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Database: PDB
Entry: 1F3A
LinkDB: 1F3A
Original site: 1F3A 
HEADER    TRANSFERASE                             01-JUN-00   1F3A              
TITLE     CRYSTAL STRUCTURE OF MGSTA1-1 IN COMPLEX WITH GSH                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE YA CHAIN;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.5.1.18;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET-11D                                   
KEYWDS    GLUTATHIONE S-TRANSFERASE, GLUTATHIONE, TRANSFERASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.GU,S.V.SINGH,X.JI                                                   
REVDAT   5   30-AUG-23 1F3A    1       AUTHOR JRNL   REMARK                     
REVDAT   4   04-OCT-17 1F3A    1       REMARK                                   
REVDAT   3   24-FEB-09 1F3A    1       VERSN                                    
REVDAT   2   01-APR-03 1F3A    1       JRNL                                     
REVDAT   1   18-OCT-00 1F3A    0                                                
JRNL        AUTH   Y.GU,S.V.SINGH,X.JI                                          
JRNL        TITL   RESIDUE R216 AND CATALYTIC EFFICIENCY OF A MURINE CLASS      
JRNL        TITL 2 ALPHA GLUTATHIONE S-TRANSFERASE TOWARD BENZO[A]PYRENE        
JRNL        TITL 3 7(R),8(S)-DIOL 9(S), 10(R)-EPOXIDE.                          
JRNL        REF    BIOCHEMISTRY                  V.  39 12552 2000              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   11027134                                                     
JRNL        DOI    10.1021/BI001396U                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   B.XIAO,S.P.SINGH,B.NANDURI,Y.C.AWASTHI,P.ZIMNIAK,X.JI        
REMARK   1  TITL   CRYSTAL STRUCTURE OF A MURINE GLUTATHIONE S-TRANSFERASE IN   
REMARK   1  TITL 2 COMPLEX WITH A GLUTATHIONE CONJUGATE OF 4-HYDROXYNON-2-ENAL  
REMARK   1  TITL 3 IN ONE SUBUNIT AND GLUTATHIONE IN THE OTHER: EVIDENCE OF     
REMARK   1  TITL 4 SIGNALING ACROSS THE DIMER INTERFACE                         
REMARK   1  REF    BIOCHEMISTRY                  V.  38 11887 1999              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  DOI    10.1021/BI990468I                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 34998                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1863                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3559                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 450                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.62                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.015                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.750                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1F3A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000011190.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X9B                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.92                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37317                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 3.710                              
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.35                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: DIFFERENCE FOURIER                                    
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, ISOPROPANOL, HEPES, PH 7.5,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 288K                     
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       49.65150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.81850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       49.65150            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       46.81850            
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: 4440 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 A 732  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 367  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     GLN A   222                                                      
REMARK 465     GLN B   222                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ILE B 221    CG1  CG2  CD1                                       
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     LYS B   220                                                      
REMARK 475     ILE B   221                                                      
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  12      -71.16    -64.08                                   
REMARK 500    GLN A  66      105.22     76.30                                   
REMARK 500    ASP A 170       96.92   -167.83                                   
REMARK 500    ALA A 218      -46.60   -169.35                                   
REMARK 500    PHE A 219     -162.49   -122.14                                   
REMARK 500    ARG B  12      -73.57    -65.57                                   
REMARK 500    GLN B  66      109.69     79.53                                   
REMARK 500    VAL B 109       26.93    -70.85                                   
REMARK 500    PRO B 113      -22.97    -33.64                                   
REMARK 500    ALA B 209      -66.66     -3.34                                   
REMARK 500    LYS B 210      -81.18    -52.34                                   
REMARK 500    GLN B 211      -47.77    -12.00                                   
REMARK 500    ALA B 218      -34.57   -152.77                                   
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 GSH A 224                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 226                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1B48   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MGSTA4-4 IN COMPLEX WITH GSH CONJUGATE OF 4-    
REMARK 900 HYDROXYNONENAL IN ONE SUBUNIT AND GSH IN THE OTHER                   
REMARK 900 RELATED ID: 1F3B   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MGSTA1-1 IN COMPLEX WITH GSH CONJUGATE OF       
REMARK 900 BENZO[A]PYRENE EPOXIDE                                               
DBREF  1F3A A    1   222  UNP    P13745   GSTA1_MOUSE      1    222             
DBREF  1F3A B    1   222  UNP    P13745   GSTA1_MOUSE      1    222             
SEQRES   1 A  222  ALA GLY LYS PRO VAL LEU HIS TYR PHE ASN ALA ARG GLY          
SEQRES   2 A  222  ARG MET GLU CYS ILE ARG TRP LEU LEU ALA ALA ALA GLY          
SEQRES   3 A  222  VAL GLU PHE GLU GLU LYS PHE ILE GLN SER PRO GLU ASP          
SEQRES   4 A  222  LEU GLU LYS LEU LYS LYS ASP GLY ASN LEU MET PHE ASP          
SEQRES   5 A  222  GLN VAL PRO MET VAL GLU ILE ASP GLY MET LYS LEU ALA          
SEQRES   6 A  222  GLN THR ARG ALA ILE LEU ASN TYR ILE ALA THR LYS TYR          
SEQRES   7 A  222  ASP LEU TYR GLY LYS ASP MET LYS GLU ARG ALA LEU ILE          
SEQRES   8 A  222  ASP MET TYR SER GLU GLY ILE LEU ASP LEU THR GLU MET          
SEQRES   9 A  222  ILE GLY GLN LEU VAL LEU CYS PRO PRO ASP GLN ARG GLU          
SEQRES  10 A  222  ALA LYS THR ALA LEU ALA LYS ASP ARG THR LYS ASN ARG          
SEQRES  11 A  222  TYR LEU PRO ALA PHE GLU LYS VAL LEU LYS SER HIS GLY          
SEQRES  12 A  222  GLN ASP TYR LEU VAL GLY ASN ARG LEU THR ARG VAL ASP          
SEQRES  13 A  222  ILE HIS LEU LEU GLU VAL LEU LEU TYR VAL GLU GLU PHE          
SEQRES  14 A  222  ASP ALA SER LEU LEU THR PRO PHE PRO LEU LEU LYS ALA          
SEQRES  15 A  222  PHE LYS SER ARG ILE SER SER LEU PRO ASN VAL LYS LYS          
SEQRES  16 A  222  PHE LEU GLN PRO GLY SER GLN ARG LYS PRO PRO MET ASP          
SEQRES  17 A  222  ALA LYS GLN ILE GLN GLU ALA ARG LYS ALA PHE LYS ILE          
SEQRES  18 A  222  GLN                                                          
SEQRES   1 B  222  ALA GLY LYS PRO VAL LEU HIS TYR PHE ASN ALA ARG GLY          
SEQRES   2 B  222  ARG MET GLU CYS ILE ARG TRP LEU LEU ALA ALA ALA GLY          
SEQRES   3 B  222  VAL GLU PHE GLU GLU LYS PHE ILE GLN SER PRO GLU ASP          
SEQRES   4 B  222  LEU GLU LYS LEU LYS LYS ASP GLY ASN LEU MET PHE ASP          
SEQRES   5 B  222  GLN VAL PRO MET VAL GLU ILE ASP GLY MET LYS LEU ALA          
SEQRES   6 B  222  GLN THR ARG ALA ILE LEU ASN TYR ILE ALA THR LYS TYR          
SEQRES   7 B  222  ASP LEU TYR GLY LYS ASP MET LYS GLU ARG ALA LEU ILE          
SEQRES   8 B  222  ASP MET TYR SER GLU GLY ILE LEU ASP LEU THR GLU MET          
SEQRES   9 B  222  ILE GLY GLN LEU VAL LEU CYS PRO PRO ASP GLN ARG GLU          
SEQRES  10 B  222  ALA LYS THR ALA LEU ALA LYS ASP ARG THR LYS ASN ARG          
SEQRES  11 B  222  TYR LEU PRO ALA PHE GLU LYS VAL LEU LYS SER HIS GLY          
SEQRES  12 B  222  GLN ASP TYR LEU VAL GLY ASN ARG LEU THR ARG VAL ASP          
SEQRES  13 B  222  ILE HIS LEU LEU GLU VAL LEU LEU TYR VAL GLU GLU PHE          
SEQRES  14 B  222  ASP ALA SER LEU LEU THR PRO PHE PRO LEU LEU LYS ALA          
SEQRES  15 B  222  PHE LYS SER ARG ILE SER SER LEU PRO ASN VAL LYS LYS          
SEQRES  16 B  222  PHE LEU GLN PRO GLY SER GLN ARG LYS PRO PRO MET ASP          
SEQRES  17 B  222  ALA LYS GLN ILE GLN GLU ALA ARG LYS ALA PHE LYS ILE          
SEQRES  18 B  222  GLN                                                          
HET    GSH  A 224      20                                                       
HET    GSH  B 226      20                                                       
HETNAM     GSH GLUTATHIONE                                                      
FORMUL   3  GSH    2(C10 H17 N3 O6 S)                                           
FORMUL   5  HOH   *450(H2 O)                                                    
HELIX    1   1 MET A   15  ALA A   25  1                                  11    
HELIX    2   2 SER A   36  ASP A   46  1                                  11    
HELIX    3   3 GLN A   66  TYR A   78  1                                  13    
HELIX    4   4 ASP A   84  LEU A  108  1                                  25    
HELIX    5   5 VAL A  109  CYS A  111  5                                   3    
HELIX    6   6 GLN A  115  ARG A  130  1                                  16    
HELIX    7   7 ARG A  130  GLY A  143  1                                  14    
HELIX    8   8 THR A  153  ALA A  171  1                                  19    
HELIX    9   9 SER A  172  THR A  175  5                                   4    
HELIX   10  10 PHE A  177  SER A  189  1                                  13    
HELIX   11  11 LEU A  190  GLN A  198  1                                   9    
HELIX   12  12 ASP A  208  LYS A  217  1                                  10    
HELIX   13  13 MET B   15  GLY B   26  1                                  12    
HELIX   14  14 SER B   36  ASP B   46  1                                  11    
HELIX   15  15 GLN B   66  TYR B   78  1                                  13    
HELIX   16  16 ASP B   84  GLN B  107  1                                  24    
HELIX   17  17 LEU B  108  CYS B  111  5                                   4    
HELIX   18  18 GLN B  115  ARG B  130  1                                  16    
HELIX   19  19 ARG B  130  GLY B  143  1                                  14    
HELIX   20  20 THR B  153  ASP B  170  1                                  18    
HELIX   21  21 ALA B  171  THR B  175  5                                   5    
HELIX   22  22 PHE B  177  SER B  189  1                                  13    
HELIX   23  23 LEU B  190  GLN B  198  1                                   9    
HELIX   24  24 ASP B  208  LYS B  217  1                                  10    
SHEET    1   A 4 GLU A  30  ILE A  34  0                                        
SHEET    2   A 4 VAL A   5  PHE A   9  1  N  LEU A   6   O  GLU A  30           
SHEET    3   A 4 MET A  56  ILE A  59 -1  O  MET A  56   N  HIS A   7           
SHEET    4   A 4 MET A  62  ALA A  65 -1  N  MET A  62   O  ILE A  59           
SHEET    1   B 4 GLU B  30  PHE B  33  0                                        
SHEET    2   B 4 VAL B   5  TYR B   8  1  O  LEU B   6   N  LYS B  32           
SHEET    3   B 4 MET B  56  ILE B  59 -1  O  MET B  56   N  HIS B   7           
SHEET    4   B 4 MET B  62  ALA B  65 -1  N  MET B  62   O  ILE B  59           
CISPEP   1 VAL A   54    PRO A   55          0         0.52                     
CISPEP   2 VAL B   54    PRO B   55          0         0.93                     
SITE     1 AC1 17 TYR A   8  ARG A  14  LYS A  44  GLN A  53                    
SITE     2 AC1 17 VAL A  54  PRO A  55  GLN A  66  THR A  67                    
SITE     3 AC1 17 HOH A 382  HOH A 498  HOH A 503  HOH A 611                    
SITE     4 AC1 17 HOH A 686  HOH A 754  ASP B 100  ARG B 130                    
SITE     5 AC1 17 HOH B 422                                                     
SITE     1 AC2 14 ASP A 100  ARG A 130  ARG B  14  LYS B  44                    
SITE     2 AC2 14 ASP B  52  GLN B  53  VAL B  54  PRO B  55                    
SITE     3 AC2 14 GLN B  66  THR B  67  HOH B 345  HOH B 464                    
SITE     4 AC2 14 HOH B 598  HOH B 636                                          
CRYST1   99.303   93.637   52.217  90.00  91.80  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      0.010070  0.000000  0.000316        0.00000                         
SCALE2      0.000000  0.010680  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019160        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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