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Database: PDB
Entry: 3TY7
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Original site: 3TY7 
HEADER    OXIDOREDUCTASE                          23-SEP-11   3TY7              
TITLE     CRYSTAL STRUCTURE OF ALDEHYDE DEHYDROGENASE FAMILY PROTEIN FROM       
TITLE    2 STAPHYLOCOCCUS AUREUS                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE ALDEHYDE DEHYDROGENASE SAV2122;                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.2.1.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 158878;                                              
SOURCE   4 STRAIN: AUREUS MU50;                                                 
SOURCE   5 GENE: SAV2122;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 MAGIC;                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL       
KEYWDS   2 GENOMICS, MCSG, STRUCTURES OF MTB PROTEINS CONFERRING SUSCEPTIBILITY 
KEYWDS   3 TO KNOWN MTB INHIBITORS, MTBI, ALPHA-BETA SANDWICH, CYTOSOL,         
KEYWDS   4 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.KIM,G.JOACHIMIAK,R.JEDRZEJCZAK,E.RUBIN,T.IOERGER,J.SACCHETTINI,     
AUTHOR   2 A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG),          
AUTHOR   3 STRUCTURES OF MTB PROTEINS CONFERRING SUSCEPTIBILITY TO KNOWN MTB    
AUTHOR   4 INHIBITORS (MTBI)                                                    
REVDAT   1   19-OCT-11 3TY7    0                                                
JRNL        AUTH   Y.KIM,G.JOACHIMIAK,R.JEDRZEJCZAK,E.RUBIN,T.IOERGER,          
JRNL        AUTH 2 J.SACCHETTINI,A.JOACHIMIAK                                   
JRNL        TITL   CRYSTAL STRUCTURE OF ALDEHYDE DEHYDROGENASE FAMILY PROTEIN   
JRNL        TITL 2 FROM STAPHYLOCOCCUS AUREUS                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_851)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.46                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 42206                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2129                            
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 32.4590 -  5.9079    0.99     2679   127  0.1611 0.1794        
REMARK   3     2  5.9079 -  4.6938    1.00     2687   136  0.1588 0.1842        
REMARK   3     3  4.6938 -  4.1018    1.00     2684   150  0.1403 0.1536        
REMARK   3     4  4.1018 -  3.7274    1.00     2659   151  0.1697 0.1816        
REMARK   3     5  3.7274 -  3.4605    1.00     2703   139  0.1857 0.2210        
REMARK   3     6  3.4605 -  3.2567    1.00     2658   158  0.1990 0.2409        
REMARK   3     7  3.2567 -  3.0937    1.00     2673   130  0.2087 0.2454        
REMARK   3     8  3.0937 -  2.9592    1.00     2718   116  0.2177 0.2691        
REMARK   3     9  2.9592 -  2.8453    1.00     2650   136  0.2250 0.2753        
REMARK   3    10  2.8453 -  2.7472    1.00     2720   128  0.2285 0.2572        
REMARK   3    11  2.7472 -  2.6613    1.00     2657   150  0.2336 0.2666        
REMARK   3    12  2.6613 -  2.5853    1.00     2646   161  0.2465 0.2842        
REMARK   3    13  2.5853 -  2.5173    0.99     2630   157  0.2672 0.3124        
REMARK   3    14  2.5173 -  2.4559    0.99     2670   150  0.2756 0.2872        
REMARK   3    15  2.4559 -  2.4000    0.98     2643   140  0.3090 0.3538        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.98                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 59.49                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.740            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.990           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 55.13                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.23250                                             
REMARK   3    B22 (A**2) : -2.23250                                             
REMARK   3    B33 (A**2) : 4.46490                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
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      :  0.003           7196                                  
REMARK   3   ANGLE     :  0.877           9714                                  
REMARK   3   CHIRALITY :  0.067           1080                                  
REMARK   3   PLANARITY :  0.004           1281                                  
REMARK   3   DIHEDRAL  : 14.076           2697                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 0:212)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  53.3568  37.3050  46.0684              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2969 T22:   0.2511                                     
REMARK   3      T33:   0.2686 T12:  -0.0077                                     
REMARK   3      T13:  -0.1239 T23:   0.0182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8084 L22:   2.7103                                     
REMARK   3      L33:   2.1419 L12:  -0.6007                                     
REMARK   3      L13:   0.4948 L23:  -0.5422                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0237 S12:   0.3573 S13:   0.1136                       
REMARK   3      S21:  -0.0620 S22:  -0.0259 S23:   0.1795                       
REMARK   3      S31:  -0.0899 S32:   0.2477 S33:   0.0532                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 213:240)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  48.0986  20.1523  45.8918              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8256 T22:   0.4289                                     
REMARK   3      T33:   0.9709 T12:   0.0798                                     
REMARK   3      T13:  -0.1418 T23:  -0.1318                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7398 L22:   3.5390                                     
REMARK   3      L33:   8.0766 L12:   2.3267                                     
REMARK   3      L13:   1.0337 L23:   0.9499                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0474 S12:   0.5884 S13:  -1.5179                       
REMARK   3      S21:  -0.9940 S22:  -0.0260 S23:   0.1713                       
REMARK   3      S31:   1.3331 S32:  -0.1250 S33:  -0.0472                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 241:415)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  53.2176  28.3558  15.2713              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4075 T22:   0.5341                                     
REMARK   3      T33:   0.3343 T12:   0.0948                                     
REMARK   3      T13:   0.1411 T23:   0.0541                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0673 L22:   2.2651                                     
REMARK   3      L33:   3.9732 L12:   0.3864                                     
REMARK   3      L13:   0.7967 L23:  -0.5585                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1720 S12:   0.1209 S13:  -0.1988                       
REMARK   3      S21:  -0.0168 S22:  -0.0244 S23:  -0.1243                       
REMARK   3      S31:   0.3376 S32:   0.4566 S33:   0.1879                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 416:475)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  32.1192  31.6198  32.9676              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2967 T22:   0.4436                                     
REMARK   3      T33:   0.6345 T12:   0.0525                                     
REMARK   3      T13:   0.0200 T23:   0.0478                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1683 L22:   1.0914                                     
REMARK   3      L33:   5.4597 L12:   0.0975                                     
REMARK   3      L13:  -1.2381 L23:  -0.5332                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0605 S12:   0.2273 S13:   0.3179                       
REMARK   3      S21:   0.0774 S22:  -0.0440 S23:  -0.0012                       
REMARK   3      S31:  -0.2567 S32:  -0.3778 S33:   0.1968                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 0:206)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  20.5774   7.3834  37.6800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2352 T22:   0.2508                                     
REMARK   3      T33:   0.2806 T12:   0.0295                                     
REMARK   3      T13:  -0.0248 T23:  -0.0544                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7734 L22:   4.3358                                     
REMARK   3      L33:   1.6582 L12:   1.1417                                     
REMARK   3      L13:  -0.1260 L23:  -0.8399                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1540 S12:   0.0883 S13:  -0.0628                       
REMARK   3      S21:   0.1252 S22:   0.0597 S23:   0.2684                       
REMARK   3      S31:   0.1345 S32:  -0.2153 S33:  -0.1982                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 207:234)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  37.5408   8.8866  39.4033              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5647 T22:   0.5609                                     
REMARK   3      T33:   0.8127 T12:   0.0186                                     
REMARK   3      T13:  -0.2183 T23:  -0.1884                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2620 L22:   5.4146                                     
REMARK   3      L33:   7.8415 L12:   1.1670                                     
REMARK   3      L13:  -1.8297 L23:  -0.1597                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0698 S12:  -0.9912 S13:   0.4865                       
REMARK   3      S21:   1.4372 S22:  -0.0843 S23:  -1.5087                       
REMARK   3      S31:  -0.5006 S32:   0.9703 S33:   0.0151                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 235:276)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  27.4530  16.0699  60.8684              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5013 T22:   0.3844                                     
REMARK   3      T33:   0.6184 T12:  -0.0322                                     
REMARK   3      T13:   0.0852 T23:  -0.0845                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4890 L22:   2.3561                                     
REMARK   3      L33:   1.9550 L12:   0.7437                                     
REMARK   3      L13:   1.6073 L23:   0.0780                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0632 S12:  -0.1062 S13:   0.3962                       
REMARK   3      S21:   0.2678 S22:   0.3098 S23:   0.5592                       
REMARK   3      S31:   0.2600 S32:  -0.2098 S33:  -0.1082                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 277:415)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  28.4287   8.3771  69.7628              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6809 T22:   0.4365                                     
REMARK   3      T33:   0.4003 T12:  -0.1252                                     
REMARK   3      T13:   0.1015 T23:   0.0559                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7287 L22:   3.6345                                     
REMARK   3      L33:   3.0326 L12:  -0.2173                                     
REMARK   3      L13:   1.9209 L23:  -0.1114                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3653 S12:  -0.3229 S13:   0.1448                       
REMARK   3      S21:   0.5614 S22:  -0.1999 S23:  -0.1141                       
REMARK   3      S31:   0.2378 S32:  -0.2381 S33:  -0.1839                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 416:475)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  27.5598  29.0760  48.9773              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3724 T22:   0.2303                                     
REMARK   3      T33:   0.6788 T12:   0.0429                                     
REMARK   3      T13:   0.1183 T23:  -0.0269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0959 L22:   0.8954                                     
REMARK   3      L33:   4.7005 L12:  -0.1764                                     
REMARK   3      L13:  -0.0620 L23:  -1.3891                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0591 S12:   0.0386 S13:   0.1081                       
REMARK   3      S21:   0.2267 S22:   0.0678 S23:   0.1022                       
REMARK   3      S31:  -0.3807 S32:  -0.3218 S33:   0.0769                       
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 3TY7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB068068.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-AUG-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97911                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42456                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.58200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: HKL3000, SHELXS,MLPHARE,RESOLVE,SOLVE                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE, 0.1 M  TRIS    
REMARK 280  PH 8.5, 30 % PEG400, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE     
REMARK 280  289K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       86.72400            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       50.07012            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       32.18967            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       86.72400            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       50.07012            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       32.18967            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       86.72400            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       50.07012            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       32.18967            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      100.14025            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       64.37933            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000      100.14025            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       64.37933            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000      100.14025            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       64.37933            
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 300 REMARK: A DIMER IN THE ASYMMETRIC UNIT                               
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: 4740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     LYS A   230                                                      
REMARK 465     ILE A   231                                                      
REMARK 465     ARG A   438                                                      
REMARK 465     LYS A   439                                                      
REMARK 465     PRO A   440                                                      
REMARK 465     ASP A   441                                                      
REMARK 465     LEU A   442                                                      
REMARK 465     PRO A   443                                                      
REMARK 465     PHE A   444                                                      
REMARK 465     GLY A   445                                                      
REMARK 465     GLY A   446                                                      
REMARK 465     TYR A   447                                                      
REMARK 465     LYS A   448                                                      
REMARK 465     GLN A   449                                                      
REMARK 465     SER A   450                                                      
REMARK 465     GLY A   451                                                      
REMARK 465     LEU A   452                                                      
REMARK 465     GLY A   453                                                      
REMARK 465     ARG A   454                                                      
REMARK 465     GLU A   455                                                      
REMARK 465     TRP A   456                                                      
REMARK 465     GLY A   457                                                      
REMARK 465     ASP A   458                                                      
REMARK 465     TYR A   459                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     ARG B   438                                                      
REMARK 465     LYS B   439                                                      
REMARK 465     PRO B   440                                                      
REMARK 465     ASP B   441                                                      
REMARK 465     LEU B   442                                                      
REMARK 465     PRO B   443                                                      
REMARK 465     PHE B   444                                                      
REMARK 465     GLY B   445                                                      
REMARK 465     GLY B   446                                                      
REMARK 465     TYR B   447                                                      
REMARK 465     LYS B   448                                                      
REMARK 465     GLN B   449                                                      
REMARK 465     SER B   450                                                      
REMARK 465     GLY B   451                                                      
REMARK 465     LEU B   452                                                      
REMARK 465     GLY B   453                                                      
REMARK 465     ARG B   454                                                      
REMARK 465     GLU B   455                                                      
REMARK 465     TRP B   456                                                      
REMARK 465     GLY B   457                                                      
REMARK 465     ASP B   458                                                      
REMARK 465     TYR B   459                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  30       -5.61     64.91                                   
REMARK 500    VAL A 102      -65.38   -104.74                                   
REMARK 500    VAL A 206      -60.05   -120.49                                   
REMARK 500    LYS A 414      -64.90    -97.79                                   
REMARK 500    GLU B  30       -5.24     66.25                                   
REMARK 500    ASN B 151      -71.74    -84.34                                   
REMARK 500    PHE B 345      -63.13   -106.89                                   
REMARK 500    ASN B 391      -62.69   -102.86                                   
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                              MG B 484  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE B  25   O                                                      
REMARK 620 2 GLU B 174   O   130.0                                              
REMARK 620 3 HOH B 540   O    99.5 119.0                                        
REMARK 620 4 GLU B  91   O    89.3  96.5 120.2                                  
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 GOL A 481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 484                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 484                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 485                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 486                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: APC105740   RELATED DB: TARGETDB                         
DBREF  3TY7 A    1   475  UNP    Q99SD6   ALD1_STAAM       1    475             
DBREF  3TY7 B    1   475  UNP    Q99SD6   ALD1_STAAM       1    475             
SEQADV 3TY7 SER A   -2  UNP  Q99SD6              EXPRESSION TAG                 
SEQADV 3TY7 ASN A   -1  UNP  Q99SD6              EXPRESSION TAG                 
SEQADV 3TY7 ALA A    0  UNP  Q99SD6              EXPRESSION TAG                 
SEQADV 3TY7 SER B   -2  UNP  Q99SD6              EXPRESSION TAG                 
SEQADV 3TY7 ASN B   -1  UNP  Q99SD6              EXPRESSION TAG                 
SEQADV 3TY7 ALA B    0  UNP  Q99SD6              EXPRESSION TAG                 
SEQRES   1 A  478  SER ASN ALA MSE ARG ASP TYR THR LYS GLN TYR ILE ASN          
SEQRES   2 A  478  GLY GLU TRP VAL GLU SER ASN SER ASN GLU THR ILE GLU          
SEQRES   3 A  478  VAL ILE ASN PRO ALA THR GLU GLU VAL ILE GLY LYS VAL          
SEQRES   4 A  478  ALA LYS GLY ASN LYS ALA ASP VAL ASP LYS ALA VAL GLU          
SEQRES   5 A  478  ALA ALA ASP ASP VAL TYR LEU GLU PHE ARG HIS THR SER          
SEQRES   6 A  478  VAL LYS GLU ARG GLN ALA LEU LEU ASP LYS ILE VAL LYS          
SEQRES   7 A  478  GLU TYR GLU ASN ARG LYS ASP ASP ILE VAL GLN ALA ILE          
SEQRES   8 A  478  THR ASP GLU LEU GLY ALA PRO LEU SER LEU SER GLU ARG          
SEQRES   9 A  478  VAL HIS TYR GLN MSE GLY LEU ASN HIS PHE VAL ALA ALA          
SEQRES  10 A  478  ARG ASP ALA LEU ASP ASN TYR GLU PHE GLU GLU ARG ARG          
SEQRES  11 A  478  GLY ASP ASP LEU VAL VAL LYS GLU ALA ILE GLY VAL SER          
SEQRES  12 A  478  GLY LEU ILE THR PRO TRP ASN PHE PRO THR ASN GLN THR          
SEQRES  13 A  478  SER LEU LYS LEU ALA ALA ALA PHE ALA ALA GLY SER PRO          
SEQRES  14 A  478  VAL VAL LEU LYS PRO SER GLU GLU THR PRO PHE ALA ALA          
SEQRES  15 A  478  VAL ILE LEU ALA GLU ILE PHE ASP LYS VAL GLY VAL PRO          
SEQRES  16 A  478  LYS GLY VAL PHE ASN LEU VAL ASN GLY ASP GLY ALA GLY          
SEQRES  17 A  478  VAL GLY ASN PRO LEU SER GLU HIS PRO LYS VAL ARG MSE          
SEQRES  18 A  478  MSE SER PHE THR GLY SER GLY PRO THR GLY SER LYS ILE          
SEQRES  19 A  478  MSE GLU LYS ALA ALA LYS ASP PHE LYS LYS VAL SER LEU          
SEQRES  20 A  478  GLU LEU GLY GLY LYS SER PRO TYR ILE VAL LEU ASP ASP          
SEQRES  21 A  478  VAL ASP ILE LYS GLU ALA ALA LYS ALA THR THR GLY LYS          
SEQRES  22 A  478  VAL VAL ASN ASN THR GLY GLN VAL CYS THR ALA GLY THR          
SEQRES  23 A  478  ARG VAL LEU VAL PRO ASN LYS ILE LYS ASP ALA PHE LEU          
SEQRES  24 A  478  ALA GLU LEU LYS GLU GLN PHE SER GLN VAL ARG VAL GLY          
SEQRES  25 A  478  ASN PRO ARG GLU ASP GLY THR GLN VAL GLY PRO ILE ILE          
SEQRES  26 A  478  SER LYS LYS GLN PHE ASP GLN VAL GLN ASN TYR ILE ASN          
SEQRES  27 A  478  LYS GLY ILE GLU GLU GLY ALA GLU LEU PHE TYR GLY GLY          
SEQRES  28 A  478  PRO GLY LYS PRO GLU GLY LEU GLU LYS GLY TYR PHE ALA          
SEQRES  29 A  478  ARG PRO THR ILE PHE ILE ASN VAL ASP ASN GLN MSE THR          
SEQRES  30 A  478  ILE ALA GLN GLU GLU ILE PHE GLY PRO VAL MSE SER VAL          
SEQRES  31 A  478  ILE THR TYR ASN ASP LEU ASP GLU ALA ILE GLN ILE ALA          
SEQRES  32 A  478  ASN ASP THR LYS TYR GLY LEU ALA GLY TYR VAL ILE GLY          
SEQRES  33 A  478  LYS ASP LYS GLU THR LEU HIS LYS VAL ALA ARG SER ILE          
SEQRES  34 A  478  GLU ALA GLY THR VAL GLU ILE ASN GLU ALA GLY ARG LYS          
SEQRES  35 A  478  PRO ASP LEU PRO PHE GLY GLY TYR LYS GLN SER GLY LEU          
SEQRES  36 A  478  GLY ARG GLU TRP GLY ASP TYR GLY ILE GLU GLU PHE LEU          
SEQRES  37 A  478  GLU VAL LYS SER ILE ALA GLY TYR PHE LYS                      
SEQRES   1 B  478  SER ASN ALA MSE ARG ASP TYR THR LYS GLN TYR ILE ASN          
SEQRES   2 B  478  GLY GLU TRP VAL GLU SER ASN SER ASN GLU THR ILE GLU          
SEQRES   3 B  478  VAL ILE ASN PRO ALA THR GLU GLU VAL ILE GLY LYS VAL          
SEQRES   4 B  478  ALA LYS GLY ASN LYS ALA ASP VAL ASP LYS ALA VAL GLU          
SEQRES   5 B  478  ALA ALA ASP ASP VAL TYR LEU GLU PHE ARG HIS THR SER          
SEQRES   6 B  478  VAL LYS GLU ARG GLN ALA LEU LEU ASP LYS ILE VAL LYS          
SEQRES   7 B  478  GLU TYR GLU ASN ARG LYS ASP ASP ILE VAL GLN ALA ILE          
SEQRES   8 B  478  THR ASP GLU LEU GLY ALA PRO LEU SER LEU SER GLU ARG          
SEQRES   9 B  478  VAL HIS TYR GLN MSE GLY LEU ASN HIS PHE VAL ALA ALA          
SEQRES  10 B  478  ARG ASP ALA LEU ASP ASN TYR GLU PHE GLU GLU ARG ARG          
SEQRES  11 B  478  GLY ASP ASP LEU VAL VAL LYS GLU ALA ILE GLY VAL SER          
SEQRES  12 B  478  GLY LEU ILE THR PRO TRP ASN PHE PRO THR ASN GLN THR          
SEQRES  13 B  478  SER LEU LYS LEU ALA ALA ALA PHE ALA ALA GLY SER PRO          
SEQRES  14 B  478  VAL VAL LEU LYS PRO SER GLU GLU THR PRO PHE ALA ALA          
SEQRES  15 B  478  VAL ILE LEU ALA GLU ILE PHE ASP LYS VAL GLY VAL PRO          
SEQRES  16 B  478  LYS GLY VAL PHE ASN LEU VAL ASN GLY ASP GLY ALA GLY          
SEQRES  17 B  478  VAL GLY ASN PRO LEU SER GLU HIS PRO LYS VAL ARG MSE          
SEQRES  18 B  478  MSE SER PHE THR GLY SER GLY PRO THR GLY SER LYS ILE          
SEQRES  19 B  478  MSE GLU LYS ALA ALA LYS ASP PHE LYS LYS VAL SER LEU          
SEQRES  20 B  478  GLU LEU GLY GLY LYS SER PRO TYR ILE VAL LEU ASP ASP          
SEQRES  21 B  478  VAL ASP ILE LYS GLU ALA ALA LYS ALA THR THR GLY LYS          
SEQRES  22 B  478  VAL VAL ASN ASN THR GLY GLN VAL CYS THR ALA GLY THR          
SEQRES  23 B  478  ARG VAL LEU VAL PRO ASN LYS ILE LYS ASP ALA PHE LEU          
SEQRES  24 B  478  ALA GLU LEU LYS GLU GLN PHE SER GLN VAL ARG VAL GLY          
SEQRES  25 B  478  ASN PRO ARG GLU ASP GLY THR GLN VAL GLY PRO ILE ILE          
SEQRES  26 B  478  SER LYS LYS GLN PHE ASP GLN VAL GLN ASN TYR ILE ASN          
SEQRES  27 B  478  LYS GLY ILE GLU GLU GLY ALA GLU LEU PHE TYR GLY GLY          
SEQRES  28 B  478  PRO GLY LYS PRO GLU GLY LEU GLU LYS GLY TYR PHE ALA          
SEQRES  29 B  478  ARG PRO THR ILE PHE ILE ASN VAL ASP ASN GLN MSE THR          
SEQRES  30 B  478  ILE ALA GLN GLU GLU ILE PHE GLY PRO VAL MSE SER VAL          
SEQRES  31 B  478  ILE THR TYR ASN ASP LEU ASP GLU ALA ILE GLN ILE ALA          
SEQRES  32 B  478  ASN ASP THR LYS TYR GLY LEU ALA GLY TYR VAL ILE GLY          
SEQRES  33 B  478  LYS ASP LYS GLU THR LEU HIS LYS VAL ALA ARG SER ILE          
SEQRES  34 B  478  GLU ALA GLY THR VAL GLU ILE ASN GLU ALA GLY ARG LYS          
SEQRES  35 B  478  PRO ASP LEU PRO PHE GLY GLY TYR LYS GLN SER GLY LEU          
SEQRES  36 B  478  GLY ARG GLU TRP GLY ASP TYR GLY ILE GLU GLU PHE LEU          
SEQRES  37 B  478  GLU VAL LYS SER ILE ALA GLY TYR PHE LYS                      
MODRES 3TY7 MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 3TY7 MSE A  106  MET  SELENOMETHIONINE                                   
MODRES 3TY7 MSE A  218  MET  SELENOMETHIONINE                                   
MODRES 3TY7 MSE A  219  MET  SELENOMETHIONINE                                   
MODRES 3TY7 MSE A  232  MET  SELENOMETHIONINE                                   
MODRES 3TY7 MSE A  373  MET  SELENOMETHIONINE                                   
MODRES 3TY7 MSE A  385  MET  SELENOMETHIONINE                                   
MODRES 3TY7 MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 3TY7 MSE B  106  MET  SELENOMETHIONINE                                   
MODRES 3TY7 MSE B  218  MET  SELENOMETHIONINE                                   
MODRES 3TY7 MSE B  219  MET  SELENOMETHIONINE                                   
MODRES 3TY7 MSE B  232  MET  SELENOMETHIONINE                                   
MODRES 3TY7 MSE B  373  MET  SELENOMETHIONINE                                   
MODRES 3TY7 MSE B  385  MET  SELENOMETHIONINE                                   
HET    MSE  A   1      16                                                       
HET    MSE  A 106       8                                                       
HET    MSE  A 218       8                                                       
HET    MSE  A 219       8                                                       
HET    MSE  A 232       8                                                       
HET    MSE  A 373       8                                                       
HET    MSE  A 385       8                                                       
HET    MSE  B   1      16                                                       
HET    MSE  B 106       8                                                       
HET    MSE  B 218       8                                                       
HET    MSE  B 219       8                                                       
HET    MSE  B 232       8                                                       
HET    MSE  B 373       8                                                       
HET    MSE  B 385       8                                                       
HET    GOL  A 481       6                                                       
HET    GOL  A 482       6                                                       
HET    GOL  A 483       6                                                       
HET    PEG  A 484       7                                                       
HET    GOL  B 481       6                                                       
HET    GOL  B 482       6                                                       
HET    GOL  B 483       6                                                       
HET     MG  B 484       1                                                       
HET    GOL  B 485       6                                                       
HET    PEG  B 486       7                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     GOL GLYCEROL                                                         
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    14(C5 H11 N O2 SE)                                           
FORMUL   3  GOL    7(C3 H8 O3)                                                  
FORMUL   6  PEG    2(C4 H10 O3)                                                 
FORMUL  10   MG    MG 2+                                                        
FORMUL  13  HOH   *163(H2 O)                                                    
HELIX    1   1 ASN A   40  HIS A   60  1                                  21    
HELIX    2   2 SER A   62  ARG A   80  1                                  19    
HELIX    3   3 ARG A   80  GLY A   93  1                                  14    
HELIX    4   4 PRO A   95  VAL A  102  1                                   8    
HELIX    5   5 VAL A  102  TYR A  121  1                                  20    
HELIX    6   6 THR A  150  GLY A  164  1                                  15    
HELIX    7   7 PRO A  176  GLY A  190  1                                  15    
HELIX    8   8 VAL A  206  HIS A  213  1                                   8    
HELIX    9   9 SER A  224  SER A  229  1                                   6    
HELIX   10  10 ASP A  259  ASN A  273  1                                  15    
HELIX   11  11 ASN A  274  GLN A  277  5                                   4    
HELIX   12  12 ILE A  291  GLN A  305  1                                  15    
HELIX   13  13 SER A  323  GLY A  341  1                                  19    
HELIX   14  14 MSE A  373  GLU A  378  1                                   6    
HELIX   15  15 ASP A  392  ASN A  401  1                                  10    
HELIX   16  16 ASP A  415  ILE A  426  1                                  12    
HELIX   17  17 ILE A  461  GLU A  463  5                                   3    
HELIX   18  18 ASN B   40  HIS B   60  1                                  21    
HELIX   19  19 SER B   62  ARG B   80  1                                  19    
HELIX   20  20 ARG B   80  GLY B   93  1                                  14    
HELIX   21  21 PRO B   95  VAL B  102  1                                   8    
HELIX   22  22 VAL B  102  LEU B  118  1                                  17    
HELIX   23  23 THR B  150  GLY B  164  1                                  15    
HELIX   24  24 PRO B  176  VAL B  189  1                                  14    
HELIX   25  25 VAL B  206  HIS B  213  1                                   8    
HELIX   26  26 SER B  224  ALA B  235  1                                  12    
HELIX   27  27 ASP B  259  ASN B  273  1                                  15    
HELIX   28  28 ASN B  274  GLN B  277  5                                   4    
HELIX   29  29 ILE B  291  GLN B  305  1                                  15    
HELIX   30  30 SER B  323  GLY B  341  1                                  19    
HELIX   31  31 MSE B  373  GLU B  378  1                                   6    
HELIX   32  32 ASP B  392  ASP B  402  1                                  11    
HELIX   33  33 ASP B  415  ILE B  426  1                                  12    
HELIX   34  34 GLY B  460  GLU B  463  5                                   4    
SHEET    1   A 3 ARG A   2  ASP A   3  0                                        
SHEET    2   A 3 VAL A  32  ALA A  37  1  O  LYS A  35   N  ARG A   2           
SHEET    3   A 3 THR A  21  ILE A  25 -1  N  ILE A  22   O  VAL A  36           
SHEET    1   B 2 LYS A   6  ILE A   9  0                                        
SHEET    2   B 2 GLU A  12  GLU A  15 -1  O  VAL A  14   N  GLN A   7           
SHEET    1   C10 GLU A 124  ARG A 127  0                                        
SHEET    2   C10 ASP A 130  ALA A 136 -1  O  ASP A 130   N  ARG A 127           
SHEET    3   C10 LEU A 465  ALA A 471 -1  O  GLU A 466   N  GLU A 135           
SHEET    4   C10 THR B 430  ILE B 433  1  O  VAL B 431   N  ALA A 471           
SHEET    5   C10 ALA B 408  ILE B 412  1  N  VAL B 411   O  GLU B 432           
SHEET    6   C10 PRO B 251  VAL B 254  1  N  ILE B 253   O  TYR B 410           
SHEET    7   C10 ARG B 284  PRO B 288  1  O  ARG B 284   N  TYR B 252           
SHEET    8   C10 VAL B 384  TYR B 390  1  O  SER B 386   N  VAL B 285           
SHEET    9   C10 THR B 364  ILE B 367  1  N  PHE B 366   O  VAL B 387           
SHEET   10   C10 GLU B 343  TYR B 346 -1  N  GLU B 343   O  ILE B 367           
SHEET    1   D 5 PHE A 196  LEU A 198  0                                        
SHEET    2   D 5 VAL A 167  LYS A 170  1  N  LEU A 169   O  ASN A 197           
SHEET    3   D 5 SER A 140  ILE A 143  1  N  LEU A 142   O  LYS A 170           
SHEET    4   D 5 MSE A 218  PHE A 221  1  O  MSE A 218   N  GLY A 141           
SHEET    5   D 5 LYS A 241  SER A 243  1  O  LYS A 241   N  MSE A 219           
SHEET    1   E10 GLU A 343  TYR A 346  0                                        
SHEET    2   E10 THR A 364  ILE A 367 -1  O  ILE A 365   N  PHE A 345           
SHEET    3   E10 VAL A 384  TYR A 390  1  O  VAL A 387   N  PHE A 366           
SHEET    4   E10 ARG A 284  PRO A 288  1  N  VAL A 285   O  ILE A 388           
SHEET    5   E10 PRO A 251  VAL A 254  1  N  TYR A 252   O  ARG A 284           
SHEET    6   E10 ALA A 408  ILE A 412  1  O  TYR A 410   N  ILE A 253           
SHEET    7   E10 THR A 430  ILE A 433  1  O  GLU A 432   N  VAL A 411           
SHEET    8   E10 LEU B 465  ALA B 471  1  O  ALA B 471   N  VAL A 431           
SHEET    9   E10 ASP B 130  ALA B 136 -1  N  LEU B 131   O  ILE B 470           
SHEET   10   E10 GLU B 124  ARG B 127 -1  N  ARG B 127   O  ASP B 130           
SHEET    1   F 3 ARG B   2  TYR B   4  0                                        
SHEET    2   F 3 VAL B  32  ALA B  37  1  O  LYS B  35   N  TYR B   4           
SHEET    3   F 3 THR B  21  ILE B  25 -1  N  ILE B  22   O  VAL B  36           
SHEET    1   G 2 LYS B   6  ILE B   9  0                                        
SHEET    2   G 2 GLU B  12  GLU B  15 -1  O  VAL B  14   N  GLN B   7           
SHEET    1   H 5 PHE B 196  LEU B 198  0                                        
SHEET    2   H 5 VAL B 167  LYS B 170  1  N  LEU B 169   O  ASN B 197           
SHEET    3   H 5 SER B 140  ILE B 143  1  N  LEU B 142   O  LYS B 170           
SHEET    4   H 5 MSE B 218  THR B 222  1  O  MSE B 218   N  GLY B 141           
SHEET    5   H 5 LYS B 241  GLU B 245  1  O  LYS B 241   N  MSE B 219           
LINK         C   ALA A   0                 N  AMSE A   1     1555   1555  1.33  
LINK         C   ALA A   0                 N  BMSE A   1     1555   1555  1.33  
LINK         C  AMSE A   1                 N  AARG A   2     1555   1555  1.33  
LINK         C  BMSE A   1                 N  BARG A   2     1555   1555  1.33  
LINK         C   GLN A 105                 N   MSE A 106     1555   1555  1.33  
LINK         C   MSE A 106                 N   GLY A 107     1555   1555  1.33  
LINK         C   ARG A 217                 N   MSE A 218     1555   1555  1.33  
LINK         C   MSE A 218                 N   MSE A 219     1555   1555  1.33  
LINK         C   MSE A 219                 N   SER A 220     1555   1555  1.33  
LINK         C   MSE A 232                 N   GLU A 233     1555   1555  1.33  
LINK         C   GLN A 372                 N   MSE A 373     1555   1555  1.33  
LINK         C   MSE A 373                 N   THR A 374     1555   1555  1.33  
LINK         C   VAL A 384                 N   MSE A 385     1555   1555  1.33  
LINK         C   MSE A 385                 N   SER A 386     1555   1555  1.33  
LINK         C   ALA B   0                 N  AMSE B   1     1555   1555  1.33  
LINK         C   ALA B   0                 N  BMSE B   1     1555   1555  1.33  
LINK         C  AMSE B   1                 N   ARG B   2     1555   1555  1.33  
LINK         C  BMSE B   1                 N   ARG B   2     1555   1555  1.33  
LINK         C   GLN B 105                 N   MSE B 106     1555   1555  1.33  
LINK         C   MSE B 106                 N   GLY B 107     1555   1555  1.33  
LINK         C   ARG B 217                 N   MSE B 218     1555   1555  1.33  
LINK         C   MSE B 218                 N   MSE B 219     1555   1555  1.33  
LINK         C   MSE B 219                 N   SER B 220     1555   1555  1.33  
LINK         C   ILE B 231                 N   MSE B 232     1555   1555  1.33  
LINK         C   MSE B 232                 N   GLU B 233     1555   1555  1.33  
LINK         C   GLN B 372                 N   MSE B 373     1555   1555  1.33  
LINK         C   MSE B 373                 N   THR B 374     1555   1555  1.33  
LINK         C   VAL B 384                 N   MSE B 385     1555   1555  1.33  
LINK         C   MSE B 385                 N   SER B 386     1555   1555  1.33  
LINK         O   ILE B  25                MG    MG B 484     1555   1555  2.76  
LINK         O   GLU B 174                MG    MG B 484     1555   1555  2.78  
LINK        MG    MG B 484                 O   HOH B 540     1555   1555  2.85  
LINK         O   GLU B  91                MG    MG B 484     1555   1555  2.98  
SITE     1 AC1  5 MSE A 232  LYS A 241  VAL A 242  MSE B 232                    
SITE     2 AC1  5 VAL B 242                                                     
SITE     1 AC2  5 ASP A   3  THR A   5  LYS A   6  GLU A  15                    
SITE     2 AC2  5 GLU B  12                                                     
SITE     1 AC3  2 TRP A  13  GLU A 184                                          
SITE     1 AC4  6 LYS A  41  ALA A  42  ASP A  45  ASN B  17                    
SITE     2 AC4  6 PEG B 486  HOH B 499                                          
SITE     1 AC5  2 GLU B  12  ASP B 187                                          
SITE     1 AC6  4 GLU A  12  ASP B   3  THR B   5  GLU B  15                    
SITE     1 AC7  4 LYS B   6  TRP B  13  VAL B 180  GLU B 184                    
SITE     1 AC8  4 ILE B  25  GLU B  91  GLU B 174  HOH B 540                    
SITE     1 AC9  2 ASN B  79  ASP B  83                                          
SITE     1 BC1  6 PEG A 484  HOH A 490  ASN B  40  LYS B  41                    
SITE     2 BC1  6 ALA B  42  ASP B  45                                          
CRYST1  173.448  173.448   96.569  90.00  90.00 120.00 H 3          18          
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      0.005765  0.003329  0.000000        0.00000                         
SCALE2      0.000000  0.006657  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010355        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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