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Database: PDB
Entry: 4UEO
LinkDB: 4UEO
Original site: 4UEO 
HEADER    OXIDOREDUCTASE                          18-DEC-14   4UEO              
TITLE     OPEN STATE OF GALACTITOL-1-PHOSPHATE 5-DEHYDROGENASE FROM E.          
TITLE    2 COLI, WITH ZINC IN THE CATALYTIC SITE.                               
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 4UEO    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.    2.00 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-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.000                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.235                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.52                          
REMARK   3   NUMBER OF REFLECTIONS             : 46912                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1975                          
REMARK   3   R VALUE            (WORKING SET) : 0.1943                          
REMARK   3   FREE R VALUE                     : 0.2558                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2376                            
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 44.2453 -  5.1400    1.00     2772   133  0.1849 0.2418        
REMARK   3     2  5.1400 -  4.0807    1.00     2703   156  0.1494 0.2239        
REMARK   3     3  4.0807 -  3.5651    0.99     2648   150  0.1681 0.2203        
REMARK   3     4  3.5651 -  3.2393    0.99     2661   157  0.1806 0.2440        
REMARK   3     5  3.2393 -  3.0072    0.98     2630   155  0.1969 0.2587        
REMARK   3     6  3.0072 -  2.8299    0.99     2617   146  0.2053 0.2500        
REMARK   3     7  2.8299 -  2.6882    0.98     2629   143  0.2037 0.2467        
REMARK   3     8  2.6882 -  2.5712    0.98     2647   122  0.2023 0.2885        
REMARK   3     9  2.5712 -  2.4722    0.98     2602   158  0.2077 0.2796        
REMARK   3    10  2.4722 -  2.3869    0.97     2600   137  0.2172 0.2950        
REMARK   3    11  2.3869 -  2.3123    0.97     2616   137  0.2146 0.2681        
REMARK   3    12  2.3123 -  2.2462    0.97     2615   123  0.2242 0.2850        
REMARK   3    13  2.2462 -  2.1871    0.93     2485   120  0.3065 0.4106        
REMARK   3    14  2.1871 -  2.1337    0.97     2576   159  0.2372 0.2719        
REMARK   3    15  2.1337 -  2.0852    0.96     2597   126  0.2545 0.3310        
REMARK   3    16  2.0852 -  2.0408    0.96     2558   123  0.2799 0.3219        
REMARK   3    17  2.0408 -  2.0000    0.95     2580   131  0.3089 0.3820        
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)     : 0.27             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.55            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.47                          
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      :  0.009           5364                                  
REMARK   3   ANGLE     :  1.409           7278                                  
REMARK   3   CHIRALITY :  0.057            838                                  
REMARK   3   PLANARITY :  0.007            940                                  
REMARK   3   DIHEDRAL  : 13.608           1952                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS.                                                        
REMARK   3   NUMBER OF TLS GROUPS: 9                                            
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID    1  THROUGH   79 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  25.3790  -6.5505  -4.3446              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3979 T22:   0.3615                                     
REMARK   3      T33:   0.4424 T12:   0.0342                                     
REMARK   3      T13:   0.0448 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8126 L22:   6.2396                                     
REMARK   3      L33:   4.9719 L12:   0.9339                                     
REMARK   3      L13:  -0.4296 L23:   3.4857                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1094 S12:  -0.3009 S13:  -0.1400                       
REMARK   3      S21:  -0.0534 S22:   0.2146 S23:  -1.0658                       
REMARK   3      S31:  -0.0662 S32:   0.6096 S33:  -0.2640                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID   80  THROUGH  183 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8306  -4.1635   5.3014              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2161 T22:   0.2632                                     
REMARK   3      T33:   0.2405 T12:   0.0284                                     
REMARK   3      T13:  -0.0256 T23:  -0.0183                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6034 L22:   2.9167                                     
REMARK   3      L33:   3.9004 L12:  -0.2934                                     
REMARK   3      L13:  -1.5237 L23:   1.5657                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0790 S12:   0.0662 S13:  -0.2502                       
REMARK   3      S21:  -0.1752 S22:  -0.1179 S23:  -0.0495                       
REMARK   3      S31:   0.1135 S32:   0.0374 S33:   0.1746                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID  184  THROUGH  322 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7731   4.7567  20.6682              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2105 T22:   0.2656                                     
REMARK   3      T33:   0.2485 T12:  -0.0109                                     
REMARK   3      T13:   0.0244 T23:   0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9652 L22:   2.4325                                     
REMARK   3      L33:   3.4366 L12:   0.7463                                     
REMARK   3      L13:  -0.9682 L23:  -0.3829                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1499 S12:  -0.1477 S13:  -0.0510                       
REMARK   3      S21:   0.2099 S22:  -0.2502 S23:  -0.0071                       
REMARK   3      S31:  -0.2482 S32:   0.2426 S33:   0.0875                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID  323  THROUGH  346 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  31.8059   6.3601   3.0294              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6651 T22:   0.5655                                     
REMARK   3      T33:   1.3104 T12:  -0.1283                                     
REMARK   3      T13:   0.2743 T23:  -0.2752                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7526 L22:   6.4077                                     
REMARK   3      L33:   1.5290 L12:  -1.4750                                     
REMARK   3      L13:   0.6554 L23:  -0.5272                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1273 S12:   0.4265 S13:  -1.0947                       
REMARK   3      S21:  -0.0804 S22:   0.4998 S23:  -1.9376                       
REMARK   3      S31:   0.0720 S32:   1.1778 S33:  -0.4723                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID    1  THROUGH   46 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.2622 -10.2486  62.6043              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7257 T22:   0.5506                                     
REMARK   3      T33:   0.5101 T12:   0.0950                                     
REMARK   3      T13:  -0.0216 T23:  -0.1549                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4023 L22:   4.8864                                     
REMARK   3      L33:   3.4792 L12:  -2.2740                                     
REMARK   3      L13:  -1.8610 L23:   2.2496                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6668 S12:  -0.7423 S13:   0.3238                       
REMARK   3      S21:   1.3369 S22:   0.9612 S23:  -0.7251                       
REMARK   3      S31:   0.5585 S32:   0.7464 S33:  -0.1918                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID   47  THROUGH   79 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.3019  -7.6173  56.8780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4637 T22:   0.4017                                     
REMARK   3      T33:   0.3864 T12:  -0.0299                                     
REMARK   3      T13:   0.0701 T23:  -0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4303 L22:   6.5806                                     
REMARK   3      L33:   5.5480 L12:  -4.0187                                     
REMARK   3      L13:  -2.5546 L23:   0.2941                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2864 S12:  -0.5522 S13:   0.1673                       
REMARK   3      S21:   0.7209 S22:  -0.0522 S23:  -0.2724                       
REMARK   3      S31:   0.1772 S32:   0.6533 S33:   0.3638                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID   80  THROUGH  155 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.9683  -7.6620  47.2457              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2975 T22:   0.3275                                     
REMARK   3      T33:   0.3158 T12:  -0.0322                                     
REMARK   3      T13:   0.0518 T23:  -0.0559                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4071 L22:   4.5822                                     
REMARK   3      L33:   7.6214 L12:   0.0191                                     
REMARK   3      L13:  -3.5133 L23:  -2.3126                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0583 S12:  -0.0656 S13:   0.0399                       
REMARK   3      S21:   0.4161 S22:  -0.0643 S23:  -0.1235                       
REMARK   3      S31:  -0.3599 S32:   0.1190 S33:   0.0033                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  156  THROUGH  322 )              
REMARK   3    ORIGIN FOR THE GROUP (A):   4.6355 -20.6340  33.9741              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3422 T22:   0.2688                                     
REMARK   3      T33:   0.2865 T12:  -0.0035                                     
REMARK   3      T13:   0.0926 T23:   0.0177                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5813 L22:   1.9878                                     
REMARK   3      L33:   2.6209 L12:   0.1466                                     
REMARK   3      L13:  -1.3826 L23:  -0.9390                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1506 S12:  -0.1769 S13:  -0.2191                       
REMARK   3      S21:   0.0774 S22:  -0.1791 S23:  -0.0655                       
REMARK   3      S31:   0.2987 S32:   0.1838 S33:   0.3091                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  323  THROUGH  346 )              
REMARK   3    ORIGIN FOR THE GROUP (A):   2.0467 -22.8999  60.3453              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1069 T22:   0.8543                                     
REMARK   3      T33:   0.5467 T12:   0.3921                                     
REMARK   3      T13:  -0.0608 T23:  -0.0662                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4374 L22:   3.8662                                     
REMARK   3      L33:   5.1425 L12:   0.2506                                     
REMARK   3      L13:   2.3807 L23:   2.5463                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4226 S12:  -0.8287 S13:  -0.1617                       
REMARK   3      S21:   1.9917 S22:   0.9355 S23:  -0.8335                       
REMARK   3      S31:   0.5184 S32:   1.5594 S33:  -0.2734                       
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 4UEO 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-62615.                                       
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               : ALBA                               
REMARK 200  BEAMLINE                       : XALOC                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.28245                            
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          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47058                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.00                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.23                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.4                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.70                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.4                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.56                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.80                               
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   (%): 46                                        
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       38.45300            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.5 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 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     ALA A  334                                                       
REMARK 475     ARG A  335                                                       
REMARK 475     ASN A  336                                                       
REMARK 475     ALA A  337                                                       
REMARK 475     MET A  338                                                       
REMARK 475     ASN B    6                                                       
REMARK 475     ASP B    7                                                       
REMARK 475     THR B    8                                                       
REMARK 475     ASP B    9                                                       
REMARK 475     GLY B   10                                                       
REMARK 475     ILE B   11                                                       
REMARK 475     VAL B   12                                                       
REMARK 475     ASP B   41                                                       
REMARK 475     LEU B   42                                                       
REMARK 475     PRO B   43                                                       
REMARK 475     ARG B   44                                                       
REMARK 475     ILE B   45                                                       
REMARK 475     PHE B   46                                                       
REMARK 475     LYS B   47                                                       
REMARK 475     ASN B   48                                                       
REMARK 475     GLY B   49                                                       
REMARK 475     ALA B   50                                                       
REMARK 475     HIS B   51                                                       
REMARK 475     TYR B   52                                                       
REMARK 475     TYR B   53                                                       
REMARK 475     PRO B   54                                                       
REMARK 475     ILE B   55                                                       
REMARK 475     THR B   56                                                       
REMARK 475     LEU B   57                                                       
REMARK 475     ASP B  332                                                       
REMARK 475     ILE B  333                                                       
REMARK 475     ALA B  334                                                       
REMARK 475     ARG B  335                                                       
REMARK 475     ASN B  336                                                       
REMARK 475     ALA B  337                                                       
REMARK 475     MET B  338                                                       
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   OE2  GLU A    94     NH1  ARG B   228              2.17            
REMARK 500   OE1  GLU A   144     O    HOH A  2026              2.19            
REMARK 500   NH1  ARG A   331     O    HOH A  2007              2.12            
REMARK 500   O    ASP A   332     NH1  ARG A   335              2.13            
REMARK 500   OD2  ASP A   332     O    HOH A  2162              2.17            
REMARK 500   O    LEU B    37     O    HOH B  2016              2.08            
REMARK 500   O    LEU B    42     N    ARG B    44              2.14            
REMARK 500   OD1  ASN B   336     N    MET B   338              2.08            
REMARK 500   O    HOH A  2007     O    HOH A  2008              1.96            
REMARK 500   O    HOH A  2059     O    HOH A  2155              2.17            
REMARK 500   O    HOH A  2060     O    HOH A  2156              2.17            
REMARK 500   O    HOH A  2113     O    HOH A  2116              2.13            
REMARK 500   O    HOH A  2150     O    HOH A  2157              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 228   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    LEU B  42   CA  -  CB  -  CG  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    PRO B  54   C   -  N   -  CA  ANGL. DEV. =  18.0 DEGREES          
REMARK 500    PRO B  54   C   -  N   -  CD  ANGL. DEV. = -17.2 DEGREES          
REMARK 500    ARG B 335   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    ARG B 335   NE  -  CZ  -  NH2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  48      -87.32     61.59                                   
REMARK 500    LEU A  57     -168.70    -76.69                                   
REMARK 500    LYS A 105       61.02   -117.81                                   
REMARK 500    SER A 111      -69.27   -146.67                                   
REMARK 500    ALA A 118      160.72    179.18                                   
REMARK 500    ALA A 169       41.42   -109.99                                   
REMARK 500    MET A 288     -141.39     58.62                                   
REMARK 500    ASN A 289       45.78   -160.09                                   
REMARK 500    SER A 322     -163.28    -76.02                                   
REMARK 500    ALA A 334      -69.89     29.16                                   
REMARK 500    ASN A 336     -107.35   -110.78                                   
REMARK 500    ALA A 337     -150.94   -145.24                                   
REMARK 500    THR B   8      131.19    -38.08                                   
REMARK 500    ILE B  11      -90.47   -102.51                                   
REMARK 500    VAL B  12     -143.37     45.99                                   
REMARK 500    ARG B  13     -179.11     65.13                                   
REMARK 500    ALA B  15     -169.25   -114.03                                   
REMARK 500    LEU B  42      -90.01    -70.82                                   
REMARK 500    PRO B  43       42.64    -66.34                                   
REMARK 500    ASN B  48     -161.28     56.79                                   
REMARK 500    ALA B  50     -107.17     67.38                                   
REMARK 500    HIS B  51      -11.97     73.72                                   
REMARK 500    TYR B  52      100.14     67.27                                   
REMARK 500    PRO B  54      173.31      3.48                                   
REMARK 500    ILE B  55      161.17     19.01                                   
REMARK 500    PHE B  90       -5.17     68.71                                   
REMARK 500    LYS B 105       58.51   -107.90                                   
REMARK 500    SER B 111      -82.18   -163.76                                   
REMARK 500    ARG B 113     -123.54    -81.25                                   
REMARK 500    PHE B 117       47.78   -106.86                                   
REMARK 500    ALA B 169       43.05   -106.84                                   
REMARK 500    MET B 288     -137.54     52.11                                   
REMARK 500    ASN B 289       42.52   -159.04                                   
REMARK 500    HIS B 319      138.21   -170.11                                   
REMARK 500    PHE B 326      -30.50   -172.42                                   
REMARK 500    GLN B 328      -77.19    -32.75                                   
REMARK 500    ALA B 329     -108.63     31.29                                   
REMARK 500    VAL B 330      116.13    -30.81                                   
REMARK 500    ARG B 331     -118.83   -125.91                                   
REMARK 500    ASP B 332       51.27   -147.56                                   
REMARK 500    ALA B 334      178.28     65.05                                   
REMARK 500    ASN B 336      173.71    151.03                                   
REMARK 500    ALA B 337       45.57    114.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG B  335     ASN B  336                  128.90                    
REMARK 500 ASN B  336     ALA B  337                 -138.08                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED            
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND ARE                    
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL                 
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE          
REMARK 525 NUMBER; I=INSERTION CODE): THESE HAVE BEEN REPOSITIONED              
REMARK 525 BY APPLYING THE SYMMETRY TRANSFORMATION INDICATED.                   
REMARK 525                                                                      
REMARK 525  M RES CSSEQI     ORIGINAL COORDINATES   SYMMETRY TRANS.    DIST.    
REMARK 525                    X       Y       Z                                 
REMARK 525    HOH S 142    -8.204   1.797  17.262    001      655      3.10     
REMARK 525    HOH S 253    36.648  11.259  -3.421    002      645      3.10     
REMARK 525    HOH S 273    38.955  10.761  -4.023    002      645      4.64     
REMARK 525    HOH S 196    17.442 -22.440 -14.819    002      655      3.29     
REMARK 525    HOH S 228    30.426 -15.827 -14.904    002      655      3.58     
REMARK 525    HOH S 178     9.142 -38.416  39.475    002      556      3.44     
REMARK 525    HOH S 225    12.378 -40.487  46.335    002      556      2.66     
REMARK 525    HOH S 272     2.044 -27.164  68.710    002      556      4.19     
REMARK 525    HOH S 193   -21.795   0.922  64.741    002      546      2.84     
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 HOH A2164   O                                                      
REMARK 620 2 HIS A  59   NE2  96.6                                              
REMARK 620 3 HOH A2026   O   130.9  82.9                                        
REMARK 620 4 CYS A  38   SG  133.0 102.9  94.0                                  
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 HOH B2017   O                                                      
REMARK 620 2 HOH B2019   O   142.0                                              
REMARK 620 N                    1                                               
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  89   SG                                                     
REMARK 620 2 CYS A  92   SG  107.0                                              
REMARK 620 3 CYS A  95   SG  124.4 106.7                                        
REMARK 620 4 CYS A 103   SG  102.0 115.7 101.4                                  
REMARK 620 N                    1     2     3                                   
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 CYS B  92   SG                                                     
REMARK 620 2 CYS B  95   SG  109.3                                              
REMARK 620 3 CYS B  89   SG  108.6 119.2                                        
REMARK 620 4 CYS B 103   SG  115.8 103.8 100.2                                  
REMARK 620 N                    1     2     3                                   
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 HIS B 267   ND1                                                    
REMARK 620 2 HIS A 267   ND1 121.3                                              
REMARK 620 3 GLU B 300   OE1 102.9 119.5                                        
REMARK 620 4 HOH A2165   O    97.5 116.0  94.5                                  
REMARK 620 N                    1     2     3                                   
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 B1347                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1348                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1348                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1349                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4UEJ   RELATED DB: PDB                                   
REMARK 900  CLOSED STATE OF GALACTITOL-1-PHOSPHATE 5-DEHYDROGENASE              
REMARK 900  FROM E. COLI IN COMPLEX WITH GLYCEROL.                              
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.                                   
DBREF  4UEO A    1   346  UNP    P0A9S3   GATD_ECOLI       1    346             
DBREF  4UEO 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  B1347       1                                                       
HET     ZN  B1348       1                                                       
HET     ZN  A1348       1                                                       
HET     ZN  A1349       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    5(ZN 2+)                                                     
FORMUL   3  HOH   *276(H2 O)                                                    
HELIX    1   1 SER A   40  LYS A   47  1                                   8    
HELIX    2   2 CYS A   92  LYS A   97  1                                   6    
HELIX    3   3 PHE A   99  CYS A  103  5                                   5    
HELIX    4   4 PRO A  136  ALA A  141  5                                   6    
HELIX    5   5 PHE A  142  ALA A  156  1                                  15    
HELIX    6   6 GLY A  170  GLY A  184  1                                  15    
HELIX    7   7 SER A  194  PHE A  204  1                                  11    
HELIX    8   8 SER A  216  LEU A  224  1                                   9    
HELIX    9   9 ARG A  225  ARG A  228  5                                   4    
HELIX   10  10 VAL A  239  ALA A  250  1                                  12    
HELIX   11  11 THR A  269  LYS A  279  1                                  11    
HELIX   12  12 GLY A  296  GLU A  308  1                                  13    
HELIX   13  13 LEU A  313  PRO A  315  5                                   3    
HELIX   14  14 SER A  322  ASP A  332  1                                  11    
HELIX   15  15 ASP B   41  ILE B   45  5                                   5    
HELIX   16  16 CYS B   92  LYS B   97  1                                   6    
HELIX   17  17 PHE B   99  CYS B  103  5                                   5    
HELIX   18  18 PRO B  136  ALA B  141  5                                   6    
HELIX   19  19 PHE B  142  ALA B  156  1                                  15    
HELIX   20  20 GLY B  170  LEU B  183  1                                  14    
HELIX   21  21 SER B  194  PHE B  204  1                                  11    
HELIX   22  22 SER B  216  ARG B  225  1                                  10    
HELIX   23  23 GLU B  226  ARG B  228  5                                   3    
HELIX   24  24 VAL B  239  ALA B  250  1                                  12    
HELIX   25  25 THR B  269  LYS B  279  1                                  11    
HELIX   26  26 GLY B  296  GLU B  308  1                                  13    
HELIX   27  27 LEU B  313  PRO B  315  5                                   3    
HELIX   28  28 PHE B  323  GLN B  328  1                                   6    
SHEET    1  AA 2 LYS A   2  ASN A   6  0                                        
SHEET    2  AA 2 VAL A  12  GLU A  16 -1  O  ARG A  13   N  VAL A   5           
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  VAL B   4  0                                        
SHEET    2  BA 2 VAL B  14  GLU B  16 -1  O  ALA B  15   N  SER B   3           
SHEET    1  BB 2 TYR B 120  LYS B 124  0                                        
SHEET    2  BB 2 GLU B  27  LEU B  37 -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  LEU B  37 -1  O  ARG B  29   N  ASP B  66           
SHEET    5  BC 6 LYS B 341  LEU B 344 -1  O  VAL B 342   N  LEU B  37           
SHEET    6  BC 6 ILE B 317  HIS B 319 -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  LEU B  37 -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           
LINK        ZN    ZN A1347                 O   HOH A2164     1555   1555  2.67  
LINK        ZN    ZN A1347                 NE2 HIS A  59     1555   1555  2.30  
LINK        ZN    ZN A1347                 O   HOH A2026     1555   1555  2.14  
LINK        ZN    ZN A1347                 SG  CYS A  38     1555   1555  2.57  
LINK        ZN    ZN A1348                 SG  CYS A  89     1555   1555  2.40  
LINK        ZN    ZN A1348                 SG  CYS A  92     1555   1555  2.33  
LINK        ZN    ZN A1348                 SG  CYS A  95     1555   1555  2.42  
LINK        ZN    ZN A1348                 SG  CYS A 103     1555   1555  2.37  
LINK        ZN    ZN A1349                 OE1 GLU B 300     1555   1655  2.31  
LINK        ZN    ZN A1349                 O   HOH A2165     1555   1555  2.33  
LINK        ZN    ZN A1349                 ND1 HIS A 267     1555   1555  2.31  
LINK        ZN    ZN A1349                 ND1 HIS B 267     1555   1555  2.25  
LINK        ZN    ZN B1347                 O   HOH B2019     1555   1555  2.48  
LINK        ZN    ZN B1347                 O   HOH B2017     1555   1555  2.16  
LINK        ZN    ZN B1348                 SG  CYS B 103     1555   1555  2.39  
LINK        ZN    ZN B1348                 SG  CYS B  89     1555   1555  2.40  
LINK        ZN    ZN B1348                 SG  CYS B  95     1555   1555  2.39  
LINK        ZN    ZN B1348                 SG  CYS B  92     1555   1555  2.34  
CISPEP   1 TYR A   53    PRO A   54          0         0.55                     
CISPEP   2 SER A  292    PRO A  293          0        -0.10                     
CISPEP   3 TRP A  294    PRO A  295          0        -1.17                     
CISPEP   4 TYR B   53    PRO B   54          0        21.09                     
CISPEP   5 SER B  292    PRO B  293          0         1.53                     
CISPEP   6 TRP B  294    PRO B  295          0        -0.38                     
SITE     1 AC1  5 CYS A  38  SER A  40  HIS A  59  HOH A2026                    
SITE     2 AC1  5 HOH A2164                                                     
SITE     1 AC2  5 CYS B  38  SER B  40  HIS B  59  HOH B2017                    
SITE     2 AC2  5 HOH B2019                                                     
SITE     1 AC3  4 CYS B  89  CYS B  92  CYS B  95  CYS B 103                    
SITE     1 AC4  5 CYS A  89  PHE A  90  CYS A  92  CYS A  95                    
SITE     2 AC4  5 CYS A 103                                                     
SITE     1 AC5  4 HIS A 267  HOH A2165  HIS B 267  GLU B 300                    
CRYST1   43.306   76.906  108.651  90.00  95.51  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      0.023091  0.000000  0.002228        0.00000                         
SCALE2      0.000000  0.013003  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009247        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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