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LongText Report for: 6q6z-pdb

Name Class
6q6z-pdb
HEADER    IMMUNE SYSTEM                           12-DEC-18   6Q6Z              
TITLE     STRUCTURE OF THE PLANT IMMUNE SIGNALING NODE EDS1 (ENHANCED DISEASE   
TITLE    2 SUSCEPTIBILITY 1) IN COMPLEX WITH NANOBODY ENB21                     
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_COMMON: LLAMA;                                              
SOURCE  11 ORGANISM_TAXID: 9844;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 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 6Q6Z    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.    3.48 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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.48                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 61.57                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 83.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 12593                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 766                             
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 61.5806 -  5.9418    1.00     2927   194  0.1786 0.2266        
REMARK   3     2  5.9418 -  4.7167    1.00     2806   198  0.2503 0.3130        
REMARK   3     3  4.7167 -  4.1207    1.00     2819   158  0.2487 0.2919        
REMARK   3     4  4.1207 -  3.7440    0.75     2052   152  0.3051 0.3304        
REMARK   3     5  3.7440 -  3.4756    0.43     1223    64  0.3321 0.3905        
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)     : 0.470            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.760           
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      :  0.003           6011                                  
REMARK   3   ANGLE     :  0.765           8120                                  
REMARK   3   CHIRALITY :  0.051            870                                  
REMARK   3   PLANARITY :  0.006           1054                                  
REMARK   3   DIHEDRAL  : 10.870           3599                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 13                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 211 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  32.5646 100.0089 156.1763              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0145 T22:   0.9341                                     
REMARK   3      T33:   1.6005 T12:   0.1177                                     
REMARK   3      T13:  -0.0445 T23:  -0.6269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2770 L22:   1.5414                                     
REMARK   3      L33:   2.1687 L12:  -0.0213                                     
REMARK   3      L13:  -0.1591 L23:  -1.1221                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1177 S12:  -0.1913 S13:   0.4521                       
REMARK   3      S21:   0.1464 S22:   0.3386 S23:  -0.8837                       
REMARK   3      S31:  -0.3541 S32:   0.5256 S33:   0.0065                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 212 THROUGH 337 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  13.8578 101.0102 160.9923              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1468 T22:   1.0736                                     
REMARK   3      T33:   0.9573 T12:   0.2814                                     
REMARK   3      T13:   0.1196 T23:  -0.3502                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6712 L22:   1.6625                                     
REMARK   3      L33:   0.9809 L12:   1.0238                                     
REMARK   3      L13:   0.0576 L23:  -0.4349                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1080 S12:   0.0775 S13:   0.2999                       
REMARK   3      S21:   0.4451 S22:   0.0222 S23:   0.5924                       
REMARK   3      S31:   0.1984 S32:  -0.4348 S33:  -0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 338 THROUGH 616 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  31.2739  77.8485 126.9279              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4544 T22:   1.0493                                     
REMARK   3      T33:   0.8662 T12:   0.2180                                     
REMARK   3      T13:   0.2693 T23:  -0.1854                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9026 L22:  -0.1484                                     
REMARK   3      L33:   2.0229 L12:   0.2474                                     
REMARK   3      L13:  -0.5823 L23:  -0.5068                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2480 S12:   0.1097 S13:   0.2581                       
REMARK   3      S21:  -0.4616 S22:   0.0112 S23:  -0.0762                       
REMARK   3      S31:   0.4819 S32:  -0.0510 S33:   0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 9 )                     
REMARK   3    ORIGIN FOR THE GROUP (A):  37.1244 120.7402 182.4673              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.5309 T22:   1.3930                                     
REMARK   3      T33:   1.9992 T12:   0.2204                                     
REMARK   3      T13:  -0.0340 T23:  -0.5581                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7280 L22:   0.0780                                     
REMARK   3      L33:   0.0927 L12:   0.2482                                     
REMARK   3      L13:  -0.2560 L23:  -0.0965                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3152 S12:  -0.6129 S13:   0.1594                       
REMARK   3      S21:  -1.2674 S22:  -0.1406 S23:  -0.5095                       
REMARK   3      S31:  -0.0080 S32:  -0.1301 S33:  -0.0335                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 11 THROUGH 24 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  31.7200 118.1624 198.9839              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9501 T22:   1.5952                                     
REMARK   3      T33:   1.9650 T12:   0.3793                                     
REMARK   3      T13:  -0.2633 T23:  -1.5134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7237 L22:   0.0521                                     
REMARK   3      L33:   1.0300 L12:  -0.0376                                     
REMARK   3      L13:  -0.7277 L23:  -0.1147                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5180 S12:  -0.5942 S13:   0.3277                       
REMARK   3      S21:  -0.2858 S22:  -0.3251 S23:   0.1926                       
REMARK   3      S31:  -0.3414 S32:   0.1773 S33:  -0.1225                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 25 THROUGH 37 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  30.8273 114.5026 175.0067              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.7322 T22:   2.1820                                     
REMARK   3      T33:   2.0128 T12:   0.9361                                     
REMARK   3      T13:  -0.4497 T23:  -0.7966                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0044 L22:   0.0006                                     
REMARK   3      L33:  -0.0008 L12:  -0.0050                                     
REMARK   3      L13:  -0.0036 L23:   0.0061                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0190 S12:   0.0374 S13:   1.6730                       
REMARK   3      S21:   0.2399 S22:   0.0861 S23:  -1.1077                       
REMARK   3      S31:  -0.1138 S32:  -0.0873 S33:   0.0001                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 38 THROUGH 44 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  35.4452 108.7204 188.9805              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.4145 T22:   0.4432                                     
REMARK   3      T33:   2.9790 T12:  -0.3248                                     
REMARK   3      T13:  -1.1978 T23:  -1.8891                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5057 L22:   0.1538                                     
REMARK   3      L33:   0.1915 L12:   0.1072                                     
REMARK   3      L13:  -0.1086 L23:  -0.0443                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1064 S12:   0.2325 S13:  -0.4373                       
REMARK   3      S21:   0.1548 S22:  -0.2448 S23:  -0.5274                       
REMARK   3      S31:   0.3325 S32:  -0.3291 S33:  -0.5298                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 45 THROUGH 57 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  38.2854 105.3231 192.5717              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9492 T22:   0.6929                                     
REMARK   3      T33:   2.4329 T12:   0.8834                                     
REMARK   3      T13:  -0.5735 T23:  -0.9654                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1730 L22:   4.0568                                     
REMARK   3      L33:   3.1342 L12:  -2.0345                                     
REMARK   3      L13:   0.0984 L23:  -1.5282                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7956 S12:  -0.3946 S13:  -0.2021                       
REMARK   3      S21:   0.9748 S22:   0.1329 S23:   0.1482                       
REMARK   3      S31:   0.0234 S32:   0.1507 S33:  -1.1370                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 58 THROUGH 75 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  25.8548 104.4948 191.4999              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7884 T22:   1.2475                                     
REMARK   3      T33:   2.3260 T12:   0.0619                                     
REMARK   3      T13:  -0.1836 T23:  -0.3811                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0796 L22:   0.0250                                     
REMARK   3      L33:   0.2722 L12:   0.0484                                     
REMARK   3      L13:   0.1631 L23:   0.1018                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6221 S12:   0.0502 S13:   0.0120                       
REMARK   3      S21:   0.1227 S22:  -1.1218 S23:   2.1831                       
REMARK   3      S31:  -0.0066 S32:   0.6901 S33:  -0.0127                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 76 THROUGH 81 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  24.6383 111.9316 190.2450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.3535 T22:   1.8424                                     
REMARK   3      T33:   2.2116 T12:  -0.6870                                     
REMARK   3      T13:   0.3573 T23:  -0.5639                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4172 L22:   0.0669                                     
REMARK   3      L33:   1.5972 L12:   0.0945                                     
REMARK   3      L13:  -0.5945 L23:   0.0414                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4622 S12:   0.9075 S13:   0.3634                       
REMARK   3      S21:   0.0627 S22:   0.6382 S23:   0.5917                       
REMARK   3      S31:  -0.3267 S32:  -0.1456 S33:   0.1356                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 82 THROUGH 99 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  29.5710 113.8062 195.2640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6865 T22:   1.2171                                     
REMARK   3      T33:   2.0525 T12:   0.1528                                     
REMARK   3      T13:  -0.1279 T23:  -0.6782                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0601 L22:   0.1931                                     
REMARK   3      L33:   0.6419 L12:  -0.0473                                     
REMARK   3      L13:   0.1758 L23:  -0.3112                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0912 S12:  -0.7937 S13:   0.6786                       
REMARK   3      S21:  -0.9230 S22:   0.0513 S23:  -0.7629                       
REMARK   3      S31:   0.4182 S32:  -0.6951 S33:   0.0100                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 100 THROUGH 105 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  38.7276 112.8192 191.3843              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0080 T22:   1.6076                                     
REMARK   3      T33:   1.9466 T12:  -0.1096                                     
REMARK   3      T13:  -1.0318 T23:  -1.3366                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0568 L22:   0.0228                                     
REMARK   3      L33:   0.5880 L12:  -0.0350                                     
REMARK   3      L13:  -0.1887 L23:   0.1208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2150 S12:  -0.1768 S13:   0.5010                       
REMARK   3      S21:  -0.4003 S22:   0.1733 S23:  -0.3873                       
REMARK   3      S31:   0.1514 S32:   0.0549 S33:   0.0966                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 106 THROUGH 130 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  39.2796 113.4153 191.1514              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6622 T22:   1.2791                                     
REMARK   3      T33:   1.8928 T12:   0.4108                                     
REMARK   3      T13:  -0.1930 T23:  -0.9672                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0845 L22:   0.0199                                     
REMARK   3      L33:   2.3417 L12:  -0.0156                                     
REMARK   3      L13:  -0.4363 L23:  -0.2455                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1037 S12:  -0.9329 S13:   0.2761                       
REMARK   3      S21:  -0.6273 S22:  -0.7150 S23:   0.1425                       
REMARK   3      S31:   0.7020 S32:   1.6101 S33:  -0.4307                       
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 6Q6Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-DEC-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200013395.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAR-17                          
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                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976254                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS XDS VERSION JAN 26, 2018,      
REMARK 200                                   AUTOPROC VERSION JAN 26, 2018      
REMARK 200  DATA SCALING SOFTWARE          : AUTOPROC AUTOPROC (VERSION         
REMARK 200                                   1.0.5), AIMLESS (VERSION 0.7.3),   
REMARK 200                                   CCP4 7.0.065, STARANISO            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12634                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.473                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 76.586                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.8                               
REMARK 200  DATA REDUNDANCY                : 19.50                              
REMARK 200  R MERGE                    (I) : 0.18200                            
REMARK 200  R SYM                      (I) : 0.18200                            
REMARK 200   FOR THE DATA SET  : 12.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.47                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.65                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 57.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 20.10                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4NFU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION CONDITIONS: RESERVOIR    
REMARK 280  COMPOSITION (CONDITION A11 OF MORPHEUS SCREEN): 20.0 % (V/V)        
REMARK 280  GLYCEROL, 10.0 % (W/V) PEG 4000, 0.03 M MAGNESIUM CHLORIDE, 0.03    
REMARK 280  M CALCIUM CHLORIDE, 0.0609 M TRIS-BASE, 0.0391 M BICINE, PH 8.5;    
REMARK 280  PROTEIN STOCK SOLUTION: 4.1 MG/ML PROTEIN, 50 MM SODIUM CHLORIDE,   
REMARK 280  1 % (V/V) GLYCEROL, 1 MM DTT, 50 MM HEPES, PH 8.0; DROP             
REMARK 280  COMPOSITION: 150 NL PROTEIN STOCK SOLUTION PLUS 150 NL RESERVOIR    
REMARK 280  SOLUTION; CRYO CONDITIONS: THE CRYSTALS WERE FLASH FROZEN           
REMARK 280  DIRECTLY FROM THE EQUILIBRATED CRYSTALLIZATION DROPS., VAPOR        
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277.15K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        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: 1390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33650 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     MET A   617                                                      
REMARK 465     ASP A   618                                                      
REMARK 465     GLU A   619                                                      
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     GLN B   107A                                                     
REMARK 465     GLN B   107B                                                     
REMARK 465     ARG B   107C                                                     
REMARK 465     LEU B   107D                                                     
REMARK 465     SER B   107E                                                     
REMARK 465     ARG B   107F                                                     
REMARK 465     SER B   107G                                                     
REMARK 465     ASP B   107H                                                     
REMARK 465     VAL B   107I                                                     
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    ASP A  98      119.42    -38.35                                   
REMARK 500    SER A 123     -132.93     57.04                                   
REMARK 500    TYR A 140      -56.06   -120.26                                   
REMARK 500    ASN A 144       77.35   -160.79                                   
REMARK 500    SER A 216       35.08    -97.47                                   
REMARK 500    LEU A 247      -37.18   -163.32                                   
REMARK 500    THR A 248     -140.41    -87.05                                   
REMARK 500    ALA A 251       54.29   -165.35                                   
REMARK 500    SER B   7      148.66   -172.89                                   
REMARK 500    ALA B  25       68.46   -102.47                                   
REMARK 500    THR B  29       96.93     52.44                                   
REMARK 500    PRO B  46      108.66    -52.57                                   
REMARK 500    VAL B  53      -70.08   -107.79                                   
REMARK 500    ARG B  58       48.76    -91.37                                   
REMARK 500    VAL B  59      -28.38   -167.41                                   
REMARK 500    ASN B  85       75.04     35.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6I8H   RELATED DB: PDB                                   
REMARK 900 EDS1 WITH A DIFFERENT NANOBODY                                       
REMARK 900 RELATED ID: 6I8G   RELATED DB: PDB                                   
REMARK 900 EDS1 WITH A DIFFERENT NANOBODY                                       
DBREF  6Q6Z A    1   623  UNP    Q9XF23   EDS1L_ARATH      1    623             
DBREF  6Q6Z B    1   147  PDB    6Q6Z     6Q6Z             1    147             
SEQADV 6Q6Z LEU A  624  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6Q6Z GLU A  625  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6Q6Z HIS A  626  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6Q6Z HIS A  627  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6Q6Z HIS A  628  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6Q6Z HIS A  629  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6Q6Z HIS A  630  UNP  Q9XF23              EXPRESSION TAG                 
SEQADV 6Q6Z 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  142  GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 B  142  ALA GLY GLY SER LEU ARG LEU SER CYS THR ALA SER GLY          
SEQRES   3 B  142  PHE THR PHE ASP SER TYR HIS MET GLY TRP PHE ARG ARG          
SEQRES   4 B  142  ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA VAL SER          
SEQRES   5 B  142  ARG VAL THR TRP LEU ILE ASP ILE ALA ASP SER VAL LYS          
SEQRES   6 B  142  GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR          
SEQRES   7 B  142  VAL TYR LEU GLU MET ASN SER LEU LYS PRO GLU ASP THR          
SEQRES   8 B  142  ALA GLN TYR PHE CYS ALA ALA SER GLN GLN ARG LEU SER          
SEQRES   9 B  142  ARG SER ASP VAL GLN TYR ASP TYR TRP GLY GLN GLY THR          
SEQRES  10 B  142  GLN VAL THR VAL SER SER ALA ALA ALA TYR PRO TYR ASP          
SEQRES  11 B  142  VAL PRO ASP TYR GLY SER HIS HIS HIS HIS HIS HIS              
HELIX    1 AA1 PHE A    3  GLY A    8  1                                   6    
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 PHE A  141  ASN A  144  5                                   4    
HELIX   10 AB1 ASP A  163  GLU A  173  1                                  11    
HELIX   11 AB2 TRP A  175  ARG A  177  5                                   3    
HELIX   12 AB3 ILE A  188  ALA A  195  5                                   8    
HELIX   13 AB4 ARG A  196  VAL A  200  5                                   5    
HELIX   14 AB5 THR A  203  ASP A  212  1                                  10    
HELIX   15 AB6 SER A  221  GLU A  246  1                                  26    
HELIX   16 AB7 ALA A  251  LEU A  262  1                                  12    
HELIX   17 AB8 ASN A  286  THR A  297  1                                  12    
HELIX   18 AB9 LEU A  308  ASP A  316  1                                   9    
HELIX   19 AC1 SER A  319  SER A  326  1                                   8    
HELIX   20 AC2 MET A  327  LYS A  330  5                                   4    
HELIX   21 AC3 ASP A  336  GLU A  338  5                                   3    
HELIX   22 AC4 ILE A  341  LEU A  348  1                                   8    
HELIX   23 AC5 SER A  351  GLN A  381  1                                  31    
HELIX   24 AC6 GLN A  381  GLU A  394  1                                  14    
HELIX   25 AC7 GLU A  394  HIS A  402  1                                   9    
HELIX   26 AC8 GLY A  405  SER A  413  1                                   9    
HELIX   27 AC9 GLU A  415  LYS A  441  1                                  27    
HELIX   28 AD1 PRO A  445  GLY A  450  5                                   6    
HELIX   29 AD2 ASP A  451  HIS A  476  1                                  26    
HELIX   30 AD3 LEU A  477  THR A  482  1                                   6    
HELIX   31 AD4 PRO A  484  GLY A  489  1                                   6    
HELIX   32 AD5 PRO A  491  LYS A  507  1                                  17    
HELIX   33 AD6 PRO A  508  GLY A  510  5                                   3    
HELIX   34 AD7 ILE A  512  LEU A  524  1                                  13    
HELIX   35 AD8 GLN A  529  LEU A  537  1                                   9    
HELIX   36 AD9 SER A  540  SER A  546  5                                   7    
HELIX   37 AE1 CYS A  547  LYS A  556  1                                  10    
HELIX   38 AE2 PRO A  559  GLY A  581  1                                  23    
HELIX   39 AE3 ASP A  584  PHE A  589  1                                   6    
HELIX   40 AE4 SER A  593  THR A  601  1                                   9    
HELIX   41 AE5 PRO A  603  HIS A  609  1                                   7    
HELIX   42 AE6 LEU A  612  MET A  616  5                                   5    
HELIX   43 AE7 LYS B   95  THR B   99  5                                   5    
SHEET    1 AA1 8 TYR A  30  ALA A  35  0                                        
SHEET    2 AA1 8 VAL A  38  PHE A  43 -1  O  VAL A  38   N  ALA A  35           
SHEET    3 AA1 8 GLN A 116  HIS A 122  1  O  VAL A 118   N  VAL A  39           
SHEET    4 AA1 8 ARG A 152  PHE A 156  1  O  ARG A 152   N  PHE A 119           
SHEET    5 AA1 8 PHE A 179  THR A 184  1  O  VAL A 180   N  CYS A 153           
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 GLN B   5  SER B   7  0                                        
SHEET    2 AA3 4 LEU B  19  THR B  24 -1  O  SER B  22   N  SER B   7           
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  ASP B  81   O  THR B  86           
SHEET    1 AA4 6 GLY B  11  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  ALA B 105 -1  N  TYR B 102   O  THR B 122           
SHEET    4 AA4 6 HIS B  38  ARG B  44 -1  N  ARG B  44   O  GLN B 101           
SHEET    5 AA4 6 GLU B  51  SER B  57 -1  O  VAL B  56   N  MET B  39           
SHEET    6 AA4 6 ILE B  65  ILE B  67 -1  O  ASP B  66   N  ALA B  55           
SSBOND   1 CYS B   23    CYS B  104                          1555   1555  2.03  
CRYST1  142.192  142.192   97.802  90.00  90.00 120.00 P 3 2 1       6          
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      0.007033  0.004060  0.000000        0.00000                         
SCALE2      0.000000  0.008121  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010225        0.00000                         
TER    4984      MET A 616                                                      
TER    5882      ALA B 130                                                      
MASTER      528    0    0   43   20    0    0    6 5880    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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