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Database: PDB
Entry: 6O0L
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Original site: 6O0L 
HEADER    APOPTOSIS                               16-FEB-19   6O0L              
TITLE     CRYSTAL STRUCTURE OF BCL-2 G101V MUTATION WITH VENETOCLAX             
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;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    BCL-2, VENETOCLAX, COMPLEX, PROTEIN-PROTEIN INTERFACE INHIBITOR,      
KEYWDS   2 RESISTANCE MUTATION, FDA APPROVED DRUG COMPLEX, APOPTOSIS            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.W.BIRKINSHAW,C.S.LUO,P.M.COLMAN,P.E.CZABOTAR                        
REVDAT   5   11-DEC-19 6O0L    1       HETSYN                                   
REVDAT   4   20-NOV-19 6O0L    1       COMPND HETNAM FORMUL                     
REVDAT   3   10-JUL-19 6O0L    1       COMPND SOURCE DBREF  SEQADV              
REVDAT   2   19-JUN-19 6O0L    1       JRNL                                     
REVDAT   1   22-MAY-19 6O0L    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.    2.20 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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.51                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 12924                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.860                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 628                             
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 47.5190 -  3.4919    1.00     3121   155  0.1762 0.2041        
REMARK   3     2  3.4919 -  2.7717    1.00     3054   158  0.2059 0.2154        
REMARK   3     3  2.7717 -  2.4214    1.00     3095   159  0.2182 0.2920        
REMARK   3     4  2.4214 -  2.2000    1.00     3026   156  0.2353 0.2787        
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)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.340           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           2550                                  
REMARK   3   ANGLE     :  0.589           3449                                  
REMARK   3   CHIRALITY :  0.038            334                                  
REMARK   3   PLANARITY :  0.003            505                                  
REMARK   3   DIHEDRAL  : 18.466           1505                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 9 THROUGH 90 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   9.2479   7.2737  -5.3664              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3344 T22:   0.3400                                     
REMARK   3      T33:   0.2133 T12:  -0.0092                                     
REMARK   3      T13:  -0.0656 T23:  -0.0210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8090 L22:   6.1047                                     
REMARK   3      L33:   2.4332 L12:  -0.3261                                     
REMARK   3      L13:   0.7418 L23:  -0.5194                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1771 S12:   0.4439 S13:  -0.2963                       
REMARK   3      S21:  -1.0320 S22:   0.2988 S23:  -0.1479                       
REMARK   3      S31:   0.0642 S32:   0.0586 S33:   0.0930                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 91 THROUGH 107 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.6490   3.2669  -5.0880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6027 T22:   0.4206                                     
REMARK   3      T33:   0.2157 T12:  -0.1655                                     
REMARK   3      T13:  -0.0976 T23:   0.0829                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3850 L22:   3.6291                                     
REMARK   3      L33:   4.7690 L12:   2.2120                                     
REMARK   3      L13:   3.0025 L23:  -0.1722                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0795 S12:   0.8164 S13:  -0.3613                       
REMARK   3      S21:  -0.3519 S22:   0.1691 S23:  -0.0911                       
REMARK   3      S31:   1.1246 S32:   0.0287 S33:  -0.4966                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 108 THROUGH 117 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.3031  19.4970  -5.6781              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6627 T22:   0.9200                                     
REMARK   3      T33:   0.5580 T12:  -0.2248                                     
REMARK   3      T13:  -0.2422 T23:   0.1463                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2951 L22:   4.7725                                     
REMARK   3      L33:   3.6344 L12:   6.2242                                     
REMARK   3      L13:  -5.3592 L23:  -4.1540                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5597 S12:  -0.6487 S13:  -0.1045                       
REMARK   3      S21:   0.9529 S22:  -0.2340 S23:  -0.0977                       
REMARK   3      S31:  -0.2328 S32:   0.1774 S33:  -0.7316                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 118 THROUGH 203 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   2.9757  13.6087   4.0071              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2752 T22:   0.2197                                     
REMARK   3      T33:   0.1604 T12:   0.0033                                     
REMARK   3      T13:  -0.0514 T23:   0.0117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4963 L22:   4.4856                                     
REMARK   3      L33:   3.6884 L12:   2.1552                                     
REMARK   3      L13:  -1.2569 L23:  -1.8068                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0757 S12:  -0.0248 S13:   0.2609                       
REMARK   3      S21:   0.0121 S22:   0.0423 S23:   0.2914                       
REMARK   3      S31:  -0.2136 S32:   0.0058 S33:  -0.1039                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 8 THROUGH 90 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   7.2728  37.0448  18.5847              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4071 T22:   0.4030                                     
REMARK   3      T33:   0.2829 T12:   0.0435                                     
REMARK   3      T13:  -0.0472 T23:   0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3195 L22:   6.2783                                     
REMARK   3      L33:   3.8076 L12:   1.1681                                     
REMARK   3      L13:  -1.2793 L23:   1.9208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0383 S12:   0.3794 S13:   0.2960                       
REMARK   3      S21:  -0.8625 S22:   0.1371 S23:   0.0797                       
REMARK   3      S31:   0.1750 S32:  -0.7281 S33:   0.0562                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 91 THROUGH 107 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2653  40.8833  18.6098              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5095 T22:   0.4285                                     
REMARK   3      T33:   0.3098 T12:  -0.1638                                     
REMARK   3      T13:   0.0373 T23:   0.0380                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6553 L22:   4.7351                                     
REMARK   3      L33:   7.5730 L12:  -1.0930                                     
REMARK   3      L13:  -4.8840 L23:   4.1487                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2229 S12:   1.0357 S13:   0.7811                       
REMARK   3      S21:  -0.8855 S22:   0.3675 S23:  -0.2476                       
REMARK   3      S31:  -0.9613 S32:   0.1756 S33:  -0.8028                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 108 THROUGH 117 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.9519  24.7179  17.9498              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8272 T22:   0.8687                                     
REMARK   3      T33:   0.4928 T12:   0.0736                                     
REMARK   3      T13:   0.1285 T23:  -0.3370                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5340 L22:   1.0236                                     
REMARK   3      L33:   1.3204 L12:   0.1186                                     
REMARK   3      L13:  -0.3319 L23:   0.6865                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0918 S12:  -0.1489 S13:   0.1130                       
REMARK   3      S21:   0.2347 S22:   0.0676 S23:  -0.1701                       
REMARK   3      S31:   0.3800 S32:   0.2134 S33:   0.9681                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 118 THROUGH 143 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.2094  22.5434  29.3811              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3731 T22:   0.2877                                     
REMARK   3      T33:   0.3973 T12:   0.0295                                     
REMARK   3      T13:  -0.0920 T23:  -0.0396                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5499 L22:   2.8032                                     
REMARK   3      L33:   6.3474 L12:   2.7276                                     
REMARK   3      L13:   2.0088 L23:   2.3679                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3670 S12:   0.2827 S13:  -0.8606                       
REMARK   3      S21:   0.8069 S22:   0.4779 S23:  -0.7723                       
REMARK   3      S31:   0.8037 S32:   0.2250 S33:  -0.5902                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 144 THROUGH 203 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8089  33.9406  27.0697              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2805 T22:   0.2647                                     
REMARK   3      T33:   0.1677 T12:   0.0085                                     
REMARK   3      T13:   0.0183 T23:   0.0132                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6277 L22:   5.5927                                     
REMARK   3      L33:   4.2495 L12:   3.5222                                     
REMARK   3      L13:   2.7365 L23:   2.1242                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0123 S12:   0.0182 S13:  -0.0839                       
REMARK   3      S21:  -0.1777 S22:   0.1392 S23:  -0.0272                       
REMARK   3      S31:  -0.1538 S32:  -0.0022 S33:  -0.1526                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: AUTHORS STATE THAT THE DATA WERE          
REMARK   3  PROCESSED AND REFINED IN SPACEGROUP P21, DESPITE BEING POSSIBLE     
REMARK   3  TO MERGE AND REFINE IN ORTHORHOMBIC SPACEGROUP P212121. THIS WAS    
REMARK   3  DUE TO POORER REFINEMENT STATISTICS IN THE ORTHORHOMBIC             
REMARK   3  SPACEGROUP.                                                         
REMARK   4                                                                      
REMARK   4 6O0L 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_1000239798.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUL-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : 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          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12909                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.510                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.560                              
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: 6O0G                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 26.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 4% PEG4K, 35% PEG400, 0.08M MES PH       
REMARK 280  6.0, 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       41.00250            
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     ASP A    75                                                      
REMARK 465     ASP A    76                                                      
REMARK 465     VAL A    77                                                      
REMARK 465     GLU A    78                                                      
REMARK 465     GLU A    79                                                      
REMARK 465     ASN A    80                                                      
REMARK 465     ARG A    81                                                      
REMARK 465     THR A    82                                                      
REMARK 465     GLU A    83                                                      
REMARK 465     ALA A    84                                                      
REMARK 465     PRO A    85                                                      
REMARK 465     GLU A    86                                                      
REMARK 465     GLY A    87                                                      
REMARK 465     THR A    88                                                      
REMARK 465     GLU A    89                                                      
REMARK 465     PRO A   204                                                      
REMARK 465     SER A   205                                                      
REMARK 465     MET A   206                                                      
REMARK 465     ARG A   207                                                      
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     ASP C    75                                                      
REMARK 465     ASP C    76                                                      
REMARK 465     VAL C    77                                                      
REMARK 465     GLU C    78                                                      
REMARK 465     GLU C    79                                                      
REMARK 465     ASN C    80                                                      
REMARK 465     ARG C    81                                                      
REMARK 465     THR C    82                                                      
REMARK 465     GLU C    83                                                      
REMARK 465     ALA C    84                                                      
REMARK 465     PRO C    85                                                      
REMARK 465     GLU C    86                                                      
REMARK 465     GLY C    87                                                      
REMARK 465     THR C    88                                                      
REMARK 465     GLU C    89                                                      
REMARK 465     PRO C   204                                                      
REMARK 465     SER C   205                                                      
REMARK 465     MET C   206                                                      
REMARK 465     ARG C   207                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LBM A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LBM C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 304                  
DBREF  6O0L A    1    75  UNP    P10415   BCL2_HUMAN       1     34             
DBREF  6O0L A   76    91  UNP    Q07817   B2CL1_HUMAN     29     44             
DBREF  6O0L A   92   207  UNP    P10415   BCL2_HUMAN      92    207             
DBREF  6O0L C    1    75  UNP    P10415   BCL2_HUMAN       1     34             
DBREF  6O0L C   76    91  UNP    Q07817   B2CL1_HUMAN     29     44             
DBREF  6O0L C   92   207  UNP    P10415   BCL2_HUMAN      92    207             
SEQADV 6O0L VAL A  101  UNP  P10415    GLY   101 ENGINEERED MUTATION            
SEQADV 6O0L VAL C  101  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    LBM  A 301      61                                                       
HET    PEG  A 302       7                                                       
HET    PEG  A 303       7                                                       
HET     CL  A 304       1                                                       
HET    LBM  C 301      61                                                       
HET    PEG  C 302       7                                                       
HET    PEG  C 303       7                                                       
HET     CL  C 304       1                                                       
HETNAM     LBM 4-{4-[(4'-CHLORO-5,5-DIMETHYL[3,4,5,6-TETRAHYDRO[1,1'-           
HETNAM   2 LBM  BIPHENYL]]-2-YL)METHYL]PIPERAZIN-1-YL}-N-[(3-NITRO-4-           
HETNAM   3 LBM  {[(OXAN-4-YL)METHYL]AMINO}PHENYL)SULFONYL]-2-[(1H-              
HETNAM   4 LBM  PYRROLO[2,3-B]PYRIDIN-5-YL)OXY]BENZAMIDE                        
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM      CL CHLORIDE ION                                                     
HETSYN     LBM VENETOCLAX, 2-((1H-PYRROLO[2,3-B]PYRIDIN-5-YL)OXY)-4-            
HETSYN   2 LBM  (4-((4'-CHLORO-5,5-DIMETHYL-3,4,5,6-TETRAHYDRO-[1,1'-           
HETSYN   3 LBM  BIPHENYL]-2-YL)METHYL)PIPERAZIN-1-YL)-N-((3-NITRO-4-            
HETSYN   4 LBM  (((TETRAHYDRO-2H-PYRAN-4-YL)METHYL)AMINO)PHENYL)                
HETSYN   5 LBM  SULFONYL)BENZAMIDE                                              
FORMUL   3  LBM    2(C45 H50 CL N7 O7 S)                                        
FORMUL   4  PEG    4(C4 H10 O3)                                                 
FORMUL   6   CL    2(CL 1-)                                                     
FORMUL  11  HOH   *22(H2 O)                                                     
HELIX    1 AA1 ASP A   10  GLN A   25  1                                  16    
HELIX    2 AA2 GLU A   91  TYR A  108  1                                  18    
HELIX    3 AA3 TYR A  108  GLN A  118  1                                  11    
HELIX    4 AA4 THR A  125  PHE A  138  1                                  14    
HELIX    5 AA5 ASN A  143  ARG A  164  1                                  22    
HELIX    6 AA6 SER A  167  HIS A  184  1                                  18    
HELIX    7 AA7 LEU A  185  ASN A  192  1                                   8    
HELIX    8 AA8 GLY A  193  GLY A  203  1                                  11    
HELIX    9 AA9 ASP C   10  GLN C   25  1                                  16    
HELIX   10 AB1 GLU C   91  TYR C  108  1                                  18    
HELIX   11 AB2 TYR C  108  GLN C  118  1                                  11    
HELIX   12 AB3 THR C  125  PHE C  138  1                                  14    
HELIX   13 AB4 ASN C  143  ARG C  164  1                                  22    
HELIX   14 AB5 SER C  167  HIS C  184  1                                  18    
HELIX   15 AB6 LEU C  185  ASN C  192  1                                   8    
HELIX   16 AB7 GLY C  193  GLY C  203  1                                  11    
SITE     1 AC1 17 ARG A  12  ALA A 100  ASP A 103  ARG A 107                    
SITE     2 AC1 17 TYR A 108  LEU A 137  TRP A 144  GLY A 145                    
SITE     3 AC1 17 VAL A 148  ALA A 149  GLU A 152  PHE A 153                    
SITE     4 AC1 17 VAL A 156  PHE A 198  TYR A 202  PEG A 303                    
SITE     5 AC1 17 HOH A 403                                                     
SITE     1 AC2  3 ARG A  12  MET A  16  PEG A 303                               
SITE     1 AC3  5 ASN A 143  THR A 178  LBM A 301  PEG A 302                    
SITE     2 AC3  5  CL A 304                                                     
SITE     1 AC4  4 GLU A 179  ASN A 182  ARG A 183  PEG A 303                    
SITE     1 AC5 19 ARG C  12  ALA C 100  ASP C 103  ARG C 107                    
SITE     2 AC5 19 TYR C 108  GLU C 136  LEU C 137  TRP C 144                    
SITE     3 AC5 19 GLY C 145  VAL C 148  ALA C 149  GLU C 152                    
SITE     4 AC5 19 PHE C 153  VAL C 156  PHE C 198  TYR C 202                    
SITE     5 AC5 19 PEG C 303  HOH C 401  HOH C 404                               
SITE     1 AC6  2 ARG C  12  PEG C 303                                          
SITE     1 AC7  6 ARG C  12  ASN C 143  ARG C 146  LBM C 301                    
SITE     2 AC7  6 PEG C 302   CL C 304                                          
SITE     1 AC8  4 GLU C 179  ASN C 182  ARG C 183  PEG C 303                    
CRYST1   33.147   82.005   47.508  90.00  90.08  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      0.030169  0.000000  0.000043        0.00000                         
SCALE2      0.000000  0.012194  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021049        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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