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LongText Report for: 4NFU-pdb

Name Class
4NFU-pdb
HEADER    SIGNALING PROTEIN                       01-NOV-13   4NFU              
TITLE     STRUCTURE OF THE CENTRAL PLANT IMMUNITY SIGNALING NODE EDS1 IN COMPLEX
TITLE    2 WITH ITS INTERACTION PARTNER SAG101                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EDS1;                                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ENHANCED DISEASE SUSCEPTIBILITY 1;                          
COMPND   5 EC: 3.-.-.-;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SENESCENCE-ASSOCIATED CARBOXYLESTERASE 101;                
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: SENESCENCE-ASSOCIATED PROTEIN 101, SAG101;                  
COMPND  11 EC: 3.1.1.1;                                                         
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS;                                    
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: EDS1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRSF-DUET-1;                              
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE  13 ORGANISM_COMMON: MOUSE-EAR CRESS;                                    
SOURCE  14 ORGANISM_TAXID: 3702;                                                
SOURCE  15 GENE: AT5G14930, F2G14.50, SAG101;                                   
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);                              
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PRSF-DUET-1                               
KEYWDS    ALPHA/BETA HYDROLASE FOLD, INNATE IMMUNITY, PATHOGEN DEFENSE,         
KEYWDS   2 PHYTOALEXIN DEFICIENT 4, PAD4, NUCLEUS, HYDROLASE, SIGNALING PROTEIN 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.WAGNER,J.STUTTMANN,S.RIETZ,R.GUEROIS,K.NIEFIND,J.E.PARKER           
REVDAT   1   11-DEC-13 4NFU    0                                                
JRNL        AUTH   S.WAGNER,J.STUTTMANN,S.RIETZ,R.GUEROIS,E.BRUNSTEIN,J.BAUTOR, 
JRNL        AUTH 2 K.NIEFIND,J.E.PARKER                                         
JRNL        TITL   STRUCTURAL BASIS FOR SIGNALING BY EXCLUSIVE EDS1 HETEROMERIC 
JRNL        TITL 2 COMPLEXES WITH SAG101 OR PAD4 IN PLANT INNATE IMMUNITY.      
JRNL        REF    CELL HOST MICROBE             V.  14     1 2013              
JRNL        REFN                   ISSN 1931-3128                               
JRNL        DOI    10.1016/J.CHOM.2013.11.006                                   
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.WAGNER,S.RIETZ,J.E.PARKER,K.NIEFIND                        
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF 
REMARK   1  TITL 2 ARABIDOPSIS THALIANA EDS1, A KEY COMPONENT OF PLANT          
REMARK   1  TITL 3 IMMUNITY, IN COMPLEX WITH ITS SIGNALLING PARTNER SAG101.     
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  67   245 2011              
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  PMID   21301097                                                     
REMARK   1  DOI    10.1107/S1744309110051249                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.21 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.4_1496)                   
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) : 2.21                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.28                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.910                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 78844                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1567                            
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 34.2824 -  4.9106    1.00     7568   148  0.1556 0.1512        
REMARK   3     2  4.9106 -  3.8995    1.00     7281   166  0.1441 0.1486        
REMARK   3     3  3.8995 -  3.4071    1.00     7263   136  0.1668 0.2112        
REMARK   3     4  3.4071 -  3.0958    1.00     7212   159  0.1990 0.2274        
REMARK   3     5  3.0958 -  2.8740    1.00     7195   158  0.1973 0.2397        
REMARK   3     6  2.8740 -  2.7046    1.00     7205   115  0.1990 0.2238        
REMARK   3     7  2.7046 -  2.5692    1.00     7146   144  0.2028 0.2513        
REMARK   3     8  2.5692 -  2.4574    1.00     7151   136  0.2079 0.2352        
REMARK   3     9  2.4574 -  2.3629    0.99     7068   144  0.2123 0.2503        
REMARK   3    10  2.3629 -  2.2813    0.90     6439   140  0.2393 0.3086        
REMARK   3    11  2.2813 -  2.2100    0.81     5749   121  0.2769 0.3056        
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)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.420           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.71                          
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      :  0.002           9544                                  
REMARK   3   ANGLE     :  0.623          12879                                  
REMARK   3   CHIRALITY :  0.023           1398                                  
REMARK   3   PLANARITY :  0.003           1643                                  
REMARK   3   DIHEDRAL  : 11.229           3592                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 2 through 70 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  62.4256   6.1975  69.2793              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3762 T22:   0.3186                                     
REMARK   3      T33:   0.3499 T12:   0.0243                                     
REMARK   3      T13:  -0.0441 T23:   0.0275                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0166 L22:   2.5322                                     
REMARK   3      L33:   5.9564 L12:  -0.0011                                     
REMARK   3      L13:  -1.8209 L23:   0.7989                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0635 S12:  -0.2437 S13:  -0.1219                       
REMARK   3      S21:   0.2926 S22:   0.1015 S23:  -0.0362                       
REMARK   3      S31:   0.3405 S32:   0.0469 S33:  -0.1020                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 71 through 184 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  56.4765   8.1981  61.7083              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2773 T22:   0.2704                                     
REMARK   3      T33:   0.3433 T12:   0.0167                                     
REMARK   3      T13:   0.0119 T23:   0.0117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2990 L22:   2.3156                                     
REMARK   3      L33:   4.8630 L12:   0.2085                                     
REMARK   3      L13:   0.3208 L23:  -0.2575                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0267 S12:   0.0530 S13:  -0.0430                       
REMARK   3      S21:   0.0276 S22:   0.2080 S23:   0.1846                       
REMARK   3      S31:   0.1233 S32:  -0.3215 S33:  -0.2376                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 185 through 337 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  78.0137  16.7361  66.5128              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3721 T22:   0.6507                                     
REMARK   3      T33:   0.4228 T12:  -0.0528                                     
REMARK   3      T13:  -0.0469 T23:  -0.0846                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3997 L22:   2.5070                                     
REMARK   3      L33:   2.3789 L12:   0.4948                                     
REMARK   3      L13:  -0.9240 L23:  -0.2371                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0561 S12:  -0.4200 S13:  -0.0034                       
REMARK   3      S21:   0.3627 S22:   0.0580 S23:  -0.4192                       
REMARK   3      S31:  -0.2378 S32:   0.7366 S33:  -0.0663                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 338 through 380 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  67.8747  32.8375  55.2166              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8260 T22:   0.4902                                     
REMARK   3      T33:   0.5989 T12:  -0.1114                                     
REMARK   3      T13:   0.0216 T23:  -0.0488                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2735 L22:   0.0345                                     
REMARK   3      L33:   5.7419 L12:   0.3086                                     
REMARK   3      L13:   5.1253 L23:   0.4004                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2299 S12:  -0.2239 S13:   0.8029                       
REMARK   3      S21:   0.0201 S22:  -0.0977 S23:   0.0078                       
REMARK   3      S31:  -1.0175 S32:  -0.0337 S33:   0.5777                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resid 381 through 524 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  50.6763  18.7293  28.6571              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3411 T22:   0.4391                                     
REMARK   3      T33:   0.3437 T12:  -0.0498                                     
REMARK   3      T13:  -0.0303 T23:   0.0363                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5154 L22:   1.5108                                     
REMARK   3      L33:   4.0316 L12:   0.3158                                     
REMARK   3      L13:   0.2399 L23:  -1.2959                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0128 S12:   0.1805 S13:  -0.0690                       
REMARK   3      S21:  -0.1747 S22:   0.1690 S23:   0.1822                       
REMARK   3      S31:   0.2607 S32:  -0.3802 S33:  -0.1346                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resid 525 through 620 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  42.8864   1.7906  21.2465              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8368 T22:   0.6113                                     
REMARK   3      T33:   0.7115 T12:  -0.2522                                     
REMARK   3      T13:  -0.2151 T23:   0.1049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6206 L22:   2.8671                                     
REMARK   3      L33:   2.7808 L12:   0.3867                                     
REMARK   3      L13:  -0.2176 L23:   2.0165                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0605 S12:   0.0596 S13:  -0.6692                       
REMARK   3      S21:  -0.2830 S22:   0.3245 S23:   0.4342                       
REMARK   3      S31:   0.9312 S32:  -0.4585 S33:  -0.3498                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'B' and (resid -2 through 272 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  97.9418  20.8056  38.3606              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4583 T22:   0.4562                                     
REMARK   3      T33:   0.4372 T12:  -0.0156                                     
REMARK   3      T13:  -0.1028 T23:   0.0272                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9042 L22:   2.1991                                     
REMARK   3      L33:   4.3791 L12:   0.4274                                     
REMARK   3      L13:  -0.3491 L23:   0.4084                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2671 S12:  -0.2094 S13:  -0.3875                       
REMARK   3      S21:   0.1442 S22:  -0.1298 S23:  -0.0074                       
REMARK   3      S31:   0.5044 S32:   0.1344 S33:  -0.1187                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'B' and (resid 273 through 537 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  67.2530  33.3492   3.8359              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3138 T22:   0.3112                                     
REMARK   3      T33:   0.3397 T12:  -0.0046                                     
REMARK   3      T13:  -0.0194 T23:   0.0086                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8609 L22:   0.5615                                     
REMARK   3      L33:   2.8006 L12:  -0.1771                                     
REMARK   3      L13:   0.7834 L23:  -0.1308                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1591 S12:   0.0494 S13:  -0.1593                       
REMARK   3      S21:   0.0099 S22:   0.0164 S23:  -0.1546                       
REMARK   3      S31:   0.0964 S32:   0.0127 S33:  -0.1884                       
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 4NFU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB083149.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0399, 1.0404, 1.0313, 0.9184     
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 78935                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.210                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 7.800                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : 0.05400                            
REMARK 200   FOR THE DATA SET  : 21.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.97200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.97200                            
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP INTEGRATED INTO AUTO-RICKSHAW (EMBL-HAMBURG)    
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.5, 5% W/V PEG4000,     
REMARK 280  5% 2-PROPANOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   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       56.29300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.69300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.82150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.69300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       56.29300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.82150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 50890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     GLN A    -1                                                      
REMARK 465     ASP A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     THR A   621                                                      
REMARK 465     ASP A   622                                                      
REMARK 465     THR A   623                                                      
REMARK 465     PRO B    36                                                      
REMARK 465     TYR B    37                                                      
REMARK 465     SER B    38                                                      
REMARK 465     ASN B    39                                                      
REMARK 465     HIS B    40                                                      
REMARK 465     ASP B    41                                                      
REMARK 465     PRO B    42                                                      
REMARK 465     GLY B    43                                                      
REMARK 465     LEU B    44                                                      
REMARK 465     GLN B    45                                                      
REMARK 465     VAL B    46                                                      
REMARK 465     SER B    47                                                      
REMARK 465     LYS B    48                                                      
REMARK 465     LYS B    49                                                      
REMARK 465     LYS B    50                                                      
REMARK 465     LYS B    51                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   927     O    HOH A   928              1.94            
REMARK 500   OE2  GLU B   392     O    HOH B   825              2.03            
REMARK 500   O    HOH B   767     O    HOH B   770              2.12            
REMARK 500   OE2  GLU A   150     O    HOH A   955              2.16            
REMARK 500   O    HOH A   893     O    HOH A   924              2.19            
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    ARG A  29      -58.37     61.87                                   
REMARK 500    ASP A  98      119.19    -39.14                                   
REMARK 500    SER A 123     -132.37     57.26                                   
REMARK 500    ASN A 144       77.95   -159.79                                   
REMARK 500    PRO A 145       92.50    -69.69                                   
REMARK 500    VAL A 161      -50.84   -120.30                                   
REMARK 500    SER A 216       35.10    -97.50                                   
REMARK 500    ASN B  34      115.49   -164.52                                   
REMARK 500    SER B  53       66.03   -100.37                                   
REMARK 500    SER B  79       35.01    -93.16                                   
REMARK 500    ALA B 146     -123.93     54.86                                   
REMARK 500    MET B 210       45.08   -107.50                                   
REMARK 500    LEU B 265       43.69    -98.07                                   
REMARK 500    ASP B 267       43.52    -90.76                                   
REMARK 500    ASP B 291       16.83     59.09                                   
REMARK 500    MET B 292       74.04     33.51                                   
REMARK 500    MET B 293       28.87    -71.69                                   
REMARK 500    PHE B 294      -51.66   -125.95                                   
REMARK 500    SER B 333       -8.65   -143.24                                   
REMARK 500    HIS B 343      -63.21   -108.49                                   
REMARK 500    CYS B 429       33.39    -88.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA B 602                 
DBREF  4NFU A    2   623  UNP    Q9XF23   Q9XF23_ARATH     2    623             
DBREF  4NFU B    2   537  UNP    Q4F883   SG101_ARATH      1    536             
SEQADV 4NFU MET A  -12  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 4NFU GLY A  -11  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 4NFU SER A  -10  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 4NFU SER A   -9  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 4NFU HIS A   -8  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 4NFU HIS A   -7  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 4NFU HIS A   -6  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 4NFU HIS A   -5  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 4NFU HIS A   -4  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 4NFU HIS A   -3  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 4NFU SER A   -2  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 4NFU GLN A   -1  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 4NFU ASP A    0  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 4NFU PRO A    1  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 4NFU SER B   -2  UNP  Q4F883              EXPRESSION TAG                 
SEQADV 4NFU GLN B   -1  UNP  Q4F883              EXPRESSION TAG                 
SEQADV 4NFU ASP B    0  UNP  Q4F883              EXPRESSION TAG                 
SEQADV 4NFU PRO B    1  UNP  Q4F883              EXPRESSION TAG                 
SEQRES   1 A  636  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 A  636  PRO ALA PHE GLU ALA LEU THR GLY ILE ASN GLY ASP LEU          
SEQRES   3 A  636  ILE THR ARG SER TRP SER ALA SER LYS GLN ALA TYR LEU          
SEQRES   4 A  636  THR GLU ARG TYR HIS LYS GLU GLU ALA GLY ALA VAL VAL          
SEQRES   5 A  636  ILE PHE ALA PHE GLN PRO SER PHE SER GLU LYS ASP PHE          
SEQRES   6 A  636  PHE ASP PRO ASP ASN LYS SER SER PHE GLY GLU ILE LYS          
SEQRES   7 A  636  LEU ASN ARG VAL GLN PHE PRO CYS MET ARG LYS ILE GLY          
SEQRES   8 A  636  LYS GLY ASP VAL ALA THR VAL ASN GLU ALA PHE LEU LYS          
SEQRES   9 A  636  ASN LEU GLU ALA VAL ILE ASP PRO ARG THR SER PHE GLN          
SEQRES  10 A  636  ALA SER VAL GLU MET ALA VAL ARG SER ARG LYS GLN ILE          
SEQRES  11 A  636  VAL PHE THR GLY HIS SER SER GLY GLY ALA THR ALA ILE          
SEQRES  12 A  636  LEU ALA THR VAL TRP TYR LEU GLU LYS TYR PHE ILE ARG          
SEQRES  13 A  636  ASN PRO ASN VAL TYR LEU GLU PRO ARG CYS VAL THR PHE          
SEQRES  14 A  636  GLY ALA PRO LEU VAL GLY ASP SER ILE PHE SER HIS ALA          
SEQRES  15 A  636  LEU GLY ARG GLU LYS TRP SER ARG PHE PHE VAL ASN PHE          
SEQRES  16 A  636  VAL THR ARG PHE ASP ILE VAL PRO ARG ILE THR LEU ALA          
SEQRES  17 A  636  ARG LYS ALA SER VAL GLU GLU THR LEU PRO HIS VAL LEU          
SEQRES  18 A  636  ALA GLN LEU ASP PRO ARG ASN SER SER VAL GLN GLU SER          
SEQRES  19 A  636  GLU GLN ARG ILE THR GLU PHE TYR THR SER VAL MET ARG          
SEQRES  20 A  636  ASP THR SER THR VAL ALA ASN GLN ALA VAL CYS GLU LEU          
SEQRES  21 A  636  THR GLY SER ALA GLU ALA ILE LEU GLU THR LEU SER SER          
SEQRES  22 A  636  PHE LEU GLU LEU SER PRO TYR ARG PRO ALA GLY THR PHE          
SEQRES  23 A  636  VAL PHE SER THR GLU LYS ARG LEU VAL ALA VAL ASN ASN          
SEQRES  24 A  636  SER ASP ALA ILE LEU GLN MET LEU PHE TYR THR CYS GLN          
SEQRES  25 A  636  ALA SER ASP GLU GLN GLU TRP SER LEU ILE PRO PHE ARG          
SEQRES  26 A  636  SER ILE ARG ASP HIS HIS SER TYR GLU GLU LEU VAL GLN          
SEQRES  27 A  636  SER MET GLY MET LYS LEU PHE ASN HIS LEU ASP GLY GLU          
SEQRES  28 A  636  ASN SER ILE GLU SER SER LEU ASN ASP LEU GLY VAL SER          
SEQRES  29 A  636  THR ARG GLY ARG GLN TYR VAL GLN ALA ALA LEU GLU GLU          
SEQRES  30 A  636  GLU LYS LYS ARG VAL GLU ASN GLN LYS LYS ILE ILE GLN          
SEQRES  31 A  636  VAL ILE GLN GLN GLU ARG PHE LEU LYS LYS LEU ALA TRP          
SEQRES  32 A  636  ILE GLU ASP GLU TYR LYS PRO LYS CYS GLN ALA HIS LYS          
SEQRES  33 A  636  ASN GLY TYR TYR ASP SER PHE LYS VAL SER ASN GLU GLU          
SEQRES  34 A  636  ASN ASP PHE LYS ALA ASN VAL LYS ARG ALA GLU LEU ALA          
SEQRES  35 A  636  GLY VAL PHE ASP GLU VAL LEU GLY LEU LEU LYS LYS CYS          
SEQRES  36 A  636  GLN LEU PRO ASP GLU PHE GLU GLY ASP ILE ASP TRP ILE          
SEQRES  37 A  636  LYS LEU ALA THR ARG TYR ARG ARG LEU VAL GLU PRO LEU          
SEQRES  38 A  636  ASP ILE ALA ASN TYR HIS ARG HIS LEU LYS ASN GLU ASP          
SEQRES  39 A  636  THR GLY PRO TYR MET LYS ARG GLY ARG PRO THR ARG TYR          
SEQRES  40 A  636  ILE TYR ALA GLN ARG GLY TYR GLU HIS HIS ILE LEU LYS          
SEQRES  41 A  636  PRO ASN GLY MET ILE ALA GLU ASP VAL PHE TRP ASN LYS          
SEQRES  42 A  636  VAL ASN GLY LEU ASN LEU GLY LEU GLN LEU GLU GLU ILE          
SEQRES  43 A  636  GLN GLU THR LEU LYS ASN SER GLY SER GLU CYS GLY SER          
SEQRES  44 A  636  CYS PHE TRP ALA GLU VAL GLU GLU LEU LYS GLY LYS PRO          
SEQRES  45 A  636  TYR GLU GLU VAL GLU VAL ARG VAL LYS THR LEU GLU GLY          
SEQRES  46 A  636  MET LEU ARG GLU TRP ILE THR ALA GLY GLU VAL ASP GLU          
SEQRES  47 A  636  LYS GLU ILE PHE LEU GLU GLY SER THR PHE ARG LYS TRP          
SEQRES  48 A  636  TRP ILE THR LEU PRO LYS ASN HIS LYS SER HIS SER PRO          
SEQRES  49 A  636  LEU ARG ASP TYR MET MET ASP GLU ILE THR ASP THR              
SEQRES   1 B  540  SER GLN ASP PRO GLU SER SER SER SER LEU LYS GLY SER          
SEQRES   2 B  540  ALA LEU GLY LYS LEU VAL VAL THR SER GLY LEU LEU HIS          
SEQRES   3 B  540  SER SER TRP SER LYS ILE LEU GLU ILE HIS ASN PRO PRO          
SEQRES   4 B  540  TYR SER ASN HIS ASP PRO GLY LEU GLN VAL SER LYS LYS          
SEQRES   5 B  540  LYS LYS ASP SER GLY LEU GLU PHE GLN ILE HIS ARG GLU          
SEQRES   6 B  540  GLU LYS PHE THR LEU VAL VAL PHE SER ALA PRO PRO ILE          
SEQRES   7 B  540  CYS ARG SER SER SER SER ASP SER THR LEU LEU HIS VAL          
SEQRES   8 B  540  LYS ASP LYS GLU ASN PRO PHE PRO PHE LEU CYS SER GLU          
SEQRES   9 B  540  ASN ASN PRO SER PHE SER LEU HIS THR PRO ALA PHE ASN          
SEQRES  10 B  540  LEU PHE THR SER ALA SER THR SER LEU THR TYR LEU LYS          
SEQRES  11 B  540  SER GLU LEU LEU GLN THR LEU LYS SER GLU LYS PRO VAL          
SEQRES  12 B  540  ILE ILE THR GLY ALA ALA LEU GLY GLY SER VAL ALA SER          
SEQRES  13 B  540  LEU TYR THR LEU TRP LEU LEU GLU THR ILE GLU PRO THR          
SEQRES  14 B  540  LEU LYS ARG PRO LEU CYS ILE THR PHE GLY SER PRO LEU          
SEQRES  15 B  540  ILE GLY ASP ALA SER LEU GLN GLN ILE LEU GLU ASN SER          
SEQRES  16 B  540  VAL ARG ASN SER CYS PHE LEU HIS VAL VAL SER ALA GLN          
SEQRES  17 B  540  THR ARG ILE LYS MET ASP PHE PHE LYS PRO PHE GLY THR          
SEQRES  18 B  540  PHE LEU ILE CYS PHE ASP SER GLY CYS VAL CYS ILE GLU          
SEQRES  19 B  540  ASP HIS VAL ALA VAL THR GLU LEU LEU ASN GLY VAL HIS          
SEQRES  20 B  540  ASP SER GLY LEU VAL ASP TYR SER GLN VAL LEU ASN ARG          
SEQRES  21 B  540  LEU ASP GLN SER MET LEU SER LEU ALA ASP SER ARG LEU          
SEQRES  22 B  540  ILE PRO GLU ASP VAL ILE LYS GLY ILE GLU LYS ARG ALA          
SEQRES  23 B  540  GLU MET LYS ASN LEU ARG PHE ASP MET MET PHE LYS LYS          
SEQRES  24 B  540  LEU ASN ASP MET LYS ILE SER MET ALA TYR ILE GLU TRP          
SEQRES  25 B  540  TYR LYS LYS LYS CYS LYS GLU VAL LYS ILE GLY TYR TYR          
SEQRES  26 B  540  ASP ARG PHE LYS THR GLN LEU ALA PHE PRO SER LYS GLU          
SEQRES  27 B  540  PHE ASP ILE ASN ILE LYS ASN HIS HIS LYS SER GLU LEU          
SEQRES  28 B  540  ASN ARG PHE TRP LYS SER VAL VAL GLU GLU VAL GLU ARG          
SEQRES  29 B  540  ARG PRO GLN SER ASP ALA SER ILE LEU LYS ARG ARG PHE          
SEQRES  30 B  540  LEU PHE SER GLY ASN ASN TYR ARG ARG MET ILE GLU PRO          
SEQRES  31 B  540  LEU ASP ILE ALA GLU TYR TYR LEU GLU GLY ARG LYS GLU          
SEQRES  32 B  540  TYR ARG THR THR GLY ARG SER HIS HIS TYR VAL MET LEU          
SEQRES  33 B  540  GLU LYS TRP PHE GLY MET GLU SER ILE LEU ILE GLU LYS          
SEQRES  34 B  540  GLU ARG CYS LYS LYS ARG ASP LEU SER ASP LEU LEU THR          
SEQRES  35 B  540  PHE ASP SER CYS PHE TRP ALA GLU VAL GLU ASP SER LEU          
SEQRES  36 B  540  ILE VAL ILE ASN GLN LEU ASN THR THR VAL GLY MET ARG          
SEQRES  37 B  540  ASP ASP VAL ARG GLU VAL LEU THR ARG LYS LEU VAL GLU          
SEQRES  38 B  540  PHE GLU GLY TYR VAL TRP GLU ILE ILE THR LYS ARG GLU          
SEQRES  39 B  540  VAL SER PRO GLU ILE PHE LEU GLU GLU SER SER PHE MET          
SEQRES  40 B  540  LYS TRP TRP LYS GLU TYR LYS LYS ILE LYS GLY PHE ASN          
SEQRES  41 B  540  SER SER TYR LEU THR GLU PHE MET ASN THR ARG LYS TYR          
SEQRES  42 B  540  GLU SER TYR GLY LYS SER GLN                                  
HET    BGC  A 701      12                                                       
HET    IPA  A 702       4                                                       
HET    IPA  A 703       4                                                       
HET    EPE  B 601      15                                                       
HET    IPA  B 602       4                                                       
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM     IPA ISOPROPYL ALCOHOL                                                
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETSYN     IPA 2-PROPANOL                                                       
HETSYN     EPE HEPES                                                            
FORMUL   3  BGC    C6 H12 O6                                                    
FORMUL   4  IPA    3(C3 H8 O)                                                   
FORMUL   6  EPE    C8 H18 N2 O4 S                                               
FORMUL   8  HOH   *302(H2 O)                                                    
HELIX    1   1 PHE A    3  GLY A    8  1                                   6    
HELIX    2   2 ASN A   10  ALA A   24  1                                  15    
HELIX    3   3 TYR A   25  THR A   27  5                                   3    
HELIX    4   4 SER A   48  PHE A   52  5                                   5    
HELIX    5   5 GLU A   87  ASP A   98  1                                  12    
HELIX    6   6 PRO A   99  THR A  101  5                                   3    
HELIX    7   7 SER A  102  SER A  113  1                                  12    
HELIX    8   8 SER A  123  TYR A  140  1                                  18    
HELIX    9   9 PHE A  141  ASN A  144  5                                   4    
HELIX   10  10 ASP A  163  GLU A  173  1                                  11    
HELIX   11  11 TRP A  175  ARG A  177  5                                   3    
HELIX   12  12 ILE A  188  ALA A  195  5                                   8    
HELIX   13  13 THR A  203  ASP A  212  1                                  10    
HELIX   14  14 SER A  221  THR A  248  1                                  28    
HELIX   15  15 ALA A  251  SER A  259  1                                   9    
HELIX   16  16 SER A  260  LEU A  262  5                                   3    
HELIX   17  17 ASN A  286  THR A  297  1                                  12    
HELIX   18  18 LEU A  308  ASP A  316  1                                   9    
HELIX   19  19 SER A  319  SER A  326  1                                   8    
HELIX   20  20 MET A  327  LYS A  330  5                                   4    
HELIX   21  21 ASP A  336  GLU A  338  5                                   3    
HELIX   22  22 ILE A  341  LEU A  348  1                                   8    
HELIX   23  23 SER A  351  GLN A  380  1                                  30    
HELIX   24  24 GLN A  381  GLU A  394  1                                  14    
HELIX   25  25 GLU A  394  HIS A  402  1                                   9    
HELIX   26  26 ASN A  404  SER A  413  1                                  10    
HELIX   27  27 GLU A  415  LYS A  441  1                                  27    
HELIX   28  28 GLU A  447  GLY A  450  5                                   4    
HELIX   29  29 ASP A  451  HIS A  476  1                                  26    
HELIX   30  30 LEU A  477  THR A  482  1                                   6    
HELIX   31  31 PRO A  484  GLY A  489  1                                   6    
HELIX   32  32 PRO A  491  LYS A  507  1                                  17    
HELIX   33  33 PRO A  508  GLY A  510  5                                   3    
HELIX   34  34 ILE A  512  GLY A  523  1                                  12    
HELIX   35  35 GLN A  529  LEU A  537  1                                   9    
HELIX   36  36 SER A  540  SER A  546  5                                   7    
HELIX   37  37 CYS A  547  LYS A  556  1                                  10    
HELIX   38  38 VAL A  563  ALA A  580  1                                  18    
HELIX   39  39 SER A  593  THR A  601  1                                   9    
HELIX   40  40 PRO A  603  HIS A  609  1                                   7    
HELIX   41  41 LEU A  612  MET A  616  5                                   5    
HELIX   42  42 SER B    3  SER B   19  1                                  17    
HELIX   43  43 GLY B   20  ASN B   34  1                                  15    
HELIX   44  44 CYS B   76  SER B   80  5                                   5    
HELIX   45  45 PHE B   95  CYS B   99  5                                   5    
HELIX   46  46 THR B  110  SER B  118  1                                   9    
HELIX   47  47 ALA B  119  SER B  136  1                                  18    
HELIX   48  48 ALA B  146  LEU B  160  1                                  15    
HELIX   49  49 ALA B  183  GLU B  190  1                                   8    
HELIX   50  50 ASN B  191  SER B  196  5                                   6    
HELIX   51  51 ASP B  232  ASN B  241  1                                  10    
HELIX   52  52 ASP B  250  LEU B  263  1                                  14    
HELIX   53  53 PRO B  272  ASN B  287  1                                  16    
HELIX   54  54 PHE B  294  VAL B  317  1                                  24    
HELIX   55  55 GLY B  320  PHE B  331  1                                  12    
HELIX   56  56 LYS B  334  HIS B  343  1                                  10    
HELIX   57  57 HIS B  343  ARG B  362  1                                  20    
HELIX   58  58 PRO B  363  PHE B  374  1                                  12    
HELIX   59  59 PHE B  374  GLU B  396  1                                  23    
HELIX   60  60 GLU B  400  GLY B  405  1                                   6    
HELIX   61  61 SER B  407  GLY B  418  1                                  12    
HELIX   62  62 GLU B  420  CYS B  429  1                                  10    
HELIX   63  63 CYS B  443  THR B  461  1                                  19    
HELIX   64  64 ARG B  465  LYS B  489  1                                  25    
HELIX   65  65 SER B  493  LEU B  498  5                                   6    
HELIX   66  66 SER B  501  GLY B  515  1                                  15    
HELIX   67  67 SER B  519  THR B  527  1                                   9    
HELIX   68  68 ARG B  528  TYR B  533  5                                   6    
SHEET    1   A 8 TYR A  30  ALA A  35  0                                        
SHEET    2   A 8 VAL A  38  PHE A  43 -1  O  ALA A  42   N  HIS A  31           
SHEET    3   A 8 GLN A 116  HIS A 122  1  O  VAL A 118   N  PHE A  41           
SHEET    4   A 8 ARG A 152  PHE A 156  1  O  ARG A 152   N  PHE A 119           
SHEET    5   A 8 PHE A 179  THR A 184  1  O  VAL A 180   N  CYS A 153           
SHEET    6   A 8 THR A 272  SER A 276  1  O  VAL A 274   N  ASN A 181           
SHEET    7   A 8 ARG A 280  VAL A 284 -1  O  VAL A 284   N  PHE A 273           
SHEET    8   A 8 LEU A 331  HIS A 334  1  O  LEU A 331   N  LEU A 281           
SHEET    1   B 2 GLU A  63  LYS A  65  0                                        
SHEET    2   B 2 THR A  84  ASN A  86 -1  O  VAL A  85   N  ILE A  64           
SHEET    1   C 7 GLU B  56  ARG B  61  0                                        
SHEET    2   C 7 THR B  66  SER B  71 -1  O  LEU B  67   N  HIS B  60           
SHEET    3   C 7 VAL B 140  ALA B 145  1  O  THR B 143   N  PHE B  70           
SHEET    4   C 7 LEU B 171  PHE B 175  1  O  LEU B 171   N  ILE B 142           
SHEET    5   C 7 PHE B 198  SER B 203  1  O  LEU B 199   N  CYS B 172           
SHEET    6   C 7 THR B 218  PHE B 223  1  O  THR B 218   N  HIS B 200           
SHEET    7   C 7 GLY B 226  ILE B 230 -1  O  GLY B 226   N  PHE B 223           
SHEET    1   D 2 SER B  83  HIS B  87  0                                        
SHEET    2   D 2 SER B 105  HIS B 109 -1  O  PHE B 106   N  LEU B  86           
SHEET    1   E 2 GLY B 181  ASP B 182  0                                        
SHEET    2   E 2 PHE B 213  LYS B 214 -1  O  LYS B 214   N  GLY B 181           
SITE     1 AC1  7 ASN A 285  ASP A 446  HOH A 835  HOH A 909                    
SITE     2 AC1  7 HOH A 932  HOH A 934  HOH A 938                               
SITE     1 AC2  1 TYR A  25                                                     
SITE     1 AC3  2 LYS A 487  ARG A 488                                          
SITE     1 AC4  9 GLU B 480  GLY B 481  TRP B 484  TYR B 510                    
SITE     2 AC4  9 ASN B 517  SER B 518  SER B 519  TYR B 520                    
SITE     3 AC4  9 LEU B 521                                                     
SITE     1 AC5  4 THR B 403  THR B 404  GLY B 405  ARG B 406                    
CRYST1  112.586  113.643  125.386  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008882  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008799  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007975        0.00000                         
TER    5025      ILE A 620                                                      
TER    9299      GLN B 537                                                      
MASTER      446    0    5   68   21    0    8    6 9618    2   39   91          
END                                                                             

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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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