COLLIMATOR,          
REMARK 200                                   DUEL SLITS                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26481                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.2                               
REMARK 200  DATA REDUNDANCY                : 8.300                              
REMARK 200  R MERGE                    (I) : 0.09200                            
REMARK 200  R SYM                      (I) : 0.09200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.24400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.6                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       45.32500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       25.60500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.69500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       25.60500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.32500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.69500            
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: 4890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 184   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG A 184   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 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    ALA A   9     -176.32    -61.28                                   
REMARK 500    GLU A  65      111.16     74.24                                   
REMARK 500    ASN A  87       -0.36     77.77                                   
REMARK 500    LEU A 105      -62.04   -102.74                                   
REMARK 500    HIS A 144     -125.95   -128.44                                   
REMARK 500    ASN B  39       35.54    -92.72                                   
REMARK 500    ASP B  59       36.96    -77.59                                   
REMARK 500    GLU B  65      113.97     72.16                                   
REMARK 500    ASN B  87       -2.59     80.21                                   
REMARK 500    LEU B 105      -60.39    -98.79                                   
REMARK 500    HIS B 144     -127.58   -123.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A  92         0.08    SIDE_CHAIN                              
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 GTS A 203                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTS B 203                 
DBREF  1A0F A    1   201  UNP    P0A9D2   GST_ECOLI        1    201             
DBREF  1A0F B    1   201  UNP    P0A9D2   GST_ECOLI        1    201             
SEQRES   1 A  201  MET LYS LEU PHE TYR LYS PRO GLY ALA CYS SER LEU ALA          
SEQRES   2 A  201  SER HIS ILE THR LEU ARG GLU SER GLY LYS ASP PHE THR          
SEQRES   3 A  201  LEU VAL SER VAL ASP LEU MET LYS LYS ARG LEU GLU ASN          
SEQRES   4 A  201  GLY ASP ASP TYR PHE ALA VAL ASN PRO LYS GLY GLN VAL          
SEQRES   5 A  201  PRO ALA LEU LEU LEU ASP ASP GLY THR LEU LEU THR GLU          
SEQRES   6 A  201  GLY VAL ALA ILE MET GLN TYR LEU ALA ASP SER VAL PRO          
SEQRES   7 A  201  ASP ARG GLN LEU LEU ALA PRO VAL ASN SER ILE SER ARG          
SEQRES   8 A  201  TYR LYS THR ILE GLU TRP LEU ASN TYR ILE ALA THR GLU          
SEQRES   9 A  201  LEU HIS LYS GLY PHE THR PRO LEU PHE ARG PRO ASP THR          
SEQRES  10 A  201  PRO GLU GLU TYR LYS PRO THR VAL ARG ALA GLN LEU GLU          
SEQRES  11 A  201  LYS LYS LEU GLN TYR VAL ASN GLU ALA LEU LYS ASP GLU          
SEQRES  12 A  201  HIS TRP ILE CYS GLY GLN ARG PHE THR ILE ALA ASP ALA          
SEQRES  13 A  201  TYR LEU PHE THR VAL LEU ARG TRP ALA TYR ALA VAL LYS          
SEQRES  14 A  201  LEU ASN LEU GLU GLY LEU GLU HIS ILE ALA ALA PHE MET          
SEQRES  15 A  201  GLN ARG MET ALA GLU ARG PRO GLU VAL GLN ASP ALA LEU          
SEQRES  16 A  201  SER ALA GLU GLY LEU LYS                                      
SEQRES   1 B  201  MET LYS LEU PHE TYR LYS PRO GLY ALA CYS SER LEU ALA          
SEQRES   2 B  201  SER HIS ILE THR LEU ARG GLU SER GLY LYS ASP PHE THR          
SEQRES   3 B  201  LEU VAL SER VAL ASP LEU MET LYS LYS ARG LEU GLU ASN          
SEQRES   4 B  201  GLY ASP ASP TYR PHE ALA VAL ASN PRO LYS GLY GLN VAL          
SEQRES   5 B  201  PRO ALA LEU LEU LEU ASP ASP GLY THR LEU LEU THR GLU          
SEQRES   6 B  201  GLY VAL ALA ILE MET GLN TYR LEU ALA ASP SER VAL PRO          
SEQRES   7 B  201  ASP ARG GLN LEU LEU ALA PRO VAL ASN SER ILE SER ARG          
SEQRES   8 B  201  TYR LYS THR ILE GLU TRP LEU ASN TYR ILE ALA THR GLU          
SEQRES   9 B  201  LEU HIS LYS GLY PHE THR PRO LEU PHE ARG PRO ASP THR          
SEQRES  10 B  201  PRO GLU GLU TYR LYS PRO THR VAL ARG ALA GLN LEU GLU          
SEQRES  11 B  201  LYS LYS LEU GLN TYR VAL ASN GLU ALA LEU LYS ASP GLU          
SEQRES  12 B  201  HIS TRP ILE CYS GLY GLN ARG PHE THR ILE ALA ASP ALA          
SEQRES  13 B  201  TYR LEU PHE THR VAL LEU ARG TRP ALA TYR ALA VAL LYS          
SEQRES  14 B  201  LEU ASN LEU GLU GLY LEU GLU HIS ILE ALA ALA PHE MET          
SEQRES  15 B  201  GLN ARG MET ALA GLU ARG PRO GLU VAL GLN ASP ALA LEU          
SEQRES  16 B  201  SER ALA GLU GLY LEU LYS                                      
HET    GTS  A 203      23                                                       
HET    GTS  B 203      23                                                       
HETNAM     GTS GLUTATHIONE SULFONIC ACID                                        
FORMUL   3  GTS    2(C10 H17 N3 O9 S)                                           
FORMUL   5  HOH   *174(H2 O)                                                    
HELIX    1   1 CYS A   10  GLU A   20  5                                  11    
HELIX    2   2 GLY A   66  ARG A   80  1                                  15    
HELIX    3   3 ILE A   89  GLU A  104  1                                  16    
HELIX    4   4 HIS A  106  PHE A  113  1                                   8    
HELIX    5   5 LYS A  122  ALA A  139  1                                  18    
HELIX    6   6 ILE A  153  VAL A  168  1                                  16    
HELIX    7   7 GLU A  176  ALA A  186  1                                  11    
HELIX    8   8 PRO A  189  ALA A  197  1                                   9    
HELIX    9   9 CYS B   10  GLU B   20  5                                  11    
HELIX   10  10 GLY B   66  ARG B   80  1                                  15    
HELIX   11  11 ILE B   89  GLU B  104  1                                  16    
HELIX   12  12 HIS B  106  PHE B  113  1                                   8    
HELIX   13  13 GLU B  119  LEU B  140  1                                  22    
HELIX   14  14 ILE B  153  ALA B  167  1                                  15    
HELIX   15  15 GLU B  176  ALA B  186  1                                  11    
HELIX   16  16 PRO B  189  GLU B  198  1                                  10    
SHEET    1   A 4 THR A  26  SER A  29  0                                        
SHEET    2   A 4 LYS A   2  TYR A   5  1  N  LEU A   3   O  THR A  26           
SHEET    3   A 4 ALA A  54  LEU A  56 -1  N  LEU A  56   O  LYS A   2           
SHEET    4   A 4 LEU A  62  THR A  64 -1  N  LEU A  63   O  LEU A  55           
SHEET    1   B 4 THR B  26  SER B  29  0                                        
SHEET    2   B 4 LYS B   2  TYR B   5  1  N  LEU B   3   O  THR B  26           
SHEET    3   B 4 ALA B  54  LEU B  56 -1  N  LEU B  56   O  LYS B   2           
SHEET    4   B 4 LEU B  62  THR B  64 -1  N  LEU B  63   O  LEU B  55           
CISPEP   1 VAL A   52    PRO A   53          0        -0.03                     
CISPEP   2 VAL B   52    PRO B   53          0        -0.05                     
SITE     1 AC1 15 ALA A   9  CYS A  10  LEU A  32  LYS A  35                    
SITE     2 AC1 15 GLN A  51  VAL A  52  GLU A  65  GLY A  66                    
SITE     3 AC1 15 HIS A 106  LYS A 107  HOH A 246  HOH A 247                    
SITE     4 AC1 15 ASN B  99  THR B 103  GLU B 104                               
SITE     1 AC2 16 ASN A  99  THR A 103  GLU A 104  ALA B   9                    
SITE     2 AC2 16 CYS B  10  LEU B  32  LYS B  35  GLN B  51                    
SITE     3 AC2 16 VAL B  52  GLU B  65  GLY B  66  HIS B 106                    
SITE     4 AC2 16 LYS B 107  TRP B 164  HOH B 234  HOH B 235                    
CRYST1   90.650   95.390   51.210  90.00  90.00  90.00 P 21 21 21    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      0.011031  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010483  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019527        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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