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LongText Report for: 5olu-pdb

Name Class
5olu-pdb
HEADER    HYDROLASE                               28-JUL-17   5OLU              
TITLE     THE CRYSTAL STRUCTURE OF A HIGHLY THERMOSTABLE CARBOXYL ESTERASE FROM 
TITLE    2 BACILLUS COAGULANS IN COMPLEX WITH GLYCEROL                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA/BETA HYDROLASE FAMILY PROTEIN;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS COAGULANS DSM 1 = ATCC 7050;           
SOURCE   3 ORGANISM_TAXID: 1121088;                                             
SOURCE   4 GENE: BF29_2874;                                                     
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STAR;                             
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET100D-TOPO                          
KEYWDS    CARBOXYL ESTERASE, LIPASE, ALPHA/BETA HYDROLASE, HYDROLASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.J.GOURLAY,C.NAKHNOUKH,M.BOLOGNESI                                   
REVDAT   1   06-DEC-17 5OLU    0                                                
JRNL        AUTH   V.DE VITIS,C.NAKHNOUKH,A.PINTO,M.L.CONTENTE,A.BARBIROLI,     
JRNL        AUTH 2 M.BOLOGNESI,F.MOLINARI,L.J.GOURLAY,D.ROMANO                  
JRNL        TITL   A STEREOSPECIFIC CARBOXYL ESTERASE FROM BACILLUS COAGULANS   
JRNL        TITL 2 HOSTING NON-LIPASE ACTIVITIES WITHIN A LIPASE-LIKE FOLD      
JRNL        REF    FEBS J.                                    2017              
JRNL        REFN                   ISSN 1742-464X                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.73                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 43626                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.149                           
REMARK   3   R VALUE            (WORKING SET) : 0.148                           
REMARK   3   FREE R VALUE                     : 0.169                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.580                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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 39.7441 -  4.3365    1.00     3221   154  0.1488 0.1670        
REMARK   3     2  4.3365 -  3.4427    1.00     3048   148  0.1312 0.1378        
REMARK   3     3  3.4427 -  3.0077    1.00     3007   143  0.1569 0.1787        
REMARK   3     4  3.0077 -  2.7327    1.00     2993   145  0.1515 0.1578        
REMARK   3     5  2.7327 -  2.5369    1.00     2970   142  0.1524 0.1916        
REMARK   3     6  2.5369 -  2.3874    1.00     2956   143  0.1431 0.1681        
REMARK   3     7  2.3874 -  2.2678    1.00     2947   141  0.1390 0.1652        
REMARK   3     8  2.2678 -  2.1691    1.00     2938   141  0.1380 0.1612        
REMARK   3     9  2.1691 -  2.0856    1.00     2926   141  0.1465 0.1750        
REMARK   3    10  2.0856 -  2.0136    1.00     2943   141  0.1504 0.1941        
REMARK   3    11  2.0136 -  1.9507    1.00     2939   142  0.1487 0.1789        
REMARK   3    12  1.9507 -  1.8949    1.00     2902   138  0.1485 0.1817        
REMARK   3    13  1.8949 -  1.8450    1.00     2918   141  0.1620 0.1879        
REMARK   3    14  1.8450 -  1.8000    1.00     2918   140  0.1938 0.2178        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.130            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.920           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           2562                                  
REMARK   3   ANGLE     :  0.856           3472                                  
REMARK   3   CHIRALITY :  0.055            359                                  
REMARK   3   PLANARITY :  0.006            453                                  
REMARK   3   DIHEDRAL  : 13.001           1489                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 22 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -26.6872 -23.3248 -12.8802              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1027 T22:   0.1812                                     
REMARK   3      T33:   0.1319 T12:  -0.0319                                     
REMARK   3      T13:  -0.0328 T23:   0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6167 L22:   2.6810                                     
REMARK   3      L33:   0.5658 L12:  -1.7333                                     
REMARK   3      L13:   0.4173 L23:  -0.3572                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1172 S12:  -0.0917 S13:   0.3243                       
REMARK   3      S21:   0.1630 S22:   0.0920 S23:  -0.2578                       
REMARK   3      S31:  -0.1938 S32:   0.3346 S33:  -0.0253                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 23 THROUGH 74 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -35.7988 -29.2647 -16.0696              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0643 T22:   0.0822                                     
REMARK   3      T33:   0.0858 T12:  -0.0040                                     
REMARK   3      T13:  -0.0151 T23:   0.0329                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8251 L22:   1.1336                                     
REMARK   3      L33:   2.0416 L12:  -0.7728                                     
REMARK   3      L13:  -1.1358 L23:   0.4956                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0065 S12:   0.0656 S13:   0.0498                       
REMARK   3      S21:  -0.0074 S22:  -0.0034 S23:  -0.0359                       
REMARK   3      S31:  -0.1295 S32:   0.0808 S33:   0.0112                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 75 THROUGH 102 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -22.0843 -31.9760 -12.1826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0724 T22:   0.2180                                     
REMARK   3      T33:   0.1315 T12:  -0.0127                                     
REMARK   3      T13:  -0.0311 T23:   0.0128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3850 L22:   1.4945                                     
REMARK   3      L33:   1.2983 L12:  -0.7472                                     
REMARK   3      L13:  -1.4375 L23:   0.0414                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1387 S12:  -0.0269 S13:  -0.0120                       
REMARK   3      S21:   0.0894 S22:   0.0799 S23:  -0.2113                       
REMARK   3      S31:   0.0372 S32:   0.3640 S33:   0.0276                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 146 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.9337 -41.4962 -11.6883              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0598 T22:   0.1217                                     
REMARK   3      T33:   0.0831 T12:   0.0174                                     
REMARK   3      T13:  -0.0108 T23:   0.0237                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8900 L22:   1.7583                                     
REMARK   3      L33:   1.5731 L12:  -0.3415                                     
REMARK   3      L13:  -0.0253 L23:   0.2193                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0109 S12:   0.0167 S13:  -0.0880                       
REMARK   3      S21:   0.0887 S22:   0.0213 S23:  -0.0693                       
REMARK   3      S31:   0.0880 S32:   0.2231 S33:  -0.0388                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 147 THROUGH 174 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.7683 -44.6815 -28.1413              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1409 T22:   0.5653                                     
REMARK   3      T33:   0.2545 T12:   0.0517                                     
REMARK   3      T13:   0.0412 T23:  -0.0466                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7974 L22:   1.5524                                     
REMARK   3      L33:   0.7652 L12:   0.9795                                     
REMARK   3      L13:  -0.7216 L23:  -0.2107                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1507 S12:   0.4669 S13:  -0.2102                       
REMARK   3      S21:  -0.0307 S22:   0.1015 S23:  -0.1325                       
REMARK   3      S31:   0.0955 S32:   0.5125 S33:   0.0174                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 175 THROUGH 188 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -32.2154 -47.4326 -37.7546              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2249 T22:   0.2356                                     
REMARK   3      T33:   0.1634 T12:   0.0549                                     
REMARK   3      T13:   0.0548 T23:  -0.0213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0989 L22:   6.8855                                     
REMARK   3      L33:   5.6005 L12:  -0.6046                                     
REMARK   3      L13:  -0.9185 L23:  -4.3206                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1683 S12:   0.3467 S13:   0.1460                       
REMARK   3      S21:  -0.7710 S22:  -0.0404 S23:  -0.2386                       
REMARK   3      S31:   0.4373 S32:   0.4299 S33:  -0.1108                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 189 THROUGH 270 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.5313 -45.0981 -21.2524              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0688 T22:   0.1719                                     
REMARK   3      T33:   0.1211 T12:   0.0310                                     
REMARK   3      T13:   0.0085 T23:   0.0169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1676 L22:   0.4973                                     
REMARK   3      L33:   0.4255 L12:  -0.1122                                     
REMARK   3      L13:   0.1872 L23:   0.1676                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0027 S12:   0.0349 S13:  -0.0320                       
REMARK   3      S21:  -0.0471 S22:  -0.0211 S23:  -0.1393                       
REMARK   3      S31:   0.0600 S32:   0.2366 S33:   0.0263                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 271 THROUGH 292 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -41.9875 -45.3354 -21.4963              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0511 T22:   0.0764                                     
REMARK   3      T33:   0.0885 T12:   0.0192                                     
REMARK   3      T13:   0.0188 T23:   0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0379 L22:   1.7671                                     
REMARK   3      L33:   2.3832 L12:  -1.2176                                     
REMARK   3      L13:   2.0288 L23:  -1.6020                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0589 S12:  -0.0393 S13:  -0.0571                       
REMARK   3      S21:   0.0212 S22:   0.1123 S23:   0.0753                       
REMARK   3      S31:  -0.0669 S32:  -0.1786 S33:  -0.0903                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 293 THROUGH 309 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -46.8302 -39.5869 -12.1188              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0375 T22:   0.0758                                     
REMARK   3      T33:   0.1014 T12:   0.0335                                     
REMARK   3      T13:   0.0170 T23:   0.0279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8110 L22:   3.7407                                     
REMARK   3      L33:   6.8415 L12:  -0.1198                                     
REMARK   3      L13:   1.2354 L23:  -1.5774                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0094 S12:  -0.1353 S13:  -0.0942                       
REMARK   3      S21:   0.1951 S22:   0.1098 S23:   0.1413                       
REMARK   3      S31:  -0.0925 S32:  -0.3554 S33:  -0.1008                       
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 5OLU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200005817.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-AUG-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43646                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 39.10                              
REMARK 200  R MERGE                    (I) : 0.11300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 34.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 37.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.58900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: 3PE6                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HAMPTON CRYSTAL SCREEN 2 CONDITION 42.   
REMARK 280  1.5 M AMMONIUM SULFATE, 12% GLYCEROL AND 0.1 M TRIS-HCL, PH 8.0,    
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
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,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       41.81800            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       41.81800            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       41.81800            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       41.81800            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       41.81800            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       41.81800            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 503  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 532  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 622  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 651  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 666  LIES ON A SPECIAL POSITION.                          
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   -35                                                      
REMARK 465     ARG A   -34                                                      
REMARK 465     GLY A   -33                                                      
REMARK 465     SER A   -32                                                      
REMARK 465     HIS A   -31                                                      
REMARK 465     HIS A   -30                                                      
REMARK 465     HIS A   -29                                                      
REMARK 465     HIS A   -28                                                      
REMARK 465     HIS A   -27                                                      
REMARK 465     HIS A   -26                                                      
REMARK 465     GLY A   -25                                                      
REMARK 465     MET A   -24                                                      
REMARK 465     ALA A   -23                                                      
REMARK 465     SER A   -22                                                      
REMARK 465     MET A   -21                                                      
REMARK 465     THR A   -20                                                      
REMARK 465     GLY A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     GLN A   -17                                                      
REMARK 465     GLN A   -16                                                      
REMARK 465     MET A   -15                                                      
REMARK 465     GLY A   -14                                                      
REMARK 465     ARG A   -13                                                      
REMARK 465     ASP A   -12                                                      
REMARK 465     LEU A   -11                                                      
REMARK 465     TYR A   -10                                                      
REMARK 465     ASP A    -9                                                      
REMARK 465     ASP A    -8                                                      
REMARK 465     ASP A    -7                                                      
REMARK 465     ASP A    -6                                                      
REMARK 465     LYS A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     PHE A    -1                                                      
REMARK 465     LYS A   310                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     TYR A 158    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASN A   265     O    HOH A   501              2.12            
REMARK 500   O    HOH A   639     O    HOH A   663              2.14            
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   2     -117.34    -88.83                                   
REMARK 500    LYS A  14      -43.19   -131.19                                   
REMARK 500    GLU A  40     -158.98   -119.06                                   
REMARK 500    SER A 114     -122.72     62.79                                   
REMARK 500    ASN A 145       -7.93     75.55                                   
REMARK 500    ARG A 283     -143.22    -84.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PEG A  412                                                       
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 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 406                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 407                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 408                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 409                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 410                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 411                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 413                 
DBREF1 5OLU A    1   310  UNP                  A0A0B5WSQ6_BACCO                 
DBREF2 5OLU A     A0A0B5WSQ6                          1         310             
SEQADV 5OLU MET A  -35  UNP  A0A0B5WSQ           INITIATING METHIONINE          
SEQADV 5OLU ARG A  -34  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU GLY A  -33  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU SER A  -32  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU HIS A  -31  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU HIS A  -30  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU HIS A  -29  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU HIS A  -28  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU HIS A  -27  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU HIS A  -26  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU GLY A  -25  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU MET A  -24  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU ALA A  -23  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU SER A  -22  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU MET A  -21  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU THR A  -20  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU GLY A  -19  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU GLY A  -18  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU GLN A  -17  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU GLN A  -16  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU MET A  -15  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU GLY A  -14  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU ARG A  -13  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU ASP A  -12  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU LEU A  -11  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU TYR A  -10  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU ASP A   -9  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU ASP A   -8  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU ASP A   -7  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU ASP A   -6  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU LYS A   -5  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU ASP A   -4  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU HIS A   -3  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU PRO A   -2  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU PHE A   -1  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQADV 5OLU THR A    0  UNP  A0A0B5WSQ           EXPRESSION TAG                 
SEQRES   1 A  346  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA          
SEQRES   2 A  346  SER MET THR GLY GLY GLN GLN MET GLY ARG ASP LEU TYR          
SEQRES   3 A  346  ASP ASP ASP ASP LYS ASP HIS PRO PHE THR MET ALA PHE          
SEQRES   4 A  346  GLN GLU LEU SER PHE GLN SER PHE ASN GLY LYS ASP ASN          
SEQRES   5 A  346  VAL LYS ALA TRP ILE TYR THR PRO ILE ARG LYS PRO ARG          
SEQRES   6 A  346  GLY ILE VAL GLN VAL VAL HIS GLY PHE GLY GLU HIS SER          
SEQRES   7 A  346  ARG ARG TYR LEU HIS MET ILE LEU LYS PHE ASN GLU ALA          
SEQRES   8 A  346  GLY PHE VAL VAL ALA ALA ASP ASP HIS VAL GLY HIS GLY          
SEQRES   9 A  346  LYS THR ALA TYR ASP SER GLY ASN TRP GLY ASP TRP GLY          
SEQRES  10 A  346  ASP LYS GLY TYR MET THR MET ALA GLU ASP GLU HIS THR          
SEQRES  11 A  346  LEU ARG LYS ILE VAL GLN GLU GLN TYR PRO ASP LEU PRO          
SEQRES  12 A  346  TYR PHE MET PHE GLY HIS SER MET GLY SER MET ILE ALA          
SEQRES  13 A  346  ARG GLY TYR ALA ALA THR HIS GLY ALA GLY LEU SER GLY          
SEQRES  14 A  346  LEU ILE LEU CYS GLY THR SER GLY ARG PHE PRO ASN ALA          
SEQRES  15 A  346  SER LYS LEU LEU PRO VAL LEU LYS ASN LEU ILE TYR GLU          
SEQRES  16 A  346  GLY LYS GLY GLN GLU THR ASP LEU SER TYR LEU GLU GLU          
SEQRES  17 A  346  LEU MET GLY TRP MET THR GLU ARG ILE GLU GLN PRO LYS          
SEQRES  18 A  346  THR PRO ASN ASP TRP ILE SER SER ASP PRO ASP ILE VAL          
SEQRES  19 A  346  ALA ASP HIS ALA ASN ASP PRO PHE ASN ASN PHE THR THR          
SEQRES  20 A  346  PRO PRO ASN ILE ARG SER LEU TYR TYR PHE VAL GLN MET          
SEQRES  21 A  346  MET GLU ILE ILE VAL GLY THR GLU TRP ALA GLU LYS VAL          
SEQRES  22 A  346  PRO VAL SER ILE PRO ILE TYR ASN ILE ALA GLY ASP GLN          
SEQRES  23 A  346  ASP PRO VAL GLY GLN TYR GLY GLU GLY VAL TYR ALA VAL          
SEQRES  24 A  346  SER ASN TRP LEU VAL GLN THR GLY HIS HIS VAL LYS THR          
SEQRES  25 A  346  LYS VAL TYR PRO GLY HIS ARG HIS GLU ILE HIS ASN ASP          
SEQRES  26 A  346  ARG ASP ILE ARG ASP GLU VAL GLU GLU GLY ILE ILE SER          
SEQRES  27 A  346  PHE ILE ASN GLY ILE ILE VAL LYS                              
HET    GOL  A 401      14                                                       
HET    GOL  A 402      14                                                       
HET    GOL  A 403      14                                                       
HET     CL  A 404       1                                                       
HET     CL  A 405       1                                                       
HET     CL  A 406       1                                                       
HET     CL  A 407       1                                                       
HET     CL  A 408       1                                                       
HET     CL  A 409       1                                                       
HET     CL  A 410       1                                                       
HET     CL  A 411       1                                                       
HET    PEG  A 412      15                                                       
HET    ACT  A 413       7                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     ACT ACETATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  GOL    3(C3 H8 O3)                                                  
FORMUL   5   CL    8(CL 1-)                                                     
FORMUL  13  PEG    C4 H10 O3                                                    
FORMUL  14  ACT    C2 H3 O2 1-                                                  
FORMUL  15  HOH   *192(H2 O)                                                    
HELIX    1 AA1 HIS A   41  ARG A   44  5                                   4    
HELIX    2 AA2 TYR A   45  ALA A   55  1                                  11    
HELIX    3 AA3 HIS A   67  GLY A   75  1                                   9    
HELIX    4 AA4 MET A   86  TYR A  103  1                                  18    
HELIX    5 AA5 SER A  114  HIS A  127  1                                  14    
HELIX    6 AA6 ASN A  145  GLU A  159  1                                  15    
HELIX    7 AA7 ASP A  166  GLY A  175  1                                  10    
HELIX    8 AA8 ASN A  188  SER A  192  5                                   5    
HELIX    9 AA9 ASP A  194  ASP A  204  1                                  11    
HELIX   10 AB1 ASN A  214  ILE A  227  1                                  14    
HELIX   11 AB2 VAL A  229  GLU A  235  1                                   7    
HELIX   12 AB3 ASP A  251  GLN A  255  5                                   5    
HELIX   13 AB4 GLY A  257  THR A  270  1                                  14    
HELIX   14 AB5 ILE A  292  VAL A  309  1                                  18    
SHEET    1 AA1 8 GLN A   4  GLN A   9  0                                        
SHEET    2 AA1 8 ASN A  16  TYR A  22 -1  O  VAL A  17   N  PHE A   8           
SHEET    3 AA1 8 PHE A  57  ASP A  63 -1  O  VAL A  59   N  TYR A  22           
SHEET    4 AA1 8 GLY A  30  VAL A  35  1  N  VAL A  32   O  VAL A  58           
SHEET    5 AA1 8 TYR A 108  HIS A 113  1  O  PHE A 111   N  GLN A  33           
SHEET    6 AA1 8 LEU A 131  CYS A 137  1  O  SER A 132   N  TYR A 108           
SHEET    7 AA1 8 ILE A 243  GLY A 248  1  O  TYR A 244   N  LEU A 136           
SHEET    8 AA1 8 VAL A 274  TYR A 279  1  O  TYR A 279   N  ALA A 247           
SITE     1 AC1  9 PHE A  38  GLU A  40  HIS A 113  SER A 114                    
SITE     2 AC1  9 HIS A 201  PHE A 209  HIS A 284  GLU A 285                    
SITE     3 AC1  9 HOH A 527                                                     
SITE     1 AC2  7 ASP A 200  ASN A 288  ARG A 290  HOH A 539                    
SITE     2 AC2  7 HOH A 544  HOH A 620  HOH A 649                               
SITE     1 AC3  6 GLN A   4  GLU A   5  TYR A  72  PRO A 205                    
SITE     2 AC3  6 PHE A 206  HOH A 514                                          
SITE     1 AC4  3 TYR A 103  PRO A 104  ASP A 105                               
SITE     1 AC5  5 ARG A  26  ASP A 194  ILE A 197  ARG A 290                    
SITE     2 AC5  5 HOH A 670                                                     
SITE     1 AC6  3 GLY A 162  ARG A 216  HOH A 631                               
SITE     1 AC7  6 GLY A 141  ARG A 142  PHE A 143  MET A 225                    
SITE     2 AC7  6 GLU A 226  VAL A 229                                          
SITE     1 AC8  1 HOH A 672                                                     
SITE     1 AC9  2 ARG A 142  TRP A 266                                          
SITE     1 AD1  5 LYS A 185  ASP A 189  VAL A 198  HOH A 599                    
SITE     2 AD1  5 HOH A 610                                                     
SITE     1 AD2  3 PHE A   8  GLN A   9  HOH A 689                               
SITE     1 AD3  5 TRP A  77  PRO A 205  ASN A 207  ASN A 208                    
SITE     2 AD3  5 THR A 211                                                     
SITE     1 AD4  3 ARG A  26  HOH A 505  HOH A 507                               
CRYST1  137.644  137.644   83.636  90.00  90.00 120.00 P 63 2 2     12          
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      0.007265  0.004195  0.000000        0.00000                         
SCALE2      0.000000  0.008389  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011957        0.00000                         
TER    4808      VAL A 309                                                      
MASTER      528    0   13   14    8    0   21    6 2689    1   64   27          
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.
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