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Database: PDB
Entry: 5UEH
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Original site: 5UEH 
HEADER    TRANSFERASE/OXIDOREDUCTASE              02-JAN-17   5UEH              
TITLE     STRUCTURE OF GSTO1 COVALENTLY CONJUGATED TO QUINOLINIC ACID           
TITLE    2 FLUOROSULFATE                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE OMEGA-1;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: GSTO-1,GLUTATHIONE S-TRANSFERASE OMEGA 1-1,GSTO 1-1,        
COMPND   5 GLUTATHIONE-DEPENDENT DEHYDROASCORBATE REDUCTASE,MONOMETHYLARSONIC   
COMPND   6 ACID REDUCTASE,MMA(V) REDUCTASE,S-(PHENACYL)GLUTATHIONE REDUCTASE,   
COMPND   7 SPG-R;                                                               
COMPND   8 EC: 2.5.1.18,1.8.5.1,1.20.4.2;                                       
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GSTO1, GSTTLP28;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ARYLFLUOROSULFATE, GST, COVALENT INHIBITOR, TRANSFERASE-              
KEYWDS   2 OXIDOREDUCTASE COMPLEX                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.E.MORTENSON,I.A.WILSON,J.W.KELLY                                    
REVDAT   2   24-JAN-18 5UEH    1       JRNL                                     
REVDAT   1   17-JAN-18 5UEH    0                                                
JRNL        AUTH   D.E.MORTENSON,G.J.BRIGHTY,L.PLATE,G.BARE,W.CHEN,S.LI,H.WANG, 
JRNL        AUTH 2 B.F.CRAVATT,S.FORLI,E.T.POWERS,K.B.SHARPLESS,I.A.WILSON,     
JRNL        AUTH 3 J.W.KELLY                                                    
JRNL        TITL   "INVERSE DRUG DISCOVERY" STRATEGY TO IDENTIFY PROTEINS THAT  
JRNL        TITL 2 ARE TARGETED BY LATENT ELECTROPHILES AS EXEMPLIFIED BY ARYL  
JRNL        TITL 3 FLUOROSULFATES.                                              
JRNL        REF    J. AM. CHEM. SOC.             V. 140   200 2018              
JRNL        REFN                   ESSN 1520-5126                               
JRNL        PMID   29265822                                                     
JRNL        DOI    10.1021/JACS.7B08366                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 17677                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 967                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1260                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 86                           
REMARK   3   BIN FREE R VALUE                    : 0.2980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1917                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 55                                      
REMARK   3   SOLVENT ATOMS            : 216                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.29000                                              
REMARK   3    B22 (A**2) : 0.29000                                              
REMARK   3    B33 (A**2) : -0.95000                                             
REMARK   3    B12 (A**2) : 0.15000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.173         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.165         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.114         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.214         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2038 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1922 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2762 ; 1.385 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4457 ; 0.930 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   242 ; 5.624 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    86 ;32.884 ;24.419       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   363 ;13.690 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;20.529 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   292 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2367 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   444 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   961 ; 1.779 ; 3.096       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   960 ; 1.780 ; 3.093       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1201 ; 2.800 ; 4.631       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1202 ; 2.799 ; 4.634       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1077 ; 2.636 ; 3.512       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1077 ; 2.634 ; 3.512       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1559 ; 4.188 ; 5.149       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  2523 ; 6.674 ;26.362       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  2523 ; 6.674 ;26.361       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5UEH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000225742.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAY-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC VARIMAX                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18695                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 8.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.91400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB 4IS0                                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5 MG/ML SOLUTION OF PROTEIN              
REMARK 280  CRYSTALLIZED FROM PRECIPITANT SOLUTION CONTAINING 2.4 M AMMONIUM    
REMARK 280  SULFATE AND 0.1 M MES SOLUTION PH 5. CRYSTALS CRYOPROTECTED BY      
REMARK 280  BRIEF IMMERSION IN SOLUTION CONTAINING 1.5 M AMMONIUM SULFATE,      
REMARK 280  25% (V/V) GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE      
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -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       46.72000            
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       93.44000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       93.44000            
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       46.72000            
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: 4220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -139.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000      -85.74150            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000       49.50288            
REMARK 350   BIOMT3   2  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     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  11    CE   NZ                                             
REMARK 470     GLU A 137    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 144    CD   OE1  OE2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    PRO A    15     OD1  ASN A   168     3454     2.15            
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    ASN A  58       70.71   -152.59                                   
REMARK 500    GLU A  85      115.40     79.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 85P A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 307                 
DBREF  5UEH A    1   241  UNP    P78417   GSTO1_HUMAN      1    241             
SEQADV 5UEH SER A    0  UNP  P78417              EXPRESSION TAG                 
SEQRES   1 A  242  SER MET SER GLY GLU SER ALA ARG SER LEU GLY LYS GLY          
SEQRES   2 A  242  SER ALA PRO PRO GLY PRO VAL PRO GLU GLY SER ILE ARG          
SEQRES   3 A  242  ILE TYR SER MET ARG PHE CYS PRO PHE ALA GLU ARG THR          
SEQRES   4 A  242  ARG LEU VAL LEU LYS ALA LYS GLY ILE ARG HIS GLU VAL          
SEQRES   5 A  242  ILE ASN ILE ASN LEU LYS ASN LYS PRO GLU TRP PHE PHE          
SEQRES   6 A  242  LYS LYS ASN PRO PHE GLY LEU VAL PRO VAL LEU GLU ASN          
SEQRES   7 A  242  SER GLN GLY GLN LEU ILE TYR GLU SER ALA ILE THR CYS          
SEQRES   8 A  242  GLU TYR LEU ASP GLU ALA TYR PRO GLY LYS LYS LEU LEU          
SEQRES   9 A  242  PRO ASP ASP PRO TYR GLU LYS ALA CYS GLN LYS MET ILE          
SEQRES  10 A  242  LEU GLU LEU PHE SER LYS VAL PRO SER LEU VAL GLY SER          
SEQRES  11 A  242  PHE ILE ARG SER GLN ASN LYS GLU ASP TYR ALA GLY LEU          
SEQRES  12 A  242  LYS GLU GLU PHE ARG LYS GLU PHE THR LYS LEU GLU GLU          
SEQRES  13 A  242  VAL LEU THR ASN LYS LYS THR THR PHE PHE GLY GLY ASN          
SEQRES  14 A  242  SER ILE SER MET ILE ASP TYR LEU ILE TRP PRO TRP PHE          
SEQRES  15 A  242  GLU ARG LEU GLU ALA MET LYS LEU ASN GLU CYS VAL ASP          
SEQRES  16 A  242  HIS THR PRO LYS LEU LYS LEU TRP MET ALA ALA MET LYS          
SEQRES  17 A  242  GLU ASP PRO THR VAL SER ALA LEU LEU THR SER GLU LYS          
SEQRES  18 A  242  ASP TRP GLN GLY PHE LEU GLU LEU TYR LEU GLN ASN SER          
SEQRES  19 A  242  PRO GLU ALA CYS ASP TYR GLY LEU                              
HET    85P  A 301      24                                                       
HET    SO4  A 302       5                                                       
HET    SO4  A 303       5                                                       
HET    SO4  A 304       5                                                       
HET    SO4  A 305       5                                                       
HET    SO4  A 306       5                                                       
HET    GOL  A 307       6                                                       
HETNAM     85P 2-(4-CHLOROPHENYL)-6-[(FLUOROSULFONYL)OXY]QUINOLINE-4-           
HETNAM   2 85P  CARBOXYLIC ACID                                                 
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  85P    C16 H9 CL F N O5 S                                           
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   8  GOL    C3 H8 O3                                                     
FORMUL   9  HOH   *216(H2 O)                                                    
HELIX    1 AA1 GLY A    3  ARG A    7  5                                   5    
HELIX    2 AA2 CYS A   32  LYS A   45  1                                  14    
HELIX    3 AA3 PRO A   60  LYS A   66  5                                   7    
HELIX    4 AA4 GLU A   85  TYR A   97  1                                  13    
HELIX    5 AA5 ASP A  106  PHE A  120  1                                  15    
HELIX    6 AA6 SER A  125  SER A  133  1                                   9    
HELIX    7 AA7 ASN A  135  LYS A  161  1                                  27    
HELIX    8 AA8 SER A  171  ARG A  183  1                                  13    
HELIX    9 AA9 ARG A  183  LYS A  188  1                                   6    
HELIX   10 AB1 LEU A  189  ASP A  194  5                                   6    
HELIX   11 AB2 THR A  196  GLU A  208  1                                  13    
HELIX   12 AB3 ASP A  209  LEU A  216  1                                   8    
HELIX   13 AB4 SER A  218  GLN A  231  1                                  14    
HELIX   14 AB5 GLU A  235  TYR A  239  5                                   5    
SHEET    1 AA1 4 HIS A  49  ASN A  53  0                                        
SHEET    2 AA1 4 ILE A  24  SER A  28  1  N  ILE A  26   O  ILE A  52           
SHEET    3 AA1 4 VAL A  74  ASN A  77 -1  O  GLU A  76   N  ARG A  25           
SHEET    4 AA1 4 LEU A  82  TYR A  84 -1  O  ILE A  83   N  LEU A  75           
LINK         OH  TYR A 229                 S21 85P A 301     1555   1555  1.66  
CISPEP   1 VAL A   72    PRO A   73          0         6.62                     
SITE     1 AC1 10 MET A  29  PHE A  31  LEU A  56  VAL A 127                    
SITE     2 AC1 10 ILE A 131  ARG A 183  ALA A 186  PHE A 225                    
SITE     3 AC1 10 TYR A 229  HOH A 563                                          
SITE     1 AC2  8 ARG A  39  HIS A  49  VAL A  51  LEU A 215                    
SITE     2 AC2  8 HOH A 421  HOH A 510  HOH A 515  HOH A 532                    
SITE     1 AC3  8 ARG A  30  LYS A 136  HOH A 421  HOH A 459                    
SITE     2 AC3  8 HOH A 473  HOH A 490  HOH A 498  HOH A 515                    
SITE     1 AC4  7 GLU A  21  GLY A  22  SER A  78  GLN A  79                    
SITE     2 AC4  7 HOH A 407  HOH A 409  HOH A 435                               
SITE     1 AC5  2 ARG A  48  LYS A 200                                          
SITE     1 AC6  2 SER A 129  ARG A 132                                          
SITE     1 AC7  5 TYR A  84  CYS A 112  HOH A 402  HOH A 416                    
SITE     2 AC7  5 HOH A 518                                                     
CRYST1   57.161   57.161  140.160  90.00  90.00 120.00 P 31 2 1      6          
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      0.017494  0.010100  0.000000        0.00000                         
SCALE2      0.000000  0.020201  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007135        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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