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Database: PDB
Entry: 5IEZ
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HEADER    APOPTOSIS/APOPTOSIS INHIBITOR           25-FEB-16   5IEZ              
TITLE     DISCOVERY OF POTENT MYELOID CELL LEUKEMIA-1 (MCL-1) INHIBITORS USING  
TITLE    2 STRUCTURE-BASED DESIGN                                               
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 172-327;                                      
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 K-12;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 83333                                       
KEYWDS    MYELOID CELL LEUKEMIA-1, BCL-2, APOPTOSIS, APOPTOSIS-APOPTOSIS        
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.ZHAO                                                                
REVDAT   4   04-DEC-19 5IEZ    1       REMARK                                   
REVDAT   3   20-SEP-17 5IEZ    1       REMARK                                   
REVDAT   2   25-JAN-17 5IEZ    1       JRNL                                     
REVDAT   1   18-JAN-17 5IEZ    0                                                
JRNL        AUTH   T.LEE,Z.BIAN,B.ZHAO,L.J.HOGDAL,J.L.SENSINTAFFAR,C.M.GOODWIN, 
JRNL        AUTH 2 J.BELMAR,S.SHAW,J.C.TARR,N.VEERASAMY,S.M.MATULIS,B.KOSS,     
JRNL        AUTH 3 M.A.FISCHER,A.L.ARNOLD,D.V.CAMPER,C.F.BROWNING,              
JRNL        AUTH 4 O.W.ROSSANESE,A.BUDHRAJA,J.OPFERMAN,L.H.BOISE,M.R.SAVONA,    
JRNL        AUTH 5 A.LETAI,E.T.OLEJNICZAK,S.W.FESIK                             
JRNL        TITL   DISCOVERY AND BIOLOGICAL CHARACTERIZATION OF POTENT MYELOID  
JRNL        TITL 2 CELL LEUKEMIA-1 INHIBITORS.                                  
JRNL        REF    FEBS LETT.                    V. 591   240 2017              
JRNL        REFN                   ISSN 1873-3468                               
JRNL        PMID   27878989                                                     
JRNL        DOI    10.1002/1873-3468.12497                                      
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.84                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.500                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 18533                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.880                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 905                             
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 29.8433 -  4.7194    0.96     3135   164  0.1741 0.2272        
REMARK   3     2  4.7194 -  3.7482    0.96     3125   132  0.1650 0.2195        
REMARK   3     3  3.7482 -  3.2751    0.94     3042   144  0.1931 0.3282        
REMARK   3     4  3.2751 -  2.9760    0.91     2907   177  0.2302 0.3137        
REMARK   3     5  2.9760 -  2.7628    0.86     2766   147  0.2379 0.3222        
REMARK   3     6  2.7628 -  2.6000    0.82     2653   141  0.2398 0.3677        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.430            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.680           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           5027                                  
REMARK   3   ANGLE     :  1.213           6801                                  
REMARK   3   CHIRALITY :  0.064            736                                  
REMARK   3   PLANARITY :  0.008            864                                  
REMARK   3   DIHEDRAL  : 17.643           2923                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 19                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 171:190 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.1642   5.4124  34.3543              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2926 T22:   0.1646                                     
REMARK   3      T33:   0.3720 T12:  -0.0138                                     
REMARK   3      T13:  -0.0252 T23:  -0.0114                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6410 L22:   5.3244                                     
REMARK   3      L33:   4.0528 L12:   3.6633                                     
REMARK   3      L13:  -0.9625 L23:  -0.3375                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2987 S12:  -0.1604 S13:   0.7154                       
REMARK   3      S21:   0.0453 S22:   0.2285 S23:  -0.3272                       
REMARK   3      S31:  -0.4457 S32:   0.0835 S33:   0.0331                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 191:202 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.9897  11.3525  36.5506              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7277 T22:   0.2906                                     
REMARK   3      T33:   0.4599 T12:   0.0165                                     
REMARK   3      T13:   0.1299 T23:  -0.1365                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3912 L22:   1.3888                                     
REMARK   3      L33:   2.3357 L12:  -1.4650                                     
REMARK   3      L13:  -0.2264 L23:  -1.2534                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0856 S12:   0.7159 S13:   0.3445                       
REMARK   3      S21:  -0.4077 S22:  -0.0891 S23:  -0.8832                       
REMARK   3      S31:   0.4463 S32:  -0.3848 S33:   0.0838                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 203:223 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.0766   3.2375  25.5280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2393 T22:   0.2982                                     
REMARK   3      T33:   0.3945 T12:   0.0667                                     
REMARK   3      T13:  -0.0130 T23:  -0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4157 L22:   4.8577                                     
REMARK   3      L33:   5.0412 L12:   2.4734                                     
REMARK   3      L13:  -0.3672 L23:   1.1509                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0417 S12:   0.6472 S13:   0.6526                       
REMARK   3      S21:   0.3610 S22:   0.0614 S23:   1.1126                       
REMARK   3      S31:  -0.8338 S32:  -1.0390 S33:   0.2049                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 224:235 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.6947 -16.4669  30.9536              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5452 T22:   0.3440                                     
REMARK   3      T33:   0.3458 T12:  -0.0006                                     
REMARK   3      T13:   0.1377 T23:  -0.0744                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2321 L22:   6.2460                                     
REMARK   3      L33:   2.0223 L12:   2.3392                                     
REMARK   3      L13:   1.3512 L23:  -1.1350                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1480 S12:   0.3409 S13:  -1.1423                       
REMARK   3      S21:   0.1054 S22:  -0.6524 S23:  -0.0769                       
REMARK   3      S31:   0.4805 S32:  -0.2917 S33:   0.2159                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 236:254 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4436 -12.3315  38.0692              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5423 T22:   0.3356                                     
REMARK   3      T33:   0.3615 T12:   0.1788                                     
REMARK   3      T13:   0.0956 T23:   0.0298                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5753 L22:   5.8185                                     
REMARK   3      L33:   3.3035 L12:   0.2449                                     
REMARK   3      L13:   0.0481 L23:  -2.7302                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4575 S12:  -0.3837 S13:  -0.2102                       
REMARK   3      S21:   0.3472 S22:   0.2282 S23:  -0.0861                       
REMARK   3      S31:   0.6346 S32:   0.2590 S33:   0.0285                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 255:283 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0301  -6.7208  30.8275              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2706 T22:   0.2171                                     
REMARK   3      T33:   0.2698 T12:  -0.0078                                     
REMARK   3      T13:   0.0142 T23:  -0.0613                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3016 L22:   3.0791                                     
REMARK   3      L33:   3.8648 L12:   0.7751                                     
REMARK   3      L13:  -0.2451 L23:  -1.5722                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1837 S12:  -0.2483 S13:   0.0009                       
REMARK   3      S21:  -0.4839 S22:   0.0150 S23:  -0.3264                       
REMARK   3      S31:   0.4507 S32:   0.2026 S33:   0.0610                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 284:308 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.4451  -0.1086  32.2569              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3625 T22:   0.2272                                     
REMARK   3      T33:   0.3473 T12:   0.0432                                     
REMARK   3      T13:  -0.0294 T23:  -0.0490                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1446 L22:   5.1660                                     
REMARK   3      L33:   3.9310 L12:   3.0647                                     
REMARK   3      L13:  -3.8040 L23:  -3.7198                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4539 S12:  -0.2184 S13:   0.0559                       
REMARK   3      S21:   0.1450 S22:  -0.3909 S23:  -0.5204                       
REMARK   3      S31:  -0.8736 S32:   0.1973 S33:  -0.1426                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 309:321 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.3633   7.3974  19.0750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5405 T22:   0.0943                                     
REMARK   3      T33:   0.3945 T12:   0.2790                                     
REMARK   3      T13:   0.1868 T23:  -0.0870                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2604 L22:   2.6239                                     
REMARK   3      L33:   9.5869 L12:   0.2084                                     
REMARK   3      L13:   8.8613 L23:  -0.7647                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6599 S12:   0.8529 S13:   1.8938                       
REMARK   3      S21:   0.0290 S22:  -0.9278 S23:  -0.0178                       
REMARK   3      S31:  -1.7837 S32:   0.3616 S33:  -0.0439                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 172:223 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.7500  -0.3960  59.6479              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4378 T22:   0.2212                                     
REMARK   3      T33:   0.2744 T12:  -0.0305                                     
REMARK   3      T13:  -0.0121 T23:   0.0832                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2211 L22:   4.2278                                     
REMARK   3      L33:   3.8894 L12:   1.0744                                     
REMARK   3      L13:  -1.1640 L23:   0.3506                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2818 S12:  -0.1409 S13:  -0.4394                       
REMARK   3      S21:  -0.3044 S22:   0.2639 S23:   0.7431                       
REMARK   3      S31:   0.6352 S32:  -0.1045 S33:   0.0349                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: ( CHAIN B AND RESID 224:254 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.4773  19.0765  56.7339              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4263 T22:   0.2273                                     
REMARK   3      T33:   0.3367 T12:  -0.0297                                     
REMARK   3      T13:   0.0265 T23:   0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3196 L22:   2.6588                                     
REMARK   3      L33:   4.0786 L12:   0.2714                                     
REMARK   3      L13:  -0.4217 L23:   1.0777                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2062 S12:   0.1942 S13:   0.2433                       
REMARK   3      S21:  -0.5703 S22:   0.3312 S23:  -0.3688                       
REMARK   3      S31:  -0.1794 S32:  -0.3306 S33:  -0.1069                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: ( CHAIN B AND RESID 255:323 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.4959   5.5834  62.6223              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2432 T22:   0.1696                                     
REMARK   3      T33:   0.2585 T12:   0.0116                                     
REMARK   3      T13:   0.0455 T23:  -0.0377                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2238 L22:   2.8037                                     
REMARK   3      L33:   4.6080 L12:  -0.1252                                     
REMARK   3      L13:   0.7752 L23:  -2.3119                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0534 S12:  -0.1268 S13:  -0.0963                       
REMARK   3      S21:   0.2101 S22:  -0.2102 S23:  -0.0693                       
REMARK   3      S31:  -0.0879 S32:   0.2320 S33:   0.2808                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: ( CHAIN C AND RESID 172:202 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.6378  42.3429  48.5230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6285 T22:   0.2548                                     
REMARK   3      T33:   0.4039 T12:  -0.0518                                     
REMARK   3      T13:   0.1403 T23:  -0.0349                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8002 L22:   1.3025                                     
REMARK   3      L33:   1.3744 L12:  -0.8999                                     
REMARK   3      L13:  -0.4765 L23:   0.4685                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3218 S12:   0.9522 S13:  -0.0374                       
REMARK   3      S21:   0.1211 S22:   0.0245 S23:  -0.1338                       
REMARK   3      S31:  -0.2024 S32:   0.1331 S33:  -0.0293                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: ( CHAIN C AND RESID 203:254 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.2951  31.1697  58.0614              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5514 T22:   0.2527                                     
REMARK   3      T33:   0.3385 T12:  -0.0428                                     
REMARK   3      T13:   0.0239 T23:   0.0052                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0374 L22:   2.5539                                     
REMARK   3      L33:   0.9725 L12:  -1.1014                                     
REMARK   3      L13:  -1.2763 L23:   0.5409                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0874 S12:  -0.3526 S13:  -0.1359                       
REMARK   3      S21:   0.0315 S22:   0.1722 S23:  -0.2757                       
REMARK   3      S31:  -0.0064 S32:   0.2421 S33:  -0.0260                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: ( CHAIN C AND RESID 255:318 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.6633  36.4648  56.0277              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4218 T22:   0.1894                                     
REMARK   3      T33:   0.3518 T12:  -0.0317                                     
REMARK   3      T13:   0.1387 T23:   0.0275                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5665 L22:   6.2741                                     
REMARK   3      L33:   2.1222 L12:  -3.0139                                     
REMARK   3      L13:  -0.8111 L23:   2.5969                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0060 S12:  -0.0828 S13:   0.2288                       
REMARK   3      S21:  -0.1505 S22:  -0.1849 S23:  -0.0178                       
REMARK   3      S31:  -0.1604 S32:  -0.2266 S33:   0.1823                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: ( CHAIN C AND RESID 319:323 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.5135  53.4775  64.8156              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9794 T22:   0.5733                                     
REMARK   3      T33:   0.5314 T12:   0.1408                                     
REMARK   3      T13:   0.1534 T23:  -0.1453                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3269 L22:   5.4061                                     
REMARK   3      L33:   8.4799 L12:  -1.6421                                     
REMARK   3      L13:  -4.4569 L23:  -1.2097                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9577 S12:  -0.4542 S13:   0.0839                       
REMARK   3      S21:   0.0633 S22:   0.8150 S23:  -0.1857                       
REMARK   3      S31:  -1.6245 S32:   1.5994 S33:  -1.2611                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: ( CHAIN D AND RESID 171:203 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0888  32.6695  17.6003              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6733 T22:   0.3122                                     
REMARK   3      T33:   0.5873 T12:  -0.1008                                     
REMARK   3      T13:  -0.1548 T23:   0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2907 L22:   5.5678                                     
REMARK   3      L33:   6.0874 L12:  -0.2195                                     
REMARK   3      L13:   0.4765 L23:  -1.6575                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4052 S12:   0.6992 S13:  -0.3411                       
REMARK   3      S21:  -2.2355 S22:   0.0233 S23:   0.4236                       
REMARK   3      S31:   0.8164 S32:  -0.2818 S33:   0.0941                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: ( CHAIN D AND RESID 204:223 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.5721  29.5715  27.9843              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4316 T22:   0.3935                                     
REMARK   3      T33:   0.5424 T12:  -0.0400                                     
REMARK   3      T13:  -0.1690 T23:   0.1121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6456 L22:   4.5154                                     
REMARK   3      L33:   7.5903 L12:  -0.7979                                     
REMARK   3      L13:  -2.4687 L23:  -0.0805                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3062 S12:  -0.2876 S13:  -1.0536                       
REMARK   3      S21:   0.6526 S22:  -0.4220 S23:   0.6741                       
REMARK   3      S31:   0.5838 S32:   0.1735 S33:  -0.0318                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: ( CHAIN D AND RESID 224:254 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.8850  49.4437  26.8257              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2893 T22:   0.2092                                     
REMARK   3      T33:   0.4868 T12:  -0.0688                                     
REMARK   3      T13:   0.0571 T23:  -0.0536                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2460 L22:   4.3648                                     
REMARK   3      L33:   2.8801 L12:  -0.2840                                     
REMARK   3      L13:   1.9008 L23:  -2.3044                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3119 S12:  -0.0814 S13:   0.7392                       
REMARK   3      S21:  -0.5613 S22:   0.1157 S23:  -0.3201                       
REMARK   3      S31:  -0.1812 S32:  -0.2526 S33:   0.1339                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: ( CHAIN D AND RESID 255:323 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.6375  35.6655  25.1883              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5447 T22:   0.2320                                     
REMARK   3      T33:   0.3177 T12:  -0.0326                                     
REMARK   3      T13:   0.0603 T23:  -0.0230                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5558 L22:   6.3161                                     
REMARK   3      L33:   2.6986 L12:  -1.5045                                     
REMARK   3      L13:   0.8001 L23:  -3.3652                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2369 S12:   0.1687 S13:  -0.2770                       
REMARK   3      S21:  -0.5254 S22:  -0.3967 S23:  -0.3014                       
REMARK   3      S31:   0.2181 S32:   0.2490 S33:   0.1318                       
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 5IEZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000218740.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAY-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9787                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18621                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.8                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : 0.10900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.2300                            
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) : 2.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.930                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MAGNESIUM CHLORIDE, BIS        
REMARK 280  -TRIS, PH 6.6, 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       68.02300            
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   169                                                      
REMARK 465     ALA A   170                                                      
REMARK 465     GLU A   322                                                      
REMARK 465     ASP A   323                                                      
REMARK 465     LEU A   324                                                      
REMARK 465     GLU A   325                                                      
REMARK 465     GLY A   326                                                      
REMARK 465     GLY A   327                                                      
REMARK 465     GLY B   169                                                      
REMARK 465     ALA B   170                                                      
REMARK 465     ASP B   171                                                      
REMARK 465     LEU B   324                                                      
REMARK 465     GLU B   325                                                      
REMARK 465     GLY B   326                                                      
REMARK 465     GLY B   327                                                      
REMARK 465     GLY C   169                                                      
REMARK 465     ALA C   170                                                      
REMARK 465     ASP C   171                                                      
REMARK 465     LEU C   324                                                      
REMARK 465     GLU C   325                                                      
REMARK 465     GLY C   326                                                      
REMARK 465     GLY C   327                                                      
REMARK 465     GLY D   169                                                      
REMARK 465     ALA D   170                                                      
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     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 171    CG   OD1  OD2                                       
REMARK 470     LYS A 244    CG   CD   CE   NZ                                   
REMARK 470     ARG A 300    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 321    CG1  CG2                                            
REMARK 470     ARG B 176    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 244    CG   CD   CE   NZ                                   
REMARK 470     LYS B 308    CG   CD   CE   NZ                                   
REMARK 470     LYS C 194    CG   CD   CE   NZ                                   
REMARK 470     LYS C 197    CG   CD   CE   NZ                                   
REMARK 470     LYS C 234    CG   CD   CE   NZ                                   
REMARK 470     ARG C 310    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 184    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 194    CG   CD   CE   NZ                                   
REMARK 470     ASP D 195    CG   OD1  OD2                                       
REMARK 470     LYS D 234    CG   CD   CE   NZ                                   
REMARK 470     ARG D 303    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 310    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL D 321    CG1  CG2                                            
REMARK 470     GLU D 322    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 323    CG   OD1  OD2                                       
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   NZ   LYS C   208     O    HOH C   501              2.07            
REMARK 500   O    ALA B   190     O    HOH B   501              2.11            
REMARK 500   O    SER D   245     O    HOH D   501              2.13            
REMARK 500   O    HOH C   519     O    HOH C   520              2.14            
REMARK 500   O    HOH A   520     O    HOH A   524              2.15            
REMARK 500   O    VAL B   265     OG   SER B   269              2.18            
REMARK 500   OG   SER B   245     NH1  ARG C   248              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA B 193     -150.19    -92.56                                   
REMARK 500    LYS B 197      148.61    -32.52                                   
REMARK 500    LYS C 238      -43.86   -138.75                                   
REMARK 500    THR D 191     -139.70   -105.47                                   
REMARK 500    ALA D 193     -149.78   -121.20                                   
REMARK 500    GLN D 221      -83.84    -61.04                                   
REMARK 500    ARG D 222       30.41    -99.20                                   
REMARK 500    ARG D 310       14.14     59.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS A  244     SER A  245                  141.12                    
REMARK 500 PRO B  198     MET B  199                  149.81                    
REMARK 500 MET B  199     GLY B  200                   38.52                    
REMARK 500 ARG D  222     ASN D  223                  139.54                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 531        DISTANCE =  6.53 ANGSTROMS                       
REMARK 525    HOH A 532        DISTANCE =  7.01 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6AL A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6AL B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6AL C 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6AL D 400                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5IF4   RELATED DB: PDB                                   
DBREF  5IEZ A  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  5IEZ B  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  5IEZ C  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
DBREF  5IEZ D  172   327  UNP    Q07820   MCL1_HUMAN     172    327             
SEQADV 5IEZ GLY A  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5IEZ ALA A  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5IEZ ASP A  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5IEZ GLY B  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5IEZ ALA B  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5IEZ ASP B  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5IEZ GLY C  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5IEZ ALA C  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5IEZ ASP C  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5IEZ GLY D  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5IEZ ALA D  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5IEZ ASP D  171  UNP  Q07820              EXPRESSION TAG                 
SEQRES   1 A  159  GLY ALA ASP ASP GLU LEU TYR ARG GLN SER LEU GLU ILE          
SEQRES   2 A  159  ILE SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS          
SEQRES   3 A  159  ASP THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG          
SEQRES   4 A  159  LYS ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL          
SEQRES   5 A  159  GLN ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG          
SEQRES   6 A  159  LYS LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU          
SEQRES   7 A  159  SER ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR          
SEQRES   8 A  159  ASN TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA          
SEQRES   9 A  159  PHE VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER          
SEQRES  10 A  159  CYS ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU          
SEQRES  11 A  159  VAL ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY          
SEQRES  12 A  159  TRP ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU          
SEQRES  13 A  159  GLU GLY GLY                                                  
SEQRES   1 B  159  GLY ALA ASP ASP GLU LEU TYR ARG GLN SER LEU GLU ILE          
SEQRES   2 B  159  ILE SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS          
SEQRES   3 B  159  ASP THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG          
SEQRES   4 B  159  LYS ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL          
SEQRES   5 B  159  GLN ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG          
SEQRES   6 B  159  LYS LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU          
SEQRES   7 B  159  SER ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR          
SEQRES   8 B  159  ASN TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA          
SEQRES   9 B  159  PHE VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER          
SEQRES  10 B  159  CYS ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU          
SEQRES  11 B  159  VAL ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY          
SEQRES  12 B  159  TRP ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU          
SEQRES  13 B  159  GLU GLY GLY                                                  
SEQRES   1 C  159  GLY ALA ASP ASP GLU LEU TYR ARG GLN SER LEU GLU ILE          
SEQRES   2 C  159  ILE SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS          
SEQRES   3 C  159  ASP THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG          
SEQRES   4 C  159  LYS ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL          
SEQRES   5 C  159  GLN ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG          
SEQRES   6 C  159  LYS LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU          
SEQRES   7 C  159  SER ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR          
SEQRES   8 C  159  ASN TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA          
SEQRES   9 C  159  PHE VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER          
SEQRES  10 C  159  CYS ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU          
SEQRES  11 C  159  VAL ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY          
SEQRES  12 C  159  TRP ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU          
SEQRES  13 C  159  GLU GLY GLY                                                  
SEQRES   1 D  159  GLY ALA ASP ASP GLU LEU TYR ARG GLN SER LEU GLU ILE          
SEQRES   2 D  159  ILE SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS          
SEQRES   3 D  159  ASP THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG          
SEQRES   4 D  159  LYS ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL          
SEQRES   5 D  159  GLN ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG          
SEQRES   6 D  159  LYS LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU          
SEQRES   7 D  159  SER ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR          
SEQRES   8 D  159  ASN TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA          
SEQRES   9 D  159  PHE VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER          
SEQRES  10 D  159  CYS ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU          
SEQRES  11 D  159  VAL ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY          
SEQRES  12 D  159  TRP ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU          
SEQRES  13 D  159  GLU GLY GLY                                                  
HET    6AL  A 400      43                                                       
HET    6AL  B 400      43                                                       
HET    6AL  C 400      43                                                       
HET    6AL  D 400      43                                                       
HETNAM     6AL 3-({6-CHLORO-3-[3-(4-CHLORO-3,5-DIMETHYLPHENOXY)                 
HETNAM   2 6AL  PROPYL]-7-(1,3,5-TRIMETHYL-1H-PYRAZOL-4-YL)-1H-INDOLE-          
HETNAM   3 6AL  2-CARBONYL}AMINO)BENZOIC ACID                                   
FORMUL   5  6AL    4(C33 H32 CL2 N4 O4)                                         
FORMUL   9  HOH   *94(H2 O)                                                     
HELIX    1 AA1 ASP A  172  THR A  191  1                                  20    
HELIX    2 AA2 SER A  202  HIS A  224  1                                  23    
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  PHE A  319  1                                  10    
HELIX    9 AA9 GLU B  173  THR B  191  1                                  19    
HELIX   10 AB1 GLY B  203  HIS B  224  1                                  22    
HELIX   11 AB2 HIS B  224  ASP B  236  1                                  13    
HELIX   12 AB3 ASN B  239  ASP B  241  5                                   3    
HELIX   13 AB4 ASP B  242  SER B  255  1                                  14    
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  LYS B  302  1                                  17    
HELIX   17 AB8 LYS B  302  GLN B  309  1                                   8    
HELIX   18 AB9 ARG B  310  PHE B  319  1                                  10    
HELIX   19 AC1 GLU C  173  GLY C  192  1                                  20    
HELIX   20 AC2 SER C  202  HIS C  224  1                                  23    
HELIX   21 AC3 HIS C  224  ASP C  236  1                                  13    
HELIX   22 AC4 ASN C  239  SER C  245  1                                   7    
HELIX   23 AC5 LEU C  246  SER C  255  1                                  10    
HELIX   24 AC6 ASN C  260  ILE C  281  1                                  22    
HELIX   25 AC7 GLN C  283  SER C  285  5                                   3    
HELIX   26 AC8 CYS C  286  GLN C  309  1                                  24    
HELIX   27 AC9 GLY C  311  PHE C  319  1                                   9    
HELIX   28 AD1 ASP D  172  THR D  191  1                                  20    
HELIX   29 AD2 ALA D  204  ASN D  223  1                                  20    
HELIX   30 AD3 HIS D  224  ASP D  236  1                                  13    
HELIX   31 AD4 ASN D  239  LEU D  246  1                                   8    
HELIX   32 AD5 LEU D  246  SER D  255  1                                  10    
HELIX   33 AD6 ASN D  260  ILE D  281  1                                  22    
HELIX   34 AD7 GLN D  283  SER D  285  5                                   3    
HELIX   35 AD8 CYS D  286  LYS D  302  1                                  17    
HELIX   36 AD9 LYS D  302  GLN D  309  1                                   8    
HELIX   37 AE1 GLY D  311  PHE D  319  1                                   9    
CISPEP   1 SER B  202    GLY B  203          0         3.46                     
CISPEP   2 GLU B  322    ASP B  323          0         6.01                     
SITE     1 AC1 15 HIS A 224  ALA A 227  PHE A 228  MET A 231                    
SITE     2 AC1 15 VAL A 249  MET A 250  PHE A 254  GLY A 257                    
SITE     3 AC1 15 VAL A 258  ARG A 263  THR A 266  LEU A 267                    
SITE     4 AC1 15 PHE A 270  GLY A 271  HOH A 507                               
SITE     1 AC2 12 HIS B 224  ALA B 227  PHE B 228  MET B 231                    
SITE     2 AC2 12 MET B 250  PHE B 254  ASN B 260  ARG B 263                    
SITE     3 AC2 12 THR B 266  LEU B 267  PHE B 270  GLY B 271                    
SITE     1 AC3 14 HIS C 224  ALA C 227  PHE C 228  MET C 231                    
SITE     2 AC3 14 LEU C 246  MET C 250  VAL C 253  PHE C 254                    
SITE     3 AC3 14 ASN C 260  ARG C 263  THR C 266  LEU C 267                    
SITE     4 AC3 14 PHE C 270  GLY C 271                                          
SITE     1 AC4 14 HIS D 224  ALA D 227  PHE D 228  MET D 231                    
SITE     2 AC4 14 LEU D 246  VAL D 249  MET D 250  PHE D 254                    
SITE     3 AC4 14 ASN D 260  ARG D 263  THR D 266  LEU D 267                    
SITE     4 AC4 14 PHE D 270  GLY D 271                                          
CRYST1   39.914  136.046   63.499  90.00 101.62  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      0.025054  0.000000  0.005151        0.00000                         
SCALE2      0.000000  0.007350  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016078        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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