GenomeNet

Database: PDB
Entry: 1B48
LinkDB: 1B48
Original site: 1B48 
HEADER    TRANSFERASE                             06-JAN-99   1B48              
TITLE     CRYSTAL STRUCTURE OF MGSTA4-4 IN COMPLEX WITH GSH CONJUGATE           
TITLE    2 OF 4-HYDROXYNONENAL IN ONE SUBUNIT AND GSH IN THE OTHER:             
TITLE    3 EVIDENCE OF SIGNALING ACROSS DIMER INTERFACE IN MGSTA4-4             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (GLUTATHIONE S-TRANSFERASE);                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GST, MGSTA4-4;                                              
COMPND   5 EC: 2.5.1.18;                                                        
COMPND   6 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 ORGAN: LUNG;                                                         
SOURCE   6 CELLULAR_LOCATION: CYTOPLASM;                                        
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE  10 EXPRESSION_SYSTEM_VARIANT: PET9A/MGSTA4;                             
SOURCE  11 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;                      
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIA                              
KEYWDS    CRYSTAL STRUCTURE, GLUTATHIONE S-TRANSFERASE, GST, SUBUNIT            
KEYWDS   2 COOPERATIVITY                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.XIAO,P.ZIMNIAK,X.JI                                                 
REVDAT   3   24-FEB-09 1B48    1       VERSN                                    
REVDAT   2   01-APR-03 1B48    1       JRNL                                     
REVDAT   1   29-SEP-99 1B48    0                                                
JRNL        AUTH   B.XIAO,S.P.SINGH,B.NANDURI,Y.C.AWASTHI,P.ZIMNIAK,            
JRNL        AUTH 2 X.JI                                                         
JRNL        TITL   CRYSTAL STRUCTURE OF A MURINE GLUTATHIONE                    
JRNL        TITL 2 S-TRANSFERASE IN COMPLEX WITH A GLUTATHIONE                  
JRNL        TITL 3 CONJUGATE OF 4-HYDROXYNON-2-ENAL IN ONE SUBUNIT              
JRNL        TITL 4 AND GLUTATHIONE IN THE OTHER: EVIDENCE OF                    
JRNL        TITL 5 SIGNALING ACROSS THE DIMER INTERFACE.                        
JRNL        REF    BIOCHEMISTRY                  V.  38 11887 1999              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   10508391                                                     
JRNL        DOI    10.1021/BI990468I                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   U.KRENGEL,K.H.SCHROTER,H.HOIER,A.ARKEMA,K.H.KALK,            
REMARK   1  AUTH 2 P.ZIMNIAK,B.W.DIJKSTRA                                       
REMARK   1  TITL   CRYSTAL STRUCTURE OF A MURINE ALPHA-CLASS                    
REMARK   1  TITL 2 GLUTATHIONE S-TRANSFERASE INVOLVED IN CELLULAR               
REMARK   1  TITL 3 DEFENSE AGAINST OXIDATIVE STRESS                             
REMARK   1  REF    FEBS LETT.                    V. 422   285 1998              
REMARK   1  REFN                   ISSN 0014-5793                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.843                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 20.000                         
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 2.6000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 87.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 15647                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R                          
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.244                           
REMARK   3   FREE R VALUE                     : 0.317                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 781                             
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           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.72                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 60.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1251                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3328                       
REMARK   3   BIN FREE R VALUE                    : 0.3589                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.34                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 73                           
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            : 3586                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 51                                      
REMARK   3   SOLVENT ATOMS            : 40                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.00                          
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) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.36                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 19.79                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.12                            
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  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: ALL DATA WERE INCLUDED IN MAP             
REMARK   3  CALCULATIONS.                                                       
REMARK   4                                                                      
REMARK   4 1B48 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB007123.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : ENRAF-NONIUS FR591                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAC SCIENCE DIP-2020               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15647                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
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     (%) : 87.4                               
REMARK 200  DATA REDUNDANCY                : 12.100                             
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 60.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.74                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.350                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1GUH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN IN HANGING           
REMARK 280  DROPS WHICH INITIALLY CONSISTED OF 0.11 MM PROTEIN IN 0.047 M       
REMARK 280  HEPES BUFFER (PH 7.5) CONTAINING 1.82 MM GLUTATHIONE, 10.91 MM      
REMARK 280  HNA-SG (GSH CONJUGATE OF 4-HYDROXYNONENAL), 9.1% ETHANOL, 4.5%      
REMARK 280  ISOPROPANOL, AND 6.5% PEG MONOMETHYL ETHER 5K (PH 7.5). THE         
REMARK 280  DROPS WERE EQUILIBRATED AT 293 K AGAINST WELL SOLUTION              
REMARK 280  CONTAINING 10% ISOPROPANOL AND 12% PEG MONOMETHYL ETHER 5K IN       
REMARK 280  80 MM HEPES BUFFER (PH 7.5).                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       57.22500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.07000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       57.22500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.07000            
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: 4420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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: 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   3       92.47    -40.55                                   
REMARK 500    LYS A   4       70.90   -119.39                                   
REMARK 500    PRO A   5       78.10    -61.44                                   
REMARK 500    TYR A   9     -166.04   -171.66                                   
REMARK 500    ALA A  24      -76.46    -54.28                                   
REMARK 500    GLU A  32       86.70    176.12                                   
REMARK 500    GLU A  36      -76.14   -104.10                                   
REMARK 500    LEU A  51      -77.37    -54.47                                   
REMARK 500    THR A  68      -87.38    -14.96                                   
REMARK 500    TYR A  79       31.30    -74.85                                   
REMARK 500    ASN A  80       72.52     37.62                                   
REMARK 500    LEU A  81       40.05   -147.04                                   
REMARK 500    LYS A 112     -112.23    -58.42                                   
REMARK 500    VAL A 149     -139.65    -86.08                                   
REMARK 500    ASN A 151       69.73     65.56                                   
REMARK 500    GLN A 152      143.47    176.17                                   
REMARK 500    GLU A 169       22.24    -77.79                                   
REMARK 500    LEU A 170      -41.88   -144.01                                   
REMARK 500    PRO A 208      159.28    -43.54                                   
REMARK 500    LYS A 221       54.84     36.20                                   
REMARK 500    PRO B   5      100.37    -42.54                                   
REMARK 500    TYR B   9      173.42    167.20                                   
REMARK 500    ARG B  13      -91.34    -55.14                                   
REMARK 500    GLU B  33     -154.47    -80.89                                   
REMARK 500    GLU B  36      -52.94   -126.92                                   
REMARK 500    LYS B  43      -70.22    -63.27                                   
REMARK 500    HIS B  49      -58.70   -136.88                                   
REMARK 500    LEU B  50       94.06    -65.10                                   
REMARK 500    THR B  68      -83.37    -22.12                                   
REMARK 500    LEU B  75      -76.20    -53.50                                   
REMARK 500    TYR B  79       57.43    -97.28                                   
REMARK 500    ASN B  80       33.53     18.88                                   
REMARK 500    LYS B  84      -64.99   -123.69                                   
REMARK 500    ARG B 131      -53.98   -170.57                                   
REMARK 500    PHE B 147     -160.01    -79.88                                   
REMARK 500    VAL B 149      -82.21   -128.32                                   
REMARK 500    ILE B 158      -70.33    -55.55                                   
REMARK 500    LEU B 175        9.98    -69.24                                   
REMARK 500    PRO B 192      -74.13    -33.94                                   
REMARK 500    ARG B 217       -6.75    -53.96                                   
REMARK 500    LYS B 221       66.48     67.27                                   
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 HAG A 223                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 223                 
DBREF  1B48 A    2   222  UNP    P24472   GSTA4_MOUSE      2    222             
DBREF  1B48 B    2   222  UNP    P24472   GSTA4_MOUSE      2    222             
SEQRES   1 A  221  ALA ALA LYS PRO LYS LEU TYR TYR PHE ASN GLY ARG GLY          
SEQRES   2 A  221  ARG MET GLU SER ILE ARG TRP LEU LEU ALA ALA ALA GLY          
SEQRES   3 A  221  VAL GLU PHE GLU GLU GLU PHE LEU GLU THR ARG GLU GLN          
SEQRES   4 A  221  TYR GLU LYS MET GLN LYS ASP GLY HIS LEU LEU PHE GLY          
SEQRES   5 A  221  GLN VAL PRO LEU VAL GLU ILE ASP GLY MET MET LEU THR          
SEQRES   6 A  221  GLN THR ARG ALA ILE LEU SER TYR LEU ALA ALA LYS TYR          
SEQRES   7 A  221  ASN LEU TYR GLY LYS ASP LEU LYS GLU ARG VAL ARG ILE          
SEQRES   8 A  221  ASP MET TYR ALA ASP GLY THR GLN ASP LEU MET MET MET          
SEQRES   9 A  221  ILE ALA VAL ALA PRO PHE LYS THR PRO LYS GLU LYS GLU          
SEQRES  10 A  221  GLU SER TYR ASP LEU ILE LEU SER ARG ALA LYS THR ARG          
SEQRES  11 A  221  TYR PHE PRO VAL PHE GLU LYS ILE LEU LYS ASP HIS GLY          
SEQRES  12 A  221  GLU ALA PHE LEU VAL GLY ASN GLN LEU SER TRP ALA ASP          
SEQRES  13 A  221  ILE GLN LEU LEU GLU ALA ILE LEU MET VAL GLU GLU LEU          
SEQRES  14 A  221  SER ALA PRO VAL LEU SER ASP PHE PRO LEU LEU GLN ALA          
SEQRES  15 A  221  PHE LYS THR ARG ILE SER ASN ILE PRO THR ILE LYS LYS          
SEQRES  16 A  221  PHE LEU GLN PRO GLY SER GLN ARG LYS PRO PRO PRO ASP          
SEQRES  17 A  221  GLY PRO TYR VAL GLU VAL VAL ARG ILE VAL LEU LYS PHE          
SEQRES   1 B  221  ALA ALA LYS PRO LYS LEU TYR TYR PHE ASN GLY ARG GLY          
SEQRES   2 B  221  ARG MET GLU SER ILE ARG TRP LEU LEU ALA ALA ALA GLY          
SEQRES   3 B  221  VAL GLU PHE GLU GLU GLU PHE LEU GLU THR ARG GLU GLN          
SEQRES   4 B  221  TYR GLU LYS MET GLN LYS ASP GLY HIS LEU LEU PHE GLY          
SEQRES   5 B  221  GLN VAL PRO LEU VAL GLU ILE ASP GLY MET MET LEU THR          
SEQRES   6 B  221  GLN THR ARG ALA ILE LEU SER TYR LEU ALA ALA LYS TYR          
SEQRES   7 B  221  ASN LEU TYR GLY LYS ASP LEU LYS GLU ARG VAL ARG ILE          
SEQRES   8 B  221  ASP MET TYR ALA ASP GLY THR GLN ASP LEU MET MET MET          
SEQRES   9 B  221  ILE ALA VAL ALA PRO PHE LYS THR PRO LYS GLU LYS GLU          
SEQRES  10 B  221  GLU SER TYR ASP LEU ILE LEU SER ARG ALA LYS THR ARG          
SEQRES  11 B  221  TYR PHE PRO VAL PHE GLU LYS ILE LEU LYS ASP HIS GLY          
SEQRES  12 B  221  GLU ALA PHE LEU VAL GLY ASN GLN LEU SER TRP ALA ASP          
SEQRES  13 B  221  ILE GLN LEU LEU GLU ALA ILE LEU MET VAL GLU GLU LEU          
SEQRES  14 B  221  SER ALA PRO VAL LEU SER ASP PHE PRO LEU LEU GLN ALA          
SEQRES  15 B  221  PHE LYS THR ARG ILE SER ASN ILE PRO THR ILE LYS LYS          
SEQRES  16 B  221  PHE LEU GLN PRO GLY SER GLN ARG LYS PRO PRO PRO ASP          
SEQRES  17 B  221  GLY PRO TYR VAL GLU VAL VAL ARG ILE VAL LEU LYS PHE          
HET    HAG  A 223      31                                                       
HET    GSH  B 223      20                                                       
HETNAM     HAG 4-S-GLUTATHIONYL-5-PENTYL-TETRAHYDRO-FURAN-2-OL                  
HETNAM     GSH GLUTATHIONE                                                      
HETSYN     HAG GSHNA                                                            
FORMUL   3  HAG    C19 H33 N3 O8 S                                              
FORMUL   4  GSH    C10 H17 N3 O6 S                                              
FORMUL   5  HOH   *40(H2 O)                                                     
HELIX    1   1 MET A   16  ALA A   26  5                                  11    
HELIX    2   2 ARG A   38  ASP A   47  1                                  10    
HELIX    3   3 THR A   68  LYS A   78  1                                  11    
HELIX    4   4 LEU A   86  PHE A  111  1                                  26    
HELIX    5   5 PRO A  114  ARG A  131  1                                  18    
HELIX    6   6 PHE A  133  ASP A  142  1                                  10    
HELIX    7   7 TRP A  155  GLU A  168  1                                  14    
HELIX    8   8 VAL A  174  ASP A  177  5                                   4    
HELIX    9   9 PRO A  179  SER A  189  1                                  11    
HELIX   10  10 PRO A  192  LEU A  198  1                                   7    
HELIX   11  11 GLY A  210  VAL A  219  1                                  10    
HELIX   12  12 GLY B   14  ALA B   25  1                                  12    
HELIX   13  13 ARG B   38  GLY B   48  1                                  11    
HELIX   14  14 THR B   68  LYS B   78  1                                  11    
HELIX   15  15 LEU B   86  ALA B  109  1                                  24    
HELIX   16  16 PRO B  114  LYS B  129  1                                  16    
HELIX   17  17 PHE B  133  HIS B  143  1                                  11    
HELIX   18  18 TRP B  155  GLU B  168  1                                  14    
HELIX   19  19 ALA B  172  ASP B  177  5                                   6    
HELIX   20  20 PRO B  179  SER B  189  1                                  11    
HELIX   21  21 PRO B  192  LEU B  198  1                                   7    
HELIX   22  22 GLY B  210  VAL B  219  1                                  10    
SHEET    1   A 3 LYS A   6  TYR A   8  0                                        
SHEET    2   A 3 LEU A  57  ILE A  60 -1  N  GLU A  59   O  LYS A   6           
SHEET    3   A 3 MET A  63  LEU A  65 -1  N  LEU A  65   O  VAL A  58           
SHEET    1   B 3 LYS B   6  TYR B   8  0                                        
SHEET    2   B 3 LEU B  57  ILE B  60 -1  N  GLU B  59   O  LYS B   6           
SHEET    3   B 3 MET B  63  LEU B  65 -1  N  LEU B  65   O  VAL B  58           
CISPEP   1 VAL A   55    PRO A   56          0         0.54                     
CISPEP   2 VAL B   55    PRO B   56          0         0.03                     
SITE     1 AC1 17 TYR A   9  GLY A  14  ARG A  15  GLN A  54                    
SITE     2 AC1 17 VAL A  55  PRO A  56  THR A  66  GLN A  67                    
SITE     3 AC1 17 THR A  68  ALA A 107  PHE A 111  TYR A 212                    
SITE     4 AC1 17 LEU A 220  PHE A 222  HOH A 304  ASP B  97                    
SITE     5 AC1 17 ARG B 131                                                     
SITE     1 AC2 11 ASP A  97  ARG A 131  TYR B  41  GLY B  53                    
SITE     2 AC2 11 GLN B  54  VAL B  55  THR B  66  GLN B  67                    
SITE     3 AC2 11 THR B  68  HOH B 310  HOH B 322                               
CRYST1  114.450   96.140   50.840  90.00  90.00  90.00 P 21 21 2     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      0.008737  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010401  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019669        0.00000                         
MTRIX1   1 -0.999560 -0.016641 -0.024543       76.44717    1                    
MTRIX2   1 -0.016804 -0.364064  0.931222        9.54691    1                    
MTRIX3   1 -0.024432  0.931225  0.363625       -5.14296    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system