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Database: PDB
Entry: 3PL7
LinkDB: 3PL7
Original site: 3PL7 
HEADER    APOPTOSIS/APOPTOSIS REGULATOR           14-NOV-10   3PL7              
TITLE     CRYSTAL STRUCTURE OF BCL-XL IN COMPLEX WITH THE BAXBH3 DOMAIN         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BCL-2-LIKE PROTEIN 1;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: BCL-XL, UNP RESIDUES 1-209;                                
COMPND   5 SYNONYM: BCL2-L-1, APOPTOSIS REGULATOR BCL-X;                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: APOPTOSIS REGULATOR BAX;                                   
COMPND  10 CHAIN: C;                                                            
COMPND  11 FRAGMENT: BH3 DOMAIN, UNP RESIDUES 48-81;                            
COMPND  12 SYNONYM: BCL-2-LIKE PROTEIN 4, BCL2-L-4;                             
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BCL2L1, BCL2L, BCLX;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 OTHER_DETAILS: SYNTHESIZED PEPTIDE                                   
KEYWDS    BCL-2 FAMILY FOLD, REGULATION OF APOPTOSIS, BAX, MITOCHONDRIA,        
KEYWDS   2 APOPTOSIS-APOPTOSIS REGULATOR COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.E.CZABOTAR,P.M.COLMAN                                               
REVDAT   2   22-JAN-14 3PL7    1       JRNL   VERSN                             
REVDAT   1   29-DEC-10 3PL7    0                                                
JRNL        AUTH   P.E.CZABOTAR,E.F.LEE,G.V.THOMPSON,A.Z.WARDAK,W.D.FAIRLIE,    
JRNL        AUTH 2 P.M.COLMAN                                                   
JRNL        TITL   MUTATION TO BAX BEYOND THE BH3 DOMAIN DISRUPTS INTERACTIONS  
JRNL        TITL 2 WITH PRO-SURVIVAL PROTEINS AND PROMOTES APOPTOSIS            
JRNL        REF    J.BIOL.CHEM.                  V. 286  7123 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21199865                                                     
JRNL        DOI    10.1074/JBC.M110.161281                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.54                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 12214                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.810                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 587                             
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 33.5467 -  4.1461    1.00     3024   150  0.1846 0.2266        
REMARK   3     2  4.1461 -  3.2918    1.00     2928   145  0.1674 0.2218        
REMARK   3     3  3.2918 -  2.8760    1.00     2881   149  0.1903 0.2960        
REMARK   3     4  2.8760 -  2.6131    0.97     2794   143  0.2314 0.3311        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 47.39                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.570           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.92                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.14890                                              
REMARK   3    B22 (A**2) : 4.24090                                              
REMARK   3    B33 (A**2) : -9.38980                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
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      :  0.008           2557                                  
REMARK   3   ANGLE     :  1.021           3451                                  
REMARK   3   CHIRALITY :  0.068            361                                  
REMARK   3   PLANARITY :  0.004            446                                  
REMARK   3   DIHEDRAL  : 16.496            913                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3891  19.5561  10.8671              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0499 T22:   0.1029                                     
REMARK   3      T33:   0.0685 T12:  -0.0385                                     
REMARK   3      T13:  -0.0276 T23:  -0.0232                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9104 L22:   0.6732                                     
REMARK   3      L33:   1.1627 L12:  -0.7776                                     
REMARK   3      L13:   0.7484 L23:  -0.4591                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1326 S12:  -0.1407 S13:  -0.1052                       
REMARK   3      S21:   0.0307 S22:   0.1408 S23:   0.1564                       
REMARK   3      S31:  -0.0328 S32:  -0.2933 S33:  -0.0063                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  42.8950  10.2581  15.2796              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1137 T22:   0.0474                                     
REMARK   3      T33:   0.1039 T12:   0.0404                                     
REMARK   3      T13:   0.0337 T23:  -0.0335                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2337 L22:   0.3908                                     
REMARK   3      L33:   2.1693 L12:  -0.5833                                     
REMARK   3      L13:  -0.1613 L23:  -0.1802                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0710 S12:   0.0558 S13:  -0.0807                       
REMARK   3      S21:  -0.0736 S22:   0.0127 S23:  -0.0681                       
REMARK   3      S31:   0.4363 S32:   0.2870 S33:   0.0610                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  26.7112  17.1012  12.4711              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1924 T22:   0.2140                                     
REMARK   3      T33:   0.2009 T12:  -0.0255                                     
REMARK   3      T13:   0.0196 T23:  -0.0190                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6360 L22:   4.9607                                     
REMARK   3      L33:   0.4723 L12:  -0.8353                                     
REMARK   3      L13:  -0.2153 L23:   0.4000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2626 S12:   0.0526 S13:   0.2554                       
REMARK   3      S21:  -0.0229 S22:   0.3903 S23:  -0.4747                       
REMARK   3      S31:   0.0662 S32:   0.0715 S33:  -0.1356                       
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 3PL7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-NOV-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062508.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95661                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12238                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 14.500                             
REMARK 200  R MERGE                    (I) : 0.10500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.59100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.100                              
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: PDB ENTRY 2YXJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG 6000, 0.2M CACL2, 0.1M TRIS,     
REMARK 280  PH 8.0, VAPOR DIFFUSION, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
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   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.57150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.57150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       35.12300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       49.52500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       35.12300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       49.52500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       56.57150            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       35.12300            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       49.52500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       56.57150            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       35.12300            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       49.52500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8720 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     MET A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ASP A    69                                                      
REMARK 465     VAL A    70                                                      
REMARK 465     GLU A    71                                                      
REMARK 465     GLU A    72                                                      
REMARK 465     ASN A    73                                                      
REMARK 465     ARG A    74                                                      
REMARK 465     THR A    75                                                      
REMARK 465     GLU A    76                                                      
REMARK 465     ALA A    77                                                      
REMARK 465     PRO A    78                                                      
REMARK 465     GLU A    79                                                      
REMARK 465     GLY A    80                                                      
REMARK 465     THR A    81                                                      
REMARK 465     ASN A   197                                                      
REMARK 465     ASN A   198                                                      
REMARK 465     ALA A   199                                                      
REMARK 465     ALA A   200                                                      
REMARK 465     ALA A   201                                                      
REMARK 465     GLU A   202                                                      
REMARK 465     SER A   203                                                      
REMARK 465     ARG A   204                                                      
REMARK 465     LYS A   205                                                      
REMARK 465     GLY A   206                                                      
REMARK 465     GLN A   207                                                      
REMARK 465     GLU A   208                                                      
REMARK 465     ARG A   209                                                      
REMARK 465     LEU A   210                                                      
REMARK 465     GLU A   211                                                      
REMARK 465     HIS A   212                                                      
REMARK 465     HIS A   213                                                      
REMARK 465     HIS A   214                                                      
REMARK 465     HIS A   215                                                      
REMARK 465     HIS A   216                                                      
REMARK 465     HIS A   217                                                      
REMARK 465     ASP C    48                                                      
REMARK 465     PRO C    49                                                      
REMARK 465     VAL C    50                                                      
REMARK 465     PRO C    51                                                      
REMARK 465     GLN C    52                                                      
REMARK 465     ASP C    53                                                      
REMARK 465     ILE C    80                                                      
REMARK 465     ALA C    81                                                      
REMARK 465     MET B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     MET B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     VAL B    70                                                      
REMARK 465     GLU B    71                                                      
REMARK 465     GLU B    72                                                      
REMARK 465     ASN B    73                                                      
REMARK 465     ARG B    74                                                      
REMARK 465     THR B    75                                                      
REMARK 465     GLU B    76                                                      
REMARK 465     ALA B    77                                                      
REMARK 465     PRO B    78                                                      
REMARK 465     GLU B    79                                                      
REMARK 465     GLY B    80                                                      
REMARK 465     THR B    81                                                      
REMARK 465     ASN B   197                                                      
REMARK 465     ASN B   198                                                      
REMARK 465     ALA B   199                                                      
REMARK 465     ALA B   200                                                      
REMARK 465     ALA B   201                                                      
REMARK 465     GLU B   202                                                      
REMARK 465     SER B   203                                                      
REMARK 465     ARG B   204                                                      
REMARK 465     LYS B   205                                                      
REMARK 465     GLY B   206                                                      
REMARK 465     GLN B   207                                                      
REMARK 465     GLU B   208                                                      
REMARK 465     ARG B   209                                                      
REMARK 465     LEU B   210                                                      
REMARK 465     GLU B   211                                                      
REMARK 465     HIS B   212                                                      
REMARK 465     HIS B   213                                                      
REMARK 465     HIS B   214                                                      
REMARK 465     HIS B   215                                                      
REMARK 465     HIS B   216                                                      
REMARK 465     HIS B   217                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     SER A   28   OG                                                  
REMARK 480     GLN A   88   OE1  NE2                                            
REMARK 480     ARG A  132   NE   CZ   NH1  NH2                                  
REMARK 480     LYS C   57   CD   CE   NZ                                        
REMARK 480     LYS C   58   CG   CD   CE   NZ                                   
REMARK 480     ASP B  107   OD1  OD2                                            
REMARK 480     GLU B  153   OE1  OE2                                            
REMARK 480     ASP B  156   OD1  OD2                                            
REMARK 480     LYS B  157   CE   NZ                                             
REMARK 480     GLU B  193   CD   OE1  OE2                                       
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    MET A 159       45.20   -100.18                                   
REMARK 500    MET B 159       45.78    -78.61                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3PK1   RELATED DB: PDB                                   
DBREF  3PL7 A    1   209  UNP    Q07817   B2CL1_HUMAN      1    209             
DBREF  3PL7 C   48    81  UNP    Q07812   BAX_HUMAN       48     81             
DBREF  3PL7 B    1   209  UNP    Q07817   B2CL1_HUMAN      1    209             
SEQADV 3PL7 MET A   -3  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 SER A   -2  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 MET A   -1  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 ALA A    0  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7     A       UNP  Q07817    MET    45 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    GLU    46 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    THR    47 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    PRO    48 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    SER    49 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    ALA    50 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    ILE    51 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    ASN    52 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    GLY    53 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    ASN    54 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    PRO    55 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    SER    56 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    TRP    57 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    HIS    58 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    LEU    59 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    ALA    60 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    ASP    61 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    SER    62 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    PRO    63 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    ALA    64 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    VAL    65 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    ASN    66 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    GLY    67 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    ALA    68 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    THR    69 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    GLY    70 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    HIS    71 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    SER    72 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    SER    73 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    SER    74 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    LEU    75 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    ASP    76 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    ALA    77 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    ARG    78 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    GLU    79 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    VAL    80 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    ILE    81 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    PRO    82 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    MET    83 DELETION                       
SEQADV 3PL7     A       UNP  Q07817    ALA    84 DELETION                       
SEQADV 3PL7 LEU A  210  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 GLU A  211  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 HIS A  212  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 HIS A  213  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 HIS A  214  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 HIS A  215  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 HIS A  216  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 HIS A  217  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 MET B   -3  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 SER B   -2  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 MET B   -1  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 ALA B    0  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7     B       UNP  Q07817    MET    45 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    GLU    46 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    THR    47 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    PRO    48 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    SER    49 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    ALA    50 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    ILE    51 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    ASN    52 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    GLY    53 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    ASN    54 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    PRO    55 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    SER    56 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    TRP    57 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    HIS    58 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    LEU    59 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    ALA    60 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    ASP    61 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    SER    62 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    PRO    63 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    ALA    64 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    VAL    65 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    ASN    66 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    GLY    67 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    ALA    68 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    THR    69 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    GLY    70 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    HIS    71 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    SER    72 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    SER    73 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    SER    74 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    LEU    75 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    ASP    76 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    ALA    77 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    ARG    78 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    GLU    79 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    VAL    80 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    ILE    81 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    PRO    82 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    MET    83 DELETION                       
SEQADV 3PL7     B       UNP  Q07817    ALA    84 DELETION                       
SEQADV 3PL7 LEU B  210  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 GLU B  211  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 HIS B  212  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 HIS B  213  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 HIS B  214  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 HIS B  215  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 HIS B  216  UNP  Q07817              EXPRESSION TAG                 
SEQADV 3PL7 HIS B  217  UNP  Q07817              EXPRESSION TAG                 
SEQRES   1 A  181  MET SER MET ALA MET SER GLN SER ASN ARG GLU LEU VAL          
SEQRES   2 A  181  VAL ASP PHE LEU SER TYR LYS LEU SER GLN LYS GLY TYR          
SEQRES   3 A  181  SER TRP SER GLN PHE SER ASP VAL GLU GLU ASN ARG THR          
SEQRES   4 A  181  GLU ALA PRO GLU GLY THR GLU SER GLU ALA VAL LYS GLN          
SEQRES   5 A  181  ALA LEU ARG GLU ALA GLY ASP GLU PHE GLU LEU ARG TYR          
SEQRES   6 A  181  ARG ARG ALA PHE SER ASP LEU THR SER GLN LEU HIS ILE          
SEQRES   7 A  181  THR PRO GLY THR ALA TYR GLN SER PHE GLU GLN VAL VAL          
SEQRES   8 A  181  ASN GLU LEU PHE ARG ASP GLY VAL ASN TRP GLY ARG ILE          
SEQRES   9 A  181  VAL ALA PHE PHE SER PHE GLY GLY ALA LEU CYS VAL GLU          
SEQRES  10 A  181  SER VAL ASP LYS GLU MET GLN VAL LEU VAL SER ARG ILE          
SEQRES  11 A  181  ALA ALA TRP MET ALA THR TYR LEU ASN ASP HIS LEU GLU          
SEQRES  12 A  181  PRO TRP ILE GLN GLU ASN GLY GLY TRP ASP THR PHE VAL          
SEQRES  13 A  181  GLU LEU TYR GLY ASN ASN ALA ALA ALA GLU SER ARG LYS          
SEQRES  14 A  181  GLY GLN GLU ARG LEU GLU HIS HIS HIS HIS HIS HIS              
SEQRES   1 C   34  ASP PRO VAL PRO GLN ASP ALA SER THR LYS LYS LEU SER          
SEQRES   2 C   34  GLU CYS LEU LYS ARG ILE GLY ASP GLU LEU ASP SER ASN          
SEQRES   3 C   34  MET GLU LEU GLN ARG MET ILE ALA                              
SEQRES   1 B  181  MET SER MET ALA MET SER GLN SER ASN ARG GLU LEU VAL          
SEQRES   2 B  181  VAL ASP PHE LEU SER TYR LYS LEU SER GLN LYS GLY TYR          
SEQRES   3 B  181  SER TRP SER GLN PHE SER ASP VAL GLU GLU ASN ARG THR          
SEQRES   4 B  181  GLU ALA PRO GLU GLY THR GLU SER GLU ALA VAL LYS GLN          
SEQRES   5 B  181  ALA LEU ARG GLU ALA GLY ASP GLU PHE GLU LEU ARG TYR          
SEQRES   6 B  181  ARG ARG ALA PHE SER ASP LEU THR SER GLN LEU HIS ILE          
SEQRES   7 B  181  THR PRO GLY THR ALA TYR GLN SER PHE GLU GLN VAL VAL          
SEQRES   8 B  181  ASN GLU LEU PHE ARG ASP GLY VAL ASN TRP GLY ARG ILE          
SEQRES   9 B  181  VAL ALA PHE PHE SER PHE GLY GLY ALA LEU CYS VAL GLU          
SEQRES  10 B  181  SER VAL ASP LYS GLU MET GLN VAL LEU VAL SER ARG ILE          
SEQRES  11 B  181  ALA ALA TRP MET ALA THR TYR LEU ASN ASP HIS LEU GLU          
SEQRES  12 B  181  PRO TRP ILE GLN GLU ASN GLY GLY TRP ASP THR PHE VAL          
SEQRES  13 B  181  GLU LEU TYR GLY ASN ASN ALA ALA ALA GLU SER ARG LYS          
SEQRES  14 B  181  GLY GLN GLU ARG LEU GLU HIS HIS HIS HIS HIS HIS              
FORMUL   4  HOH   *38(H2 O)                                                     
HELIX    1   1 GLN A    3  GLN A   19  1                                  17    
HELIX    2   2 SER A   23  SER A   28  5                                   6    
HELIX    3   3 GLU A   82  TYR A  101  1                                  20    
HELIX    4   4 TYR A  101  ASP A  107  1                                   7    
HELIX    5   5 THR A  109  HIS A  113  5                                   5    
HELIX    6   6 THR A  118  ARG A  132  1                                  15    
HELIX    7   7 ASN A  136  LYS A  157  1                                  22    
HELIX    8   8 VAL A  161  LEU A  178  1                                  18    
HELIX    9   9 LEU A  178  ASN A  185  1                                   8    
HELIX   10  10 GLY A  187  GLY A  196  1                                  10    
HELIX   11  11 ALA C   54  MET C   79  1                                  26    
HELIX   12  12 SER B    4  LYS B   20  1                                  17    
HELIX   13  13 TRP B   24  SER B   28  5                                   5    
HELIX   14  14 GLU B   82  LEU B  112  1                                  31    
HELIX   15  15 ALA B  119  ARG B  132  1                                  14    
HELIX   16  16 ASN B  136  LYS B  157  1                                  22    
HELIX   17  17 MET B  159  VAL B  161  5                                   3    
HELIX   18  18 LEU B  162  LEU B  178  1                                  17    
HELIX   19  19 LEU B  178  ASN B  185  1                                   8    
HELIX   20  20 GLY B  187  GLY B  196  1                                  10    
CRYST1   70.246   99.050  113.143  90.00  90.00  90.00 C 2 2 21     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      0.014236  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010096  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008838        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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