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Database: PDB
Entry: 1GSH
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Original site: 1GSH 
HEADER    GLUTATHIONE BIOSYNTHESIS LIGASE         16-MAY-95   1GSH              
TITLE     STRUCTURE OF ESCHERICHIA COLI GLUTATHIONE SYNTHETASE AT PH 7.5        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE BIOSYNTHETIC LIGASE;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: GLUTATHIONE SYNTHASE;                                       
COMPND   5 EC: 6.3.2.3;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 37762;                                               
SOURCE   4 STRAIN: B;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM109;                                     
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PKGS00, A DERIVATIVE OF PKK223-3;         
SOURCE   9 EXPRESSION_SYSTEM_GENE: GSHII                                        
KEYWDS    GLUTATHIONE BIOSYNTHESIS, GLUTATHIONE SYNTHASE, GLUTATHIONE           
KEYWDS   2 BIOSYNTHESIS LIGASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.MATSUDA,H.KATO,H.YAMAGUCHI,T.NISHIOKA,Y.KATSUBE,J.ODA               
REVDAT   4   19-FEB-14 1GSH    1       REMARK                                   
REVDAT   3   13-JUL-11 1GSH    1       VERSN                                    
REVDAT   2   24-FEB-09 1GSH    1       VERSN                                    
REVDAT   1   11-JUL-96 1GSH    0                                                
JRNL        AUTH   K.MATSUDA,K.MIZUGUCHI,T.NISHIOKA,H.KATO,N.GO,J.ODA           
JRNL        TITL   CRYSTAL STRUCTURE OF GLUTATHIONE SYNTHETASE AT OPTIMAL PH:   
JRNL        TITL 2 DOMAIN ARCHITECTURE AND STRUCTURAL SIMILARITY WITH OTHER     
JRNL        TITL 3 PROTEINS.                                                    
JRNL        REF    PROTEIN ENG.                  V.   9  1083 1996              
JRNL        REFN                   ISSN 0269-2139                               
JRNL        PMID   9010922                                                      
JRNL        DOI    10.1093/PROTEIN/9.12.1083                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   H.KATO,T.TANAKA,H.YAMAGUCHI,T.HARA,T.NISHIOKA,Y.KATSUBE,     
REMARK   1  AUTH 2 J.ODA                                                        
REMARK   1  TITL   FLEXIBLE LOOP THAT IS NOVEL CATALYTIC MACHINERY IN A LIGASE. 
REMARK   1  TITL 2 ATOMIC STRUCTURE AND FUNCTION OF THE LOOPLESS GLUTATHIONE    
REMARK   1  TITL 3 SYNTHETASE                                                   
REMARK   1  REF    BIOCHEMISTRY                  V.  33  4995 1994              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.HIRATAKE,H.KATO,J.ODA                                      
REMARK   1  TITL   MECHANISM-BASED INACTIVATION OF GLUTATHIONE SYNTHETASE BY    
REMARK   1  TITL 2 PHOSPHINIC ACID TRANSITION-STATE ANALOGUE                    
REMARK   1  REF    J.AM.CHEM.SOC.                V. 116 12059 1994              
REMARK   1  REFN                   ISSN 0002-7863                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   T.HIBI,H.KATO,T.NISHIOKA,J.ODA,H.YAMAGUCHI,Y.KATSUBE,        
REMARK   1  AUTH 2 K.TANIZAWA,T.FUKUI                                           
REMARK   1  TITL   USE OF ADENOSINE (5')POLYPHOSPHO(5')PYRIDOXALS TO STUDY THE  
REMARK   1  TITL 2 SUBSTRATE-BINDING REGION OF GLUTATHIONE SYNTHETASE FROM      
REMARK   1  TITL 3 ESCHERICHIA COLI B                                           
REMARK   1  REF    BIOCHEMISTRY                  V.  32  1548 1993              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   T.TANAKA,H.YAMAGUCHI,H.KATO,T.NISHIOKA,Y.KATSUBE,J.ODA       
REMARK   1  TITL   FLEXIBILITY IMPAIRED BY MUTATIONS REVEALED THE               
REMARK   1  TITL 2 MULTIFUNCTIONAL ROLES OF THE LOOP IN GLUTATHIONE SYNTHETASE  
REMARK   1  REF    BIOCHEMISTRY                  V.  32 12398 1993              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   H.YAMAGUCHI,H.KATO,Y.HATA,T.NISHIOKA,A.KIMURA,J.ODA,         
REMARK   1  AUTH 2 Y.KATSUBE                                                    
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF THE GLUTATHIONE SYNTHETASE    
REMARK   1  TITL 2 FROM ESCHERICHIA COLI B AT 2.0 A RESOLUTION                  
REMARK   1  REF    J.MOL.BIOL.                   V. 229  1083 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   H.YAMAGUCHI,H.KATO,Y.HATA,T.NISHIOKA,J.ODA,Y.KATSUBE         
REMARK   1  TITL   STRUCTURAL STUDIES ON GLUTATHIONE SYNTHETASE FROM            
REMARK   1  TITL 2 ESCHERICHIA COLI B                                           
REMARK   1  REF    PHOTON FACTORY ACTIVITY       V.   9    85 1992              
REMARK   1  REF  2 REPORT                                                       
REMARK   1  REFN                   ISSN 0912-1803                               
REMARK   1 REFERENCE 7                                                          
REMARK   1  AUTH   H.KATO,H.YAMAGUCHI,Y.HATA,T.NISHIOKA,Y.KATSUBE,J.ODA         
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY STUDIES OF GLUTATHIONE 
REMARK   1  TITL 2 SYNTHETASE FROM ESCHERICHIA COLI B                           
REMARK   1  REF    J.MOL.BIOL.                   V. 209   503 1989              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 24108                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
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           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
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            : 2369                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 96                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.20                          
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) : 0.18                            
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) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.773                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.350                          
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.005                           
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) : 18.270; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 21.410; 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  : PARAM19X.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPH19X.PRO                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1GSH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
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        : 18-MAR-91                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6A                              
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          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : WEIS                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30967                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE PREPARED AT PH 7.5 BY      
REMARK 280  MICRODIALYSIS METHOD WITH AMMONIUM SULFATE AS THE PRECIPITATING     
REMARK 280  AGENT. THE INNER SOLUTION 100 MICROLITER CONTAINED 1.5 % (W/V)      
REMARK 280  GSHASE, 5 MM MGCL2 AND 10 % SATURATED AMMONIUM SULFATE IN 50 MM     
REMARK 280  TRIS-HCL BUFFER (PH 7.5). THE INNER SOLUTION WAS DIALYZED AGAINST   
REMARK 280  50 MM TRIS-HCL BUFFER (PH 7.5) WHICH CONTAINED 5 MM MGCL2 AND 25    
REMARK 280  % SATURATED AMMONIUM SULFATE.TRIS-HCL BUFFER, MICRODIALYSIS         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+2/3                                            
REMARK 290       6555   X-Y,X,Z+1/3                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+2/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+1/3                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.33333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       56.66667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      113.33333            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       56.66667            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      113.33333            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       56.66667            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      113.33333            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       56.66667            
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: TETRAMERIC                        
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 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      113.33333            
REMARK 350   BIOMT1   3  0.500000 -0.866025  0.000000       43.90000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000       76.03703            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000      113.33333            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000       43.90000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000       76.03703            
REMARK 350   BIOMT3   4  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     GLY A   164                                                      
REMARK 465     MET A   165                                                      
REMARK 465     GLY A   166                                                      
REMARK 465     GLY A   167                                                      
REMARK 465     ILE A   226                                                      
REMARK 465     PRO A   227                                                      
REMARK 465     GLN A   228                                                      
REMARK 465     GLY A   229                                                      
REMARK 465     GLY A   230                                                      
REMARK 465     GLU A   231                                                      
REMARK 465     THR A   232                                                      
REMARK 465     ARG A   233                                                      
REMARK 465     GLY A   234                                                      
REMARK 465     ASN A   235                                                      
REMARK 465     LEU A   236                                                      
REMARK 465     ALA A   237                                                      
REMARK 465     ALA A   238                                                      
REMARK 465     GLY A   239                                                      
REMARK 465     GLY A   240                                                      
REMARK 465     ARG A   241                                                      
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    HIS A  36   NE2   HIS A  36   CD2    -0.069                       
REMARK 500    HIS A  53   NE2   HIS A  53   CD2    -0.082                       
REMARK 500    HIS A 154   NE2   HIS A 154   CD2    -0.069                       
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   4   CA  -  CB  -  CG  ANGL. DEV. =  17.2 DEGREES          
REMARK 500    ARG A  30   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A  31   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    TYR A  44   CB  -  CG  -  CD2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG A  51   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A  55   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    TRP A  66   CD1 -  CG  -  CD2 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    TRP A  66   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 104   NE  -  CZ  -  NH1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG A 120   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    TRP A 130   CD1 -  CG  -  CD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    TRP A 130   CB  -  CG  -  CD1 ANGL. DEV. =  -8.9 DEGREES          
REMARK 500    TRP A 130   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    TRP A 130   CG  -  CD2 -  CE3 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG A 142   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    TRP A 151   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    TRP A 151   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ARG A 193   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 210   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG A 225   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 245   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 245   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    TRP A 252   CD1 -  CG  -  CD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    TRP A 252   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG A 278   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 291   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 312   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  65       91.98   -160.10                                   
REMARK 500    PHE A 131       49.71   -142.39                                   
REMARK 500    SER A 155      -29.90     64.08                                   
REMARK 500    SER A 169       63.15   -101.71                                   
REMARK 500    ALA A 203       -7.78    -57.51                                   
REMARK 500    THR A 285      -61.18    -94.78                                   
REMARK 500    THR A 288     -158.87   -124.21                                   
REMARK 500    CYS A 289       11.78     85.61                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1GSH A    1   316  UNP    P04425   GSHB_ECOLI       1    316             
SEQRES   1 A  316  MET ILE LYS LEU GLY ILE VAL MET ASP PRO ILE ALA ASN          
SEQRES   2 A  316  ILE ASN ILE LYS LYS ASP SER SER PHE ALA MET LEU LEU          
SEQRES   3 A  316  GLU ALA GLN ARG ARG GLY TYR GLU LEU HIS TYR MET GLU          
SEQRES   4 A  316  MET GLY ASP LEU TYR LEU ILE ASN GLY GLU ALA ARG ALA          
SEQRES   5 A  316  HIS THR ARG THR LEU ASN VAL LYS GLN ASN TYR GLU GLU          
SEQRES   6 A  316  TRP PHE SER PHE VAL GLY GLU GLN ASP LEU PRO LEU ALA          
SEQRES   7 A  316  ASP LEU ASP VAL ILE LEU MET ARG LYS ASP PRO PRO PHE          
SEQRES   8 A  316  ASP THR GLU PHE ILE TYR ALA THR TYR ILE LEU GLU ARG          
SEQRES   9 A  316  ALA GLU GLU LYS GLY THR LEU ILE VAL ASN LYS PRO GLN          
SEQRES  10 A  316  SER LEU ARG ASP CYS ASN GLU LYS LEU PHE THR ALA TRP          
SEQRES  11 A  316  PHE SER ASP LEU THR PRO GLU THR LEU VAL THR ARG ASN          
SEQRES  12 A  316  LYS ALA GLN LEU LYS ALA PHE TRP GLU LYS HIS SER ASP          
SEQRES  13 A  316  ILE ILE LEU LYS PRO LEU ASP GLY MET GLY GLY ALA SER          
SEQRES  14 A  316  ILE PHE ARG VAL LYS GLU GLY ASP PRO ASN LEU GLY VAL          
SEQRES  15 A  316  ILE ALA GLU THR LEU THR GLU HIS GLY THR ARG TYR CYS          
SEQRES  16 A  316  MET ALA GLN ASN TYR LEU PRO ALA ILE LYS ASP GLY ASP          
SEQRES  17 A  316  LYS ARG VAL LEU VAL VAL ASP GLY GLU PRO VAL PRO TYR          
SEQRES  18 A  316  CYS LEU ALA ARG ILE PRO GLN GLY GLY GLU THR ARG GLY          
SEQRES  19 A  316  ASN LEU ALA ALA GLY GLY ARG GLY GLU PRO ARG PRO LEU          
SEQRES  20 A  316  THR GLU SER ASP TRP LYS ILE ALA ARG GLN ILE GLY PRO          
SEQRES  21 A  316  THR LEU LYS GLU LYS GLY LEU ILE PHE VAL GLY LEU ASP          
SEQRES  22 A  316  ILE ILE GLY ASP ARG LEU THR GLU ILE ASN VAL THR SER          
SEQRES  23 A  316  PRO THR CYS ILE ARG GLU ILE GLU ALA GLU PHE PRO VAL          
SEQRES  24 A  316  SER ILE THR GLY MET LEU MET ASP ALA ILE GLU ALA ARG          
SEQRES  25 A  316  LEU GLN GLN GLN                                              
FORMUL   2  HOH   *96(H2 O)                                                     
HELIX    1   1 ILE A   11  ASN A   13  5                                   3    
HELIX    2   2 SER A   20  ARG A   30  1                                  11    
HELIX    3   3 MET A   40  ASP A   42  5                                   3    
HELIX    4   4 LEU A   77  ASP A   79  5                                   3    
HELIX    5   5 THR A   93  LYS A  108  1                                  16    
HELIX    6   6 PRO A  116  ASP A  121  1                                   6    
HELIX    7   7 LEU A  126  LEU A  134  5                                   9    
HELIX    8   8 LYS A  144  HIS A  154  1                                  11    
HELIX    9   9 LEU A  180  LEU A  187  1                                   8    
HELIX   10  10 PRO A  202  ASP A  206  5                                   5    
HELIX   11  11 GLU A  249  GLU A  264  1                                  16    
HELIX   12  12 ILE A  290  GLU A  296  1                                   7    
HELIX   13  13 ILE A  301  GLN A  314  1                                  14    
SHEET    1   A 4 GLU A  34  MET A  38  0                                        
SHEET    2   A 4 LYS A   3  VAL A   7  1  N  LEU A   4   O  GLU A  34           
SHEET    3   A 4 VAL A  82  MET A  85  1  N  VAL A  82   O  GLY A   5           
SHEET    4   A 4 LEU A 111  VAL A 113  1  N  LEU A 111   O  ILE A  83           
SHEET    1   B 3 LEU A  43  ILE A  46  0                                        
SHEET    2   B 3 GLU A  49  VAL A  59 -1  N  ARG A  51   O  TYR A  44           
SHEET    3   B 3 PHE A  67  PRO A  76 -1  N  LEU A  75   O  ALA A  52           
SHEET    1   C 4 THR A 138  THR A 141  0                                        
SHEET    2   C 4 CYS A 195  ASN A 199 -1  N  ALA A 197   O  LEU A 139           
SHEET    3   C 4 ILE A 157  PRO A 161 -1  N  LYS A 160   O  MET A 196           
SHEET    4   C 4 PHE A 171  VAL A 173 -1  N  VAL A 173   O  ILE A 157           
SHEET    1   D 5 ARG A 278  ASN A 283  0                                        
SHEET    2   D 5 PHE A 269  ILE A 275 -1  N  ILE A 275   O  ARG A 278           
SHEET    3   D 5 ASP A 208  VAL A 214 -1  N  VAL A 213   O  VAL A 270           
SHEET    4   D 5 TYR A 221  ARG A 225 -1  N  ARG A 225   O  ASP A 208           
SHEET    5   D 5 GLU A 243  PRO A 246 -1  N  ARG A 245   O  CYS A 222           
CISPEP   1 PRO A   89    PRO A   90          0        11.79                     
CISPEP   2 VAL A  113    ASN A  114          0         0.67                     
CRYST1   87.800   87.800  170.000  90.00  90.00 120.00 P 62 2 2     12          
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      0.011390  0.006576  0.000000        0.00000                         
SCALE2      0.000000  0.013151  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005882        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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