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Database: PDB
Entry: 4GCI
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Original site: 4GCI 
HEADER    TRANSFERASE                             30-JUL-12   4GCI              
TITLE     CRYSTAL STRUCTURE OF GLUTAHTIONE S-TRANSFERASE HOMOLOG FROM YERSINIA  
TITLE    2 PESTIS, TARGET EFI-501894, WITH BOUND GLUTATHIONE, MONOCLINIC FORM   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GLUTATHIONINE S-TRANSFERASE;                                
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: YERSINIA PESTIS;                                
SOURCE   3 ORGANISM_TAXID: 632;                                                 
SOURCE   4 GENE: GST, GST2, Y1968, YP_2153;                                     
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    GST, GLUTATHIONE S-TRANSFERASE, ENZYME FUNCTION INITIATIVE, EFI,      
KEYWDS   2 STRUCTURAL GENOMICS, TRANSFERASE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.W.VETTING,R.TORO,R.BHOSLE,N.F.AL OBAIDI,L.L.MORISCO,S.R.WASSERMAN,  
AUTHOR   2 S.SOJITRA,E.WASHINGTON,A.SCOTT GLENN,S.CHOWDHURY,B.EVANS,J.HAMMONDS, 
AUTHOR   3 B.HILLERICH,J.LOVE,R.D.SEIDEL,H.J.IMKER,R.N.ARMSTRONG,J.A.GERLT,     
AUTHOR   4 S.C.ALMO,ENZYME FUNCTION INITIATIVE (EFI)                            
REVDAT   1   29-AUG-12 4GCI    0                                                
JRNL        AUTH   M.W.VETTING,R.TORO,R.BHOSLE,N.F.AL OBAIDI,L.L.MORISCO,       
JRNL        AUTH 2 S.R.WASSERMAN,S.SOJITRA,E.WASHINGTON,A.SCOTT GLENN,          
JRNL        AUTH 3 S.CHOWDHURY,B.EVANS,J.HAMMONDS,B.HILLERICH,J.LOVE,           
JRNL        AUTH 4 R.D.SEIDEL,H.J.IMKER,R.N.ARMSTRONG,J.A.GERLT,S.C.ALMO,       
JRNL        AUTH 5 ENZYME FUNCTION INITIATIVE (EFI)                             
JRNL        TITL   CRYSTAL STRUCTURE OF GLUTAHTIONE S-TRANSFERASE HOMOLOG FROM  
JRNL        TITL 2 YERSINIA PESTIS, TARGET EFI-501894, WITH BOUND GLUTATHIONE,  
JRNL        TITL 3 MONOCLINIC FORM                                              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.87                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 72757                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3669                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 22.8755 -  4.4334    0.97     2628   152  0.1678 0.1825        
REMARK   3     2  4.4334 -  3.5230    1.00     2704   139  0.1489 0.1742        
REMARK   3     3  3.5230 -  3.0789    1.00     2667   140  0.1599 0.2185        
REMARK   3     4  3.0789 -  2.7979    1.00     2674   150  0.1733 0.2111        
REMARK   3     5  2.7979 -  2.5977    1.00     2639   150  0.1787 0.2039        
REMARK   3     6  2.5977 -  2.4447    1.00     2679   145  0.1754 0.2095        
REMARK   3     7  2.4447 -  2.3224    1.00     2637   141  0.1707 0.1979        
REMARK   3     8  2.3224 -  2.2214    1.00     2658   149  0.1763 0.2237        
REMARK   3     9  2.2214 -  2.1360    1.00     2652   154  0.1698 0.2164        
REMARK   3    10  2.1360 -  2.0623    1.00     2660   147  0.1710 0.1852        
REMARK   3    11  2.0623 -  1.9979    1.00     2669   134  0.1800 0.2051        
REMARK   3    12  1.9979 -  1.9408    1.00     2651   140  0.1759 0.1919        
REMARK   3    13  1.9408 -  1.8897    1.00     2667   133  0.1716 0.2308        
REMARK   3    14  1.8897 -  1.8436    1.00     2676   132  0.1736 0.1955        
REMARK   3    15  1.8436 -  1.8017    1.00     2602   141  0.1770 0.2098        
REMARK   3    16  1.8017 -  1.7634    1.00     2683   153  0.1870 0.2304        
REMARK   3    17  1.7634 -  1.7281    1.00     2650   141  0.1933 0.2490        
REMARK   3    18  1.7281 -  1.6955    1.00     2634   136  0.2012 0.2282        
REMARK   3    19  1.6955 -  1.6653    1.00     2695   143  0.1965 0.2364        
REMARK   3    20  1.6653 -  1.6370    1.00     2622   136  0.1962 0.2155        
REMARK   3    21  1.6370 -  1.6106    1.00     2645   144  0.2032 0.2455        
REMARK   3    22  1.6106 -  1.5859    1.00     2675   131  0.2068 0.2148        
REMARK   3    23  1.5859 -  1.5626    1.00     2656   137  0.2220 0.2890        
REMARK   3    24  1.5626 -  1.5406    1.00     2644   135  0.2390 0.2512        
REMARK   3    25  1.5406 -  1.5197    1.00     2618   127  0.2563 0.2623        
REMARK   3    26  1.5197 -  1.5000    1.00     2703   139  0.2721 0.3087        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.120            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.800           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           3359                                  
REMARK   3   ANGLE     :  1.038           4566                                  
REMARK   3   CHIRALITY :  0.064            513                                  
REMARK   3   PLANARITY :  0.005            588                                  
REMARK   3   DIHEDRAL  : 13.813           1268                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 0 through 105 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3789  96.4799  74.2720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2456 T22:   0.2268                                     
REMARK   3      T33:   0.1723 T12:   0.0022                                     
REMARK   3      T13:  -0.0379 T23:  -0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1849 L22:   1.4593                                     
REMARK   3      L33:   1.7261 L12:  -0.2167                                     
REMARK   3      L13:  -0.7764 L23:  -0.0565                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0103 S12:  -0.1920 S13:   0.0528                       
REMARK   3      S21:   0.3008 S22:   0.0554 S23:  -0.0815                       
REMARK   3      S31:  -0.1242 S32:   0.0409 S33:  -0.0479                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 106 through 141 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -18.0576  84.4018  59.3598              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2132 T22:   0.2883                                     
REMARK   3      T33:   0.3019 T12:  -0.0035                                     
REMARK   3      T13:  -0.0204 T23:  -0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7999 L22:   1.1439                                     
REMARK   3      L33:   0.9015 L12:  -0.7025                                     
REMARK   3      L13:   0.0393 L23:   0.3185                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1072 S12:   0.0949 S13:  -0.2030                       
REMARK   3      S21:  -0.1493 S22:  -0.1236 S23:   0.3642                       
REMARK   3      S31:  -0.0060 S32:  -0.2931 S33:   0.0201                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 142 through 168 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.4989  82.0903  67.6262              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2186 T22:   0.2095                                     
REMARK   3      T33:   0.2097 T12:   0.0126                                     
REMARK   3      T13:  -0.0205 T23:   0.0136                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9664 L22:   1.5054                                     
REMARK   3      L33:   1.1167 L12:  -0.2790                                     
REMARK   3      L13:  -0.0249 L23:   0.4077                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0006 S12:  -0.0820 S13:  -0.1007                       
REMARK   3      S21:   0.1231 S22:   0.0396 S23:  -0.0848                       
REMARK   3      S31:   0.0814 S32:   0.0609 S33:  -0.0482                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 169 through 188 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.4844  74.6610  65.7684              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2534 T22:   0.2290                                     
REMARK   3      T33:   0.3340 T12:  -0.0110                                     
REMARK   3      T13:   0.0210 T23:   0.0199                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3724 L22:   2.4802                                     
REMARK   3      L33:   2.1436 L12:  -0.5786                                     
REMARK   3      L13:  -0.4211 L23:   0.5014                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0740 S12:   0.1620 S13:  -0.2371                       
REMARK   3      S21:   0.1316 S22:   0.0737 S23:   0.3309                       
REMARK   3      S31:   0.2416 S32:  -0.0151 S33:  -0.0284                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resid 189 through 201 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2453  83.3663  82.0030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3987 T22:   0.3171                                     
REMARK   3      T33:   0.2097 T12:  -0.0039                                     
REMARK   3      T13:  -0.0420 T23:   0.0580                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6634 L22:   3.5874                                     
REMARK   3      L33:   3.1747 L12:  -1.5153                                     
REMARK   3      L13:  -0.5903 L23:   0.6366                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0880 S12:  -0.3551 S13:  -0.2506                       
REMARK   3      S21:   0.5144 S22:   0.0822 S23:   0.1000                       
REMARK   3      S31:   0.3501 S32:  -0.1679 S33:  -0.1653                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'B' and (resid 1 through 105 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   0.9391  97.5939  49.4698              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2029 T22:   0.2100                                     
REMARK   3      T33:   0.2333 T12:  -0.0015                                     
REMARK   3      T13:   0.0147 T23:  -0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9492 L22:   1.6047                                     
REMARK   3      L33:   2.0476 L12:  -0.0869                                     
REMARK   3      L13:  -0.1012 L23:  -0.6242                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0227 S12:   0.0737 S13:  -0.0258                       
REMARK   3      S21:  -0.1583 S22:  -0.0235 S23:  -0.1281                       
REMARK   3      S31:   0.0957 S32:   0.0752 S33:  -0.0165                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'B' and (resid 106 through 141 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -20.9979 101.0212  56.3308              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2333 T22:   0.2805                                     
REMARK   3      T33:   0.3416 T12:   0.0256                                     
REMARK   3      T13:   0.0153 T23:   0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0978 L22:   0.9951                                     
REMARK   3      L33:   0.3562 L12:   0.8436                                     
REMARK   3      L13:  -0.4391 L23:  -0.4391                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0194 S12:   0.0561 S13:   0.0556                       
REMARK   3      S21:   0.0091 S22:   0.0244 S23:   0.3115                       
REMARK   3      S31:   0.0183 S32:  -0.0993 S33:  -0.0470                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'B' and (resid 142 through 201 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.2429 111.8051  51.3192              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2040 T22:   0.2004                                     
REMARK   3      T33:   0.2835 T12:   0.0145                                     
REMARK   3      T13:   0.0153 T23:   0.0110                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9722 L22:   2.0358                                     
REMARK   3      L33:   1.5156 L12:   0.3880                                     
REMARK   3      L13:  -0.6256 L23:  -0.7450                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0605 S12:   0.0250 S13:   0.3604                       
REMARK   3      S21:   0.0324 S22:   0.0674 S23:   0.2356                       
REMARK   3      S31:  -0.1662 S32:  -0.1402 S33:  -0.1030                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4GCI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB074011.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JUL-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 72798                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 53.257                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.57700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4G9H                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN (10 MM HEPES PH 7.5, 100 MM      
REMARK 280  NACL); RESERVOIR (0.2 M AMMONIUM ACETATE, 0.1 M BIS-TRIS:HCL PH     
REMARK 280  5.5, 25% (W/V) PEG 3350); CRYOPROTECTION (RESERVOIR, + 20%          
REMARK 280  ETHYLENE GLYCOL), SITTING DROP VAPOR DIFFUCTION, TEMPERATURE 298K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       44.66900            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     MET A    -1                                                      
REMARK 465     LYS A   202                                                      
REMARK 465     ALA A   203                                                      
REMARK 465     GLU A   204                                                      
REMARK 465     ASN A   205                                                      
REMARK 465     LEU A   206                                                      
REMARK 465     TYR A   207                                                      
REMARK 465     PHE A   208                                                      
REMARK 465     GLN A   209                                                      
REMARK 465     MET B    -1                                                      
REMARK 465     LYS B   202                                                      
REMARK 465     ALA B   203                                                      
REMARK 465     GLU B   204                                                      
REMARK 465     ASN B   205                                                      
REMARK 465     LEU B   206                                                      
REMARK 465     TYR B   207                                                      
REMARK 465     PHE B   208                                                      
REMARK 465     GLN B   209                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   444     O    HOH B   557     1455     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A  47      -65.83    -92.25                                   
REMARK 500    GLU A  66      111.97     73.51                                   
REMARK 500    LEU A 106      -68.38   -103.36                                   
REMARK 500    GLU B  66      113.33     76.63                                   
REMARK 500    LEU B 106      -63.37   -100.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EFI-501894   RELATED DB: TARGETTRACK                     
DBREF  4GCI A    1   202  UNP    Q8D0L3   Q8D0L3_YERPE     1    202             
DBREF  4GCI B    1   202  UNP    Q8D0L3   Q8D0L3_YERPE     1    202             
SEQADV 4GCI MET A   -1  UNP  Q8D0L3              INITIATING METHIONINE          
SEQADV 4GCI VAL A    0  UNP  Q8D0L3              EXPRESSION TAG                 
SEQADV 4GCI ALA A  203  UNP  Q8D0L3              EXPRESSION TAG                 
SEQADV 4GCI GLU A  204  UNP  Q8D0L3              EXPRESSION TAG                 
SEQADV 4GCI ASN A  205  UNP  Q8D0L3              EXPRESSION TAG                 
SEQADV 4GCI LEU A  206  UNP  Q8D0L3              EXPRESSION TAG                 
SEQADV 4GCI TYR A  207  UNP  Q8D0L3              EXPRESSION TAG                 
SEQADV 4GCI PHE A  208  UNP  Q8D0L3              EXPRESSION TAG                 
SEQADV 4GCI GLN A  209  UNP  Q8D0L3              EXPRESSION TAG                 
SEQADV 4GCI MET B   -1  UNP  Q8D0L3              INITIATING METHIONINE          
SEQADV 4GCI VAL B    0  UNP  Q8D0L3              EXPRESSION TAG                 
SEQADV 4GCI ALA B  203  UNP  Q8D0L3              EXPRESSION TAG                 
SEQADV 4GCI GLU B  204  UNP  Q8D0L3              EXPRESSION TAG                 
SEQADV 4GCI ASN B  205  UNP  Q8D0L3              EXPRESSION TAG                 
SEQADV 4GCI LEU B  206  UNP  Q8D0L3              EXPRESSION TAG                 
SEQADV 4GCI TYR B  207  UNP  Q8D0L3              EXPRESSION TAG                 
SEQADV 4GCI PHE B  208  UNP  Q8D0L3              EXPRESSION TAG                 
SEQADV 4GCI GLN B  209  UNP  Q8D0L3              EXPRESSION TAG                 
SEQRES   1 A  211  MET VAL MET MET LYS LEU PHE TYR LYS PRO GLY ALA CYS          
SEQRES   2 A  211  SER LEU SER PRO HIS ILE VAL LEU ARG GLU ALA GLY LEU          
SEQRES   3 A  211  ASP PHE SER ILE GLU ARG VAL ASP LEU VAL THR LYS LYS          
SEQRES   4 A  211  THR GLU THR GLY ALA ASP TYR LEU SER ILE ASN PRO LYS          
SEQRES   5 A  211  GLY GLN VAL PRO ALA LEU VAL LEU ASP ASP GLY SER LEU          
SEQRES   6 A  211  LEU THR GLU GLY VAL ALA ILE VAL GLN TYR LEU ALA ASP          
SEQRES   7 A  211  LYS VAL PRO ASP ARG HIS LEU ILE ALA PRO SER GLY THR          
SEQRES   8 A  211  LEU SER ARG TYR HIS ALA ILE GLU TRP LEU ASN PHE ILE          
SEQRES   9 A  211  ALA THR GLU LEU HIS LYS GLY PHE SER PRO LEU PHE ASN          
SEQRES  10 A  211  PRO ASN THR PRO ASP GLU TYR LYS THR ILE VAL ARG GLU          
SEQRES  11 A  211  ARG LEU ASP LYS GLN PHE SER TYR VAL ASP SER VAL LEU          
SEQRES  12 A  211  ALA GLU HIS ASP TYR LEU LEU GLY LYS LYS PHE SER VAL          
SEQRES  13 A  211  ALA ASP ALA TYR LEU PHE THR VAL SER ARG TRP ALA ASN          
SEQRES  14 A  211  ALA LEU ASN LEU GLN ILE LYS GLU ARG SER HIS LEU ASP          
SEQRES  15 A  211  GLN TYR MET ALA ARG VAL ALA GLU ARG PRO ALA VAL LYS          
SEQRES  16 A  211  ALA ALA LEU ALA ALA GLU ASP ILE LYS ALA GLU ASN LEU          
SEQRES  17 A  211  TYR PHE GLN                                                  
SEQRES   1 B  211  MET VAL MET MET LYS LEU PHE TYR LYS PRO GLY ALA CYS          
SEQRES   2 B  211  SER LEU SER PRO HIS ILE VAL LEU ARG GLU ALA GLY LEU          
SEQRES   3 B  211  ASP PHE SER ILE GLU ARG VAL ASP LEU VAL THR LYS LYS          
SEQRES   4 B  211  THR GLU THR GLY ALA ASP TYR LEU SER ILE ASN PRO LYS          
SEQRES   5 B  211  GLY GLN VAL PRO ALA LEU VAL LEU ASP ASP GLY SER LEU          
SEQRES   6 B  211  LEU THR GLU GLY VAL ALA ILE VAL GLN TYR LEU ALA ASP          
SEQRES   7 B  211  LYS VAL PRO ASP ARG HIS LEU ILE ALA PRO SER GLY THR          
SEQRES   8 B  211  LEU SER ARG TYR HIS ALA ILE GLU TRP LEU ASN PHE ILE          
SEQRES   9 B  211  ALA THR GLU LEU HIS LYS GLY PHE SER PRO LEU PHE ASN          
SEQRES  10 B  211  PRO ASN THR PRO ASP GLU TYR LYS THR ILE VAL ARG GLU          
SEQRES  11 B  211  ARG LEU ASP LYS GLN PHE SER TYR VAL ASP SER VAL LEU          
SEQRES  12 B  211  ALA GLU HIS ASP TYR LEU LEU GLY LYS LYS PHE SER VAL          
SEQRES  13 B  211  ALA ASP ALA TYR LEU PHE THR VAL SER ARG TRP ALA ASN          
SEQRES  14 B  211  ALA LEU ASN LEU GLN ILE LYS GLU ARG SER HIS LEU ASP          
SEQRES  15 B  211  GLN TYR MET ALA ARG VAL ALA GLU ARG PRO ALA VAL LYS          
SEQRES  16 B  211  ALA ALA LEU ALA ALA GLU ASP ILE LYS ALA GLU ASN LEU          
SEQRES  17 B  211  TYR PHE GLN                                                  
HET     CL  A 301       1                                                       
HET    GSH  A 302      20                                                       
HET    GSH  B 301      20                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GSH GLUTATHIONE                                                      
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  GSH    2(C10 H17 N3 O6 S)                                           
FORMUL   6  HOH   *511(H2 O)                                                    
HELIX    1   1 SER A   12  ALA A   22  1                                  11    
HELIX    2   2 ASP A   43  ILE A   47  5                                   5    
HELIX    3   3 GLU A   66  VAL A   78  1                                  13    
HELIX    4   4 PRO A   79  HIS A   82  5                                   4    
HELIX    5   5 THR A   89  LEU A  106  1                                  18    
HELIX    6   6 HIS A  107  GLY A  109  5                                   3    
HELIX    7   7 PHE A  110  ASN A  115  1                                   6    
HELIX    8   8 PRO A  119  ALA A  142  1                                  24    
HELIX    9   9 SER A  153  LEU A  169  1                                  17    
HELIX   10  10 ARG A  176  ALA A  187  1                                  12    
HELIX   11  11 ARG A  189  GLU A  199  1                                  11    
HELIX   12  12 SER B   12  GLY B   23  1                                  12    
HELIX   13  13 ASP B   43  ILE B   47  5                                   5    
HELIX   14  14 GLU B   66  VAL B   78  1                                  13    
HELIX   15  15 PRO B   79  HIS B   82  5                                   4    
HELIX   16  16 THR B   89  LEU B  106  1                                  18    
HELIX   17  17 LEU B  106  ASN B  115  1                                  10    
HELIX   18  18 PRO B  119  ALA B  142  1                                  24    
HELIX   19  19 SER B  153  LEU B  169  1                                  17    
HELIX   20  20 ARG B  176  ALA B  187  1                                  12    
HELIX   21  21 ARG B  189  GLU B  199  1                                  11    
SHEET    1   A 5 LYS A  37  THR A  38  0                                        
SHEET    2   A 5 PHE A  26  ASP A  32 -1  N  ASP A  32   O  LYS A  37           
SHEET    3   A 5 MET A   2  TYR A   6  1  N  LEU A   4   O  GLU A  29           
SHEET    4   A 5 ALA A  55  VAL A  57 -1  O  ALA A  55   N  PHE A   5           
SHEET    5   A 5 LEU A  63  THR A  65 -1  O  LEU A  64   N  LEU A  56           
SHEET    1   B 5 LYS B  37  THR B  38  0                                        
SHEET    2   B 5 PHE B  26  ASP B  32 -1  N  ASP B  32   O  LYS B  37           
SHEET    3   B 5 MET B   2  TYR B   6  1  N  LEU B   4   O  SER B  27           
SHEET    4   B 5 ALA B  55  VAL B  57 -1  O  ALA B  55   N  PHE B   5           
SHEET    5   B 5 LEU B  63  THR B  65 -1  O  LEU B  64   N  LEU B  56           
CISPEP   1 VAL A   53    PRO A   54          0        -2.07                     
CISPEP   2 VAL B   53    PRO B   54          0        -3.60                     
SITE     1 AC1  3 ASP A  25  PHE A  26  HOH A 623                               
SITE     1 AC2 19 CYS A  11  LEU A  33  LYS A  36  GLY A  51                    
SITE     2 AC2 19 GLN A  52  VAL A  53  GLU A  66  GLY A  67                    
SITE     3 AC2 19 HIS A 107  LYS A 108  HOH A 402  HOH A 408                    
SITE     4 AC2 19 HOH A 425  HOH A 489  HOH A 570  HOH A 637                    
SITE     5 AC2 19 ASN B 100  THR B 104  GLU B 105                               
SITE     1 AC3 17 ASN A 100  THR A 104  GLU A 105  CYS B  11                    
SITE     2 AC3 17 LEU B  33  LYS B  36  GLN B  52  VAL B  53                    
SITE     3 AC3 17 GLU B  66  GLY B  67  HIS B 107  HOH B 403                    
SITE     4 AC3 17 HOH B 408  HOH B 420  HOH B 486  HOH B 573                    
SITE     5 AC3 17 HOH B 647                                                     
CRYST1   48.741   89.338   57.546  90.00 112.26  90.00 P 1 21 1      4          
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      0.020516  0.000000  0.008398        0.00000                         
SCALE2      0.000000  0.011193  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018777        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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