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Database: PDB
Entry: 4U3J
LinkDB: 4U3J
Original site: 4U3J 
HEADER    STRUCTURAL PROTEIN/PROTEIN BINDING      22-JUL-14   4U3J              
TITLE     TOG2:ALPHA/BETA-TUBULIN COMPLEX                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUBULIN ALPHA-1 CHAIN;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: TUBULIN BETA CHAIN;                                        
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: BETA-TUBULIN;                                               
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES;                                                       
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: PROTEIN STU2;                                              
COMPND  13 CHAIN: C;                                                            
COMPND  14 FRAGMENT: TOG2 DOMAIN (UNP RESIDUES 318-560);                        
COMPND  15 SYNONYM: SUPPRESSOR OF TUBULIN 2;                                    
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: TUB1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JEL1;                                      
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  11 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  12 ORGANISM_TAXID: 4932;                                                
SOURCE  13 GENE: TUB2;                                                          
SOURCE  14 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: JEL1;                                      
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  19 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  20 ORGANISM_TAXID: 4932;                                                
SOURCE  21 GENE: STU2;                                                          
SOURCE  22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  23 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  24 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  25 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  26 EXPRESSION_SYSTEM_PLASMID: PET-29B                                   
KEYWDS    COMPLEX, STRUCTURAL PROTEIN-PROTEIN BINDING COMPLEX                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.AYAZ,L.M.RICE                                                       
REVDAT   4   25-DEC-19 4U3J    1       REMARK                                   
REVDAT   3   27-SEP-17 4U3J    1       SOURCE REMARK                            
REVDAT   2   01-OCT-14 4U3J    1       JRNL                                     
REVDAT   1   20-AUG-14 4U3J    0                                                
JRNL        AUTH   P.AYAZ,S.MUNYOKI,E.A.GEYER,F.A.PIEDRA,E.S.VU,R.BROMBERG,     
JRNL        AUTH 2 Z.OTWINOWSKI,N.V.GRISHIN,C.A.BRAUTIGAM,L.M.RICE              
JRNL        TITL   A TETHERED DELIVERY MECHANISM EXPLAINS THE CATALYTIC ACTION  
JRNL        TITL 2 OF A MICROTUBULE POLYMERASE.                                 
JRNL        REF    ELIFE                         V.   3 03069 2014              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   25097237                                                     
JRNL        DOI    10.7554/ELIFE.03069                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.81 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1627)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.81                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.07                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.480                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 26230                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1305                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 34.0713 -  5.8357    0.99     3245   172  0.1853 0.1962        
REMARK   3     2  5.8357 -  4.6357    0.99     3192   165  0.1937 0.2405        
REMARK   3     3  4.6357 -  4.0508    0.99     3190   168  0.1768 0.2305        
REMARK   3     4  4.0508 -  3.6809    0.99     3178   158  0.2081 0.2538        
REMARK   3     5  3.6809 -  3.4173    0.98     3093   172  0.2418 0.2883        
REMARK   3     6  3.4173 -  3.2160    0.95     3043   157  0.2665 0.3088        
REMARK   3     7  3.2160 -  3.0551    0.85     2729   146  0.2993 0.3333        
REMARK   3     8  3.0551 -  2.9221    0.66     2110   110  0.3198 0.3548        
REMARK   3     9  2.9221 -  2.8097    0.36     1145    57  0.3296 0.4115        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.430            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.700           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           8677                                  
REMARK   3   ANGLE     :  0.656          11784                                  
REMARK   3   CHIRALITY :  0.026           1318                                  
REMARK   3   PLANARITY :  0.003           1526                                  
REMARK   3   DIHEDRAL  : 15.335           3151                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 24                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 89 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -79.2425 -12.7991  29.1083              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3924 T22:   0.5042                                     
REMARK   3      T33:   0.3389 T12:   0.1130                                     
REMARK   3      T13:  -0.0664 T23:   0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1699 L22:   1.5138                                     
REMARK   3      L33:   2.5875 L12:  -1.7443                                     
REMARK   3      L13:   0.3899 L23:   1.1625                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0370 S12:   0.2180 S13:  -0.0825                       
REMARK   3      S21:  -0.2541 S22:   0.0753 S23:   0.2486                       
REMARK   3      S31:  -0.4820 S32:  -0.4269 S33:  -0.0078                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 90 THROUGH 129 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -64.8881 -23.5810  22.6410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4799 T22:   0.4939                                     
REMARK   3      T33:   0.3306 T12:   0.0470                                     
REMARK   3      T13:  -0.0257 T23:   0.0082                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8888 L22:   1.0598                                     
REMARK   3      L33:   1.7640 L12:   1.3191                                     
REMARK   3      L13:   0.7153 L23:   1.1244                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1377 S12:   0.6687 S13:  -0.0915                       
REMARK   3      S21:  -0.9382 S22:  -0.1227 S23:   0.2159                       
REMARK   3      S31:   0.1535 S32:  -0.2092 S33:  -0.0001                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 130 THROUGH 183 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -61.2537 -15.5633  30.8850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4322 T22:   0.2974                                     
REMARK   3      T33:   0.3911 T12:   0.0121                                     
REMARK   3      T13:  -0.0080 T23:  -0.0315                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1287 L22:   1.9771                                     
REMARK   3      L33:   0.2941 L12:   0.0185                                     
REMARK   3      L13:  -0.3750 L23:   0.3537                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0032 S12:   0.2895 S13:   0.3562                       
REMARK   3      S21:  -0.1175 S22:  -0.2944 S23:  -0.2583                       
REMARK   3      S31:  -0.3144 S32:   0.4087 S33:  -0.0017                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 184 THROUGH 224 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -61.4292 -16.6918  43.9216              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3399 T22:   0.3278                                     
REMARK   3      T33:   0.3519 T12:  -0.0242                                     
REMARK   3      T13:  -0.0586 T23:  -0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9627 L22:   1.8649                                     
REMARK   3      L33:   0.1464 L12:  -1.0127                                     
REMARK   3      L13:   0.5336 L23:   0.3741                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0927 S12:  -0.4198 S13:  -0.0326                       
REMARK   3      S21:   0.1027 S22:  -0.1649 S23:   0.2066                       
REMARK   3      S31:  -0.3804 S32:   0.4144 S33:   0.0016                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 225 THROUGH 260 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -69.0204  -3.3803  37.4320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6015 T22:   0.4293                                     
REMARK   3      T33:   0.6213 T12:   0.0255                                     
REMARK   3      T13:  -0.0403 T23:   0.0685                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4550 L22:   1.1757                                     
REMARK   3      L33:   0.3716 L12:  -1.1957                                     
REMARK   3      L13:  -0.3984 L23:   0.7430                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0607 S12:   0.2519 S13:   0.8920                       
REMARK   3      S21:  -0.3891 S22:   0.1015 S23:   0.3755                       
REMARK   3      S31:  -0.6230 S32:  -0.3631 S33:   0.0001                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 261 THROUGH 280 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -62.0233  -5.2024  43.8677              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3462 T22:   0.2282                                     
REMARK   3      T33:   0.5076 T12:  -0.0328                                     
REMARK   3      T13:  -0.1335 T23:  -0.0329                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8438 L22:   1.7264                                     
REMARK   3      L33:   2.3286 L12:  -1.1366                                     
REMARK   3      L13:   0.6192 L23:   0.1606                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1289 S12:  -0.1879 S13:   0.3591                       
REMARK   3      S21:   0.0757 S22:  -0.1016 S23:  -0.0962                       
REMARK   3      S31:  -0.4590 S32:  -0.0756 S33:   0.0006                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 288 THROUGH 301 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -66.6640   0.8635  54.8549              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6696 T22:   0.4633                                     
REMARK   3      T33:   0.7202 T12:   0.1011                                     
REMARK   3      T13:  -0.0141 T23:  -0.0988                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1600 L22:   0.3546                                     
REMARK   3      L33:   0.0830 L12:  -0.2195                                     
REMARK   3      L13:  -0.0940 L23:   0.1316                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4055 S12:  -1.3352 S13:   0.0910                       
REMARK   3      S21:   0.4752 S22:  -0.0119 S23:   0.7012                       
REMARK   3      S31:  -0.1379 S32:  -0.2130 S33:  -0.0066                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 302 THROUGH 315 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -56.0340  -4.5269  51.0968              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5025 T22:   0.3821                                     
REMARK   3      T33:   0.6130 T12:  -0.0659                                     
REMARK   3      T13:  -0.0633 T23:  -0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1840 L22:   0.4702                                     
REMARK   3      L33:   1.2234 L12:  -0.3399                                     
REMARK   3      L13:  -0.1853 L23:   0.2438                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4308 S12:   0.1444 S13:  -0.2493                       
REMARK   3      S21:  -0.4128 S22:  -0.5985 S23:  -0.4852                       
REMARK   3      S31:  -0.1685 S32:  -0.0651 S33:   0.0030                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 316 THROUGH 325 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -71.0607   5.5632  44.8561              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4551 T22:   0.4603                                     
REMARK   3      T33:   0.8512 T12:  -0.0158                                     
REMARK   3      T13:   0.0422 T23:  -0.0203                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2322 L22:   0.2334                                     
REMARK   3      L33:   0.9233 L12:  -0.1796                                     
REMARK   3      L13:   0.4956 L23:  -0.3290                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0353 S12:  -0.0121 S13:   1.5616                       
REMARK   3      S21:  -1.8089 S22:   0.4483 S23:   0.0770                       
REMARK   3      S31:  -0.0149 S32:   0.1513 S33:   0.0089                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 326 THROUGH 339 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -65.9893  12.8558  52.8979              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8498 T22:   0.9243                                     
REMARK   3      T33:   1.2371 T12:  -0.0176                                     
REMARK   3      T13:  -0.1977 T23:   0.2872                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1907 L22:   0.2418                                     
REMARK   3      L33:   0.4315 L12:   0.0555                                     
REMARK   3      L13:  -0.1375 L23:   0.2823                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4742 S12:  -0.4344 S13:   1.2783                       
REMARK   3      S21:   1.1313 S22:  -0.5291 S23:   0.1566                       
REMARK   3      S31:   0.6138 S32:   1.1087 S33:  -0.0002                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 340 THROUGH 382 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -67.5375   1.3887  46.0136              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7001 T22:   0.5171                                     
REMARK   3      T33:   0.4419 T12:   0.0656                                     
REMARK   3      T13:  -0.0421 T23:   0.0943                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6289 L22:   2.1441                                     
REMARK   3      L33:   2.6466 L12:  -3.0739                                     
REMARK   3      L13:  -1.3129 L23:   0.5503                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3812 S12:  -0.6184 S13:   0.7386                       
REMARK   3      S21:  -0.0668 S22:  -0.4835 S23:   0.2243                       
REMARK   3      S31:  -0.3744 S32:   0.1434 S33:  -0.0046                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 383 THROUGH 402 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -48.4321 -19.8714  46.5140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3397 T22:   0.4007                                     
REMARK   3      T33:   0.4960 T12:   0.0207                                     
REMARK   3      T13:  -0.0379 T23:  -0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2866 L22:   2.6657                                     
REMARK   3      L33:  -0.0887 L12:  -1.0542                                     
REMARK   3      L13:  -0.2629 L23:   0.0510                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6533 S12:  -0.1478 S13:   0.3046                       
REMARK   3      S21:   1.1470 S22:   0.5675 S23:   0.0124                       
REMARK   3      S31:   0.0607 S32:   0.0972 S33:  -0.0103                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 403 THROUGH 415 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -48.6341 -33.5740  33.9468              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3003 T22:   0.2723                                     
REMARK   3      T33:   0.3190 T12:   0.0383                                     
REMARK   3      T13:   0.0303 T23:   0.0156                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4162 L22:   1.0350                                     
REMARK   3      L33:   1.4256 L12:   0.0759                                     
REMARK   3      L13:  -0.4756 L23:   0.2466                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3786 S12:   0.0650 S13:  -0.0006                       
REMARK   3      S21:  -0.6246 S22:  -0.2538 S23:  -0.2009                       
REMARK   3      S31:  -0.2212 S32:  -0.1770 S33:  -0.0227                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 416 THROUGH 438 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -43.6204 -14.4108  39.1329              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3902 T22:   0.5086                                     
REMARK   3      T33:   0.5090 T12:  -0.0577                                     
REMARK   3      T13:   0.0278 T23:   0.0438                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5642 L22:   1.1295                                     
REMARK   3      L33:   1.1325 L12:  -1.5699                                     
REMARK   3      L13:   1.1490 L23:  -0.2588                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2502 S12:  -0.2606 S13:   0.5489                       
REMARK   3      S21:  -0.4177 S22:   0.4735 S23:  -0.3467                       
REMARK   3      S31:  -0.5184 S32:   0.6681 S33:   0.0084                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 126 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -72.1311 -57.2018  31.7535              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3997 T22:   0.4567                                     
REMARK   3      T33:   0.5469 T12:  -0.1112                                     
REMARK   3      T13:  -0.0246 T23:  -0.0919                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7768 L22:   2.0502                                     
REMARK   3      L33:   3.1165 L12:  -0.5590                                     
REMARK   3      L13:  -0.7107 L23:  -0.5862                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0446 S12:   0.4135 S13:  -0.4215                       
REMARK   3      S21:  -0.1470 S22:  -0.0377 S23:   0.7076                       
REMARK   3      S31:   0.4234 S32:  -0.6141 S33:  -0.0007                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 127 THROUGH 236 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -59.7548 -56.9079  39.9917              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4247 T22:   0.3017                                     
REMARK   3      T33:   0.4533 T12:   0.0168                                     
REMARK   3      T13:   0.0316 T23:   0.0084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6517 L22:   1.6896                                     
REMARK   3      L33:   2.8475 L12:  -1.0205                                     
REMARK   3      L13:  -0.2485 L23:   0.6663                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1160 S12:  -0.0777 S13:  -0.2424                       
REMARK   3      S21:   0.1595 S22:  -0.1117 S23:   0.0169                       
REMARK   3      S31:   0.5857 S32:   0.0999 S33:  -0.0036                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 237 THROUGH 266 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -61.2038 -40.8357  40.5043              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3970 T22:   0.3062                                     
REMARK   3      T33:   0.3370 T12:   0.0793                                     
REMARK   3      T13:   0.0228 T23:   0.0662                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6235 L22:   3.5926                                     
REMARK   3      L33:   3.7722 L12:   2.5809                                     
REMARK   3      L13:  -0.0433 L23:   0.4853                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0339 S12:  -0.3216 S13:   0.7816                       
REMARK   3      S21:   0.0699 S22:  -0.1432 S23:   0.4463                       
REMARK   3      S31:   0.0087 S32:  -0.1646 S33:  -0.0002                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 267 THROUGH 371 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -63.8757 -41.6252  55.9078              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5265 T22:   0.4299                                     
REMARK   3      T33:   0.5040 T12:   0.0069                                     
REMARK   3      T13:   0.0551 T23:   0.0419                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9044 L22:   0.6498                                     
REMARK   3      L33:   1.9337 L12:  -0.9954                                     
REMARK   3      L13:  -1.3675 L23:  -0.2591                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0573 S12:  -0.4710 S13:  -0.0908                       
REMARK   3      S21:   0.4900 S22:   0.0381 S23:   0.3750                       
REMARK   3      S31:   0.1375 S32:  -0.1201 S33:  -0.0004                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 372 THROUGH 404 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -44.8403 -65.6692  42.6290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6652 T22:   0.4357                                     
REMARK   3      T33:   0.5234 T12:   0.1652                                     
REMARK   3      T13:  -0.0666 T23:   0.0939                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0862 L22:   1.4440                                     
REMARK   3      L33:   1.0183 L12:   0.3536                                     
REMARK   3      L13:  -0.7967 L23:  -0.8440                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1067 S12:  -0.2224 S13:  -0.5351                       
REMARK   3      S21:   0.2593 S22:   0.2083 S23:  -0.5566                       
REMARK   3      S31:   0.6842 S32:   0.1213 S33:   0.0015                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 405 THROUGH 430 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -41.4218 -51.6619  43.8344              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4168 T22:   0.6769                                     
REMARK   3      T33:   0.4306 T12:   0.0744                                     
REMARK   3      T13:  -0.0380 T23:   0.0922                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1303 L22:   1.2922                                     
REMARK   3      L33:   0.7242 L12:  -0.8029                                     
REMARK   3      L13:   0.9125 L23:  -0.3176                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5388 S12:  -0.0267 S13:  -0.1425                       
REMARK   3      S21:   0.6216 S22:   0.7246 S23:  -0.6071                       
REMARK   3      S31:   0.2732 S32:   0.9653 S33:  -0.1109                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 319 THROUGH 369 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -39.5903 -74.5645   7.3706              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8178 T22:   0.7902                                     
REMARK   3      T33:   0.4548 T12:   0.2447                                     
REMARK   3      T13:  -0.0052 T23:  -0.2624                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2436 L22:   2.9736                                     
REMARK   3      L33:   2.1375 L12:  -1.2266                                     
REMARK   3      L13:   0.7237 L23:   0.9302                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1719 S12:   0.5326 S13:  -1.2200                       
REMARK   3      S21:   0.0677 S22:  -0.0597 S23:  -0.2511                       
REMARK   3      S31:   0.9461 S32:   0.5984 S33:   0.0498                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 370 THROUGH 445 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -41.6341 -60.7834   9.0511              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4998 T22:   0.5914                                     
REMARK   3      T33:   0.3353 T12:   0.1280                                     
REMARK   3      T13:   0.0135 T23:  -0.0992                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6665 L22:   4.3644                                     
REMARK   3      L33:   1.9723 L12:   0.1156                                     
REMARK   3      L13:   0.5731 L23:  -1.2285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1627 S12:   0.5690 S13:  -0.3129                       
REMARK   3      S21:  -0.4581 S22:   0.1014 S23:  -0.0213                       
REMARK   3      S31:  -0.0225 S32:   0.1674 S33:   0.0002                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 446 THROUGH 533 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -41.0216 -40.5690   9.0016              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5635 T22:   0.6766                                     
REMARK   3      T33:   0.3746 T12:   0.0140                                     
REMARK   3      T13:   0.0275 T23:   0.1026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2753 L22:   5.2481                                     
REMARK   3      L33:   2.7864 L12:  -0.0452                                     
REMARK   3      L13:   0.3087 L23:   1.9787                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1609 S12:   0.3047 S13:   0.3646                       
REMARK   3      S21:  -1.0080 S22:   0.1973 S23:  -0.1845                       
REMARK   3      S31:  -0.4363 S32:   0.4616 S33:   0.0094                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 534 THROUGH 559 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -37.6049 -25.9183  16.5537              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7533 T22:   0.7419                                     
REMARK   3      T33:   0.7155 T12:  -0.0060                                     
REMARK   3      T13:   0.1681 T23:   0.1271                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4790 L22:   1.4125                                     
REMARK   3      L33:   1.2723 L12:   0.6967                                     
REMARK   3      L13:   0.5681 L23:   1.3114                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0009 S12:   0.2062 S13:   1.2861                       
REMARK   3      S21:  -0.8676 S22:   0.2859 S23:  -0.5893                       
REMARK   3      S31:  -1.6228 S32:   0.3710 S33:   0.0001                       
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 4U3J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000202744.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
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                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26235                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.810                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.5                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.14300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.81                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 35.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.92400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 4FFB,2QK1                                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% (V/V) PEG3350, 0.25 M (NH4)2SO4,     
REMARK 280  0.1 M MES, PH 6.1, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE       
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       55.95450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.78650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       55.95450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       44.78650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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     LYS A   281                                                      
REMARK 465     ALA A   282                                                      
REMARK 465     PHE A   283                                                      
REMARK 465     HIS A   284                                                      
REMARK 465     GLU A   285                                                      
REMARK 465     SER A   286                                                      
REMARK 465     ASN A   287                                                      
REMARK 465     ASP A   439                                                      
REMARK 465     SER A   440                                                      
REMARK 465     TYR A   441                                                      
REMARK 465     ALA A   442                                                      
REMARK 465     GLU A   443                                                      
REMARK 465     GLU A   444                                                      
REMARK 465     GLU A   445                                                      
REMARK 465     GLU A   446                                                      
REMARK 465     PHE A   447                                                      
REMARK 465     ARG B   175                                                      
REMARK 465     SER B   176                                                      
REMARK 465     ASP B   177                                                      
REMARK 465     ARG B   213                                                      
REMARK 465     THR B   214                                                      
REMARK 465     LEU B   217                                                      
REMARK 465     ASN B   218                                                      
REMARK 465     ILE B   276                                                      
REMARK 465     GLY B   277                                                      
REMARK 465     SER B   278                                                      
REMARK 465     GLN B   279                                                      
REMARK 465     SER B   280                                                      
REMARK 465     PHE B   281                                                      
REMARK 465     GLU B   431                                                      
REMARK 465     ASP B   432                                                      
REMARK 465     ASP B   433                                                      
REMARK 465     GLU B   434                                                      
REMARK 465     GLU B   435                                                      
REMARK 465     VAL B   436                                                      
REMARK 465     ASP B   437                                                      
REMARK 465     GLU B   438                                                      
REMARK 465     ASN B   439                                                      
REMARK 465     GLY B   440                                                      
REMARK 465     ASP B   441                                                      
REMARK 465     PHE B   442                                                      
REMARK 465     GLY B   443                                                      
REMARK 465     ALA B   444                                                      
REMARK 465     PRO B   445                                                      
REMARK 465     GLN B   446                                                      
REMARK 465     ASN B   447                                                      
REMARK 465     GLN B   448                                                      
REMARK 465     ASP B   449                                                      
REMARK 465     GLU B   450                                                      
REMARK 465     PRO B   451                                                      
REMARK 465     ILE B   452                                                      
REMARK 465     THR B   453                                                      
REMARK 465     GLU B   454                                                      
REMARK 465     ASN B   455                                                      
REMARK 465     PHE B   456                                                      
REMARK 465     GLU B   457                                                      
REMARK 465     HIS B   458                                                      
REMARK 465     HIS B   459                                                      
REMARK 465     HIS B   460                                                      
REMARK 465     HIS B   461                                                      
REMARK 465     HIS B   462                                                      
REMARK 465     HIS B   463                                                      
REMARK 465     MET C   318                                                      
REMARK 465     LEU C   560                                                      
REMARK 465     HIS C   561                                                      
REMARK 465     HIS C   562                                                      
REMARK 465     HIS C   563                                                      
REMARK 465     HIS C   564                                                      
REMARK 465     HIS C   565                                                      
REMARK 465     HIS C   566                                                      
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     MET A   1    CG   SD   CE                                        
REMARK 470     ARG A   2    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A  38    CG   OD1  OD2                                       
REMARK 470     LYS A  42    CG   CD   CE   NZ                                   
REMARK 470     GLU A  47    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  48    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 164    CG   CD   CE   NZ                                   
REMARK 470     ASN A 338    CG   OD1  ND2                                       
REMARK 470     LYS A 340    CG   CD   CE   NZ                                   
REMARK 470     LEU A 344    CG   CD1  CD2                                       
REMARK 470     CYS A 348    SG                                                  
REMARK 470     LYS A 353    CG   CD   CE   NZ                                   
REMARK 470     ASN A 366    CG   OD1  ND2                                       
REMARK 470     MET B   1    CG   SD   CE                                        
REMARK 470     HIS B  39    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B  44    CG   CD   CE   NZ                                   
REMARK 470     SER B  56    OG                                                  
REMARK 470     LYS B  58    CG   CD   CE   NZ                                   
REMARK 470     ILE B  81    CG1  CG2  CD1                                       
REMARK 470     ASN B  83    CG   OD1  ND2                                       
REMARK 470     GLN B  94    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 174    CG   CD   CE   NZ                                   
REMARK 470     LYS B 216    CG   CD   CE   NZ                                   
REMARK 470     THR B 274    OG1  CG2                                            
REMARK 470     SER B 283    OG                                                  
REMARK 470     GLN B 291    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 320    CG   CD   CE   NZ                                   
REMARK 470     GLU B 343    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 392    CG   CD   CE   NZ                                   
REMARK 470     VAL B 430    CG1  CG2                                            
REMARK 470     LYS C 330    CG   CD   CE   NZ                                   
REMARK 470     ASP C 331    CG   OD1  OD2                                       
REMARK 470     GLU C 334    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 358    CG   CD   OE1  NE2                                  
REMARK 470     ARG C 454    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 464    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 469    CG   CD   CE   NZ                                   
REMARK 470     LYS C 489    CG   CD   CE   NZ                                   
REMARK 470     LYS C 531    CG   CD   CE   NZ                                   
REMARK 470     LYS C 540    CG   CD   CE   NZ                                   
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   OD2  ASP C   546     HZ2  LYS C   549              1.51            
REMARK 500  HH11  ARG C   550     OE2  GLU C   554              1.59            
REMARK 500   O    ASN A   187     HG1  THR A   191              1.59            
REMARK 500   NH1  ARG C   550     OE2  GLU C   554              2.12            
REMARK 500   OD2  ASP C   546     NZ   LYS C   549              2.16            
REMARK 500   OH   TYR A   109     OE1  GLU A   418              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  41      -61.97     65.43                                   
REMARK 500    GLU A  48      -92.39    179.08                                   
REMARK 500    THR A 110      -88.80   -104.79                                   
REMARK 500    ASP A 323       90.45    -62.13                                   
REMARK 500    LYS A 340       95.16     88.04                                   
REMARK 500    THR A 341       70.21   -118.86                                   
REMARK 500    PRO A 349      -91.18    -70.49                                   
REMARK 500    GLU B  45      -74.09    -61.83                                   
REMARK 500    ARG B  46       47.88    -88.04                                   
REMARK 500    ASN B  78       44.43    -92.92                                   
REMARK 500    SER B  95     -158.50    -87.36                                   
REMARK 500    THR B 107      -99.03   -100.52                                   
REMARK 500    SER B 129       76.79   -160.43                                   
REMARK 500    PRO B 173       76.43    -64.32                                   
REMARK 500    GLN B 245      -41.91   -168.89                                   
REMARK 500    LEU B 263       72.13   -106.21                                   
REMARK 500    LEU B 273      -98.73   -108.99                                   
REMARK 500    THR B 274      174.63     63.34                                   
REMARK 500    MET B 300       30.31    -91.27                                   
REMARK 500    ALA B 302       76.19    -65.51                                   
REMARK 500    ASN B 337       40.58    -91.77                                   
REMARK 500    PRO B 358     -166.55    -65.74                                   
REMARK 500    ASN B 370       69.03   -102.71                                   
REMARK 500    VAL C 355      -76.30   -137.03                                   
REMARK 500    LYS C 404     -154.54     56.39                                   
REMARK 500    PHE C 408       94.45    -67.97                                   
REMARK 500    LYS C 489       26.63   -140.81                                   
REMARK 500    LEU C 499      -80.72    -62.36                                   
REMARK 500    GLU C 502      -50.55   -129.44                                   
REMARK 500    ILE C 532      -71.35    -82.82                                   
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 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 604   O                                                      
REMARK 620 2 HOH A 606   O    75.5                                              
REMARK 620 3 GTP A 502   O3G  49.3  73.2                                        
REMARK 620 4 GTP A 502   O2B  81.5 133.0  60.8                                  
REMARK 620 5 HOH A 607   O   152.3  79.8 111.2 107.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GTP B 502   O3G                                                    
REMARK 620 2 GTP B 502   O2G  65.7                                              
REMARK 620 3 HOH B 608   O   135.4  80.0                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GTP A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GTP B 502                 
DBREF  4U3J A    1   447  UNP    P09733   TBA1_YEAST       1    447             
DBREF  4U3J B    1   457  UNP    P02557   TBB_YEAST        1    457             
DBREF  4U3J C  318   560  UNP    P46675   STU2_YEAST     318    560             
SEQADV 4U3J ARG B  175  UNP  P02557    THR   175 ENGINEERED MUTATION            
SEQADV 4U3J ARG B  179  UNP  P02557    VAL   179 ENGINEERED MUTATION            
SEQADV 4U3J HIS B  458  UNP  P02557              EXPRESSION TAG                 
SEQADV 4U3J HIS B  459  UNP  P02557              EXPRESSION TAG                 
SEQADV 4U3J HIS B  460  UNP  P02557              EXPRESSION TAG                 
SEQADV 4U3J HIS B  461  UNP  P02557              EXPRESSION TAG                 
SEQADV 4U3J HIS B  462  UNP  P02557              EXPRESSION TAG                 
SEQADV 4U3J HIS B  463  UNP  P02557              EXPRESSION TAG                 
SEQADV 4U3J HIS C  561  UNP  P46675              EXPRESSION TAG                 
SEQADV 4U3J HIS C  562  UNP  P46675              EXPRESSION TAG                 
SEQADV 4U3J HIS C  563  UNP  P46675              EXPRESSION TAG                 
SEQADV 4U3J HIS C  564  UNP  P46675              EXPRESSION TAG                 
SEQADV 4U3J HIS C  565  UNP  P46675              EXPRESSION TAG                 
SEQADV 4U3J HIS C  566  UNP  P46675              EXPRESSION TAG                 
SEQRES   1 A  447  MET ARG GLU VAL ILE SER ILE ASN VAL GLY GLN ALA GLY          
SEQRES   2 A  447  CYS GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR SER LEU          
SEQRES   3 A  447  GLU HIS GLY ILE LYS PRO ASP GLY HIS LEU GLU ASP GLY          
SEQRES   4 A  447  LEU SER LYS PRO LYS GLY GLY GLU GLU GLY PHE SER THR          
SEQRES   5 A  447  PHE PHE HIS GLU THR GLY TYR GLY LYS PHE VAL PRO ARG          
SEQRES   6 A  447  ALA ILE TYR VAL ASP LEU GLU PRO ASN VAL ILE ASP GLU          
SEQRES   7 A  447  VAL ARG ASN GLY PRO TYR LYS ASP LEU PHE HIS PRO GLU          
SEQRES   8 A  447  GLN LEU ILE SER GLY LYS GLU ASP ALA ALA ASN ASN TYR          
SEQRES   9 A  447  ALA ARG GLY HIS TYR THR VAL GLY ARG GLU ILE LEU GLY          
SEQRES  10 A  447  ASP VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS          
SEQRES  11 A  447  ASP GLY LEU GLN GLY PHE LEU PHE THR HIS SER LEU GLY          
SEQRES  12 A  447  GLY GLY THR GLY SER GLY LEU GLY SER LEU LEU LEU GLU          
SEQRES  13 A  447  GLU LEU SER ALA GLU TYR GLY LYS LYS SER LYS LEU GLU          
SEQRES  14 A  447  PHE ALA VAL TYR PRO ALA PRO GLN VAL SER THR SER VAL          
SEQRES  15 A  447  VAL GLU PRO TYR ASN THR VAL LEU THR THR HIS THR THR          
SEQRES  16 A  447  LEU GLU HIS ALA ASP CYS THR PHE MET VAL ASP ASN GLU          
SEQRES  17 A  447  ALA ILE TYR ASP MET CYS LYS ARG ASN LEU ASP ILE PRO          
SEQRES  18 A  447  ARG PRO SER PHE ALA ASN LEU ASN ASN LEU ILE ALA GLN          
SEQRES  19 A  447  VAL VAL SER SER VAL THR ALA SER LEU ARG PHE ASP GLY          
SEQRES  20 A  447  SER LEU ASN VAL ASP LEU ASN GLU PHE GLN THR ASN LEU          
SEQRES  21 A  447  VAL PRO TYR PRO ARG ILE HIS PHE PRO LEU VAL SER TYR          
SEQRES  22 A  447  SER PRO VAL LEU SER LYS SER LYS ALA PHE HIS GLU SER          
SEQRES  23 A  447  ASN SER VAL SER GLU ILE THR ASN ALA CYS PHE GLU PRO          
SEQRES  24 A  447  GLY ASN GLN MET VAL LYS CYS ASP PRO ARG ASP GLY LYS          
SEQRES  25 A  447  TYR MET ALA THR CYS LEU LEU TYR ARG GLY ASP VAL VAL          
SEQRES  26 A  447  THR ARG ASP VAL GLN ARG ALA VAL GLU GLN VAL LYS ASN          
SEQRES  27 A  447  LYS LYS THR VAL GLN LEU VAL ASP TRP CYS PRO THR GLY          
SEQRES  28 A  447  PHE LYS ILE GLY ILE CYS TYR GLU PRO PRO THR ALA THR          
SEQRES  29 A  447  PRO ASN SER GLN LEU ALA THR VAL ASP ARG ALA VAL CYS          
SEQRES  30 A  447  MET LEU SER ASN THR THR SER ILE ALA GLU ALA TRP LYS          
SEQRES  31 A  447  ARG ILE ASP ARG LYS PHE ASP LEU MET TYR ALA LYS ARG          
SEQRES  32 A  447  ALA PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU          
SEQRES  33 A  447  GLY GLU PHE THR GLU ALA ARG GLU ASP LEU ALA ALA LEU          
SEQRES  34 A  447  GLU ARG ASP TYR ILE GLU VAL GLY ALA ASP SER TYR ALA          
SEQRES  35 A  447  GLU GLU GLU GLU PHE                                          
SEQRES   1 B  463  MET ARG GLU ILE ILE HIS ILE SER THR GLY GLN CYS GLY          
SEQRES   2 B  463  ASN GLN ILE GLY ALA ALA PHE TRP GLU THR ILE CYS GLY          
SEQRES   3 B  463  GLU HIS GLY LEU ASP PHE ASN GLY THR TYR HIS GLY HIS          
SEQRES   4 B  463  ASP ASP ILE GLN LYS GLU ARG LEU ASN VAL TYR PHE ASN          
SEQRES   5 B  463  GLU ALA SER SER GLY LYS TRP VAL PRO ARG SER ILE ASN          
SEQRES   6 B  463  VAL ASP LEU GLU PRO GLY THR ILE ASP ALA VAL ARG ASN          
SEQRES   7 B  463  SER ALA ILE GLY ASN LEU PHE ARG PRO ASP ASN TYR ILE          
SEQRES   8 B  463  PHE GLY GLN SER SER ALA GLY ASN VAL TRP ALA LYS GLY          
SEQRES   9 B  463  HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL MET          
SEQRES  10 B  463  ASP VAL ILE ARG ARG GLU ALA GLU GLY CYS ASP SER LEU          
SEQRES  11 B  463  GLN GLY PHE GLN ILE THR HIS SER LEU GLY GLY GLY THR          
SEQRES  12 B  463  GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG          
SEQRES  13 B  463  GLU GLU PHE PRO ASP ARG MET MET ALA THR PHE SER VAL          
SEQRES  14 B  463  LEU PRO SER PRO LYS ARG SER ASP THR ARG VAL GLU PRO          
SEQRES  15 B  463  TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU HIS          
SEQRES  16 B  463  SER ASP GLU THR PHE CYS ILE ASP ASN GLU ALA LEU TYR          
SEQRES  17 B  463  ASP ILE CYS GLN ARG THR LEU LYS LEU ASN GLN PRO SER          
SEQRES  18 B  463  TYR GLY ASP LEU ASN ASN LEU VAL SER SER VAL MET SER          
SEQRES  19 B  463  GLY VAL THR THR SER LEU ARG TYR PRO GLY GLN LEU ASN          
SEQRES  20 B  463  SER ASP LEU ARG LYS LEU ALA VAL ASN LEU VAL PRO PHE          
SEQRES  21 B  463  PRO ARG LEU HIS PHE PHE MET VAL GLY TYR ALA PRO LEU          
SEQRES  22 B  463  THR ALA ILE GLY SER GLN SER PHE ARG SER LEU THR VAL          
SEQRES  23 B  463  PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET          
SEQRES  24 B  463  MET ALA ALA ALA ASP PRO ARG ASN GLY ARG TYR LEU THR          
SEQRES  25 B  463  VAL ALA ALA PHE PHE ARG GLY LYS VAL SER VAL LYS GLU          
SEQRES  26 B  463  VAL GLU ASP GLU MET HIS LYS VAL GLN SER LYS ASN SER          
SEQRES  27 B  463  ASP TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL GLN THR          
SEQRES  28 B  463  ALA VAL CYS SER VAL ALA PRO GLN GLY LEU ASP MET ALA          
SEQRES  29 B  463  ALA THR PHE ILE ALA ASN SER THR SER ILE GLN GLU LEU          
SEQRES  30 B  463  PHE LYS ARG VAL GLY ASP GLN PHE SER ALA MET PHE LYS          
SEQRES  31 B  463  ARG LYS ALA PHE LEU HIS TRP TYR THR SER GLU GLY MET          
SEQRES  32 B  463  ASP GLU LEU GLU PHE SER GLU ALA GLU SER ASN MET ASN          
SEQRES  33 B  463  ASP LEU VAL SER GLU TYR GLN GLN TYR GLN GLU ALA THR          
SEQRES  34 B  463  VAL GLU ASP ASP GLU GLU VAL ASP GLU ASN GLY ASP PHE          
SEQRES  35 B  463  GLY ALA PRO GLN ASN GLN ASP GLU PRO ILE THR GLU ASN          
SEQRES  36 B  463  PHE GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 C  249  MET LEU PRO GLU GLU THR ILE LEU ASP LYS LEU PRO LYS          
SEQRES   2 C  249  ASP PHE GLN GLU ARG ILE THR SER SER LYS TRP LYS ASP          
SEQRES   3 C  249  ARG VAL GLU ALA LEU GLU GLU PHE TRP ASP SER VAL LEU          
SEQRES   4 C  249  SER GLN THR LYS LYS LEU LYS SER THR SER GLN ASN TYR          
SEQRES   5 C  249  SER ASN LEU LEU GLY ILE TYR GLY HIS ILE ILE GLN LYS          
SEQRES   6 C  249  ASP ALA ASN ILE GLN ALA VAL ALA LEU ALA ALA GLN SER          
SEQRES   7 C  249  VAL GLU LEU ILE CYS ASP LYS LEU LYS THR PRO GLY PHE          
SEQRES   8 C  249  SER LYS ASP TYR VAL SER LEU VAL PHE THR PRO LEU LEU          
SEQRES   9 C  249  ASP ARG THR LYS GLU LYS LYS PRO SER VAL ILE GLU ALA          
SEQRES  10 C  249  ILE ARG LYS ALA LEU LEU THR ILE CYS LYS TYR TYR ASP          
SEQRES  11 C  249  PRO LEU ALA SER SER GLY ARG ASN GLU ASP MET LEU LYS          
SEQRES  12 C  249  ASP ILE LEU GLU HIS MET LYS HIS LYS THR PRO GLN ILE          
SEQRES  13 C  249  ARG MET GLU CYS THR GLN LEU PHE ASN ALA SER MET LYS          
SEQRES  14 C  249  GLU GLU LYS ASP GLY TYR SER THR LEU GLN ARG TYR LEU          
SEQRES  15 C  249  LYS ASP GLU VAL VAL PRO ILE VAL ILE GLN ILE VAL ASN          
SEQRES  16 C  249  ASP THR GLN PRO ALA ILE ARG THR ILE GLY PHE GLU SER          
SEQRES  17 C  249  PHE ALA ILE LEU ILE LYS ILE PHE GLY MET ASN THR PHE          
SEQRES  18 C  249  VAL LYS THR LEU GLU HIS LEU ASP ASN LEU LYS ARG LYS          
SEQRES  19 C  249  LYS ILE GLU GLU THR VAL LYS THR LEU HIS HIS HIS HIS          
SEQRES  20 C  249  HIS HIS                                                      
HET     MG  A 501       1                                                       
HET    GTP  A 502      42                                                       
HET     MG  B 501       1                                                       
HET    GTP  B 502      42                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GTP GUANOSINE-5'-TRIPHOSPHATE                                        
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   5  GTP    2(C10 H16 N5 O14 P3)                                         
FORMUL   8  HOH   *21(H2 O)                                                     
HELIX    1 AA1 GLY A   10  HIS A   28  1                                  19    
HELIX    2 AA2 GLU A   72  GLY A   82  1                                  11    
HELIX    3 AA3 ASN A  103  TYR A  109  1                                   7    
HELIX    4 AA4 VAL A  111  ASP A  128  1                                  18    
HELIX    5 AA5 SER A  148  TYR A  162  1                                  15    
HELIX    6 AA6 ALA A  175  SER A  179  5                                   5    
HELIX    7 AA7 VAL A  183  LEU A  196  1                                  14    
HELIX    8 AA8 ASN A  207  ASN A  217  1                                  11    
HELIX    9 AA9 SER A  224  THR A  240  1                                  17    
HELIX   10 AB1 THR A  240  PHE A  245  1                                   6    
HELIX   11 AB2 ASP A  252  VAL A  261  1                                  10    
HELIX   12 AB3 VAL A  289  CYS A  296  1                                   8    
HELIX   13 AB4 PHE A  297  GLN A  302  5                                   6    
HELIX   14 AB5 VAL A  325  LYS A  339  1                                  15    
HELIX   15 AB6 ILE A  385  ALA A  401  1                                  17    
HELIX   16 AB7 PHE A  405  GLY A  411  1                                   7    
HELIX   17 AB8 GLU A  416  GLY A  437  1                                  22    
HELIX   18 AB9 GLY B   10  HIS B   28  1                                  19    
HELIX   19 AC1 ASP B   41  ARG B   46  1                                   6    
HELIX   20 AC2 LEU B   47  VAL B   49  5                                   3    
HELIX   21 AC3 GLU B   69  ASN B   78  1                                  10    
HELIX   22 AC4 ARG B   86  ASP B   88  5                                   3    
HELIX   23 AC5 VAL B  100  TYR B  106  1                                   7    
HELIX   24 AC6 LEU B  112  GLY B  126  1                                  15    
HELIX   25 AC7 GLY B  142  PHE B  159  1                                  18    
HELIX   26 AC8 VAL B  180  SER B  196  1                                  17    
HELIX   27 AC9 ASN B  204  GLN B  212  1                                   9    
HELIX   28 AD1 SER B  221  THR B  237  1                                  17    
HELIX   29 AD2 THR B  237  TYR B  242  1                                   6    
HELIX   30 AD3 ASP B  249  VAL B  258  1                                  10    
HELIX   31 AD4 THR B  285  ASP B  295  1                                  11    
HELIX   32 AD5 ALA B  296  MET B  299  5                                   4    
HELIX   33 AD6 ASP B  304  GLY B  308  5                                   5    
HELIX   34 AD7 SER B  322  ASN B  337  1                                  16    
HELIX   35 AD8 SER B  338  PHE B  341  5                                   4    
HELIX   36 AD9 ILE B  374  LYS B  390  1                                  17    
HELIX   37 AE1 LEU B  395  SER B  400  1                                   6    
HELIX   38 AE2 ASP B  404  GLU B  427  1                                  24    
HELIX   39 AE3 ILE C  324  LEU C  328  5                                   5    
HELIX   40 AE4 ASP C  331  THR C  337  1                                   7    
HELIX   41 AE5 LYS C  340  VAL C  355  1                                  16    
HELIX   42 AE6 LEU C  356  THR C  359  5                                   4    
HELIX   43 AE7 TYR C  369  ASP C  383  1                                  15    
HELIX   44 AE8 ASN C  385  LYS C  404  1                                  20    
HELIX   45 AE9 SER C  409  ARG C  423  1                                  15    
HELIX   46 AF1 THR C  424  GLU C  426  5                                   3    
HELIX   47 AF2 LYS C  428  TYR C  446  1                                  19    
HELIX   48 AF3 ASN C  455  MET C  466  1                                  12    
HELIX   49 AF4 THR C  470  GLU C  488  1                                  19    
HELIX   50 AF5 TYR C  492  TYR C  498  1                                   7    
HELIX   51 AF6 GLU C  502  ASN C  512  1                                  11    
HELIX   52 AF7 GLN C  515  GLY C  534  1                                  20    
HELIX   53 AF8 PHE C  538  GLU C  543  1                                   6    
HELIX   54 AF9 ASP C  546  THR C  559  1                                  14    
SHEET    1 AA1 6 LEU A  93  SER A  95  0                                        
SHEET    2 AA1 6 ALA A  66  ASP A  70  1  N  TYR A  68   O  ILE A  94           
SHEET    3 AA1 6 VAL A   4  VAL A   9  1  N  ASN A   8   O  ILE A  67           
SHEET    4 AA1 6 GLY A 135  SER A 141  1  O  THR A 139   N  ILE A   7           
SHEET    5 AA1 6 SER A 166  TYR A 173  1  O  PHE A 170   N  PHE A 138           
SHEET    6 AA1 6 CYS A 201  ASP A 206  1  O  PHE A 203   N  GLU A 169           
SHEET    1 AA2 2 PHE A  54  GLU A  56  0                                        
SHEET    2 AA2 2 PHE A  62  PRO A  64 -1  O  VAL A  63   N  HIS A  55           
SHEET    1 AA3 4 LEU A 270  SER A 274  0                                        
SHEET    2 AA3 4 ARG A 374  THR A 382 -1  O  SER A 380   N  LEU A 270           
SHEET    3 AA3 4 TYR A 313  GLY A 322 -1  N  LEU A 319   O  CYS A 377           
SHEET    4 AA3 4 PHE A 352  CYS A 357  1  O  GLY A 355   N  TYR A 320           
SHEET    1 AA410 TYR B  90  PHE B  92  0                                        
SHEET    2 AA410 SER B  63  ASP B  67  1  N  ASN B  65   O  ILE B  91           
SHEET    3 AA410 ILE B   4  THR B   9  1  N  SER B   8   O  VAL B  66           
SHEET    4 AA410 GLY B 132  SER B 138  1  O  GLN B 134   N  ILE B   7           
SHEET    5 AA410 MET B 163  LEU B 170  1  O  PHE B 167   N  ILE B 135           
SHEET    6 AA410 GLU B 198  ASP B 203  1  O  PHE B 200   N  THR B 166           
SHEET    7 AA410 PHE B 265  ALA B 271  1  O  PHE B 266   N  THR B 199           
SHEET    8 AA410 MET B 363  SER B 371 -1  O  ALA B 365   N  ALA B 271           
SHEET    9 AA410 TYR B 310  GLY B 319 -1  N  PHE B 316   O  THR B 366           
SHEET   10 AA410 VAL B 349  CYS B 354  1  O  GLN B 350   N  VAL B 313           
SHEET    1 AA5 2 PHE B  51  GLU B  53  0                                        
SHEET    2 AA5 2 TRP B  59  PRO B  61 -1  O  VAL B  60   N  ASN B  52           
LINK        MG    MG A 501                 O   HOH A 604     1555   1555  2.33  
LINK        MG    MG A 501                 O   HOH A 606     1555   1555  2.03  
LINK        MG    MG A 501                 O3G GTP A 502     1555   1555  2.95  
LINK        MG    MG A 501                 O2B GTP A 502     1555   1555  2.35  
LINK        MG    MG A 501                 O   HOH A 607     1555   1555  2.35  
LINK        MG    MG B 501                 O3G GTP B 502     1555   1555  2.00  
LINK        MG    MG B 501                 O2G GTP B 502     1555   1555  2.50  
LINK        MG    MG B 501                 O   HOH B 608     1555   1555  2.16  
CISPEP   1 GLY A   46    GLU A   47          0         0.81                     
CISPEP   2 SER A  274    PRO A  275          0         1.00                     
CISPEP   3 VAL A  342    GLN A  343          0        -2.45                     
CISPEP   4 PRO B  243    GLY B  244          0        -0.21                     
CISPEP   5 ALA B  271    PRO B  272          0         2.16                     
CISPEP   6 GLN B  359    GLY B  360          0         0.65                     
CISPEP   7 THR C  405    PRO C  406          0         1.12                     
SITE     1 AC1  6 GLN A  11  GLU A  72  GTP A 502  HOH A 604                    
SITE     2 AC1  6 HOH A 606  HOH A 607                                          
SITE     1 AC2 24 GLY A  10  GLN A  11  ALA A  12  GLN A  15                    
SITE     2 AC2 24 ALA A 101  ASN A 102  SER A 141  GLY A 144                    
SITE     3 AC2 24 GLY A 145  THR A 146  GLY A 147  VAL A 178                    
SITE     4 AC2 24 THR A 180  GLU A 184  ASN A 207  PHE A 225                    
SITE     5 AC2 24 ASN A 229  ILE A 232   MG A 501  HOH A 604                    
SITE     6 AC2 24 HOH A 606  HOH A 607  HOH A 609  LYS B 252                    
SITE     1 AC3  2 GTP B 502  HOH B 608                                          
SITE     1 AC4 17 GLY B  10  GLN B  11  CYS B  12  GLN B  15                    
SITE     2 AC4 17 ALA B  97  ASN B  99  SER B 138  GLY B 141                    
SITE     3 AC4 17 GLY B 142  THR B 143  GLY B 144  GLU B 181                    
SITE     4 AC4 17 ASN B 204  TYR B 222  ASN B 226   MG B 501                    
SITE     5 AC4 17 HOH B 608                                                     
CRYST1  111.909   89.573  135.508  90.00 112.31  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008936  0.000000  0.003666        0.00000                         
SCALE2      0.000000  0.011164  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007976        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system