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Database: PDB
Entry: 5FDO
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Original site: 5FDO 
HEADER    APOPTOSIS/APOPTOSIS INHIBITOR           16-DEC-15   5FDO              
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 FRAGMENT: UNP RESIDUES 172-320;                                      
COMPND   6 SYNONYM: BCL-2-LIKE PROTEIN 3,BCL2-L-3,BCL-2-RELATED PROTEIN         
COMPND   7 EAT/MCL1,MCL1/EAT;                                                   
COMPND   8 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 5FDO    1       REMARK                                   
REVDAT   3   20-SEP-17 5FDO    1       JRNL   REMARK                            
REVDAT   2   23-MAR-16 5FDO    1       JRNL                                     
REVDAT   1   02-MAR-16 5FDO    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.    2.80 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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.78                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.500                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 19447                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.291                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.250                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1020                            
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 29.7778 -  5.3474    0.99     2952   131  0.2014 0.2794        
REMARK   3     2  5.3474 -  4.2483    1.00     2777   159  0.1843 0.2492        
REMARK   3     3  4.2483 -  3.7125    0.99     2704   160  0.1924 0.2706        
REMARK   3     4  3.7125 -  3.3735    0.99     2682   156  0.2162 0.3091        
REMARK   3     5  3.3735 -  3.1320    0.98     2653   141  0.2483 0.3337        
REMARK   3     6  3.1320 -  2.9475    0.94     2508   154  0.2780 0.3534        
REMARK   3     7  2.9475 -  2.8000    0.80     2151   119  0.2755 0.3299        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.430            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.340           
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      :  0.012           4811                                  
REMARK   3   ANGLE     :  1.670           6479                                  
REMARK   3   CHIRALITY :  0.096            700                                  
REMARK   3   PLANARITY :  0.011            816                                  
REMARK   3   DIHEDRAL  : 17.508           2813                                  
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 171 THROUGH 190 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.4093  20.7037 -14.8021              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2249 T22:   0.4268                                     
REMARK   3      T33:   0.2655 T12:   0.1056                                     
REMARK   3      T13:   0.0916 T23:   0.0828                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4637 L22:   2.5597                                     
REMARK   3      L33:   6.2852 L12:  -0.2762                                     
REMARK   3      L13:  -7.0757 L23:   1.1764                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1238 S12:   0.8462 S13:  -0.2733                       
REMARK   3      S21:  -0.5189 S22:  -0.3109 S23:   0.2923                       
REMARK   3      S31:  -0.1862 S32:  -1.0477 S33:   0.0979                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 191 THROUGH 223 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5175  28.3382 -21.1478              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5664 T22:   0.3706                                     
REMARK   3      T33:   0.2659 T12:   0.1079                                     
REMARK   3      T13:  -0.1021 T23:   0.0449                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6724 L22:   6.3268                                     
REMARK   3      L33:   2.8237 L12:  -1.6579                                     
REMARK   3      L13:  -0.1181 L23:  -0.0913                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5258 S12:   0.9312 S13:  -0.0138                       
REMARK   3      S21:  -0.9079 S22:  -0.2061 S23:   0.0460                       
REMARK   3      S31:  -0.9032 S32:  -0.5101 S33:  -0.2610                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 224 THROUGH 254 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   9.2580  16.2051  -8.6345              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3264 T22:   0.2479                                     
REMARK   3      T33:   0.6081 T12:  -0.0833                                     
REMARK   3      T13:  -0.1980 T23:  -0.0543                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9584 L22:   4.8250                                     
REMARK   3      L33:   4.8026 L12:  -1.1960                                     
REMARK   3      L13:  -1.4547 L23:  -0.0775                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0825 S12:  -0.3985 S13:  -0.2021                       
REMARK   3      S21:   0.4261 S22:   0.1342 S23:  -0.6126                       
REMARK   3      S31:  -0.2448 S32:   0.6071 S33:  -0.0933                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 255 THROUGH 280 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.0571  23.9713 -11.4753              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1974 T22:  -0.0005                                     
REMARK   3      T33:   0.2946 T12:  -0.0395                                     
REMARK   3      T13:  -0.0240 T23:  -0.0383                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0156 L22:   6.6678                                     
REMARK   3      L33:   2.1596 L12:  -2.2156                                     
REMARK   3      L13:  -1.5977 L23:   2.4060                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1198 S12:  -0.0747 S13:  -0.0062                       
REMARK   3      S21:   0.4825 S22:   0.2170 S23:  -0.4857                       
REMARK   3      S31:  -0.0940 S32:   0.1611 S33:  -0.1687                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 281 THROUGH 301 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.6116  14.5664 -11.2370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2740 T22:   0.0758                                     
REMARK   3      T33:   0.1826 T12:   0.1936                                     
REMARK   3      T13:  -0.0374 T23:  -0.2652                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7072 L22:   5.9667                                     
REMARK   3      L33:   3.4899 L12:  -1.7470                                     
REMARK   3      L13:  -0.9246 L23:   3.9153                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2032 S12:   0.1013 S13:  -0.6362                       
REMARK   3      S21:   0.3447 S22:   0.0252 S23:   0.2080                       
REMARK   3      S31:   0.2623 S32:  -0.2554 S33:   0.5136                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 302 THROUGH 309 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.4226  31.1466  -1.5144              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5027 T22:   0.1483                                     
REMARK   3      T33:   0.3254 T12:   0.2017                                     
REMARK   3      T13:   0.2351 T23:  -0.0241                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8626 L22:   0.4702                                     
REMARK   3      L33:   1.2840 L12:  -0.4413                                     
REMARK   3      L13:  -0.4707 L23:  -0.2728                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1043 S12:  -0.0005 S13:   0.3646                       
REMARK   3      S21:  -0.2030 S22:  -0.1280 S23:  -0.0042                       
REMARK   3      S31:  -0.3513 S32:  -0.1817 S33:  -0.1082                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 310 THROUGH 320 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.0012  35.4481 -12.7598              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7792 T22:   0.2472                                     
REMARK   3      T33:   0.2994 T12:   0.2984                                     
REMARK   3      T13:   0.1537 T23:   0.0902                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2283 L22:   1.9968                                     
REMARK   3      L33:   1.6221 L12:   3.4941                                     
REMARK   3      L13:  -0.8217 L23:   0.5178                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0565 S12:   0.4038 S13:   0.9800                       
REMARK   3      S21:  -0.3509 S22:   0.2023 S23:   0.3042                       
REMARK   3      S31:  -0.6553 S32:  -0.2995 S33:  -0.2286                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 171 THROUGH 205 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.5875  50.8138 -24.1409              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0093 T22:   0.2541                                     
REMARK   3      T33:   0.1590 T12:  -0.2777                                     
REMARK   3      T13:  -0.0255 T23:   0.2132                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2293 L22:   2.4790                                     
REMARK   3      L33:   0.8907 L12:  -0.1733                                     
REMARK   3      L13:  -0.0009 L23:  -0.7792                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0326 S12:   0.6321 S13:   0.4833                       
REMARK   3      S21:  -0.4706 S22:  -0.0374 S23:   0.1321                       
REMARK   3      S31:  -0.1267 S32:   0.1185 S33:  -0.0696                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 206 THROUGH 239 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.3914  43.8407 -12.7565              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8129 T22:   0.2837                                     
REMARK   3      T33:   0.5226 T12:  -0.1694                                     
REMARK   3      T13:   0.0868 T23:  -0.0551                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2713 L22:   4.5952                                     
REMARK   3      L33:   2.2423 L12:   0.3903                                     
REMARK   3      L13:  -0.4127 L23:   1.6848                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2504 S12:   0.0602 S13:   0.0024                       
REMARK   3      S21:   0.7351 S22:  -0.2273 S23:   0.4660                       
REMARK   3      S31:   0.0229 S32:  -0.2887 S33:   0.3719                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 240 THROUGH 254 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.7813  46.7530  -4.5094              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0758 T22:   0.5407                                     
REMARK   3      T33:   0.3488 T12:  -0.3438                                     
REMARK   3      T13:   0.0824 T23:  -0.1033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9137 L22:   1.0342                                     
REMARK   3      L33:   4.4908 L12:   1.2104                                     
REMARK   3      L13:   2.4245 L23:   1.7864                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1368 S12:  -0.6138 S13:   0.4087                       
REMARK   3      S21:   0.6001 S22:  -0.1093 S23:   0.0022                       
REMARK   3      S31:   0.4417 S32:   0.1308 S33:  -0.0334                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 255 THROUGH 260 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.7128  31.0952 -12.2471              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6970 T22:   0.3098                                     
REMARK   3      T33:   0.6953 T12:  -0.0156                                     
REMARK   3      T13:  -0.0831 T23:  -0.1157                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6830 L22:   6.7989                                     
REMARK   3      L33:   6.8734 L12:   2.1766                                     
REMARK   3      L13:  -6.0950 L23:  -3.0357                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2277 S12:  -1.2651 S13:   0.6686                       
REMARK   3      S21:   2.1289 S22:  -0.3718 S23:  -0.5483                       
REMARK   3      S31:  -1.3458 S32:  -0.0327 S33:   0.0904                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 261 THROUGH 320 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.3566  43.7041 -16.7994              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6832 T22:   0.2828                                     
REMARK   3      T33:   0.1416 T12:  -0.2689                                     
REMARK   3      T13:  -0.0600 T23:   0.0260                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9823 L22:   2.8745                                     
REMARK   3      L33:   2.6642 L12:   0.0990                                     
REMARK   3      L13:  -0.1385 L23:   1.4707                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1001 S12:   0.3029 S13:   0.0009                       
REMARK   3      S21:   0.0087 S22:  -0.0060 S23:   0.1318                       
REMARK   3      S31:  -0.5298 S32:   0.1985 S33:  -0.0151                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 171 THROUGH 189 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -20.0182  58.9966  -7.4111              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5472 T22:   0.3369                                     
REMARK   3      T33:   0.4473 T12:   0.4167                                     
REMARK   3      T13:  -0.0295 T23:  -0.0324                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3905 L22:   1.5012                                     
REMARK   3      L33:   1.4512 L12:  -0.0639                                     
REMARK   3      L13:  -0.1541 L23:   0.1594                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0467 S12:   0.0081 S13:   0.1239                       
REMARK   3      S21:  -0.1467 S22:   0.1079 S23:  -0.4825                       
REMARK   3      S31:  -0.5045 S32:  -0.0375 S33:  -0.0485                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 190 THROUGH 203 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.4206  67.0071 -12.9449              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9134 T22:   0.3699                                     
REMARK   3      T33:   0.9303 T12:   0.0232                                     
REMARK   3      T13:   0.1747 T23:  -0.1300                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3678 L22:   5.9566                                     
REMARK   3      L33:   7.0674 L12:   3.6039                                     
REMARK   3      L13:  -0.1539 L23:   4.4625                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1999 S12:   0.1174 S13:   1.1146                       
REMARK   3      S21:  -1.6579 S22:   0.5214 S23:   0.5351                       
REMARK   3      S31:  -2.3193 S32:  -0.5413 S33:  -0.4958                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 204 THROUGH 254 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.0833  61.6165 -17.6128              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2886 T22:   0.7882                                     
REMARK   3      T33:   0.6713 T12:   0.6629                                     
REMARK   3      T13:  -0.1808 T23:   0.0682                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9217 L22:   2.0374                                     
REMARK   3      L33:   0.9237 L12:  -1.0761                                     
REMARK   3      L13:   0.2033 L23:  -0.1808                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3182 S12:   0.5090 S13:   0.3982                       
REMARK   3      S21:  -0.3678 S22:  -0.1306 S23:   0.3334                       
REMARK   3      S31:  -0.9246 S32:  -0.2081 S33:   0.0596                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 255 THROUGH 320 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -26.3854  56.0656 -13.1408              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5699 T22:   0.3181                                     
REMARK   3      T33:   0.4918 T12:   0.5663                                     
REMARK   3      T13:  -0.1760 T23:  -0.2175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3529 L22:   2.6489                                     
REMARK   3      L33:   0.8650 L12:  -1.3125                                     
REMARK   3      L13:  -0.0585 L23:  -0.1267                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1442 S12:   0.0332 S13:   0.5357                       
REMARK   3      S21:  -0.2786 S22:  -0.1139 S23:  -0.2146                       
REMARK   3      S31:  -0.4964 S32:  -0.1263 S33:  -0.1448                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 171 THROUGH 190 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   9.9764  62.1015  14.4115              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3393 T22:   0.4019                                     
REMARK   3      T33:   0.6931 T12:  -0.1772                                     
REMARK   3      T13:  -0.0447 T23:   0.1305                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7357 L22:   7.9631                                     
REMARK   3      L33:   1.3947 L12:  -1.6386                                     
REMARK   3      L13:   0.4868 L23:  -3.3023                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0523 S12:   0.2558 S13:   0.1169                       
REMARK   3      S21:  -1.1893 S22:  -0.1476 S23:   0.5785                       
REMARK   3      S31:  -1.0177 S32:  -0.1530 S33:   0.0771                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 191 THROUGH 260 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  17.7630  72.4429  16.3735              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3356 T22:   0.6913                                     
REMARK   3      T33:   0.9697 T12:  -0.3557                                     
REMARK   3      T13:  -0.0873 T23:   0.1658                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5839 L22:   4.6137                                     
REMARK   3      L33:   4.3525 L12:   0.1349                                     
REMARK   3      L13:   0.4972 L23:  -3.1617                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6580 S12:   0.4876 S13:   0.7161                       
REMARK   3      S21:  -0.5206 S22:   0.4997 S23:   0.8352                       
REMARK   3      S31:  -1.5784 S32:  -0.1021 S33:  -0.0066                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 261 THROUGH 310 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  17.1956  66.7306  16.1919              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3436 T22:   0.5958                                     
REMARK   3      T33:   0.6016 T12:  -0.4695                                     
REMARK   3      T13:  -0.0642 T23:   0.0344                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4300 L22:   2.4766                                     
REMARK   3      L33:   2.8390 L12:  -0.1760                                     
REMARK   3      L13:  -0.7161 L23:  -0.8853                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3330 S12:   0.3636 S13:   0.9174                       
REMARK   3      S21:  -0.8505 S22:   0.3046 S23:   0.4070                       
REMARK   3      S31:  -0.8034 S32:   0.0147 S33:   0.0355                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 311 THROUGH 320 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.6976  64.1870  28.8365              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9837 T22:   0.8524                                     
REMARK   3      T33:   0.6961 T12:  -0.2214                                     
REMARK   3      T13:   0.0911 T23:  -0.0459                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7757 L22:   8.7130                                     
REMARK   3      L33:   6.1204 L12:  -3.0497                                     
REMARK   3      L13:  -0.3534 L23:   6.0469                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4724 S12:  -0.0356 S13:   0.1544                       
REMARK   3      S21:  -0.1926 S22:   0.4181 S23:   0.7585                       
REMARK   3      S31:  -0.0416 S32:  -0.6542 S33:   0.0922                       
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 5FDO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000216380.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0 - 8.5                          
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-D                            
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 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19447                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : 0.09000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
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   (%): 59.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01                     
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 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       60.69050            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       60.69050            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       60.69050            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       60.69050            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       60.69050            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       60.69050            
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     ASP A   195                                                      
REMARK 465     THR A   196                                                      
REMARK 465     LYS A   197                                                      
REMARK 465     PRO A   198                                                      
REMARK 465     MET A   199                                                      
REMARK 465     GLY A   200                                                      
REMARK 465     ARG A   201                                                      
REMARK 465     SER A   202                                                      
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     GLY D   192                                                      
REMARK 465     ALA D   193                                                      
REMARK 465     LYS D   194                                                      
REMARK 465     ASP D   195                                                      
REMARK 465     THR D   196                                                      
REMARK 465     LYS D   197                                                      
REMARK 465     PRO D   198                                                      
REMARK 465     MET D   199                                                      
REMARK 465     GLY D   200                                                      
REMARK 465     ARG D   201                                                      
REMARK 465     SER D   202                                                      
REMARK 465     ASP D   256                                                      
REMARK 465     GLY D   257                                                      
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     LYS B 194    CG   CD   CE   NZ                                   
REMARK 470     THR B 196    OG1  CG2                                            
REMARK 470     LYS B 197    CG   CD   CE   NZ                                   
REMARK 470     PRO B 198    CG   CD                                             
REMARK 470     ARG B 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 194    CG   CD   CE   NZ                                   
REMARK 470     ASP C 195    CG   OD1  OD2                                       
REMARK 470     VAL D 258    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    ASP D   242     OG   SER D   245              2.12            
REMARK 500   NH2  ARG B   263     O28  5X2 B   400              2.12            
REMARK 500   O    ALA D   190     NZ   LYS D   279              2.13            
REMARK 500   NH2  ARG C   310     OE1  GLU C   317              2.13            
REMARK 500   O    GLY C   203     NH2  ARG C   207              2.14            
REMARK 500   O    VAL B   265     OG   SER B   269              2.16            
REMARK 500   NH2  ARG A   310     OE2  GLU A   317              2.17            
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 B   292     NZ   LYS C   238     2665     2.18            
REMARK 500   OG   SER A   245     NH1  ARG A   248     7555     2.19            
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    LYS C 279   CD    LYS C 279   CE     -0.168                       
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    PRO B 198   N   -  CA  -  CB  ANGL. DEV. =   7.8 DEGREES          
REMARK 500    LEU B 306   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    LEU D 210   CA  -  CB  -  CG  ANGL. DEV. =  20.1 DEGREES          
REMARK 500    GLU D 317   CA  -  CB  -  CG  ANGL. DEV. =  15.5 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    THR A 191       41.58    -97.12                                   
REMARK 500    ALA A 193      166.10    175.34                                   
REMARK 500    ASP A 236       79.91     54.87                                   
REMARK 500    ASN A 239     -158.29   -124.80                                   
REMARK 500    LEU A 246      -18.34    -48.59                                   
REMARK 500    VAL A 258       80.59    -60.94                                   
REMARK 500    PHE A 319       36.51    -99.15                                   
REMARK 500    ALA B 193       23.76     44.68                                   
REMARK 500    ASP B 195      -76.50   -117.71                                   
REMARK 500    LYS B 197     -135.20   -100.41                                   
REMARK 500    PRO B 198       82.95   -176.13                                   
REMARK 500    SER B 202       80.21     44.46                                   
REMARK 500    ASP B 236       76.53     52.94                                   
REMARK 500    ASN B 239     -152.29   -117.52                                   
REMARK 500    ASP B 256      -39.98   -137.76                                   
REMARK 500    LYS C 194       91.31   -179.87                                   
REMARK 500    ASN C 239     -154.54   -126.13                                   
REMARK 500    ASP C 256       49.18    -88.32                                   
REMARK 500    ASP D 236       79.37     51.46                                   
REMARK 500    ASN D 239     -156.39   -123.92                                   
REMARK 500    SER D 285      -17.13    -48.95                                   
REMARK 500    PHE D 319       41.71   -105.26                                   
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 5X2 A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5X2 B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5X2 C 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5X2 D 400                 
DBREF  5FDO A  172   320  UNP    Q07820   MCL1_HUMAN     172    320             
DBREF  5FDO B  172   320  UNP    Q07820   MCL1_HUMAN     172    320             
DBREF  5FDO C  172   320  UNP    Q07820   MCL1_HUMAN     172    320             
DBREF  5FDO D  172   320  UNP    Q07820   MCL1_HUMAN     172    320             
SEQADV 5FDO GLY A  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5FDO GLY B  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5FDO GLY C  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5FDO GLY D  171  UNP  Q07820              EXPRESSION TAG                 
SEQRES   1 A  150  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 A  150  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 A  150  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 A  150  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 A  150  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 A  150  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 A  150  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 A  150  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 A  150  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 A  150  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 A  150  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 A  150  GLY PHE VAL GLU PHE PHE HIS                                  
SEQRES   1 B  150  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 B  150  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 B  150  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 B  150  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 B  150  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 B  150  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 B  150  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 B  150  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 B  150  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 B  150  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 B  150  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 B  150  GLY PHE VAL GLU PHE PHE HIS                                  
SEQRES   1 C  150  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 C  150  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 C  150  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 C  150  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 C  150  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 C  150  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 C  150  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 C  150  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 C  150  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 C  150  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 C  150  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 C  150  GLY PHE VAL GLU PHE PHE HIS                                  
SEQRES   1 D  150  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 D  150  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 D  150  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 D  150  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 D  150  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 D  150  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 D  150  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 D  150  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 D  150  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 D  150  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 D  150  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 D  150  GLY PHE VAL GLU PHE PHE HIS                                  
HET    5X2  A 400      34                                                       
HET    5X2  B 400      34                                                       
HET    5X2  C 400      34                                                       
HET    5X2  D 400      34                                                       
HETNAM     5X2 3-[3-(4-CHLORANYL-3,5-DIMETHYL-PHENOXY)PROPYL]-~{N}-             
HETNAM   2 5X2  (PHENYLSULFONYL)-1~{H}-INDOLE-2-CARBOXAMIDE                     
FORMUL   5  5X2    4(C26 H25 CL N2 O4 S)                                        
HELIX    1 AA1 ASP A  172  THR A  191  1                                  20    
HELIX    2 AA2 ALA A  204  HIS A  224  1                                  21    
HELIX    3 AA3 HIS A  224  ASP A  236  1                                  13    
HELIX    4 AA4 ASN A  239  LEU A  246  1                                   8    
HELIX    5 AA5 LEU A  246  SER A  255  1                                  10    
HELIX    6 AA6 ASN A  260  ILE A  281  1                                  22    
HELIX    7 AA7 GLN A  283  SER A  285  5                                   3    
HELIX    8 AA8 CYS A  286  LYS A  302  1                                  17    
HELIX    9 AA9 LYS A  302  GLN A  309  1                                   8    
HELIX   10 AB1 ARG A  310  PHE A  319  1                                  10    
HELIX   11 AB2 ASP B  172  GLY B  192  1                                  21    
HELIX   12 AB3 GLY B  203  HIS B  224  1                                  22    
HELIX   13 AB4 HIS B  224  ASP B  236  1                                  13    
HELIX   14 AB5 ASN B  239  LEU B  246  1                                   8    
HELIX   15 AB6 LEU B  246  SER B  255  1                                  10    
HELIX   16 AB7 ASN B  260  ILE B  281  1                                  22    
HELIX   17 AB8 GLN B  283  SER B  285  5                                   3    
HELIX   18 AB9 CYS B  286  LYS B  302  1                                  17    
HELIX   19 AC1 LYS B  302  GLN B  309  1                                   8    
HELIX   20 AC2 ARG B  310  PHE B  319  1                                  10    
HELIX   21 AC3 ASP C  172  THR C  191  1                                  20    
HELIX   22 AC4 ALA C  204  HIS C  224  1                                  21    
HELIX   23 AC5 HIS C  224  ASP C  236  1                                  13    
HELIX   24 AC6 ASN C  239  LEU C  246  1                                   8    
HELIX   25 AC7 LEU C  246  SER C  255  1                                  10    
HELIX   26 AC8 ASN C  260  ILE C  281  1                                  22    
HELIX   27 AC9 GLN C  283  SER C  285  5                                   3    
HELIX   28 AD1 CYS C  286  GLN C  309  1                                  24    
HELIX   29 AD2 ARG C  310  PHE C  319  1                                  10    
HELIX   30 AD3 ASP D  172  THR D  191  1                                  20    
HELIX   31 AD4 ALA D  204  HIS D  224  1                                  21    
HELIX   32 AD5 HIS D  224  ASP D  236  1                                  13    
HELIX   33 AD6 ASN D  239  SER D  255  1                                  17    
HELIX   34 AD7 ASN D  260  ILE D  281  1                                  22    
HELIX   35 AD8 GLN D  283  SER D  285  5                                   3    
HELIX   36 AD9 CYS D  286  LYS D  302  1                                  17    
HELIX   37 AE1 LYS D  302  GLN D  309  1                                   8    
HELIX   38 AE2 ARG D  310  PHE D  319  1                                  10    
CISPEP   1 ALA A  193    LYS A  194          0       -16.86                     
CISPEP   2 SER B  202    GLY B  203          0       -19.17                     
CISPEP   3 GLY B  257    VAL B  258          0         2.84                     
SITE     1 AC1 15 PHE A 228  MET A 231  LEU A 246  MET A 250                    
SITE     2 AC1 15 VAL A 253  ASN A 260  GLY A 262  ARG A 263                    
SITE     3 AC1 15 THR A 266  LEU A 267  PHE A 270  GLY A 271                    
SITE     4 AC1 15 ILE A 294  ASN B 223  HIS B 224                               
SITE     1 AC2 13 ASN A 223  HIS A 224  PHE B 228  MET B 231                    
SITE     2 AC2 13 LEU B 246  MET B 250  ASN B 260  GLY B 262                    
SITE     3 AC2 13 ARG B 263  THR B 266  LEU B 267  PHE B 270                    
SITE     4 AC2 13 GLY B 271                                                     
SITE     1 AC3 10 HIS C 224  PHE C 228  MET C 231  MET C 250                    
SITE     2 AC3 10 VAL C 253  ARG C 263  THR C 266  LEU C 267                    
SITE     3 AC3 10 PHE C 270  GLY C 271                                          
SITE     1 AC4 13 ALA D 227  PHE D 228  MET D 231  LEU D 246                    
SITE     2 AC4 13 VAL D 249  MET D 250  VAL D 253  GLY D 262                    
SITE     3 AC4 13 ARG D 263  THR D 266  LEU D 267  PHE D 270                    
SITE     4 AC4 13 GLY D 271                                                     
CRYST1  149.870  149.870  121.381  90.00  90.00 120.00 P 63 2 2     48          
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      0.006672  0.003852  0.000000        0.00000                         
SCALE2      0.000000  0.007705  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008239        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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