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Database: PDB
Entry: 1AQW
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Original site: 1AQW 
HEADER    TRANSFERASE/SUBSTRATE                   03-AUG-97   1AQW              
TITLE     GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH GLUTATHIONE                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE;                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: GST;                                                        
COMPND   5 EC: 2.5.1.18;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: PLACENTA;                                                     
SOURCE   6 CELLULAR_LOCATION: CYTOSOL;                                          
SOURCE   7 GENE: GTP_HUMAN;                                                     
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE, GLUTATHIONE S-TRANSFERASE, CLASS PI, TRANSFERASE-        
KEYWDS   2 SUBSTRATE COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.PRADE,R.HUBER,T.H.MANOHARAN,W.E.FAHL,W.REUTER                       
REVDAT   5   21-DEC-11 1AQW    1       HET                                      
REVDAT   4   27-JUL-11 1AQW    1       REMARK                                   
REVDAT   3   13-JUL-11 1AQW    1       VERSN                                    
REVDAT   2   24-FEB-09 1AQW    1       VERSN                                    
REVDAT   1   18-MAR-98 1AQW    0                                                
JRNL        AUTH   L.PRADE,R.HUBER,T.H.MANOHARAN,W.E.FAHL,W.REUTER              
JRNL        TITL   STRUCTURES OF CLASS PI GLUTATHIONE S-TRANSFERASE FROM HUMAN  
JRNL        TITL 2 PLACENTA IN COMPLEX WITH SUBSTRATE, TRANSITION-STATE         
JRNL        TITL 3 ANALOGUE AND INHIBITOR.                                      
JRNL        REF    STRUCTURE                     V.   5  1287 1997              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   9351803                                                      
JRNL        DOI    10.1016/S0969-2126(97)00281-5                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.REINEMER,H.W.DIRR,R.LADENSTEIN,R.HUBER,M.LO BELLO,         
REMARK   1  AUTH 2 G.FEDERICI,M.W.PARKER                                        
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE          
REMARK   1  TITL 2 S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH            
REMARK   1  TITL 3 S-HEXYLGLUTATHIONE AT 2.8 A RESOLUTION                       
REMARK   1  REF    J.MOL.BIOL.                   V. 227   214 1992              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.5                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 79175                          
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) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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           : 30                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.82                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2333                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4049                       
REMARK   3   BIN FREE R VALUE                    : 0.4004                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
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            : 6552                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 128                                     
REMARK   3   SOLVENT ATOMS            : 351                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.39                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.75                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.37                            
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) : 1.500 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.000 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.000 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.500 ; 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  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1AQW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
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        : 15-AUG-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 291                                
REMARK 200  PH                             : 6.5                                
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          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (AGROVATA, ROTAVATA)          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 80112                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 18.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       37.33500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: 4000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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    PRO A   2     -177.97    -64.50                                   
REMARK 500    GLN A  64      109.71     79.79                                   
REMARK 500    ASN A 110       38.16   -154.31                                   
REMARK 500    THR A 141     -101.56   -131.92                                   
REMARK 500    GLN B  64      111.48     82.54                                   
REMARK 500    ASN B 110       46.57   -162.96                                   
REMARK 500    THR B 141     -117.79   -115.29                                   
REMARK 500    TYR C   3      119.01     37.25                                   
REMARK 500    GLN C  64      112.71     80.83                                   
REMARK 500    ASN C 110       41.86   -148.49                                   
REMARK 500    THR C 141     -107.71   -114.30                                   
REMARK 500    GLN D  64      109.81     79.97                                   
REMARK 500    THR D 141     -120.41   -114.24                                   
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 2201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 2500                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 2101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 2600                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH C 2401                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES C 2700                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH D 2301                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES D 2800                
DBREF  1AQW A    1   209  UNP    P09211   GTP_HUMAN        1    209             
DBREF  1AQW B    1   209  UNP    P09211   GTP_HUMAN        1    209             
DBREF  1AQW C    1   209  UNP    P09211   GTP_HUMAN        1    209             
DBREF  1AQW D    1   209  UNP    P09211   GTP_HUMAN        1    209             
SEQRES   1 A  209  PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG          
SEQRES   2 A  209  CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN          
SEQRES   3 A  209  SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN          
SEQRES   4 A  209  GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN LEU          
SEQRES   5 A  209  PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER          
SEQRES   6 A  209  ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU          
SEQRES   7 A  209  TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET          
SEQRES   8 A  209  VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR ILE          
SEQRES   9 A  209  SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP ASP          
SEQRES  10 A  209  TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU          
SEQRES  11 A  209  THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE          
SEQRES  12 A  209  VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU          
SEQRES  13 A  209  ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY CYS          
SEQRES  14 A  209  LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG          
SEQRES  15 A  209  LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER          
SEQRES  16 A  209  PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS          
SEQRES  17 A  209  GLN                                                          
SEQRES   1 B  209  PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG          
SEQRES   2 B  209  CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN          
SEQRES   3 B  209  SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN          
SEQRES   4 B  209  GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN LEU          
SEQRES   5 B  209  PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER          
SEQRES   6 B  209  ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU          
SEQRES   7 B  209  TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET          
SEQRES   8 B  209  VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR ILE          
SEQRES   9 B  209  SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP ASP          
SEQRES  10 B  209  TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU          
SEQRES  11 B  209  THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE          
SEQRES  12 B  209  VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU          
SEQRES  13 B  209  ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY CYS          
SEQRES  14 B  209  LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG          
SEQRES  15 B  209  LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER          
SEQRES  16 B  209  PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS          
SEQRES  17 B  209  GLN                                                          
SEQRES   1 C  209  PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG          
SEQRES   2 C  209  CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN          
SEQRES   3 C  209  SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN          
SEQRES   4 C  209  GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN LEU          
SEQRES   5 C  209  PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER          
SEQRES   6 C  209  ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU          
SEQRES   7 C  209  TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET          
SEQRES   8 C  209  VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR ILE          
SEQRES   9 C  209  SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP ASP          
SEQRES  10 C  209  TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU          
SEQRES  11 C  209  THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE          
SEQRES  12 C  209  VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU          
SEQRES  13 C  209  ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY CYS          
SEQRES  14 C  209  LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG          
SEQRES  15 C  209  LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER          
SEQRES  16 C  209  PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS          
SEQRES  17 C  209  GLN                                                          
SEQRES   1 D  209  PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG          
SEQRES   2 D  209  CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN          
SEQRES   3 D  209  SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN          
SEQRES   4 D  209  GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN LEU          
SEQRES   5 D  209  PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER          
SEQRES   6 D  209  ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU          
SEQRES   7 D  209  TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET          
SEQRES   8 D  209  VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR ILE          
SEQRES   9 D  209  SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP ASP          
SEQRES  10 D  209  TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU          
SEQRES  11 D  209  THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE          
SEQRES  12 D  209  VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU          
SEQRES  13 D  209  ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY CYS          
SEQRES  14 D  209  LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG          
SEQRES  15 D  209  LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER          
SEQRES  16 D  209  PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS          
SEQRES  17 D  209  GLN                                                          
HET    GSH  A2201      20                                                       
HET    MES  A2500      12                                                       
HET    GSH  B2101      20                                                       
HET    MES  B2600      12                                                       
HET    GSH  C2401      20                                                       
HET    MES  C2700      12                                                       
HET    GSH  D2301      20                                                       
HET    MES  D2800      12                                                       
HETNAM     GSH GLUTATHIONE                                                      
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
FORMUL   5  GSH    4(C10 H17 N3 O6 S)                                           
FORMUL   6  MES    4(C6 H13 N O4 S)                                             
FORMUL  13  HOH   *351(H2 O)                                                    
HELIX    1   1 GLY A   12  ASP A   23  5                                  12    
HELIX    2   2 VAL A   35  GLU A   40  1                                   6    
HELIX    3   3 SER A   42  SER A   46  1                                   5    
HELIX    4   4 SER A   65  LEU A   76  1                                  12    
HELIX    5   5 GLN A   83  THR A  109  1                                  27    
HELIX    6   6 TYR A  111  GLN A  135  1                                  25    
HELIX    7   7 GLN A  137  GLY A  139  5                                   3    
HELIX    8   8 PHE A  150  LEU A  165  1                                  16    
HELIX    9   9 PRO A  174  SER A  184  1                                  11    
HELIX   10  10 PRO A  187  ALA A  194  1                                   8    
HELIX   11  11 PRO A  196  VAL A  199  1                                   4    
HELIX   12  12 GLY B   12  ASP B   23  5                                  12    
HELIX   13  13 VAL B   35  GLU B   40  1                                   6    
HELIX   14  14 SER B   42  SER B   46  1                                   5    
HELIX   15  15 SER B   65  LEU B   76  1                                  12    
HELIX   16  16 GLN B   83  THR B  109  1                                  27    
HELIX   17  17 TYR B  111  SER B  134  1                                  24    
HELIX   18  18 GLN B  137  GLY B  139  5                                   3    
HELIX   19  19 PHE B  150  LEU B  165  1                                  16    
HELIX   20  20 PRO B  174  ALA B  185  1                                  12    
HELIX   21  21 PRO B  187  ALA B  194  1                                   8    
HELIX   22  22 PRO B  196  VAL B  199  1                                   4    
HELIX   23  23 GLY C   12  ASP C   23  5                                  12    
HELIX   24  24 VAL C   35  GLU C   40  1                                   6    
HELIX   25  25 SER C   42  SER C   46  1                                   5    
HELIX   26  26 SER C   65  LEU C   76  1                                  12    
HELIX   27  27 GLN C   83  THR C  109  1                                  27    
HELIX   28  28 TYR C  111  SER C  134  1                                  24    
HELIX   29  29 GLN C  137  GLY C  139  5                                   3    
HELIX   30  30 PHE C  150  LEU C  165  1                                  16    
HELIX   31  31 CYS C  169  ALA C  172  5                                   4    
HELIX   32  32 PRO C  174  SER C  184  1                                  11    
HELIX   33  33 PRO C  187  ALA C  194  1                                   8    
HELIX   34  34 PRO C  196  VAL C  199  1                                   4    
HELIX   35  35 GLY D   12  ASP D   23  5                                  12    
HELIX   36  36 VAL D   35  GLU D   40  1                                   6    
HELIX   37  37 SER D   42  SER D   46  1                                   5    
HELIX   38  38 SER D   65  LEU D   76  1                                  12    
HELIX   39  39 GLN D   83  TYR D  108  1                                  26    
HELIX   40  40 TYR D  111  GLN D  135  1                                  25    
HELIX   41  41 GLN D  137  GLY D  139  5                                   3    
HELIX   42  42 PHE D  150  LEU D  165  1                                  16    
HELIX   43  43 PRO D  174  ALA D  185  1                                  12    
HELIX   44  44 PRO D  187  ALA D  194  1                                   8    
HELIX   45  45 PRO D  196  VAL D  199  1                                   4    
SHEET    1   A 4 TRP A  28  VAL A  33  0                                        
SHEET    2   A 4 TYR A   3  PHE A   8  1  N  TYR A   3   O  LYS A  29           
SHEET    3   A 4 LYS A  54  ASP A  57 -1  N  GLN A  56   O  THR A   4           
SHEET    4   A 4 LEU A  60  TYR A  63 -1  N  LEU A  62   O  PHE A  55           
SHEET    1   B 4 TRP B  28  VAL B  33  0                                        
SHEET    2   B 4 TYR B   3  PHE B   8  1  N  TYR B   3   O  LYS B  29           
SHEET    3   B 4 LYS B  54  ASP B  57 -1  N  GLN B  56   O  THR B   4           
SHEET    4   B 4 LEU B  60  TYR B  63 -1  N  LEU B  62   O  PHE B  55           
SHEET    1   C 4 LYS C  29  VAL C  33  0                                        
SHEET    2   C 4 THR C   4  PHE C   8  1  N  VAL C   5   O  LYS C  29           
SHEET    3   C 4 LYS C  54  ASP C  57 -1  N  GLN C  56   O  THR C   4           
SHEET    4   C 4 LEU C  60  TYR C  63 -1  N  LEU C  62   O  PHE C  55           
SHEET    1   D 4 TRP D  28  VAL D  33  0                                        
SHEET    2   D 4 TYR D   3  PHE D   8  1  N  TYR D   3   O  LYS D  29           
SHEET    3   D 4 LYS D  54  ASP D  57 -1  N  GLN D  56   O  THR D   4           
SHEET    4   D 4 LEU D  60  TYR D  63 -1  N  LEU D  62   O  PHE D  55           
CISPEP   1 PRO A    1    PRO A    2          0        -0.16                     
CISPEP   2 LEU A   52    PRO A   53          0        -0.41                     
CISPEP   3 LEU B   52    PRO B   53          0         0.57                     
CISPEP   4 LEU C   52    PRO C   53          0         0.47                     
CISPEP   5 LEU D   52    PRO D   53          0         0.60                     
SITE     1 AC1 13 TYR A   7  PHE A   8  ARG A  13  TRP A  38                    
SITE     2 AC1 13 LYS A  44  GLN A  51  LEU A  52  GLN A  64                    
SITE     3 AC1 13 SER A  65  HOH A3036  HOH A3247  HOH A3289                    
SITE     4 AC1 13 ASP B  98                                                     
SITE     1 AC2  6 ALA A  22  TRP A  28  GLU A  30  PHE A 192                    
SITE     2 AC2  6 GLU A 197  ASP C 171                                          
SITE     1 AC3 12 ASP A  98  TYR B   7  PHE B   8  ARG B  13                    
SITE     2 AC3 12 TRP B  38  LYS B  44  GLN B  51  LEU B  52                    
SITE     3 AC3 12 GLN B  64  SER B  65  HOH B3009  HOH B3095                    
SITE     1 AC4  5 ALA B  22  TRP B  28  GLU B  30  GLU B 197                    
SITE     2 AC4  5 ASP D 171                                                     
SITE     1 AC5 15 TYR C   7  PHE C   8  ARG C  13  TRP C  38                    
SITE     2 AC5 15 LYS C  44  GLN C  51  LEU C  52  PRO C  53                    
SITE     3 AC5 15 GLN C  64  SER C  65  HOH C3042  HOH C3098                    
SITE     4 AC5 15 HOH C3136  HOH C3343  ASP D  98                               
SITE     1 AC6  6 ALA C  22  TRP C  28  GLU C  30  PHE C 192                    
SITE     2 AC6  6 GLU C 197  HOH C3112                                          
SITE     1 AC7 14 ASP C  98  TYR D   7  PHE D   8  ARG D  13                    
SITE     2 AC7 14 TRP D  38  LYS D  44  GLN D  51  LEU D  52                    
SITE     3 AC7 14 PRO D  53  GLN D  64  SER D  65  HOH D3006                    
SITE     4 AC7 14 HOH D3073  HOH D3146                                          
SITE     1 AC8  5 ALA D  22  TRP D  28  GLU D  30  PHE D 192                    
SITE     2 AC8  5 GLU D 197                                                     
CRYST1   90.290   74.670   69.500  90.00  90.07  90.00 P 1 21 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      0.011075  0.000000  0.000014        0.00000                         
SCALE2      0.000000  0.013392  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014388        0.00000                         
MTRIX1   1 -0.999936 -0.010898 -0.003149        6.96130    1                    
MTRIX2   1 -0.010998  0.999371  0.033717       -0.33552    1                    
MTRIX3   1  0.002779  0.033750 -0.999426       29.98716    1                    
MTRIX1   2 -0.999950 -0.003618  0.009287       96.65886    1                    
MTRIX2   2 -0.003880  0.999590 -0.028351        1.51576    1                    
MTRIX3   2 -0.009180 -0.028386 -0.999555      100.08378    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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