Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 6yq4-pdb

Name Class
6yq4-pdb
HEADER    HYDROLASE                               16-APR-20   6YQ4              
TITLE     CRYSTAL STRUCTURE OF FUSOBACTERIUM NUCLEATUM TANNASE                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TANNASE;                                                   
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: FUSOBACTERIUM NUCLEATUM SUBSP. NUCLEATUM ATCC   
SOURCE   3 25586;                                                               
SOURCE   4 ORGANISM_TAXID: 190304;                                              
SOURCE   5 GENE: FN0616;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TANNASE, COLORECTAL CANCER, PATHOGEN, GALLOTANNINS, HYDROLASE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.MANCHENO,J.ANGUITA,H.RODRIGUEZ                                    
REVDAT   1   24-MAR-21 6YQ4    0                                                
JRNL        AUTH   J.M.MANCHENO,E.ATONDO,J.TOMAS-CORTAZAR,J.LUIS LAVIN,         
JRNL        AUTH 2 L.PLAZA-VINUESA,I.MARTIN-RUIZ,D.BARRIALES,A.PALACIOS,        
JRNL        AUTH 3 C.DANIEL NAVO,L.SAMPEDRO,A.PENA-CEARRA,                      
JRNL        AUTH 4 M.ANGEL PASCUAL-ITOIZ,J.CASTELO,A.CARRERAS-GONZALEZ,         
JRNL        AUTH 5 D.CASTELLANA,A.PELLON,S.DELGADO,P.RUAS-MADIEDO,              
JRNL        AUTH 6 B.DE LAS RIVAS,L.ABECIA,R.MUNOZ,G.JIMENEZ-OSES,J.ANGUITA,    
JRNL        AUTH 7 H.RODRIGUEZ                                                  
JRNL        TITL   A STRUCTURALLY UNIQUE FUSOBACTERIUM NUCLEATUM TANNASE        
JRNL        TITL 2 PROVIDES DETOXICANT ACTIVITY AGAINST GALLOTANNINS AND        
JRNL        TITL 3 PATHOGEN RESISTANCE.                                         
JRNL        REF    MICROB BIOTECHNOL                          2020              
JRNL        REFN                   ISSN 1751-7915                               
JRNL        PMID   33336898                                                     
JRNL        DOI    10.1111/1751-7915.13732                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.79                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 60840                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3103                            
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 47.7900 -  6.7148    0.99     2731   128  0.1513 0.2093        
REMARK   3     2  6.7148 -  5.3320    0.99     2668   142  0.1599 0.2090        
REMARK   3     3  5.3320 -  4.6587    0.98     2591   161  0.1322 0.1903        
REMARK   3     4  4.6587 -  4.2330    0.99     2661   128  0.1196 0.1813        
REMARK   3     5  4.2330 -  3.9298    0.99     2628   150  0.1391 0.2060        
REMARK   3     6  3.9298 -  3.6982    1.00     2657   131  0.1528 0.2602        
REMARK   3     7  3.6982 -  3.5130    1.00     2636   156  0.1554 0.2295        
REMARK   3     8  3.5130 -  3.3601    0.99     2621   142  0.1656 0.2559        
REMARK   3     9  3.3601 -  3.2308    0.98     2604   138  0.1751 0.2669        
REMARK   3    10  3.2308 -  3.1193    0.99     2559   171  0.1926 0.2997        
REMARK   3    11  3.1193 -  3.0218    0.99     2651   132  0.1907 0.2786        
REMARK   3    12  3.0218 -  2.9355    0.99     2626   134  0.1920 0.3002        
REMARK   3    13  2.9355 -  2.8582    1.00     2645   144  0.2083 0.3116        
REMARK   3    14  2.8582 -  2.7885    0.99     2592   154  0.2187 0.2801        
REMARK   3    15  2.7885 -  2.7251    0.99     2648   138  0.2110 0.3009        
REMARK   3    16  2.7251 -  2.6671    1.00     2632   135  0.2130 0.2854        
REMARK   3    17  2.6671 -  2.6138    0.99     2612   138  0.2221 0.3176        
REMARK   3    18  2.6138 -  2.5644    0.98     2579   120  0.2117 0.3144        
REMARK   3    19  2.5644 -  2.5186    0.99     2632   133  0.2277 0.3160        
REMARK   3    20  2.5186 -  2.4759    0.99     2569   140  0.2394 0.3389        
REMARK   3    21  2.4759 -  2.4360    0.99     2646   157  0.2496 0.3313        
REMARK   3    22  2.4360 -  2.3990    0.97     2549   131  0.2528 0.3654        
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)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.000           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.66                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 5 THROUGH 58 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -17.6560   3.1061  -1.5523              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4972 T22:   0.2548                                     
REMARK   3      T33:   0.3757 T12:   0.0445                                     
REMARK   3      T13:  -0.0544 T23:  -0.1374                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6984 L22:   7.3210                                     
REMARK   3      L33:   3.3718 L12:   2.6911                                     
REMARK   3      L13:  -0.6376 L23:  -3.3494                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1123 S12:  -0.2190 S13:   0.4777                       
REMARK   3      S21:   0.2226 S22:  -0.1709 S23:   0.2732                       
REMARK   3      S31:  -0.4610 S32:  -0.0334 S33:   0.0395                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 59 THROUGH 239 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -17.6159 -13.3387  -6.0048              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2800 T22:   0.2210                                     
REMARK   3      T33:   0.1899 T12:   0.0211                                     
REMARK   3      T13:  -0.0155 T23:  -0.0371                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6344 L22:   1.9926                                     
REMARK   3      L33:   1.2379 L12:   0.0330                                     
REMARK   3      L13:   0.3015 L23:   0.3587                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0446 S12:  -0.2152 S13:   0.2294                       
REMARK   3      S21:  -0.0001 S22:  -0.1417 S23:   0.1011                       
REMARK   3      S31:  -0.1636 S32:  -0.1626 S33:   0.0768                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 240 THROUGH 279 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.3642 -34.2624  -6.6488              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2627 T22:   0.2119                                     
REMARK   3      T33:   0.1925 T12:  -0.0125                                     
REMARK   3      T13:   0.0195 T23:   0.0725                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5122 L22:   1.8726                                     
REMARK   3      L33:   3.4919 L12:  -2.4461                                     
REMARK   3      L13:   1.4308 L23:  -0.5160                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0951 S12:   0.1069 S13:  -0.0974                       
REMARK   3      S21:   0.1828 S22:   0.0497 S23:  -0.2919                       
REMARK   3      S31:   0.0525 S32:   0.2286 S33:  -0.2030                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 280 THROUGH 494 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -12.2732 -28.4455 -14.5839              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2608 T22:   0.1809                                     
REMARK   3      T33:   0.1834 T12:   0.0200                                     
REMARK   3      T13:  -0.0161 T23:   0.0168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5324 L22:   2.0315                                     
REMARK   3      L33:   1.3600 L12:  -0.2385                                     
REMARK   3      L13:   0.1519 L23:   0.3824                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0766 S12:   0.0244 S13:  -0.1163                       
REMARK   3      S21:  -0.1223 S22:  -0.1271 S23:  -0.0541                       
REMARK   3      S31:   0.0981 S32:   0.0343 S33:   0.0750                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 5 THROUGH 58 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -10.0147 -37.4642 -51.6785              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4921 T22:   0.7992                                     
REMARK   3      T33:   0.2865 T12:   0.2452                                     
REMARK   3      T13:   0.0156 T23:   0.0583                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1680 L22:   8.0217                                     
REMARK   3      L33:   5.2905 L12:  -1.8575                                     
REMARK   3      L13:  -1.4502 L23:   2.6737                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1950 S12:  -0.1791 S13:  -0.0077                       
REMARK   3      S21:   0.2408 S22:   0.0759 S23:  -0.5095                       
REMARK   3      S31:   0.8807 S32:   1.2144 S33:   0.0609                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 59 THROUGH 211 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -21.3713 -30.5472 -52.3722              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3343 T22:   0.3854                                     
REMARK   3      T33:   0.1793 T12:   0.0419                                     
REMARK   3      T13:   0.0324 T23:   0.0365                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1681 L22:   2.3956                                     
REMARK   3      L33:   3.2090 L12:  -0.4327                                     
REMARK   3      L13:  -0.8675 L23:   0.0303                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0948 S12:   0.1511 S13:   0.0581                       
REMARK   3      S21:  -0.1981 S22:   0.0334 S23:  -0.2165                       
REMARK   3      S31:   0.3303 S32:   0.5047 S33:   0.0161                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 212 THROUGH 279 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -45.0712 -28.4093 -37.3237              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4129 T22:   0.3744                                     
REMARK   3      T33:   0.2086 T12:   0.0045                                     
REMARK   3      T13:   0.0401 T23:  -0.0234                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6186 L22:   1.9287                                     
REMARK   3      L33:   5.1737 L12:   0.3898                                     
REMARK   3      L13:  -0.7244 L23:   0.5312                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0398 S12:  -0.2301 S13:  -0.3543                       
REMARK   3      S21:   0.1289 S22:   0.1003 S23:   0.3382                       
REMARK   3      S31:   0.5253 S32:  -0.7848 S33:  -0.0997                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 280 THROUGH 494 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -43.3016 -28.7582 -48.5036              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3762 T22:   0.4449                                     
REMARK   3      T33:   0.2230 T12:  -0.0404                                     
REMARK   3      T13:  -0.0196 T23:   0.0425                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2697 L22:   1.4769                                     
REMARK   3      L33:   3.1590 L12:   0.1333                                     
REMARK   3      L13:  -0.1777 L23:   0.1823                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0355 S12:   0.1683 S13:   0.0203                       
REMARK   3      S21:  -0.0976 S22:   0.0053 S23:   0.2264                       
REMARK   3      S31:   0.3348 S32:  -0.7685 S33:   0.0551                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 5 THROUGH 81 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  23.1766 -84.6652 -42.8040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5821 T22:   0.4272                                     
REMARK   3      T33:   0.3293 T12:   0.1184                                     
REMARK   3      T13:   0.0869 T23:  -0.0865                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1640 L22:   3.2048                                     
REMARK   3      L33:   2.9049 L12:  -0.8245                                     
REMARK   3      L13:  -0.3268 L23:   0.9898                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1754 S12:   0.3120 S13:  -0.3890                       
REMARK   3      S21:  -0.3802 S22:   0.2444 S23:  -0.5792                       
REMARK   3      S31:   0.1864 S32:   0.4272 S33:  -0.1166                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 82 THROUGH 114 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6072 -72.8803 -42.8642              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4114 T22:   0.3515                                     
REMARK   3      T33:   0.3061 T12:   0.0927                                     
REMARK   3      T13:   0.0742 T23:  -0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5831 L22:   2.9519                                     
REMARK   3      L33:   1.3204 L12:  -1.5685                                     
REMARK   3      L13:  -2.1711 L23:   1.4537                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1499 S12:  -0.2400 S13:   0.6784                       
REMARK   3      S21:  -0.2110 S22:   0.2697 S23:  -0.5404                       
REMARK   3      S31:   0.1186 S32:   0.1961 S33:  -0.1386                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 115 THROUGH 279 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.8071 -70.3335 -36.8928              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3352 T22:   0.3190                                     
REMARK   3      T33:   0.1697 T12:   0.0197                                     
REMARK   3      T13:  -0.0397 T23:   0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8153 L22:   2.3871                                     
REMARK   3      L33:   1.6160 L12:  -0.5765                                     
REMARK   3      L13:  -0.3216 L23:   0.6750                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0874 S12:   0.2669 S13:   0.0190                       
REMARK   3      S21:  -0.3053 S22:   0.0146 S23:   0.1712                       
REMARK   3      S31:   0.1439 S32:  -0.1081 S33:   0.0686                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 280 THROUGH 494 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.8842 -60.9138 -29.2238              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3017 T22:   0.2506                                     
REMARK   3      T33:   0.2144 T12:   0.0469                                     
REMARK   3      T13:  -0.0460 T23:   0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2025 L22:   1.9256                                     
REMARK   3      L33:   1.3832 L12:  -0.8068                                     
REMARK   3      L13:  -0.0996 L23:   0.3391                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1452 S12:   0.0094 S13:   0.2374                       
REMARK   3      S21:   0.0023 S22:   0.1170 S23:   0.0126                       
REMARK   3      S31:   0.0734 S32:  -0.0103 S33:   0.0338                       
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 6YQ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-APR-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292108062.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JUL-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALBA                               
REMARK 200  BEAMLINE                       : XALOC                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
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                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60896                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.390                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.791                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 6.620                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.3100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.39                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
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: 4J0D                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, TRIS-HCL, PH 8.5, VAPOR        
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       45.53350            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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     VAL A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     ARG A   396                                                      
REMARK 465     ASN A   397                                                      
REMARK 465     GLY A   398                                                      
REMARK 465     LYS A   399                                                      
REMARK 465     PHE A   400                                                      
REMARK 465     ASN A   401                                                      
REMARK 465     ASP A   402                                                      
REMARK 465     LYS A   403                                                      
REMARK 465     ASN A   404                                                      
REMARK 465     ASN A   405                                                      
REMARK 465     LYS A   406                                                      
REMARK 465     ILE A   407                                                      
REMARK 465     LYS A   495                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     ASN B     4                                                      
REMARK 465     GLY B   398                                                      
REMARK 465     LYS B   399                                                      
REMARK 465     PHE B   400                                                      
REMARK 465     ASN B   401                                                      
REMARK 465     ASP B   402                                                      
REMARK 465     LYS B   403                                                      
REMARK 465     ASN B   404                                                      
REMARK 465     ASN B   405                                                      
REMARK 465     LYS B   406                                                      
REMARK 465     ILE B   407                                                      
REMARK 465     LYS B   495                                                      
REMARK 465     MET C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     ASN C     4                                                      
REMARK 465     PHE C   395                                                      
REMARK 465     ARG C   396                                                      
REMARK 465     ASN C   397                                                      
REMARK 465     GLY C   398                                                      
REMARK 465     LYS C   399                                                      
REMARK 465     PHE C   400                                                      
REMARK 465     ASN C   401                                                      
REMARK 465     ASP C   402                                                      
REMARK 465     LYS C   403                                                      
REMARK 465     ASN C   404                                                      
REMARK 465     ASN C   405                                                      
REMARK 465     LYS C   406                                                      
REMARK 465     LYS C   495                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NZ   LYS B   125     O    HOH B   601              1.92            
REMARK 500   NZ   LYS A   125     O    HOH A   601              1.94            
REMARK 500   NH1  ARG C   246     OD2  ASP C   446              2.10            
REMARK 500   O    GLU A   242     O    HOH A   602              2.12            
REMARK 500   O    HOH A   755     O    HOH A   771              2.13            
REMARK 500   O    TYR C   103     OG   SER C   106              2.14            
REMARK 500   O    TYR C   243     NH2  ARG C   246              2.14            
REMARK 500   O    HOH A   700     O    HOH C   704              2.14            
REMARK 500   OG   SER B   408     O    HOH B   602              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS A 373   CD  -  CE  -  NZ  ANGL. DEV. = -15.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  23      -12.72   -140.41                                   
REMARK 500    TYR A  37       34.26    -98.08                                   
REMARK 500    ASN A  67     -168.96   -129.45                                   
REMARK 500    SER A 166     -121.51     71.43                                   
REMARK 500    THR A 196      -96.58   -122.01                                   
REMARK 500    CYS A 207       53.44     37.19                                   
REMARK 500    THR A 210     -169.51   -118.89                                   
REMARK 500    ASP A 283     -164.70    -78.88                                   
REMARK 500    SER A 322      -62.89    -25.49                                   
REMARK 500    GLU A 331     -103.74   -114.33                                   
REMARK 500    MET A 350      -73.74    -97.43                                   
REMARK 500    ASP A 481       45.73   -140.97                                   
REMARK 500    ASN B  23       47.13   -164.12                                   
REMARK 500    ASN B  40       72.54   -118.43                                   
REMARK 500    GLN B  47       57.85    -98.75                                   
REMARK 500    ASP B  95        4.81   -174.81                                   
REMARK 500    LYS B 159       61.32   -118.26                                   
REMARK 500    SER B 166     -120.23     64.67                                   
REMARK 500    THR B 196     -122.08   -125.65                                   
REMARK 500    CYS B 207       68.25     18.47                                   
REMARK 500    THR B 249       22.65     43.93                                   
REMARK 500    SER B 251      165.94     64.58                                   
REMARK 500    THR B 252      118.78   -163.78                                   
REMARK 500    PHE B 324       34.52    -84.49                                   
REMARK 500    GLU B 331     -139.90    -95.04                                   
REMARK 500    ASN B 333      -37.73     66.75                                   
REMARK 500    PHE B 395      -20.99    168.16                                   
REMARK 500    ASP B 481       45.90   -150.75                                   
REMARK 500    ASN C  23      -33.48   -157.64                                   
REMARK 500    ASN C  34       31.04     72.41                                   
REMARK 500    ASP C  95       31.61    -78.46                                   
REMARK 500    SER C 166     -116.99     65.65                                   
REMARK 500    THR C 196      -94.77   -128.03                                   
REMARK 500    CYS C 207       61.62     28.34                                   
REMARK 500    GLU C 233       80.69    -35.98                                   
REMARK 500    SER C 247      -75.54   -144.02                                   
REMARK 500    THR C 249       83.09     81.27                                   
REMARK 500    ARG C 250      176.48     75.50                                   
REMARK 500    SER C 251     -152.11    -85.79                                   
REMARK 500    ASP C 283     -167.01    -76.74                                   
REMARK 500    ASP C 292      157.12    -43.31                                   
REMARK 500    GLU C 331      -85.84   -125.82                                   
REMARK 500    MET C 350      -60.95    -94.13                                   
REMARK 500    PHE C 356      -51.37   -122.49                                   
REMARK 500    ASP C 371     -167.15   -125.31                                   
REMARK 500    PHE C 379       17.70   -144.76                                   
REMARK 500    ASP C 481       42.13   -141.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP B  393     TYR B  394                  142.83                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 150   O                                                      
REMARK 620 2 ASP A 150   OD2  74.1                                              
REMARK 620 3 MET A 153   O    74.8 131.5                                        
REMARK 620 4 GLY A 155   O   164.2  97.7 119.6                                  
REMARK 620 5 HOH A 676   O   103.9  73.9  78.6  86.3                            
REMARK 620 6 HOH A 759   O    90.6 127.2  89.2  83.6 157.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 503  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 150   O                                                      
REMARK 620 2 ASP B 150   OD2  77.1                                              
REMARK 620 3 MET B 153   O    81.5 139.5                                        
REMARK 620 4 GLY B 155   O   165.5 109.3 100.0                                  
REMARK 620 5 HOH B 680   O   109.5  76.0  79.5  84.8                            
REMARK 620 6 HOH B 685   O    83.7 120.9  89.9  81.9 161.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 150   O                                                      
REMARK 620 2 ASP C 150   OD2  87.8                                              
REMARK 620 3 MET C 153   O    90.1 166.7                                        
REMARK 620 4 GLY C 155   O   149.2  83.0 105.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SPD B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 502                  
DBREF  6YQ4 A    1   495  UNP    Q8RFS1   Q8RFS1_FUSNN     1    495             
DBREF  6YQ4 B    1   495  UNP    Q8RFS1   Q8RFS1_FUSNN     1    495             
DBREF  6YQ4 C    1   495  UNP    Q8RFS1   Q8RFS1_FUSNN     1    495             
SEQRES   1 A  495  MET VAL LYS ASN ASP TYR ASP LEU LYS PHE ASN PRO ASP          
SEQRES   2 A  495  LYS TYR ILE SER LYS GLU ILE LYS ILE ASN GLY LYS LYS          
SEQRES   3 A  495  ILE LYS TYR ARG ALA TYR GLU ASN ILE ILE TYR ILE LYS          
SEQRES   4 A  495  ASN PRO ILE ASP LYS ASP TYR GLN ASN MET ASN ILE TYR          
SEQRES   5 A  495  ILE PRO GLU GLU TYR PHE ASN ASN LEU SER ILE GLY SER          
SEQRES   6 A  495  TYR ASN SER ASN ASN ALA PRO ILE PHE PHE PRO ASN THR          
SEQRES   7 A  495  VAL GLY GLY TYR MET PRO GLY LYS ALA ASP THR VAL GLY          
SEQRES   8 A  495  LEU GLY ARG ASP GLY LYS ALA ASN SER LEU THR TYR ALA          
SEQRES   9 A  495  LEU SER LYS GLY TYR VAL VAL ALA ALA PRO GLY ALA ARG          
SEQRES  10 A  495  GLY ARG THR LEU THR ASP ASP LYS GLY ASN TYR ILE GLY          
SEQRES  11 A  495  LYS ALA PRO ALA ALA ILE VAL ASP LEU LYS ALA ALA VAL          
SEQRES  12 A  495  ARG TYR LEU TYR LEU ASN ASP GLU VAL MET PRO GLY ASP          
SEQRES  13 A  495  ALA ASN LYS ILE ILE SER ASN GLY THR SER ALA GLY GLY          
SEQRES  14 A  495  ALA LEU SER ALA LEU LEU GLY ALA SER GLY ASN SER GLN          
SEQRES  15 A  495  ASP TYR LEU PRO TYR LEU LYS GLU ILE GLY ALA ALA GLU          
SEQRES  16 A  495  THR ARG ASP ASP ILE PHE ALA VAL SER ALA TYR CYS PRO          
SEQRES  17 A  495  ILE THR ASN LEU GLU ASN ALA ASP SER ALA TYR GLU TRP          
SEQRES  18 A  495  MET TYR ASN GLY VAL ASN SER TYR SER ARG MET GLU PHE          
SEQRES  19 A  495  THR ARG ASN THR SER ALA GLN GLU TYR ASN ASP ARG SER          
SEQRES  20 A  495  LEU THR ARG SER THR VAL GLN GLY ASN LEU THR ASN ASP          
SEQRES  21 A  495  GLU ILE ASN ILE SER ASN LYS LEU LYS THR LEU PHE PRO          
SEQRES  22 A  495  ILE TYR LEU ASN SER LEU LYS LEU THR ASP ASP GLY GLY          
SEQRES  23 A  495  ASN LEU LEU THR LEU ASP LYS SER GLY ASN GLY SER PHE          
SEQRES  24 A  495  LYS THR TYR LEU SER ILE ILE ILE ARG ASN SER ALA ASN          
SEQRES  25 A  495  ARG ALA LEU ARG GLU GLY LYS ASP ILE SER GLN PHE LYS          
SEQRES  26 A  495  LYS ALA PHE THR ILE GLU ASN ASN LYS VAL VAL ALA VAL          
SEQRES  27 A  495  ASN LEU ASP VAL TYR THR HIS ILE GLY ASP ARG MET LYS          
SEQRES  28 A  495  SER PRO PRO ALA PHE ASP SER LEU ASP ALA SER SER GLY          
SEQRES  29 A  495  GLU ASN ASN LEU PHE GLY ASP LYS LYS SER ASP SER LYS          
SEQRES  30 A  495  HIS PHE THR LYS PHE SER PHE ASP ILE ASN ASN LYS ALA          
SEQRES  31 A  495  ALA ILE ASP TYR PHE ARG ASN GLY LYS PHE ASN ASP LYS          
SEQRES  32 A  495  ASN ASN LYS ILE SER ILE PRO LYS MET ALA ASP LYS ASN          
SEQRES  33 A  495  ILE ILE LYS MET MET ASN PRO MET TYR TYR ILE ASP SER          
SEQRES  34 A  495  ASN THR SER THR LYS TYR TRP ARG ILE ARG HIS GLY ALA          
SEQRES  35 A  495  ILE ASP LYS ASP THR SER LEU ALA ILE PRO ALA ILE LEU          
SEQRES  36 A  495  ALA LEU LYS LEU LYS ASN SER GLY LYS ILE VAL ASN PHE          
SEQRES  37 A  495  ALA ALA PRO TRP GLY GLN GLY HIS GLY GLY ASP TYR ASP          
SEQRES  38 A  495  LEU GLU GLU LEU PHE ASN TRP ILE ASP ASN VAL VAL LYS          
SEQRES  39 A  495  LYS                                                          
SEQRES   1 B  495  MET VAL LYS ASN ASP TYR ASP LEU LYS PHE ASN PRO ASP          
SEQRES   2 B  495  LYS TYR ILE SER LYS GLU ILE LYS ILE ASN GLY LYS LYS          
SEQRES   3 B  495  ILE LYS TYR ARG ALA TYR GLU ASN ILE ILE TYR ILE LYS          
SEQRES   4 B  495  ASN PRO ILE ASP LYS ASP TYR GLN ASN MET ASN ILE TYR          
SEQRES   5 B  495  ILE PRO GLU GLU TYR PHE ASN ASN LEU SER ILE GLY SER          
SEQRES   6 B  495  TYR ASN SER ASN ASN ALA PRO ILE PHE PHE PRO ASN THR          
SEQRES   7 B  495  VAL GLY GLY TYR MET PRO GLY LYS ALA ASP THR VAL GLY          
SEQRES   8 B  495  LEU GLY ARG ASP GLY LYS ALA ASN SER LEU THR TYR ALA          
SEQRES   9 B  495  LEU SER LYS GLY TYR VAL VAL ALA ALA PRO GLY ALA ARG          
SEQRES  10 B  495  GLY ARG THR LEU THR ASP ASP LYS GLY ASN TYR ILE GLY          
SEQRES  11 B  495  LYS ALA PRO ALA ALA ILE VAL ASP LEU LYS ALA ALA VAL          
SEQRES  12 B  495  ARG TYR LEU TYR LEU ASN ASP GLU VAL MET PRO GLY ASP          
SEQRES  13 B  495  ALA ASN LYS ILE ILE SER ASN GLY THR SER ALA GLY GLY          
SEQRES  14 B  495  ALA LEU SER ALA LEU LEU GLY ALA SER GLY ASN SER GLN          
SEQRES  15 B  495  ASP TYR LEU PRO TYR LEU LYS GLU ILE GLY ALA ALA GLU          
SEQRES  16 B  495  THR ARG ASP ASP ILE PHE ALA VAL SER ALA TYR CYS PRO          
SEQRES  17 B  495  ILE THR ASN LEU GLU ASN ALA ASP SER ALA TYR GLU TRP          
SEQRES  18 B  495  MET TYR ASN GLY VAL ASN SER TYR SER ARG MET GLU PHE          
SEQRES  19 B  495  THR ARG ASN THR SER ALA GLN GLU TYR ASN ASP ARG SER          
SEQRES  20 B  495  LEU THR ARG SER THR VAL GLN GLY ASN LEU THR ASN ASP          
SEQRES  21 B  495  GLU ILE ASN ILE SER ASN LYS LEU LYS THR LEU PHE PRO          
SEQRES  22 B  495  ILE TYR LEU ASN SER LEU LYS LEU THR ASP ASP GLY GLY          
SEQRES  23 B  495  ASN LEU LEU THR LEU ASP LYS SER GLY ASN GLY SER PHE          
SEQRES  24 B  495  LYS THR TYR LEU SER ILE ILE ILE ARG ASN SER ALA ASN          
SEQRES  25 B  495  ARG ALA LEU ARG GLU GLY LYS ASP ILE SER GLN PHE LYS          
SEQRES  26 B  495  LYS ALA PHE THR ILE GLU ASN ASN LYS VAL VAL ALA VAL          
SEQRES  27 B  495  ASN LEU ASP VAL TYR THR HIS ILE GLY ASP ARG MET LYS          
SEQRES  28 B  495  SER PRO PRO ALA PHE ASP SER LEU ASP ALA SER SER GLY          
SEQRES  29 B  495  GLU ASN ASN LEU PHE GLY ASP LYS LYS SER ASP SER LYS          
SEQRES  30 B  495  HIS PHE THR LYS PHE SER PHE ASP ILE ASN ASN LYS ALA          
SEQRES  31 B  495  ALA ILE ASP TYR PHE ARG ASN GLY LYS PHE ASN ASP LYS          
SEQRES  32 B  495  ASN ASN LYS ILE SER ILE PRO LYS MET ALA ASP LYS ASN          
SEQRES  33 B  495  ILE ILE LYS MET MET ASN PRO MET TYR TYR ILE ASP SER          
SEQRES  34 B  495  ASN THR SER THR LYS TYR TRP ARG ILE ARG HIS GLY ALA          
SEQRES  35 B  495  ILE ASP LYS ASP THR SER LEU ALA ILE PRO ALA ILE LEU          
SEQRES  36 B  495  ALA LEU LYS LEU LYS ASN SER GLY LYS ILE VAL ASN PHE          
SEQRES  37 B  495  ALA ALA PRO TRP GLY GLN GLY HIS GLY GLY ASP TYR ASP          
SEQRES  38 B  495  LEU GLU GLU LEU PHE ASN TRP ILE ASP ASN VAL VAL LYS          
SEQRES  39 B  495  LYS                                                          
SEQRES   1 C  495  MET VAL LYS ASN ASP TYR ASP LEU LYS PHE ASN PRO ASP          
SEQRES   2 C  495  LYS TYR ILE SER LYS GLU ILE LYS ILE ASN GLY LYS LYS          
SEQRES   3 C  495  ILE LYS TYR ARG ALA TYR GLU ASN ILE ILE TYR ILE LYS          
SEQRES   4 C  495  ASN PRO ILE ASP LYS ASP TYR GLN ASN MET ASN ILE TYR          
SEQRES   5 C  495  ILE PRO GLU GLU TYR PHE ASN ASN LEU SER ILE GLY SER          
SEQRES   6 C  495  TYR ASN SER ASN ASN ALA PRO ILE PHE PHE PRO ASN THR          
SEQRES   7 C  495  VAL GLY GLY TYR MET PRO GLY LYS ALA ASP THR VAL GLY          
SEQRES   8 C  495  LEU GLY ARG ASP GLY LYS ALA ASN SER LEU THR TYR ALA          
SEQRES   9 C  495  LEU SER LYS GLY TYR VAL VAL ALA ALA PRO GLY ALA ARG          
SEQRES  10 C  495  GLY ARG THR LEU THR ASP ASP LYS GLY ASN TYR ILE GLY          
SEQRES  11 C  495  LYS ALA PRO ALA ALA ILE VAL ASP LEU LYS ALA ALA VAL          
SEQRES  12 C  495  ARG TYR LEU TYR LEU ASN ASP GLU VAL MET PRO GLY ASP          
SEQRES  13 C  495  ALA ASN LYS ILE ILE SER ASN GLY THR SER ALA GLY GLY          
SEQRES  14 C  495  ALA LEU SER ALA LEU LEU GLY ALA SER GLY ASN SER GLN          
SEQRES  15 C  495  ASP TYR LEU PRO TYR LEU LYS GLU ILE GLY ALA ALA GLU          
SEQRES  16 C  495  THR ARG ASP ASP ILE PHE ALA VAL SER ALA TYR CYS PRO          
SEQRES  17 C  495  ILE THR ASN LEU GLU ASN ALA ASP SER ALA TYR GLU TRP          
SEQRES  18 C  495  MET TYR ASN GLY VAL ASN SER TYR SER ARG MET GLU PHE          
SEQRES  19 C  495  THR ARG ASN THR SER ALA GLN GLU TYR ASN ASP ARG SER          
SEQRES  20 C  495  LEU THR ARG SER THR VAL GLN GLY ASN LEU THR ASN ASP          
SEQRES  21 C  495  GLU ILE ASN ILE SER ASN LYS LEU LYS THR LEU PHE PRO          
SEQRES  22 C  495  ILE TYR LEU ASN SER LEU LYS LEU THR ASP ASP GLY GLY          
SEQRES  23 C  495  ASN LEU LEU THR LEU ASP LYS SER GLY ASN GLY SER PHE          
SEQRES  24 C  495  LYS THR TYR LEU SER ILE ILE ILE ARG ASN SER ALA ASN          
SEQRES  25 C  495  ARG ALA LEU ARG GLU GLY LYS ASP ILE SER GLN PHE LYS          
SEQRES  26 C  495  LYS ALA PHE THR ILE GLU ASN ASN LYS VAL VAL ALA VAL          
SEQRES  27 C  495  ASN LEU ASP VAL TYR THR HIS ILE GLY ASP ARG MET LYS          
SEQRES  28 C  495  SER PRO PRO ALA PHE ASP SER LEU ASP ALA SER SER GLY          
SEQRES  29 C  495  GLU ASN ASN LEU PHE GLY ASP LYS LYS SER ASP SER LYS          
SEQRES  30 C  495  HIS PHE THR LYS PHE SER PHE ASP ILE ASN ASN LYS ALA          
SEQRES  31 C  495  ALA ILE ASP TYR PHE ARG ASN GLY LYS PHE ASN ASP LYS          
SEQRES  32 C  495  ASN ASN LYS ILE SER ILE PRO LYS MET ALA ASP LYS ASN          
SEQRES  33 C  495  ILE ILE LYS MET MET ASN PRO MET TYR TYR ILE ASP SER          
SEQRES  34 C  495  ASN THR SER THR LYS TYR TRP ARG ILE ARG HIS GLY ALA          
SEQRES  35 C  495  ILE ASP LYS ASP THR SER LEU ALA ILE PRO ALA ILE LEU          
SEQRES  36 C  495  ALA LEU LYS LEU LYS ASN SER GLY LYS ILE VAL ASN PHE          
SEQRES  37 C  495  ALA ALA PRO TRP GLY GLN GLY HIS GLY GLY ASP TYR ASP          
SEQRES  38 C  495  LEU GLU GLU LEU PHE ASN TRP ILE ASP ASN VAL VAL LYS          
SEQRES  39 C  495  LYS                                                          
HET    GOL  A 501       6                                                       
HET     MG  A 502       1                                                       
HET    GOL  B 501       6                                                       
HET    SPD  B 502      10                                                       
HET     MG  B 503       1                                                       
HET    GOL  C 501       6                                                       
HET     MG  C 502       1                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SPD SPERMIDINE                                                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     SPD N-(2-AMINO-PROPYL)-1,4-DIAMINOBUTANE; PA(34)                     
FORMUL   4  GOL    3(C3 H8 O3)                                                  
FORMUL   5   MG    3(MG 2+)                                                     
FORMUL   7  SPD    C7 H19 N3                                                    
FORMUL  11  HOH   *407(H2 O)                                                    
HELIX    1 AA1 GLU A   56  ASN A   59  5                                   4    
HELIX    2 AA2 ASN A   99  LYS A  107  1                                   9    
HELIX    3 AA3 PRO A  133  ASN A  149  1                                  17    
HELIX    4 AA4 SER A  166  SER A  178  1                                  13    
HELIX    5 AA5 SER A  181  ASP A  183  5                                   3    
HELIX    6 AA6 TYR A  184  GLY A  192  1                                   9    
HELIX    7 AA7 ASN A  211  ASN A  224  1                                  14    
HELIX    8 AA8 SER A  239  ASP A  245  1                                   7    
HELIX    9 AA9 THR A  258  LYS A  280  1                                  23    
HELIX   10 AB1 GLY A  297  GLU A  317  1                                  21    
HELIX   11 AB2 ILE A  321  LYS A  326  5                                   6    
HELIX   12 AB3 ASN A  339  HIS A  345  1                                   7    
HELIX   13 AB4 SER A  363  PHE A  369  1                                   7    
HELIX   14 AB5 THR A  380  PHE A  395  1                                  16    
HELIX   15 AB6 ASP A  414  MET A  421  1                                   8    
HELIX   16 AB7 ASN A  422  TYR A  426  5                                   5    
HELIX   17 AB8 LEU A  449  SER A  462  1                                  14    
HELIX   18 AB9 ASP A  481  LYS A  494  1                                  14    
HELIX   19 AC1 GLU B   56  ASN B   59  5                                   4    
HELIX   20 AC2 ASN B   99  LYS B  107  1                                   9    
HELIX   21 AC3 PRO B  133  ASN B  149  1                                  17    
HELIX   22 AC4 SER B  166  SER B  178  1                                  13    
HELIX   23 AC5 SER B  181  ASP B  183  5                                   3    
HELIX   24 AC6 TYR B  184  GLY B  192  1                                   9    
HELIX   25 AC7 ASN B  211  ASN B  224  1                                  14    
HELIX   26 AC8 SER B  239  ASP B  245  1                                   7    
HELIX   27 AC9 ARG B  246  THR B  249  5                                   4    
HELIX   28 AD1 THR B  258  LEU B  279  1                                  22    
HELIX   29 AD2 GLY B  297  GLU B  317  1                                  21    
HELIX   30 AD3 ILE B  321  LYS B  326  5                                   6    
HELIX   31 AD4 ASN B  339  THR B  344  1                                   6    
HELIX   32 AD5 HIS B  345  GLY B  347  5                                   3    
HELIX   33 AD6 SER B  363  PHE B  369  1                                   7    
HELIX   34 AD7 THR B  380  TYR B  394  1                                  15    
HELIX   35 AD8 ASP B  414  ASN B  422  1                                   9    
HELIX   36 AD9 PRO B  423  TYR B  426  5                                   4    
HELIX   37 AE1 LEU B  449  SER B  462  1                                  14    
HELIX   38 AE2 ASP B  481  LYS B  494  1                                  14    
HELIX   39 AE3 GLU C   56  ASN C   59  5                                   4    
HELIX   40 AE4 ASN C   99  GLY C  108  1                                  10    
HELIX   41 AE5 PRO C  133  ASP C  150  1                                  18    
HELIX   42 AE6 SER C  166  SER C  178  1                                  13    
HELIX   43 AE7 SER C  181  ASP C  183  5                                   3    
HELIX   44 AE8 TYR C  184  ILE C  191  1                                   8    
HELIX   45 AE9 ASN C  211  ASN C  224  1                                  14    
HELIX   46 AF1 SER C  239  ARG C  246  1                                   8    
HELIX   47 AF2 THR C  258  LEU C  279  1                                  22    
HELIX   48 AF3 GLY C  297  GLU C  317  1                                  21    
HELIX   49 AF4 ILE C  321  LYS C  326  5                                   6    
HELIX   50 AF5 ASN C  339  HIS C  345  1                                   7    
HELIX   51 AF6 SER C  363  PHE C  369  1                                   7    
HELIX   52 AF7 THR C  380  ASP C  393  1                                  14    
HELIX   53 AF8 ASP C  414  MET C  421  1                                   8    
HELIX   54 AF9 ASN C  422  TYR C  426  5                                   5    
HELIX   55 AG1 LEU C  449  SER C  462  1                                  14    
HELIX   56 AG2 ASP C  481  VAL C  493  1                                  13    
SHEET    1 AA1 9 ILE A  16  LYS A  21  0                                        
SHEET    2 AA1 9 LYS A  26  ILE A  36 -1  O  ILE A  27   N  ILE A  20           
SHEET    3 AA1 9 ASN A  48  PRO A  54 -1  O  ILE A  51   N  TYR A  32           
SHEET    4 AA1 9 VAL A 110  PRO A 114 -1  O  VAL A 111   N  TYR A  52           
SHEET    5 AA1 9 ILE A  73  PRO A  76  1  N  PHE A  74   O  VAL A 110           
SHEET    6 AA1 9 ILE A 160  ASN A 163  1  O  ILE A 161   N  PHE A  75           
SHEET    7 AA1 9 ALA A 202  TYR A 206  1  O  ALA A 202   N  SER A 162           
SHEET    8 AA1 9 TYR A 435  ARG A 439  1  O  ARG A 437   N  ALA A 205           
SHEET    9 AA1 9 ILE A 465  ALA A 469  1  O  ASN A 467   N  TRP A 436           
SHEET    1 AA2 2 SER A 228  MET A 232  0                                        
SHEET    2 AA2 2 THR A 252  ASN A 256 -1  O  VAL A 253   N  ARG A 231           
SHEET    1 AA3 2 PHE A 328  ILE A 330  0                                        
SHEET    2 AA3 2 VAL A 335  VAL A 338 -1  O  VAL A 336   N  THR A 329           
SHEET    1 AA4 9 ILE B  16  LYS B  21  0                                        
SHEET    2 AA4 9 LYS B  26  ILE B  36 -1  O  ALA B  31   N  ILE B  16           
SHEET    3 AA4 9 ASN B  48  PRO B  54 -1  O  MET B  49   N  ILE B  35           
SHEET    4 AA4 9 VAL B 110  PRO B 114 -1  O  ALA B 113   N  ASN B  50           
SHEET    5 AA4 9 ILE B  73  PRO B  76  1  N  PHE B  74   O  ALA B 112           
SHEET    6 AA4 9 ILE B 160  ASN B 163  1  O  ILE B 161   N  ILE B  73           
SHEET    7 AA4 9 ALA B 202  TYR B 206  1  O  SER B 204   N  SER B 162           
SHEET    8 AA4 9 TYR B 435  ARG B 439  1  O  ARG B 437   N  VAL B 203           
SHEET    9 AA4 9 ILE B 465  ALA B 469  1  O  ASN B 467   N  TRP B 436           
SHEET    1 AA5 2 LEU B  92  GLY B  93  0                                        
SHEET    2 AA5 2 LYS B  97  ALA B  98 -1  O  LYS B  97   N  GLY B  93           
SHEET    1 AA6 2 SER B 228  ARG B 231  0                                        
SHEET    2 AA6 2 VAL B 253  ASN B 256 -1  O  VAL B 253   N  ARG B 231           
SHEET    1 AA7 2 PHE B 328  ILE B 330  0                                        
SHEET    2 AA7 2 VAL B 335  VAL B 338 -1  O  VAL B 336   N  THR B 329           
SHEET    1 AA8 9 ILE C  16  LYS C  21  0                                        
SHEET    2 AA8 9 LYS C  26  ILE C  36 -1  O  TYR C  29   N  LYS C  18           
SHEET    3 AA8 9 ASN C  48  PRO C  54 -1  O  ILE C  51   N  TYR C  32           
SHEET    4 AA8 9 VAL C 110  PRO C 114 -1  O  ALA C 113   N  ASN C  50           
SHEET    5 AA8 9 ILE C  73  PRO C  76  1  N  PHE C  74   O  VAL C 110           
SHEET    6 AA8 9 ILE C 160  ASN C 163  1  O  ILE C 161   N  ILE C  73           
SHEET    7 AA8 9 ALA C 202  TYR C 206  1  O  SER C 204   N  SER C 162           
SHEET    8 AA8 9 TYR C 435  ARG C 439  1  O  ARG C 437   N  VAL C 203           
SHEET    9 AA8 9 ILE C 465  ALA C 469  1  O  ASN C 467   N  TRP C 436           
SHEET    1 AA9 2 SER C 228  ARG C 231  0                                        
SHEET    2 AA9 2 VAL C 253  ASN C 256 -1  O  VAL C 253   N  ARG C 231           
SHEET    1 AB1 2 PHE C 328  ILE C 330  0                                        
SHEET    2 AB1 2 VAL C 335  VAL C 338 -1  O  VAL C 336   N  THR C 329           
LINK         O   ASP A 150                MG    MG A 502     1555   1555  2.52  
LINK         OD2 ASP A 150                MG    MG A 502     1555   1555  2.43  
LINK         O   MET A 153                MG    MG A 502     1555   1555  2.29  
LINK         O   GLY A 155                MG    MG A 502     1555   1555  2.10  
LINK        MG    MG A 502                 O   HOH A 676     1555   1555  2.66  
LINK        MG    MG A 502                 O   HOH A 759     1555   1555  2.81  
LINK         O   ASP B 150                MG    MG B 503     1555   1555  2.49  
LINK         OD2 ASP B 150                MG    MG B 503     1555   1555  2.18  
LINK         O   MET B 153                MG    MG B 503     1555   1555  2.41  
LINK         O   GLY B 155                MG    MG B 503     1555   1555  2.19  
LINK        MG    MG B 503                 O   HOH B 680     1555   1555  2.68  
LINK        MG    MG B 503                 O   HOH B 685     1555   1555  2.87  
LINK         O   ASP C 150                MG    MG C 502     1555   1555  2.47  
LINK         OD2 ASP C 150                MG    MG C 502     1555   1555  2.56  
LINK         O   MET C 153                MG    MG C 502     1555   1555  2.37  
LINK         O   GLY C 155                MG    MG C 502     1555   1555  2.42  
CISPEP   1 ALA A  132    PRO A  133          0         5.90                     
CISPEP   2 PRO A  353    PRO A  354          0        -2.85                     
CISPEP   3 ALA B  132    PRO B  133          0        -1.46                     
CISPEP   4 PRO B  353    PRO B  354          0        -3.99                     
CISPEP   5 ALA C  132    PRO C  133          0        -1.24                     
CISPEP   6 PRO C  353    PRO C  354          0       -11.20                     
SITE     1 AC1  5 GLY A  81  TYR A  82  LYS A 351  GLU A 365                    
SITE     2 AC1  5 ASP A 446                                                     
SITE     1 AC2  6 ASP A 150  MET A 153  PRO A 154  GLY A 155                    
SITE     2 AC2  6 HOH A 676  HOH A 759                                          
SITE     1 AC3  6 GLY B  81  TYR B 243  LYS B 351  GLU B 365                    
SITE     2 AC3  6 ASP B 446  SPD B 502                                          
SITE     1 AC4  8 ARG B 231  SER B 352  ALA B 355  GLY B 364                    
SITE     2 AC4  8 GLU B 365  GOL B 501  HOH B 604  HOH B 626                    
SITE     1 AC5  5 ASP B 150  MET B 153  GLY B 155  HOH B 680                    
SITE     2 AC5  5 HOH B 685                                                     
SITE     1 AC6  4 GLY C  81  LYS C 351  GLU C 365  ASP C 446                    
SITE     1 AC7  3 ASP C 150  MET C 153  GLY C 155                               
CRYST1   71.840   91.067  124.068  90.00 101.70  90.00 P 1 21 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      0.013920  0.000000  0.002882        0.00000                         
SCALE2      0.000000  0.010981  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008231        0.00000                         
TER    3753      LYS A 494                                                      
TER    7517      LYS B 494                                                      
TER   11267      LYS C 494                                                      
MASTER      627    0    7   56   41    0   12    611686    3   49  117          
END                                                                             

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

Acknowledgements and disclaimer