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Entry: 4FFB
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HEADER    HYDROLASE                               31-MAY-12   4FFB              
TITLE     A TOG:ALPHA/BETA-TUBULIN COMPLEX STRUCTURE REVEALS CONFORMATION-BASED 
TITLE    2 MECHANISMS FOR A MICROTUBULE POLYMERASE                              
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 EC: 3.6.5.6;                                                         
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES;                                                       
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: PROTEIN STU2;                                              
COMPND  14 CHAIN: C;                                                            
COMPND  15 FRAGMENT: TOG1 DOMAIN;                                               
COMPND  16 SYNONYM: SUPPRESSOR OF TUBULIN 2;                                    
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 559292;                                              
SOURCE   5 STRAIN: ATCC 204508 / S288C;                                         
SOURCE   6 GENE: TUB1, YML085C;                                                 
SOURCE   7 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: JEL1;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: P426GAL1;                                 
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  14 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  15 ORGANISM_TAXID: 559292;                                              
SOURCE  16 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  17 GENE: TUB2, YFL037W;                                                 
SOURCE  18 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: JEL1;                                      
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: P424GAL1;                                 
SOURCE  23 MOL_ID: 3;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  25 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  26 ORGANISM_TAXID: 559292;                                              
SOURCE  27 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  28 GENE: L2108, STU2, YLR045C;                                          
SOURCE  29 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  30 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  31 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  32 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  33 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    TUBULIN FOLD, HEAT REPEATS, CYTOSKELETON, MICROTUBULE, TUBULIN, TOG   
KEYWDS   2 DOMAIN, HYDROLASE                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.AYAZ,X.YE,P.HUDDLESTON,C.A.BRAUTIGAM,L.M.RICE                       
REVDAT   2   28-AUG-13 4FFB    1       JRNL                                     
REVDAT   1   15-AUG-12 4FFB    0                                                
JRNL        AUTH   P.AYAZ,X.YE,P.HUDDLESTON,C.A.BRAUTIGAM,L.M.RICE              
JRNL        TITL   A TOG: ALPHA BETA-TUBULIN COMPLEX STRUCTURE REVEALS          
JRNL        TITL 2 CONFORMATION-BASED MECHANISMS FOR A MICROTUBULE POLYMERASE.  
JRNL        REF    SCIENCE                       V. 337   857 2012              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   22904013                                                     
JRNL        DOI    10.1126/SCIENCE.1221698                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.88 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1063)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.88                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.95                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 74.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 26174                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1039                            
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 44.9508 -  5.5101    1.00     4891   204  0.2064 0.2366        
REMARK   3     2  5.5101 -  4.3747    1.00     4849   202  0.1859 0.2653        
REMARK   3     3  4.3747 -  3.8221    1.00     4789   195  0.1924 0.2718        
REMARK   3     4  3.8221 -  3.4728    0.89     4257   177  0.2262 0.2854        
REMARK   3     5  3.4728 -  3.2239    0.65     3091   127  0.2373 0.2996        
REMARK   3     6  3.2239 -  3.0339    0.46     2176    91  0.2530 0.2837        
REMARK   3     7  3.0339 -  2.8820    0.23     1082    43  0.2460 0.3613        
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)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.610           
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           8706                                  
REMARK   3   ANGLE     :  0.697          11815                                  
REMARK   3   CHIRALITY :  0.049           1322                                  
REMARK   3   PLANARITY :  0.003           1525                                  
REMARK   3   DIHEDRAL  : 16.840           3171                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 17                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 1:53)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  37.8330  11.5133  49.1908              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5788 T22:   0.3592                                     
REMARK   3      T33:   0.4138 T12:  -0.0941                                     
REMARK   3      T13:   0.0776 T23:  -0.0708                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2492 L22:   0.9494                                     
REMARK   3      L33:   1.7955 L12:  -0.3452                                     
REMARK   3      L13:  -0.0764 L23:  -0.0696                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0104 S12:  -0.1299 S13:   0.2589                       
REMARK   3      S21:  -0.0361 S22:   0.1160 S23:  -0.2916                       
REMARK   3      S31:  -0.5386 S32:   0.3524 S33:  -0.0002                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 54:244)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.3712   3.9787  39.1497              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4006 T22:   0.2812                                     
REMARK   3      T33:   0.3261 T12:   0.0092                                     
REMARK   3      T13:   0.0817 T23:   0.0407                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5507 L22:   2.0731                                     
REMARK   3      L33:   1.0899 L12:   0.8456                                     
REMARK   3      L13:   0.3024 L23:   0.2697                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0390 S12:   0.0330 S13:   0.2365                       
REMARK   3      S21:  -0.0605 S22:   0.0131 S23:   0.1521                       
REMARK   3      S31:  -0.1409 S32:   0.1238 S33:   0.0001                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 245:301)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  45.1191  -7.0916  43.9910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3837 T22:   0.4626                                     
REMARK   3      T33:   0.6325 T12:  -0.0345                                     
REMARK   3      T13:  -0.0367 T23:  -0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2868 L22:   2.2024                                     
REMARK   3      L33:   0.7875 L12:  -0.3091                                     
REMARK   3      L13:   0.0110 L23:   0.7838                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0093 S12:  -0.3564 S13:  -0.0544                       
REMARK   3      S21:   0.0079 S22:   0.1233 S23:  -0.4083                       
REMARK   3      S31:   0.1372 S32:   0.5008 S33:   0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 302:439)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  38.6437 -11.5948  37.1867              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4621 T22:   0.2856                                     
REMARK   3      T33:   0.4172 T12:   0.0132                                     
REMARK   3      T13:   0.0243 T23:   0.0573                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9017 L22:   1.7585                                     
REMARK   3      L33:   1.9595 L12:   0.3733                                     
REMARK   3      L13:   0.9648 L23:   0.7821                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2248 S12:   0.1843 S13:  -0.3993                       
REMARK   3      S21:   0.1003 S22:   0.0059 S23:  -0.4049                       
REMARK   3      S31:   0.3040 S32:   0.4249 S33:   0.0005                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 1:62)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.9687   5.4913  50.5561              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6794 T22:   0.7070                                     
REMARK   3      T33:   0.7485 T12:   0.1706                                     
REMARK   3      T13:   0.1233 T23:   0.0617                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5761 L22:   1.1586                                     
REMARK   3      L33:   1.4738 L12:  -0.1214                                     
REMARK   3      L13:   0.1338 L23:  -0.8139                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0238 S12:  -0.3587 S13:   0.5677                       
REMARK   3      S21:   0.7193 S22:   0.1533 S23:   0.3298                       
REMARK   3      S31:  -1.2101 S32:  -0.3795 S33:   0.0345                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 63:241)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.5560  -2.2622  38.3520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4238 T22:   0.6940                                     
REMARK   3      T33:   0.6460 T12:   0.1199                                     
REMARK   3      T13:   0.0402 T23:   0.2155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0701 L22:   1.5388                                     
REMARK   3      L33:   2.4291 L12:  -0.3858                                     
REMARK   3      L13:  -0.1258 L23:   0.1479                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0870 S12:  -0.0560 S13:   0.1529                       
REMARK   3      S21:   0.1124 S22:   0.2259 S23:   0.4545                       
REMARK   3      S31:  -0.2335 S32:  -0.8149 S33:   0.0019                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 242:298)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   1.9880 -13.7281  45.4075              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4691 T22:   0.5084                                     
REMARK   3      T33:   0.5397 T12:   0.0053                                     
REMARK   3      T13:   0.0071 T23:   0.1528                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5631 L22:   1.0652                                     
REMARK   3      L33:   1.2720 L12:   0.0454                                     
REMARK   3      L13:  -0.1935 L23:   0.2840                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0426 S12:  -0.3745 S13:  -0.3449                       
REMARK   3      S21:   0.3136 S22:   0.1779 S23:   0.3872                       
REMARK   3      S31:  -0.0775 S32:  -0.5329 S33:  -0.0030                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 299:336)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3695 -19.6951  47.2377              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5314 T22:   0.6732                                     
REMARK   3      T33:   0.6075 T12:   0.0090                                     
REMARK   3      T13:   0.0153 T23:   0.1655                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6018 L22:   0.5336                                     
REMARK   3      L33:   1.3948 L12:  -0.3267                                     
REMARK   3      L13:  -0.2168 L23:  -0.5269                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2117 S12:  -0.6009 S13:  -0.5892                       
REMARK   3      S21:   0.2897 S22:   0.1874 S23:  -0.1731                       
REMARK   3      S31:   0.5856 S32:  -0.5500 S33:   0.0456                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 337:432)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2335 -17.0098  31.2013              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4576 T22:   0.5205                                     
REMARK   3      T33:   0.6653 T12:  -0.0826                                     
REMARK   3      T13:   0.0030 T23:   0.1647                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8673 L22:   1.6665                                     
REMARK   3      L33:   2.0359 L12:  -0.5663                                     
REMARK   3      L13:   0.5871 L23:   0.0261                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0973 S12:   0.2163 S13:  -0.4830                       
REMARK   3      S21:  -0.1691 S22:   0.2155 S23:   0.3463                       
REMARK   3      S31:   0.1115 S32:  -0.6117 S33:   0.0013                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain 'C' and (resseq 11:22)                           
REMARK   3    ORIGIN FOR THE GROUP (A): -32.2289  14.3476  13.0115              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9400 T22:   1.2463                                     
REMARK   3      T33:   1.0412 T12:   0.2734                                     
REMARK   3      T13:  -0.0691 T23:   0.4202                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0332 L22:   0.0865                                     
REMARK   3      L33:   0.0175 L12:  -0.0473                                     
REMARK   3      L13:   0.0129 L23:  -0.0365                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4011 S12:  -0.0930 S13:   0.1720                       
REMARK   3      S21:  -0.0452 S22:  -0.2813 S23:   0.4240                       
REMARK   3      S31:  -0.4163 S32:   0.0389 S33:  -0.0026                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain 'C' and (resseq 23:38)                           
REMARK   3    ORIGIN FOR THE GROUP (A): -26.9593   7.0337   7.4176              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4745 T22:   1.4338                                     
REMARK   3      T33:   0.9299 T12:   0.1078                                     
REMARK   3      T13:  -0.2486 T23:   0.4824                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6038 L22:   1.4682                                     
REMARK   3      L33:   3.6626 L12:   0.3619                                     
REMARK   3      L13:  -0.5764 L23:  -1.6582                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7324 S12:   0.2730 S13:  -0.0382                       
REMARK   3      S21:  -0.3950 S22:   0.3561 S23:   0.5083                       
REMARK   3      S31:  -0.0600 S32:  -0.7372 S33:  -0.5118                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain 'C' and (resseq 39:110)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.1733  14.3786   4.7587              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8176 T22:   1.1142                                     
REMARK   3      T33:   0.8948 T12:   0.1731                                     
REMARK   3      T13:  -0.2312 T23:   0.4837                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3844 L22:   0.3548                                     
REMARK   3      L33:   0.1998 L12:  -0.1286                                     
REMARK   3      L13:  -0.2151 L23:   0.2089                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1114 S12:  -0.0056 S13:   0.3647                       
REMARK   3      S21:  -0.2338 S22:  -0.3411 S23:   0.6669                       
REMARK   3      S31:  -0.4094 S32:  -0.6556 S33:  -0.1514                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: chain 'C' and (resseq 111:131)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.5671   5.0930   6.7745              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4642 T22:   0.9571                                     
REMARK   3      T33:   0.4566 T12:   0.1836                                     
REMARK   3      T13:  -0.3000 T23:   0.6805                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1489 L22:   0.1015                                     
REMARK   3      L33:   0.1874 L12:   0.0351                                     
REMARK   3      L13:  -0.0391 L23:   0.0970                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2203 S12:   0.4651 S13:   0.2709                       
REMARK   3      S21:  -0.3679 S22:  -0.1930 S23:   0.1563                       
REMARK   3      S31:  -0.5100 S32:   0.0199 S33:  -0.7062                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: chain 'C' and (resseq 132:169)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   0.8623  11.6666   6.7975              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7230 T22:   0.7903                                     
REMARK   3      T33:   0.6855 T12:   0.1305                                     
REMARK   3      T13:  -0.0722 T23:   0.3095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5403 L22:   0.4511                                     
REMARK   3      L33:   0.1544 L12:   0.2365                                     
REMARK   3      L13:   0.0591 L23:  -0.1956                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0872 S12:   0.6435 S13:   0.5844                       
REMARK   3      S21:  -0.2328 S22:  -0.0719 S23:   0.1969                       
REMARK   3      S31:  -0.1902 S32:  -0.0820 S33:  -0.0019                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: chain 'C' and (resseq 170:212)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   9.7546   8.6211   5.3630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6721 T22:   0.9108                                     
REMARK   3      T33:   0.6493 T12:  -0.0240                                     
REMARK   3      T13:  -0.0791 T23:   0.3234                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7075 L22:   0.1521                                     
REMARK   3      L33:   0.6756 L12:   0.2413                                     
REMARK   3      L13:   0.0590 L23:   0.2644                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1916 S12:   0.7640 S13:   0.4465                       
REMARK   3      S21:  -0.1277 S22:  -0.0357 S23:   0.1641                       
REMARK   3      S31:  -0.3700 S32:   0.4130 S33:  -0.0013                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: chain 'C' and (resseq 213:241)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8448   1.6999   7.2350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8335 T22:   0.9288                                     
REMARK   3      T33:   0.7184 T12:   0.0335                                     
REMARK   3      T13:   0.0247 T23:   0.2664                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0517 L22:   0.0759                                     
REMARK   3      L33:   0.2528 L12:  -0.0691                                     
REMARK   3      L13:  -0.0320 L23:   0.0402                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0825 S12:   0.4598 S13:   0.3235                       
REMARK   3      S21:  -0.9581 S22:   0.1969 S23:  -0.3293                       
REMARK   3      S31:   0.2128 S32:   0.5031 S33:   0.0284                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: chain 'C' and (resseq 242:272)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.9796   8.8111 -18.0195              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3171 T22:   0.9892                                     
REMARK   3      T33:   0.4273 T12:   0.1970                                     
REMARK   3      T13:  -0.0032 T23:   0.1805                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1176 L22:   0.0775                                     
REMARK   3      L33:   0.0958 L12:   0.0080                                     
REMARK   3      L13:   0.1628 L23:   0.0373                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0276 S12:   0.3431 S13:  -0.2033                       
REMARK   3      S21:   0.2899 S22:   0.1696 S23:   0.5752                       
REMARK   3      S31:  -0.1795 S32:   0.1572 S33:  -0.0231                       
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 4FFB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072829.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-NOV-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.9                                
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) : 0.9794                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED 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 : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39347                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.880                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.88                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 22.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.96700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.900                              
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: PDB ENTRY 1SA0 CHAIN A, 1SA0 CHAIN  B, 2QK1          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (V/V) PEG 400, 0.1 M MES PH 5.9,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                     
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       49.02000            
REMARK 290   SMTRY3   2  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     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     TYR B    36                                                      
REMARK 465     HIS B    37                                                      
REMARK 465     GLY B    38                                                      
REMARK 465     ARG B   175                                                      
REMARK 465     SER B   176                                                      
REMARK 465     ASP B   177                                                      
REMARK 465     SER B   278                                                      
REMARK 465     GLN B   279                                                      
REMARK 465     SER B   280                                                      
REMARK 465     PHE B   281                                                      
REMARK 465     ARG B   282                                                      
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     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     GLU C     4                                                      
REMARK 465     GLU C     5                                                      
REMARK 465     GLU C     6                                                      
REMARK 465     VAL C     7                                                      
REMARK 465     ASP C     8                                                      
REMARK 465     TYR C     9                                                      
REMARK 465     THR C    10                                                      
REMARK 465     VAL C    41                                                      
REMARK 465     GLY C    42                                                      
REMARK 465     ASP C    43                                                      
REMARK 465     ILE C    44                                                      
REMARK 465     SER C    45                                                      
REMARK 465     ARG C    46                                                      
REMARK 465     ASP C    47                                                      
REMARK 465     ASP C    48                                                      
REMARK 465     ASN C    49                                                      
REMARK 465     ILE C    50                                                      
REMARK 465     SER C    88                                                      
REMARK 465     SER C    89                                                      
REMARK 465     SER C    90                                                      
REMARK 465     THR C   214                                                      
REMARK 465     GLY C   215                                                      
REMARK 465     ASN C   216                                                      
REMARK 465     ASN C   217                                                      
REMARK 465     SER C   218                                                      
REMARK 465     ASP C   219                                                      
REMARK 465     LEU C   220                                                      
REMARK 465     LEU C   221                                                      
REMARK 465     GLU C   222                                                      
REMARK 465     GLU C   223                                                      
REMARK 465     ILE C   224                                                      
REMARK 465     GLU C   247                                                      
REMARK 465     PRO C   248                                                      
REMARK 465     SER C   249                                                      
REMARK 465     SER C   250                                                      
REMARK 465     SER C   251                                                      
REMARK 465     LYS C   252                                                      
REMARK 465     MET C   253                                                      
REMARK 465     HIS C   273                                                      
REMARK 465     HIS C   274                                                      
REMARK 465     HIS C   275                                                      
REMARK 465     HIS C   276                                                      
REMARK 465     HIS C   277                                                      
REMARK 465     HIS C   278                                                      
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 334    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 340    CG   CD   CE   NZ                                   
REMARK 470     ASN A 366    CG   OD1  ND2                                       
REMARK 470     HIS B  39    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER B 283    OG                                                  
REMARK 470     GLU B 427    CG   CD   OE1  OE2                                  
REMARK 470     THR C  11    OG1  CG2                                            
REMARK 470     GLN C  51    CG   CD   OE1  NE2                                  
REMARK 470     ILE C  52    CG1  CG2  CD1                                       
REMARK 470     LEU C  91    CG   CD1  CD2                                       
REMARK 470     LYS C  92    CG   CD   CE   NZ                                   
REMARK 470     GLN C 178    CG   CD   OE1  NE2                                  
REMARK 470     HIS C 187    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS C 243    CG   CD   CE   NZ                                   
REMARK 470     ASP C 246    CG   OD1  OD2                                       
REMARK 470     GLU C 258    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 259    CG   CD   CE   NZ                                   
REMARK 470     LYS C 264    CG   CD   CE   NZ                                   
REMARK 470     ARG C 266    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER C 267    OG                                                  
REMARK 470     GLU C 270    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 271    CG   CD   OE1  OE2                                  
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   O    PHE C   226     N    LYS C   228              2.05            
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      -31.09     70.23                                   
REMARK 500    GLU A  48       86.88    175.05                                   
REMARK 500    ASN A 102       19.36     54.05                                   
REMARK 500    THR A 110      -86.32    -89.04                                   
REMARK 500    CYS A 201      116.59   -163.39                                   
REMARK 500    ARG A 222       88.07   -150.78                                   
REMARK 500    HIS A 267       36.46   -148.73                                   
REMARK 500    ASN A 287     -144.38   -114.70                                   
REMARK 500    ASN A 301       19.24   -140.42                                   
REMARK 500    ARG A 309       40.90   -100.62                                   
REMARK 500    ASP A 323       79.55    -63.95                                   
REMARK 500    THR A 341      -78.87    -68.44                                   
REMARK 500    ALA A 438     -137.13    -78.02                                   
REMARK 500    ARG B   2       74.75     42.26                                   
REMARK 500    ASP B  41      -27.04     69.83                                   
REMARK 500    GLU B  45      -76.42    -60.41                                   
REMARK 500    ARG B  46       32.60    -83.63                                   
REMARK 500    SER B  55       73.67    -58.11                                   
REMARK 500    SER B  56       -1.77   -168.17                                   
REMARK 500    LEU B  68       40.10    -87.06                                   
REMARK 500    GLU B  69      134.72    171.29                                   
REMARK 500    SER B  96     -174.14    -61.07                                   
REMARK 500    THR B 107      -96.34    -88.11                                   
REMARK 500    GLU B 125       21.41    -77.76                                   
REMARK 500    SER B 129       76.96   -162.01                                   
REMARK 500    ARG B 179       13.12    -69.52                                   
REMARK 500    LYS B 216       34.61     38.71                                   
REMARK 500    ASN B 218      -74.66    -54.03                                   
REMARK 500    GLN B 245     -152.04   -116.97                                   
REMARK 500    LEU B 263       62.13   -118.52                                   
REMARK 500    ALA B 302       46.77    -76.64                                   
REMARK 500    GLN B 359      123.36     46.38                                   
REMARK 500    PHE B 394        2.41     59.11                                   
REMARK 500    GLN B 426       48.25    -88.16                                   
REMARK 500    THR B 429       96.65    -65.46                                   
REMARK 500    GLU B 431     -151.84    -78.03                                   
REMARK 500    ASN C  39       27.47    -77.93                                   
REMARK 500    THR C  65       71.88   -114.94                                   
REMARK 500    LYS C  92      100.39     66.05                                   
REMARK 500    PRO C 146        3.52    -63.33                                   
REMARK 500    LYS C 212       -6.48    -57.44                                   
REMARK 500    PHE C 226     -106.59    -50.87                                   
REMARK 500    LYS C 227      -38.43     26.25                                   
REMARK 500    LYS C 243       60.00   -169.57                                   
REMARK 500    GLU C 270       56.01    -96.45                                   
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 GTP A 502   O2B                                                    
REMARK 620 2 GTP A 502   O2G  77.1                                              
REMARK 620 3 GLU A  72   OE2 135.9 138.1                                        
REMARK 620 N                    1     2                                         
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   O2B                                                    
REMARK 620 2 GTP B 502   O2G  83.2                                              
REMARK 620 3 GTP B 502   O3G  63.8  50.9                                        
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  4FFB A    1   447  UNP    P09733   TBA1_YEAST       1    447             
DBREF  4FFB B    1   457  UNP    P02557   TBB_YEAST        1    457             
DBREF  4FFB C    1   272  UNP    P46675   STU2_YEAST       1    272             
SEQADV 4FFB ARG B  175  UNP  P02557    THR   175 ENGINEERED MUTATION            
SEQADV 4FFB ARG B  179  UNP  P02557    VAL   179 ENGINEERED MUTATION            
SEQADV 4FFB HIS B  458  UNP  P02557              EXPRESSION TAG                 
SEQADV 4FFB HIS B  459  UNP  P02557              EXPRESSION TAG                 
SEQADV 4FFB HIS B  460  UNP  P02557              EXPRESSION TAG                 
SEQADV 4FFB HIS B  461  UNP  P02557              EXPRESSION TAG                 
SEQADV 4FFB HIS B  462  UNP  P02557              EXPRESSION TAG                 
SEQADV 4FFB HIS B  463  UNP  P02557              EXPRESSION TAG                 
SEQADV 4FFB HIS C  273  UNP  P46675              EXPRESSION TAG                 
SEQADV 4FFB HIS C  274  UNP  P46675              EXPRESSION TAG                 
SEQADV 4FFB HIS C  275  UNP  P46675              EXPRESSION TAG                 
SEQADV 4FFB HIS C  276  UNP  P46675              EXPRESSION TAG                 
SEQADV 4FFB HIS C  277  UNP  P46675              EXPRESSION TAG                 
SEQADV 4FFB HIS C  278  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  278  MET SER GLY GLU GLU GLU VAL ASP TYR THR THR LEU PRO          
SEQRES   2 C  278  LEU GLU GLU ARG LEU THR TYR LYS LEU TRP LYS ALA ARG          
SEQRES   3 C  278  LEU GLU ALA TYR LYS GLU LEU ASN GLN LEU PHE ARG ASN          
SEQRES   4 C  278  SER VAL GLY ASP ILE SER ARG ASP ASP ASN ILE GLN ILE          
SEQRES   5 C  278  TYR TRP ARG ASP PRO THR LEU PHE ALA GLN TYR ILE THR          
SEQRES   6 C  278  ASP SER ASN VAL VAL ALA GLN GLU GLN ALA ILE VAL ALA          
SEQRES   7 C  278  LEU ASN SER LEU ILE ASP ALA PHE ALA SER SER SER LEU          
SEQRES   8 C  278  LYS ASN ALA HIS ASN ILE THR LEU ILE SER THR TRP THR          
SEQRES   9 C  278  PRO LEU LEU VAL GLU LYS GLY LEU THR SER SER ARG ALA          
SEQRES  10 C  278  THR THR LYS THR GLN SER MET SER CYS ILE LEU SER LEU          
SEQRES  11 C  278  CYS GLY LEU ASP THR SER ILE THR GLN SER VAL GLU LEU          
SEQRES  12 C  278  VAL ILE PRO PHE PHE GLU LYS LYS LEU PRO LYS LEU ILE          
SEQRES  13 C  278  ALA ALA ALA ALA ASN CYS VAL TYR GLU LEU MET ALA ALA          
SEQRES  14 C  278  PHE GLY LEU THR ASN VAL ASN VAL GLN THR PHE LEU PRO          
SEQRES  15 C  278  GLU LEU LEU LYS HIS VAL PRO GLN LEU ALA GLY HIS GLY          
SEQRES  16 C  278  ASP ARG ASN VAL ARG SER GLN THR MET ASN LEU ILE VAL          
SEQRES  17 C  278  GLU ILE TYR LYS VAL THR GLY ASN ASN SER ASP LEU LEU          
SEQRES  18 C  278  GLU GLU ILE LEU PHE LYS LYS LEU LYS PRO ILE GLN VAL          
SEQRES  19 C  278  LYS ASP LEU HIS LYS LEU PHE ALA LYS VAL GLY ASP GLU          
SEQRES  20 C  278  PRO SER SER SER LYS MET LEU PHE GLU TRP GLU LYS ARG          
SEQRES  21 C  278  GLU LEU GLU LYS LYS ARG SER GLN GLU GLU GLU ALA HIS          
SEQRES  22 C  278  HIS HIS HIS HIS HIS                                          
HET     MG  A 501       1                                                       
HET    GTP  A 502      32                                                       
HET     MG  B 501       1                                                       
HET    GTP  B 502      32                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GTP GUANOSINE-5'-TRIPHOSPHATE                                        
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   5  GTP    2(C10 H16 N5 O14 P3)                                         
HELIX    1   1 GLY A   10  HIS A   28  1                                  19    
HELIX    2   2 GLY A   49  PHE A   53  1                                   5    
HELIX    3   3 PRO A   73  ASN A   81  1                                   9    
HELIX    4   4 HIS A   89  GLU A   91  5                                   3    
HELIX    5   5 ASN A  103  TYR A  109  1                                   7    
HELIX    6   6 VAL A  111  GLU A  114  5                                   4    
HELIX    7   7 ILE A  115  GLN A  129  1                                  15    
HELIX    8   8 GLY A  145  TYR A  162  1                                  18    
HELIX    9   9 ALA A  175  SER A  179  5                                   5    
HELIX   10  10 VAL A  183  THR A  195  1                                  13    
HELIX   11  11 ASN A  207  ASN A  217  1                                  11    
HELIX   12  12 SER A  224  THR A  240  1                                  17    
HELIX   13  13 THR A  240  PHE A  245  1                                   6    
HELIX   14  14 ASP A  252  VAL A  261  1                                  10    
HELIX   15  15 SER A  288  CYS A  296  1                                   9    
HELIX   16  16 PHE A  297  GLN A  302  5                                   6    
HELIX   17  17 VAL A  325  LYS A  339  1                                  15    
HELIX   18  18 ILE A  385  ALA A  401  1                                  17    
HELIX   19  19 VAL A  406  GLY A  411  1                                   6    
HELIX   20  20 GLU A  416  VAL A  436  1                                  21    
HELIX   21  21 GLY B   10  GLY B   29  1                                  20    
HELIX   22  22 ASP B   41  ARG B   46  1                                   6    
HELIX   23  23 LEU B   47  VAL B   49  5                                   3    
HELIX   24  24 GLU B   69  ASN B   78  1                                  10    
HELIX   25  25 SER B   79  ASN B   83  5                                   5    
HELIX   26  26 ARG B   86  ASP B   88  5                                   3    
HELIX   27  27 VAL B  100  TYR B  106  1                                   7    
HELIX   28  28 GLY B  109  GLU B  125  1                                  17    
HELIX   29  29 SER B  145  PHE B  159  1                                  15    
HELIX   30  30 VAL B  180  SER B  196  1                                  17    
HELIX   31  31 ASN B  204  THR B  214  1                                  11    
HELIX   32  32 SER B  221  THR B  237  1                                  17    
HELIX   33  33 THR B  237  TYR B  242  1                                   6    
HELIX   34  34 ASP B  249  VAL B  258  1                                  10    
HELIX   35  35 THR B  285  ASP B  295  1                                  11    
HELIX   36  36 ALA B  296  MET B  299  5                                   4    
HELIX   37  37 SER B  322  ASN B  337  1                                  16    
HELIX   38  38 ILE B  374  LYS B  390  1                                  17    
HELIX   39  39 PHE B  394  SER B  400  1                                   7    
HELIX   40  40 ASP B  404  TYR B  425  1                                  22    
HELIX   41  41 PRO C   13  LEU C   18  1                                   6    
HELIX   42  42 LEU C   22  ASN C   39  1                                  18    
HELIX   43  43 PRO C   57  ILE C   64  1                                   8    
HELIX   44  44 ASN C   68  ASP C   84  1                                  17    
HELIX   45  45 LYS C   92  GLY C  111  1                                  20    
HELIX   46  46 ARG C  116  LEU C  133  1                                  18    
HELIX   47  47 ILE C  137  ILE C  145  1                                   9    
HELIX   48  48 PRO C  146  LYS C  150  5                                   5    
HELIX   49  49 LEU C  152  GLY C  171  1                                  20    
HELIX   50  50 ASN C  176  LEU C  185  1                                  10    
HELIX   51  51 HIS C  187  GLY C  193  1                                   7    
HELIX   52  52 ASP C  196  LYS C  212  1                                  17    
HELIX   53  53 LYS C  230  ALA C  242  1                                  13    
HELIX   54  54 PHE C  255  GLU C  269  1                                  15    
SHEET    1   A 6 LEU A  93  SER A  95  0                                        
SHEET    2   A 6 ALA A  66  ASP A  70  1  N  TYR A  68   O  ILE A  94           
SHEET    3   A 6 VAL A   4  VAL A   9  1  N  ASN A   8   O  VAL A  69           
SHEET    4   A 6 GLY A 135  SER A 141  1  O  GLY A 135   N  ILE A   5           
SHEET    5   A 6 SER A 166  TYR A 173  1  O  PHE A 170   N  PHE A 138           
SHEET    6   A 6 CYS A 201  ASP A 206  1  O  VAL A 205   N  ALA A 171           
SHEET    1   B 2 PHE A  54  GLY A  58  0                                        
SHEET    2   B 2 LYS A  61  PRO A  64 -1  O  VAL A  63   N  HIS A  55           
SHEET    1   C 4 LEU A 270  SER A 274  0                                        
SHEET    2   C 4 ARG A 374  THR A 382 -1  O  SER A 380   N  LEU A 270           
SHEET    3   C 4 TYR A 313  GLY A 322 -1  N  ARG A 321   O  ALA A 375           
SHEET    4   C 4 PHE A 352  CYS A 357  1  O  LYS A 353   N  LEU A 318           
SHEET    1   D10 TYR B  90  PHE B  92  0                                        
SHEET    2   D10 SER B  63  ASP B  67  1  N  ASN B  65   O  ILE B  91           
SHEET    3   D10 ILE B   4  THR B   9  1  N  SER B   8   O  ILE B  64           
SHEET    4   D10 GLY B 132  SER B 138  1  O  GLN B 134   N  ILE B   7           
SHEET    5   D10 MET B 163  LEU B 170  1  O  MET B 163   N  PHE B 133           
SHEET    6   D10 GLU B 198  ASP B 203  1  O  PHE B 200   N  THR B 166           
SHEET    7   D10 PHE B 265  ALA B 271  1  O  PHE B 266   N  CYS B 201           
SHEET    8   D10 MET B 363  SER B 371 -1  O  ALA B 365   N  ALA B 271           
SHEET    9   D10 TYR B 310  GLY B 319 -1  N  THR B 312   O  ASN B 370           
SHEET   10   D10 VAL B 349  CYS B 354  1  O  ALA B 352   N  PHE B 317           
SHEET    1   E 2 PHE B  51  GLU B  53  0                                        
SHEET    2   E 2 TRP B  59  PRO B  61 -1  O  VAL B  60   N  ASN B  52           
LINK        MG    MG A 501                 O2B GTP A 502     1555   1555  2.07  
LINK        MG    MG A 501                 O2G GTP A 502     1555   1555  2.08  
LINK        MG    MG B 501                 O2B GTP B 502     1555   1555  2.59  
LINK         OE2 GLU A  72                MG    MG A 501     1555   1555  2.65  
LINK        MG    MG B 501                 O2G GTP B 502     1555   1555  2.85  
LINK        MG    MG B 501                 O3G GTP B 502     1555   1555  2.92  
CISPEP   1 GLY A   46    GLU A   47          0         3.78                     
CISPEP   2 SER A  274    PRO A  275          0        -1.73                     
CISPEP   3 ALA B  271    PRO B  272          0         1.03                     
CISPEP   4 GLN B  359    GLY B  360          0         4.48                     
CISPEP   5 LEU C   12    PRO C   13          0        -1.75                     
CISPEP   6 PHE C   86    ALA C   87          0         0.07                     
SITE     1 AC1  3 GLN A  11  GLU A  72  GTP A 502                               
SITE     1 AC2 21 GLY A  10  GLN A  11  ALA A  12  GLN A  15                    
SITE     2 AC2 21 ALA A 100  ALA A 101  ASN A 102  SER A 141                    
SITE     3 AC2 21 GLY A 144  GLY A 145  THR A 146  GLY A 147                    
SITE     4 AC2 21 VAL A 178  THR A 180  GLU A 184  ASN A 207                    
SITE     5 AC2 21 PHE A 225  ASN A 229  ILE A 232   MG A 501                    
SITE     6 AC2 21 LYS B 252                                                     
SITE     1 AC3  2 GLU B  69  GTP B 502                                          
SITE     1 AC4 19 GLY B  10  GLN B  11  CYS B  12  GLN B  15                    
SITE     2 AC4 19 ASP B  67  SER B  96  ALA B  97  GLY B  98                    
SITE     3 AC4 19 ASN B  99  SER B 138  GLY B 141  GLY B 142                    
SITE     4 AC4 19 THR B 143  GLY B 144  GLU B 181  ASN B 204                    
SITE     5 AC4 19 TYR B 222  ASN B 226   MG B 501                               
CRYST1   89.120   98.040   91.366  90.00 100.31  90.00 P 1 21 1      2          
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      0.011221  0.000000  0.002041        0.00000                         
SCALE2      0.000000  0.010200  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011125        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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