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LongText Report for: 2WUD-pdb

Name Class
2WUD-pdb
HEADER    HYDROLASE                               02-OCT-09   2WUD              
TITLE     CRYSTAL STRUCTURE OF S114A MUTANT OF HSAD FROM                        
TITLE    2 MYCOBACTERIUM TUBERCULOSIS                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOATE                  
COMPND   3  HYDROLASE BPHD;                                                     
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: HSAD, 2-HYDROXY-6-PHENYLHEXA-2\,4-DIENOIC ACID              
COMPND   6  HYDROLASE;                                                          
COMPND   7 EC: 3.7.1.8;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 83332;                                               
SOURCE   4 STRAIN: H37RV;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 668369;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;                                  
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PT7-7                                     
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.A.LACK,K.C.YAM,E.D.LOWE,G.P.HORSMAN,R.OWEN,E.SIM,                   
AUTHOR   2 L.D.ELTIS                                                            
REVDAT   2   10-NOV-09 2WUD    1       JRNL   REMARK                            
REVDAT   1   20-OCT-09 2WUD    0                                                
JRNL        AUTH   N.A.LACK,K.C.YAM,E.D.LOWE,G.P.HORSMAN,R.OWEN,E.SIM,          
JRNL        AUTH 2 L.D.ELTIS                                                    
JRNL        TITL   CHARACTERIZATION OF A C-C HYDROLASE FROM                     
JRNL        TITL 2 MYCOBACTERIUM TUBERCULOSIS INVOLVED IN CHOLESTEROL           
JRNL        TITL 3 METABOLISM                                                   
JRNL        REF    J.BIOL.CHEM.                               2009              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   19875455                                                     
JRNL        DOI    10.1074/JBC.M109.058081                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.1                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.8                           
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2                              
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 35439                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) :  5.0                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1779                            
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 49.7929 -  4.9363    0.97     2663   133  0.1776 0.1930        
REMARK   3     2  4.9363 -  3.9186    1.00     2659   112  0.1408 0.1440        
REMARK   3     3  3.9186 -  3.4234    1.00     2616   136  0.1572 0.1929        
REMARK   3     4  3.4234 -  3.1105    1.00     2590   147  0.1758 0.2349        
REMARK   3     5  3.1105 -  2.8875    1.00     2574   159  0.1808 0.2658        
REMARK   3     6  2.8875 -  2.7173    0.99     2569   135  0.2064 0.2288        
REMARK   3     7  2.7173 -  2.5812    0.99     2582   142  0.2118 0.2529        
REMARK   3     8  2.5812 -  2.4689    1.00     2568   140  0.2065 0.2841        
REMARK   3     9  2.4689 -  2.3738    1.00     2576   133  0.2127 0.2658        
REMARK   3    10  2.3738 -  2.2919    1.00     2580   141  0.2184 0.2846        
REMARK   3    11  2.2919 -  2.2203    1.00     2573   137  0.2296 0.2909        
REMARK   3    12  2.2203 -  2.1568    1.00     2568   138  0.2346 0.2719        
REMARK   3    13  2.1568 -  2.1000    0.99     2542   126  0.2358 0.2936        
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              : 0.347                                         
REMARK   3   B_SOL              : 44.943                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.30             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.41            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.55                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.86                          
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           NULL                                  
REMARK   3   ANGLE     :  0.746           NULL                                  
REMARK   3   CHIRALITY :  0.066           NULL                                  
REMARK   3   PLANARITY :  0.003           NULL                                  
REMARK   3   DIHEDRAL  : 10.285           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 7:36)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.9639  -7.4300  17.2730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0808 T22:   0.1583                                     
REMARK   3      T33:   0.0980 T12:  -0.0589                                     
REMARK   3      T13:   0.0037 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9263 L22:   1.6073                                     
REMARK   3      L33:   1.1858 L12:   0.2766                                     
REMARK   3      L13:  -0.4568 L23:   0.1103                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1008 S22:   0.2160 S33:  -0.0693                       
REMARK   3      S12:   0.3360 S13:   0.0994 S21:  -0.1915                       
REMARK   3      S23:  -0.3042 S31:  -0.1946 S32:   0.0388                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 37:84)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -10.8419 -14.9273  22.1954              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0930 T22:   0.0964                                     
REMARK   3      T33:   0.1026 T12:  -0.0363                                     
REMARK   3      T13:   0.0055 T23:   0.0153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0499 L22:   1.0539                                     
REMARK   3      L33:   0.1931 L12:   0.6237                                     
REMARK   3      L13:  -0.3586 L23:  -0.3350                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0412 S22:  -0.0155 S33:   0.0383                       
REMARK   3      S12:  -0.0954 S13:  -0.0747 S21:  -0.1307                       
REMARK   3      S23:  -0.2203 S31:   0.0837 S32:  -0.0508                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 85:156)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -18.6005 -11.5292  31.8675              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0905 T22:   0.0727                                     
REMARK   3      T33:   0.0908 T12:  -0.0290                                     
REMARK   3      T13:  -0.0096 T23:  -0.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7669 L22:   0.2461                                     
REMARK   3      L33:   0.8284 L12:  -0.0857                                     
REMARK   3      L13:  -0.1578 L23:  -0.2568                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0402 S22:  -0.0054 S33:   0.0302                       
REMARK   3      S12:   0.1177 S13:   0.0430 S21:  -0.0364                       
REMARK   3      S23:  -0.0452 S31:  -0.0008 S32:   0.0317                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 157:205)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   0.5303 -23.9953  33.9934              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0823 T22:   0.1699                                     
REMARK   3      T33:   0.1613 T12:  -0.0203                                     
REMARK   3      T13:   0.0154 T23:   0.0252                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3740 L22:   0.7834                                     
REMARK   3      L33:   0.1971 L12:  -0.4941                                     
REMARK   3      L13:  -0.0836 L23:   0.0627                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0224 S22:   0.0130 S33:   0.0129                       
REMARK   3      S12:   0.0593 S13:  -0.0543 S21:   0.0212                       
REMARK   3      S23:  -0.2452 S31:  -0.0424 S32:   0.1795                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 206:213)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.1638  -8.0560  42.2106              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1369 T22:   0.2515                                     
REMARK   3      T33:   0.1554 T12:  -0.0361                                     
REMARK   3      T13:  -0.0745 T23:   0.0889                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4174 L22:   0.0733                                     
REMARK   3      L33:   5.6544 L12:   1.2881                                     
REMARK   3      L13:  -6.0632 L23:  -1.3689                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2929 S22:  -0.4827 S33:   0.2354                       
REMARK   3      S12:  -0.8639 S13:  -0.5219 S21:   0.0665                       
REMARK   3      S23:  -0.0561 S31:  -0.3362 S32:   0.7804                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 214:230)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -24.4819  -9.0986  40.8924              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1319 T22:   0.1232                                     
REMARK   3      T33:   0.0700 T12:  -0.0373                                     
REMARK   3      T13:  -0.0064 T23:   0.0301                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8272 L22:  -0.0958                                     
REMARK   3      L33:   1.8024 L12:   0.1924                                     
REMARK   3      L13:   0.4337 L23:   0.9320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1769 S22:   0.1102 S33:   0.0541                       
REMARK   3      S12:   0.2376 S13:   0.1284 S21:  -0.1215                       
REMARK   3      S23:   0.0271 S31:  -0.2975 S32:   0.3702                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 231:288)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -22.2256 -25.8258  29.8621              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0693 T22:   0.0797                                     
REMARK   3      T33:   0.0447 T12:  -0.0234                                     
REMARK   3      T13:   0.0065 T23:  -0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0626 L22:   0.8472                                     
REMARK   3      L33:   0.5343 L12:   0.1955                                     
REMARK   3      L13:   0.2296 L23:  -0.3635                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0878 S22:   0.0540 S33:   0.0332                       
REMARK   3      S12:   0.0492 S13:  -0.0209 S21:  -0.0837                       
REMARK   3      S23:  -0.0552 S31:   0.0222 S32:   0.0167                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 7:37)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  22.7854 -41.5917  28.4007              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0796 T22:   0.2170                                     
REMARK   3      T33:   0.1786 T12:   0.0047                                     
REMARK   3      T13:  -0.0834 T23:  -0.1259                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2370 L22:   1.5032                                     
REMARK   3      L33:   2.7800 L12:   0.0273                                     
REMARK   3      L13:  -0.3130 L23:   0.8893                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0554 S22:  -0.0019 S33:  -0.0845                       
REMARK   3      S12:  -0.8303 S13:   0.4981 S21:   0.1922                       
REMARK   3      S23:  -0.3004 S31:   0.0087 S32:   0.2105                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 38:84)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  15.3507 -42.2194  23.1758              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1071 T22:   0.1475                                     
REMARK   3      T33:   0.2142 T12:  -0.0002                                     
REMARK   3      T13:  -0.0344 T23:  -0.0882                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6400 L22:  -0.2205                                     
REMARK   3      L33:   0.6699 L12:  -0.0193                                     
REMARK   3      L13:   0.8301 L23:   0.6570                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0980 S22:   0.0251 S33:   0.0946                       
REMARK   3      S12:  -0.3460 S13:   0.4858 S21:   0.0150                       
REMARK   3      S23:  -0.0617 S31:  -0.1084 S32:  -0.1601                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 85:156)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4273 -50.4119  13.7120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0923 T22:   0.1325                                     
REMARK   3      T33:   0.1388 T12:  -0.0287                                     
REMARK   3      T13:  -0.0096 T23:   0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3930 L22:   0.1056                                     
REMARK   3      L33:   0.5240 L12:  -0.5296                                     
REMARK   3      L13:   0.3973 L23:   0.2560                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0169 S22:   0.0052 S33:   0.0063                       
REMARK   3      S12:  -0.1209 S13:   0.1877 S21:   0.0130                       
REMARK   3      S23:  -0.1121 S31:   0.0073 S32:  -0.0456                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 157:205)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5975 -30.9044  11.7318              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2031 T22:   0.0608                                     
REMARK   3      T33:   0.2120 T12:  -0.0333                                     
REMARK   3      T13:  -0.0196 T23:   0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6389 L22:  -0.5165                                     
REMARK   3      L33:   0.3617 L12:  -0.0967                                     
REMARK   3      L13:  -0.1706 L23:   0.6580                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0024 S22:  -0.0313 S33:   0.0395                       
REMARK   3      S12:  -0.0532 S13:   0.0966 S21:   0.0259                       
REMARK   3      S23:   0.1646 S31:  -0.0810 S32:   0.0572                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 206:213)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  22.0426 -37.2878   3.2148              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6305 T22:   0.5010                                     
REMARK   3      T33:   0.3512 T12:   0.0809                                     
REMARK   3      T13:  -0.1201 T23:  -0.0677                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2036 L22:  -1.9320                                     
REMARK   3      L33:   1.3412 L12:  -0.3548                                     
REMARK   3      L13:  -3.3200 L23:   9.3203                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0175 S22:   0.2419 S33:  -0.1642                       
REMARK   3      S12:   0.5554 S13:  -0.0743 S21:  -0.5491                       
REMARK   3      S23:   0.0281 S31:  -0.6554 S32:  -0.1243                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 214:230)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  20.5649 -56.3454   4.6993              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1009 T22:   0.1799                                     
REMARK   3      T33:   0.0857 T12:  -0.0218                                     
REMARK   3      T13:  -0.0157 T23:   0.0204                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7108 L22:   0.9757                                     
REMARK   3      L33:   0.6173 L12:   0.1535                                     
REMARK   3      L13:  -0.7379 L23:   0.0829                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1097 S22:  -0.0342 S33:  -0.0784                       
REMARK   3      S12:   0.0092 S13:  -0.0456 S21:  -0.0507                       
REMARK   3      S23:   0.0094 S31:  -0.1512 S32:   0.2140                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 231:288)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   4.0307 -53.5793  15.8107              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0580 T22:   0.0970                                     
REMARK   3      T33:   0.0520 T12:  -0.0239                                     
REMARK   3      T13:  -0.0124 T23:  -0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0580 L22:   0.3670                                     
REMARK   3      L33:   0.2278 L12:  -0.0939                                     
REMARK   3      L13:   0.2881 L23:   0.0649                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0113 S22:  -0.0159 S33:   0.0107                       
REMARK   3      S12:  -0.2243 S13:   0.0230 S21:   0.0709                       
REMARK   3      S23:  -0.0209 S31:   0.0070 S32:  -0.0253                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3      REFERENCE SELECTION: (CHAIN A)                                  
REMARK   3      SELECTION          : (CHAIN B)                                  
REMARK   3      ATOM PAIRS NUMBER  : 2185                                       
REMARK   3      RMSD               : 0.311                                      
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2WUD COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  02-OCT-09.                 
REMARK 100 THE PDBE ID CODE IS EBI-41325.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-MAR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : BRUKER MICROSTAR                   
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MONTEL 200 OPTICS                  
REMARK 200  OPTICS                         : MONTEL 200 OPTICS                  
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRUKER SMART 6000                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT                              
REMARK 200  DATA SCALING SOFTWARE          : SADABS                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35484                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.10                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 59.80                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.2                                
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.70                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.8                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.32                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.80                               
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 2VF2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.9                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM KSCN, 24% PEG 3350, 100MM          
REMARK 280  BIS-TRIS PROPANE                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X,Y+1/2,Z+1/2                                           
REMARK 290       6555   -X,-Y+1/2,Z+1/2                                         
REMARK 290       7555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       8555   X,-Y+1/2,-Z+1/2                                         
REMARK 290       9555   X+1/2,Y,Z+1/2                                           
REMARK 290      10555   -X+1/2,-Y,Z+1/2                                         
REMARK 290      11555   -X+1/2,Y,-Z+1/2                                         
REMARK 290      12555   X+1/2,-Y,-Z+1/2                                         
REMARK 290      13555   X+1/2,Y+1/2,Z                                           
REMARK 290      14555   -X+1/2,-Y+1/2,Z                                         
REMARK 290      15555   -X+1/2,Y+1/2,-Z                                         
REMARK 290      16555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  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        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       59.38250            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       91.29600            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       59.38250            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       91.29600            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       59.38250            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       91.29600            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       59.38250            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       91.29600            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       56.12700            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       91.29600            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       56.12700            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       91.29600            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000       56.12700            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       91.29600            
REMARK 290   SMTRY1  12  1.000000  0.000000  0.000000       56.12700            
REMARK 290   SMTRY2  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       91.29600            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       56.12700            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       59.38250            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       56.12700            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       59.38250            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       56.12700            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       59.38250            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       56.12700            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       59.38250            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.96 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -56.12700            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       91.29600            
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000       -0.00000            
REMARK 350   BIOMT2   3  0.000000 -1.000000  0.000000      -59.38250            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000       91.29600            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000      -56.12700            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      -59.38250            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.48 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350   BIOMT1   2  1.000000  0.000000  0.000000       -0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000     -118.76500            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000       -0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000     -118.76500            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, SER 114 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, SER 114 TO ALA                        
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     GLY A   289                                                      
REMARK 465     GLY A   290                                                      
REMARK 465     ARG A   291                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     GLY B   289                                                      
REMARK 465     GLY B   290                                                      
REMARK 465     ARG B   291                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 187   CD    GLU A 187   OE1    -0.101                       
REMARK 500    GLU A 200   CD    GLU A 200   OE2    -0.088                       
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: 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 133   CD  -  NE  -  CZ  ANGL. DEV. =  10.4 DEGREES          
REMARK 500    ARG A 133   NE  -  CZ  -  NH1 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    ARG A 133   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ARG B 133   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG B 133   NE  -  CZ  -  NH2 ANGL. DEV. =   4.9 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    ALA A 114     -124.66     51.57                                   
REMARK 500    VAL A 243      -61.52   -100.71                                   
REMARK 500    LYS B  81       79.65   -117.54                                   
REMARK 500    ALA B 114     -118.30     53.05                                   
REMARK 500    VAL B 243      -62.63   -100.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN A 113        21.8      L          L   OUTSIDE RANGE           
REMARK 500    ASN B 113        25.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1289                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN B1289                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VF2   RELATED DB: PDB                                   
REMARK 900  X-RAY CRYSTAL STRUCTURE OF HSAD FROM                                
REMARK 900  MYCOBACTERIUM TUBERCULOSIS                                          
REMARK 900 RELATED ID: 2WUE   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF S114A MUTANT OF HSAD                           
REMARK 900  FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX                          
REMARK 900  WITH HOPODA                                                         
REMARK 900 RELATED ID: 2WUF   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF S114A MUTANT OF HSAD                           
REMARK 900  FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX                          
REMARK 900  WITH 4,9DSHA                                                        
REMARK 900 RELATED ID: 2WUG   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF S114A MUTANT OF HSAD                           
REMARK 900  FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX                          
REMARK 900  WITH HOPDA                                                          
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 S114A MUTANT                                                         
DBREF  2WUD A    1   291  UNP    P96851   P96851_MYCTU     1    291             
DBREF  2WUD B    1   291  UNP    P96851   P96851_MYCTU     1    291             
SEQADV 2WUD ALA A  114  UNP  P96851    SER   114 ENGINEERED MUTATION            
SEQADV 2WUD ALA B  114  UNP  P96851    SER   114 ENGINEERED MUTATION            
SEQRES   1 A  291  MET THR ALA THR GLU GLU LEU THR PHE GLU SER THR SER          
SEQRES   2 A  291  ARG PHE ALA GLU VAL ASP VAL ASP GLY PRO LEU LYS LEU          
SEQRES   3 A  291  HIS TYR HIS GLU ALA GLY VAL GLY ASN ASP GLN THR VAL          
SEQRES   4 A  291  VAL LEU LEU HIS GLY GLY GLY PRO GLY ALA ALA SER TRP          
SEQRES   5 A  291  THR ASN PHE SER ARG ASN ILE ALA VAL LEU ALA ARG HIS          
SEQRES   6 A  291  PHE HIS VAL LEU ALA VAL ASP GLN PRO GLY TYR GLY HIS          
SEQRES   7 A  291  SER ASP LYS ARG ALA GLU HIS GLY GLN PHE ASN ARG TYR          
SEQRES   8 A  291  ALA ALA MET ALA LEU LYS GLY LEU PHE ASP GLN LEU GLY          
SEQRES   9 A  291  LEU GLY ARG VAL PRO LEU VAL GLY ASN ALA LEU GLY GLY          
SEQRES  10 A  291  GLY THR ALA VAL ARG PHE ALA LEU ASP TYR PRO ALA ARG          
SEQRES  11 A  291  ALA GLY ARG LEU VAL LEU MET GLY PRO GLY GLY LEU SER          
SEQRES  12 A  291  ILE ASN LEU PHE ALA PRO ASP PRO THR GLU GLY VAL LYS          
SEQRES  13 A  291  ARG LEU SER LYS PHE SER VAL ALA PRO THR ARG GLU ASN          
SEQRES  14 A  291  LEU GLU ALA PHE LEU ARG VAL MET VAL TYR ASP LYS ASN          
SEQRES  15 A  291  LEU ILE THR PRO GLU LEU VAL ASP GLN ARG PHE ALA LEU          
SEQRES  16 A  291  ALA SER THR PRO GLU SER LEU THR ALA THR ARG ALA MET          
SEQRES  17 A  291  GLY LYS SER PHE ALA GLY ALA ASP PHE GLU ALA GLY MET          
SEQRES  18 A  291  MET TRP ARG GLU VAL TYR ARG LEU ARG GLN PRO VAL LEU          
SEQRES  19 A  291  LEU ILE TRP GLY ARG GLU ASP ARG VAL ASN PRO LEU ASP          
SEQRES  20 A  291  GLY ALA LEU VAL ALA LEU LYS THR ILE PRO ARG ALA GLN          
SEQRES  21 A  291  LEU HIS VAL PHE GLY GLN CYS GLY HIS TRP VAL GLN VAL          
SEQRES  22 A  291  GLU LYS PHE ASP GLU PHE ASN LYS LEU THR ILE GLU PHE          
SEQRES  23 A  291  LEU GLY GLY GLY ARG                                          
SEQRES   1 B  291  MET THR ALA THR GLU GLU LEU THR PHE GLU SER THR SER          
SEQRES   2 B  291  ARG PHE ALA GLU VAL ASP VAL ASP GLY PRO LEU LYS LEU          
SEQRES   3 B  291  HIS TYR HIS GLU ALA GLY VAL GLY ASN ASP GLN THR VAL          
SEQRES   4 B  291  VAL LEU LEU HIS GLY GLY GLY PRO GLY ALA ALA SER TRP          
SEQRES   5 B  291  THR ASN PHE SER ARG ASN ILE ALA VAL LEU ALA ARG HIS          
SEQRES   6 B  291  PHE HIS VAL LEU ALA VAL ASP GLN PRO GLY TYR GLY HIS          
SEQRES   7 B  291  SER ASP LYS ARG ALA GLU HIS GLY GLN PHE ASN ARG TYR          
SEQRES   8 B  291  ALA ALA MET ALA LEU LYS GLY LEU PHE ASP GLN LEU GLY          
SEQRES   9 B  291  LEU GLY ARG VAL PRO LEU VAL GLY ASN ALA LEU GLY GLY          
SEQRES  10 B  291  GLY THR ALA VAL ARG PHE ALA LEU ASP TYR PRO ALA ARG          
SEQRES  11 B  291  ALA GLY ARG LEU VAL LEU MET GLY PRO GLY GLY LEU SER          
SEQRES  12 B  291  ILE ASN LEU PHE ALA PRO ASP PRO THR GLU GLY VAL LYS          
SEQRES  13 B  291  ARG LEU SER LYS PHE SER VAL ALA PRO THR ARG GLU ASN          
SEQRES  14 B  291  LEU GLU ALA PHE LEU ARG VAL MET VAL TYR ASP LYS ASN          
SEQRES  15 B  291  LEU ILE THR PRO GLU LEU VAL ASP GLN ARG PHE ALA LEU          
SEQRES  16 B  291  ALA SER THR PRO GLU SER LEU THR ALA THR ARG ALA MET          
SEQRES  17 B  291  GLY LYS SER PHE ALA GLY ALA ASP PHE GLU ALA GLY MET          
SEQRES  18 B  291  MET TRP ARG GLU VAL TYR ARG LEU ARG GLN PRO VAL LEU          
SEQRES  19 B  291  LEU ILE TRP GLY ARG GLU ASP ARG VAL ASN PRO LEU ASP          
SEQRES  20 B  291  GLY ALA LEU VAL ALA LEU LYS THR ILE PRO ARG ALA GLN          
SEQRES  21 B  291  LEU HIS VAL PHE GLY GLN CYS GLY HIS TRP VAL GLN VAL          
SEQRES  22 B  291  GLU LYS PHE ASP GLU PHE ASN LYS LEU THR ILE GLU PHE          
SEQRES  23 B  291  LEU GLY GLY GLY ARG                                          
HET    SCN  A1289       3                                                       
HET    SCN  B1289       3                                                       
HETNAM     SCN THIOCYANATE ION                                                  
FORMUL   3  SCN    2(C N S 1-)                                                  
FORMUL   4  HOH   *275(H2 O)                                                    
HELIX    1   1 THR A    8  THR A   12  1                                   5    
HELIX    2   2 ALA A   50  PHE A   55  1                                   6    
HELIX    3   3 ASN A   58  ARG A   64  1                                   7    
HELIX    4   4 GLN A   87  LYS A   97  1                                  11    
HELIX    5   5 THR A  119  TYR A  127  1                                   9    
HELIX    6   6 VAL A  155  ALA A  164  1                                  10    
HELIX    7   7 THR A  166  VAL A  176  1                                  11    
HELIX    8   8 ASP A  180  ILE A  184  5                                   5    
HELIX    9   9 THR A  185  SER A  197  1                                  13    
HELIX   10  10 THR A  198  MET A  208  1                                  11    
HELIX   11  11 MET A  221  GLU A  225  5                                   5    
HELIX   12  12 GLU A  225  LEU A  229  5                                   5    
HELIX   13  13 ALA A  249  ILE A  256  1                                   8    
HELIX   14  14 TRP A  270  LYS A  275  1                                   6    
HELIX   15  15 LYS A  275  LEU A  287  1                                  13    
HELIX   16  16 THR B    8  THR B   12  1                                   5    
HELIX   17  17 ALA B   50  PHE B   55  1                                   6    
HELIX   18  18 ASN B   58  ARG B   64  1                                   7    
HELIX   19  19 GLN B   87  LYS B   97  1                                  11    
HELIX   20  20 THR B  119  TYR B  127  1                                   9    
HELIX   21  21 PRO B  128  ALA B  131  5                                   4    
HELIX   22  22 VAL B  155  ALA B  164  1                                  10    
HELIX   23  23 THR B  166  VAL B  176  1                                  11    
HELIX   24  24 ASP B  180  ILE B  184  5                                   5    
HELIX   25  25 THR B  185  SER B  197  1                                  13    
HELIX   26  26 THR B  198  MET B  208  1                                  11    
HELIX   27  27 MET B  221  GLU B  225  5                                   5    
HELIX   28  28 GLU B  225  LEU B  229  5                                   5    
HELIX   29  29 ALA B  249  ILE B  256  1                                   8    
HELIX   30  30 TRP B  270  LYS B  275  1                                   6    
HELIX   31  31 LYS B  275  LEU B  287  1                                  13    
SHEET    1  AA 5 SER A  13  VAL A  18  0                                        
SHEET    2  AA 5 LEU A  24  ALA A  31 -1  O  LEU A  24   N  VAL A  18           
SHEET    3  AA 5 HIS A  67  VAL A  71 -1  O  VAL A  68   N  ALA A  31           
SHEET    4  AA 5 THR A  38  LEU A  42  1  O  VAL A  39   N  LEU A  69           
SHEET    5  AA 5 LEU A 110  VAL A 111  1  O  VAL A 111   N  LEU A  42           
SHEET    1  AB 3 LEU A 134  LEU A 136  0                                        
SHEET    2  AB 3 VAL A 233  TRP A 237  1  O  LEU A 234   N  LEU A 136           
SHEET    3  AB 3 ALA A 259  VAL A 263  1  O  GLN A 260   N  LEU A 235           
SHEET    1  BA 5 SER B  13  VAL B  18  0                                        
SHEET    2  BA 5 LEU B  24  ALA B  31 -1  O  LEU B  24   N  VAL B  18           
SHEET    3  BA 5 HIS B  67  VAL B  71 -1  O  VAL B  68   N  ALA B  31           
SHEET    4  BA 5 THR B  38  LEU B  42  1  O  VAL B  39   N  LEU B  69           
SHEET    5  BA 5 LEU B 110  VAL B 111  1  O  VAL B 111   N  LEU B  42           
SHEET    1  BB 3 LEU B 134  LEU B 136  0                                        
SHEET    2  BB 3 VAL B 233  TRP B 237  1  O  LEU B 234   N  LEU B 136           
SHEET    3  BB 3 ALA B 259  VAL B 263  1  O  GLN B 260   N  LEU B 235           
CISPEP   1 ASP A  150    PRO A  151          0        -0.56                     
CISPEP   2 ASP B  150    PRO B  151          0        -0.29                     
SITE     1 AC1  6 LYS A  97  TYR A 127  PRO A 128  ALA A 129                    
SITE     2 AC1  6 ARG A 130  ARG B 130                                          
SITE     1 AC2  1 ARG B  57                                                     
CRYST1  112.254  118.765  182.592  90.00  90.00  90.00 F 2 2 2      32          
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      0.008908  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008420  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005477        0.00000                         
MTRIX1   1  0.034051  0.999419  0.001446       31.16240    1                    
MTRIX2   1  0.999372 -0.034035 -0.009898      -31.52060    1                    
MTRIX3   1 -0.009844  0.001782 -0.999950       45.83120    1                    
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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