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Entry: 6ATF
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HEADER    IMMUNE SYSTEM                           29-AUG-17   6ATF              
TITLE     HLA-DRB1*1402 IN COMPLEX WITH VIMENTIN59-71                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;   
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 26-206;                                       
COMPND   5 SYNONYM: MHC CLASS II ANTIGEN DRA;                                   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: MHC CLASS II ANTIGEN;                                      
COMPND   9 CHAIN: B, E;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 30-219;                                       
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: VIMENTIN59-71;                                             
COMPND  14 CHAIN: C, F;                                                         
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HLA-DRA, HLA-DRA1;                                             
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: HLA-DRB1;                                                      
SOURCE  13 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  18 ORGANISM_TAXID: 32630                                                
KEYWDS    HLA CLASS II, IMMUNE SYSTEM                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.W.SCALLY,Y.T.TING,J.ROSSJOHN                                        
REVDAT   3   29-JUL-20 6ATF    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE   ATOM                              
REVDAT   2   18-OCT-17 6ATF    1       JRNL                                     
REVDAT   1   13-SEP-17 6ATF    0                                                
JRNL        AUTH   S.W.SCALLY,S.C.LAW,Y.T.TING,J.V.HEEMST,J.SOKOLOVE,           
JRNL        AUTH 2 A.J.DEUTSCH,E.BRIDIE CLEMENS,A.K.MOUSTAKAS,G.K.PAPADOPOULOS, 
JRNL        AUTH 3 D.V.WOUDE,I.SMOLIK,C.A.HITCHON,D.B.ROBINSON,E.D.FERUCCI,     
JRNL        AUTH 4 C.N.BERNSTEIN,X.MENG,V.ANAPARTI,T.HUIZINGA,K.KEDZIERSKA,     
JRNL        AUTH 5 H.H.REID,S.RAYCHAUDHURI,R.E.TOES,J.ROSSJOHN,H.EL-GABALAWY,   
JRNL        AUTH 6 R.THOMAS                                                     
JRNL        TITL   MOLECULAR BASIS FOR INCREASED SUSCEPTIBILITY OF INDIGENOUS   
JRNL        TITL 2 NORTH AMERICANS TO SEROPOSITIVE RHEUMATOID ARTHRITIS.        
JRNL        REF    ANN. RHEUM. DIS.              V.  76  1915 2017              
JRNL        REFN                   ISSN 1468-2060                               
JRNL        PMID   28801345                                                     
JRNL        DOI    10.1136/ANNRHEUMDIS-2017-211300                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.48                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 72003                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3632                            
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 33.4876 -  5.6173    1.00     2697   161  0.1840 0.1813        
REMARK   3     2  5.6173 -  4.4619    1.00     2680   136  0.1443 0.1807        
REMARK   3     3  4.4619 -  3.8989    1.00     2664   138  0.1351 0.1613        
REMARK   3     4  3.8989 -  3.5428    1.00     2622   154  0.1504 0.1718        
REMARK   3     5  3.5428 -  3.2891    1.00     2669   134  0.1545 0.1793        
REMARK   3     6  3.2891 -  3.0954    1.00     2636   140  0.1623 0.1900        
REMARK   3     7  3.0954 -  2.9404    1.00     2655   126  0.1682 0.2424        
REMARK   3     8  2.9404 -  2.8125    1.00     2669   139  0.1728 0.1923        
REMARK   3     9  2.8125 -  2.7043    1.00     2617   137  0.1724 0.1953        
REMARK   3    10  2.7043 -  2.6110    1.00     2635   137  0.1776 0.2138        
REMARK   3    11  2.6110 -  2.5294    1.00     2636   154  0.1701 0.2163        
REMARK   3    12  2.5294 -  2.4571    1.00     2603   138  0.1779 0.2380        
REMARK   3    13  2.4571 -  2.3924    1.00     2628   135  0.1817 0.2258        
REMARK   3    14  2.3924 -  2.3341    1.00     2631   138  0.1762 0.2285        
REMARK   3    15  2.3341 -  2.2810    1.00     2631   139  0.1723 0.2226        
REMARK   3    16  2.2810 -  2.2325    1.00     2606   142  0.1706 0.2027        
REMARK   3    17  2.2325 -  2.1879    1.00     2635   144  0.1768 0.2031        
REMARK   3    18  2.1879 -  2.1466    1.00     2629   122  0.1775 0.2084        
REMARK   3    19  2.1466 -  2.1083    1.00     2599   149  0.1755 0.2180        
REMARK   3    20  2.1083 -  2.0725    1.00     2640   156  0.1860 0.2240        
REMARK   3    21  2.0725 -  2.0391    1.00     2570   149  0.1913 0.2209        
REMARK   3    22  2.0391 -  2.0077    1.00     2627   147  0.1913 0.2327        
REMARK   3    23  2.0077 -  1.9782    1.00     2619   138  0.1940 0.2438        
REMARK   3    24  1.9782 -  1.9503    0.99     2629   127  0.2069 0.2515        
REMARK   3    25  1.9503 -  1.9240    0.99     2590   138  0.2224 0.2449        
REMARK   3    26  1.9240 -  1.8990    0.97     2554   114  0.2395 0.2651        
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)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.860           
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      :  0.004           6626                                  
REMARK   3   ANGLE     :  0.913           9006                                  
REMARK   3   CHIRALITY :  0.037            976                                  
REMARK   3   PLANARITY :  0.004           1173                                  
REMARK   3   DIHEDRAL  : 13.950           2416                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 26 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  44.8748   4.3740 114.3068              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0935 T22:   0.0835                                     
REMARK   3      T33:   0.0882 T12:   0.0286                                     
REMARK   3      T13:   0.0063 T23:  -0.0257                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9374 L22:   1.5101                                     
REMARK   3      L33:   2.3719 L12:   0.1547                                     
REMARK   3      L13:   0.9481 L23:  -1.6767                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0262 S12:   0.0541 S13:  -0.1246                       
REMARK   3      S21:  -0.0183 S22:   0.0161 S23:  -0.0145                       
REMARK   3      S31:   0.0409 S32:  -0.0099 S33:   0.0315                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 27 THROUGH 55 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  44.4942  -5.4391 106.3641              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1722 T22:   0.0957                                     
REMARK   3      T33:   0.2074 T12:   0.0014                                     
REMARK   3      T13:   0.0137 T23:  -0.0399                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4698 L22:   2.9424                                     
REMARK   3      L33:   2.6927 L12:   0.1300                                     
REMARK   3      L13:  -1.0495 L23:   1.1705                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0435 S12:   0.2013 S13:  -0.7121                       
REMARK   3      S21:   0.0450 S22:   0.0370 S23:  -0.1817                       
REMARK   3      S31:   0.4525 S32:   0.1390 S33:  -0.0621                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 56 THROUGH 76 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  54.8203   4.9213 123.0097              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1270 T22:   0.1289                                     
REMARK   3      T33:   0.1248 T12:   0.0108                                     
REMARK   3      T13:  -0.0124 T23:   0.0570                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2868 L22:   2.0370                                     
REMARK   3      L33:   6.1252 L12:   0.4379                                     
REMARK   3      L13:   0.5256 L23:   2.7864                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0271 S12:  -0.0391 S13:  -0.1392                       
REMARK   3      S21:   0.1117 S22:  -0.0979 S23:  -0.0476                       
REMARK   3      S31:   0.2036 S32:   0.1495 S33:   0.0371                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 77 THROUGH 101 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  27.7839   1.9457 119.2004              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1347 T22:   0.0901                                     
REMARK   3      T33:   0.0777 T12:  -0.0450                                     
REMARK   3      T13:   0.0271 T23:   0.0517                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2149 L22:   1.4552                                     
REMARK   3      L33:   2.0635 L12:   1.0425                                     
REMARK   3      L13:   1.3183 L23:   0.4831                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2552 S12:   0.0680 S13:   0.2383                       
REMARK   3      S21:  -0.1145 S22:   0.0671 S23:   0.2984                       
REMARK   3      S31:   0.0886 S32:  -0.1981 S33:   0.1743                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 102 THROUGH 154 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  29.3496  -2.8826 117.4500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1173 T22:   0.0566                                     
REMARK   3      T33:   0.1011 T12:   0.0068                                     
REMARK   3      T13:   0.0113 T23:   0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5143 L22:   0.4807                                     
REMARK   3      L33:   2.0489 L12:   1.0677                                     
REMARK   3      L13:   0.0104 L23:   0.2202                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0580 S12:   0.0371 S13:  -0.0873                       
REMARK   3      S21:  -0.0561 S22:  -0.0027 S23:  -0.0212                       
REMARK   3      S31:   0.1388 S32:  -0.0963 S33:   0.0341                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 155 THROUGH 166 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  17.0165  -9.3731 119.6624              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2098 T22:   0.2958                                     
REMARK   3      T33:   0.1926 T12:  -0.1524                                     
REMARK   3      T13:   0.0246 T23:   0.0349                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6990 L22:   2.0348                                     
REMARK   3      L33:   0.8732 L12:   0.6968                                     
REMARK   3      L13:  -1.1159 L23:  -0.4919                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0794 S12:   0.1497 S13:  -0.2749                       
REMARK   3      S21:   0.1937 S22:  -0.0055 S23:   0.1109                       
REMARK   3      S31:   0.4523 S32:  -0.6433 S33:  -0.0903                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 167 THROUGH 181 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  21.2619  -0.7732 124.9657              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0877 T22:   0.2442                                     
REMARK   3      T33:   0.1169 T12:   0.0010                                     
REMARK   3      T13:   0.0443 T23:   0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6475 L22:   3.2397                                     
REMARK   3      L33:   1.9228 L12:   0.4442                                     
REMARK   3      L13:  -1.7281 L23:   0.1619                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0908 S12:  -0.5505 S13:   0.2290                       
REMARK   3      S21:   0.0965 S22:  -0.2460 S23:   0.3560                       
REMARK   3      S31:   0.1915 S32:  -0.6189 S33:   0.2058                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 89 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  51.5002  14.2851 112.2493              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0834 T22:   0.0799                                     
REMARK   3      T33:   0.0847 T12:   0.0050                                     
REMARK   3      T13:  -0.0043 T23:   0.0115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4842 L22:   0.8720                                     
REMARK   3      L33:   1.9618 L12:   0.2826                                     
REMARK   3      L13:  -0.0362 L23:  -0.2674                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0324 S12:   0.0721 S13:   0.0438                       
REMARK   3      S21:   0.0167 S22:  -0.0042 S23:  -0.0407                       
REMARK   3      S31:  -0.1739 S32:   0.0245 S33:   0.0388                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 90 THROUGH 190 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  14.6741   7.2527  98.5826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1272 T22:   0.1000                                     
REMARK   3      T33:   0.1116 T12:  -0.0290                                     
REMARK   3      T13:  -0.0015 T23:  -0.0347                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3862 L22:   0.9096                                     
REMARK   3      L33:   1.2438 L12:  -1.3576                                     
REMARK   3      L13:  -0.0069 L23:   0.1976                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0278 S12:   0.2289 S13:  -0.0740                       
REMARK   3      S21:  -0.0646 S22:  -0.0501 S23:   0.1312                       
REMARK   3      S31:  -0.0972 S32:  -0.1137 S33:   0.0234                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 3 THROUGH 26 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  27.8349  35.3216 114.5136              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0601 T22:   0.0676                                     
REMARK   3      T33:   0.0806 T12:   0.0131                                     
REMARK   3      T13:  -0.0078 T23:  -0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3276 L22:   0.7218                                     
REMARK   3      L33:   6.9659 L12:   0.6905                                     
REMARK   3      L13:  -0.5393 L23:   0.1290                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0318 S12:   0.0330 S13:   0.1230                       
REMARK   3      S21:   0.0011 S22:   0.0738 S23:   0.0173                       
REMARK   3      S31:  -0.1886 S32:   0.1387 S33:  -0.0124                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 27 THROUGH 55 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  28.2067  45.1556 106.5348              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1603 T22:   0.0883                                     
REMARK   3      T33:   0.1921 T12:   0.0130                                     
REMARK   3      T13:  -0.0090 T23:   0.0378                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6831 L22:   3.1217                                     
REMARK   3      L33:   3.2826 L12:  -0.0203                                     
REMARK   3      L13:   0.9876 L23:  -0.9194                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0403 S12:   0.1190 S13:   0.6620                       
REMARK   3      S21:   0.0419 S22:  -0.0411 S23:   0.1262                       
REMARK   3      S31:  -0.5050 S32:  -0.0877 S33:  -0.0428                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 56 THROUGH 76 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  17.7305  34.7548 123.7334              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1141 T22:   0.1287                                     
REMARK   3      T33:   0.1187 T12:   0.0120                                     
REMARK   3      T13:   0.0167 T23:  -0.0576                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3707 L22:   2.3568                                     
REMARK   3      L33:   6.3124 L12:   0.3844                                     
REMARK   3      L13:  -0.6712 L23:  -2.8386                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0512 S12:  -0.1105 S13:   0.1784                       
REMARK   3      S21:   0.1743 S22:   0.0487 S23:   0.0811                       
REMARK   3      S31:  -0.1556 S32:  -0.2789 S33:  -0.0244                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 77 THROUGH 101 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  44.9114  37.7896 119.4162              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1068 T22:   0.1283                                     
REMARK   3      T33:   0.0563 T12:  -0.0427                                     
REMARK   3      T13:  -0.0389 T23:  -0.0137                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8805 L22:   1.3746                                     
REMARK   3      L33:   1.6637 L12:   0.5629                                     
REMARK   3      L13:  -1.3421 L23:  -0.2592                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2101 S12:   0.1277 S13:  -0.2167                       
REMARK   3      S21:  -0.1240 S22:   0.0065 S23:  -0.2866                       
REMARK   3      S31:  -0.0596 S32:   0.1414 S33:   0.2011                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 102 THROUGH 154 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  43.3467  42.5925 117.6392              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1415 T22:   0.0659                                     
REMARK   3      T33:   0.0774 T12:  -0.0067                                     
REMARK   3      T13:  -0.0067 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5030 L22:   0.5633                                     
REMARK   3      L33:   1.6464 L12:   0.7740                                     
REMARK   3      L13:   0.0125 L23:  -0.2977                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0738 S12:   0.0658 S13:   0.0776                       
REMARK   3      S21:  -0.0863 S22:  -0.0070 S23:   0.0076                       
REMARK   3      S31:  -0.2345 S32:   0.0466 S33:   0.0522                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 155 THROUGH 181 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  52.9306  44.0000 122.6793              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1455 T22:   0.2504                                     
REMARK   3      T33:   0.1219 T12:  -0.0741                                     
REMARK   3      T13:  -0.0201 T23:  -0.0115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7808 L22:   2.9815                                     
REMARK   3      L33:   2.1483 L12:   1.6257                                     
REMARK   3      L13:  -0.2312 L23:  -0.5502                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2056 S12:  -0.4220 S13:  -0.0500                       
REMARK   3      S21:   0.1365 S22:  -0.2842 S23:  -0.2508                       
REMARK   3      S31:  -0.3550 S32:   0.6931 S33:   0.0959                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 2 THROUGH 51 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  24.6225  24.9498 114.8585              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0666 T22:   0.0834                                     
REMARK   3      T33:   0.0769 T12:   0.0062                                     
REMARK   3      T13:   0.0049 T23:  -0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2263 L22:   1.1205                                     
REMARK   3      L33:   2.2714 L12:   0.0271                                     
REMARK   3      L13:  -0.0206 L23:   0.2678                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0064 S12:   0.0203 S13:  -0.0719                       
REMARK   3      S21:  -0.0153 S22:   0.0069 S23:  -0.0317                       
REMARK   3      S31:   0.0632 S32:   0.0538 S33:  -0.0115                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 52 THROUGH 89 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  16.4904  26.0611 108.9023              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0875 T22:   0.0981                                     
REMARK   3      T33:   0.0820 T12:   0.0132                                     
REMARK   3      T13:  -0.0046 T23:  -0.0296                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4708 L22:   1.9143                                     
REMARK   3      L33:   2.6823 L12:   1.1179                                     
REMARK   3      L13:  -1.2133 L23:  -0.6971                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0561 S12:   0.2325 S13:  -0.0353                       
REMARK   3      S21:   0.0439 S22:   0.0604 S23:   0.1401                       
REMARK   3      S31:   0.1647 S32:  -0.2314 S33:   0.0246                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 90 THROUGH 190 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  57.9331  32.6263  98.6132              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1244 T22:   0.1182                                     
REMARK   3      T33:   0.1141 T12:  -0.0253                                     
REMARK   3      T13:   0.0046 T23:   0.0316                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2446 L22:   0.9146                                     
REMARK   3      L33:   0.9269 L12:  -1.5301                                     
REMARK   3      L13:   0.0310 L23:  -0.2779                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0487 S12:   0.3019 S13:   0.1171                       
REMARK   3      S21:  -0.0514 S22:  -0.0914 S23:  -0.1469                       
REMARK   3      S31:   0.0791 S32:   0.0915 S33:   0.0393                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 13 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  56.2762   6.7543 113.7522              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1107 T22:   0.1055                                     
REMARK   3      T33:   0.1149 T12:   0.0222                                     
REMARK   3      T13:  -0.0143 T23:   0.0103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0257 L22:   2.9951                                     
REMARK   3      L33:   5.4895 L12:   1.6338                                     
REMARK   3      L13:   2.7332 L23:   3.2107                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0230 S12:   0.1596 S13:  -0.2537                       
REMARK   3      S21:   0.1848 S22:   0.2620 S23:  -0.3039                       
REMARK   3      S31:   0.0713 S32:   0.4030 S33:  -0.2565                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 13 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  16.4243  32.9560 113.9199              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1178 T22:   0.1190                                     
REMARK   3      T33:   0.1236 T12:   0.0195                                     
REMARK   3      T13:   0.0411 T23:  -0.0114                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1334 L22:   1.7834                                     
REMARK   3      L33:   3.2018 L12:   0.7958                                     
REMARK   3      L13:  -1.1652 L23:  -1.6368                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1157 S12:   0.0531 S13:   0.2743                       
REMARK   3      S21:   0.3078 S22:   0.1703 S23:   0.3597                       
REMARK   3      S31:  -0.2924 S32:  -0.2484 S33:  -0.3016                       
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 6ATF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229810.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : .95370                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 72027                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.482                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 4MCY                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG 3350, 0.2M POTASSIUM NITRATE,    
REMARK 280  0.1M BIS-TRIS-PROPANE PH 7.3, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 294K                                                    
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       38.88500            
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                                                    
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, G                            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, H                            
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     ILE A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     SER A   183                                                      
REMARK 465     GLY A   184                                                      
REMARK 465     ASP A   185                                                      
REMARK 465     ASP A   186                                                      
REMARK 465     ASP A   187                                                      
REMARK 465     ASP A   188                                                      
REMARK 465     LYS A   189                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     THR B   191                                                      
REMARK 465     GLY B   192                                                      
REMARK 465     GLY B   193                                                      
REMARK 465     ASP B   194                                                      
REMARK 465     ASP B   195                                                      
REMARK 465     ASP B   196                                                      
REMARK 465     ASP B   197                                                      
REMARK 465     LYS B   198                                                      
REMARK 465     ILE D     1                                                      
REMARK 465     LYS D     2                                                      
REMARK 465     THR D   182                                                      
REMARK 465     SER D   183                                                      
REMARK 465     GLY D   184                                                      
REMARK 465     ASP D   185                                                      
REMARK 465     ASP D   186                                                      
REMARK 465     ASP D   187                                                      
REMARK 465     ASP D   188                                                      
REMARK 465     LYS D   189                                                      
REMARK 465     GLY E    -1                                                      
REMARK 465     SER E     0                                                      
REMARK 465     GLY E     1                                                      
REMARK 465     THR E   191                                                      
REMARK 465     GLY E   192                                                      
REMARK 465     GLY E   193                                                      
REMARK 465     ASP E   194                                                      
REMARK 465     ASP E   195                                                      
REMARK 465     ASP E   196                                                      
REMARK 465     ASP E   197                                                      
REMARK 465     LYS E   198                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  71    CG   CD   OE1  OE2                                  
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    GLN B  34      -10.44     75.77                                   
REMARK 500    TYR B  78      -61.05   -121.83                                   
REMARK 500    THR B  90      -72.39   -123.12                                   
REMARK 500    ASN B 113       22.24   -140.38                                   
REMARK 500    GLN E  34      -10.71     75.89                                   
REMARK 500    TYR E  78      -61.54   -121.59                                   
REMARK 500    THR E  90      -73.03   -122.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6ATF A    1   181  UNP    P01903   DRA_HUMAN       26    206             
DBREF1 6ATF B    1   190  UNP                  A0A0A1I7H6_HUMAN                 
DBREF2 6ATF B     A0A0A1I7H6                         30         219             
DBREF  6ATF D    1   181  UNP    P01903   DRA_HUMAN       26    206             
DBREF1 6ATF E    1   190  UNP                  A0A0A1I7H6_HUMAN                 
DBREF2 6ATF E     A0A0A1I7H6                         30         219             
DBREF  6ATF C    1    13  PDB    6ATF     6ATF             1     13             
DBREF  6ATF F    1    13  PDB    6ATF     6ATF             1     13             
SEQADV 6ATF THR A  182  UNP  P01903              EXPRESSION TAG                 
SEQADV 6ATF SER A  183  UNP  P01903              EXPRESSION TAG                 
SEQADV 6ATF GLY A  184  UNP  P01903              EXPRESSION TAG                 
SEQADV 6ATF ASP A  185  UNP  P01903              EXPRESSION TAG                 
SEQADV 6ATF ASP A  186  UNP  P01903              EXPRESSION TAG                 
SEQADV 6ATF ASP A  187  UNP  P01903              EXPRESSION TAG                 
SEQADV 6ATF ASP A  188  UNP  P01903              EXPRESSION TAG                 
SEQADV 6ATF LYS A  189  UNP  P01903              EXPRESSION TAG                 
SEQADV 6ATF GLY B   -1  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF SER B    0  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF THR B  191  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF GLY B  192  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF GLY B  193  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF ASP B  194  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF ASP B  195  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF ASP B  196  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF ASP B  197  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF LYS B  198  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF THR D  182  UNP  P01903              EXPRESSION TAG                 
SEQADV 6ATF SER D  183  UNP  P01903              EXPRESSION TAG                 
SEQADV 6ATF GLY D  184  UNP  P01903              EXPRESSION TAG                 
SEQADV 6ATF ASP D  185  UNP  P01903              EXPRESSION TAG                 
SEQADV 6ATF ASP D  186  UNP  P01903              EXPRESSION TAG                 
SEQADV 6ATF ASP D  187  UNP  P01903              EXPRESSION TAG                 
SEQADV 6ATF ASP D  188  UNP  P01903              EXPRESSION TAG                 
SEQADV 6ATF LYS D  189  UNP  P01903              EXPRESSION TAG                 
SEQADV 6ATF GLY E   -1  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF SER E    0  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF THR E  191  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF GLY E  192  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF GLY E  193  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF ASP E  194  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF ASP E  195  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF ASP E  196  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF ASP E  197  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQADV 6ATF LYS E  198  UNP  A0A0A1I7H           EXPRESSION TAG                 
SEQRES   1 A  189  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR          
SEQRES   2 A  189  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE          
SEQRES   3 A  189  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS          
SEQRES   4 A  189  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA          
SEQRES   5 A  189  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL          
SEQRES   6 A  189  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN          
SEQRES   7 A  189  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL          
SEQRES   8 A  189  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL          
SEQRES   9 A  189  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL          
SEQRES  10 A  189  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR          
SEQRES  11 A  189  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS          
SEQRES  12 A  189  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER          
SEQRES  13 A  189  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 A  189  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP THR          
SEQRES  15 A  189  SER GLY ASP ASP ASP ASP LYS                                  
SEQRES   1 B  200  GLY SER GLY ASP THR ARG PRO ARG PHE LEU GLU TYR SER          
SEQRES   2 B  200  THR SER GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL          
SEQRES   3 B  200  ARG PHE LEU GLU ARG TYR PHE HIS ASN GLN GLU GLU ASN          
SEQRES   4 B  200  VAL ARG PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL          
SEQRES   5 B  200  THR GLU LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER          
SEQRES   6 B  200  GLN LYS ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP          
SEQRES   7 B  200  THR TYR CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE          
SEQRES   8 B  200  THR VAL GLN ARG ARG VAL HIS PRO LYS VAL THR VAL TYR          
SEQRES   9 B  200  PRO SER LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU          
SEQRES  10 B  200  VAL CYS SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU          
SEQRES  11 B  200  VAL ARG TRP PHE ARG ASN GLY GLN GLU GLU LYS THR GLY          
SEQRES  12 B  200  VAL VAL SER THR GLY LEU ILE HIS ASN GLY ASP TRP THR          
SEQRES  13 B  200  PHE GLN THR LEU VAL MET LEU GLU THR VAL PRO ARG SER          
SEQRES  14 B  200  GLY GLU VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL          
SEQRES  15 B  200  THR SER PRO LEU THR VAL GLU TRP ARG ALA THR GLY GLY          
SEQRES  16 B  200  ASP ASP ASP ASP LYS                                          
SEQRES   1 D  189  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR          
SEQRES   2 D  189  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE          
SEQRES   3 D  189  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS          
SEQRES   4 D  189  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA          
SEQRES   5 D  189  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL          
SEQRES   6 D  189  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN          
SEQRES   7 D  189  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL          
SEQRES   8 D  189  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL          
SEQRES   9 D  189  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL          
SEQRES  10 D  189  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR          
SEQRES  11 D  189  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS          
SEQRES  12 D  189  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER          
SEQRES  13 D  189  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 D  189  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP THR          
SEQRES  15 D  189  SER GLY ASP ASP ASP ASP LYS                                  
SEQRES   1 E  200  GLY SER GLY ASP THR ARG PRO ARG PHE LEU GLU TYR SER          
SEQRES   2 E  200  THR SER GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL          
SEQRES   3 E  200  ARG PHE LEU GLU ARG TYR PHE HIS ASN GLN GLU GLU ASN          
SEQRES   4 E  200  VAL ARG PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL          
SEQRES   5 E  200  THR GLU LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER          
SEQRES   6 E  200  GLN LYS ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP          
SEQRES   7 E  200  THR TYR CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE          
SEQRES   8 E  200  THR VAL GLN ARG ARG VAL HIS PRO LYS VAL THR VAL TYR          
SEQRES   9 E  200  PRO SER LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU          
SEQRES  10 E  200  VAL CYS SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU          
SEQRES  11 E  200  VAL ARG TRP PHE ARG ASN GLY GLN GLU GLU LYS THR GLY          
SEQRES  12 E  200  VAL VAL SER THR GLY LEU ILE HIS ASN GLY ASP TRP THR          
SEQRES  13 E  200  PHE GLN THR LEU VAL MET LEU GLU THR VAL PRO ARG SER          
SEQRES  14 E  200  GLY GLU VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL          
SEQRES  15 E  200  THR SER PRO LEU THR VAL GLU TRP ARG ALA THR GLY GLY          
SEQRES  16 E  200  ASP ASP ASP ASP LYS                                          
SEQRES   1 C   13  GLY VAL TYR ALA THR ARG SER SER ALA VAL ARG LEU ARG          
SEQRES   1 F   13  GLY VAL TYR ALA THR ARG SER SER ALA VAL ARG LEU ARG          
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET    NAG  A 500      14                                                       
HET    EDO  B 201       4                                                       
HET    EDO  B 202       4                                                       
HET    EDO  B 203       4                                                       
HET    EDO  B 204       4                                                       
HET    PGE  B 205      10                                                       
HET    PGE  B 206      10                                                       
HET    NAG  D 500      14                                                       
HET    EDO  E 201       4                                                       
HET    EDO  E 202       4                                                       
HET    EDO  E 203       4                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   7  NAG    6(C8 H15 N O6)                                               
FORMUL  10  EDO    7(C2 H6 O2)                                                  
FORMUL  14  PGE    2(C6 H14 O4)                                                 
FORMUL  20  HOH   *1017(H2 O)                                                   
HELIX    1 AA1 LEU A   45  PHE A   51  5                                   7    
HELIX    2 AA2 GLU A   55  SER A   77  1                                  23    
HELIX    3 AA3 THR B   51  LEU B   53  5                                   3    
HELIX    4 AA4 GLY B   54  SER B   63  1                                  10    
HELIX    5 AA5 GLN B   64  ALA B   73  1                                  10    
HELIX    6 AA6 ALA B   73  TYR B   78  1                                   6    
HELIX    7 AA7 TYR B   78  GLU B   87  1                                  10    
HELIX    8 AA8 SER B   88  THR B   90  5                                   3    
HELIX    9 AA9 LEU D   45  PHE D   51  5                                   7    
HELIX   10 AB1 GLU D   55  SER D   77  1                                  23    
HELIX   11 AB2 THR E   51  LEU E   53  5                                   3    
HELIX   12 AB3 GLY E   54  SER E   63  1                                  10    
HELIX   13 AB4 GLN E   64  ALA E   73  1                                  10    
HELIX   14 AB5 ALA E   73  TYR E   78  1                                   6    
HELIX   15 AB6 TYR E   78  GLU E   87  1                                  10    
HELIX   16 AB7 SER E   88  THR E   90  5                                   3    
SHEET    1 AA1 8 GLU A  40  TRP A  43  0                                        
SHEET    2 AA1 8 ASP A  29  ASP A  35 -1  N  HIS A  33   O  VAL A  42           
SHEET    3 AA1 8 SER A  19  PHE A  26 -1  N  PHE A  26   O  ASP A  29           
SHEET    4 AA1 8 HIS A   5  ASN A  15 -1  N  ILE A   8   O  ASP A  25           
SHEET    5 AA1 8 PHE B   7  PHE B  18 -1  O  PHE B  17   N  HIS A   5           
SHEET    6 AA1 8 ARG B  23  HIS B  32 -1  O  LEU B  27   N  GLU B  14           
SHEET    7 AA1 8 GLU B  35  ASP B  41 -1  O  PHE B  40   N  GLU B  28           
SHEET    8 AA1 8 TYR B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39           
SHEET    1 AA2 4 GLU A  88  THR A  93  0                                        
SHEET    2 AA2 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92           
SHEET    3 AA2 4 PHE A 145  PHE A 153 -1  O  LYS A 147   N  ILE A 109           
SHEET    4 AA2 4 SER A 133  GLU A 134 -1  N  SER A 133   O  TYR A 150           
SHEET    1 AA3 4 GLU A  88  THR A  93  0                                        
SHEET    2 AA3 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92           
SHEET    3 AA3 4 PHE A 145  PHE A 153 -1  O  LYS A 147   N  ILE A 109           
SHEET    4 AA3 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  ARG A 146           
SHEET    1 AA4 4 LYS A 126  VAL A 128  0                                        
SHEET    2 AA4 4 ASN A 118  ARG A 123 -1  N  ARG A 123   O  LYS A 126           
SHEET    3 AA4 4 TYR A 161  GLU A 166 -1  O  ARG A 164   N  THR A 120           
SHEET    4 AA4 4 LEU A 174  TRP A 178 -1  O  TRP A 178   N  TYR A 161           
SHEET    1 AA5 4 LYS B  98  SER B 104  0                                        
SHEET    2 AA5 4 LEU B 114  PHE B 122 -1  O  VAL B 116   N  TYR B 102           
SHEET    3 AA5 4 PHE B 155  GLU B 162 -1  O  THR B 157   N  VAL B 119           
SHEET    4 AA5 4 VAL B 142  SER B 144 -1  N  VAL B 143   O  MET B 160           
SHEET    1 AA6 4 LYS B  98  SER B 104  0                                        
SHEET    2 AA6 4 LEU B 114  PHE B 122 -1  O  VAL B 116   N  TYR B 102           
SHEET    3 AA6 4 PHE B 155  GLU B 162 -1  O  THR B 157   N  VAL B 119           
SHEET    4 AA6 4 ILE B 148  HIS B 149 -1  N  ILE B 148   O  GLN B 156           
SHEET    1 AA7 4 GLN B 136  GLU B 138  0                                        
SHEET    2 AA7 4 GLU B 128  ARG B 133 -1  N  ARG B 133   O  GLN B 136           
SHEET    3 AA7 4 VAL B 170  GLU B 176 -1  O  GLN B 174   N  ARG B 130           
SHEET    4 AA7 4 LEU B 184  ARG B 189 -1  O  TRP B 188   N  TYR B 171           
SHEET    1 AA8 8 GLU D  40  TRP D  43  0                                        
SHEET    2 AA8 8 ASP D  29  ASP D  35 -1  N  HIS D  33   O  VAL D  42           
SHEET    3 AA8 8 SER D  19  PHE D  26 -1  N  PHE D  26   O  ASP D  29           
SHEET    4 AA8 8 HIS D   5  ASN D  15 -1  N  ILE D   8   O  ASP D  25           
SHEET    5 AA8 8 PHE E   7  PHE E  18 -1  O  PHE E  17   N  HIS D   5           
SHEET    6 AA8 8 ARG E  23  HIS E  32 -1  O  PHE E  31   N  TYR E  10           
SHEET    7 AA8 8 GLU E  35  ASP E  41 -1  O  PHE E  40   N  GLU E  28           
SHEET    8 AA8 8 TYR E  47  ALA E  49 -1  O  ARG E  48   N  ARG E  39           
SHEET    1 AA9 4 GLU D  88  THR D  93  0                                        
SHEET    2 AA9 4 ASN D 103  PHE D 112 -1  O  ILE D 106   N  LEU D  92           
SHEET    3 AA9 4 PHE D 145  PHE D 153 -1  O  LEU D 151   N  LEU D 105           
SHEET    4 AA9 4 SER D 133  GLU D 134 -1  N  SER D 133   O  TYR D 150           
SHEET    1 AB1 4 GLU D  88  THR D  93  0                                        
SHEET    2 AB1 4 ASN D 103  PHE D 112 -1  O  ILE D 106   N  LEU D  92           
SHEET    3 AB1 4 PHE D 145  PHE D 153 -1  O  LEU D 151   N  LEU D 105           
SHEET    4 AB1 4 LEU D 138  PRO D 139 -1  N  LEU D 138   O  ARG D 146           
SHEET    1 AB2 4 LYS D 126  VAL D 128  0                                        
SHEET    2 AB2 4 ASN D 118  ARG D 123 -1  N  ARG D 123   O  LYS D 126           
SHEET    3 AB2 4 TYR D 161  GLU D 166 -1  O  ARG D 164   N  THR D 120           
SHEET    4 AB2 4 LEU D 174  TRP D 178 -1  O  TRP D 178   N  TYR D 161           
SHEET    1 AB3 4 LYS E  98  SER E 104  0                                        
SHEET    2 AB3 4 LEU E 114  PHE E 122 -1  O  VAL E 116   N  TYR E 102           
SHEET    3 AB3 4 PHE E 155  GLU E 162 -1  O  LEU E 161   N  LEU E 115           
SHEET    4 AB3 4 VAL E 142  SER E 144 -1  N  VAL E 143   O  MET E 160           
SHEET    1 AB4 4 LYS E  98  SER E 104  0                                        
SHEET    2 AB4 4 LEU E 114  PHE E 122 -1  O  VAL E 116   N  TYR E 102           
SHEET    3 AB4 4 PHE E 155  GLU E 162 -1  O  LEU E 161   N  LEU E 115           
SHEET    4 AB4 4 ILE E 148  HIS E 149 -1  N  ILE E 148   O  GLN E 156           
SHEET    1 AB5 4 GLN E 136  GLU E 138  0                                        
SHEET    2 AB5 4 GLU E 128  ARG E 133 -1  N  TRP E 131   O  GLU E 138           
SHEET    3 AB5 4 VAL E 170  GLU E 176 -1  O  GLN E 174   N  ARG E 130           
SHEET    4 AB5 4 LEU E 184  ARG E 189 -1  O  TRP E 188   N  TYR E 171           
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.03  
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.05  
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.02  
SSBOND   4 CYS D  107    CYS D  163                          1555   1555  2.03  
SSBOND   5 CYS E   15    CYS E   79                          1555   1555  2.06  
SSBOND   6 CYS E  117    CYS E  173                          1555   1555  2.04  
LINK         ND2 ASN A  78                 C1  NAG A 500     1555   1555  1.45  
LINK         ND2 ASN A 118                 C1  NAG G   1     1555   1555  1.44  
LINK         ND2 ASN D  78                 C1  NAG D 500     1555   1555  1.45  
LINK         ND2 ASN D 118                 C1  NAG H   1     1555   1555  1.43  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.44  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.43  
CISPEP   1 ASN A   15    PRO A   16          0         2.03                     
CISPEP   2 THR A  113    PRO A  114          0         0.32                     
CISPEP   3 TYR B  123    PRO B  124          0         4.77                     
CISPEP   4 ASN D   15    PRO D   16          0         1.91                     
CISPEP   5 THR D  113    PRO D  114          0        -0.35                     
CISPEP   6 TYR E  123    PRO E  124          0         4.06                     
CRYST1   66.980   77.770   94.540  90.00 109.52  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014930  0.000000  0.005293        0.00000                         
SCALE2      0.000000  0.012858  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011223        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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