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Database: PDB
Entry: 1GUK
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HEADER    TRANSFERASE                             11-DEC-97   1GUK              
TITLE     CRYSTAL STRUCTURE OF MURINE ALPHA-CLASS GSTA4-4                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE A4-4;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MGSTA4-4, GST5.7;                                           
COMPND   5 EC: 2.5.1.18;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 ORGAN: LUNG;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GLUTATHIONE S-TRANSFERASE, GST, CRYSTAL STRUCTURE,                    
KEYWDS   2 OXIDATIVE STRESS, TRANSFERASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.KRENGEL,K.H.SCHROTER,H.HOIER,B.W.DIJKSTRA                           
REVDAT   2   24-FEB-09 1GUK    1       VERSN                                    
REVDAT   1   08-APR-98 1GUK    0                                                
JRNL        AUTH   U.KRENGEL,K.H.SCHROTER,H.HOIER,A.ARKEMA,K.H.KALK,            
JRNL        AUTH 2 P.ZIMNIAK,B.W.DIJKSTRA                                       
JRNL        TITL   CRYSTAL STRUCTURE OF A MURINE ALPHA-CLASS                    
JRNL        TITL 2 GLUTATHIONE S-TRANSFERASE INVOLVED IN CELLULAR               
JRNL        TITL 3 DEFENSE AGAINST OXIDATIVE STRESS.                            
JRNL        REF    FEBS LETT.                    V. 422   285 1998              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   9498801                                                      
JRNL        DOI    10.1016/S0014-5793(98)00026-X                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.843                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 5.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 77.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 9798                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R                          
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.234                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.03                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1089                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3140                       
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3432                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.34                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.71                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.23                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 2.91                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : TOPHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: DURING THE REFINEMENT, 10% OF THE         
REMARK   3  REFLECTIONS WERE SET ASIDE TO CALCULATE THE FREE R-FACTOR. THE      
REMARK   3  LAST CYCLE, WHICH RESULTED IN AN R-FACTOR OF 22.9% AND A FREE       
REMARK   3  R-FACTOR OF 30.3%, WAS THEN REPEATED USING ALL THE REFLECTIONS      
REMARK   3  FOR THE FINAL RESULTS.                                              
REMARK   4                                                                      
REMARK   4 1GUK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAR-94                          
REMARK 200  TEMPERATURE           (KELVIN) : 295                                
REMARK 200  PH                             : 8.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.5                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.04                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 180 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10477                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.0                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.07600                            
REMARK 200  R SYM                      (I) : 0.07600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.31900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.843                                          
REMARK 200 STARTING MODEL: HGSTA1-1 DIMER (1GUH)                                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION BY HANGING DROP          
REMARK 280  VAPOR DIFFUSION RESERVOIR: 9% PEG 8000, 0.1 M TRIS/HCL PH 8.1,      
REMARK 280  5% MPD PROTEIN: 10 MG/ML DISSOLVED IN H20 DROP: 5 + 5               
REMARK 280  MICROLITER, VAPOR DIFFUSION - HANGING DROP                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       57.15000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.95000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       57.15000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.95000            
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: 2540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     LEU A   220                                                      
REMARK 465     LYS A   221                                                      
REMARK 465     PHE A   222                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     LYS B     4                                                      
REMARK 465     PRO B   114                                                      
REMARK 465     LYS B   115                                                      
REMARK 465     GLU B   116                                                      
REMARK 465     LYS B   117                                                      
REMARK 465     GLU B   118                                                      
REMARK 465     GLU B   119                                                      
REMARK 465     LEU B   220                                                      
REMARK 465     LYS B   221                                                      
REMARK 465     PHE B   222                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A   9     -178.48    171.76                                   
REMARK 500    ARG A  13      -76.58    -80.02                                   
REMARK 500    GLU A  33      108.22   -168.35                                   
REMARK 500    GLU A  36      -78.90    -86.92                                   
REMARK 500    ARG A  38      -48.20     -7.27                                   
REMARK 500    LEU A  51      -71.65    -47.05                                   
REMARK 500    MET A  64       79.69   -103.69                                   
REMARK 500    THR A  66      -15.13   -142.39                                   
REMARK 500    THR A  68      -78.01    -41.62                                   
REMARK 500    ASN A  80       64.00    -45.53                                   
REMARK 500    GLU A 145      154.05    -15.33                                   
REMARK 500    PRO A 173      -77.54    -57.04                                   
REMARK 500    VAL A 174      -27.20     57.04                                   
REMARK 500    LEU A 175      -10.40   -153.55                                   
REMARK 500    PHE A 178       74.77   -112.56                                   
REMARK 500    TYR B   9     -178.55    171.65                                   
REMARK 500    ARG B  13      -75.85    -79.79                                   
REMARK 500    GLU B  33      109.00   -168.28                                   
REMARK 500    GLU B  36      -78.83    -87.24                                   
REMARK 500    ARG B  38      -47.94     -6.92                                   
REMARK 500    PRO B  56      157.50    -49.81                                   
REMARK 500    THR B  66      -21.79   -144.59                                   
REMARK 500    THR B  68      -74.88    -45.40                                   
REMARK 500    ASN B  80       64.99    -46.61                                   
REMARK 500    ARG B 131      -60.75    -97.72                                   
REMARK 500    GLU B 145      157.30    -13.41                                   
REMARK 500    PRO B 173      -76.73    -53.27                                   
REMARK 500    VAL B 174      -19.88     55.00                                   
REMARK 500    LEU B 175      -14.98   -156.32                                   
REMARK 500    ASP B 209      -75.75   -130.72                                   
REMARK 500    PRO B 211       47.28    -67.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 VAL A  174     LEU A  175                 -147.11                    
REMARK 500 PRO B  211     TYR B  212                  131.96                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    PHE A 178         0.09    SIDE_CHAIN                              
REMARK 500    PHE A 184         0.08    SIDE_CHAIN                              
REMARK 500    TYR A 212         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    PRO A 173         12.57                                           
REMARK 500    PRO B 173         13.20                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1GUK A    1   222  UNP    P24472   GSTA4_MOUSE      1    222             
DBREF  1GUK B    1   222  UNP    P24472   GSTA4_MOUSE      1    222             
SEQRES   1 A  222  MET ALA ALA LYS PRO LYS LEU TYR TYR PHE ASN GLY ARG          
SEQRES   2 A  222  GLY ARG MET GLU SER ILE ARG TRP LEU LEU ALA ALA ALA          
SEQRES   3 A  222  GLY VAL GLU PHE GLU GLU GLU PHE LEU GLU THR ARG GLU          
SEQRES   4 A  222  GLN TYR GLU LYS MET GLN LYS ASP GLY HIS LEU LEU PHE          
SEQRES   5 A  222  GLY GLN VAL PRO LEU VAL GLU ILE ASP GLY MET MET LEU          
SEQRES   6 A  222  THR GLN THR ARG ALA ILE LEU SER TYR LEU ALA ALA LYS          
SEQRES   7 A  222  TYR ASN LEU TYR GLY LYS ASP LEU LYS GLU ARG VAL ARG          
SEQRES   8 A  222  ILE ASP MET TYR ALA ASP GLY THR GLN ASP LEU MET MET          
SEQRES   9 A  222  MET ILE ALA VAL ALA PRO PHE LYS THR PRO LYS GLU LYS          
SEQRES  10 A  222  GLU GLU SER TYR ASP LEU ILE LEU SER ARG ALA LYS THR          
SEQRES  11 A  222  ARG TYR PHE PRO VAL PHE GLU LYS ILE LEU LYS ASP HIS          
SEQRES  12 A  222  GLY GLU ALA PHE LEU VAL GLY ASN GLN LEU SER TRP ALA          
SEQRES  13 A  222  ASP ILE GLN LEU LEU GLU ALA ILE LEU MET VAL GLU GLU          
SEQRES  14 A  222  LEU SER ALA PRO VAL LEU SER ASP PHE PRO LEU LEU GLN          
SEQRES  15 A  222  ALA PHE LYS THR ARG ILE SER ASN ILE PRO THR ILE LYS          
SEQRES  16 A  222  LYS PHE LEU GLN PRO GLY SER GLN ARG LYS PRO PRO PRO          
SEQRES  17 A  222  ASP GLY PRO TYR VAL GLU VAL VAL ARG ILE VAL LEU LYS          
SEQRES  18 A  222  PHE                                                          
SEQRES   1 B  222  MET ALA ALA LYS PRO LYS LEU TYR TYR PHE ASN GLY ARG          
SEQRES   2 B  222  GLY ARG MET GLU SER ILE ARG TRP LEU LEU ALA ALA ALA          
SEQRES   3 B  222  GLY VAL GLU PHE GLU GLU GLU PHE LEU GLU THR ARG GLU          
SEQRES   4 B  222  GLN TYR GLU LYS MET GLN LYS ASP GLY HIS LEU LEU PHE          
SEQRES   5 B  222  GLY GLN VAL PRO LEU VAL GLU ILE ASP GLY MET MET LEU          
SEQRES   6 B  222  THR GLN THR ARG ALA ILE LEU SER TYR LEU ALA ALA LYS          
SEQRES   7 B  222  TYR ASN LEU TYR GLY LYS ASP LEU LYS GLU ARG VAL ARG          
SEQRES   8 B  222  ILE ASP MET TYR ALA ASP GLY THR GLN ASP LEU MET MET          
SEQRES   9 B  222  MET ILE ALA VAL ALA PRO PHE LYS THR PRO LYS GLU LYS          
SEQRES  10 B  222  GLU GLU SER TYR ASP LEU ILE LEU SER ARG ALA LYS THR          
SEQRES  11 B  222  ARG TYR PHE PRO VAL PHE GLU LYS ILE LEU LYS ASP HIS          
SEQRES  12 B  222  GLY GLU ALA PHE LEU VAL GLY ASN GLN LEU SER TRP ALA          
SEQRES  13 B  222  ASP ILE GLN LEU LEU GLU ALA ILE LEU MET VAL GLU GLU          
SEQRES  14 B  222  LEU SER ALA PRO VAL LEU SER ASP PHE PRO LEU LEU GLN          
SEQRES  15 B  222  ALA PHE LYS THR ARG ILE SER ASN ILE PRO THR ILE LYS          
SEQRES  16 B  222  LYS PHE LEU GLN PRO GLY SER GLN ARG LYS PRO PRO PRO          
SEQRES  17 B  222  ASP GLY PRO TYR VAL GLU VAL VAL ARG ILE VAL LEU LYS          
SEQRES  18 B  222  PHE                                                          
HELIX    1   1 GLU A   17  ALA A   26  1                                  10    
HELIX    2   2 GLU A   39  LYS A   46  1                                   8    
HELIX    3   3 THR A   68  LYS A   78  1                                  11    
HELIX    4   4 LEU A   86  PHE A  111  1                                  26    
HELIX    5   5 PRO A  114  THR A  130  1                                  17    
HELIX    6   6 PHE A  133  HIS A  143  1                                  11    
HELIX    7   7 ASP A  157  GLU A  168  1                                  12    
HELIX    8   8 PRO A  179  SER A  189  1                                  11    
HELIX    9   9 PRO A  192  PHE A  197  1                                   6    
HELIX   10  10 GLY A  210  ILE A  218  1                                   9    
HELIX   11  11 GLU B   17  ALA B   26  1                                  10    
HELIX   12  12 GLU B   39  LYS B   46  1                                   8    
HELIX   13  13 THR B   68  LYS B   78  1                                  11    
HELIX   14  14 LEU B   86  PHE B  111  1                                  26    
HELIX   15  15 TYR B  121  THR B  130  1                                  10    
HELIX   16  16 PHE B  133  HIS B  143  1                                  11    
HELIX   17  17 ASP B  157  GLU B  168  1                                  12    
HELIX   18  18 PRO B  179  SER B  189  1                                  11    
HELIX   19  19 PRO B  192  LEU B  198  1                                   7    
HELIX   20  20 VAL B  213  ILE B  218  1                                   6    
SHEET    1   A 4 GLU A  31  PHE A  34  0                                        
SHEET    2   A 4 LYS A   6  TYR A   9  1  N  LEU A   7   O  GLU A  31           
SHEET    3   A 4 LEU A  57  ILE A  60 -1  N  GLU A  59   O  LYS A   6           
SHEET    4   A 4 MET A  63  LEU A  65 -1  N  LEU A  65   O  VAL A  58           
SHEET    1   B 4 GLU B  31  PHE B  34  0                                        
SHEET    2   B 4 LYS B   6  TYR B   9  1  N  LEU B   7   O  GLU B  31           
SHEET    3   B 4 LEU B  57  ILE B  60 -1  N  GLU B  59   O  LYS B   6           
SHEET    4   B 4 MET B  63  LEU B  65 -1  N  LEU B  65   O  VAL B  58           
CISPEP   1 VAL A   55    PRO A   56          0        11.96                     
CISPEP   2 VAL B   55    PRO B   56          0        11.22                     
CRYST1  114.300   95.900   50.800  90.00  90.00  90.00 P 21 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      0.008749  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010428  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019685        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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