GenomeNet

Database: PDB
Entry: 4YQV
LinkDB: 4YQV
Original site: 4YQV 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       13-MAR-15   4YQV              
TITLE     GLUTATHIONE S-TRANSFERASE OMEGA 1 BOUND TO COVALENT INHIBITOR C4-10   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE OMEGA-1;                         
COMPND   3 CHAIN: A, B, C;                                                      
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;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2                                   
KEYWDS    COVALENT INHIBITOR, THIOLTRANSFERASE, CHLOROACETAMIDE, TRANSFERASE-   
KEYWDS   2 TRANSFERASE INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.STUCKEY                                                           
REVDAT   2   19-OCT-16 4YQV    1       JRNL                                     
REVDAT   1   12-OCT-16 4YQV    0                                                
JRNL        AUTH   K.RAMKUMAR,S.SAMANTA,A.KYANI,S.YANG,S.TAMURA,E.ZIEMKE,       
JRNL        AUTH 2 J.A.STUCKEY,S.LI,K.CHINNASWAMY,H.OTAKE,B.DEBNATH,            
JRNL        AUTH 3 V.YAROVENKO,J.S.SEBOLT-LEOPOLD,M.LJUNGMAN,N.NEAMATI          
JRNL        TITL   MECHANISTIC EVALUATION AND TRANSCRIPTIONAL SIGNATURE OF A    
JRNL        TITL 2 GLUTATHIONE S-TRANSFERASE OMEGA 1 INHIBITOR.                 
JRNL        REF    NAT COMMUN                    V.   7 13084 2016              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   27703239                                                     
JRNL        DOI    10.1038/NCOMMS13084                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.06 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.06                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 46430                          
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)  : 0.196                          
REMARK   3   R VALUE            (WORKING SET)  : 0.195                          
REMARK   3   FREE R VALUE                      : 0.220                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.050                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2345                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.06                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.11                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 62.11                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2238                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2160                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2131                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2130                   
REMARK   3   BIN FREE R VALUE                        : 0.2660                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.78                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 107                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5604                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 51                                      
REMARK   3   SOLVENT ATOMS            : 405                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.91                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.47                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.88920                                             
REMARK   3    B22 (A**2) : 2.33250                                              
REMARK   3    B33 (A**2) : -1.44330                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 7.64560                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.260               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.217               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.166               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.213               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.166               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5812   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 7875   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2650   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 137    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 873    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5812   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 733    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7058   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.92                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.83                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.75                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: {A|5 - 241}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):    5.6370  -11.2144   24.7660           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0717 T22:   -0.1026                                    
REMARK   3     T33:   -0.0894 T12:    0.0119                                    
REMARK   3     T13:   -0.0306 T23:    0.0117                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4884 L22:    1.5609                                    
REMARK   3     L33:    2.0926 L12:   -0.3698                                    
REMARK   3     L13:   -0.2769 L23:    0.2881                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0171 S12:    0.0589 S13:    0.0747                     
REMARK   3     S21:    0.0139 S22:    0.0213 S23:   -0.1471                     
REMARK   3     S31:    0.2174 S32:    0.2242 S33:   -0.0042                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: {B|5 - 241}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):   20.0852   22.5042   -3.7386           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0751 T22:   -0.0980                                    
REMARK   3     T33:   -0.1013 T12:   -0.0033                                    
REMARK   3     T13:    0.0104 T23:   -0.0641                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.0595 L22:    2.0531                                    
REMARK   3     L33:    1.3351 L12:   -0.2007                                    
REMARK   3     L13:    0.1779 L23:   -0.2228                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0737 S12:    0.1047 S13:   -0.2371                     
REMARK   3     S21:   -0.0410 S22:   -0.0290 S23:    0.1785                     
REMARK   3     S31:    0.1875 S32:   -0.1307 S33:    0.1028                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: {C|5 - 241}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):   47.4435   23.5553  -15.2433           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0953 T22:   -0.0486                                    
REMARK   3     T33:   -0.0574 T12:    0.0065                                    
REMARK   3     T13:    0.0094 T23:    0.0710                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9870 L22:    1.3725                                    
REMARK   3     L33:    2.0275 L12:   -0.4303                                    
REMARK   3     L13:    0.3116 L23:    0.1422                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0390 S12:    0.1465 S13:    0.0821                     
REMARK   3     S21:    0.0038 S22:   -0.0621 S23:   -0.1393                     
REMARK   3     S31:    0.1040 S32:    0.1696 S33:    0.1011                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4YQV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000207911.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9786                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46437                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.060                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1EEM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: COMPLEX WAS CONCENTRATED TO 26.2         
REMARK 280  MG/ML. CRYSTALS OF THE COMPLEX GREW FROM SITTING DROPS              
REMARK 280  CONTAINING EQUAL VOLUMES OF PROTEIN COMPLEX AND WELL SOLUTION       
REMARK 280  (22.5% PEG 3350, 90 MM MES PH 6.5 AND 10 MM BACL2)., VAPOR          
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       93.16000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.68650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       93.16000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       35.68650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 1830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 -1.000000  0.000000  0.000000      -16.20559            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       59.81147            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 1910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 646  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 659  LIES ON A SPECIAL POSITION.                          
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    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     ASN C    -1                                                      
REMARK 465     ALA C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     GLU C     4                                                      
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    CD   CE   NZ                                        
REMARK 470     LYS A  57    CG   CD   CE   NZ                                   
REMARK 470     LYS A  65    CG   CD   CE   NZ                                   
REMARK 470     LYS A 100    CG   CD   CE   NZ                                   
REMARK 470     GLN A 134    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 136    CG   CD   CE   NZ                                   
REMARK 470     GLU A 137    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 139    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 148    CG   CD   CE   NZ                                   
REMARK 470     HIS A 195    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 216    CG   CD1  CD2                                       
REMARK 470     GLU A 219    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 220    CG   CD   CE   NZ                                   
REMARK 470     LEU A 241    CG   CD1  CD2                                       
REMARK 470     LYS B  11    CD   CE   NZ                                        
REMARK 470     GLU B  61    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  65    CG   CD   CE   NZ                                   
REMARK 470     LYS B 100    CG   CD   CE   NZ                                   
REMARK 470     LYS B 122    CG   CD   CE   NZ                                   
REMARK 470     LYS B 136    CG   CD   CE   NZ                                   
REMARK 470     GLU B 219    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 220    CG   CD   CE   NZ                                   
REMARK 470     LEU B 241    CG   CD1  CD2                                       
REMARK 470     LYS C  11    CD   CE   NZ                                        
REMARK 470     LYS C  57    CG   CD   CE   NZ                                   
REMARK 470     LYS C  65    CG   CD   CE   NZ                                   
REMARK 470     LYS C 100    CG   CD   CE   NZ                                   
REMARK 470     LYS C 136    CG   CD   CE   NZ                                   
REMARK 470     GLU C 137    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 138    CG   OD1  OD2                                       
REMARK 470     LYS C 148    CG   CD   CE   NZ                                   
REMARK 470     GLU C 219    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 220    CG   CD   CE   NZ                                   
REMARK 470     LEU C 241    CG   CD1  CD2                                       
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  85      115.23     84.03                                   
REMARK 500    ASN B  58       57.15   -143.22                                   
REMARK 500    GLU B  85      118.80     82.84                                   
REMARK 500    GLN B 134      -69.28    -99.35                                   
REMARK 500    GLU C  85      113.77     79.75                                   
REMARK 500    GLN C 134      -98.62   -124.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 720        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH B 721        DISTANCE =  7.70 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     4GG A  500                                                       
REMARK 610     4GG B  500                                                       
REMARK 610     4GG C  500                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 4GG A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 4GG B 500 and CYS B    
REMARK 800  32                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 4GG C 500 and CYS C    
REMARK 800  32                                                                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4YQM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YQU   RELATED DB: PDB                                   
DBREF  4YQV A    1   241  UNP    P78417   GSTO1_HUMAN      1    241             
DBREF  4YQV B    1   241  UNP    P78417   GSTO1_HUMAN      1    241             
DBREF  4YQV C    1   241  UNP    P78417   GSTO1_HUMAN      1    241             
SEQADV 4YQV SER A   -2  UNP  P78417              EXPRESSION TAG                 
SEQADV 4YQV ASN A   -1  UNP  P78417              EXPRESSION TAG                 
SEQADV 4YQV ALA A    0  UNP  P78417              EXPRESSION TAG                 
SEQADV 4YQV SER B   -2  UNP  P78417              EXPRESSION TAG                 
SEQADV 4YQV ASN B   -1  UNP  P78417              EXPRESSION TAG                 
SEQADV 4YQV ALA B    0  UNP  P78417              EXPRESSION TAG                 
SEQADV 4YQV SER C   -2  UNP  P78417              EXPRESSION TAG                 
SEQADV 4YQV ASN C   -1  UNP  P78417              EXPRESSION TAG                 
SEQADV 4YQV ALA C    0  UNP  P78417              EXPRESSION TAG                 
SEQRES   1 A  244  SER ASN ALA MET SER GLY GLU SER ALA ARG SER LEU GLY          
SEQRES   2 A  244  LYS GLY SER ALA PRO PRO GLY PRO VAL PRO GLU GLY SER          
SEQRES   3 A  244  ILE ARG ILE TYR SER MET ARG PHE CYS PRO PHE ALA GLU          
SEQRES   4 A  244  ARG THR ARG LEU VAL LEU LYS ALA LYS GLY ILE ARG HIS          
SEQRES   5 A  244  GLU VAL ILE ASN ILE ASN LEU LYS ASN LYS PRO GLU TRP          
SEQRES   6 A  244  PHE PHE LYS LYS ASN PRO PHE GLY LEU VAL PRO VAL LEU          
SEQRES   7 A  244  GLU ASN SER GLN GLY GLN LEU ILE TYR GLU SER ALA ILE          
SEQRES   8 A  244  THR CYS GLU TYR LEU ASP GLU ALA TYR PRO GLY LYS LYS          
SEQRES   9 A  244  LEU LEU PRO ASP ASP PRO TYR GLU LYS ALA CYS GLN LYS          
SEQRES  10 A  244  MET ILE LEU GLU LEU PHE SER LYS VAL PRO SER LEU VAL          
SEQRES  11 A  244  GLY SER PHE ILE ARG SER GLN ASN LYS GLU ASP TYR ALA          
SEQRES  12 A  244  GLY LEU LYS GLU GLU PHE ARG LYS GLU PHE THR LYS LEU          
SEQRES  13 A  244  GLU GLU VAL LEU THR ASN LYS LYS THR THR PHE PHE GLY          
SEQRES  14 A  244  GLY ASN SER ILE SER MET ILE ASP TYR LEU ILE TRP PRO          
SEQRES  15 A  244  TRP PHE GLU ARG LEU GLU ALA MET LYS LEU ASN GLU CYS          
SEQRES  16 A  244  VAL ASP HIS THR PRO LYS LEU LYS LEU TRP MET ALA ALA          
SEQRES  17 A  244  MET LYS GLU ASP PRO THR VAL SER ALA LEU LEU THR SER          
SEQRES  18 A  244  GLU LYS ASP TRP GLN GLY PHE LEU GLU LEU TYR LEU GLN          
SEQRES  19 A  244  ASN SER PRO GLU ALA CYS ASP TYR GLY LEU                      
SEQRES   1 B  244  SER ASN ALA MET SER GLY GLU SER ALA ARG SER LEU GLY          
SEQRES   2 B  244  LYS GLY SER ALA PRO PRO GLY PRO VAL PRO GLU GLY SER          
SEQRES   3 B  244  ILE ARG ILE TYR SER MET ARG PHE CYS PRO PHE ALA GLU          
SEQRES   4 B  244  ARG THR ARG LEU VAL LEU LYS ALA LYS GLY ILE ARG HIS          
SEQRES   5 B  244  GLU VAL ILE ASN ILE ASN LEU LYS ASN LYS PRO GLU TRP          
SEQRES   6 B  244  PHE PHE LYS LYS ASN PRO PHE GLY LEU VAL PRO VAL LEU          
SEQRES   7 B  244  GLU ASN SER GLN GLY GLN LEU ILE TYR GLU SER ALA ILE          
SEQRES   8 B  244  THR CYS GLU TYR LEU ASP GLU ALA TYR PRO GLY LYS LYS          
SEQRES   9 B  244  LEU LEU PRO ASP ASP PRO TYR GLU LYS ALA CYS GLN LYS          
SEQRES  10 B  244  MET ILE LEU GLU LEU PHE SER LYS VAL PRO SER LEU VAL          
SEQRES  11 B  244  GLY SER PHE ILE ARG SER GLN ASN LYS GLU ASP TYR ALA          
SEQRES  12 B  244  GLY LEU LYS GLU GLU PHE ARG LYS GLU PHE THR LYS LEU          
SEQRES  13 B  244  GLU GLU VAL LEU THR ASN LYS LYS THR THR PHE PHE GLY          
SEQRES  14 B  244  GLY ASN SER ILE SER MET ILE ASP TYR LEU ILE TRP PRO          
SEQRES  15 B  244  TRP PHE GLU ARG LEU GLU ALA MET LYS LEU ASN GLU CYS          
SEQRES  16 B  244  VAL ASP HIS THR PRO LYS LEU LYS LEU TRP MET ALA ALA          
SEQRES  17 B  244  MET LYS GLU ASP PRO THR VAL SER ALA LEU LEU THR SER          
SEQRES  18 B  244  GLU LYS ASP TRP GLN GLY PHE LEU GLU LEU TYR LEU GLN          
SEQRES  19 B  244  ASN SER PRO GLU ALA CYS ASP TYR GLY LEU                      
SEQRES   1 C  244  SER ASN ALA MET SER GLY GLU SER ALA ARG SER LEU GLY          
SEQRES   2 C  244  LYS GLY SER ALA PRO PRO GLY PRO VAL PRO GLU GLY SER          
SEQRES   3 C  244  ILE ARG ILE TYR SER MET ARG PHE CYS PRO PHE ALA GLU          
SEQRES   4 C  244  ARG THR ARG LEU VAL LEU LYS ALA LYS GLY ILE ARG HIS          
SEQRES   5 C  244  GLU VAL ILE ASN ILE ASN LEU LYS ASN LYS PRO GLU TRP          
SEQRES   6 C  244  PHE PHE LYS LYS ASN PRO PHE GLY LEU VAL PRO VAL LEU          
SEQRES   7 C  244  GLU ASN SER GLN GLY GLN LEU ILE TYR GLU SER ALA ILE          
SEQRES   8 C  244  THR CYS GLU TYR LEU ASP GLU ALA TYR PRO GLY LYS LYS          
SEQRES   9 C  244  LEU LEU PRO ASP ASP PRO TYR GLU LYS ALA CYS GLN LYS          
SEQRES  10 C  244  MET ILE LEU GLU LEU PHE SER LYS VAL PRO SER LEU VAL          
SEQRES  11 C  244  GLY SER PHE ILE ARG SER GLN ASN LYS GLU ASP TYR ALA          
SEQRES  12 C  244  GLY LEU LYS GLU GLU PHE ARG LYS GLU PHE THR LYS LEU          
SEQRES  13 C  244  GLU GLU VAL LEU THR ASN LYS LYS THR THR PHE PHE GLY          
SEQRES  14 C  244  GLY ASN SER ILE SER MET ILE ASP TYR LEU ILE TRP PRO          
SEQRES  15 C  244  TRP PHE GLU ARG LEU GLU ALA MET LYS LEU ASN GLU CYS          
SEQRES  16 C  244  VAL ASP HIS THR PRO LYS LEU LYS LEU TRP MET ALA ALA          
SEQRES  17 C  244  MET LYS GLU ASP PRO THR VAL SER ALA LEU LEU THR SER          
SEQRES  18 C  244  GLU LYS ASP TRP GLN GLY PHE LEU GLU LEU TYR LEU GLN          
SEQRES  19 C  244  ASN SER PRO GLU ALA CYS ASP TYR GLY LEU                      
HET    4GG  A 500      17                                                       
HET    4GG  B 500      17                                                       
HET    4GG  C 500      17                                                       
HETNAM     4GG 2-(ETHYLSULFANYL)-N-METHYL-N-[(1-PHENYL-1H-PYRAZOL-4-            
HETNAM   2 4GG  YL)METHYL]ACETAMIDE                                             
FORMUL   4  4GG    3(C15 H19 N3 O S)                                            
FORMUL   7  HOH   *405(H2 O)                                                    
HELIX    1 AA1 CYS A   32  LYS A   45  1                                  14    
HELIX    2 AA2 TRP A   62  ASN A   67  1                                   6    
HELIX    3 AA3 GLU A   85  TYR A   97  1                                  13    
HELIX    4 AA4 ASP A  106  SER A  121  1                                  16    
HELIX    5 AA5 LYS A  122  ARG A  132  1                                  11    
HELIX    6 AA6 ASN A  135  LYS A  161  1                                  27    
HELIX    7 AA7 SER A  171  ARG A  183  1                                  13    
HELIX    8 AA8 LEU A  189  ASP A  194  5                                   6    
HELIX    9 AA9 THR A  196  ASP A  209  1                                  14    
HELIX   10 AB1 ASP A  209  LEU A  215  1                                   7    
HELIX   11 AB2 SER A  218  GLN A  231  1                                  14    
HELIX   12 AB3 GLU A  235  TYR A  239  5                                   5    
HELIX   13 AB4 CYS B   32  LYS B   45  1                                  14    
HELIX   14 AB5 PRO B   60  LYS B   66  5                                   7    
HELIX   15 AB6 GLU B   85  TYR B   97  1                                  13    
HELIX   16 AB7 ASP B  106  SER B  121  1                                  16    
HELIX   17 AB8 SER B  121  SER B  133  1                                  13    
HELIX   18 AB9 ASN B  135  LYS B  161  1                                  27    
HELIX   19 AC1 SER B  171  ARG B  183  1                                  13    
HELIX   20 AC2 LEU B  189  ASP B  194  5                                   6    
HELIX   21 AC3 THR B  196  GLU B  208  1                                  13    
HELIX   22 AC4 ASP B  209  LEU B  215  1                                   7    
HELIX   23 AC5 SER B  218  GLN B  231  1                                  14    
HELIX   24 AC6 GLU B  235  TYR B  239  5                                   5    
HELIX   25 AC7 CYS C   32  LYS C   45  1                                  14    
HELIX   26 AC8 PRO C   60  LYS C   66  5                                   7    
HELIX   27 AC9 GLU C   85  TYR C   97  1                                  13    
HELIX   28 AD1 ASP C  106  SER C  121  1                                  16    
HELIX   29 AD2 SER C  121  SER C  133  1                                  13    
HELIX   30 AD3 ASN C  135  LYS C  161  1                                  27    
HELIX   31 AD4 SER C  171  ARG C  183  1                                  13    
HELIX   32 AD5 LEU C  189  ASP C  194  5                                   6    
HELIX   33 AD6 THR C  196  ASP C  209  1                                  14    
HELIX   34 AD7 ASP C  209  LEU C  215  1                                   7    
HELIX   35 AD8 SER C  218  GLN C  231  1                                  14    
HELIX   36 AD9 GLU C  235  TYR C  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  VAL A  74   N  TYR A  27           
SHEET    4 AA1 4 LEU A  82  TYR A  84 -1  O  ILE A  83   N  LEU A  75           
SHEET    1 AA2 4 HIS B  49  ASN B  53  0                                        
SHEET    2 AA2 4 ILE B  24  SER B  28  1  N  SER B  28   O  ILE B  52           
SHEET    3 AA2 4 VAL B  74  ASN B  77 -1  O  GLU B  76   N  ARG B  25           
SHEET    4 AA2 4 LEU B  82  TYR B  84 -1  O  ILE B  83   N  LEU B  75           
SHEET    1 AA3 4 GLU C  50  ASN C  53  0                                        
SHEET    2 AA3 4 ILE C  24  SER C  28  1  N  ILE C  26   O  ILE C  52           
SHEET    3 AA3 4 VAL C  74  ASN C  77 -1  O  VAL C  74   N  TYR C  27           
SHEET    4 AA3 4 LEU C  82  TYR C  84 -1  O  ILE C  83   N  LEU C  75           
LINK         SG  CYS A  32                 C13 4GG A 500     1555   1555  1.84  
LINK         SG  CYS B  32                 C13 4GG B 500     1555   1555  1.87  
LINK         SG  CYS C  32                 C13 4GG C 500     1555   1555  1.87  
CISPEP   1 VAL A   72    PRO A   73          0        -0.52                     
CISPEP   2 VAL B   72    PRO B   73          0         3.03                     
CISPEP   3 VAL C   72    PRO C   73          0         3.54                     
SITE     1 AC1 10 MET A  29  PHE A  31  CYS A  32  PRO A  33                    
SITE     2 AC1 10 PHE A  34  LEU A  56  ILE A 131  ARG A 183                    
SITE     3 AC1 10 TRP A 222  PHE A 225                                          
SITE     1 AC2 13 MET B  29  ARG B  30  PHE B  31  PRO B  33                    
SITE     2 AC2 13 PHE B  34  ALA B  35  GLU B  36  ILE B 131                    
SITE     3 AC2 13 ARG B 183  TRP B 222  PHE B 225  LEU B 226                    
SITE     4 AC2 13 HOH B 609                                                     
SITE     1 AC3 13 MET C  29  ARG C  30  PHE C  31  PRO C  33                    
SITE     2 AC3 13 PHE C  34  ALA C  35  GLU C  36  LEU C  56                    
SITE     3 AC3 13 ILE C 131  ARG C 183  TRP C 222  PHE C 225                    
SITE     4 AC3 13 HOH C 628                                                     
CRYST1  186.320   71.373   61.968  90.00 105.16  90.00 C 1 2 1      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      0.005367  0.000000  0.001454        0.00000                         
SCALE2      0.000000  0.014011  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016719        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system