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Database: PDB
Entry: 6O0O
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Original site: 6O0O 
HEADER    APOPTOSIS                               17-FEB-19   6O0O              
TITLE     CRYSTAL STRUCTURE OF BCL-2 G101V MUTATION WITH S55746                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APOPTOSIS REGULATOR BCL-2,BCL-2-LIKE PROTEIN 1,APOPTOSIS   
COMPND   3 REGULATOR BCL-2;                                                     
COMPND   4 CHAIN: A, C;                                                         
COMPND   5 SYNONYM: BCL2-L-1,APOPTOSIS REGULATOR BCL-X;                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BCL2, BCL2L1, BCL2L, BCLX;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    BCL-2, S55746, COMPLEX, PROTEIN-PROTEIN INTERFACE INHIBITOR,          
KEYWDS   2 RESISTANCE MUTATION, APOPTOSIS                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.W.BIRKINSHAW,C.S.LUO,P.M.COLMAN,P.E.CZABOTAR                        
REVDAT   3   10-JUL-19 6O0O    1       COMPND SOURCE DBREF  SEQADV              
REVDAT   2   19-JUN-19 6O0O    1       JRNL                                     
REVDAT   1   22-MAY-19 6O0O    0                                                
JRNL        AUTH   R.W.BIRKINSHAW,J.N.GONG,C.S.LUO,D.LIO,C.A.WHITE,             
JRNL        AUTH 2 M.A.ANDERSON,P.BLOMBERY,G.LESSENE,I.J.MAJEWSKI,R.THIJSSEN,   
JRNL        AUTH 3 A.W.ROBERTS,D.C.S.HUANG,P.M.COLMAN,P.E.CZABOTAR              
JRNL        TITL   STRUCTURES OF BCL-2 IN COMPLEX WITH VENETOCLAX REVEAL THE    
JRNL        TITL 2 MOLECULAR BASIS OF RESISTANCE MUTATIONS.                     
JRNL        REF    NAT COMMUN                    V.  10  2385 2019              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   31160589                                                     
JRNL        DOI    10.1038/S41467-019-10363-1                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.14_3260                                     
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.43                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 74.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 16500                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 816                             
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 37.4359 -  3.6298    1.00     3569   189  0.1824 0.2193        
REMARK   3     2  3.6298 -  2.8814    1.00     3499   185  0.2349 0.2878        
REMARK   3     3  2.8814 -  2.5173    0.96     3362   176  0.2649 0.3550        
REMARK   3     4  2.5173 -  2.2872    0.72     2533   129  0.2591 0.3189        
REMARK   3     5  2.2872 -  2.1232    0.51     1780    95  0.2793 0.3655        
REMARK   3     6  2.1232 -  1.9981    0.27      941    42  0.2936 0.4024        
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)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.250           
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      :  0.004           2471                                  
REMARK   3   ANGLE     :  0.543           3353                                  
REMARK   3   CHIRALITY :  0.038            327                                  
REMARK   3   PLANARITY :  0.004            507                                  
REMARK   3   DIHEDRAL  : 13.999           1463                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 9 THROUGH 50 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  23.3349   5.8981  11.2590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8213 T22:   0.3347                                     
REMARK   3      T33:   0.2966 T12:  -0.1926                                     
REMARK   3      T13:  -0.0382 T23:   0.0376                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6656 L22:   1.8838                                     
REMARK   3      L33:   3.2050 L12:  -0.1732                                     
REMARK   3      L13:   0.4971 L23:  -1.9728                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0139 S12:  -0.0414 S13:   0.2867                       
REMARK   3      S21:   0.8516 S22:  -0.0651 S23:   0.1352                       
REMARK   3      S31:  -0.7917 S32:  -0.0163 S33:  -0.0892                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 51 THROUGH 66 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  10.9032   8.9583   6.4604              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7715 T22:   0.3371                                     
REMARK   3      T33:   0.2229 T12:   0.2288                                     
REMARK   3      T13:   0.2519 T23:   0.0435                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3841 L22:   0.8130                                     
REMARK   3      L33:   1.3638 L12:   0.6135                                     
REMARK   3      L13:  -1.0329 L23:   0.1518                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2917 S12:  -0.2656 S13:   0.3502                       
REMARK   3      S21:   0.2369 S22:   0.0627 S23:   0.1923                       
REMARK   3      S31:  -0.5173 S32:  -0.1320 S33:   2.3863                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 67 THROUGH 77 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   4.2627  -6.2165  10.8434              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5808 T22:   1.1147                                     
REMARK   3      T33:   1.0042 T12:   0.0497                                     
REMARK   3      T13:   0.1859 T23:   0.2587                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3711 L22:   2.2285                                     
REMARK   3      L33:   3.4591 L12:   0.2999                                     
REMARK   3      L13:   1.5841 L23:  -2.0683                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3579 S12:   0.1407 S13:  -0.4840                       
REMARK   3      S21:   0.1961 S22:  -0.1102 S23:  -0.6518                       
REMARK   3      S31:   0.0527 S32:  -0.0936 S33:  -0.1001                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 78 THROUGH 102 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  16.5565 -10.3357   2.1359              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5113 T22:   0.3211                                     
REMARK   3      T33:   0.2265 T12:  -0.0650                                     
REMARK   3      T13:  -0.0688 T23:   0.0092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1707 L22:   3.7079                                     
REMARK   3      L33:   5.7134 L12:  -1.3113                                     
REMARK   3      L13:   2.2199 L23:  -4.1367                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1761 S12:   0.2406 S13:   0.0525                       
REMARK   3      S21:  -0.8025 S22:   0.2362 S23:   0.4824                       
REMARK   3      S31:   0.5223 S32:  -0.1283 S33:  -0.3059                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 162 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.4565   0.8011   2.3879              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3202 T22:   0.2172                                     
REMARK   3      T33:   0.1300 T12:  -0.0365                                     
REMARK   3      T13:   0.0211 T23:   0.0321                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0274 L22:   1.8776                                     
REMARK   3      L33:   3.7052 L12:  -0.1073                                     
REMARK   3      L13:   0.1934 L23:  -1.7525                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1734 S12:  -0.1218 S13:   0.1316                       
REMARK   3      S21:   0.1229 S22:   0.0216 S23:   0.1257                       
REMARK   3      S31:   0.0346 S32:   0.0383 S33:  -0.0921                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 10 THROUGH 50 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  27.0846 -36.7333  21.0507              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0266 T22:   0.2195                                     
REMARK   3      T33:   0.4024 T12:   0.1108                                     
REMARK   3      T13:   0.0423 T23:  -0.0722                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1825 L22:   0.7013                                     
REMARK   3      L33:   1.0148 L12:   0.0858                                     
REMARK   3      L13:   0.3291 L23:  -0.3874                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1227 S12:  -0.4099 S13:  -0.2551                       
REMARK   3      S21:  -0.0701 S22:   0.1718 S23:  -0.3615                       
REMARK   3      S31:   0.3572 S32:   0.5121 S33:   0.6839                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 51 THROUGH 66 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  23.9635 -39.9776  34.1526              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4208 T22:   0.2705                                     
REMARK   3      T33:   0.5209 T12:   0.0245                                     
REMARK   3      T13:  -0.2176 T23:   0.0666                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5734 L22:   5.9727                                     
REMARK   3      L33:   2.3975 L12:  -3.3748                                     
REMARK   3      L13:  -1.5300 L23:   0.3454                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3656 S12:  -0.3686 S13:  -0.5689                       
REMARK   3      S21:   0.7056 S22:   0.1356 S23:   0.3357                       
REMARK   3      S31:  -0.4435 S32:  -0.1811 S33:  -0.0449                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 67 THROUGH 77 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7083 -24.9055  36.1925              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1385 T22:   0.8652                                     
REMARK   3      T33:   0.5667 T12:   0.1430                                     
REMARK   3      T13:   0.0673 T23:   0.1097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3954 L22:   1.6081                                     
REMARK   3      L33:   2.2193 L12:   0.1406                                     
REMARK   3      L13:   0.2520 L23:  -1.8103                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5251 S12:   0.3109 S13:  -0.2761                       
REMARK   3      S21:   0.4736 S22:   0.4318 S23:   0.2352                       
REMARK   3      S31:   0.0270 S32:   0.0669 S33:  -0.2469                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 78 THROUGH 122 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0207 -24.6614  31.3940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4587 T22:   0.3443                                     
REMARK   3      T33:   0.3532 T12:   0.0721                                     
REMARK   3      T13:  -0.2128 T23:  -0.0117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7267 L22:   0.9648                                     
REMARK   3      L33:   2.1473 L12:  -0.3313                                     
REMARK   3      L13:   0.9041 L23:  -1.3161                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1030 S12:  -0.1729 S13:   0.1325                       
REMARK   3      S21:   1.0880 S22:   0.1804 S23:  -0.3758                       
REMARK   3      S31:  -0.5330 S32:  -0.1164 S33:   0.2796                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 123 THROUGH 162 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  35.0954 -33.1483  29.7811              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2240 T22:   0.2965                                     
REMARK   3      T33:   0.4055 T12:   0.0733                                     
REMARK   3      T13:  -0.1013 T23:  -0.0333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6995 L22:   1.3507                                     
REMARK   3      L33:   2.1917 L12:  -0.7995                                     
REMARK   3      L13:   1.2415 L23:  -1.4625                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1640 S12:   0.3347 S13:  -0.1590                       
REMARK   3      S21:  -0.0848 S22:  -0.2488 S23:  -0.4728                       
REMARK   3      S31:   0.3996 S32:   0.5412 S33:   0.0836                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: AUTHORS STATE THAT THE DIFFRACTION DATA   
REMARK   3  WERE ELLIPSOIDALLY TRUNCATED AFTER 2.7 ANGSTROM. TWO COPIES OF      
REMARK   3  BCL-2 AND S55746 ARE PRESENT IN THE ASSYMETRIC UNIT. THE MODEL      
REMARK   3  FROM CHAIN A IS THE PREFERRED CHAIN FOR ANALYSIS AS THE ELECTRON    
REMARK   3  DENSITY FOR CHAIN C IS OF POORER QUALITY.                           
REMARK   4                                                                      
REMARK   4 6O0O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000239801.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-DEC-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : DOUBLE-CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22155                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.998                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.430                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 74.3                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.2900                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 21.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4LVT                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NACL 0.1M SUCCINIC ACID-NAOH        
REMARK 280  PH5.0 10% PEG200, VAPOR DIFFUSION, TEMPERATURE 291K                 
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       34.29200            
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                                                    
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: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     ASP A    34                                                      
REMARK 465     ASP A    35                                                      
REMARK 465     VAL A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     GLU A    38                                                      
REMARK 465     ASN A    39                                                      
REMARK 465     ARG A    40                                                      
REMARK 465     THR A    41                                                      
REMARK 465     GLU A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     PRO A    44                                                      
REMARK 465     GLU A    45                                                      
REMARK 465     GLY A    46                                                      
REMARK 465     THR A    47                                                      
REMARK 465     GLU A    48                                                      
REMARK 465     SER A    49                                                      
REMARK 465     PRO A   163                                                      
REMARK 465     SER A   164                                                      
REMARK 465     MET A   165                                                      
REMARK 465     ARG A   166                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     ALA C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     ARG C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     GLY C     8                                                      
REMARK 465     TYR C     9                                                      
REMARK 465     GLY C    33                                                      
REMARK 465     ASP C    34                                                      
REMARK 465     ASP C    35                                                      
REMARK 465     VAL C    36                                                      
REMARK 465     GLU C    37                                                      
REMARK 465     GLU C    38                                                      
REMARK 465     ASN C    39                                                      
REMARK 465     ARG C    40                                                      
REMARK 465     THR C    41                                                      
REMARK 465     GLU C    42                                                      
REMARK 465     ALA C    43                                                      
REMARK 465     PRO C    44                                                      
REMARK 465     GLU C    45                                                      
REMARK 465     GLY C    46                                                      
REMARK 465     THR C    47                                                      
REMARK 465     GLU C    48                                                      
REMARK 465     SER C    49                                                      
REMARK 465     PRO C   163                                                      
REMARK 465     SER C   164                                                      
REMARK 465     MET C   165                                                      
REMARK 465     ARG C   166                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  50    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER C    64     OE2  GLU C   111              2.14            
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    HIS C 143      -50.57   -126.45                                   
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 F3Q A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue F3Q C 201                 
DBREF  6O0O A    1    34  UNP    P10415   BCL2_HUMAN       1     34             
DBREF  6O0O A   35    50  UNP    Q07817   B2CL1_HUMAN     29     44             
DBREF  6O0O A   51   166  UNP    P10415   BCL2_HUMAN      92    207             
DBREF  6O0O C    1    34  UNP    P10415   BCL2_HUMAN       1     34             
DBREF  6O0O C   35    50  UNP    Q07817   B2CL1_HUMAN     29     44             
DBREF  6O0O C   51   166  UNP    P10415   BCL2_HUMAN      92    207             
SEQADV 6O0O VAL A   60  UNP  P10415    GLY   101 ENGINEERED MUTATION            
SEQADV 6O0O VAL C   60  UNP  P10415    GLY   101 ENGINEERED MUTATION            
SEQRES   1 A  166  MET ALA HIS ALA GLY ARG THR GLY TYR ASP ASN ARG GLU          
SEQRES   2 A  166  ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER GLN ARG          
SEQRES   3 A  166  GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL GLU GLU ASN          
SEQRES   4 A  166  ARG THR GLU ALA PRO GLU GLY THR GLU SER GLU VAL VAL          
SEQRES   5 A  166  HIS LEU THR LEU ARG GLN ALA VAL ASP ASP PHE SER ARG          
SEQRES   6 A  166  ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER GLN LEU          
SEQRES   7 A  166  HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE ALA THR          
SEQRES   8 A  166  VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN TRP GLY          
SEQRES   9 A  166  ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL MET CYS          
SEQRES  10 A  166  VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU VAL ASP          
SEQRES  11 A  166  ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN ARG HIS          
SEQRES  12 A  166  LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP ASP ALA          
SEQRES  13 A  166  PHE VAL GLU LEU TYR GLY PRO SER MET ARG                      
SEQRES   1 C  166  MET ALA HIS ALA GLY ARG THR GLY TYR ASP ASN ARG GLU          
SEQRES   2 C  166  ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER GLN ARG          
SEQRES   3 C  166  GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL GLU GLU ASN          
SEQRES   4 C  166  ARG THR GLU ALA PRO GLU GLY THR GLU SER GLU VAL VAL          
SEQRES   5 C  166  HIS LEU THR LEU ARG GLN ALA VAL ASP ASP PHE SER ARG          
SEQRES   6 C  166  ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER GLN LEU          
SEQRES   7 C  166  HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE ALA THR          
SEQRES   8 C  166  VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN TRP GLY          
SEQRES   9 C  166  ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL MET CYS          
SEQRES  10 C  166  VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU VAL ASP          
SEQRES  11 C  166  ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN ARG HIS          
SEQRES  12 C  166  LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP ASP ALA          
SEQRES  13 C  166  PHE VAL GLU LEU TYR GLY PRO SER MET ARG                      
HET    F3Q  A 201      53                                                       
HET    F3Q  C 201      53                                                       
HETNAM     F3Q ~{N}-(4-HYDROXYPHENYL)-3-[6-[[(3~{S})-3-(MORPHOLIN-4-            
HETNAM   2 F3Q  YLMETHYL)-3,4-DIHYDRO-1~{H}-ISOQUINOLIN-2-                      
HETNAM   3 F3Q  YL]CARBONYL]-1,3-BENZODIOXOL-5-YL]-~{N}-PHENYL-5,6,7,           
HETNAM   4 F3Q  8-TETRAHYDROINDOLIZINE-1-CARBOXAMIDE                            
FORMUL   3  F3Q    2(C43 H42 N4 O6)                                             
FORMUL   5  HOH   *15(H2 O)                                                     
HELIX    1 AA1 ASP A   10  ARG A   26  1                                  17    
HELIX    2 AA2 VAL A   51  TYR A   67  1                                  17    
HELIX    3 AA3 TYR A   67  LEU A   78  1                                  12    
HELIX    4 AA4 THR A   84  PHE A   97  1                                  14    
HELIX    5 AA5 ASN A  102  ARG A  123  1                                  22    
HELIX    6 AA6 PRO A  127  LEU A  144  1                                  18    
HELIX    7 AA7 LEU A  144  ASN A  151  1                                   8    
HELIX    8 AA8 GLY A  153  TYR A  161  1                                   9    
HELIX    9 AA9 ASN C   11  GLN C   25  1                                  15    
HELIX   10 AB1 VAL C   51  TYR C   67  1                                  17    
HELIX   11 AB2 TYR C   67  SER C   76  1                                  10    
HELIX   12 AB3 THR C   84  PHE C   97  1                                  14    
HELIX   13 AB4 ASN C  102  ARG C  123  1                                  22    
HELIX   14 AB5 PRO C  127  HIS C  143  1                                  17    
HELIX   15 AB6 LEU C  144  ASN C  151  1                                   8    
HELIX   16 AB7 GLY C  153  TYR C  161  1                                   9    
SITE     1 AC1 13 PHE A  63  TYR A  67  ASP A  70  PHE A  71                    
SITE     2 AC1 13 MET A  74  ARG A  88  VAL A  92  GLU A  95                    
SITE     3 AC1 13 LEU A  96  GLY A 104  ARG A 105  ALA A 108                    
SITE     4 AC1 13 PHE A 112                                                     
SITE     1 AC2 12 PHE C  63  TYR C  67  ASP C  70  MET C  74                    
SITE     2 AC2 12 VAL C  92  GLU C  95  LEU C  96  GLY C 104                    
SITE     3 AC2 12 ARG C 105  ALA C 108  GLU C 111  PHE C 112                    
CRYST1   37.684   68.584   64.489  90.00  96.67  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.026536  0.000000  0.003101        0.00000                         
SCALE2      0.000000  0.014581  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015612        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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