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Database: PDB
Entry: 4UEJ
LinkDB: 4UEJ
Original site: 4UEJ 
HEADER    OXIDOREDUCTASE                          18-DEC-14   4UEJ              
TITLE     CLOSED STATE OF GALACTITOL-1-PHOSPHATE 5-DEHYDROGENASE FROM           
TITLE    2 E. COLI IN COMPLEX WITH GLYCEROL.                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GALACTITOL-1-PHOSPHATE 5-DEHYDROGENASE;                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.1.1.251;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.BENAVENTE,M.ESTEBAN-TORRES,G.W.KOHRING,A.CORTES-CABRERA,F.GAGO,     
AUTHOR   2 I.ACEBRON,B.DE LAS RIVAS,R.MUNOZ,J.M.MANCHENO                        
REVDAT   1   15-JUL-15 4UEJ    0                                                
JRNL        AUTH   R.BENAVENTE,M.ESTEBAN-TORRES,G.W.KOHRING,A.CORTES-CABRERA,   
JRNL        AUTH 2 P.A.SANCHEZ-MURCIA,F.GAGO,I.ACEBRON,B.DE LAS RIVAS,R.MUNOZ,  
JRNL        AUTH 3 J.M.MANCHENO                                                 
JRNL        TITL   ENANTIOSELECTIVE OXIDATION OF GALACTITOL 1-PHOSPHATE BY      
JRNL        TITL 2 GALACTITOL-1-PHOSPHATE 5-DEHYDROGENASE FROM ESCHERICHIA      
JRNL        TITL 3 COLI                                                         
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  71  1540 2015              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   26143925                                                     
JRNL        DOI    10.1107/S1399004715009281                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.74 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT 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) : 1.74                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.672                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.35                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.85                          
REMARK   3   NUMBER OF REFLECTIONS             : 69940                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1872                          
REMARK   3   R VALUE            (WORKING SET) : 0.1850                          
REMARK   3   FREE R VALUE                     : 0.2281                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3523                            
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 41.6843 -  5.0848    0.99     2747   140  0.1943 0.2335        
REMARK   3     2  5.0848 -  4.0371    0.98     2679   137  0.1569 0.2023        
REMARK   3     3  4.0371 -  3.5271    1.00     2693   154  0.1624 0.1898        
REMARK   3     4  3.5271 -  3.2047    1.00     2684   159  0.1745 0.1998        
REMARK   3     5  3.2047 -  2.9751    1.00     2657   161  0.1857 0.2208        
REMARK   3     6  2.9751 -  2.7997    1.00     2695   145  0.1890 0.2369        
REMARK   3     7  2.7997 -  2.6595    1.00     2684   145  0.1944 0.2374        
REMARK   3     8  2.6595 -  2.5438    0.97     2564   169  0.1974 0.2317        
REMARK   3     9  2.5438 -  2.4459    1.00     2679   136  0.1846 0.2317        
REMARK   3    10  2.4459 -  2.3615    0.99     2655   146  0.1869 0.2227        
REMARK   3    11  2.3615 -  2.2876    0.99     2680   122  0.1784 0.2273        
REMARK   3    12  2.2876 -  2.2222    0.99     2664   134  0.1756 0.2312        
REMARK   3    13  2.2222 -  2.1637    0.99     2665   144  0.1733 0.2364        
REMARK   3    14  2.1637 -  2.1110    0.99     2668   132  0.1851 0.2366        
REMARK   3    15  2.1110 -  2.0630    0.99     2623   135  0.1874 0.2150        
REMARK   3    16  2.0630 -  2.0191    0.98     2662   144  0.1806 0.2405        
REMARK   3    17  2.0191 -  1.9787    0.99     2633   141  0.1933 0.2482        
REMARK   3    18  1.9787 -  1.9413    0.99     2651   144  0.1932 0.2591        
REMARK   3    19  1.9413 -  1.9067    0.99     2635   141  0.1978 0.2513        
REMARK   3    20  1.9067 -  1.8744    0.99     2654   126  0.1982 0.2625        
REMARK   3    21  1.8744 -  1.8441    0.97     2606   115  0.2061 0.2934        
REMARK   3    22  1.8441 -  1.8157    0.98     2650   119  0.2195 0.2654        
REMARK   3    23  1.8157 -  1.7890    0.98     2614   154  0.2267 0.2886        
REMARK   3    24  1.7890 -  1.7638    0.98     2631   134  0.2382 0.2813        
REMARK   3    25  1.7638 -  1.7400    0.98     2644   146  0.2420 0.2929        
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)     : 0.20             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.98            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.58                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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      :  0.007           5482                                  
REMARK   3   ANGLE     :  1.113           7457                                  
REMARK   3   CHIRALITY :  0.043            859                                  
REMARK   3   PLANARITY :  0.006            967                                  
REMARK   3   DIHEDRAL  : 12.624           2004                                  
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 1 THROUGH 102 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  68.2749  -2.0309  10.6540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2402 T22:   0.2696                                     
REMARK   3      T33:   0.1754 T12:  -0.0066                                     
REMARK   3      T13:   0.0061 T23:  -0.0685                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6354 L22:   0.8226                                     
REMARK   3      L33:   2.9073 L12:  -0.6187                                     
REMARK   3      L13:   0.5437 L23:  -0.1496                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0658 S12:   0.4346 S13:  -0.3105                       
REMARK   3      S21:  -0.1731 S22:  -0.0068 S23:   0.0590                       
REMARK   3      S31:   0.2404 S32:   0.2572 S33:  -0.0244                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 182 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  69.1273   3.3460  23.0025              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0986 T22:   0.0998                                     
REMARK   3      T33:   0.1192 T12:  -0.0015                                     
REMARK   3      T13:   0.0071 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3841 L22:   0.7324                                     
REMARK   3      L33:   3.1767 L12:   0.0935                                     
REMARK   3      L13:  -0.3022 L23:   0.0892                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0147 S12:   0.2050 S13:  -0.0757                       
REMARK   3      S21:  -0.1630 S22:   0.0086 S23:  -0.0176                       
REMARK   3      S31:  -0.0869 S32:   0.1851 S33:  -0.0114                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 285 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  63.9310  -4.7084  43.0176              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0860 T22:   0.1152                                     
REMARK   3      T33:   0.1388 T12:   0.0147                                     
REMARK   3      T13:  -0.0056 T23:   0.0405                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1174 L22:   0.5961                                     
REMARK   3      L33:   1.3256 L12:   0.3859                                     
REMARK   3      L13:  -0.2931 L23:  -0.3926                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0554 S12:  -0.3156 S13:  -0.3686                       
REMARK   3      S21:   0.0432 S22:  -0.0819 S23:  -0.0856                       
REMARK   3      S31:   0.1566 S32:   0.1850 S33:  -0.0161                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 286 THROUGH 346 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  74.5182  -0.7828  22.7240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1874 T22:   0.1677                                     
REMARK   3      T33:   0.1617 T12:   0.0456                                     
REMARK   3      T13:  -0.0020 T23:  -0.0370                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2540 L22:   1.1828                                     
REMARK   3      L33:   2.0519 L12:  -0.4232                                     
REMARK   3      L13:  -0.1004 L23:   1.1341                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0548 S12:   0.3237 S13:  -0.2880                       
REMARK   3      S21:  -0.0646 S22:   0.0159 S23:  -0.0254                       
REMARK   3      S31:   0.2544 S32:   0.2640 S33:  -0.0302                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 102 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  84.0513  37.5313  71.7712              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1626 T22:   0.0914                                     
REMARK   3      T33:   0.1014 T12:  -0.0151                                     
REMARK   3      T13:   0.0082 T23:  -0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1505 L22:   1.0389                                     
REMARK   3      L33:   2.1632 L12:  -0.6047                                     
REMARK   3      L13:   0.4491 L23:  -0.2590                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0138 S12:   0.0939 S13:  -0.1383                       
REMARK   3      S21:  -0.1228 S22:  -0.0227 S23:   0.1002                       
REMARK   3      S31:   0.1524 S32:  -0.0037 S33:   0.0254                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 103 THROUGH 182 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  85.0940  43.0427  84.0647              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0755 T22:   0.0622                                     
REMARK   3      T33:   0.1040 T12:   0.0023                                     
REMARK   3      T13:   0.0053 T23:   0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4764 L22:   0.2014                                     
REMARK   3      L33:   3.5071 L12:   0.0845                                     
REMARK   3      L13:  -0.4208 L23:   0.2913                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0039 S12:  -0.0176 S13:   0.0645                       
REMARK   3      S21:  -0.0859 S22:  -0.0165 S23:   0.0106                       
REMARK   3      S31:  -0.1221 S32:   0.0898 S33:   0.0195                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 183 THROUGH 285 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  80.1375  34.8263 103.8899              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0826 T22:   0.1185                                     
REMARK   3      T33:   0.0976 T12:   0.0150                                     
REMARK   3      T13:   0.0006 T23:   0.0218                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4570 L22:   0.6932                                     
REMARK   3      L33:   1.0482 L12:   0.2598                                     
REMARK   3      L13:  -0.2176 L23:  -0.2858                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0386 S12:  -0.2828 S13:  -0.2776                       
REMARK   3      S21:   0.0329 S22:  -0.0568 S23:  -0.0467                       
REMARK   3      S31:   0.1126 S32:   0.1695 S33:   0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 286 THROUGH 346 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  90.7482  38.8168  83.8136              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1125 T22:   0.1123                                     
REMARK   3      T33:   0.0599 T12:  -0.0032                                     
REMARK   3      T13:   0.0101 T23:   0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2072 L22:   2.1867                                     
REMARK   3      L33:   2.8050 L12:  -0.7211                                     
REMARK   3      L13:  -0.0318 L23:   0.8334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0509 S12:  -0.0562 S13:  -0.0987                       
REMARK   3      S21:  -0.0054 S22:  -0.0408 S23:  -0.0825                       
REMARK   3      S31:   0.1081 S32:   0.1326 S33:  -0.0147                       
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 4UEJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-MAY-15.                  
REMARK 100 THE PDBE ID CODE IS EBI-62610.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96885                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10144                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.74                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.19                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 6.9                                
REMARK 200  R MERGE                    (I) : 0.10                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.20                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.6                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.60                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.20                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4A2C                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       39.40500            
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: 4420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -118.7 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLN A   102     O    HOH A  2121              2.18            
REMARK 500   OD1  ASN A   336     O    HOH A  2308              2.20            
REMARK 500   O    LYS B    31     O    HOH B  2040              2.06            
REMARK 500   O2   GOL B  1349     O    HOH B  2057              2.20            
REMARK 500   O    HOH A  2056     O    HOH A  2138              2.20            
REMARK 500   O    HOH A  2074     O    HOH A  2075              2.18            
REMARK 500   O    HOH A  2077     O    HOH A  2189              2.17            
REMARK 500   O    HOH A  2093     O    HOH A  2224              2.13            
REMARK 500   O    HOH A  2165     O    HOH B  2297              2.11            
REMARK 500   O    HOH A  2179     O    HOH A  2193              2.20            
REMARK 500   O    HOH A  2208     O    HOH A  2209              2.14            
REMARK 500   O    HOH A  2254     O    HOH A  2275              2.18            
REMARK 500   O    HOH B  2023     O    HOH B  2095              2.19            
REMARK 500   O    HOH B  2026     O    HOH B  2028              2.20            
REMARK 500   O    HOH B  2072     O    HOH B  2188              2.18            
REMARK 500   O    HOH B  2212     O    HOH B  2269              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   OE2  GLU A   308    ZN     ZN A  1349     2756     1.92            
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    SER A 111      -56.59   -146.23                                   
REMARK 500    ASN A 161       17.25     59.51                                   
REMARK 500    MET A 288     -140.07     59.63                                   
REMARK 500    ASN A 289       48.70   -162.11                                   
REMARK 500    ALA A 334     -121.29     47.41                                   
REMARK 500    THR B   8      165.56    -46.24                                   
REMARK 500    ASP B   9       36.48     34.38                                   
REMARK 500    LYS B  47       29.11   -142.19                                   
REMARK 500    LYS B 105       59.31   -165.44                                   
REMARK 500    SER B 111      -55.83   -147.53                                   
REMARK 500    MET B 288     -137.75     53.98                                   
REMARK 500    ASN B 289       51.14   -165.81                                   
REMARK 500    SER B 322     -164.29    -79.47                                   
REMARK 500    ALA B 334     -132.75     51.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1347  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 103   SG                                                     
REMARK 620 2 CYS A  92   SG  117.2                                              
REMARK 620 3 CYS A  95   SG  104.3 105.0                                        
REMARK 620 4 CYS A  89   SG  104.0 106.3 120.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1347  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  92   SG                                                     
REMARK 620 2 CYS B  89   SG  106.6                                              
REMARK 620 3 CYS B  95   SG  105.5 120.2                                        
REMARK 620 4 CYS B 103   SG  119.5 102.9 103.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1348  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  38   SG                                                     
REMARK 620 2 GOL A1350   O2   97.5                                              
REMARK 620 3 HIS A  59   NE2 102.1 110.0                                        
REMARK 620 4 GOL A1350   O1  169.2  75.5  88.1                                  
REMARK 620 5 HOH A2053   O    90.5 134.3 112.1  88.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1348  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GOL B1349   O2                                                     
REMARK 620 2 GOL B1349   O1   75.1                                              
REMARK 620 3 CYS B  38   SG  103.4 164.9                                        
REMARK 620 4 HIS B  59   NE2 105.0  91.6 103.3                                  
REMARK 620 5 HOH B2052   O   139.6  82.2  90.1 108.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1349  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2263   O                                                      
REMARK 620 2 HIS A 267   ND1 105.2                                              
REMARK 620 3 HIS B 267   ND1 106.3 121.5                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1347                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1348                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1349                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1350                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1347                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1348                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1349                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4UEK   RELATED DB: PDB                                   
REMARK 900  GALACTITOL-1-PHOSPHATE 5-DEHYDROGENASE FROM E. COLI                 
REMARK 900  WITH TRIS WITHIN THE ACTIVE SITE.                                   
REMARK 900 RELATED ID: 4UEO   RELATED DB: PDB                                   
REMARK 900  OPEN STATE OF GALACTITOL-1-PHOSPHATE 5-DEHYDROGENASE                
REMARK 900  FROM E. COLI, WITH ZINC IN THE CATALYTIC SITE.                      
DBREF  4UEJ A    1   346  UNP    P0A9S3   GATD_ECOLI       1    346             
DBREF  4UEJ B    1   346  UNP    P0A9S3   GATD_ECOLI       1    346             
SEQRES   1 A  346  MET LYS SER VAL VAL ASN ASP THR ASP GLY ILE VAL ARG          
SEQRES   2 A  346  VAL ALA GLU SER VAL ILE PRO GLU ILE LYS HIS GLN ASP          
SEQRES   3 A  346  GLU VAL ARG VAL LYS ILE ALA SER SER GLY LEU CYS GLY          
SEQRES   4 A  346  SER ASP LEU PRO ARG ILE PHE LYS ASN GLY ALA HIS TYR          
SEQRES   5 A  346  TYR PRO ILE THR LEU GLY HIS GLU PHE SER GLY TYR ILE          
SEQRES   6 A  346  ASP ALA VAL GLY SER GLY VAL ASP ASP LEU HIS PRO GLY          
SEQRES   7 A  346  ASP ALA VAL ALA CYS VAL PRO LEU LEU PRO CYS PHE THR          
SEQRES   8 A  346  CYS PRO GLU CYS LEU LYS GLY PHE TYR SER GLN CYS ALA          
SEQRES   9 A  346  LYS TYR ASP PHE ILE GLY SER ARG ARG ASP GLY GLY PHE          
SEQRES  10 A  346  ALA GLU TYR ILE VAL VAL LYS ARG LYS ASN VAL PHE ALA          
SEQRES  11 A  346  LEU PRO THR ASP MET PRO ILE GLU ASP GLY ALA PHE ILE          
SEQRES  12 A  346  GLU PRO ILE THR VAL GLY LEU HIS ALA PHE HIS LEU ALA          
SEQRES  13 A  346  GLN GLY CYS GLU ASN LYS ASN VAL ILE ILE ILE GLY ALA          
SEQRES  14 A  346  GLY THR ILE GLY LEU LEU ALA ILE GLN CYS ALA VAL ALA          
SEQRES  15 A  346  LEU GLY ALA LYS SER VAL THR ALA ILE ASP ILE SER SER          
SEQRES  16 A  346  GLU LYS LEU ALA LEU ALA LYS SER PHE GLY ALA MET GLN          
SEQRES  17 A  346  THR PHE ASN SER SER GLU MET SER ALA PRO GLN MET GLN          
SEQRES  18 A  346  SER VAL LEU ARG GLU LEU ARG PHE ASN GLN LEU ILE LEU          
SEQRES  19 A  346  GLU THR ALA GLY VAL PRO GLN THR VAL GLU LEU ALA VAL          
SEQRES  20 A  346  GLU ILE ALA GLY PRO HIS ALA GLN LEU ALA LEU VAL GLY          
SEQRES  21 A  346  THR LEU HIS GLN ASP LEU HIS LEU THR SER ALA THR PHE          
SEQRES  22 A  346  GLY LYS ILE LEU ARG LYS GLU LEU THR VAL ILE GLY SER          
SEQRES  23 A  346  TRP MET ASN TYR SER SER PRO TRP PRO GLY GLN GLU TRP          
SEQRES  24 A  346  GLU THR ALA SER ARG LEU LEU THR GLU ARG LYS LEU SER          
SEQRES  25 A  346  LEU GLU PRO LEU ILE ALA HIS ARG GLY SER PHE GLU SER          
SEQRES  26 A  346  PHE ALA GLN ALA VAL ARG ASP ILE ALA ARG ASN ALA MET          
SEQRES  27 A  346  PRO GLY LYS VAL LEU LEU ILE PRO                              
SEQRES   1 B  346  MET LYS SER VAL VAL ASN ASP THR ASP GLY ILE VAL ARG          
SEQRES   2 B  346  VAL ALA GLU SER VAL ILE PRO GLU ILE LYS HIS GLN ASP          
SEQRES   3 B  346  GLU VAL ARG VAL LYS ILE ALA SER SER GLY LEU CYS GLY          
SEQRES   4 B  346  SER ASP LEU PRO ARG ILE PHE LYS ASN GLY ALA HIS TYR          
SEQRES   5 B  346  TYR PRO ILE THR LEU GLY HIS GLU PHE SER GLY TYR ILE          
SEQRES   6 B  346  ASP ALA VAL GLY SER GLY VAL ASP ASP LEU HIS PRO GLY          
SEQRES   7 B  346  ASP ALA VAL ALA CYS VAL PRO LEU LEU PRO CYS PHE THR          
SEQRES   8 B  346  CYS PRO GLU CYS LEU LYS GLY PHE TYR SER GLN CYS ALA          
SEQRES   9 B  346  LYS TYR ASP PHE ILE GLY SER ARG ARG ASP GLY GLY PHE          
SEQRES  10 B  346  ALA GLU TYR ILE VAL VAL LYS ARG LYS ASN VAL PHE ALA          
SEQRES  11 B  346  LEU PRO THR ASP MET PRO ILE GLU ASP GLY ALA PHE ILE          
SEQRES  12 B  346  GLU PRO ILE THR VAL GLY LEU HIS ALA PHE HIS LEU ALA          
SEQRES  13 B  346  GLN GLY CYS GLU ASN LYS ASN VAL ILE ILE ILE GLY ALA          
SEQRES  14 B  346  GLY THR ILE GLY LEU LEU ALA ILE GLN CYS ALA VAL ALA          
SEQRES  15 B  346  LEU GLY ALA LYS SER VAL THR ALA ILE ASP ILE SER SER          
SEQRES  16 B  346  GLU LYS LEU ALA LEU ALA LYS SER PHE GLY ALA MET GLN          
SEQRES  17 B  346  THR PHE ASN SER SER GLU MET SER ALA PRO GLN MET GLN          
SEQRES  18 B  346  SER VAL LEU ARG GLU LEU ARG PHE ASN GLN LEU ILE LEU          
SEQRES  19 B  346  GLU THR ALA GLY VAL PRO GLN THR VAL GLU LEU ALA VAL          
SEQRES  20 B  346  GLU ILE ALA GLY PRO HIS ALA GLN LEU ALA LEU VAL GLY          
SEQRES  21 B  346  THR LEU HIS GLN ASP LEU HIS LEU THR SER ALA THR PHE          
SEQRES  22 B  346  GLY LYS ILE LEU ARG LYS GLU LEU THR VAL ILE GLY SER          
SEQRES  23 B  346  TRP MET ASN TYR SER SER PRO TRP PRO GLY GLN GLU TRP          
SEQRES  24 B  346  GLU THR ALA SER ARG LEU LEU THR GLU ARG LYS LEU SER          
SEQRES  25 B  346  LEU GLU PRO LEU ILE ALA HIS ARG GLY SER PHE GLU SER          
SEQRES  26 B  346  PHE ALA GLN ALA VAL ARG ASP ILE ALA ARG ASN ALA MET          
SEQRES  27 B  346  PRO GLY LYS VAL LEU LEU ILE PRO                              
HET     ZN  A1347       1                                                       
HET     ZN  A1348       1                                                       
HET     ZN  A1349       1                                                       
HET    GOL  A1350       6                                                       
HET     ZN  B1347       1                                                       
HET     ZN  B1348       1                                                       
HET    GOL  B1349       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM      ZN ZINC ION                                                         
HETSYN     GOL GLYCERIN; PROPANE_1,2,3-TRIOL                                    
FORMUL   3  GOL    2(C3 H8 O3)                                                  
FORMUL   4   ZN    5(ZN 2+)                                                     
FORMUL   5  HOH   *654(H2 O)                                                    
HELIX    1   1 THR A    8  GLY A   10  5                                   3    
HELIX    2   2 SER A   40  LYS A   47  1                                   8    
HELIX    3   3 CYS A   92  LYS A   97  1                                   6    
HELIX    4   4 PHE A   99  CYS A  103  5                                   5    
HELIX    5   5 PRO A  136  ALA A  141  5                                   6    
HELIX    6   6 PHE A  142  ALA A  156  1                                  15    
HELIX    7   7 GLY A  170  LEU A  183  1                                  14    
HELIX    8   8 SER A  195  PHE A  204  1                                  10    
HELIX    9   9 SER A  216  LEU A  224  1                                   9    
HELIX   10  10 ARG A  225  ARG A  228  5                                   4    
HELIX   11  11 VAL A  239  ALA A  250  1                                  12    
HELIX   12  12 THR A  269  LYS A  279  1                                  11    
HELIX   13  13 GLY A  296  GLU A  308  1                                  13    
HELIX   14  14 LEU A  313  PRO A  315  5                                   3    
HELIX   15  15 SER A  322  ALA A  334  1                                  13    
HELIX   16  16 THR B    8  GLY B   10  5                                   3    
HELIX   17  17 SER B   40  LYS B   47  1                                   8    
HELIX   18  18 CYS B   92  LYS B   97  1                                   6    
HELIX   19  19 PHE B   99  CYS B  103  5                                   5    
HELIX   20  20 PRO B  136  ALA B  141  5                                   6    
HELIX   21  21 PHE B  142  ALA B  156  1                                  15    
HELIX   22  22 GLY B  170  LEU B  183  1                                  14    
HELIX   23  23 SER B  194  PHE B  204  1                                  11    
HELIX   24  24 SER B  216  LEU B  224  1                                   9    
HELIX   25  25 ARG B  225  ARG B  228  5                                   4    
HELIX   26  26 VAL B  239  ALA B  250  1                                  12    
HELIX   27  27 THR B  269  LYS B  279  1                                  11    
HELIX   28  28 GLY B  296  GLU B  308  1                                  13    
HELIX   29  29 LEU B  313  PRO B  315  5                                   3    
HELIX   30  30 SER B  322  ALA B  334  1                                  13    
SHEET    1  AA 2 LYS A   2  ASP A   7  0                                        
SHEET    2  AA 2 ILE A  11  GLU A  16 -1  O  ILE A  11   N  ASP A   7           
SHEET    1  AB 2 TYR A 120  LYS A 124  0                                        
SHEET    2  AB 2 GLU A  27  GLY A  36 -1  O  VAL A  28   N  VAL A 123           
SHEET    1  AC 6 VAL A 128  ALA A 130  0                                        
SHEET    2  AC 6 ALA A  80  CYS A  83 -1  O  ALA A  82   N  PHE A 129           
SHEET    3  AC 6 GLU A  60  VAL A  68 -1  O  PHE A  61   N  CYS A  83           
SHEET    4  AC 6 GLU A  27  GLY A  36 -1  O  ARG A  29   N  ASP A  66           
SHEET    5  AC 6 LYS A 341  LEU A 344 -1  O  LEU A 344   N  SER A  35           
SHEET    6  AC 6 ILE A 317  GLY A 321 -1  N  ALA A 318   O  LYS A 341           
SHEET    1  AD 5 VAL A 128  ALA A 130  0                                        
SHEET    2  AD 5 ALA A  80  CYS A  83 -1  O  ALA A  82   N  PHE A 129           
SHEET    3  AD 5 GLU A  60  VAL A  68 -1  O  PHE A  61   N  CYS A  83           
SHEET    4  AD 5 GLU A  27  GLY A  36 -1  O  ARG A  29   N  ASP A  66           
SHEET    5  AD 5 TYR A 120  LYS A 124 -1  O  ILE A 121   N  VAL A  30           
SHEET    1  AE 2 LEU A  86  LEU A  87  0                                        
SHEET    2  AE 2 ASP A 107  PHE A 108 -1  O  ASP A 107   N  LEU A  87           
SHEET    1  AF12 GLN A 208  ASN A 211  0                                        
SHEET    2  AF12 SER A 187  ASP A 192  1  O  ALA A 190   N  PHE A 210           
SHEET    3  AF12 ASN A 163  ILE A 167  1  O  VAL A 164   N  THR A 189           
SHEET    4  AF12 GLN A 231  GLU A 235  1  O  LEU A 232   N  ILE A 165           
SHEET    5  AF12 GLN A 255  LEU A 258  1  O  GLN A 255   N  ILE A 233           
SHEET    6  AF12 THR A 282  GLY A 285  1  O  THR A 282   N  LEU A 256           
SHEET    7  AF12 THR B 282  GLY B 285 -1  O  VAL B 283   N  VAL A 283           
SHEET    8  AF12 GLN B 255  LEU B 258  1  O  LEU B 256   N  ILE B 284           
SHEET    9  AF12 GLN B 231  GLU B 235  1  O  GLN B 231   N  GLN B 255           
SHEET   10  AF12 ASN B 163  ILE B 167  1  O  ASN B 163   N  LEU B 232           
SHEET   11  AF12 SER B 187  ASP B 192  1  O  SER B 187   N  VAL B 164           
SHEET   12  AF12 GLN B 208  ASN B 211  1  O  GLN B 208   N  ALA B 190           
SHEET    1  AG 2 LEU A 266  LEU A 268  0                                        
SHEET    2  AG 2 LEU B 266  LEU B 268 -1  O  LEU B 266   N  LEU A 268           
SHEET    1  BA 2 LYS B   2  ASP B   7  0                                        
SHEET    2  BA 2 ILE B  11  GLU B  16 -1  O  ILE B  11   N  ASP B   7           
SHEET    1  BB 2 TYR B 120  LYS B 124  0                                        
SHEET    2  BB 2 GLU B  27  GLY B  36 -1  O  VAL B  28   N  VAL B 123           
SHEET    1  BC 6 VAL B 128  ALA B 130  0                                        
SHEET    2  BC 6 ALA B  80  CYS B  83 -1  O  ALA B  82   N  PHE B 129           
SHEET    3  BC 6 GLU B  60  VAL B  68 -1  O  PHE B  61   N  CYS B  83           
SHEET    4  BC 6 GLU B  27  GLY B  36 -1  O  ARG B  29   N  ASP B  66           
SHEET    5  BC 6 LYS B 341  LEU B 344 -1  O  LEU B 344   N  SER B  35           
SHEET    6  BC 6 ILE B 317  GLY B 321 -1  N  ALA B 318   O  LYS B 341           
SHEET    1  BD 5 VAL B 128  ALA B 130  0                                        
SHEET    2  BD 5 ALA B  80  CYS B  83 -1  O  ALA B  82   N  PHE B 129           
SHEET    3  BD 5 GLU B  60  VAL B  68 -1  O  PHE B  61   N  CYS B  83           
SHEET    4  BD 5 GLU B  27  GLY B  36 -1  O  ARG B  29   N  ASP B  66           
SHEET    5  BD 5 TYR B 120  LYS B 124 -1  O  ILE B 121   N  VAL B  30           
SHEET    1  BE 2 LEU B  86  LEU B  87  0                                        
SHEET    2  BE 2 ASP B 107  PHE B 108 -1  O  ASP B 107   N  LEU B  87           
LINK        ZN    ZN A1347                 SG  CYS A 103     1555   1555  2.46  
LINK        ZN    ZN A1347                 SG  CYS A  92     1555   1555  2.33  
LINK        ZN    ZN A1347                 SG  CYS A  95     1555   1555  2.31  
LINK        ZN    ZN A1347                 SG  CYS A  89     1555   1555  2.35  
LINK        ZN    ZN A1348                 O1  GOL A1350     1555   1555  2.20  
LINK        ZN    ZN A1348                 O2  GOL A1350     1555   1555  2.22  
LINK        ZN    ZN A1348                 SG  CYS A  38     1555   1555  2.69  
LINK        ZN    ZN A1348                 O   HOH A2053     1555   1555  2.01  
LINK        ZN    ZN A1348                 NE2 HIS A  59     1555   1555  2.09  
LINK        ZN    ZN A1349                 ND1 HIS A 267     1555   1555  1.99  
LINK        ZN    ZN A1349                 O   HOH A2263     1555   1555  2.22  
LINK        ZN    ZN A1349                 ND1 HIS B 267     1555   1555  1.95  
LINK        ZN    ZN B1347                 SG  CYS B 103     1555   1555  2.38  
LINK        ZN    ZN B1347                 SG  CYS B  95     1555   1555  2.33  
LINK        ZN    ZN B1347                 SG  CYS B  89     1555   1555  2.36  
LINK        ZN    ZN B1347                 SG  CYS B  92     1555   1555  2.31  
LINK        ZN    ZN B1348                 O   HOH B2052     1555   1555  2.04  
LINK        ZN    ZN B1348                 NE2 HIS B  59     1555   1555  2.11  
LINK        ZN    ZN B1348                 SG  CYS B  38     1555   1555  2.69  
LINK        ZN    ZN B1348                 O2  GOL B1349     1555   1555  2.20  
LINK        ZN    ZN B1348                 O1  GOL B1349     1555   1555  2.23  
CISPEP   1 TYR A   53    PRO A   54          0        -3.19                     
CISPEP   2 SER A  292    PRO A  293          0         0.29                     
CISPEP   3 TRP A  294    PRO A  295          0         0.01                     
CISPEP   4 TYR B   53    PRO B   54          0        -3.62                     
CISPEP   5 SER B  292    PRO B  293          0        -0.27                     
CISPEP   6 TRP B  294    PRO B  295          0         0.44                     
SITE     1 AC1  4 CYS A  89  CYS A  92  CYS A  95  CYS A 103                    
SITE     1 AC2  4 CYS A  38  HIS A  59  GOL A1350  HOH A2053                    
SITE     1 AC3  3 HIS A 267  HOH A2263  HIS B 267                               
SITE     1 AC4  6 SER A  40  HIS A  59  GLU A 144  VAL A 148                    
SITE     2 AC4  6  ZN A1348  HOH A2053                                          
SITE     1 AC5  4 CYS B  89  CYS B  92  CYS B  95  CYS B 103                    
SITE     1 AC6  4 CYS B  38  HIS B  59  GOL B1349  HOH B2052                    
SITE     1 AC7  6 SER B  40  HIS B  59  GLU B 144   ZN B1348                    
SITE     2 AC7  6 HOH B2052  HOH B2057                                          
CRYST1   65.311   78.810   68.244  90.00  94.75  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      0.015311  0.000000  0.001272        0.00000                         
SCALE2      0.000000  0.012689  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014704        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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