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Database: PDB
Entry: 1ZL9
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Original site: 1ZL9 
HEADER    TRANSFERASE                             05-MAY-05   1ZL9              
TITLE     CRYSTAL STRUCTURE OF A MAJOR NEMATODE C.ELEGANS SPECIFIC GST (CE01613)
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE 5;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GST CLASS-SIGMA;                                            
COMPND   5 EC: 2.5.1.18;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;                         
SOURCE   3 ORGANISM_TAXID: 6239;                                                
SOURCE   4 GENE: GST-5, CE01613;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 PLYSS;                            
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET23D(NOVAGEN)                           
KEYWDS    GLUTATHIONE TRANSFERASE, C.ELEGANS, TRANSFERASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.A.KRIKSUNOV,Q.LIU,D.J.SCHULLER,A.M.CAMPBELL,J.BARRETT,P.M.BROPHY,   
AUTHOR   2 Q.HAO                                                                
REVDAT   3   14-DEC-11 1ZL9    1       HET    HETATM HETNAM FORMUL              
REVDAT   3 2                   1       REMARK                                   
REVDAT   2   24-FEB-09 1ZL9    1       VERSN                                    
REVDAT   1   17-MAY-05 1ZL9    0                                                
JRNL        AUTH   I.A.KRIKSUNOV,Q.LIU,D.J.SCHULLER,A.M.CAMPBELL,J.BARRETT,     
JRNL        AUTH 2 P.M.BROPHY,Q.HAO                                             
JRNL        TITL   CRYSTAL STRUCTURE OF A MAJOR NEMATODE C.ELEGANS SPECIFIC GST 
JRNL        TITL 2 (CE01613)                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.01 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) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 32388                          
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) : 0.152                           
REMARK   3   R VALUE            (WORKING SET) : 0.151                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 867                             
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) : 2.01                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.06                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2249                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1560                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 59                           
REMARK   3   BIN FREE R VALUE                    : 0.2030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3298                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 459                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.80000                                             
REMARK   3    B22 (A**2) : 0.89000                                              
REMARK   3    B33 (A**2) : -0.09000                                             
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): 0.144         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.145         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.084         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.901         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3428 ; 0.022 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3020 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4630 ; 1.748 ; 1.951       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7052 ; 1.156 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   412 ; 5.810 ; 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):   476 ; 0.286 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3832 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   742 ; 0.015 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   750 ; 0.220 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3321 ; 0.260 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1819 ; 0.090 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   339 ; 0.177 ; 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):     8 ; 0.200 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    28 ; 0.244 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    21 ; 0.196 ; 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):  2056 ; 1.146 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3278 ; 2.057 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 3.392 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1352 ; 5.194 ; 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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1ZL9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB032849.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-FEB-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9160                             
REMARK 200  MONOCHROMATOR                  : RH-COATED SI MONOCHROMATIC         
REMARK 200                                   MIRRORS                            
REMARK 200  OPTICS                         : RH-COATED SI MONOCHROMATIC         
REMARK 200                                   MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : ADXV, DENZO                        
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33450                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.400                              
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: 1TW9                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 65% MPD, PH 7.0, VAPOR DIFFUSION,        
REMARK 280  HANGING DROP, TEMPERATURE 298.0K                                    
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       29.48000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.79800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.13600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       46.79800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.48000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.13600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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: 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   O    ALA A    41     OG1  THR A    45              2.04            
REMARK 500   O    HOH A   650     O    HOH A   747              2.10            
REMARK 500   O    HOH A   589     O    HOH A   730              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR B 100   CE2   TYR B 100   CD2    -0.094                       
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 168   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ASP B  59   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG B 202   NE  -  CZ  -  NH1 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ARG B 202   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.1 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    ARG A  12      -73.85    -71.16                                   
REMARK 500    TRP A  39      -73.53    -59.82                                   
REMARK 500    GLN A  65      111.83     80.53                                   
REMARK 500    ARG B  12      -76.06    -77.31                                   
REMARK 500    GLN B  65      115.61     82.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ALA A  41        14.1      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1TW9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A NEMATODE-SPECIFIC GLUTATHIONE-S-              
REMARK 900 TRANSFERASE                                                          
DBREF  1ZL9 A    1   207  UNP    Q09596   GST5_CAEEL       1    207             
DBREF  1ZL9 B    1   207  UNP    Q09596   GST5_CAEEL       1    207             
SEQRES   1 A  207  MET VAL SER TYR LYS LEU THR TYR PHE ASN GLY ARG GLY          
SEQRES   2 A  207  ALA GLY GLU VAL SER ARG GLN ILE PHE ALA TYR ALA GLY          
SEQRES   3 A  207  GLN GLN TYR GLU ASP ASN ARG VAL THR GLN GLU GLN TRP          
SEQRES   4 A  207  PRO ALA LEU LYS GLU THR CYS ALA ALA PRO PHE GLY GLN          
SEQRES   5 A  207  LEU PRO PHE LEU GLU VAL ASP GLY LYS LYS LEU ALA GLN          
SEQRES   6 A  207  SER HIS ALA ILE ALA ARG PHE LEU ALA ARG GLU PHE LYS          
SEQRES   7 A  207  LEU ASN GLY LYS THR ALA TRP GLU GLU ALA GLN VAL ASN          
SEQRES   8 A  207  SER LEU ALA ASP GLN TYR LYS ASP TYR SER SER GLU ALA          
SEQRES   9 A  207  ARG PRO TYR PHE TYR ALA VAL MET GLY PHE GLY PRO GLY          
SEQRES  10 A  207  ASP VAL GLU THR LEU LYS LYS ASP ILE PHE LEU PRO ALA          
SEQRES  11 A  207  PHE GLU LYS PHE TYR GLY PHE LEU VAL ASN PHE LEU LYS          
SEQRES  12 A  207  ALA SER GLY SER GLY PHE LEU VAL GLY ASP SER LEU THR          
SEQRES  13 A  207  TRP ILE ASP LEU ALA ILE ALA GLN HIS SER ALA ASP LEU          
SEQRES  14 A  207  ILE ALA LYS GLY GLY ASP PHE SER LYS PHE PRO GLU LEU          
SEQRES  15 A  207  LYS ALA HIS ALA GLU LYS ILE GLN ALA ILE PRO GLN ILE          
SEQRES  16 A  207  LYS LYS TRP ILE GLU THR ARG PRO VAL THR PRO PHE              
SEQRES   1 B  207  MET VAL SER TYR LYS LEU THR TYR PHE ASN GLY ARG GLY          
SEQRES   2 B  207  ALA GLY GLU VAL SER ARG GLN ILE PHE ALA TYR ALA GLY          
SEQRES   3 B  207  GLN GLN TYR GLU ASP ASN ARG VAL THR GLN GLU GLN TRP          
SEQRES   4 B  207  PRO ALA LEU LYS GLU THR CYS ALA ALA PRO PHE GLY GLN          
SEQRES   5 B  207  LEU PRO PHE LEU GLU VAL ASP GLY LYS LYS LEU ALA GLN          
SEQRES   6 B  207  SER HIS ALA ILE ALA ARG PHE LEU ALA ARG GLU PHE LYS          
SEQRES   7 B  207  LEU ASN GLY LYS THR ALA TRP GLU GLU ALA GLN VAL ASN          
SEQRES   8 B  207  SER LEU ALA ASP GLN TYR LYS ASP TYR SER SER GLU ALA          
SEQRES   9 B  207  ARG PRO TYR PHE TYR ALA VAL MET GLY PHE GLY PRO GLY          
SEQRES  10 B  207  ASP VAL GLU THR LEU LYS LYS ASP ILE PHE LEU PRO ALA          
SEQRES  11 B  207  PHE GLU LYS PHE TYR GLY PHE LEU VAL ASN PHE LEU LYS          
SEQRES  12 B  207  ALA SER GLY SER GLY PHE LEU VAL GLY ASP SER LEU THR          
SEQRES  13 B  207  TRP ILE ASP LEU ALA ILE ALA GLN HIS SER ALA ASP LEU          
SEQRES  14 B  207  ILE ALA LYS GLY GLY ASP PHE SER LYS PHE PRO GLU LEU          
SEQRES  15 B  207  LYS ALA HIS ALA GLU LYS ILE GLN ALA ILE PRO GLN ILE          
SEQRES  16 B  207  LYS LYS TRP ILE GLU THR ARG PRO VAL THR PRO PHE              
HET    GSH  A 501      20                                                       
HET    GSH  B 502      20                                                       
HETNAM     GSH GLUTATHIONE                                                      
FORMUL   3  GSH    2(C10 H17 N3 O6 S)                                           
FORMUL   5  HOH   *459(H2 O)                                                    
HELIX    1   1 ARG A   12  ALA A   14  5                                   3    
HELIX    2   2 GLY A   15  GLY A   26  1                                  12    
HELIX    3   3 GLN A   38  THR A   45  1                                   8    
HELIX    4   4 GLN A   65  PHE A   77  1                                  13    
HELIX    5   5 THR A   83  MET A  112  1                                  30    
HELIX    6   6 ASP A  118  ILE A  126  1                                   9    
HELIX    7   7 ILE A  126  GLY A  146  1                                  21    
HELIX    8   8 THR A  156  LYS A  172  1                                  17    
HELIX    9   9 PHE A  179  ILE A  192  1                                  14    
HELIX   10  10 ILE A  192  ARG A  202  1                                  11    
HELIX   11  11 ARG B   12  ALA B   14  5                                   3    
HELIX   12  12 GLY B   15  GLY B   26  1                                  12    
HELIX   13  13 GLN B   38  THR B   45  1                                   8    
HELIX   14  14 GLN B   65  PHE B   77  1                                  13    
HELIX   15  15 THR B   83  GLY B  113  1                                  31    
HELIX   16  16 ASP B  118  ILE B  126  1                                   9    
HELIX   17  17 ILE B  126  GLY B  146  1                                  21    
HELIX   18  18 THR B  156  LYS B  172  1                                  17    
HELIX   19  19 PHE B  179  ILE B  192  1                                  14    
HELIX   20  20 ILE B  192  ARG B  202  1                                  11    
SHEET    1   A 4 GLU A  30  VAL A  34  0                                        
SHEET    2   A 4 TYR A   4  PHE A   9  1  N  LEU A   6   O  GLU A  30           
SHEET    3   A 4 PHE A  55  VAL A  58 -1  O  GLU A  57   N  LYS A   5           
SHEET    4   A 4 LYS A  61  ALA A  64 -1  O  LEU A  63   N  LEU A  56           
SHEET    1   B 4 GLU B  30  VAL B  34  0                                        
SHEET    2   B 4 TYR B   4  PHE B   9  1  N  TYR B   8   O  VAL B  34           
SHEET    3   B 4 PHE B  55  VAL B  58 -1  O  PHE B  55   N  THR B   7           
SHEET    4   B 4 LYS B  61  ALA B  64 -1  O  LEU B  63   N  LEU B  56           
CISPEP   1 LEU A   53    PRO A   54          0         0.36                     
CISPEP   2 LEU B   53    PRO B   54          0         2.78                     
SITE     1 AC1 17 PHE A   9  TRP A  39  LYS A  43  GLN A  52                    
SITE     2 AC1 17 LEU A  53  PRO A  54  GLN A  65  SER A  66                    
SITE     3 AC1 17 HOH A 508  HOH A 559  HOH A 605  HOH A 612                    
SITE     4 AC1 17 HOH A 614  HOH A 682  HOH A 732  HOH A 750                    
SITE     5 AC1 17 ASP B  99                                                     
SITE     1 AC2 16 ASP A  99  PHE B   9  TRP B  39  LYS B  43                    
SITE     2 AC2 16 GLN B  52  LEU B  53  PRO B  54  GLN B  65                    
SITE     3 AC2 16 SER B  66  HOH B 513  HOH B 582  HOH B 593                    
SITE     4 AC2 16 HOH B 651  HOH B 652  HOH B 660  HOH B 666                    
CRYST1   58.960   88.272   93.596  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      0.016961  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011329  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010684        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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