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Database: PDB
Entry: 1YKC
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HEADER    TRANSFERASE                             17-JAN-05   1YKC              
TITLE     HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18) COMPLEXED WITH    
TITLE    2 GLUTATHIONE-DISULFIDE                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE MU 2;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GSTM2-2, GST CLASS-MU 2;                                    
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 GENE: GSTM2, GST4;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET3A;                                
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET3A-HGSTM2                              
KEYWDS    TRANSFERASE, GLUTATHIONE, CONJUGATION, GLUTATHIONE-DISULFIDE,         
KEYWDS   2 PROSTAGLANDIN E2, SYNTHASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.V.PATSKOVSKY,L.N.PATSKOVSKA,I.LISTOWSKY,S.C.ALMO                    
REVDAT   3   11-OCT-17 1YKC    1       REMARK                                   
REVDAT   2   24-FEB-09 1YKC    1       VERSN                                    
REVDAT   1   25-JAN-05 1YKC    0                                                
JRNL        AUTH   Y.V.PATSKOVSKY,L.N.PATSKOVSKA,I.LISTOWSKY,S.C.ALMO           
JRNL        TITL   SELECTIVE INHIBITORS OF PROSTAGLANDIN SYNTHASE ACTIVITY OF   
JRNL        TITL 2 HUMAN GLUTATHIONE S-TRANSFERASE M2-2                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   L.N.PATSKOVSKA,A.A.FEDOROV,Y.V.PATSKOVSKY,S.C.ALMO,          
REMARK   1  AUTH 2 I.LISTOWSKY                                                  
REMARK   1  TITL   EXPRESSION, CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS   
REMARK   1  TITL 2 OF LIGAND-FREE HUMAN GLUTATHIONE S-TRANSFERASE M2-2          
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  54   458 1998              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   S.RAGHUNATHAN,R.J.CHANDROSS,R.H.KRETSINGER,T.J.ALLISON,      
REMARK   1  AUTH 2 C.J.PENINGTON,G.S.RULE                                       
REMARK   1  TITL   CRYSTAL STRUCTURE OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE  
REMARK   1  TITL 2 GSTM2-2. EFFECTS OF LATTICE PACKING ON CONFORMATIONAL        
REMARK   1  TITL 3 HETEROGENEITY                                                
REMARK   1  REF    J.MOL.BIOL.                   V. 238   815 1994              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   W.R.VORACHEK,W.R.PEARSON,G.S.RULE                            
REMARK   1  TITL   CLONING, EXPRESSION, AND CHARACTERIZATION OF A CLASS-MU      
REMARK   1  TITL 2 GLUTATHIONE TRANSFERASE FROM HUMAN MUSCLE, THE PRODUCT OF    
REMARK   1  TITL 3 THE GST4 LOCUS                                               
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  88  4443 1991              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 152191.070                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 27617                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 846                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.23                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3663                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE                    : 0.3390                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 143                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.028                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3614                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 80                                      
REMARK   3   SOLVENT ATOMS            : 396                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 8.50                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.95000                                             
REMARK   3    B22 (A**2) : 5.22000                                              
REMARK   3    B33 (A**2) : -0.27000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.25                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.33                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.37                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.340                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.180 ; 2.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.860 ; 3.500                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.050 ; 3.500                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.310 ; 4.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.25                                                 
REMARK   3   BSOL        : 11.09                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN.PARAM                                  
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1YKC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JAN-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000031613.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28914                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
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     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 11.70                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : 0.07600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.25000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP, CCP4                                          
REMARK 200 STARTING MODEL: PDB ENTRY 2GTU                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, PH 6.50, VAPOR DIFFUSION,       
REMARK 280  SITTING DROP, TEMPERATURE 290K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       28.30500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.25000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.39500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.25000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.30500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.39500            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HOMODIMER. THE ASYMMETRIC UNIT  
REMARK 300 CONTAINS ONE FULL HOMODIMER (CHAINS A AND B)                         
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: 4850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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    TYR A   6      170.25    179.85                                   
REMARK 500    ASN A   8       43.08    -78.13                                   
REMARK 500    GLU A  48       19.15   -141.94                                   
REMARK 500    PRO A  57      116.68    -39.23                                   
REMARK 500    GLN A  71      104.16     72.06                                   
REMARK 500    ASN B   8       41.00    -75.14                                   
REMARK 500    PRO B  57      122.58    -30.89                                   
REMARK 500    GLN B  71      112.14     79.14                                   
REMARK 500    LEU B  85       43.66   -101.79                                   
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 GDS A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDS B 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2GTU   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF LIGAND-FREE HUMAN GLUTATHIONE-S-TRANSFERASE M2-2        
REMARK 900 RELATED ID: 1XW5   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN GLUTATHIONE-S-TRANSFERASE M2-2 COMPLEXED WITH     
REMARK 900 GLUTATHIONE                                                          
DBREF  1YKC A    1   217  UNP    P28161   GSTM2_HUMAN      1    217             
DBREF  1YKC B    1   217  UNP    P28161   GSTM2_HUMAN      1    217             
SEQRES   1 A  217  PRO MET THR LEU GLY TYR TRP ASN ILE ARG GLY LEU ALA          
SEQRES   2 A  217  HIS SER ILE ARG LEU LEU LEU GLU TYR THR ASP SER SER          
SEQRES   3 A  217  TYR GLU GLU LYS LYS TYR THR MET GLY ASP ALA PRO ASP          
SEQRES   4 A  217  TYR ASP ARG SER GLN TRP LEU ASN GLU LYS PHE LYS LEU          
SEQRES   5 A  217  GLY LEU ASP PHE PRO ASN LEU PRO TYR LEU ILE ASP GLY          
SEQRES   6 A  217  THR HIS LYS ILE THR GLN SER ASN ALA ILE LEU ARG TYR          
SEQRES   7 A  217  ILE ALA ARG LYS HIS ASN LEU CYS GLY GLU SER GLU LYS          
SEQRES   8 A  217  GLU GLN ILE ARG GLU ASP ILE LEU GLU ASN GLN PHE MET          
SEQRES   9 A  217  ASP SER ARG MET GLN LEU ALA LYS LEU CYS TYR ASP PRO          
SEQRES  10 A  217  ASP PHE GLU LYS LEU LYS PRO GLU TYR LEU GLN ALA LEU          
SEQRES  11 A  217  PRO GLU MET LEU LYS LEU TYR SER GLN PHE LEU GLY LYS          
SEQRES  12 A  217  GLN PRO TRP PHE LEU GLY ASP LYS ILE THR PHE VAL ASP          
SEQRES  13 A  217  PHE ILE ALA TYR ASP VAL LEU GLU ARG ASN GLN VAL PHE          
SEQRES  14 A  217  GLU PRO SER CYS LEU ASP ALA PHE PRO ASN LEU LYS ASP          
SEQRES  15 A  217  PHE ILE SER ARG PHE GLU GLY LEU GLU LYS ILE SER ALA          
SEQRES  16 A  217  TYR MET LYS SER SER ARG PHE LEU PRO ARG PRO VAL PHE          
SEQRES  17 A  217  THR LYS MET ALA VAL TRP GLY ASN LYS                          
SEQRES   1 B  217  PRO MET THR LEU GLY TYR TRP ASN ILE ARG GLY LEU ALA          
SEQRES   2 B  217  HIS SER ILE ARG LEU LEU LEU GLU TYR THR ASP SER SER          
SEQRES   3 B  217  TYR GLU GLU LYS LYS TYR THR MET GLY ASP ALA PRO ASP          
SEQRES   4 B  217  TYR ASP ARG SER GLN TRP LEU ASN GLU LYS PHE LYS LEU          
SEQRES   5 B  217  GLY LEU ASP PHE PRO ASN LEU PRO TYR LEU ILE ASP GLY          
SEQRES   6 B  217  THR HIS LYS ILE THR GLN SER ASN ALA ILE LEU ARG TYR          
SEQRES   7 B  217  ILE ALA ARG LYS HIS ASN LEU CYS GLY GLU SER GLU LYS          
SEQRES   8 B  217  GLU GLN ILE ARG GLU ASP ILE LEU GLU ASN GLN PHE MET          
SEQRES   9 B  217  ASP SER ARG MET GLN LEU ALA LYS LEU CYS TYR ASP PRO          
SEQRES  10 B  217  ASP PHE GLU LYS LEU LYS PRO GLU TYR LEU GLN ALA LEU          
SEQRES  11 B  217  PRO GLU MET LEU LYS LEU TYR SER GLN PHE LEU GLY LYS          
SEQRES  12 B  217  GLN PRO TRP PHE LEU GLY ASP LYS ILE THR PHE VAL ASP          
SEQRES  13 B  217  PHE ILE ALA TYR ASP VAL LEU GLU ARG ASN GLN VAL PHE          
SEQRES  14 B  217  GLU PRO SER CYS LEU ASP ALA PHE PRO ASN LEU LYS ASP          
SEQRES  15 B  217  PHE ILE SER ARG PHE GLU GLY LEU GLU LYS ILE SER ALA          
SEQRES  16 B  217  TYR MET LYS SER SER ARG PHE LEU PRO ARG PRO VAL PHE          
SEQRES  17 B  217  THR LYS MET ALA VAL TRP GLY ASN LYS                          
HET    GDS  A 400      40                                                       
HET    GDS  B 401      40                                                       
HETNAM     GDS OXIDIZED GLUTATHIONE DISULFIDE                                   
FORMUL   3  GDS    2(C20 H32 N6 O12 S2)                                         
FORMUL   5  HOH   *396(H2 O)                                                    
HELIX    1   1 ALA A   13  THR A   23  1                                  11    
HELIX    2   2 ARG A   42  ASN A   47  1                                   6    
HELIX    3   3 GLU A   48  LEU A   52  5                                   5    
HELIX    4   4 GLN A   71  LYS A   82  1                                  12    
HELIX    5   5 SER A   89  ASP A  116  1                                  28    
HELIX    6   6 ASP A  118  GLY A  142  1                                  25    
HELIX    7   7 THR A  153  GLU A  170  1                                  18    
HELIX    8   8 PHE A  177  LEU A  190  1                                  14    
HELIX    9   9 LEU A  190  SER A  199  1                                  10    
HELIX   10  10 ALA B   13  THR B   23  1                                  11    
HELIX   11  11 ARG B   42  ASN B   47  1                                   6    
HELIX   12  12 GLN B   71  HIS B   83  1                                  13    
HELIX   13  13 SER B   89  ASP B  116  1                                  28    
HELIX   14  14 ASP B  118  GLY B  142  1                                  25    
HELIX   15  15 THR B  153  GLU B  170  1                                  18    
HELIX   16  16 PRO B  171  ASP B  175  5                                   5    
HELIX   17  17 PHE B  177  GLY B  189  1                                  13    
HELIX   18  18 LEU B  190  MET B  197  1                                   8    
SHEET    1   A 4 TYR A  27  TYR A  32  0                                        
SHEET    2   A 4 MET A   2  TRP A   7  1  N  TYR A   6   O  TYR A  32           
SHEET    3   A 4 TYR A  61  ASP A  64 -1  O  ILE A  63   N  THR A   3           
SHEET    4   A 4 HIS A  67  THR A  70 -1  O  ILE A  69   N  LEU A  62           
SHEET    1   B 4 TYR B  27  TYR B  32  0                                        
SHEET    2   B 4 MET B   2  TRP B   7  1  N  MET B   2   O  GLU B  28           
SHEET    3   B 4 TYR B  61  ASP B  64 -1  O  TYR B  61   N  GLY B   5           
SHEET    4   B 4 HIS B  67  THR B  70 -1  O  HIS B  67   N  ASP B  64           
CISPEP   1 ALA A   37    PRO A   38          0         0.03                     
CISPEP   2 LEU A   59    PRO A   60          0        -0.23                     
CISPEP   3 ARG A  205    PRO A  206          0        -0.17                     
CISPEP   4 ALA B   37    PRO B   38          0         0.49                     
CISPEP   5 LEU B   59    PRO B   60          0         1.80                     
CISPEP   6 ARG B  205    PRO B  206          0         0.01                     
SITE     1 AC1 22 TYR A   6  TRP A   7  GLY A  11  LEU A  12                    
SITE     2 AC1 22 ARG A  42  TRP A  45  LYS A  49  ASN A  58                    
SITE     3 AC1 22 LEU A  59  GLN A  71  SER A  72  ARG A 107                    
SITE     4 AC1 22 ALA A 111  TYR A 115  ARG A 165  PHE A 208                    
SITE     5 AC1 22 HOH A 404  HOH A 421  HOH A 467  HOH A 469                    
SITE     6 AC1 22 HOH A 589  ASP B 105                                          
SITE     1 AC2 26 ASP A 105  HOH A 484  TYR B   6  TRP B   7                    
SITE     2 AC2 26 GLY B  11  LEU B  12  ARG B  42  TRP B  45                    
SITE     3 AC2 26 LYS B  49  ASN B  58  LEU B  59  GLN B  71                    
SITE     4 AC2 26 SER B  72  ARG B 107  ALA B 111  TYR B 115                    
SITE     5 AC2 26 ARG B 165  PHE B 208  HOH B 415  HOH B 492                    
SITE     6 AC2 26 HOH B 505  HOH B 538  HOH B 548  HOH B 585                    
SITE     7 AC2 26 HOH B 589  HOH B 599                                          
CRYST1   56.610   74.790  116.500  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017665  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013371  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008584        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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