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Database: PDB
Entry: 1GLV
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Original site: 1GLV 
HEADER    GLUTATHIONE BIOSYNTHESIS LIGASE         12-MAR-93   1GLV              
TITLE     THREE-DIMENSIONAL STRUCTURE OF THE GLUTATHIONE SYNTHETASE FROM        
TITLE    2 ESCHERICHIA COLI B AT 2.0 ANGSTROMS RESOLUTION                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE SYNTHASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 6.3.2.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562                                                  
KEYWDS    GLUTATHIONE BIOSYNTHESIS LIGASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.YAMAGUCHI,H.KATO,T.TANAKA,Y.KATSUBE                                 
REVDAT   4   29-NOV-17 1GLV    1       HELIX                                    
REVDAT   3   24-FEB-09 1GLV    1       VERSN                                    
REVDAT   2   01-APR-03 1GLV    1       JRNL                                     
REVDAT   1   31-JAN-94 1GLV    0                                                
JRNL        AUTH   H.YAMAGUCHI,H.KATO,Y.HATA,T.NISHIOKA,A.KIMURA,J.ODA,         
JRNL        AUTH 2 Y.KATSUBE                                                    
JRNL        TITL   THREE-DIMENSIONAL STRUCTURE OF THE GLUTATHIONE SYNTHETASE    
JRNL        TITL 2 FROM ESCHERICHIA COLI B AT 2.0 A RESOLUTION.                 
JRNL        REF    J.MOL.BIOL.                   V. 229  1083 1993              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   8445637                                                      
JRNL        DOI    10.1006/JMBI.1993.1106                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
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   1 REFERENCE 2                                                          
REMARK   1  AUTH   H.KATO,M.KOBAYASHI,K.MURATA,T.NISHIOKA,J.ODA                 
REMARK   1  TITL   OVEREXPRESSION OF GLUTATHIONE SYNTHETASE IN ESCHERICHIA COLI 
REMARK   1  REF    AGRIC.BIOL.CHEM.              V.  53  3071 1989              
REMARK   1  REFN                   ISSN 0002-1369                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   H.KATO,T.TANAKA,T.NISHIOKA,A.KIMURA,J.ODA                    
REMARK   1  TITL   ROLE OF CYSTEINE RESIDUES IN GLUTATHIONE SYNTHETASE FROM     
REMARK   1  TITL 2 ESCHERICHIA COLI B: CHEMICAL MODIFICATION AND                
REMARK   1  TITL 3 OLIGONUCLEOTIDE SITE-DIRECTED MUTAGENESIS                    
REMARK   1  REF    J.BIOL.CHEM.                  V. 263 11646 1988              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 9009                           
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 + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
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                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2381                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 18                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.018 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1GLV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000173613.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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      113.23333            
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       56.61667            
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      113.23333            
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       56.61667            
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      113.23333            
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       56.61667            
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      113.23333            
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       56.61667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE ASYMMETRIC UNIT OF THE CRYSTAL CONTAINS ONE SUBUNIT OF   
REMARK 300 THE TETRAMERIC MOLECULE.  SUBUNITS IN THE TETRAMERIC                 
REMARK 300 MOLECULE CAN BE GENERATED BY APPLYING FOLLOWING OPERATIONS           
REMARK 300 TO THE FRACTIONAL CRYSTALLOGRAPHIC COORDINATES XFRAC,                
REMARK 300 YFRAC, ZFRAC.                                                        
REMARK 300                                                                      
REMARK 300    0    1    0      XFRAC          0           XFRAC2                
REMARK 300    1    0    0   X  YFRAC  +       0      =    YFRAC2                
REMARK 300    0    0   -1      ZFRAC      0.6666666       ZFRAC2                
REMARK 300                                                                      
REMARK 300   -1    0    0      XFRAC          1           XFRAC3                
REMARK 300    0   -1    0   X  YFRAC  +       1      =    XFRAC3                
REMARK 300    0    0    1      ZFRAC          0           XFRAC3                
REMARK 300                                                                      
REMARK 300    0   -1    0      XFRAC          1           XFRAC4                
REMARK 300   -1    0    0   X  YFRAC  +       1      =    YFRAC4                
REMARK 300    0    0   -1      ZFRAC      0.6666666       ZFRAC4                
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: MONOMERIC                         
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THE LOOP REGION FROM ILE 226 TO ARG 241 IN THE WILD TYPE             
REMARK 400 ENZYME WERE REPLACED WITH THREE GLY RESIDUES, GLY 226, GLY           
REMARK 400 227 AND GLY 228.  GLY 228 CONNECTS WITH GLY 242.                     
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 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    GLY A    48     NH1  ARG A   104              1.87            
REMARK 500   OG   SER A   118     O    LYS A   265              2.06            
REMARK 500   NH1  ARG A    51     OD1  ASP A    74              2.08            
REMARK 500   OH   TYR A    44     NH1  ARG A    51              2.13            
REMARK 500   OD2  ASP A   156     NH2  ARG A   172              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  19   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    MET A  24   CA  -  CB  -  CG  ANGL. DEV. = -12.5 DEGREES          
REMARK 500    GLU A  27   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    GLU A  27   CG  -  CD  -  OE1 ANGL. DEV. =  14.5 DEGREES          
REMARK 500    ARG A  30   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG A  31   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    TYR A  44   CB  -  CG  -  CD1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG A  51   CD  -  NE  -  CZ  ANGL. DEV. = -14.1 DEGREES          
REMARK 500    ARG A  51   NE  -  CZ  -  NH1 ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    ARG A  51   NE  -  CZ  -  NH2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    LYS A  60   CA  -  CB  -  CG  ANGL. DEV. =  13.4 DEGREES          
REMARK 500    LYS A  60   O   -  C   -  N   ANGL. DEV. =  11.6 DEGREES          
REMARK 500    ASP A  81   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A  88   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    TYR A 100   CB  -  CG  -  CD2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    TYR A 100   CB  -  CG  -  CD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG A 104   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    ARG A 104   NE  -  CZ  -  NH2 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    VAL A 113   CB  -  CA  -  C   ANGL. DEV. =  12.8 DEGREES          
REMARK 500    ASN A 114   C   -  N   -  CA  ANGL. DEV. =  58.2 DEGREES          
REMARK 500    ARG A 120   NE  -  CZ  -  NH1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP A 121   CB  -  CG  -  OD1 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ASP A 121   CB  -  CG  -  OD2 ANGL. DEV. =  -8.9 DEGREES          
REMARK 500    GLU A 124   CA  -  CB  -  CG  ANGL. DEV. =  24.9 DEGREES          
REMARK 500    LYS A 125   CB  -  CA  -  C   ANGL. DEV. = -12.8 DEGREES          
REMARK 500    GLU A 152   OE1 -  CD  -  OE2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    HIS A 190   CA  -  CB  -  CG  ANGL. DEV. = -11.3 DEGREES          
REMARK 500    ARG A 210   NE  -  CZ  -  NH2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A 215   CB  -  CG  -  OD1 ANGL. DEV. =  10.7 DEGREES          
REMARK 500    ARG A 225   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ASP A 251   CB  -  CG  -  OD1 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ASP A 251   CB  -  CG  -  OD2 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    ARG A 278   NE  -  CZ  -  NH1 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ARG A 278   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    GLU A 281   CA  -  CB  -  CG  ANGL. DEV. =  18.6 DEGREES          
REMARK 500    GLU A 281   CG  -  CD  -  OE2 ANGL. DEV. =  13.1 DEGREES          
REMARK 500    ARG A 291   NE  -  CZ  -  NH1 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    ASP A 307   CB  -  CG  -  OD2 ANGL. DEV. =  -7.3 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    PRO A  10      107.33    -26.56                                   
REMARK 500    ILE A  16       -9.60    -54.32                                   
REMARK 500    ASN A  62      102.65   -164.03                                   
REMARK 500    GLU A  65       93.61   -161.47                                   
REMARK 500    CYS A 122       79.66   -103.19                                   
REMARK 500    THR A 128       -5.94    -58.62                                   
REMARK 500    SER A 155      -48.81     62.96                                   
REMARK 500    SER A 169       40.50   -155.66                                   
REMARK 500    ARG A 245      161.19    175.64                                   
REMARK 500    THR A 285      -82.05    -77.70                                   
REMARK 500    THR A 288     -157.81   -129.17                                   
REMARK 500    CYS A 289       10.68     84.61                                   
REMARK 500    GLN A 315      -85.37    -66.30                                   
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    ARG A  30         0.16    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED.  IN              
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED *S1* AND *S2*.  STRANDS 1 AND 2 ARE           
REMARK 700 IDENTICAL.                                                           
DBREF  1GLV A    1   316  UNP    P04425   GSHB_ECOLI       1    316             
SEQADV 1GLV     A       UNP  P04425    ILE   226 DELETION                       
SEQADV 1GLV     A       UNP  P04425    PRO   227 DELETION                       
SEQADV 1GLV     A       UNP  P04425    GLN   228 DELETION                       
SEQADV 1GLV     A       UNP  P04425    GLY   229 DELETION                       
SEQADV 1GLV     A       UNP  P04425    GLY   230 DELETION                       
SEQADV 1GLV     A       UNP  P04425    GLU   231 DELETION                       
SEQADV 1GLV     A       UNP  P04425    THR   232 DELETION                       
SEQADV 1GLV     A       UNP  P04425    ARG   233 DELETION                       
SEQADV 1GLV     A       UNP  P04425    GLY   234 DELETION                       
SEQADV 1GLV     A       UNP  P04425    ASN   235 DELETION                       
SEQADV 1GLV     A       UNP  P04425    LEU   236 DELETION                       
SEQADV 1GLV     A       UNP  P04425    ALA   237 DELETION                       
SEQADV 1GLV     A       UNP  P04425    ALA   238 DELETION                       
SEQADV 1GLV GLY A  228  UNP  P04425    ARG   241 CONFLICT                       
SEQRES   1 A  303  MET ILE LYS LEU GLY ILE VAL MET ASP PRO ILE ALA ASN          
SEQRES   2 A  303  ILE ASN ILE LYS LYS ASP SER SER PHE ALA MET LEU LEU          
SEQRES   3 A  303  GLU ALA GLN ARG ARG GLY TYR GLU LEU HIS TYR MET GLU          
SEQRES   4 A  303  MET GLY ASP LEU TYR LEU ILE ASN GLY GLU ALA ARG ALA          
SEQRES   5 A  303  HIS THR ARG THR LEU ASN VAL LYS GLN ASN TYR GLU GLU          
SEQRES   6 A  303  TRP PHE SER PHE VAL GLY GLU GLN ASP LEU PRO LEU ALA          
SEQRES   7 A  303  ASP LEU ASP VAL ILE LEU MET ARG LYS ASP PRO PRO PHE          
SEQRES   8 A  303  ASP THR GLU PHE ILE TYR ALA THR TYR ILE LEU GLU ARG          
SEQRES   9 A  303  ALA GLU GLU LYS GLY THR LEU ILE VAL ASN LYS PRO GLN          
SEQRES  10 A  303  SER LEU ARG ASP CYS ASN GLU LYS LEU PHE THR ALA TRP          
SEQRES  11 A  303  PHE SER ASP LEU THR PRO GLU THR LEU VAL THR ARG ASN          
SEQRES  12 A  303  LYS ALA GLN LEU LYS ALA PHE TRP GLU LYS HIS SER ASP          
SEQRES  13 A  303  ILE ILE LEU LYS PRO LEU ASP GLY MET GLY GLY ALA SER          
SEQRES  14 A  303  ILE PHE ARG VAL LYS GLU GLY ASP PRO ASN LEU GLY VAL          
SEQRES  15 A  303  ILE ALA GLU THR LEU THR GLU HIS GLY THR ARG TYR CYS          
SEQRES  16 A  303  MET ALA GLN ASN TYR LEU PRO ALA ILE LYS ASP GLY ASP          
SEQRES  17 A  303  LYS ARG VAL LEU VAL VAL ASP GLY GLU PRO VAL PRO TYR          
SEQRES  18 A  303  CYS LEU ALA ARG GLY GLY GLY GLY GLU PRO ARG PRO LEU          
SEQRES  19 A  303  THR GLU SER ASP TRP LYS ILE ALA ARG GLN ILE GLY PRO          
SEQRES  20 A  303  THR LEU LYS GLU LYS GLY LEU ILE PHE VAL GLY LEU ASP          
SEQRES  21 A  303  ILE ILE GLY ASP ARG LEU THR GLU ILE ASN VAL THR SER          
SEQRES  22 A  303  PRO THR CYS ILE ARG GLU ILE GLU ALA GLU PHE PRO VAL          
SEQRES  23 A  303  SER ILE THR GLY MET LEU MET ASP ALA ILE GLU ALA ARG          
SEQRES  24 A  303  LEU GLN GLN GLN                                              
FORMUL   2  HOH   *18(H2 O)                                                     
HELIX    1  H1 SER A   20  ARG A   30  1                                  11    
HELIX    2  H2 THR A   93  GLU A  107  1                                  15    
HELIX    3  H3 PRO A  116  ASP A  121  1                                   6    
HELIX    4  H4 PHE A  127  TRP A  130  5                                   4    
HELIX    5  H5 LYS A  144  HIS A  154  1                                  11    
HELIX    6  H6 LEU A  180  LEU A  187  1                                   8    
HELIX    7  H7 PRO A  202  ASP A  206  5                                   5    
HELIX    8  H8 GLU A  249  GLU A  264  1KINKED AT PRO 260                 16    
HELIX    9  H9 ILE A  290  GLU A  296  1                                   7    
HELIX   10 H10 ILE A  301  GLN A  314  1                                  14    
SHEET    1  S1 6 PHE A  67  PRO A  76  0                                        
SHEET    2  S1 6 GLU A  49  VAL A  59 -1                                        
SHEET    3  S1 6 GLU A  34  MET A  38 -1                                        
SHEET    4  S1 6 LYS A   3  MET A   8  1                                        
SHEET    5  S1 6 VAL A  82  ARG A  86  1                                        
SHEET    6  S1 6 LEU A 111  VAL A 113  1                                        
SHEET    1  S2 3 PHE A  67  PRO A  76  0                                        
SHEET    2  S2 3 GLU A  49  VAL A  59 -1                                        
SHEET    3  S2 3 LEU A  43  ILE A  46 -1                                        
SHEET    1  S3 4 THR A 138  THR A 141  0                                        
SHEET    2  S3 4 CYS A 195  ASN A 199 -1                                        
SHEET    3  S3 4 ILE A 157  PRO A 161 -1                                        
SHEET    4  S3 4 PHE A 171  VAL A 173 -1                                        
SHEET    1  S4 5 GLU A 243  PRO A 246  0                                        
SHEET    2  S4 5 TYR A 221  ARG A 225 -1                                        
SHEET    3  S4 5 ASP A 208  VAL A 214 -1                                        
SHEET    4  S4 5 PHE A 269  ILE A 275 -1                                        
SHEET    5  S4 5 ARG A 278  ASN A 283 -1                                        
CISPEP   1 PRO A   89    PRO A   90          0         1.76                     
CISPEP   2 VAL A  113    ASN A  114          0         0.89                     
CRYST1   87.700   87.700  169.850  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      0.011403  0.006583  0.000000        0.00000                         
SCALE2      0.000000  0.013166  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005888        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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