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Database: PDB
Entry: 5VWV
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HEADER    APOPTOSIS                               23-MAY-17   5VWV              
TITLE     BAK CORE LATCH DIMER IN COMPLEX WITH BIM-BH3 - CUBIC                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BCL-2 HOMOLOGOUS ANTAGONIST/KILLER;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 23-186;                                       
COMPND   5 SYNONYM: APOPTOSIS REGULATOR BAK,BCL-2-LIKE PROTEIN 7,BCL2-L-7;      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: BCL-2-LIKE PROTEIN 11;                                     
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 141-165;                                      
COMPND  12 SYNONYM: BCL2-L-11,BCL2-INTERACTING MEDIATOR OF CELL DEATH;          
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 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: BAK1, BAK, BCL2L7, CDN1;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    APOPTOSIS, BCL-2 FAMILY, ACTIVATOR                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.BROUWER,P.M.COLMAN,P.E.CZABOTAR                                   
REVDAT   2   29-NOV-17 5VWV    1       JRNL                                     
REVDAT   1   15-NOV-17 5VWV    0                                                
JRNL        AUTH   J.M.BROUWER,P.LAN,A.D.COWAN,J.P.BERNARDINI,R.W.BIRKINSHAW,   
JRNL        AUTH 2 M.F.VAN DELFT,B.E.SLEEBS,A.Y.ROBIN,A.WARDAK,I.K.TAN,         
JRNL        AUTH 3 B.RELJIC,E.F.LEE,W.D.FAIRLIE,M.J.CALL,B.J.SMITH,G.DEWSON,    
JRNL        AUTH 4 G.LESSENE,P.M.COLMAN,P.E.CZABOTAR                            
JRNL        TITL   CONVERSION OF BIM-BH3 FROM ACTIVATOR TO INHIBITOR OF BAK     
JRNL        TITL 2 THROUGH STRUCTURE-BASED DESIGN.                              
JRNL        REF    MOL. CELL                     V.  68   659 2017              
JRNL        REFN                   ISSN 1097-4164                               
JRNL        PMID   29149594                                                     
JRNL        DOI    10.1016/J.MOLCEL.2017.11.001                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.03                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 37157                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.158                           
REMARK   3   R VALUE            (WORKING SET) : 0.157                           
REMARK   3   FREE R VALUE                     : 0.177                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.370                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1996                            
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 42.0422 -  4.5712    1.00     2757   155  0.1617 0.1678        
REMARK   3     2  4.5712 -  3.6289    1.00     2580   147  0.1297 0.1608        
REMARK   3     3  3.6289 -  3.1704    1.00     2539   144  0.1363 0.1501        
REMARK   3     4  3.1704 -  2.8806    1.00     2540   144  0.1513 0.1681        
REMARK   3     5  2.8806 -  2.6742    1.00     2493   142  0.1448 0.1766        
REMARK   3     6  2.6742 -  2.5165    1.00     2493   142  0.1507 0.1806        
REMARK   3     7  2.5165 -  2.3905    1.00     2487   141  0.1514 0.1808        
REMARK   3     8  2.3905 -  2.2864    1.00     2492   142  0.1562 0.1532        
REMARK   3     9  2.2864 -  2.1984    1.00     2466   140  0.1590 0.1600        
REMARK   3    10  2.1984 -  2.1226    1.00     2471   141  0.1680 0.2251        
REMARK   3    11  2.1226 -  2.0562    1.00     2465   139  0.2073 0.2276        
REMARK   3    12  2.0562 -  1.9974    1.00     2461   141  0.2265 0.2853        
REMARK   3    13  1.9974 -  1.9448    1.00     2455   139  0.2478 0.2693        
REMARK   3    14  1.9448 -  1.8974    1.00     2462   139  0.2904 0.3014        
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)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.300           
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      :  0.007           1625                                  
REMARK   3   ANGLE     :  0.755           2188                                  
REMARK   3   CHIRALITY :  0.048            228                                  
REMARK   3   PLANARITY :  0.005            289                                  
REMARK   3   DIHEDRAL  : 20.589            950                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 17 THROUGH 23 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  15.6169   9.7950 136.4117              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7751 T22:   0.7773                                     
REMARK   3      T33:   1.1269 T12:   0.2218                                     
REMARK   3      T13:   0.2172 T23:  -0.0410                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9887 L22:   2.2619                                     
REMARK   3      L33:   7.0027 L12:  -3.1134                                     
REMARK   3      L13:   0.6024 L23:  -1.2057                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4618 S12:   0.8847 S13:  -2.1062                       
REMARK   3      S21:  -0.7168 S22:  -0.9307 S23:  -0.8246                       
REMARK   3      S31:   1.4837 S32:   1.7299 S33:   1.3274                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 24 THROUGH 53 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  13.7285  28.9185 146.0283              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1381 T22:   0.2280                                     
REMARK   3      T33:   0.2349 T12:   0.0702                                     
REMARK   3      T13:   0.0251 T23:  -0.0201                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1759 L22:   2.0345                                     
REMARK   3      L33:   5.1595 L12:   2.9422                                     
REMARK   3      L13:   0.5678 L23:   2.0663                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1957 S12:  -0.0660 S13:   0.0216                       
REMARK   3      S21:   0.3056 S22:  -0.1980 S23:  -0.0320                       
REMARK   3      S31:   0.0897 S32:  -0.1260 S33:   0.0700                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 54 THROUGH 69 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  15.1640  30.2519 152.5410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2436 T22:   0.2941                                     
REMARK   3      T33:   0.2936 T12:   0.0297                                     
REMARK   3      T13:   0.0077 T23:  -0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3490 L22:   4.6191                                     
REMARK   3      L33:   2.6544 L12:  -3.6880                                     
REMARK   3      L13:  -1.6245 L23:   2.0571                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0865 S12:  -0.2024 S13:  -0.1272                       
REMARK   3      S21:   0.2441 S22:   0.0019 S23:   0.0393                       
REMARK   3      S31:   0.1754 S32:   0.2756 S33:   0.0781                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 70 THROUGH 100 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1958  36.5061 138.7494              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2309 T22:   0.2558                                     
REMARK   3      T33:   0.2673 T12:  -0.0047                                     
REMARK   3      T13:   0.0299 T23:  -0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0554 L22:   4.1541                                     
REMARK   3      L33:   1.4889 L12:  -5.1461                                     
REMARK   3      L13:   0.1596 L23:  -1.0107                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2469 S12:   0.4924 S13:   0.7712                       
REMARK   3      S21:  -0.2376 S22:  -0.2490 S23:  -0.5009                       
REMARK   3      S31:  -0.1269 S32:   0.1273 S33:  -0.0133                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 101 THROUGH 149 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0080  32.7051 141.0201              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1652 T22:   0.2087                                     
REMARK   3      T33:   0.1961 T12:   0.0449                                     
REMARK   3      T13:  -0.0085 T23:   0.0360                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0803 L22:   2.4873                                     
REMARK   3      L33:   3.1949 L12:  -1.1416                                     
REMARK   3      L13:  -1.0213 L23:   1.3249                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1047 S12:   0.3995 S13:  -0.0513                       
REMARK   3      S21:  -0.1335 S22:  -0.1019 S23:   0.1391                       
REMARK   3      S31:  -0.0442 S32:  -0.2234 S33:   0.0099                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 150 THROUGH 164 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.5963  36.0408 167.9171              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2626 T22:   0.2046                                     
REMARK   3      T33:   0.2751 T12:  -0.0258                                     
REMARK   3      T13:   0.0072 T23:  -0.0241                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.8232 L22:   6.1405                                     
REMARK   3      L33:   4.8485 L12:   1.0417                                     
REMARK   3      L13:  -6.4034 L23:  -1.6311                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0965 S12:   0.1431 S13:  -0.4133                       
REMARK   3      S21:   0.0800 S22:  -0.1358 S23:   0.4535                       
REMARK   3      S31:   0.7188 S32:  -0.4790 S33:   0.1371                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 165 THROUGH 186 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.6273  46.7169 179.9949              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2998 T22:   0.3045                                     
REMARK   3      T33:   0.3040 T12:   0.0253                                     
REMARK   3      T13:   0.1322 T23:  -0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0596 L22:   6.0825                                     
REMARK   3      L33:   2.7941 L12:  -0.8287                                     
REMARK   3      L13:   0.1264 L23:   1.4339                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0873 S12:  -0.2852 S13:   0.0401                       
REMARK   3      S21:   0.7324 S22:   0.0219 S23:   0.6576                       
REMARK   3      S31:   0.0403 S32:  -0.3116 S33:   0.0517                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 141 THROUGH 165 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.7163  34.5216 129.5200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3563 T22:   0.5424                                     
REMARK   3      T33:   0.2565 T12:   0.0376                                     
REMARK   3      T13:   0.0399 T23:   0.0698                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5166 L22:   7.5706                                     
REMARK   3      L33:   5.6249 L12:  -5.6378                                     
REMARK   3      L13:  -5.1318 L23:   4.3763                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5855 S12:   1.0716 S13:   0.4984                       
REMARK   3      S21:  -0.9585 S22:  -0.3335 S23:  -0.3949                       
REMARK   3      S31:  -0.2365 S32:   0.1013 S33:  -0.2228                       
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 5VWV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227122.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JUL-14                          
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                  : ADSC QUANTUM 315R                  
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37157                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.897                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.032                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 47.80                              
REMARK 200  R MERGE                    (I) : 0.21620                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.2600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 47.00                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.480                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 75.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18 % GLYCEROL, 21.6 % PEG (POLY          
REMARK 280  -ETHYLENE GLYCOL) 1500 AND 0.5 % ETHYL ACETATE, VAPOR DIFFUSION,    
REMARK 280  SITTING DROP, TEMPERATURE 281K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 3 2                         
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       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290      13555   Y+3/4,X+1/4,-Z+1/4                                      
REMARK 290      14555   -Y+3/4,-X+3/4,-Z+3/4                                    
REMARK 290      15555   Y+1/4,-X+1/4,Z+3/4                                      
REMARK 290      16555   -Y+1/4,X+3/4,Z+1/4                                      
REMARK 290      17555   X+3/4,Z+1/4,-Y+1/4                                      
REMARK 290      18555   -X+1/4,Z+3/4,Y+1/4                                      
REMARK 290      19555   -X+3/4,-Z+3/4,-Y+3/4                                    
REMARK 290      20555   X+1/4,-Z+1/4,Y+3/4                                      
REMARK 290      21555   Z+3/4,Y+1/4,-X+1/4                                      
REMARK 290      22555   Z+1/4,-Y+1/4,X+3/4                                      
REMARK 290      23555   -Z+1/4,Y+3/4,X+1/4                                      
REMARK 290      24555   -Z+3/4,-Y+3/4,-X+3/4                                    
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       69.70200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.70200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       69.70200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.70200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       69.70200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       69.70200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       69.70200            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       69.70200            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       69.70200            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       69.70200            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       69.70200            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       69.70200            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       69.70200            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       69.70200            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       69.70200            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       69.70200            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       69.70200            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       69.70200            
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000      104.55300            
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000       34.85100            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       34.85100            
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000      104.55300            
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000      104.55300            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      104.55300            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       34.85100            
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000       34.85100            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      104.55300            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       34.85100            
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000      104.55300            
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000       34.85100            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000      104.55300            
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000       34.85100            
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000       34.85100            
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000       34.85100            
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000      104.55300            
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000       34.85100            
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000      104.55300            
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000      104.55300            
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000      104.55300            
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000       34.85100            
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000       34.85100            
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000      104.55300            
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000      104.55300            
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000       34.85100            
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000       34.85100            
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000       34.85100            
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000       34.85100            
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000      104.55300            
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000       34.85100            
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000      104.55300            
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000       34.85100            
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000      104.55300            
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000      104.55300            
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000      104.55300            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14470 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 17470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -112.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000      -34.85100            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000       34.85100            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       34.85100            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 437  LIES ON A SPECIAL POSITION.                          
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   O    HOH A   336     O    HOH A   415    13455     2.18            
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    ASP A  83      -70.67    -44.23                                   
REMARK 500    ALA B 164       66.36   -108.82                                   
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 TFA A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 208                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 201                 
DBREF  5VWV A   23   186  UNP    Q16611   BAK_HUMAN       23    186             
DBREF  5VWV B  141   165  UNP    O43521   B2L11_HUMAN    141    165             
SEQADV 5VWV GLY A   17  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWV PRO A   18  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWV LEU A   19  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWV GLY A   20  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWV SER A   21  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWV MET A   22  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWV SER A  166  UNP  Q16611    CYS   166 ENGINEERED MUTATION            
SEQADV 5VWV ARG B  147  UNP  O43521    TRP   147 ENGINEERED MUTATION            
SEQADV 5VWV THR B  162  UNP  O43521    TYR   162 ENGINEERED MUTATION            
SEQRES   1 A  170  GLY PRO LEU GLY SER MET SER GLU GLU GLN VAL ALA GLN          
SEQRES   2 A  170  ASP THR GLU GLU VAL PHE ARG SER TYR VAL PHE TYR ARG          
SEQRES   3 A  170  HIS GLN GLN GLU GLN GLU ALA GLU GLY VAL ALA ALA PRO          
SEQRES   4 A  170  ALA ASP PRO GLU MET VAL THR LEU PRO LEU GLN PRO SER          
SEQRES   5 A  170  SER THR MET GLY GLN VAL GLY ARG GLN LEU ALA ILE ILE          
SEQRES   6 A  170  GLY ASP ASP ILE ASN ARG ARG TYR ASP SER GLU PHE GLN          
SEQRES   7 A  170  THR MET LEU GLN HIS LEU GLN PRO THR ALA GLU ASN ALA          
SEQRES   8 A  170  TYR GLU TYR PHE THR LYS ILE ALA THR SER LEU PHE GLU          
SEQRES   9 A  170  SER GLY ILE ASN TRP GLY ARG VAL VAL ALA LEU LEU GLY          
SEQRES  10 A  170  PHE GLY TYR ARG LEU ALA LEU HIS VAL TYR GLN HIS GLY          
SEQRES  11 A  170  LEU THR GLY PHE LEU GLY GLN VAL THR ARG PHE VAL VAL          
SEQRES  12 A  170  ASP PHE MET LEU HIS HIS SER ILE ALA ARG TRP ILE ALA          
SEQRES  13 A  170  GLN ARG GLY GLY TRP VAL ALA ALA LEU ASN LEU GLY ASN          
SEQRES  14 A  170  GLY                                                          
SEQRES   1 B   25  ASP MET ARG PRO GLU ILE ARG ILE ALA GLN GLU LEU ARG          
SEQRES   2 B   25  ARG ILE GLY ASP GLU PHE ASN ALA THR TYR ALA ARG              
HET    TFA  A 201       7                                                       
HET    EDO  A 202      10                                                       
HET    EDO  A 203      10                                                       
HET    EDO  A 204      10                                                       
HET    EDO  A 205      10                                                       
HET    EDO  A 206      10                                                       
HET     CL  A 207       1                                                       
HET    GOL  A 208      14                                                       
HET    EDO  B 201      10                                                       
HETNAM     TFA TRIFLUOROACETIC ACID                                             
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  TFA    C2 H F3 O2                                                   
FORMUL   4  EDO    6(C2 H6 O2)                                                  
FORMUL   9   CL    CL 1-                                                        
FORMUL  10  GOL    C3 H8 O3                                                     
FORMUL  12  HOH   *186(H2 O)                                                    
HELIX    1 AA1 SER A   23  GLY A   51  1                                  29    
HELIX    2 AA2 VAL A   52  ALA A   54  5                                   3    
HELIX    3 AA3 ASP A   57  VAL A   61  5                                   5    
HELIX    4 AA4 SER A   69  ARG A   88  1                                  20    
HELIX    5 AA5 TYR A   89  GLN A  101  1                                  13    
HELIX    6 AA6 ASN A  106  GLU A  120  1                                  15    
HELIX    7 AA7 ASN A  124  HIS A  145  1                                  22    
HELIX    8 AA8 GLY A  149  HIS A  165  1                                  17    
HELIX    9 AA9 SER A  166  ARG A  174  1                                   9    
HELIX   10 AB1 GLY A  175  LEU A  183  5                                   9    
HELIX   11 AB2 ARG B  143  ALA B  164  1                                  22    
SITE     1 AC1  8 ARG A  42  ASN A  86  PHE A  93  GLY A 133                    
SITE     2 AC1  8 ARG A 137  HOH A 313  LEU B 152  ILE B 155                    
SITE     1 AC2  2 GLU A  92  ARG B 147                                          
SITE     1 AC3  2 GLU A 105  ASN A 185                                          
SITE     1 AC4  2 ILE A 123  ASN A 124                                          
SITE     1 AC5  7 GLN A  44  GLU A  48  ARG A  76  HIS A  99                    
SITE     2 AC5  7 GLN A 101  EDO A 206  HOH A 390                               
SITE     1 AC6  3 GLN A  44  GLN A 101  EDO A 205                               
SITE     1 AC7  3 HIS A  99  ARG B 147  HOH B 308                               
SITE     1 AC8  6 GLN A  94  LEU A  97  ARG A 137  HIS A 141                    
SITE     2 AC8  6 GLN A 144  HOH A 303                                          
SITE     1 AC9  3 ALA A 179  LEU A 183  ARG B 165                               
CRYST1  139.404  139.404  139.404  90.00  90.00  90.00 P 41 3 2     24          
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      0.007173  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007173  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007173        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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