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LongText Report for: 6i8g-pdb

Name Class
6i8g-pdb
HEADER    IMMUNE SYSTEM                           20-NOV-18   6I8G              
TITLE     STRUCTURE OF THE PLANT IMMUNE SIGNALING NODE EDS1 (ENHANCED DISEASE   
TITLE    2 SUSCEPTIBILITY 1) IN COMPLEX WITH NANOBODY ENB73                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN EDS1L;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ENHANCED DISEASE SUSCEPTIBILITY 1-LIKE;                     
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: EDS1-SPECIFIC NANOBODY;                                    
COMPND   8 CHAIN: B;                                                            
COMPND   9 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: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: LAMA GLAMA;                                     
SOURCE  10 ORGANISM_TAXID: 9844;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ENHANCED DISEASE SUSCEPTIBILITY 1, PLANT INNATE IMMUNE SYSTEM,        
KEYWDS   2 ALPHA/BETA HYDROLASE FOLD, NANOBODY, IMMUNE SYSTEM                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.NIEFIND,M.VOSS,C.TOELZER                                            
REVDAT   1   02-OCT-19 6I8G    0                                                
JRNL        AUTH   M.VOSS,C.TOELZER,D.D.BHANDARI,J.E.PARKER,K.NIEFIND           
JRNL        TITL   ARABIDOPSIS IMMUNITY REGULATOR EDS1 IN A PAD4/SAG101-UNBOUND 
JRNL        TITL 2 FORM IS A MONOMER WITH AN INHERENTLY INACTIVE CONFORMATION.  
JRNL        REF    J.STRUCT.BIOL.                             2019              
JRNL        REFN                   ESSN 1095-8657                               
JRNL        PMID   31550533                                                     
JRNL        DOI    10.1016/J.JSB.2019.09.007                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.WAGNER,J.STUTTMANN,S.RIETZ,R.GUEROIS,E.BRUNSTEIN,J.BAUTOR, 
REMARK   1  AUTH 2 K.NIEFIND,J.E.PARKER                                         
REMARK   1  TITL   STRUCTURAL BASIS FOR SIGNALING BY EXCLUSIVE EDS1 HETEROMERIC 
REMARK   1  TITL 2 COMPLEXES WITH SAG101 OR PAD4 IN PLANT INNATE IMMUNITY.      
REMARK   1  REF    CELL HOST MICROBE             V.  14   619 2013              
REMARK   1  REFN                   ESSN 1934-6069                               
REMARK   1  PMID   24331460                                                     
REMARK   1  DOI    10.1016/J.CHOM.2013.11.006                                   
REMARK   1 REFERENCE 2                                                          
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  REF  2 STRUCT. BIOL. CRYST. COMMUN.                                 
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  PMID   21301097                                                     
REMARK   1  DOI    10.1107/S1744309110051249                                    
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   S.RIETZ,A.STAMM,S.MALONEK,S.WAGNER,D.BECKER,                 
REMARK   1  AUTH 2 N.MEDINA-ESCOBAR,A.C.VLOT,B.J.FEYS,K.NIEFIND,J.E.PARKER      
REMARK   1  TITL   DIFFERENT ROLES OF ENHANCED DISEASE SUSCEPTIBILITY1 (EDS1)   
REMARK   1  TITL 2 BOUND TO AND DISSOCIATED FROM PHYTOALEXIN DEFICIENT4 (PAD4)  
REMARK   1  TITL 3 IN ARABIDOPSIS IMMUNITY.                                     
REMARK   1  REF    NEW PHYTOL.                   V. 191   107 2011              
REMARK   1  REFN                   ISSN 1469-8137                               
REMARK   1  PMID   21434927                                                     
REMARK   1  DOI    10.1111/J.1469-8137.2011.03675.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.34 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.14_3260: ???)                              
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 52.57                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 71.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 31537                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.110                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1295                            
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 52.5833 -  4.8745    1.00     4848   202  0.1537 0.1594        
REMARK   3     2  4.8745 -  3.8694    0.96     4569   199  0.1437 0.1845        
REMARK   3     3  3.8694 -  3.3804    0.98     4620   199  0.1930 0.2442        
REMARK   3     4  3.3804 -  3.0713    0.99     4663   198  0.2350 0.2695        
REMARK   3     5  3.0713 -  2.8512    0.94     4461   182  0.2736 0.2879        
REMARK   3     6  2.8512 -  2.6831    0.73     3433   157  0.2885 0.2944        
REMARK   3     7  2.6831 -  2.5487    0.51     2407    91  0.2871 0.3319        
REMARK   3     8  2.5487 -  2.4378    0.22      998    63  0.3096 0.3280        
REMARK   3     9  2.4378 -  2.3440    0.05      243     4  0.2912 0.3445        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.260            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.740           
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      :  0.002           6138                                  
REMARK   3   ANGLE     :  0.522           8302                                  
REMARK   3   CHIRALITY :  0.040            890                                  
REMARK   3   PLANARITY :  0.004           1079                                  
REMARK   3   DIHEDRAL  : 15.396           3680                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 211 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): 140.9226 -30.7636 104.9686              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2258 T22:   0.1315                                     
REMARK   3      T33:   0.2307 T12:  -0.0329                                     
REMARK   3      T13:  -0.0081 T23:  -0.0058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9118 L22:   1.7859                                     
REMARK   3      L33:   2.5561 L12:  -0.7885                                     
REMARK   3      L13:  -0.5838 L23:   0.4871                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0879 S12:   0.0635 S13:  -0.2017                       
REMARK   3      S21:   0.0921 S22:   0.0762 S23:   0.0262                       
REMARK   3      S31:   0.3075 S32:   0.0365 S33:  -0.0083                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 212 THROUGH 325 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 159.5783 -31.2154 110.2968              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3015 T22:   0.4677                                     
REMARK   3      T33:   0.3901 T12:   0.0939                                     
REMARK   3      T13:  -0.0714 T23:  -0.0769                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3673 L22:   2.8686                                     
REMARK   3      L33:   0.8199 L12:   0.2222                                     
REMARK   3      L13:  -0.5415 L23:   0.5868                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1090 S12:  -0.1631 S13:  -0.1106                       
REMARK   3      S21:   0.1902 S22:   0.2694 S23:  -0.5227                       
REMARK   3      S31:   0.1425 S32:   0.6417 S33:   0.0338                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 326 THROUGH 619 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 143.6273 -15.8264  72.8895              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2687 T22:   0.4344                                     
REMARK   3      T33:   0.4483 T12:  -0.0052                                     
REMARK   3      T13:   0.0731 T23:   0.0932                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0865 L22:   0.7598                                     
REMARK   3      L33:   3.4215 L12:  -0.0713                                     
REMARK   3      L13:   1.1129 L23:  -0.0941                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0217 S12:   0.6796 S13:   0.3460                       
REMARK   3      S21:  -0.1395 S22:  -0.0432 S23:   0.0105                       
REMARK   3      S31:  -0.0703 S32:   0.3494 S33:  -0.0157                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 17 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): 136.9273 -32.0743 148.3217              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6670 T22:   0.2444                                     
REMARK   3      T33:   0.2667 T12:   0.0049                                     
REMARK   3      T13:   0.0178 T23:  -0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2691 L22:   0.0522                                     
REMARK   3      L33:   0.0945 L12:  -0.1422                                     
REMARK   3      L13:   0.0495 L23:  -0.0088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2600 S12:  -0.0924 S13:   0.2615                       
REMARK   3      S21:   0.0540 S22:  -0.2594 S23:   0.1121                       
REMARK   3      S31:  -0.6005 S32:   0.0581 S33:   0.0009                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 32 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): 134.1452 -31.9076 136.3049              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5062 T22:   0.1896                                     
REMARK   3      T33:   0.3694 T12:   0.0473                                     
REMARK   3      T13:  -0.0835 T23:  -0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1465 L22:   0.2310                                     
REMARK   3      L33:   1.5826 L12:   0.0595                                     
REMARK   3      L13:   0.2097 L23:  -0.4157                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2272 S12:  -0.1322 S13:  -0.0166                       
REMARK   3      S21:  -0.1027 S22:   0.1823 S23:   0.4133                       
REMARK   3      S31:  -0.5762 S32:  -0.4898 S33:   0.0039                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 33 THROUGH 51 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): 146.2132 -37.1055 143.5073              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5125 T22:   0.3568                                     
REMARK   3      T33:   0.3160 T12:  -0.1584                                     
REMARK   3      T13:  -0.0441 T23:  -0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3401 L22:   0.0007                                     
REMARK   3      L33:   0.8022 L12:  -0.0121                                     
REMARK   3      L13:  -0.5276 L23:   0.0178                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1772 S12:  -0.3523 S13:  -0.0150                       
REMARK   3      S21:   0.2235 S22:  -0.1051 S23:  -0.2543                       
REMARK   3      S31:  -0.4790 S32:   0.5970 S33:  -0.0168                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 52 THROUGH 60 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): 138.5526 -43.3439 131.3518              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5630 T22:   0.2734                                     
REMARK   3      T33:   0.4247 T12:  -0.0459                                     
REMARK   3      T13:  -0.0782 T23:   0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1034 L22:   0.0036                                     
REMARK   3      L33:   0.7281 L12:  -0.0026                                     
REMARK   3      L13:   0.0096 L23:  -0.0558                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0193 S12:   0.1789 S13:  -0.5034                       
REMARK   3      S21:  -0.2919 S22:   0.4691 S23:   0.2708                       
REMARK   3      S31:   0.3739 S32:   0.2311 S33:   0.0100                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 61 THROUGH 83 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): 134.6268 -40.6225 142.0638              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4926 T22:   0.2451                                     
REMARK   3      T33:   0.3376 T12:  -0.0063                                     
REMARK   3      T13:  -0.0463 T23:   0.0724                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1560 L22:   0.1467                                     
REMARK   3      L33:   0.1866 L12:   0.1288                                     
REMARK   3      L13:  -0.0674 L23:  -0.0678                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1690 S12:  -0.0662 S13:   0.0200                       
REMARK   3      S21:  -0.4179 S22:  -0.1698 S23:   0.2629                       
REMARK   3      S31:  -0.2354 S32:  -0.0681 S33:  -0.0003                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 84 THROUGH 107 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 144.2069 -38.3669 142.9939              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4340 T22:   0.1997                                     
REMARK   3      T33:   0.3223 T12:  -0.0236                                     
REMARK   3      T13:   0.0131 T23:  -0.0155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3183 L22:   0.0731                                     
REMARK   3      L33:   0.3391 L12:   0.1230                                     
REMARK   3      L13:  -0.2100 L23:  -0.1793                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4382 S12:  -0.1260 S13:   0.1176                       
REMARK   3      S21:  -0.1040 S22:  -0.3012 S23:   0.0897                       
REMARK   3      S31:  -0.4215 S32:   0.2891 S33:   0.0134                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 108 THROUGH 126 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 144.2898 -33.1050 146.5476              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6282 T22:   0.2967                                     
REMARK   3      T33:   0.3872 T12:  -0.0870                                     
REMARK   3      T13:   0.0015 T23:   0.0167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2941 L22:   0.2068                                     
REMARK   3      L33:   0.2693 L12:  -0.1419                                     
REMARK   3      L13:   0.0626 L23:   0.1186                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2556 S12:  -0.3395 S13:   0.4651                       
REMARK   3      S21:   0.1362 S22:  -0.1329 S23:  -0.2885                       
REMARK   3      S31:  -0.3875 S32:   0.1101 S33:   0.0218                       
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 6I8G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-NOV-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200012027.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JAN-18                          
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                       : MASSIF-3                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.967700                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 4M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JAN 26, 2018,          
REMARK 200                                   AUTOPROC                           
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS, AUTOPROC VERSION 1.0.5,   
REMARK 200                                   STARANISO                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31550                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.344                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 83.773                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 71.1                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.11700                            
REMARK 200  R SYM                      (I) : 0.11700                            
REMARK 200   FOR THE DATA SET  : 8.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 15.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.87000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.87000                            
REMARK 200   FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4NFU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR COMPOSITION: 17.5 % (W/V)      
REMARK 280  PEG3350, 0.2 M SODIUM CITRATE, 0.1 M BIS-TRIS BUFFER, PH 8.5;       
REMARK 280  PROTEIN STOCK SOLUTION: 2.8 MG/ML PROTEIN IN 50 MM SODIUM           
REMARK 280  CHLORIDE, 1 % (V/V) GLYCEROLE, 1MM DTT, 50 MM HEPES, PH 8.0;        
REMARK 280  DROP COMPOSITION: 1 MIKROLITER PROTEIN STOCK SOLUTION + 1           
REMARK 280  MIKROLITER RESERVOIR SOLUTION; CRYSTALS WERE CRYOPROTECTED IN       
REMARK 280  17.5 % (W/V) PEG3350, 20 % (V/V) ETHYLENE GLYCOL, 0.2 M SODIUM      
REMARK 280  CITRATE, 0.1 M BIS-TRIS BUFFER, PH 8.5., VAPOR DIFFUSION,           
REMARK 280  SITTING DROP, TEMPERATURE 277.15K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       88.75200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.11600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       88.75200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.11600            
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: 1540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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     1                                                      
REMARK 465     ILE A   620                                                      
REMARK 465     THR A   621                                                      
REMARK 465     ASP A   622                                                      
REMARK 465     THR A   623                                                      
REMARK 465     LEU A   624                                                      
REMARK 465     GLU A   625                                                      
REMARK 465     HIS A   626                                                      
REMARK 465     HIS A   627                                                      
REMARK 465     HIS A   628                                                      
REMARK 465     HIS A   629                                                      
REMARK 465     HIS A   630                                                      
REMARK 465     HIS A   631                                                      
REMARK 465     ALA B   131                                                      
REMARK 465     TYR B   132                                                      
REMARK 465     PRO B   133                                                      
REMARK 465     TYR B   134                                                      
REMARK 465     ASP B   135                                                      
REMARK 465     VAL B   136                                                      
REMARK 465     PRO B   137                                                      
REMARK 465     ASP B   138                                                      
REMARK 465     TYR B   139                                                      
REMARK 465     GLY B   140                                                      
REMARK 465     SER B   141                                                      
REMARK 465     HIS B   142                                                      
REMARK 465     HIS B   143                                                      
REMARK 465     HIS B   144                                                      
REMARK 465     HIS B   145                                                      
REMARK 465     HIS B   146                                                      
REMARK 465     HIS B   147                                                      
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      -62.91     67.79                                   
REMARK 500    SER A 123     -136.47     62.70                                   
REMARK 500    TYR A 140      -58.05   -124.04                                   
REMARK 500    VAL A 218       36.52    -89.21                                   
REMARK 500    GLN A 219       73.18     51.51                                   
REMARK 500    GLU A 220     -108.10    -77.41                                   
REMARK 500    THR A 248        6.52   -165.18                                   
REMARK 500    ALA A 251     -104.02     55.10                                   
REMARK 500    ALA A 253      -75.67   -117.14                                   
REMARK 500    THR A 257     -154.71    -74.15                                   
REMARK 500    LEU A 258      -14.64     67.02                                   
REMARK 500    PHE A 261      -65.27    -96.96                                   
REMARK 500    LEU A 262       68.70   -106.12                                   
REMARK 500    CYS A 298       31.49    -96.07                                   
REMARK 500    SER A 301      -37.84   -130.34                                   
REMARK 500    VAL B 110       70.86     53.57                                   
REMARK 500    SER B 128     -118.04    -75.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6I8G A    1   623  UNP    Q9XF23   EDS1L_ARATH      1    623             
DBREF  6I8G B    1   147  PDB    6I8G     6I8G             1    147             
SEQADV 6I8G LEU A  624  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6I8G GLU A  625  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6I8G HIS A  626  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6I8G HIS A  627  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6I8G HIS A  628  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6I8G HIS A  629  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6I8G HIS A  630  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6I8G HIS A  631  UNP  Q9XF23              EXPRESSION TAG                 
SEQRES   1 A  631  MET ALA PHE GLU ALA LEU THR GLY ILE ASN GLY ASP LEU          
SEQRES   2 A  631  ILE THR ARG SER TRP SER ALA SER LYS GLN ALA TYR LEU          
SEQRES   3 A  631  THR GLU ARG TYR HIS LYS GLU GLU ALA GLY ALA VAL VAL          
SEQRES   4 A  631  ILE PHE ALA PHE GLN PRO SER PHE SER GLU LYS ASP PHE          
SEQRES   5 A  631  PHE ASP PRO ASP ASN LYS SER SER PHE GLY GLU ILE LYS          
SEQRES   6 A  631  LEU ASN ARG VAL GLN PHE PRO CYS MET ARG LYS ILE GLY          
SEQRES   7 A  631  LYS GLY ASP VAL ALA THR VAL ASN GLU ALA PHE LEU LYS          
SEQRES   8 A  631  ASN LEU GLU ALA VAL ILE ASP PRO ARG THR SER PHE GLN          
SEQRES   9 A  631  ALA SER VAL GLU MET ALA VAL ARG SER ARG LYS GLN ILE          
SEQRES  10 A  631  VAL PHE THR GLY HIS SER SER GLY GLY ALA THR ALA ILE          
SEQRES  11 A  631  LEU ALA THR VAL TRP TYR LEU GLU LYS TYR PHE ILE ARG          
SEQRES  12 A  631  ASN PRO ASN VAL TYR LEU GLU PRO ARG CYS VAL THR PHE          
SEQRES  13 A  631  GLY ALA PRO LEU VAL GLY ASP SER ILE PHE SER HIS ALA          
SEQRES  14 A  631  LEU GLY ARG GLU LYS TRP SER ARG PHE PHE VAL ASN PHE          
SEQRES  15 A  631  VAL THR ARG PHE ASP ILE VAL PRO ARG ILE THR LEU ALA          
SEQRES  16 A  631  ARG LYS ALA SER VAL GLU GLU THR LEU PRO HIS VAL LEU          
SEQRES  17 A  631  ALA GLN LEU ASP PRO ARG ASN SER SER VAL GLN GLU SER          
SEQRES  18 A  631  GLU GLN ARG ILE THR GLU PHE TYR THR SER VAL MET ARG          
SEQRES  19 A  631  ASP THR SER THR VAL ALA ASN GLN ALA VAL CYS GLU LEU          
SEQRES  20 A  631  THR GLY SER ALA GLU ALA ILE LEU GLU THR LEU SER SER          
SEQRES  21 A  631  PHE LEU GLU LEU SER PRO TYR ARG PRO ALA GLY THR PHE          
SEQRES  22 A  631  VAL PHE SER THR GLU LYS ARG LEU VAL ALA VAL ASN ASN          
SEQRES  23 A  631  SER ASP ALA ILE LEU GLN MET LEU PHE TYR THR CYS GLN          
SEQRES  24 A  631  ALA SER ASP GLU GLN GLU TRP SER LEU ILE PRO PHE ARG          
SEQRES  25 A  631  SER ILE ARG ASP HIS HIS SER TYR GLU GLU LEU VAL GLN          
SEQRES  26 A  631  SER MET GLY MET LYS LEU PHE ASN HIS LEU ASP GLY GLU          
SEQRES  27 A  631  ASN SER ILE GLU SER SER LEU ASN ASP LEU GLY VAL SER          
SEQRES  28 A  631  THR ARG GLY ARG GLN TYR VAL GLN ALA ALA LEU GLU GLU          
SEQRES  29 A  631  GLU LYS LYS ARG VAL GLU ASN GLN LYS LYS ILE ILE GLN          
SEQRES  30 A  631  VAL ILE GLN GLN GLU ARG PHE LEU LYS LYS LEU ALA TRP          
SEQRES  31 A  631  ILE GLU ASP GLU TYR LYS PRO LYS CYS GLN ALA HIS LYS          
SEQRES  32 A  631  ASN GLY TYR TYR ASP SER PHE LYS VAL SER ASN GLU GLU          
SEQRES  33 A  631  ASN ASP PHE LYS ALA ASN VAL LYS ARG ALA GLU LEU ALA          
SEQRES  34 A  631  GLY VAL PHE ASP GLU VAL LEU GLY LEU LEU LYS LYS CYS          
SEQRES  35 A  631  GLN LEU PRO ASP GLU PHE GLU GLY ASP ILE ASP TRP ILE          
SEQRES  36 A  631  LYS LEU ALA THR ARG TYR ARG ARG LEU VAL GLU PRO LEU          
SEQRES  37 A  631  ASP ILE ALA ASN TYR HIS ARG HIS LEU LYS ASN GLU ASP          
SEQRES  38 A  631  THR GLY PRO TYR MET LYS ARG GLY ARG PRO THR ARG TYR          
SEQRES  39 A  631  ILE TYR ALA GLN ARG GLY TYR GLU HIS HIS ILE LEU LYS          
SEQRES  40 A  631  PRO ASN GLY MET ILE ALA GLU ASP VAL PHE TRP ASN LYS          
SEQRES  41 A  631  VAL ASN GLY LEU ASN LEU GLY LEU GLN LEU GLU GLU ILE          
SEQRES  42 A  631  GLN GLU THR LEU LYS ASN SER GLY SER GLU CYS GLY SER          
SEQRES  43 A  631  CYS PHE TRP ALA GLU VAL GLU GLU LEU LYS GLY LYS PRO          
SEQRES  44 A  631  TYR GLU GLU VAL GLU VAL ARG VAL LYS THR LEU GLU GLY          
SEQRES  45 A  631  MET LEU ARG GLU TRP ILE THR ALA GLY GLU VAL ASP GLU          
SEQRES  46 A  631  LYS GLU ILE PHE LEU GLU GLY SER THR PHE ARG LYS TRP          
SEQRES  47 A  631  TRP ILE THR LEU PRO LYS ASN HIS LYS SER HIS SER PRO          
SEQRES  48 A  631  LEU ARG ASP TYR MET MET ASP GLU ILE THR ASP THR LEU          
SEQRES  49 A  631  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 B  143  GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 B  143  ALA GLY GLY SER LEU ARG LEU SER CYS ALA THR SER THR          
SEQRES   3 B  143  HIS THR ALA GLY GLN TYR THR MET ALA TRP PHE ARG GLN          
SEQRES   4 B  143  ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA VAL LEU ARG          
SEQRES   5 B  143  TRP SER ASP TYR SER THR ASP TYR ALA ASN SER VAL LYS          
SEQRES   6 B  143  ASN ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR          
SEQRES   7 B  143  VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR          
SEQRES   8 B  143  ALA VAL TYR TYR CYS ALA ALA GLY TRP PRO VAL LYS VAL          
SEQRES   9 B  143  ILE SER SER ALA ASP GLU TYR ILE ASN TRP GLY GLN GLY          
SEQRES  10 B  143  THR GLN VAL THR VAL SER SER ALA ALA ALA TYR PRO TYR          
SEQRES  11 B  143  ASP VAL PRO ASP TYR GLY SER HIS HIS HIS HIS HIS HIS          
FORMUL   3  HOH   *169(H2 O)                                                    
HELIX    1 AA1 ALA A    2  GLY A    8  1                                   7    
HELIX    2 AA2 ASN A   10  ALA A   24  1                                  15    
HELIX    3 AA3 TYR A   25  THR A   27  5                                   3    
HELIX    4 AA4 SER A   48  PHE A   52  5                                   5    
HELIX    5 AA5 GLU A   87  ASP A   98  1                                  12    
HELIX    6 AA6 PRO A   99  THR A  101  5                                   3    
HELIX    7 AA7 SER A  102  SER A  113  1                                  12    
HELIX    8 AA8 SER A  123  TYR A  140  1                                  18    
HELIX    9 AA9 ASP A  163  GLU A  173  1                                  11    
HELIX   10 AB1 TRP A  175  ARG A  177  5                                   3    
HELIX   11 AB2 ILE A  188  ALA A  195  5                                   8    
HELIX   12 AB3 ARG A  196  GLU A  201  1                                   6    
HELIX   13 AB4 THR A  203  ASP A  212  1                                  10    
HELIX   14 AB5 SER A  221  GLY A  249  1                                  29    
HELIX   15 AB6 ASN A  286  THR A  297  1                                  12    
HELIX   16 AB7 LEU A  308  ASP A  316  1                                   9    
HELIX   17 AB8 SER A  319  SER A  326  1                                   8    
HELIX   18 AB9 ILE A  341  LEU A  348  1                                   8    
HELIX   19 AC1 SER A  351  GLN A  381  1                                  31    
HELIX   20 AC2 GLN A  381  GLU A  394  1                                  14    
HELIX   21 AC3 GLU A  394  HIS A  402  1                                   9    
HELIX   22 AC4 ASN A  404  SER A  413  1                                  10    
HELIX   23 AC5 GLU A  415  LYS A  441  1                                  27    
HELIX   24 AC6 GLU A  447  GLY A  450  5                                   4    
HELIX   25 AC7 ASP A  451  HIS A  476  1                                  26    
HELIX   26 AC8 LEU A  477  THR A  482  1                                   6    
HELIX   27 AC9 PRO A  484  GLY A  489  1                                   6    
HELIX   28 AD1 PRO A  491  LYS A  507  1                                  17    
HELIX   29 AD2 PRO A  508  GLY A  510  5                                   3    
HELIX   30 AD3 ILE A  512  LEU A  524  1                                  13    
HELIX   31 AD4 GLN A  529  LEU A  537  1                                   9    
HELIX   32 AD5 SER A  540  SER A  546  5                                   7    
HELIX   33 AD6 CYS A  547  LYS A  556  1                                  10    
HELIX   34 AD7 VAL A  563  ALA A  580  1                                  18    
HELIX   35 AD8 SER A  593  THR A  601  1                                   9    
HELIX   36 AD9 PRO A  603  HIS A  609  1                                   7    
HELIX   37 AE1 LEU A  612  MET A  616  5                                   5    
HELIX   38 AE2 LYS B   95  THR B   99  5                                   5    
HELIX   39 AE3 SER B  112A ASP B  113  5                                   3    
SHEET    1 AA1 8 TYR A  30  ALA A  35  0                                        
SHEET    2 AA1 8 VAL A  38  PHE A  43 -1  O  ILE A  40   N  GLU A  33           
SHEET    3 AA1 8 GLN A 116  HIS A 122  1  O  VAL A 118   N  PHE A  41           
SHEET    4 AA1 8 PRO A 151  PHE A 156  1  O  ARG A 152   N  PHE A 119           
SHEET    5 AA1 8 PHE A 179  THR A 184  1  O  PHE A 182   N  THR A 155           
SHEET    6 AA1 8 THR A 272  SER A 276  1  O  VAL A 274   N  ASN A 181           
SHEET    7 AA1 8 ARG A 280  VAL A 284 -1  O  VAL A 284   N  PHE A 273           
SHEET    8 AA1 8 LEU A 331  HIS A 334  1  O  LEU A 331   N  LEU A 281           
SHEET    1 AA2 2 GLU A  63  LYS A  65  0                                        
SHEET    2 AA2 2 THR A  84  ASN A  86 -1  O  VAL A  85   N  ILE A  64           
SHEET    1 AA3 4 LEU B   4  SER B   7  0                                        
SHEET    2 AA3 4 LEU B  19  THR B  25 -1  O  ALA B  24   N  GLN B   5           
SHEET    3 AA3 4 THR B  86  MET B  91 -1  O  MET B  91   N  LEU B  19           
SHEET    4 AA3 4 PHE B  76  ASP B  81 -1  N  THR B  77   O  GLN B  90           
SHEET    1 AA4 6 LEU B  12  GLN B  14  0                                        
SHEET    2 AA4 6 THR B 122  SER B 127  1  O  THR B 125   N  VAL B  13           
SHEET    3 AA4 6 ALA B 100  GLY B 107 -1  N  TYR B 102   O  THR B 122           
SHEET    4 AA4 6 THR B  38  GLN B  44 -1  N  GLN B  44   O  VAL B 101           
SHEET    5 AA4 6 GLU B  51  LEU B  56 -1  O  GLU B  51   N  ARG B  43           
SHEET    6 AA4 6 THR B  65  TYR B  67 -1  O  ASP B  66   N  VAL B  55           
SHEET    1 AA5 4 LEU B  12  GLN B  14  0                                        
SHEET    2 AA5 4 THR B 122  SER B 127  1  O  THR B 125   N  VAL B  13           
SHEET    3 AA5 4 ALA B 100  GLY B 107 -1  N  TYR B 102   O  THR B 122           
SHEET    4 AA5 4 TYR B 115  TRP B 118 -1  O  ASN B 117   N  ALA B 106           
SSBOND   1 CYS B   23    CYS B  104                          1555   1555  2.04  
CISPEP   1 TRP B  108    PRO B  109          0         0.78                     
CRYST1  177.504   68.232  105.273  90.00 123.44  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005634  0.000000  0.003721        0.00000                         
SCALE2      0.000000  0.014656  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011384        0.00000                         
TER    5030      GLU A 619                                                      
TER    6003      ALA B 130                                                      
MASTER      460    0    0   39   24    0    0    6 6149    2    2   60          
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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