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Database: PDB
Entry: 5TUV
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HEADER    TRANSCRIPTION                           07-NOV-16   5TUV              
TITLE     CRYSTAL STRUCTURE OF THE E2F5-DP1-P107 TERNARY COMPLEX                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSCRIPTION FACTOR DP1;                                  
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 199-350;                                      
COMPND   5 SYNONYM: DRTF1-POLYPEPTIDE 1,DRTF1,E2F DIMERIZATION PARTNER 1;       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: TRANSCRIPTION FACTOR E2F5;                                 
COMPND   9 CHAIN: B, E;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 124-232;                                      
COMPND  11 SYNONYM: E2F-5;                                                      
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: RETINOBLASTOMA-LIKE PROTEIN 1;                             
COMPND  15 CHAIN: C, F;                                                         
COMPND  16 FRAGMENT: UNP RESIDUES 994-1031;                                     
COMPND  17 SYNONYM: 107 KDA RETINOBLASTOMA-ASSOCIATED PROTEIN,P107,PRB1;        
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TFDP1, DP1;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: E2F5;                                                          
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: RBL1;                                                          
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    TRANSCRIPTION FACTOR, CELL-CYCLE REGULATION, TRANSCRIPTION            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.J.LIBAN,S.M.TRIPATHI,S.M.RUBIN                                      
REVDAT   5   04-DEC-19 5TUV    1       REMARK                                   
REVDAT   4   27-SEP-17 5TUV    1       REMARK                                   
REVDAT   3   24-MAY-17 5TUV    1       JRNL                                     
REVDAT   2   10-MAY-17 5TUV    1       JRNL                                     
REVDAT   1   03-MAY-17 5TUV    0                                                
JRNL        AUTH   T.J.LIBAN,E.M.MEDINA,S.TRIPATHI,S.SENGUPTA,R.W.HENRY,        
JRNL        AUTH 2 N.E.BUCHLER,S.M.RUBIN                                        
JRNL        TITL   CONSERVATION AND DIVERGENCE OF C-TERMINAL DOMAIN STRUCTURE   
JRNL        TITL 2 IN THE RETINOBLASTOMA PROTEIN FAMILY.                        
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 114  4942 2017              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   28439018                                                     
JRNL        DOI    10.1073/PNAS.1619170114                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.27                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 15296                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.240                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 802                             
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 49.2730 -  5.2679    0.99     2467   130  0.2071 0.2512        
REMARK   3     2  5.2679 -  4.1820    1.00     2426   137  0.1869 0.2231        
REMARK   3     3  4.1820 -  3.6536    1.00     2396   143  0.2017 0.2597        
REMARK   3     4  3.6536 -  3.3196    1.00     2436   116  0.2260 0.2867        
REMARK   3     5  3.3196 -  3.0817    1.00     2386   132  0.2464 0.2896        
REMARK   3     6  3.0817 -  2.9000    1.00     2383   144  0.2734 0.3281        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.680           
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           3584                                  
REMARK   3   ANGLE     :  0.816           4856                                  
REMARK   3   CHIRALITY :  0.030            565                                  
REMARK   3   PLANARITY :  0.004            640                                  
REMARK   3   DIHEDRAL  : 13.968           1303                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 198 THROUGH 246 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  24.2733  46.5872 -30.3637              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6570 T22:   0.6619                                     
REMARK   3      T33:   0.4287 T12:   0.0146                                     
REMARK   3      T13:   0.0207 T23:  -0.2777                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3441 L22:   1.3457                                     
REMARK   3      L33:   1.6695 L12:  -0.1487                                     
REMARK   3      L13:  -2.0960 L23:  -0.1488                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0725 S12:   0.5562 S13:  -0.8543                       
REMARK   3      S21:  -0.3023 S22:   0.1834 S23:  -0.1965                       
REMARK   3      S31:   0.0470 S32:   0.0971 S33:  -0.1701                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 247 THROUGH 261 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.9662  46.6903 -11.2564              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5713 T22:   0.6170                                     
REMARK   3      T33:   0.5027 T12:   0.1718                                     
REMARK   3      T13:  -0.0810 T23:   0.1083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2855 L22:   0.3292                                     
REMARK   3      L33:   0.6976 L12:  -0.6191                                     
REMARK   3      L13:  -0.0237 L23:   0.1705                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4664 S12:  -0.2404 S13:   0.1562                       
REMARK   3      S21:   0.5025 S22:   0.3043 S23:  -0.1157                       
REMARK   3      S31:  -0.9955 S32:  -1.0676 S33:  -0.1122                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 262 THROUGH 305 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  17.8038  41.4381  -5.7618              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3631 T22:   0.2293                                     
REMARK   3      T33:   0.4209 T12:   0.0033                                     
REMARK   3      T13:   0.0209 T23:   0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4837 L22:   2.8543                                     
REMARK   3      L33:   1.7127 L12:  -0.6235                                     
REMARK   3      L13:   0.0559 L23:   0.0958                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2579 S12:   0.0717 S13:  -0.1754                       
REMARK   3      S21:  -0.0715 S22:  -0.1191 S23:   0.3478                       
REMARK   3      S31:   0.6286 S32:   0.0415 S33:  -0.1657                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 124 THROUGH 162 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  32.8631  53.4280 -36.7363              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6228 T22:   1.1547                                     
REMARK   3      T33:   0.5000 T12:   0.2062                                     
REMARK   3      T13:  -0.0611 T23:  -0.1708                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8342 L22:   1.2175                                     
REMARK   3      L33:   2.1038 L12:   0.0862                                     
REMARK   3      L13:  -2.8446 L23:  -0.0718                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2628 S12:   1.5106 S13:  -0.1530                       
REMARK   3      S21:  -0.4542 S22:  -0.0678 S23:  -0.0971                       
REMARK   3      S31:  -0.4149 S32:  -0.3661 S33:  -0.2038                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 163 THROUGH 170 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   2.3862  55.7824 -19.9058              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5938 T22:   0.2778                                     
REMARK   3      T33:   0.5697 T12:   0.0631                                     
REMARK   3      T13:   0.0089 T23:   0.0935                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7460 L22:   5.1041                                     
REMARK   3      L33:   3.5245 L12:  -0.6680                                     
REMARK   3      L13:  -1.1602 L23:   0.0500                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3876 S12:   0.4708 S13:   1.2033                       
REMARK   3      S21:   0.0163 S22:   0.0067 S23:  -0.0154                       
REMARK   3      S31:  -1.1592 S32:   0.4660 S33:  -0.2096                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 171 THROUGH 181 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.9434  38.8373 -14.7329              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3308 T22:   0.3870                                     
REMARK   3      T33:   0.5891 T12:   0.0510                                     
REMARK   3      T13:  -0.2629 T23:  -0.0859                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6350 L22:   2.8621                                     
REMARK   3      L33:   4.7149 L12:  -2.9505                                     
REMARK   3      L13:  -0.8504 L23:  -1.5695                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1255 S12:  -0.1363 S13:  -0.5494                       
REMARK   3      S21:  -0.2400 S22:  -0.1709 S23:   0.4164                       
REMARK   3      S31:   0.8282 S32:  -0.3443 S33:  -0.7975                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 182 THROUGH 191 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1760  36.8571  -7.7729              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3547 T22:   0.3032                                     
REMARK   3      T33:   0.3529 T12:   0.0433                                     
REMARK   3      T13:  -0.0747 T23:  -0.0549                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1082 L22:   8.4715                                     
REMARK   3      L33:   6.2593 L12:   3.4461                                     
REMARK   3      L13:  -0.4134 L23:   0.5434                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3172 S12:   0.0941 S13:  -1.2017                       
REMARK   3      S21:  -0.4377 S22:  -0.0282 S23:  -0.6878                       
REMARK   3      S31:   0.4733 S32:  -0.4990 S33:  -0.0132                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 192 THROUGH 215 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  26.9445  43.2501  -2.8826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2737 T22:   0.2360                                     
REMARK   3      T33:   0.4055 T12:   0.1807                                     
REMARK   3      T13:  -0.1451 T23:  -0.0927                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8231 L22:   7.5143                                     
REMARK   3      L33:   2.2944 L12:  -3.8666                                     
REMARK   3      L13:   1.8053 L23:  -3.1742                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0468 S12:  -0.5995 S13:   0.2958                       
REMARK   3      S21:   0.3601 S22:   0.3175 S23:  -1.0298                       
REMARK   3      S31:  -0.2193 S32:   0.5814 S33:   0.2689                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 216 THROUGH 230 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  13.0710  48.3240  -4.0771              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3292 T22:   0.2946                                     
REMARK   3      T33:   0.2086 T12:   0.0234                                     
REMARK   3      T13:   0.0208 T23:  -0.0504                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5761 L22:   6.6639                                     
REMARK   3      L33:   3.9440 L12:   0.0102                                     
REMARK   3      L13:   1.0329 L23:   1.2407                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2491 S12:   0.2223 S13:   0.3372                       
REMARK   3      S21:  -0.8128 S22:  -0.1396 S23:   0.2289                       
REMARK   3      S31:  -0.0313 S32:  -0.0717 S33:   0.0472                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1000 THROUGH 1023 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  26.4888  42.7592 -12.9145              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4651 T22:   0.3018                                     
REMARK   3      T33:   0.2593 T12:   0.0427                                     
REMARK   3      T13:   0.0014 T23:  -0.0421                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2573 L22:   6.8993                                     
REMARK   3      L33:   4.0740 L12:  -1.6057                                     
REMARK   3      L13:   0.5287 L23:  -1.2528                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2048 S12:   1.1709 S13:   0.0397                       
REMARK   3      S21:  -1.2830 S22:  -0.2778 S23:  -0.6957                       
REMARK   3      S31:   0.3908 S32:   0.6827 S33:  -0.0998                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1024 THROUGH 1028 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  40.6342  32.0536  -6.6723              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8678 T22:  -0.2137                                     
REMARK   3      T33:   1.0238 T12:   0.6719                                     
REMARK   3      T13:  -0.4241 T23:   0.0889                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9038 L22:   0.9637                                     
REMARK   3      L33:   1.9675 L12:  -1.6672                                     
REMARK   3      L13:   2.3886 L23:  -1.3791                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7651 S12:   0.3074 S13:   0.7042                       
REMARK   3      S21:   0.2408 S22:   0.4091 S23:   1.0071                       
REMARK   3      S31:  -0.5584 S32:  -0.5991 S33:   0.7682                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 208 THROUGH 243 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.7645  39.7597  33.5201              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5779 T22:   0.8791                                     
REMARK   3      T33:   0.4029 T12:   0.0180                                     
REMARK   3      T13:   0.1089 T23:  -0.0634                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6148 L22:   3.0153                                     
REMARK   3      L33:   2.4415 L12:  -2.3063                                     
REMARK   3      L13:  -2.4059 L23:   0.5482                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1074 S12:  -0.5325 S13:   0.3967                       
REMARK   3      S21:   0.5765 S22:   0.0364 S23:   0.1972                       
REMARK   3      S31:  -0.5012 S32:  -0.4701 S33:  -0.1262                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 244 THROUGH 271 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.5274  33.4291  13.2935              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3321 T22:   0.4593                                     
REMARK   3      T33:   0.4777 T12:  -0.0633                                     
REMARK   3      T13:   0.0967 T23:  -0.0199                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0872 L22:   2.2364                                     
REMARK   3      L33:   1.9010 L12:  -0.6623                                     
REMARK   3      L13:  -0.0916 L23:  -0.9269                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1552 S12:   0.0939 S13:   0.2031                       
REMARK   3      S21:  -0.1855 S22:  -0.0973 S23:  -0.2738                       
REMARK   3      S31:   0.5357 S32:   0.5614 S33:  -0.0148                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 272 THROUGH 290 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4963  48.5507   3.6307              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2671 T22:   0.3414                                     
REMARK   3      T33:   0.3285 T12:  -0.0465                                     
REMARK   3      T13:   0.0345 T23:  -0.0201                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0914 L22:   3.9503                                     
REMARK   3      L33:   2.7319 L12:   2.0388                                     
REMARK   3      L13:  -0.6847 L23:  -1.2009                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3053 S12:  -0.1533 S13:   0.0694                       
REMARK   3      S21:   0.0853 S22:  -0.2444 S23:   0.5668                       
REMARK   3      S31:  -0.5019 S32:  -0.1863 S33:   0.0083                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 291 THROUGH 306 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.5894  33.5206  20.6965              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2987 T22:   0.4944                                     
REMARK   3      T33:   0.4881 T12:  -0.1261                                     
REMARK   3      T13:   0.0361 T23:  -0.0565                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9425 L22:   5.0015                                     
REMARK   3      L33:   8.0316 L12:  -3.0649                                     
REMARK   3      L13:   3.8065 L23:  -5.6851                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2075 S12:  -0.8552 S13:   0.0710                       
REMARK   3      S21:   0.2805 S22:   0.2574 S23:   0.5032                       
REMARK   3      S31:   0.1897 S32:  -0.6970 S33:  -0.1979                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 125 THROUGH 162 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.7634  50.3448  45.2871              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9987 T22:   1.0412                                     
REMARK   3      T33:   0.6487 T12:   0.0116                                     
REMARK   3      T13:   0.1733 T23:   0.0166                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8089 L22:   2.0219                                     
REMARK   3      L33:   1.8522 L12:  -2.0839                                     
REMARK   3      L13:  -1.3479 L23:  -0.0578                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2374 S12:  -0.3068 S13:   0.1530                       
REMARK   3      S21:   0.5917 S22:  -0.2562 S23:   0.0213                       
REMARK   3      S31:  -0.2649 S32:   0.1638 S33:   0.2038                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 163 THROUGH 181 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2295  31.5486  21.4323              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4248 T22:   0.8213                                     
REMARK   3      T33:   0.4100 T12:  -0.0570                                     
REMARK   3      T13:  -0.0089 T23:   0.1222                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8040 L22:   2.1657                                     
REMARK   3      L33:   2.5040 L12:   0.7396                                     
REMARK   3      L13:   1.8945 L23:   0.3126                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4195 S12:  -0.5264 S13:   0.5759                       
REMARK   3      S21:   0.0349 S22:  -0.2847 S23:   0.3206                       
REMARK   3      S31:  -0.2995 S32:   0.7772 S33:   0.2386                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 182 THROUGH 231 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.9702  43.7139   9.7195              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3059 T22:   0.3278                                     
REMARK   3      T33:   0.4358 T12:  -0.0674                                     
REMARK   3      T13:   0.0326 T23:  -0.0162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5897 L22:   3.4987                                     
REMARK   3      L33:   1.9440 L12:  -1.1945                                     
REMARK   3      L13:  -1.2197 L23:  -1.0530                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0564 S12:  -0.1500 S13:   0.0672                       
REMARK   3      S21:   0.2438 S22:   0.1778 S23:   0.3870                       
REMARK   3      S31:  -0.0472 S32:  -0.0266 S33:  -0.0710                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 1001 THROUGH 1014 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   2.4571  46.5601  21.2429              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9546 T22:   0.7370                                     
REMARK   3      T33:   0.6761 T12:   0.0404                                     
REMARK   3      T13:   0.2372 T23:  -0.0261                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2750 L22:   4.8042                                     
REMARK   3      L33:   0.9536 L12:  -0.7809                                     
REMARK   3      L13:   0.9922 L23:  -1.5219                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2599 S12:  -0.5354 S13:  -0.5049                       
REMARK   3      S21:   1.1425 S22:   0.2945 S23:   0.3811                       
REMARK   3      S31:  -0.5796 S32:  -0.2710 S33:  -0.1956                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 1015 THROUGH 1024 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.9921  40.6771  15.9863              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3639 T22:   0.8612                                     
REMARK   3      T33:   0.7397 T12:   0.0754                                     
REMARK   3      T13:   0.1158 T23:   0.0763                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5538 L22:   7.4882                                     
REMARK   3      L33:   9.3849 L12:  -1.2265                                     
REMARK   3      L13:   2.0869 L23:  -3.0654                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4941 S12:  -1.0803 S13:  -0.5253                       
REMARK   3      S21:   0.3917 S22:   0.4561 S23:   1.5831                       
REMARK   3      S31:   0.5333 S32:  -0.7922 S33:  -0.3368                       
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 5TUV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000224830.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-FEB-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15301                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.570                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 10.60                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: AUTOSOL                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES PH 7.0, 7% PEG 5000, 5% 1    
REMARK 280  -PROPANOL, 2% 2-PROPANOL, VAPOR DIFFUSION, SITTING DROP,            
REMARK 280  TEMPERATURE 295K                                                    
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       28.67000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL                        
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17330 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 24570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -117.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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     GLY A   196                                                      
REMARK 465     GLU A   197                                                      
REMARK 465     SER A   248                                                      
REMARK 465     ALA A   306                                                      
REMARK 465     CYS A   307                                                      
REMARK 465     GLY A   308                                                      
REMARK 465     LEU A   309                                                      
REMARK 465     GLU A   310                                                      
REMARK 465     SER A   311                                                      
REMARK 465     GLY A   312                                                      
REMARK 465     SER A   313                                                      
REMARK 465     CYS A   314                                                      
REMARK 465     SER A   315                                                      
REMARK 465     ALA A   316                                                      
REMARK 465     GLU A   317                                                      
REMARK 465     ASP A   318                                                      
REMARK 465     LEU A   319                                                      
REMARK 465     LYS A   320                                                      
REMARK 465     MET A   321                                                      
REMARK 465     ALA A   322                                                      
REMARK 465     ARG A   323                                                      
REMARK 465     SER A   324                                                      
REMARK 465     LEU A   325                                                      
REMARK 465     VAL A   326                                                      
REMARK 465     PRO A   327                                                      
REMARK 465     LYS A   328                                                      
REMARK 465     ALA A   329                                                      
REMARK 465     LEU A   330                                                      
REMARK 465     GLU A   331                                                      
REMARK 465     PRO A   332                                                      
REMARK 465     TYR A   333                                                      
REMARK 465     VAL A   334                                                      
REMARK 465     THR A   335                                                      
REMARK 465     GLU A   336                                                      
REMARK 465     MET A   337                                                      
REMARK 465     ALA A   338                                                      
REMARK 465     GLN A   339                                                      
REMARK 465     GLY A   340                                                      
REMARK 465     THR A   341                                                      
REMARK 465     VAL A   342                                                      
REMARK 465     GLY A   343                                                      
REMARK 465     GLY A   344                                                      
REMARK 465     VAL A   345                                                      
REMARK 465     PHE A   346                                                      
REMARK 465     ILE A   347                                                      
REMARK 465     THR A   348                                                      
REMARK 465     THR A   349                                                      
REMARK 465     ALA A   350                                                      
REMARK 465     GLY B   121                                                      
REMARK 465     HIS B   122                                                      
REMARK 465     MET B   123                                                      
REMARK 465     GLN B   207                                                      
REMARK 465     ASN B   208                                                      
REMARK 465     GLY B   209                                                      
REMARK 465     LYS B   231                                                      
REMARK 465     GLU B   232                                                      
REMARK 465     GLY C   991                                                      
REMARK 465     GLU C   992                                                      
REMARK 465     PHE C   993                                                      
REMARK 465     SER C   994                                                      
REMARK 465     GLY C   995                                                      
REMARK 465     LEU C   996                                                      
REMARK 465     THR C   997                                                      
REMARK 465     PRO C   998                                                      
REMARK 465     ARG C   999                                                      
REMARK 465     LYS C  1029                                                      
REMARK 465     LYS C  1030                                                      
REMARK 465     ARG C  1031                                                      
REMARK 465     GLY D   196                                                      
REMARK 465     GLU D   197                                                      
REMARK 465     PHE D   198                                                      
REMARK 465     ALA D   199                                                      
REMARK 465     GLN D   200                                                      
REMARK 465     GLU D   201                                                      
REMARK 465     CYS D   202                                                      
REMARK 465     GLN D   203                                                      
REMARK 465     ASN D   204                                                      
REMARK 465     LEU D   205                                                      
REMARK 465     GLU D   206                                                      
REMARK 465     VAL D   207                                                      
REMARK 465     GLN D   246                                                      
REMARK 465     ALA D   247                                                      
REMARK 465     SER D   248                                                      
REMARK 465     ARG D   249                                                      
REMARK 465     CYS D   307                                                      
REMARK 465     GLY D   308                                                      
REMARK 465     LEU D   309                                                      
REMARK 465     GLU D   310                                                      
REMARK 465     SER D   311                                                      
REMARK 465     GLY D   312                                                      
REMARK 465     SER D   313                                                      
REMARK 465     CYS D   314                                                      
REMARK 465     SER D   315                                                      
REMARK 465     ALA D   316                                                      
REMARK 465     GLU D   317                                                      
REMARK 465     ASP D   318                                                      
REMARK 465     LEU D   319                                                      
REMARK 465     LYS D   320                                                      
REMARK 465     MET D   321                                                      
REMARK 465     ALA D   322                                                      
REMARK 465     ARG D   323                                                      
REMARK 465     SER D   324                                                      
REMARK 465     LEU D   325                                                      
REMARK 465     VAL D   326                                                      
REMARK 465     PRO D   327                                                      
REMARK 465     LYS D   328                                                      
REMARK 465     ALA D   329                                                      
REMARK 465     LEU D   330                                                      
REMARK 465     GLU D   331                                                      
REMARK 465     PRO D   332                                                      
REMARK 465     TYR D   333                                                      
REMARK 465     VAL D   334                                                      
REMARK 465     THR D   335                                                      
REMARK 465     GLU D   336                                                      
REMARK 465     MET D   337                                                      
REMARK 465     ALA D   338                                                      
REMARK 465     GLN D   339                                                      
REMARK 465     GLY D   340                                                      
REMARK 465     THR D   341                                                      
REMARK 465     VAL D   342                                                      
REMARK 465     GLY D   343                                                      
REMARK 465     GLY D   344                                                      
REMARK 465     VAL D   345                                                      
REMARK 465     PHE D   346                                                      
REMARK 465     ILE D   347                                                      
REMARK 465     THR D   348                                                      
REMARK 465     THR D   349                                                      
REMARK 465     ALA D   350                                                      
REMARK 465     GLY E   121                                                      
REMARK 465     HIS E   122                                                      
REMARK 465     MET E   123                                                      
REMARK 465     LYS E   124                                                      
REMARK 465     GLY E   206                                                      
REMARK 465     GLN E   207                                                      
REMARK 465     ASN E   208                                                      
REMARK 465     GLY E   209                                                      
REMARK 465     GLU E   232                                                      
REMARK 465     GLY F   991                                                      
REMARK 465     GLU F   992                                                      
REMARK 465     PHE F   993                                                      
REMARK 465     SER F   994                                                      
REMARK 465     GLY F   995                                                      
REMARK 465     LEU F   996                                                      
REMARK 465     THR F   997                                                      
REMARK 465     PRO F   998                                                      
REMARK 465     ARG F   999                                                      
REMARK 465     SER F  1000                                                      
REMARK 465     GLU F  1025                                                      
REMARK 465     GLN F  1026                                                      
REMARK 465     ARG F  1027                                                      
REMARK 465     THR F  1028                                                      
REMARK 465     LYS F  1029                                                      
REMARK 465     LYS F  1030                                                      
REMARK 465     ARG F  1031                                                      
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     PHE A 198    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A 203    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 214    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 217    CG   CD   CE   NZ                                   
REMARK 470     GLN A 218    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 222    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 225    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 234    CG   CD   CE   NZ                                   
REMARK 470     GLN A 238    CG   CD   OE1  NE2                                  
REMARK 470     HIS A 242    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 244    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 268    CG   CD   CE   NZ                                   
REMARK 470     LYS A 269    CG   CD   CE   NZ                                   
REMARK 470     ARG B 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 131    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 133    CG   CD1  CD2                                       
REMARK 470     LYS B 134    CG   CD   CE   NZ                                   
REMARK 470     ASP B 139    CG   OD1  OD2                                       
REMARK 470     GLU B 141    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 143    CG   CD   CE   NZ                                   
REMARK 470     LYS B 159    CG   CD   CE   NZ                                   
REMARK 470     GLU B 176    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 183    CG   OD1  ND2                                       
REMARK 470     GLN B 210    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 218    CG   CD   CE   NZ                                   
REMARK 470     LYS C1015    CG   CD   CE   NZ                                   
REMARK 470     GLU D 214    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 217    CG   CD   CE   NZ                                   
REMARK 470     GLN D 218    CG   CD   OE1  NE2                                  
REMARK 470     GLN D 220    CG   CD   OE1  NE2                                  
REMARK 470     LEU D 223    CG   CD1  CD2                                       
REMARK 470     GLN D 224    CG   CD   OE1  NE2                                  
REMARK 470     GLU D 225    CG   CD   OE1  OE2                                  
REMARK 470     LEU D 228    CG   CD1  CD2                                       
REMARK 470     LYS D 234    CG   CD   CE   NZ                                   
REMARK 470     LYS D 268    CG   CD   CE   NZ                                   
REMARK 470     LYS D 269    CG   CD   CE   NZ                                   
REMARK 470     GLU E 125    CG   CD   OE1  OE2                                  
REMARK 470     VAL E 126    CG1  CG2                                            
REMARK 470     ILE E 127    CG1  CG2  CD1                                       
REMARK 470     ARG E 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU E 133    CG   CD1  CD2                                       
REMARK 470     LYS E 134    CG   CD   CE   NZ                                   
REMARK 470     GLU E 138    CG   CD   OE1  OE2                                  
REMARK 470     LEU E 140    CG   CD1  CD2                                       
REMARK 470     GLU E 141    CG   CD   OE1  OE2                                  
REMARK 470     LEU E 142    CG   CD1  CD2                                       
REMARK 470     LYS E 143    CG   CD   CE   NZ                                   
REMARK 470     ARG E 145    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E 146    CG   CD   OE1  OE2                                  
REMARK 470     GLN E 149    CG   CD   OE1  NE2                                  
REMARK 470     LYS E 151    CG   CD   CE   NZ                                   
REMARK 470     LEU E 154    CG   CD1  CD2                                       
REMARK 470     GLN E 155    CG   CD   OE1  NE2                                  
REMARK 470     GLN E 156    CG   CD   OE1  NE2                                  
REMARK 470     ILE E 158    CG1  CG2  CD1                                       
REMARK 470     LYS E 159    CG   CD   CE   NZ                                   
REMARK 470     ASP E 163    CG   OD1  OD2                                       
REMARK 470     GLU E 176    CG   CD   OE1  OE2                                  
REMARK 470     GLN E 197    CG   CD   OE1  NE2                                  
REMARK 470     GLU E 199    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 204    CG   CD   OE1  OE2                                  
REMARK 470     MET E 205    CG   SD   CE                                        
REMARK 470     LYS E 218    CG   CD   CE   NZ                                   
REMARK 470     LYS E 231    CG   CD   CE   NZ                                   
REMARK 470     LYS F1005    CG   CD   CE   NZ                                   
REMARK 470     ASN F1007    CG   OD1  ND2                                       
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    LYS F  1005     OG   SER F  1009              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    ARG A 209      -71.10    -49.16                                   
REMARK 500    SER A 255        8.58     59.48                                   
REMARK 500    SER A 277     -163.25   -109.05                                   
REMARK 500    ASP B 185     -177.38     65.90                                   
REMARK 500    PRO B 203       68.05    -69.04                                   
REMARK 500    ASP E 163       55.56   -119.09                                   
REMARK 500    SER E 221     -158.55   -166.24                                   
REMARK 500    ASN F1007      -21.62     63.61                                   
REMARK 500    GLN F1023       36.59    -89.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5TUU   RELATED DB: PDB                                   
DBREF  5TUV A  199   350  UNP    Q14186   TFDP1_HUMAN    199    350             
DBREF  5TUV B  124   232  UNP    Q15329   E2F5_HUMAN     124    232             
DBREF  5TUV C  994  1031  UNP    P28749   RBL1_HUMAN     994   1031             
DBREF  5TUV D  199   350  UNP    Q14186   TFDP1_HUMAN    199    350             
DBREF  5TUV E  124   232  UNP    Q15329   E2F5_HUMAN     124    232             
DBREF  5TUV F  994  1031  UNP    P28749   RBL1_HUMAN     994   1031             
SEQADV 5TUV GLY A  196  UNP  Q14186              EXPRESSION TAG                 
SEQADV 5TUV GLU A  197  UNP  Q14186              EXPRESSION TAG                 
SEQADV 5TUV PHE A  198  UNP  Q14186              EXPRESSION TAG                 
SEQADV 5TUV GLY B  121  UNP  Q15329              EXPRESSION TAG                 
SEQADV 5TUV HIS B  122  UNP  Q15329              EXPRESSION TAG                 
SEQADV 5TUV MET B  123  UNP  Q15329              EXPRESSION TAG                 
SEQADV 5TUV GLY C  991  UNP  P28749              EXPRESSION TAG                 
SEQADV 5TUV GLU C  992  UNP  P28749              EXPRESSION TAG                 
SEQADV 5TUV PHE C  993  UNP  P28749              EXPRESSION TAG                 
SEQADV 5TUV GLY D  196  UNP  Q14186              EXPRESSION TAG                 
SEQADV 5TUV GLU D  197  UNP  Q14186              EXPRESSION TAG                 
SEQADV 5TUV PHE D  198  UNP  Q14186              EXPRESSION TAG                 
SEQADV 5TUV GLY E  121  UNP  Q15329              EXPRESSION TAG                 
SEQADV 5TUV HIS E  122  UNP  Q15329              EXPRESSION TAG                 
SEQADV 5TUV MET E  123  UNP  Q15329              EXPRESSION TAG                 
SEQADV 5TUV GLY F  991  UNP  P28749              EXPRESSION TAG                 
SEQADV 5TUV GLU F  992  UNP  P28749              EXPRESSION TAG                 
SEQADV 5TUV PHE F  993  UNP  P28749              EXPRESSION TAG                 
SEQRES   1 A  155  GLY GLU PHE ALA GLN GLU CYS GLN ASN LEU GLU VAL GLU          
SEQRES   2 A  155  ARG GLN ARG ARG LEU GLU ARG ILE LYS GLN LYS GLN SER          
SEQRES   3 A  155  GLN LEU GLN GLU LEU ILE LEU GLN GLN ILE ALA PHE LYS          
SEQRES   4 A  155  ASN LEU VAL GLN ARG ASN ARG HIS ALA GLU GLN GLN ALA          
SEQRES   5 A  155  SER ARG PRO PRO PRO PRO ASN SER VAL ILE HIS LEU PRO          
SEQRES   6 A  155  PHE ILE ILE VAL ASN THR SER LYS LYS THR VAL ILE ASP          
SEQRES   7 A  155  CYS SER ILE SER ASN ASP LYS PHE GLU TYR LEU PHE ASN          
SEQRES   8 A  155  PHE ASP ASN THR PHE GLU ILE HIS ASP ASP ILE GLU VAL          
SEQRES   9 A  155  LEU LYS ARG MET GLY MET ALA CYS GLY LEU GLU SER GLY          
SEQRES  10 A  155  SER CYS SER ALA GLU ASP LEU LYS MET ALA ARG SER LEU          
SEQRES  11 A  155  VAL PRO LYS ALA LEU GLU PRO TYR VAL THR GLU MET ALA          
SEQRES  12 A  155  GLN GLY THR VAL GLY GLY VAL PHE ILE THR THR ALA              
SEQRES   1 B  112  GLY HIS MET LYS GLU VAL ILE ASP ARG LEU ARG TYR LEU          
SEQRES   2 B  112  LYS ALA GLU ILE GLU ASP LEU GLU LEU LYS GLU ARG GLU          
SEQRES   3 B  112  LEU ASP GLN GLN LYS LEU TRP LEU GLN GLN SER ILE LYS          
SEQRES   4 B  112  ASN VAL MET ASP ASP SER ILE ASN ASN ARG PHE SER TYR          
SEQRES   5 B  112  VAL THR HIS GLU ASP ILE CYS ASN CYS PHE ASN GLY ASP          
SEQRES   6 B  112  THR LEU LEU ALA ILE GLN ALA PRO SER GLY THR GLN LEU          
SEQRES   7 B  112  GLU VAL PRO ILE PRO GLU MET GLY GLN ASN GLY GLN LYS          
SEQRES   8 B  112  LYS TYR GLN ILE ASN LEU LYS SER HIS SER GLY PRO ILE          
SEQRES   9 B  112  HIS VAL LEU LEU ILE ASN LYS GLU                              
SEQRES   1 C   41  GLY GLU PHE SER GLY LEU THR PRO ARG SER ALA LEU LEU          
SEQRES   2 C   41  TYR LYS PHE ASN GLY SER PRO SER LYS SER LEU LYS ASP          
SEQRES   3 C   41  ILE ASN ASN MET ILE ARG GLN GLY GLU GLN ARG THR LYS          
SEQRES   4 C   41  LYS ARG                                                      
SEQRES   1 D  155  GLY GLU PHE ALA GLN GLU CYS GLN ASN LEU GLU VAL GLU          
SEQRES   2 D  155  ARG GLN ARG ARG LEU GLU ARG ILE LYS GLN LYS GLN SER          
SEQRES   3 D  155  GLN LEU GLN GLU LEU ILE LEU GLN GLN ILE ALA PHE LYS          
SEQRES   4 D  155  ASN LEU VAL GLN ARG ASN ARG HIS ALA GLU GLN GLN ALA          
SEQRES   5 D  155  SER ARG PRO PRO PRO PRO ASN SER VAL ILE HIS LEU PRO          
SEQRES   6 D  155  PHE ILE ILE VAL ASN THR SER LYS LYS THR VAL ILE ASP          
SEQRES   7 D  155  CYS SER ILE SER ASN ASP LYS PHE GLU TYR LEU PHE ASN          
SEQRES   8 D  155  PHE ASP ASN THR PHE GLU ILE HIS ASP ASP ILE GLU VAL          
SEQRES   9 D  155  LEU LYS ARG MET GLY MET ALA CYS GLY LEU GLU SER GLY          
SEQRES  10 D  155  SER CYS SER ALA GLU ASP LEU LYS MET ALA ARG SER LEU          
SEQRES  11 D  155  VAL PRO LYS ALA LEU GLU PRO TYR VAL THR GLU MET ALA          
SEQRES  12 D  155  GLN GLY THR VAL GLY GLY VAL PHE ILE THR THR ALA              
SEQRES   1 E  112  GLY HIS MET LYS GLU VAL ILE ASP ARG LEU ARG TYR LEU          
SEQRES   2 E  112  LYS ALA GLU ILE GLU ASP LEU GLU LEU LYS GLU ARG GLU          
SEQRES   3 E  112  LEU ASP GLN GLN LYS LEU TRP LEU GLN GLN SER ILE LYS          
SEQRES   4 E  112  ASN VAL MET ASP ASP SER ILE ASN ASN ARG PHE SER TYR          
SEQRES   5 E  112  VAL THR HIS GLU ASP ILE CYS ASN CYS PHE ASN GLY ASP          
SEQRES   6 E  112  THR LEU LEU ALA ILE GLN ALA PRO SER GLY THR GLN LEU          
SEQRES   7 E  112  GLU VAL PRO ILE PRO GLU MET GLY GLN ASN GLY GLN LYS          
SEQRES   8 E  112  LYS TYR GLN ILE ASN LEU LYS SER HIS SER GLY PRO ILE          
SEQRES   9 E  112  HIS VAL LEU LEU ILE ASN LYS GLU                              
SEQRES   1 F   41  GLY GLU PHE SER GLY LEU THR PRO ARG SER ALA LEU LEU          
SEQRES   2 F   41  TYR LYS PHE ASN GLY SER PRO SER LYS SER LEU LYS ASP          
SEQRES   3 F   41  ILE ASN ASN MET ILE ARG GLN GLY GLU GLN ARG THR LYS          
SEQRES   4 F   41  LYS ARG                                                      
HELIX    1 AA1 ALA A  199  GLN A  245  1                                  47    
HELIX    2 AA2 ASP A  296  MET A  303  1                                   8    
HELIX    3 AA3 VAL B  126  ASP B  163  1                                  38    
HELIX    4 AA4 ASP B  164  PHE B  170  1                                   7    
HELIX    5 AA5 THR B  174  PHE B  182  1                                   9    
HELIX    6 AA6 PRO C 1010  GLY C 1024  1                                  15    
HELIX    7 AA7 ARG D  209  GLU D  244  1                                  36    
HELIX    8 AA8 ASP D  296  ARG D  302  1                                   7    
HELIX    9 AA9 ASP E  128  LYS E  134  1                                   7    
HELIX   10 AB1 ALA E  135  MET E  162  1                                  28    
HELIX   11 AB2 ASP E  164  PHE E  170  1                                   7    
HELIX   12 AB3 HIS E  175  CYS E  181  1                                   7    
HELIX   13 AB4 SER F 1011  GLN F 1023  1                                  13    
SHEET    1 AA1 2 ILE A 257  HIS A 258  0                                        
SHEET    2 AA1 2 TYR B 172  VAL B 173 -1  O  VAL B 173   N  ILE A 257           
SHEET    1 AA2 9 GLU A 292  ASP A 295  0                                        
SHEET    2 AA2 9 PHE A 261  THR A 266 -1  N  ASN A 265   O  GLU A 292           
SHEET    3 AA2 9 THR B 186  GLN B 191 -1  O  LEU B 188   N  VAL A 264           
SHEET    4 AA2 9 ILE B 224  ILE B 229 -1  O  HIS B 225   N  GLN B 191           
SHEET    5 AA2 9 ILE D 272  ILE D 276 -1  O  CYS D 274   N  VAL B 226           
SHEET    6 AA2 9 GLU D 282  PHE D 287 -1  O  ASN D 286   N  ASP D 273           
SHEET    7 AA2 9 TYR E 213  LYS E 218 -1  O  TYR E 213   N  PHE D 287           
SHEET    8 AA2 9 GLN E 197  VAL E 200 -1  N  GLN E 197   O  LYS E 218           
SHEET    9 AA2 9 LEU F1002  LYS F1005 -1  O  TYR F1004   N  LEU E 198           
SHEET    1 AA3 9 ALA C1001  LYS C1005  0                                        
SHEET    2 AA3 9 GLN B 197  PRO B 201 -1  N  LEU B 198   O  TYR C1004           
SHEET    3 AA3 9 TYR B 213  LYS B 218 -1  O  ASN B 216   N  GLU B 199           
SHEET    4 AA3 9 TYR A 283  PHE A 287 -1  N  TYR A 283   O  LEU B 217           
SHEET    5 AA3 9 ILE A 272  ILE A 276 -1  N  SER A 275   O  LEU A 284           
SHEET    6 AA3 9 ILE E 224  ASN E 230 -1  O  LEU E 228   N  ILE A 272           
SHEET    7 AA3 9 THR E 186  GLN E 191 -1  N  ALA E 189   O  LEU E 227           
SHEET    8 AA3 9 ILE D 262  THR D 266 -1  N  THR D 266   O  THR E 186           
SHEET    9 AA3 9 PHE D 291  ASP D 295 -1  O  HIS D 294   N  ILE D 263           
SHEET    1 AA4 2 VAL D 256  HIS D 258  0                                        
SHEET    2 AA4 2 TYR E 172  THR E 174 -1  O  VAL E 173   N  ILE D 257           
CISPEP   1 LEU A  259    PRO A  260          0        -0.38                     
CISPEP   2 LEU D  259    PRO D  260          0        -2.12                     
CRYST1   60.980   57.340   99.198  90.00  96.64  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016399  0.000000  0.001909        0.00000                         
SCALE2      0.000000  0.017440  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010149        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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