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Database: PDB
Entry: 3GX0
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Original site: 3GX0 
HEADER    TRANSFERASE                             01-APR-09   3GX0              
TITLE     CRYSTAL STRUCTURE OF GSH-DEPENDENT DISULFIDE BOND                     
TITLE    2 OXIDOREDUCTASE                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GST-LIKE PROTEIN YFCG;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: GSH-DEPENDENT DISULFIDE BOND OXIDOREDUCTASE;                
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K-12;                                                        
SOURCE   5 GENE: YFCG;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET20B(+)                                 
KEYWDS    TRANSFERASE, GLUTATHIONE, GLUTATHIONE DISULFIDE, DISULFIDE            
KEYWDS   2 BOND OXIDOREDUCTASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.LADNER,J.M.HARP,M.C.WADINGTON,R.N.ARMSTRONG                       
REVDAT   2   28-JUL-09 3GX0    1       JRNL                                     
REVDAT   1   07-JUL-09 3GX0    0                                                
JRNL        AUTH   M.C.WADINGTON,J.E.LADNER,N.V.STOURMAN,J.M.HARP,              
JRNL        AUTH 2 R.N.ARMSTRONG                                                
JRNL        TITL   ANALYSIS OF THE STRUCTURE AND FUNCTION OF YFCG FROM          
JRNL        TITL 2 ESCHERICHIA COLI REVEALS AN EFFICIENT AND UNIQUE             
JRNL        TITL 3 DISULFIDE BOND REDUCTASE.                                    
JRNL        REF    BIOCHEMISTRY                  V.  48  6559 2009              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   19537707                                                     
JRNL        DOI    10.1021/BI9008825                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 11342                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 584                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.42                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1486                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.96                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2490                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 93                           
REMARK   3   BIN FREE R VALUE                    : 0.3570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1658                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 93                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.87                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.01000                                             
REMARK   3    B22 (A**2) : -1.01000                                             
REMARK   3    B33 (A**2) : 2.02000                                              
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): 0.296         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.235         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.168         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.966         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.914                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1749 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2380 ; 1.662 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   205 ; 6.691 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    84 ;37.998 ;23.214       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   274 ;15.647 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;16.945 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   248 ; 0.122 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1371 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   852 ; 0.204 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1175 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   107 ; 0.160 ; 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):    68 ; 0.246 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.213 ; 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):  1043 ; 0.905 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1643 ; 1.594 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   815 ; 2.240 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   736 ; 3.427 ; 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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3GX0 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052411.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
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          : BRUKER AXS MICROSTAR               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MONTEL GRADED MULTILAYER           
REMARK 200                                   OPTICS FROM BRUKER NONIUS          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRUKER PLATINUM 135                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT                              
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12571                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 10.900                             
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.350                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN IN 20 MM POTASSIUM               
REMARK 280  DIHYDROGEN PHOSPHATE, 2 MM DTT, 1MM EDTA, 10 MM GLUTATHIONE.        
REMARK 280  WELL SOLUTION: 20% W/V PEG 3000, 100 MM ACETATE., VAPOR             
REMARK 280  DIFFUSION, HANGING DROP                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.99500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       34.24500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       34.24500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       27.99750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       34.24500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       34.24500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       83.99250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       34.24500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       34.24500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       27.99750            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       34.24500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       34.24500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       83.99250            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       55.99500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      111.99000            
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     LYS A   205                                                      
REMARK 465     ALA A   206                                                      
REMARK 465     GLN A   207                                                      
REMARK 465     LEU A   208                                                      
REMARK 465     GLY A   209                                                      
REMARK 465     ASP A   210                                                      
REMARK 465     GLU A   211                                                      
REMARK 465     ARG A   212                                                      
REMARK 465     SER A   213                                                      
REMARK 465     ASP A   214                                                      
REMARK 465     SER A   215                                                      
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   OG   SER A    47     O    HOH A   304              2.09            
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    LEU A  67   CA  -  CB  -  CG  ANGL. DEV. =  17.8 DEGREES          
REMARK 500    ARG A  92   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 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  71      110.80     78.56                                   
REMARK 500    HIS A 120       10.51   -140.16                                   
REMARK 500    ALA A 121      -44.97   -144.92                                   
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 301                 
DBREF  3GX0 A    1   215  UNP    P77526   YFCG_ECOLI       1    215             
SEQRES   1 A  215  MET ILE ASP LEU TYR PHE ALA PRO THR PRO ASN GLY HIS          
SEQRES   2 A  215  LYS ILE THR LEU PHE LEU GLU GLU ALA GLU LEU ASP TYR          
SEQRES   3 A  215  ARG LEU ILE LYS VAL ASP LEU GLY LYS GLY GLY GLN PHE          
SEQRES   4 A  215  ARG PRO GLU PHE LEU ARG ILE SER PRO ASN ASN LYS ILE          
SEQRES   5 A  215  PRO ALA ILE VAL ASP HIS SER PRO ALA ASP GLY GLY GLU          
SEQRES   6 A  215  PRO LEU SER LEU PHE GLU SER GLY ALA ILE LEU LEU TYR          
SEQRES   7 A  215  LEU ALA GLU LYS THR GLY LEU PHE LEU SER HIS GLU THR          
SEQRES   8 A  215  ARG GLU ARG ALA ALA THR LEU GLN TRP LEU PHE TRP GLN          
SEQRES   9 A  215  VAL GLY GLY LEU GLY PRO MET LEU GLY GLN ASN HIS HIS          
SEQRES  10 A  215  PHE ASN HIS ALA ALA PRO GLN THR ILE PRO TYR ALA ILE          
SEQRES  11 A  215  GLU ARG TYR GLN VAL GLU THR GLN ARG LEU TYR HIS VAL          
SEQRES  12 A  215  LEU ASN LYS ARG LEU GLU ASN SER PRO TRP LEU GLY GLY          
SEQRES  13 A  215  GLU ASN TYR SER ILE ALA ASP ILE ALA CYS TRP PRO TRP          
SEQRES  14 A  215  VAL ASN ALA TRP THR ARG GLN ARG ILE ASP LEU ALA MET          
SEQRES  15 A  215  TYR PRO ALA VAL LYS ASN TRP HIS GLU ARG ILE ARG SER          
SEQRES  16 A  215  ARG PRO ALA THR GLY GLN ALA LEU LEU LYS ALA GLN LEU          
SEQRES  17 A  215  GLY ASP GLU ARG SER ASP SER                                  
HET    GDS  A 301      40                                                       
HETNAM     GDS OXIDIZED GLUTATHIONE DISULFIDE                                   
FORMUL   2  GDS    C20 H32 N6 O12 S2                                            
FORMUL   3  HOH   *93(H2 O)                                                     
HELIX    1   1 THR A    9  GLU A   23  1                                  15    
HELIX    2   2 GLY A   36  PHE A   39  5                                   4    
HELIX    3   3 ARG A   40  ARG A   45  1                                   6    
HELIX    4   4 GLU A   71  GLY A   84  1                                  14    
HELIX    5   5 GLU A   90  GLY A  107  1                                  18    
HELIX    6   6 GLY A  107  ALA A  121  1                                  15    
HELIX    7   7 ILE A  126  SER A  151  1                                  26    
HELIX    8   8 SER A  160  ASN A  171  1                                  12    
HELIX    9   9 ALA A  172  ARG A  177  5                                   6    
HELIX   10  10 ASP A  179  MET A  182  5                                   4    
HELIX   11  11 TYR A  183  SER A  195  1                                  13    
HELIX   12  12 ARG A  196  LEU A  204  1                                   9    
SHEET    1   A 4 TYR A  26  LYS A  30  0                                        
SHEET    2   A 4 ILE A   2  PHE A   6  1  N  LEU A   4   O  ARG A  27           
SHEET    3   A 4 ALA A  54  ASP A  57 -1  O  ALA A  54   N  TYR A   5           
SHEET    4   A 4 LEU A  67  PHE A  70 -1  O  LEU A  67   N  ASP A  57           
CISPEP   1 ILE A   52    PRO A   53          0        -1.50                     
SITE     1 AC1 19 THR A   9  ASN A  11  GLN A  38  ASN A  50                    
SITE     2 AC1 19 LYS A  51  ILE A  52  GLU A  71  SER A  72                    
SITE     3 AC1 19 GLY A 109  PRO A 110  GLY A 113  ARG A 132                    
SITE     4 AC1 19 TRP A 169  HOH A 220  HOH A 271  HOH A 272                    
SITE     5 AC1 19 HOH A 273  HOH A 289  HOH A 297                               
CRYST1   68.490   68.490  111.990  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014601  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014601  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008929        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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