GenomeNet

Database: PDB
Entry: 5FDR
LinkDB: 5FDR
Original site: 5FDR 
HEADER    APOPTOSIS/APOPTOSIS INHIBITOR           16-DEC-15   5FDR              
TITLE     MCL-1 COMPLEXED WITH SMALL MOLECULE INHIBITOR                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INDUCED MYELOID LEUKEMIA CELL DIFFERENTIATION PROTEIN MCL- 
COMPND   3 1;                                                                   
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 SYNONYM: BCL-2-LIKE PROTEIN 3,BCL2-L-3,BCL-2-RELATED PROTEIN         
COMPND   6 EAT/MCL1,MCL1/EAT;                                                   
COMPND   7 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: MCL1, BCL2L3;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    MCL-1, INHIBITOR, APOPTOSIS-APOPTOSIS INHIBITOR COMPLEX               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.ZHAO                                                                
REVDAT   4   04-DEC-19 5FDR    1       REMARK                                   
REVDAT   3   20-SEP-17 5FDR    1       JRNL   REMARK                            
REVDAT   2   23-MAR-16 5FDR    1       JRNL                                     
REVDAT   1   02-MAR-16 5FDR    0                                                
JRNL        AUTH   N.F.PELZ,Z.BIAN,B.ZHAO,S.SHAW,J.C.TARR,J.BELMAR,C.GREGG,     
JRNL        AUTH 2 D.V.CAMPER,C.M.GOODWIN,A.L.ARNOLD,J.L.SENSINTAFFAR,          
JRNL        AUTH 3 A.FRIBERG,O.W.ROSSANESE,T.LEE,E.T.OLEJNICZAK,S.W.FESIK       
JRNL        TITL   DISCOVERY OF 2-INDOLE-ACYLSULFONAMIDE MYELOID CELL LEUKEMIA  
JRNL        TITL 2 1 (MCL-1) INHIBITORS USING FRAGMENT-BASED METHODS.           
JRNL        REF    J.MED.CHEM.                   V.  59  2054 2016              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   26878343                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.5B01660                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.75                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.490                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 22089                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.880                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1079                            
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 28.7530 -  5.1911    0.98     2747   158  0.2355 0.2899        
REMARK   3     2  5.1911 -  4.1242    0.98     2735   139  0.2100 0.2491        
REMARK   3     3  4.1242 -  3.6040    0.99     2719   152  0.2061 0.2676        
REMARK   3     4  3.6040 -  3.2750    0.98     2669   144  0.2228 0.2915        
REMARK   3     5  3.2750 -  3.0405    0.95     2644   133  0.2299 0.2987        
REMARK   3     6  3.0405 -  2.8615    0.92     2524   123  0.2432 0.3269        
REMARK   3     7  2.8615 -  2.7183    0.91     2527   109  0.2413 0.3027        
REMARK   3     8  2.7183 -  2.6000    0.88     2445   121  0.2272 0.3141        
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)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.120           
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      :  0.010           5027                                  
REMARK   3   ANGLE     :  1.326           6791                                  
REMARK   3   CHIRALITY :  0.070            729                                  
REMARK   3   PLANARITY :  0.009            857                                  
REMARK   3   DIHEDRAL  : 19.742           3009                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 17                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 171 THROUGH 235 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  35.5063   3.6874   5.0344              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2610 T22:   0.2361                                     
REMARK   3      T33:   0.2239 T12:   0.0268                                     
REMARK   3      T13:  -0.1508 T23:  -0.0596                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3953 L22:   3.9194                                     
REMARK   3      L33:   2.3393 L12:  -0.3004                                     
REMARK   3      L13:  -1.2634 L23:  -0.2063                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2079 S12:   0.4874 S13:  -0.2058                       
REMARK   3      S21:  -0.3739 S22:  -0.0814 S23:  -0.1273                       
REMARK   3      S31:  -0.2234 S32:  -0.2318 S33:  -0.2608                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 236 THROUGH 260 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  39.6233  11.3093  19.2484              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4774 T22:   0.1709                                     
REMARK   3      T33:   0.2519 T12:   0.0227                                     
REMARK   3      T13:  -0.0701 T23:  -0.0174                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3397 L22:   0.1843                                     
REMARK   3      L33:   2.5110 L12:   0.1706                                     
REMARK   3      L13:  -1.2504 L23:   0.1359                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2157 S12:  -0.2678 S13:   0.6928                       
REMARK   3      S21:  -0.3370 S22:   0.1878 S23:  -0.2402                       
REMARK   3      S31:  -0.4524 S32:   0.4802 S33:   0.2077                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 261 THROUGH 325 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  40.0040   3.5408   8.4730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2156 T22:   0.1858                                     
REMARK   3      T33:   0.1000 T12:  -0.0577                                     
REMARK   3      T13:  -0.0356 T23:   0.0325                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1204 L22:   3.4579                                     
REMARK   3      L33:   1.8448 L12:  -0.1836                                     
REMARK   3      L13:  -1.2807 L23:   0.9981                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0732 S12:  -0.0602 S13:  -0.1414                       
REMARK   3      S21:  -0.3340 S22:   0.2292 S23:  -0.0724                       
REMARK   3      S31:  -0.0544 S32:   0.1064 S33:  -0.1058                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 171 THROUGH 191 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.8842 -32.2008   7.6419              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4858 T22:   0.1784                                     
REMARK   3      T33:   0.4834 T12:   0.0322                                     
REMARK   3      T13:  -0.0051 T23:  -0.1008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5893 L22:   3.1631                                     
REMARK   3      L33:   4.5911 L12:  -2.2389                                     
REMARK   3      L13:   0.9344 L23:  -0.9627                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4995 S12:   0.1297 S13:  -0.7549                       
REMARK   3      S21:   0.1481 S22:   0.0089 S23:  -0.2920                       
REMARK   3      S31:   1.1661 S32:   0.1327 S33:  -0.2674                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 192 THROUGH 223 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  34.6495 -28.2816   1.7751              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3953 T22:   0.0489                                     
REMARK   3      T33:   0.5290 T12:  -0.0093                                     
REMARK   3      T13:   0.0257 T23:  -0.2750                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1191 L22:   2.4226                                     
REMARK   3      L33:   2.6130 L12:  -0.3188                                     
REMARK   3      L13:   0.1163 L23:   1.0576                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0700 S12:   0.2010 S13:  -0.1120                       
REMARK   3      S21:  -0.0525 S22:  -0.0514 S23:  -0.4193                       
REMARK   3      S31:   0.2919 S32:   0.6816 S33:  -0.3349                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 224 THROUGH 254 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  29.7374 -19.9866  22.1007              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1776 T22:   0.1908                                     
REMARK   3      T33:   0.3426 T12:   0.0106                                     
REMARK   3      T13:  -0.0075 T23:   0.0318                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5215 L22:   4.5162                                     
REMARK   3      L33:   6.7120 L12:   0.8319                                     
REMARK   3      L13:  -0.3749 L23:  -0.7309                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1485 S12:  -0.5399 S13:  -0.1321                       
REMARK   3      S21:   0.3186 S22:  -0.5603 S23:  -0.3416                       
REMARK   3      S31:  -0.3808 S32:   0.0742 S33:   0.2354                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 255 THROUGH 321 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  26.8768 -23.3285   9.0144              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2818 T22:   0.1419                                     
REMARK   3      T33:   0.4717 T12:   0.0497                                     
REMARK   3      T13:   0.0172 T23:  -0.0757                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3311 L22:   3.6516                                     
REMARK   3      L33:   4.6876 L12:   0.3820                                     
REMARK   3      L13:   1.0279 L23:   0.1815                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1464 S12:   0.0302 S13:   0.1559                       
REMARK   3      S21:   0.1799 S22:  -0.0912 S23:   0.4581                       
REMARK   3      S31:   0.0065 S32:  -0.3139 S33:   0.2009                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 172 THROUGH 203 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  21.2399 -11.2852  46.4263              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4153 T22:   0.2387                                     
REMARK   3      T33:   0.2003 T12:  -0.0225                                     
REMARK   3      T13:   0.0173 T23:   0.0672                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5438 L22:   5.7967                                     
REMARK   3      L33:   5.9723 L12:  -0.1181                                     
REMARK   3      L13:   0.7993 L23:  -0.5282                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0477 S12:  -1.2424 S13:  -0.2179                       
REMARK   3      S21:   0.7528 S22:   0.0023 S23:   0.4498                       
REMARK   3      S31:  -0.0053 S32:   0.1950 S33:  -0.0337                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 204 THROUGH 239 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9075  -4.9765  36.8288              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1969 T22:   0.2052                                     
REMARK   3      T33:   0.3400 T12:   0.0250                                     
REMARK   3      T13:   0.1011 T23:  -0.0608                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9029 L22:   2.5481                                     
REMARK   3      L33:   2.5689 L12:   0.7396                                     
REMARK   3      L13:   1.7063 L23:  -0.1246                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0776 S12:  -0.0837 S13:   0.4220                       
REMARK   3      S21:   0.1917 S22:  -0.2269 S23:   0.4846                       
REMARK   3      S31:  -0.0675 S32:  -0.2912 S33:   0.2856                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 240 THROUGH 260 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  24.1281 -13.2620  28.9909              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3841 T22:   0.2903                                     
REMARK   3      T33:   0.2113 T12:   0.0110                                     
REMARK   3      T13:   0.1771 T23:  -0.0573                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6322 L22:   1.7904                                     
REMARK   3      L33:   2.9166 L12:  -1.2209                                     
REMARK   3      L13:   0.7340 L23:   0.3899                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0932 S12:   0.4298 S13:  -0.2599                       
REMARK   3      S21:  -0.7395 S22:   0.6096 S23:  -0.0444                       
REMARK   3      S31:   0.2516 S32:   0.0774 S33:  -0.2892                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 261 THROUGH 283 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.7335  -9.8246  35.9616              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3206 T22:   0.2356                                     
REMARK   3      T33:  -0.1240 T12:   0.0291                                     
REMARK   3      T13:   0.0679 T23:  -0.0668                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5642 L22:   2.8063                                     
REMARK   3      L33:   0.9911 L12:   2.1741                                     
REMARK   3      L13:   0.8507 L23:   1.2407                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0588 S12:  -0.2114 S13:  -0.5736                       
REMARK   3      S21:  -0.0197 S22:  -0.3574 S23:   0.1376                       
REMARK   3      S31:  -0.1932 S32:  -0.1579 S33:   0.1859                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 284 THROUGH 308 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  26.8234 -12.2466  38.5153              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2487 T22:   0.2224                                     
REMARK   3      T33:   0.3003 T12:   0.0989                                     
REMARK   3      T13:   0.0603 T23:  -0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3241 L22:   8.1864                                     
REMARK   3      L33:   4.4591 L12:   3.5741                                     
REMARK   3      L13:   2.6470 L23:   2.0821                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2770 S12:  -0.2788 S13:  -0.5709                       
REMARK   3      S21:   0.4854 S22:   0.4548 S23:  -0.6806                       
REMARK   3      S31:   0.3581 S32:   0.3172 S33:  -0.1662                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 309 THROUGH 324 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  25.2773   4.3890  45.8402              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0292 T22:   0.4233                                     
REMARK   3      T33:   0.0466 T12:   0.2280                                     
REMARK   3      T13:   0.1363 T23:  -0.2665                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6100 L22:   5.4104                                     
REMARK   3      L33:   2.2574 L12:  -1.1421                                     
REMARK   3      L13:  -0.6431 L23:   1.2595                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0249 S12:  -0.4484 S13:   0.0799                       
REMARK   3      S21:   0.0974 S22:   0.6783 S23:  -0.5902                       
REMARK   3      S31:  -0.1347 S32:  -0.0448 S33:   0.1071                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 172 THROUGH 202 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  46.1948  30.0116  42.1266              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5101 T22:   0.2256                                     
REMARK   3      T33:   1.1796 T12:   0.1596                                     
REMARK   3      T13:  -0.1588 T23:  -0.3073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1845 L22:   1.8422                                     
REMARK   3      L33:   3.7458 L12:   0.0456                                     
REMARK   3      L13:  -1.4337 L23:  -0.4372                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4377 S12:  -0.4465 S13:   1.4638                       
REMARK   3      S21:   0.6207 S22:  -0.1383 S23:  -0.5164                       
REMARK   3      S31:  -1.1761 S32:  -0.2050 S33:  -0.1715                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 203 THROUGH 235 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  53.1724  18.2001  39.4181              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2934 T22:   0.1508                                     
REMARK   3      T33:   0.4270 T12:   0.0062                                     
REMARK   3      T13:  -0.0105 T23:  -0.0448                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2364 L22:   2.8278                                     
REMARK   3      L33:   0.2567 L12:  -1.4206                                     
REMARK   3      L13:  -0.2659 L23:   0.2300                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3519 S12:  -0.0301 S13:   0.8107                       
REMARK   3      S21:   0.1567 S22:   0.1259 S23:  -0.5704                       
REMARK   3      S31:  -0.1200 S32:   0.2945 S33:   0.0643                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 236 THROUGH 254 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  42.9056  19.5096  25.3029              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2960 T22:   0.3767                                     
REMARK   3      T33:   0.4003 T12:   0.0381                                     
REMARK   3      T13:  -0.0554 T23:  -0.0274                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2603 L22:   4.7427                                     
REMARK   3      L33:   7.2056 L12:  -0.8852                                     
REMARK   3      L13:  -0.2941 L23:  -2.1145                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1183 S12:   1.0258 S13:   0.7048                       
REMARK   3      S21:  -0.7707 S22:  -0.3872 S23:  -0.2359                       
REMARK   3      S31:   0.1925 S32:  -0.5001 S33:   0.2252                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 255 THROUGH 321 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  44.0325  19.9783  39.4338              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2412 T22:   0.1754                                     
REMARK   3      T33:   0.3604 T12:   0.0059                                     
REMARK   3      T13:   0.0057 T23:  -0.1357                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1132 L22:   3.2713                                     
REMARK   3      L33:   6.0415 L12:  -0.9058                                     
REMARK   3      L13:  -0.1770 L23:  -0.2284                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2483 S12:  -0.3663 S13:   0.6889                       
REMARK   3      S21:  -0.0795 S22:   0.0343 S23:  -0.0505                       
REMARK   3      S31:  -0.3596 S32:  -0.4782 S33:   0.2627                       
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 5FDR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000216426.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.987                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22089                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : 0.11000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4HW2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, BIS-TRIS, MAGNESIUM            
REMARK 280  CHLORIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K           
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       57.50250            
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, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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   170                                                      
REMARK 465     GLY A   326                                                      
REMARK 465     GLY A   327                                                      
REMARK 465     GLY B   170                                                      
REMARK 465     LYS B   197                                                      
REMARK 465     PRO B   198                                                      
REMARK 465     GLU B   322                                                      
REMARK 465     ASP B   323                                                      
REMARK 465     LEU B   324                                                      
REMARK 465     GLU B   325                                                      
REMARK 465     GLY B   326                                                      
REMARK 465     GLY B   327                                                      
REMARK 465     GLY C   170                                                      
REMARK 465     ASP C   171                                                      
REMARK 465     ALA C   193                                                      
REMARK 465     LYS C   194                                                      
REMARK 465     ASP C   195                                                      
REMARK 465     THR C   196                                                      
REMARK 465     LYS C   197                                                      
REMARK 465     PRO C   198                                                      
REMARK 465     MET C   199                                                      
REMARK 465     GLY C   200                                                      
REMARK 465     ARG C   201                                                      
REMARK 465     SER C   202                                                      
REMARK 465     GLU C   325                                                      
REMARK 465     GLY C   326                                                      
REMARK 465     GLY C   327                                                      
REMARK 465     GLY D   170                                                      
REMARK 465     ASP D   171                                                      
REMARK 465     LYS D   197                                                      
REMARK 465     PRO D   198                                                      
REMARK 465     GLU D   322                                                      
REMARK 465     ASP D   323                                                      
REMARK 465     LEU D   324                                                      
REMARK 465     GLU D   325                                                      
REMARK 465     GLY D   326                                                      
REMARK 465     GLY D   327                                                      
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     ASP A 195    CG   OD1  OD2                                       
REMARK 470     LYS A 197    CG   CD   CE   NZ                                   
REMARK 470     ARG A 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 325    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 194    CG   CD   CE   NZ                                   
REMARK 470     ASP B 195    CG   OD1  OD2                                       
REMARK 470     THR B 196    OG1  CG2                                            
REMARK 470     SER B 202    OG                                                  
REMARK 470     VAL B 321    CG1  CG2                                            
REMARK 470     LYS D 194    CG   CD   CE   NZ                                   
REMARK 470     ASP D 195    CG   OD1  OD2                                       
REMARK 470     THR D 196    OG1  CG2                                            
REMARK 470     VAL D 321    CG1  CG2                                            
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    LEU A   179     OG   SER A   183              2.06            
REMARK 500   NH2  ARG A   310     OE2  GLU A   317              2.10            
REMARK 500   O    LEU A   235     NH1  ARG D   248              2.13            
REMARK 500   NH2  ARG A   176     O    ARG A   201              2.14            
REMARK 500   NH1  ARG B   176     OE1  GLU B   180              2.14            
REMARK 500   O    LEU D   179     OG   SER D   183              2.17            
REMARK 500   NH2  ARG B   215     O    PHE B   319              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLU A   292     NH2  ARG B   207     2755     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B 292   CD    GLU B 292   OE1    -0.087                       
REMARK 500    GLU B 292   CD    GLU B 292   OE2    -0.084                       
REMARK 500    VAL C 321   CB    VAL C 321   CG1    -0.131                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG D 201   CD  -  NE  -  CZ  ANGL. DEV. =   8.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 195       70.90    -64.57                                   
REMARK 500    LYS A 197      142.15     81.69                                   
REMARK 500    ARG A 201      130.48     65.10                                   
REMARK 500    ASP A 236       72.60     51.97                                   
REMARK 500    HIS A 320       92.97      0.58                                   
REMARK 500    VAL A 321      100.93    -54.23                                   
REMARK 500    ARG B 201      -90.77     85.53                                   
REMARK 500    ALA B 204      -50.56    118.89                                   
REMARK 500    ASP B 236       72.61     51.55                                   
REMARK 500    GLU B 292      -76.11    -31.86                                   
REMARK 500    ASP C 236       71.72     50.62                                   
REMARK 500    HIS C 320      140.69     -6.46                                   
REMARK 500    THR D 191     -167.01   -108.47                                   
REMARK 500    ALA D 193     -154.64   -161.32                                   
REMARK 500    ARG D 201     -118.48     47.74                                   
REMARK 500    SER D 202       42.09    -94.90                                   
REMARK 500    ASP D 236       76.78     51.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5X3 A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5X3 B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5X3 C 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5X3 D 400                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4HW2   RELATED DB: PDB                                   
REMARK 900 4HW2 CONTAINS THE SAME PROTEIN                                       
DBREF  5FDR A  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  5FDR B  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  5FDR C  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  5FDR D  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
SEQADV 5FDR GLY A  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5FDR ASP A  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5FDR GLY B  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5FDR ASP B  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5FDR GLY C  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5FDR ASP C  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5FDR GLY D  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5FDR ASP D  171  UNP  Q07820              EXPRESSION TAG                 
SEQRES   1 A  158  GLY ASP ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE          
SEQRES   2 A  158  SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP          
SEQRES   3 A  158  THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS          
SEQRES   4 A  158  ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN          
SEQRES   5 A  158  ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS          
SEQRES   6 A  158  LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER          
SEQRES   7 A  158  ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN          
SEQRES   8 A  158  TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE          
SEQRES   9 A  158  VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS          
SEQRES  10 A  158  ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL          
SEQRES  11 A  158  ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP          
SEQRES  12 A  158  ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU          
SEQRES  13 A  158  GLY GLY                                                      
SEQRES   1 B  158  GLY ASP ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE          
SEQRES   2 B  158  SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP          
SEQRES   3 B  158  THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS          
SEQRES   4 B  158  ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN          
SEQRES   5 B  158  ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS          
SEQRES   6 B  158  LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER          
SEQRES   7 B  158  ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN          
SEQRES   8 B  158  TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE          
SEQRES   9 B  158  VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS          
SEQRES  10 B  158  ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL          
SEQRES  11 B  158  ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP          
SEQRES  12 B  158  ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU          
SEQRES  13 B  158  GLY GLY                                                      
SEQRES   1 C  158  GLY ASP ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE          
SEQRES   2 C  158  SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP          
SEQRES   3 C  158  THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS          
SEQRES   4 C  158  ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN          
SEQRES   5 C  158  ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS          
SEQRES   6 C  158  LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER          
SEQRES   7 C  158  ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN          
SEQRES   8 C  158  TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE          
SEQRES   9 C  158  VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS          
SEQRES  10 C  158  ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL          
SEQRES  11 C  158  ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP          
SEQRES  12 C  158  ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU          
SEQRES  13 C  158  GLY GLY                                                      
SEQRES   1 D  158  GLY ASP ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE          
SEQRES   2 D  158  SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP          
SEQRES   3 D  158  THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS          
SEQRES   4 D  158  ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN          
SEQRES   5 D  158  ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS          
SEQRES   6 D  158  LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER          
SEQRES   7 D  158  ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN          
SEQRES   8 D  158  TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE          
SEQRES   9 D  158  VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS          
SEQRES  10 D  158  ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL          
SEQRES  11 D  158  ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP          
SEQRES  12 D  158  ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU          
SEQRES  13 D  158  GLY GLY                                                      
HET    5X3  A 400      44                                                       
HET    5X3  B 400      44                                                       
HET    5X3  C 400      44                                                       
HET    5X3  D 400      44                                                       
HETNAM     5X3 5-[[6-CHLORANYL-3-[3-(4-CHLORANYL-3,5-DIMETHYL-                  
HETNAM   2 5X3  PHENOXY)PROPYL]-7-(3,5-DIMETHYL-1~{H}-PYRAZOL-4-YL)-            
HETNAM   3 5X3  1~{H}-INDOL-2-YL]CARBONYLSULFAMOYL]FURAN-2-CARBOXYLIC           
HETNAM   4 5X3  ACID                                                            
FORMUL   5  5X3    4(C30 H28 CL2 N4 O7 S)                                       
HELIX    1 AA1 GLU A  173  GLY A  192  1                                  20    
HELIX    2 AA2 GLY A  203  HIS A  224  1                                  22    
HELIX    3 AA3 HIS A  224  ASP A  236  1                                  13    
HELIX    4 AA4 ASN A  239  SER A  255  1                                  17    
HELIX    5 AA5 ASN A  260  ILE A  281  1                                  22    
HELIX    6 AA6 GLN A  283  SER A  285  5                                   3    
HELIX    7 AA7 CYS A  286  GLN A  309  1                                  24    
HELIX    8 AA8 ARG A  310  HIS A  320  1                                  11    
HELIX    9 AA9 ASP B  172  GLY B  192  1                                  21    
HELIX   10 AB1 ALA B  204  HIS B  224  1                                  21    
HELIX   11 AB2 HIS B  224  ASP B  236  1                                  13    
HELIX   12 AB3 ASN B  239  SER B  245  1                                   7    
HELIX   13 AB4 LEU B  246  SER B  255  1                                  10    
HELIX   14 AB5 ASN B  260  ILE B  281  1                                  22    
HELIX   15 AB6 GLN B  283  SER B  285  5                                   3    
HELIX   16 AB7 CYS B  286  GLN B  309  1                                  24    
HELIX   17 AB8 ARG B  310  PHE B  319  1                                  10    
HELIX   18 AB9 GLU C  173  THR C  191  1                                  19    
HELIX   19 AC1 ALA C  204  HIS C  224  1                                  21    
HELIX   20 AC2 HIS C  224  ASP C  236  1                                  13    
HELIX   21 AC3 ASN C  239  SER C  255  1                                  17    
HELIX   22 AC4 ASN C  260  ILE C  281  1                                  22    
HELIX   23 AC5 GLN C  283  SER C  285  5                                   3    
HELIX   24 AC6 CYS C  286  GLN C  309  1                                  24    
HELIX   25 AC7 ARG C  310  HIS C  320  1                                  11    
HELIX   26 AC8 GLU D  173  THR D  191  1                                  19    
HELIX   27 AC9 SER D  202  HIS D  224  1                                  23    
HELIX   28 AD1 HIS D  224  ASP D  236  1                                  13    
HELIX   29 AD2 ASN D  239  LEU D  246  1                                   8    
HELIX   30 AD3 LEU D  246  SER D  255  1                                  10    
HELIX   31 AD4 ASN D  260  ILE D  281  1                                  22    
HELIX   32 AD5 GLN D  283  SER D  285  5                                   3    
HELIX   33 AD6 CYS D  286  GLN D  309  1                                  24    
HELIX   34 AD7 ARG D  310  HIS D  320  1                                  11    
CISPEP   1 ARG A  201    SER A  202          0        -3.86                     
SITE     1 AC1 16 HIS A 224  ALA A 227  PHE A 228  MET A 231                    
SITE     2 AC1 16 MET A 250  VAL A 253  ASN A 260  GLY A 262                    
SITE     3 AC1 16 ARG A 263  THR A 266  LEU A 267  PHE A 270                    
SITE     4 AC1 16 GLY A 271  THR B 226  ASP C 256  GLY C 257                    
SITE     1 AC2 14 GLY A 219  ARG A 222  ASN A 223  ALA B 227                    
SITE     2 AC2 14 PHE B 228  MET B 231  VAL B 249  MET B 250                    
SITE     3 AC2 14 VAL B 253  ASP B 256  GLY B 257  ARG B 263                    
SITE     4 AC2 14 LEU B 267  PHE B 270                                          
SITE     1 AC3 15 ASP A 256  GLY A 257  HIS C 224  ALA C 227                    
SITE     2 AC3 15 PHE C 228  MET C 231  MET C 250  VAL C 253                    
SITE     3 AC3 15 ASN C 260  GLY C 262  ARG C 263  THR C 266                    
SITE     4 AC3 15 LEU C 267  PHE C 270  THR D 226                               
SITE     1 AC4 16 GLY C 219  ARG C 222  ASN C 223  ALA D 227                    
SITE     2 AC4 16 PHE D 228  MET D 231  MET D 250  VAL D 253                    
SITE     3 AC4 16 PHE D 254  ASP D 256  GLY D 257  ARG D 263                    
SITE     4 AC4 16 THR D 266  LEU D 267  PHE D 270  ILE D 294                    
CRYST1   35.040  115.005   95.327  90.00  91.17  90.00 P 1 21 1      8          
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      0.028539  0.000000  0.000581        0.00000                         
SCALE2      0.000000  0.008695  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010492        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system