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Database: PDB
Entry: 5VWW
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Original site: 5VWW 
HEADER    APOPTOSIS                               23-MAY-17   5VWW              
TITLE     BAK CORE LATCH DIMER IN COMPLEX WITH BIM-RT - TETRAGONAL              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BCL-2 HOMOLOGOUS ANTAGONIST/KILLER;                        
COMPND   3 CHAIN: A, B;                                                         
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: C, D;                                                         
COMPND  11 FRAGMENT: UNP RESIDUES 141-166;                                      
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 5VWW    1       JRNL                                     
REVDAT   1   15-NOV-17 5VWW    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.    2.80 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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 9611                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.020                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 963                             
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 39.8848 -  5.3566    1.00     1338   150  0.2089 0.2536        
REMARK   3     2  5.3566 -  4.2533    1.00     1255   142  0.2074 0.2617        
REMARK   3     3  4.2533 -  3.7161    1.00     1231   133  0.2152 0.3210        
REMARK   3     4  3.7161 -  3.3765    1.00     1215   142  0.2268 0.2898        
REMARK   3     5  3.3765 -  3.1346    1.00     1219   128  0.2623 0.3015        
REMARK   3     6  3.1346 -  2.9498    1.00     1201   136  0.2913 0.3365        
REMARK   3     7  2.9498 -  2.8022    0.99     1189   132  0.3055 0.3203        
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)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.040           
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           2784                                  
REMARK   3   ANGLE     :  0.424           3753                                  
REMARK   3   CHIRALITY :  0.035            393                                  
REMARK   3   PLANARITY :  0.002            489                                  
REMARK   3   DIHEDRAL  : 16.112           1612                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 19 THROUGH 48 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -25.9569  14.7226 -18.8623              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5702 T22:   0.5362                                     
REMARK   3      T33:   0.6490 T12:  -0.1305                                     
REMARK   3      T13:  -0.0640 T23:  -0.0594                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7080 L22:   6.4679                                     
REMARK   3      L33:   3.8005 L12:  -1.3193                                     
REMARK   3      L13:   4.4407 L23:  -1.9833                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4615 S12:  -0.2796 S13:   0.8485                       
REMARK   3      S21:   0.4019 S22:  -0.2922 S23:  -0.5573                       
REMARK   3      S31:  -2.4833 S32:   1.1994 S33:   0.5328                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 49 THROUGH 69 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -30.4193  20.1650  -9.3309              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6491 T22:   1.2876                                     
REMARK   3      T33:   2.1240 T12:  -0.1466                                     
REMARK   3      T13:  -0.1814 T23:   0.5875                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5441 L22:   9.5269                                     
REMARK   3      L33:   8.0998 L12:  -2.1670                                     
REMARK   3      L13:  -2.2011 L23:   8.4831                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.1370 S12:  -0.9308 S13:   0.6266                       
REMARK   3      S21:  -0.4705 S22:  -0.5174 S23:  -1.1956                       
REMARK   3      S31:  -1.0281 S32:   0.8411 S33:  -0.6513                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 70 THROUGH 119 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -24.4627   2.4417 -10.9415              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3943 T22:   0.4939                                     
REMARK   3      T33:   0.5357 T12:  -0.0852                                     
REMARK   3      T13:   0.0214 T23:   0.0349                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1038 L22:   6.4495                                     
REMARK   3      L33:   8.9339 L12:  -2.1039                                     
REMARK   3      L13:   2.2043 L23:  -1.9830                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0593 S12:   0.2057 S13:   0.3992                       
REMARK   3      S21:   0.2394 S22:  -0.1040 S23:  -0.4904                       
REMARK   3      S31:  -0.2922 S32:   0.4769 S33:   0.1098                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 120 THROUGH 173 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.6058   9.1624  -3.2388              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7620 T22:   0.6519                                     
REMARK   3      T33:   0.7269 T12:  -0.0603                                     
REMARK   3      T13:  -0.3291 T23:   0.0980                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5826 L22:   3.9924                                     
REMARK   3      L33:   7.0781 L12:   1.5028                                     
REMARK   3      L13:   4.3543 L23:   1.6863                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4309 S12:  -0.1435 S13:  -0.2729                       
REMARK   3      S21:   1.2367 S22:  -0.2725 S23:  -1.2976                       
REMARK   3      S31:   0.3880 S32:   0.5322 S33:  -0.2168                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 174 THROUGH 181 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   9.4253  15.8368  20.8009              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.1919 T22:   2.6173                                     
REMARK   3      T33:   1.7438 T12:   0.1695                                     
REMARK   3      T13:  -2.3670 T23:  -0.0556                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5705 L22:   1.3826                                     
REMARK   3      L33:   1.5001 L12:  -0.8886                                     
REMARK   3      L13:   0.9294 L23:  -1.4449                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2674 S12:  -1.1579 S13:   0.2069                       
REMARK   3      S21:   0.0552 S22:  -0.2996 S23:  -0.0929                       
REMARK   3      S31:  -0.7012 S32:   0.4668 S33:  -0.6354                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 23 THROUGH 69 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   0.7116  10.7348  13.2905              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1561 T22:   2.2834                                     
REMARK   3      T33:   1.0134 T12:  -0.4473                                     
REMARK   3      T13:  -0.5403 T23:   0.1043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9908 L22:   7.0937                                     
REMARK   3      L33:   8.1069 L12:   4.9666                                     
REMARK   3      L13:  -6.7606 L23:  -2.1048                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1038 S12:  -3.4908 S13:  -2.3384                       
REMARK   3      S21:   1.2578 S22:  -0.8688 S23:  -1.1226                       
REMARK   3      S31:   1.5055 S32:  -0.6903 S33:   0.4959                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 70 THROUGH 100 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.4987  24.1685  11.6269              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7742 T22:   1.6983                                     
REMARK   3      T33:   1.5659 T12:   0.0150                                     
REMARK   3      T13:  -0.5597 T23:  -0.2478                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5186 L22:   6.2364                                     
REMARK   3      L33:   0.9689 L12:  -3.3447                                     
REMARK   3      L13:  -2.4567 L23:   2.0723                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8039 S12:  -2.1683 S13:   1.2921                       
REMARK   3      S21:   0.8479 S22:   0.6273 S23:   0.1933                       
REMARK   3      S31:   1.0400 S32:  -0.4774 S33:  -0.7955                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 101 THROUGH 124 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.2727  24.1834  -0.0790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3658 T22:   1.1717                                     
REMARK   3      T33:   2.5870 T12:  -0.0239                                     
REMARK   3      T13:  -0.7442 T23:   0.1216                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1416 L22:   4.7247                                     
REMARK   3      L33:   2.1426 L12:  -2.7285                                     
REMARK   3      L13:   1.0457 L23:  -2.3769                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6597 S12:   0.1427 S13:   1.8241                       
REMARK   3      S21:   0.3177 S22:  -0.6933 S23:  -2.1173                       
REMARK   3      S31:  -1.5226 S32:   1.3190 S33:   1.2845                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 125 THROUGH 185 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.5909  12.7676 -12.5939              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6088 T22:   0.6419                                     
REMARK   3      T33:   0.7043 T12:  -0.1356                                     
REMARK   3      T13:  -0.1025 T23:   0.0622                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.0948 L22:   3.2240                                     
REMARK   3      L33:   6.8143 L12:   0.4265                                     
REMARK   3      L13:   6.8232 L23:   0.8380                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4030 S12:  -0.2569 S13:   0.7834                       
REMARK   3      S21:   0.0859 S22:  -0.1002 S23:  -0.7754                       
REMARK   3      S31:  -0.8154 S32:   0.4078 S33:   0.4116                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 142 THROUGH 166 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -31.9216  -4.6896 -14.7045              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6361 T22:   0.6404                                     
REMARK   3      T33:   0.5582 T12:   0.1066                                     
REMARK   3      T13:   0.0262 T23:  -0.0524                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7087 L22:   4.6371                                     
REMARK   3      L33:   5.0614 L12:  -4.6881                                     
REMARK   3      L13:   4.8539 L23:  -4.6889                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5146 S12:   0.1683 S13:  -0.7854                       
REMARK   3      S21:  -0.2106 S22:  -0.2614 S23:   0.9063                       
REMARK   3      S31:   0.0557 S32:  -0.0597 S33:  -0.4109                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 143 THROUGH 161 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   2.6823  32.8794   7.5024              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4765 T22:   1.4113                                     
REMARK   3      T33:   2.5743 T12:  -0.0373                                     
REMARK   3      T13:  -0.5178 T23:  -0.6663                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7166 L22:   3.5630                                     
REMARK   3      L33:   8.2634 L12:  -0.4335                                     
REMARK   3      L13:   3.6780 L23:  -2.4460                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7409 S12:  -0.2481 S13:   2.2095                       
REMARK   3      S21:   0.6775 S22:   0.2760 S23:  -0.3125                       
REMARK   3      S31:   0.5136 S32:   1.0381 S33:  -0.9038                       
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 5VWW 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_1000227123.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-APR-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                  : NULL                               
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   : 9619                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 14.00                              
REMARK 200  R MERGE                    (I) : 0.11960                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.7700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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   (%): 40.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.5 % MPD (2-METHYL-2,4-PENTANEDIOL),   
REMARK 280  38 MM IMIDAZOLE PH 6.5, 12.5 % PEG 1000, 12.5 % PEG 3350, 30 MM     
REMARK 280  SODIUM FLUORIDE, 30 MM SODIUM IODIDE, 62 MM SODIUM MES PH 6.5       
REMARK 280  AND 30 MM SODIUM BROMIDE, VAPOR DIFFUSION, TEMPERATURE 281K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.73000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       43.89500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       43.89500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       71.59500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       43.89500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       43.89500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       23.86500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       43.89500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.89500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       71.59500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       43.89500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.89500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       23.86500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       47.73000            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10660 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 17340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -126.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    17                                                      
REMARK 465     PRO A    18                                                      
REMARK 465     GLY A    51                                                      
REMARK 465     VAL A    52                                                      
REMARK 465     ALA A    53                                                      
REMARK 465     ALA A    54                                                      
REMARK 465     PRO A    55                                                      
REMARK 465     ALA A    56                                                      
REMARK 465     ASP A    57                                                      
REMARK 465     PRO A    58                                                      
REMARK 465     GLU A    59                                                      
REMARK 465     MET A    60                                                      
REMARK 465     VAL A    61                                                      
REMARK 465     THR A    62                                                      
REMARK 465     LEU A    63                                                      
REMARK 465     PRO A    64                                                      
REMARK 465     LEU A    65                                                      
REMARK 465     GLN A    66                                                      
REMARK 465     ASN A   182                                                      
REMARK 465     LEU A   183                                                      
REMARK 465     GLY A   184                                                      
REMARK 465     ASN A   185                                                      
REMARK 465     GLY A   186                                                      
REMARK 465     GLY B    17                                                      
REMARK 465     PRO B    18                                                      
REMARK 465     LEU B    19                                                      
REMARK 465     GLY B    20                                                      
REMARK 465     SER B    21                                                      
REMARK 465     MET B    22                                                      
REMARK 465     GLU B    46                                                      
REMARK 465     GLN B    47                                                      
REMARK 465     GLU B    48                                                      
REMARK 465     ALA B    49                                                      
REMARK 465     GLU B    50                                                      
REMARK 465     GLY B    51                                                      
REMARK 465     VAL B    52                                                      
REMARK 465     ALA B    53                                                      
REMARK 465     ALA B    54                                                      
REMARK 465     PRO B    55                                                      
REMARK 465     ALA B    56                                                      
REMARK 465     ASP B    57                                                      
REMARK 465     PRO B    58                                                      
REMARK 465     GLU B    59                                                      
REMARK 465     MET B    60                                                      
REMARK 465     VAL B    61                                                      
REMARK 465     THR B    62                                                      
REMARK 465     LEU B    63                                                      
REMARK 465     PRO B    64                                                      
REMARK 465     LEU B    65                                                      
REMARK 465     GLN B    66                                                      
REMARK 465     GLY B   186                                                      
REMARK 465     ASP C   141                                                      
REMARK 465     ASP D   141                                                      
REMARK 465     MET D   142                                                      
REMARK 465     THR D   162                                                      
REMARK 465     TYR D   163                                                      
REMARK 465     ALA D   164                                                      
REMARK 465     ARG D   165                                                      
REMARK 465     ARG D   166                                                      
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   O    TYR A   143     OH   TYR B   143              2.15            
REMARK 500   OH   TYR A   143     O    TYR B   143              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  68      -74.46    -96.31                                   
REMARK 500    SER A 166       13.72     58.13                                   
REMARK 500    SER B 166       14.01     57.32                                   
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 MPD A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BR C 201                  
DBREF  5VWW A   23   186  UNP    Q16611   BAK_HUMAN       23    186             
DBREF  5VWW B   23   186  UNP    Q16611   BAK_HUMAN       23    186             
DBREF  5VWW C  141   166  UNP    O43521   B2L11_HUMAN    141    166             
DBREF  5VWW D  141   166  UNP    O43521   B2L11_HUMAN    141    166             
SEQADV 5VWW GLY A   17  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWW PRO A   18  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWW LEU A   19  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWW GLY A   20  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWW SER A   21  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWW MET A   22  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWW SER A  166  UNP  Q16611    CYS   166 ENGINEERED MUTATION            
SEQADV 5VWW GLY B   17  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWW PRO B   18  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWW LEU B   19  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWW GLY B   20  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWW SER B   21  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWW MET B   22  UNP  Q16611              EXPRESSION TAG                 
SEQADV 5VWW SER B  166  UNP  Q16611    CYS   166 ENGINEERED MUTATION            
SEQADV 5VWW ARG C  147  UNP  O43521    TRP   147 ENGINEERED MUTATION            
SEQADV 5VWW THR C  162  UNP  O43521    TYR   162 ENGINEERED MUTATION            
SEQADV 5VWW ARG D  147  UNP  O43521    TRP   147 ENGINEERED MUTATION            
SEQADV 5VWW THR D  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  170  GLY PRO LEU GLY SER MET SER GLU GLU GLN VAL ALA GLN          
SEQRES   2 B  170  ASP THR GLU GLU VAL PHE ARG SER TYR VAL PHE TYR ARG          
SEQRES   3 B  170  HIS GLN GLN GLU GLN GLU ALA GLU GLY VAL ALA ALA PRO          
SEQRES   4 B  170  ALA ASP PRO GLU MET VAL THR LEU PRO LEU GLN PRO SER          
SEQRES   5 B  170  SER THR MET GLY GLN VAL GLY ARG GLN LEU ALA ILE ILE          
SEQRES   6 B  170  GLY ASP ASP ILE ASN ARG ARG TYR ASP SER GLU PHE GLN          
SEQRES   7 B  170  THR MET LEU GLN HIS LEU GLN PRO THR ALA GLU ASN ALA          
SEQRES   8 B  170  TYR GLU TYR PHE THR LYS ILE ALA THR SER LEU PHE GLU          
SEQRES   9 B  170  SER GLY ILE ASN TRP GLY ARG VAL VAL ALA LEU LEU GLY          
SEQRES  10 B  170  PHE GLY TYR ARG LEU ALA LEU HIS VAL TYR GLN HIS GLY          
SEQRES  11 B  170  LEU THR GLY PHE LEU GLY GLN VAL THR ARG PHE VAL VAL          
SEQRES  12 B  170  ASP PHE MET LEU HIS HIS SER ILE ALA ARG TRP ILE ALA          
SEQRES  13 B  170  GLN ARG GLY GLY TRP VAL ALA ALA LEU ASN LEU GLY ASN          
SEQRES  14 B  170  GLY                                                          
SEQRES   1 C   26  ASP MET ARG PRO GLU ILE ARG ILE ALA GLN GLU LEU ARG          
SEQRES   2 C   26  ARG ILE GLY ASP GLU PHE ASN ALA THR TYR ALA ARG ARG          
SEQRES   1 D   26  ASP MET ARG PRO GLU ILE ARG ILE ALA GLN GLU LEU ARG          
SEQRES   2 D   26  ARG ILE GLY ASP GLU PHE ASN ALA THR TYR ALA ARG ARG          
HET    MPD  A 201       8                                                       
HET     BR  A 202       1                                                       
HET    IMD  A 203       5                                                       
HET     BR  C 201       1                                                       
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETNAM      BR BROMIDE ION                                                      
HETNAM     IMD IMIDAZOLE                                                        
FORMUL   5  MPD    C6 H14 O2                                                    
FORMUL   6   BR    2(BR 1-)                                                     
FORMUL   7  IMD    C3 H5 N2 1+                                                  
FORMUL   9  HOH   *19(H2 O)                                                     
HELIX    1 AA1 SER A   23  ALA A   49  1                                  27    
HELIX    2 AA2 SER A   69  GLN A  101  1                                  33    
HELIX    3 AA3 ASN A  106  GLU A  120  1                                  15    
HELIX    4 AA4 ASN A  124  GLY A  146  1                                  23    
HELIX    5 AA5 GLY A  146  HIS A  165  1                                  20    
HELIX    6 AA6 SER A  166  ARG A  174  1                                   9    
HELIX    7 AA7 GLY A  176  LEU A  181  5                                   6    
HELIX    8 AA8 GLU B   24  GLN B   45  1                                  22    
HELIX    9 AA9 SER B   69  GLN B  101  1                                  33    
HELIX   10 AB1 ASN B  106  GLU B  120  1                                  15    
HELIX   11 AB2 ASN B  124  GLY B  146  1                                  23    
HELIX   12 AB3 GLY B  146  HIS B  165  1                                  20    
HELIX   13 AB4 SER B  166  ARG B  174  1                                   9    
HELIX   14 AB5 GLY B  176  LEU B  183  5                                   8    
HELIX   15 AB6 ARG C  143  ALA C  164  1                                  22    
HELIX   16 AB7 PRO D  144  ALA D  161  1                                  18    
SITE     1 AC1  6 ASN A  86  TYR A  89  ASP A  90  PHE A  93                    
SITE     2 AC1  6 GLY A 133  HOH A 301                                          
SITE     1 AC2  3 ASN A 124  TRP A 125  ASN C 160                               
SITE     1 AC3  2 THR A  70  ARG C 147                                          
CRYST1   87.790   87.790   95.460  90.00  90.00  90.00 P 43 21 2    16          
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      0.011391  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011391  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010476        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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