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Database: PDB
Entry: 4YQM
LinkDB: 4YQM
Original site: 4YQM 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       13-MAR-15   4YQM              
TITLE     GLUTATHIONE S-TRANSFERASE OMEGA 1 BOUND TO COVALENT INHIBITOR C1-27   
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 4YQM    1       JRNL                                     
REVDAT   1   12-OCT-16 4YQM    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.    2.38 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) : 2.38                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 30710                          
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)  : 0.207                          
REMARK   3   R VALUE            (WORKING SET)  : 0.205                          
REMARK   3   FREE R VALUE                      : 0.237                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.040                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1547                           
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               : 15                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.38                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.46                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 92.01                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2807                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2310                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2648                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2300                   
REMARK   3   BIN FREE R VALUE                        : 0.2480                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.66                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 159                      
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            : 5586                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 87                                      
REMARK   3   SOLVENT ATOMS            : 121                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 54.36                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.35                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.47520                                             
REMARK   3    B22 (A**2) : -0.34180                                             
REMARK   3    B33 (A**2) : 3.81700                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.83430                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.310               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.407               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.239               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.433               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.245               
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      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5866   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 7980   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2674   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 134    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 865    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5866   ; 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   : 734    ; 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   : 6738   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.95                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.68                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.85                     
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):    6.2681  -11.3570   25.0458           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1220 T22:   -0.1918                                    
REMARK   3     T33:   -0.1807 T12:    0.0613                                    
REMARK   3     T13:   -0.0045 T23:    0.0483                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.6605 L22:    4.1342                                    
REMARK   3     L33:    2.1389 L12:   -1.0119                                    
REMARK   3     L13:   -0.4270 L23:    1.4181                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.3940 S12:    0.2770 S13:    0.1438                     
REMARK   3     S21:   -0.3168 S22:   -0.2036 S23:   -0.4889                     
REMARK   3     S31:    0.1065 S32:    0.1253 S33:   -0.1904                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: {B|5 - 241}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):   19.1725   22.5620   -3.9050           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1240 T22:   -0.1650                                    
REMARK   3     T33:   -0.2136 T12:   -0.0686                                    
REMARK   3     T13:    0.0921 T23:   -0.0565                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.6280 L22:    2.9835                                    
REMARK   3     L33:    1.7381 L12:   -0.0663                                    
REMARK   3     L13:   -0.0185 L23:   -0.2465                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2849 S12:    0.1800 S13:   -0.3215                     
REMARK   3     S21:    0.0902 S22:    0.1010 S23:    0.2520                     
REMARK   3     S31:    0.2760 S32:   -0.2206 S33:    0.1839                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: {C|5 - 241}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):   46.2041   23.2008  -15.6867           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0942 T22:   -0.1242                                    
REMARK   3     T33:   -0.1104 T12:    0.0430                                    
REMARK   3     T13:    0.0369 T23:    0.0879                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8946 L22:    1.5478                                    
REMARK   3     L33:    3.3403 L12:   -0.3901                                    
REMARK   3     L13:    0.3815 L23:   -0.4825                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0086 S12:    0.1753 S13:    0.1578                     
REMARK   3     S21:   -0.0969 S22:   -0.1442 S23:   -0.3157                     
REMARK   3     S31:    0.4785 S32:    0.2689 S33:    0.1356                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4YQM 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_1000207907.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAR-13                          
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) : 1.0781                             
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   : 30716                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.380                              
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     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.38                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24500                            
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   (%): 47.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 3350 AND 100 MM MES PH 6.5       
REMARK 280  WITH A DROP CONFIGURATION OF 2 UL OF COMPLEX, 1.8 UL WELL AND       
REMARK 280  0.2 UL 40% TERT-BUTANOL., VAPOR DIFFUSION, SITTING DROP,            
REMARK 280  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       91.41900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.62350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       91.41900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       35.62350            
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: 2900 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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      -15.04713            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       59.99378            
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: 2810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 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     ARG A  48    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A  57    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     LYS A 161    CD   CE   NZ                                        
REMARK 470     ASN A 168    CG   OD1  ND2                                       
REMARK 470     LYS A 188    CG   CD   CE   NZ                                   
REMARK 470     ASP A 194    CG   OD1  OD2                                       
REMARK 470     HIS A 195    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 198    CG   CD   CE   NZ                                   
REMARK 470     LYS A 200    CG   CD   CE   NZ                                   
REMARK 470     LEU A 241    CG   CD1  CD2                                       
REMARK 470     LYS B  11    CD   CE   NZ                                        
REMARK 470     LYS B  57    CG   CD   CE   NZ                                   
REMARK 470     LYS B 100    CG   CD   CE   NZ                                   
REMARK 470     GLN B 134    CG   CD   OE1  NE2                                  
REMARK 470     ASN B 135    CG   OD1  ND2                                       
REMARK 470     LYS B 136    CG   CD   CE   NZ                                   
REMARK 470     LYS B 188    CG   CD   CE   NZ                                   
REMARK 470     GLU B 191    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 194    CG   OD1  OD2                                       
REMARK 470     LYS B 198    CD   CE   NZ                                        
REMARK 470     LYS B 220    CD   CE   NZ                                        
REMARK 470     GLU B 235    CG   CD   OE1  OE2                                  
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     GLU C  61    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  65    CG   CD   CE   NZ                                   
REMARK 470     LYS C 100    CG   CD   CE   NZ                                   
REMARK 470     LYS C 122    CD   CE   NZ                                        
REMARK 470     ARG C 132    CZ   NH1  NH2                                       
REMARK 470     LYS C 136    CG   CD   CE   NZ                                   
REMARK 470     GLU C 137    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 148    CG   CD   CE   NZ                                   
REMARK 470     GLU C 185    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 220    CG   CD   CE   NZ                                   
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ALA B   35   N                                                   
REMARK 480     ALA C   35   N                                                   
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    ARG A  30      -19.66    -49.18                                   
REMARK 500    ASN A  58       66.00   -152.76                                   
REMARK 500    GLU A  85      115.87     86.87                                   
REMARK 500    ASN B  58       50.68   -161.91                                   
REMARK 500    GLU B  85      119.26     86.02                                   
REMARK 500    ASN B 232       72.08     52.90                                   
REMARK 500    MET C  29      118.11   -162.72                                   
REMARK 500    GLU C  85      110.83     85.26                                   
REMARK 500    SER C 121      -32.01    -38.83                                   
REMARK 500    ARG C 132       67.70   -110.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     4G9 B   301                                                      
REMARK 615     4G9 C   301                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 4G9 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 4G9 B 301 and CYS B    
REMARK 800  32                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 4G9 C 301 and CYS C    
REMARK 800  32                                                                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4YQU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YQV   RELATED DB: PDB                                   
DBREF  4YQM A    1   241  UNP    P78417   GSTO1_HUMAN      1    241             
DBREF  4YQM B    1   241  UNP    P78417   GSTO1_HUMAN      1    241             
DBREF  4YQM C    1   241  UNP    P78417   GSTO1_HUMAN      1    241             
SEQADV 4YQM SER A   -2  UNP  P78417              EXPRESSION TAG                 
SEQADV 4YQM ASN A   -1  UNP  P78417              EXPRESSION TAG                 
SEQADV 4YQM ALA A    0  UNP  P78417              EXPRESSION TAG                 
SEQADV 4YQM SER B   -2  UNP  P78417              EXPRESSION TAG                 
SEQADV 4YQM ASN B   -1  UNP  P78417              EXPRESSION TAG                 
SEQADV 4YQM ALA B    0  UNP  P78417              EXPRESSION TAG                 
SEQADV 4YQM SER C   -2  UNP  P78417              EXPRESSION TAG                 
SEQADV 4YQM ASN C   -1  UNP  P78417              EXPRESSION TAG                 
SEQADV 4YQM 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    4G9  A 301      27                                                       
HET    MES  A 302      12                                                       
HET    4G9  B 301      27                                                       
HET    MES  B 302      12                                                       
HET    4G9  C 301      27                                                       
HET    MES  C 302      12                                                       
HETNAM     4G9 2-CHLORO-N-[4-CHLORO-3-(DIMETHYLSULFAMOYL)                       
HETNAM   2 4G9  PHENYL]ACETAMIDE                                                
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
FORMUL   4  4G9    3(C10 H12 CL2 N2 O3 S)                                       
FORMUL   5  MES    3(C6 H13 N O4 S)                                             
FORMUL  10  HOH   *121(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 GLU A  137  LYS A  161  1                                  25    
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  GLU A  208  1                                  13    
HELIX   10 AB1 ASP A  209  LEU A  216  1                                   8    
HELIX   11 AB2 SER A  218  LEU A  230  1                                  13    
HELIX   12 AB3 CYS B   32  LYS B   45  1                                  14    
HELIX   13 AB4 PRO B   60  LYS B   66  5                                   7    
HELIX   14 AB5 GLU B   85  TYR B   97  1                                  13    
HELIX   15 AB6 ASP B  106  SER B  121  1                                  16    
HELIX   16 AB7 LYS B  122  ARG B  132  1                                  11    
HELIX   17 AB8 ASN B  135  LYS B  161  1                                  27    
HELIX   18 AB9 SER B  171  ARG B  183  1                                  13    
HELIX   19 AC1 LEU B  189  ASP B  194  5                                   6    
HELIX   20 AC2 THR B  196  ASP B  209  1                                  14    
HELIX   21 AC3 ASP B  209  LEU B  215  1                                   7    
HELIX   22 AC4 SER B  218  GLN B  231  1                                  14    
HELIX   23 AC5 CYS C   32  LYS C   45  1                                  14    
HELIX   24 AC6 PRO C   60  LYS C   66  5                                   7    
HELIX   25 AC7 GLU C   85  TYR C   97  1                                  13    
HELIX   26 AC8 ASP C  106  SER C  121  1                                  16    
HELIX   27 AC9 LYS C  122  ARG C  132  1                                  11    
HELIX   28 AD1 ASN C  135  LYS C  161  1                                  27    
HELIX   29 AD2 SER C  171  ARG C  183  1                                  13    
HELIX   30 AD3 LEU C  189  ASP C  194  5                                   6    
HELIX   31 AD4 THR C  196  ASP C  209  1                                  14    
HELIX   32 AD5 ASP C  209  LEU C  215  1                                   7    
HELIX   33 AD6 SER C  218  GLN C  231  1                                  14    
HELIX   34 AD7 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  SER A  28   O  ILE A  52           
SHEET    3 AA1 4 VAL A  74  GLU A  76 -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           
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  GLU B  76 -1  O  VAL B  74   N  TYR B  27           
SHEET    4 AA2 4 LEU B  82  TYR B  84 -1  O  ILE B  83   N  LEU B  75           
SHEET    1 AA3 4 HIS C  49  ASN C  53  0                                        
SHEET    2 AA3 4 ILE C  24  SER C  28  1  N  SER C  28   O  ILE C  52           
SHEET    3 AA3 4 VAL C  74  ASN C  77 -1  O  GLU C  76   N  ARG C  25           
SHEET    4 AA3 4 LEU C  82  TYR C  84 -1  O  ILE C  83   N  LEU C  75           
LINK         SG  CYS A  32                 C7  4G9 A 301     1555   1555  1.81  
LINK         SG  CYS B  32                 C7  4G9 B 301     1555   1555  1.82  
LINK         SG  CYS C  32                 C7  4G9 C 301     1555   1555  1.83  
CISPEP   1 VAL A   72    PRO A   73          0         1.49                     
CISPEP   2 VAL B   72    PRO B   73          0         2.45                     
CISPEP   3 VAL C   72    PRO C   73          0         0.38                     
SITE     1 AC1  7 CYS A  32  PRO A  33  PHE A  34  VAL A 127                    
SITE     2 AC1  7 GLY A 128  ARG A 132  TRP A 180                               
SITE     1 AC2  6 PHE A  34  PHE A  69  PRO A  73  GLU A  85                    
SITE     2 AC2  6 SER A  86  GLU A 118                                          
SITE     1 AC3  6 PHE B  34  PHE B  69  GLU B  85  SER B  86                    
SITE     2 AC3  6 HOH B 431  GLU C 118                                          
SITE     1 AC4  6 GLU B 118  PHE C  34  PHE C  69  PRO C  73                    
SITE     2 AC4  6 GLU C  85  SER C  86                                          
SITE     1 AC5 11 MET B  29  ARG B  30  PHE B  31  PRO B  33                    
SITE     2 AC5 11 PHE B  34  GLU B  36  PRO B 124  VAL B 127                    
SITE     3 AC5 11 TRP B 180  TYR B 229  HOH B 405                               
SITE     1 AC6 11 MET C  29  ARG C  30  PHE C  31  PRO C  33                    
SITE     2 AC6 11 PHE C  34  GLU C  36  PRO C 124  VAL C 127                    
SITE     3 AC6 11 ILE C 131  TRP C 180  HOH C 408                               
CRYST1  182.838   71.247   61.852  90.00 104.08  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      0.005469  0.000000  0.001372        0.00000                         
SCALE2      0.000000  0.014036  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016668        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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