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Database: PDB
Entry: 1N2A
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Original site: 1N2A 
HEADER    TRANSFERASE                             22-OCT-02   1N2A              
TITLE     CRYSTAL STRUCTURE OF A BACTERIAL GLUTATHIONE TRANSFERASE              
TITLE    2 FROM ESCHERICHIA COLI WITH GLUTATHIONE SULFONATE IN THE              
TITLE    3 ACTIVE SITE                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.5.1.18;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: GT_1787923;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL-21(DE3);                                
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET20                                     
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.L.RIFE,J.F.PARSONS,G.XIAO,G.L.GILLILAND,R.N.ARMSTRONG               
REVDAT   3   24-FEB-09 1N2A    1       VERSN                                    
REVDAT   2   25-NOV-03 1N2A    1       JRNL                                     
REVDAT   1   04-NOV-03 1N2A    0                                                
JRNL        AUTH   C.L.RIFE,J.F.PARSONS,G.XIAO,G.L.GILLILAND,                   
JRNL        AUTH 2 R.N.ARMSTRONG                                                
JRNL        TITL   CONSERVED STRUCTURAL ELEMENTS IN GLUTATHIONE                 
JRNL        TITL 2 TRANSFERASE HOMOLOGUES ENCODED IN THE GENOME OF              
JRNL        TITL 3 ESCHERICHIA COLI                                             
JRNL        REF    PROTEINS                      V.  53   777 2003              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   14635120                                                     
JRNL        DOI    10.1002/PROT.10452                                           
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.17                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 4.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 23318                          
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 + TEST SET) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2563                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 807                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2110                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 88                           
REMARK   3   BIN FREE R VALUE                    : 0.2960                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3107                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 46                                      
REMARK   3   SOLVENT ATOMS            : 153                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.229         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.202         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.121         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.128         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3220 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2961 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4364 ; 1.858 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6900 ; 1.056 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   384 ; 6.240 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   495 ; 0.141 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3485 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   640 ; 0.007 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   740 ; 0.223 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3234 ; 0.235 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1682 ; 0.088 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   138 ; 0.171 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    13 ; 0.160 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    47 ; 0.343 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.118 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1939 ; 1.164 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3121 ; 2.081 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1281 ; 2.894 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1243 ; 4.759 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 1N2A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB017429.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-SEP-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 113                                
REMARK 200  PH                             : 4.7                                
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) : 1.54                               
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23318                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.04200                            
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1AOF                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3000, B-N-OCTYL-                     
REMARK 280  GLUCOPYRANOSIDE, GLUTATHIONE SULFONATE, SODIUM ACETATE, PH          
REMARK 280  4.7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                
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       23.80800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.46350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.58300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.46350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.80800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       28.58300            
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 DIMER COMPOSED OF CHAINS A      
REMARK 300 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: 4890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU B    32                                                      
REMARK 465     MET B    33                                                      
REMARK 465     LYS B    34                                                      
REMARK 465     LYS B    35                                                      
REMARK 465     ARG B    36                                                      
REMARK 465     LEU B    37                                                      
REMARK 465     GLU B    38                                                      
REMARK 465     ASN B    39                                                      
REMARK 465     GLY B    40                                                      
REMARK 465     ASP B    41                                                      
REMARK 465     ASP B    42                                                      
REMARK 465     ASP B   142                                                      
REMARK 465     GLU B   143                                                      
REMARK 465     HIS B   144                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG1  THR A    64     OE2  GLU B    96              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  24   CB  -  CG  -  OD2 ANGL. DEV. =   7.8 DEGREES          
REMARK 500    ASP A  59   CB  -  CG  -  OD2 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ARG A  80   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ASP A 116   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP A 142   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    LEU A 200   O   -  C   -  N   ANGL. DEV. = -10.0 DEGREES          
REMARK 500    ASP B  31   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP B  79   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    CYS B 147   CA  -  CB  -  SG  ANGL. DEV. =   7.4 DEGREES          
REMARK 500    ARG B 184   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG B 184   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  65      111.82     78.11                                   
REMARK 500    ASN A  87       -7.66     70.94                                   
REMARK 500    LEU A 105      -63.42    -97.60                                   
REMARK 500    HIS A 144     -104.18   -126.14                                   
REMARK 500    CYS A 147      -66.89    -95.57                                   
REMARK 500    GLU B  65      107.36     73.76                                   
REMARK 500    LEU B 105      -64.43   -102.69                                   
REMARK 500    LEU B 112       14.33    -67.41                                   
REMARK 500    PHE B 113      -35.75   -132.27                                   
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 GTS A 301                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTS B 401                 
DBREF  1N2A A    1   201  UNP    P0A9D2   GST_ECOLI        1    201             
DBREF  1N2A B    1   201  UNP    P0A9D2   GST_ECOLI        1    201             
SEQRES   1 A  201  MET LYS LEU PHE TYR LYS PRO GLY ALA CYS SER LEU ALA          
SEQRES   2 A  201  SER HIS ILE THR LEU ARG GLU SER GLY LYS ASP PHE THR          
SEQRES   3 A  201  LEU VAL SER VAL ASP LEU MET LYS LYS ARG LEU GLU ASN          
SEQRES   4 A  201  GLY ASP ASP TYR PHE ALA VAL ASN PRO LYS GLY GLN VAL          
SEQRES   5 A  201  PRO ALA LEU LEU LEU ASP ASP GLY THR LEU LEU THR GLU          
SEQRES   6 A  201  GLY VAL ALA ILE MET GLN TYR LEU ALA ASP SER VAL PRO          
SEQRES   7 A  201  ASP ARG GLN LEU LEU ALA PRO VAL ASN SER ILE SER ARG          
SEQRES   8 A  201  TYR LYS THR ILE GLU TRP LEU ASN TYR ILE ALA THR GLU          
SEQRES   9 A  201  LEU HIS LYS GLY PHE THR PRO LEU PHE ARG PRO ASP THR          
SEQRES  10 A  201  PRO GLU GLU TYR LYS PRO THR VAL ARG ALA GLN LEU GLU          
SEQRES  11 A  201  LYS LYS LEU GLN TYR VAL ASN GLU ALA LEU LYS ASP GLU          
SEQRES  12 A  201  HIS TRP ILE CYS GLY GLN ARG PHE THR ILE ALA ASP ALA          
SEQRES  13 A  201  TYR LEU PHE THR VAL LEU ARG TRP ALA TYR ALA VAL LYS          
SEQRES  14 A  201  LEU ASN LEU GLU GLY LEU GLU HIS ILE ALA ALA PHE MET          
SEQRES  15 A  201  GLN ARG MET ALA GLU ARG PRO GLU VAL GLN ASP ALA LEU          
SEQRES  16 A  201  SER ALA GLU GLY LEU LYS                                      
SEQRES   1 B  201  MET LYS LEU PHE TYR LYS PRO GLY ALA CYS SER LEU ALA          
SEQRES   2 B  201  SER HIS ILE THR LEU ARG GLU SER GLY LYS ASP PHE THR          
SEQRES   3 B  201  LEU VAL SER VAL ASP LEU MET LYS LYS ARG LEU GLU ASN          
SEQRES   4 B  201  GLY ASP ASP TYR PHE ALA VAL ASN PRO LYS GLY GLN VAL          
SEQRES   5 B  201  PRO ALA LEU LEU LEU ASP ASP GLY THR LEU LEU THR GLU          
SEQRES   6 B  201  GLY VAL ALA ILE MET GLN TYR LEU ALA ASP SER VAL PRO          
SEQRES   7 B  201  ASP ARG GLN LEU LEU ALA PRO VAL ASN SER ILE SER ARG          
SEQRES   8 B  201  TYR LYS THR ILE GLU TRP LEU ASN TYR ILE ALA THR GLU          
SEQRES   9 B  201  LEU HIS LYS GLY PHE THR PRO LEU PHE ARG PRO ASP THR          
SEQRES  10 B  201  PRO GLU GLU TYR LYS PRO THR VAL ARG ALA GLN LEU GLU          
SEQRES  11 B  201  LYS LYS LEU GLN TYR VAL ASN GLU ALA LEU LYS ASP GLU          
SEQRES  12 B  201  HIS TRP ILE CYS GLY GLN ARG PHE THR ILE ALA ASP ALA          
SEQRES  13 B  201  TYR LEU PHE THR VAL LEU ARG TRP ALA TYR ALA VAL LYS          
SEQRES  14 B  201  LEU ASN LEU GLU GLY LEU GLU HIS ILE ALA ALA PHE MET          
SEQRES  15 B  201  GLN ARG MET ALA GLU ARG PRO GLU VAL GLN ASP ALA LEU          
SEQRES  16 B  201  SER ALA GLU GLY LEU LYS                                      
HET    GTS  A 301      23                                                       
HET    GTS  B 401      23                                                       
HETNAM     GTS GLUTATHIONE SULFONIC ACID                                        
FORMUL   3  GTS    2(C10 H17 N3 O9 S)                                           
FORMUL   5  HOH   *153(H2 O)                                                    
HELIX    1   1 SER A   11  SER A   21  1                                  11    
HELIX    2   2 ASP A   42  VAL A   46  5                                   5    
HELIX    3   3 GLU A   65  SER A   76  1                                  12    
HELIX    4   4 VAL A   77  GLN A   81  5                                   5    
HELIX    5   5 SER A   88  LEU A  105  1                                  18    
HELIX    6   6 LEU A  105  ARG A  114  1                                  10    
HELIX    7   7 PRO A  118  GLU A  120  5                                   3    
HELIX    8   8 TYR A  121  LEU A  140  1                                  20    
HELIX    9   9 THR A  152  VAL A  168  1                                  17    
HELIX   10  10 LEU A  175  GLU A  187  1                                  13    
HELIX   11  11 ARG A  188  GLU A  198  1                                  11    
HELIX   12  12 SER B   11  SER B   21  1                                  11    
HELIX   13  13 GLU B   65  VAL B   77  1                                  13    
HELIX   14  14 PRO B   78  GLN B   81  5                                   4    
HELIX   15  15 SER B   88  LEU B  105  1                                  18    
HELIX   16  16 LEU B  105  THR B  110  1                                   6    
HELIX   17  17 PRO B  111  PHE B  113  5                                   3    
HELIX   18  18 TYR B  121  LEU B  140  1                                  20    
HELIX   19  19 THR B  152  VAL B  168  1                                  17    
HELIX   20  20 LEU B  175  ARG B  188  1                                  14    
HELIX   21  21 ARG B  188  GLU B  198  1                                  11    
SHEET    1   A 5 ARG A  36  LEU A  37  0                                        
SHEET    2   A 5 THR A  26  ASP A  31 -1  N  ASP A  31   O  ARG A  36           
SHEET    3   A 5 LYS A   2  TYR A   5  1  N  LEU A   3   O  VAL A  28           
SHEET    4   A 5 ALA A  54  LEU A  56 -1  O  ALA A  54   N  PHE A   4           
SHEET    5   A 5 LEU A  62  THR A  64 -1  O  LEU A  63   N  LEU A  55           
SHEET    1   B 4 THR B  26  SER B  29  0                                        
SHEET    2   B 4 LYS B   2  TYR B   5  1  N  LEU B   3   O  THR B  26           
SHEET    3   B 4 ALA B  54  LEU B  56 -1  O  LEU B  56   N  LYS B   2           
SHEET    4   B 4 LEU B  62  THR B  64 -1  O  LEU B  63   N  LEU B  55           
CISPEP   1 VAL A   52    PRO A   53          0         5.13                     
CISPEP   2 VAL B   52    PRO B   53          0         1.26                     
SITE     1 AC1 19 ALA A   9  CYS A  10  LYS A  35  GLN A  51                    
SITE     2 AC1 19 VAL A  52  PRO A  53  GLU A  65  GLY A  66                    
SITE     3 AC1 19 HIS A 106  LYS A 107  PHE A 113  TRP A 164                    
SITE     4 AC1 19 HOH A 302  HOH A 306  HOH A 381  HOH A 391                    
SITE     5 AC1 19 ASN B  99  THR B 103  GLU B 104                               
SITE     1 AC2 16 ASN A  99  THR A 103  GLU A 104  ALA B   9                    
SITE     2 AC2 16 CYS B  10  GLN B  51  VAL B  52  PRO B  53                    
SITE     3 AC2 16 GLU B  65  GLY B  66  HIS B 106  TRP B 164                    
SITE     4 AC2 16 HOH B 407  HOH B 427  HOH B 434  HOH B 445                    
CRYST1   47.616   57.166  134.927  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      0.021001  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017493  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007411        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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