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Database: PDB
Entry: 6O0M
LinkDB: 6O0M
Original site: 6O0M 
HEADER    APOPTOSIS                               16-FEB-19   6O0M              
TITLE     CRYSTAL STRUCTURE OF BCL-2 F104L 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;                                                            
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, 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 6O0M    1       REMARK HETSYN LINK                       
REVDAT   4   20-NOV-19 6O0M    1       COMPND HETNAM FORMUL                     
REVDAT   3   10-JUL-19 6O0M    1       COMPND SOURCE REMARK DBREF               
REVDAT   3 2                   1       SEQADV LINK                              
REVDAT   2   19-JUN-19 6O0M    1       JRNL                                     
REVDAT   1   22-MAY-19 6O0M    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.    1.75 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) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.90                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 15011                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 743                             
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 43.9137 -  2.9923    1.00     3007   159  0.1685 0.2110        
REMARK   3     2  2.9923 -  2.3751    1.00     2863   147  0.1654 0.2156        
REMARK   3     3  2.3751 -  2.0749    1.00     2815   153  0.1582 0.1857        
REMARK   3     4  2.0749 -  1.8852    1.00     2812   142  0.1742 0.2467        
REMARK   3     5  1.8852 -  1.7501    0.99     2771   142  0.2529 0.3062        
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)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.000           
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           1475                                  
REMARK   3   ANGLE     :  0.714           2009                                  
REMARK   3   CHIRALITY :  0.040            188                                  
REMARK   3   PLANARITY :  0.004            325                                  
REMARK   3   DIHEDRAL  : 19.029            898                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 164 THROUGH 203 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.4957   7.0503  -7.4584              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1304 T22:   0.1097                                     
REMARK   3      T33:   0.1105 T12:   0.0090                                     
REMARK   3      T13:  -0.0165 T23:  -0.0230                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2290 L22:   1.9376                                     
REMARK   3      L33:   2.1729 L12:  -0.5398                                     
REMARK   3      L13:  -1.3655 L23:   0.7735                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0361 S12:  -0.1392 S13:   0.2142                       
REMARK   3      S21:   0.0424 S22:   0.0457 S23:  -0.1879                       
REMARK   3      S31:   0.0038 S32:   0.1117 S33:  -0.0696                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 8 THROUGH 90 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   2.8167  -4.4824  -8.3853              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1295 T22:   0.1050                                     
REMARK   3      T33:   0.1527 T12:   0.0067                                     
REMARK   3      T13:  -0.0066 T23:   0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5855 L22:   5.8176                                     
REMARK   3      L33:   4.9175 L12:   0.9510                                     
REMARK   3      L13:   0.5289 L23:   2.4881                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0088 S12:  -0.1715 S13:  -0.1310                       
REMARK   3      S21:   0.3528 S22:   0.0310 S23:  -0.1189                       
REMARK   3      S31:   0.3186 S32:   0.0645 S33:   0.0143                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 91 THROUGH 107 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.9229  -4.8194  -3.8582              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2055 T22:   0.1388                                     
REMARK   3      T33:   0.1859 T12:   0.0134                                     
REMARK   3      T13:   0.0142 T23:   0.0208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.1962 L22:   3.0720                                     
REMARK   3      L33:   5.6952 L12:  -0.7920                                     
REMARK   3      L13:   1.3280 L23:  -0.2208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0463 S12:  -0.2401 S13:  -0.3943                       
REMARK   3      S21:   0.3111 S22:   0.0451 S23:  -0.1101                       
REMARK   3      S31:   0.3241 S32:   0.1238 S33:  -0.2103                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 108 THROUGH 118 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.5727  -3.3672 -21.0642              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2813 T22:   0.2923                                     
REMARK   3      T33:   0.2367 T12:  -0.0151                                     
REMARK   3      T13:  -0.0395 T23:  -0.0370                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.3725 L22:   6.9987                                     
REMARK   3      L33:   6.3188 L12:  -0.0511                                     
REMARK   3      L13:  -2.7719 L23:   5.1893                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3351 S12:   1.0312 S13:   0.0055                       
REMARK   3      S21:  -0.6525 S22:   0.2655 S23:   0.1932                       
REMARK   3      S31:  -0.3209 S32:  -0.2464 S33:   0.0878                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 119 THROUGH 163 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.2772   5.1678 -17.7190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1501 T22:   0.0884                                     
REMARK   3      T33:   0.1250 T12:   0.0099                                     
REMARK   3      T13:  -0.0142 T23:   0.0112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5912 L22:   2.9757                                     
REMARK   3      L33:   2.7116 L12:  -0.3854                                     
REMARK   3      L13:  -0.8369 L23:   0.3321                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1556 S12:   0.2559 S13:   0.1589                       
REMARK   3      S21:  -0.2809 S22:  -0.0706 S23:  -0.0868                       
REMARK   3      S31:  -0.0475 S32:  -0.1369 S33:  -0.0420                       
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 6O0M 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_1000239800.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-NOV-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
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                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15022                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.580                              
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   (%): 33.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG4K, 40% PEG400, 0.1M MES PH 6.0,   
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 291K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       16.84500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.90000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.13500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       43.90000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.84500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       24.13500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 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     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 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  91    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   OH   TYR A    18     OE2  GLU A   152              2.15            
REMARK 500   OH   TYR A     9     OD1  ASP A   196              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CE   MET A    16     O1   PEG A   303     1655     1.38            
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 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 PEG A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 305                 
DBREF  6O0M A    1    34  UNP    P10415   BCL2_HUMAN       1     34             
DBREF  6O0M A   76    91  UNP    Q07817   B2CL1_HUMAN     29     44             
DBREF  6O0M A   92   207  UNP    P10415   BCL2_HUMAN      92    207             
SEQADV 6O0M LEU A  104  UNP  P10415    PHE   104 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 GLY ASP ASP LEU 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                      
HET    LBM  A 301     122                                                       
HET    PEG  A 302       7                                                       
HET    PEG  A 303       7                                                       
HET    PEG  A 304       7                                                       
HET    PEG  A 305       7                                                       
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                                            
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   2  LBM    C45 H50 CL N7 O7 S                                           
FORMUL   3  PEG    4(C4 H10 O3)                                                 
FORMUL   7  HOH   *86(H2 O)                                                     
HELIX    1 AA1 ASP A   10  ARG A   26  1                                  17    
HELIX    2 AA2 TRP A   30  ASP A   34  5                                   5    
HELIX    3 AA3 GLU A   91  TYR A  108  1                                  18    
HELIX    4 AA4 TYR A  108  LEU A  119  1                                  12    
HELIX    5 AA5 THR A  125  PHE A  138  1                                  14    
HELIX    6 AA6 ASN A  143  ARG A  164  1                                  22    
HELIX    7 AA7 SER A  167  HIS A  184  1                                  18    
HELIX    8 AA8 LEU A  185  ASN A  192  1                                   8    
HELIX    9 AA9 GLY A  193  GLY A  203  1                                  11    
SITE     1 AC1 24 ARG A  12  ALA A 100  ASP A 103  LEU A 104                    
SITE     2 AC1 24 ARG A 107  PHE A 112  MET A 115  GLU A 136                    
SITE     3 AC1 24 ASN A 143  TRP A 144  GLY A 145  VAL A 148                    
SITE     4 AC1 24 ALA A 149  GLU A 152  PHE A 153  VAL A 156                    
SITE     5 AC1 24 GLN A 190  PHE A 198  TYR A 202  PEG A 302                    
SITE     6 AC1 24 PEG A 305  HOH A 405  HOH A 446  HOH A 458                    
SITE     1 AC2  3 TYR A 108  LBM A 301  PEG A 303                               
SITE     1 AC3  8 ARG A  12  MET A  16  ALA A 174  LEU A 175                    
SITE     2 AC3  8 THR A 178  PEG A 302  HOH A 423  HOH A 433                    
SITE     1 AC4  6 ARG A 127  PHE A 130  ASN A 163  TRP A 176                    
SITE     2 AC4  6 TYR A 180  HOH A 439                                          
SITE     1 AC5  4 ARG A  12  ASP A 191  LBM A 301  HOH A 409                    
CRYST1   33.690   48.270   87.800  90.00  90.00  90.00 P 21 21 21    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      0.029683  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.020717  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011390        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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