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Database: PDB
Entry: 4ZII
LinkDB: 4ZII
Original site: 4ZII 
HEADER    APOPTOSIS                               28-APR-15   4ZII              
TITLE     CRYSTAL STRUCTURE OF CORE/LATCH DIMER OF BAXI66A IN COMPLEX WITH      
TITLE    2 BIDBH3                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APOPTOSIS REGULATOR BAX;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: BCL-2-LIKE PROTEIN 4,BCL2-L-4;                              
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: BH3-INTERACTING DOMAIN DEATH AGONIST;                      
COMPND   9 CHAIN: C;                                                            
COMPND  10 FRAGMENT: BH3 MOTIF;                                                 
COMPND  11 SYNONYM: P22 BID,BID;                                                
COMPND  12 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: BAX, BCL2L4;                                                   
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    BAX, APOPTOSIS, BH3 DOMAIN, STRUCTURAL GENOMICS                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.E.CZABOTAR,A.Y.ROBIN,K.KRISHNA KUMAR,D.WESTPHAL,A.Z.WARDAK,         
AUTHOR   2 G.V.THOMPSON,G.DEWSON,P.M.COLMAN                                     
REVDAT   2   20-SEP-17 4ZII    1       SOURCE REMARK                            
REVDAT   1   22-JUL-15 4ZII    0                                                
JRNL        AUTH   A.Y.ROBIN,K.KRISHNA KUMAR,D.WESTPHAL,A.Z.WARDAK,             
JRNL        AUTH 2 G.V.THOMPSON,G.DEWSON,P.M.COLMAN,P.E.CZABOTAR                
JRNL        TITL   CRYSTAL STRUCTURE OF BAX BOUND TO THE BH3 PEPTIDE OF BIM     
JRNL        TITL 2 IDENTIFIES IMPORTANT CONTACTS FOR INTERACTION.               
JRNL        REF    CELL DEATH DIS                V.   6 E1809 2015              
JRNL        REFN                   ISSN 2041-4889                               
JRNL        PMID   26158515                                                     
JRNL        DOI    10.1038/CDDIS.2015.141                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.19 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.42                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 11049                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.010                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1106                            
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 46.4316 -  4.3812    0.99     1349   151  0.1584 0.1977        
REMARK   3     2  4.3812 -  3.4779    1.00     1265   140  0.1449 0.1942        
REMARK   3     3  3.4779 -  3.0383    0.99     1261   141  0.1781 0.2327        
REMARK   3     4  3.0383 -  2.7606    1.00     1234   137  0.1810 0.2235        
REMARK   3     5  2.7606 -  2.5627    0.99     1231   136  0.1885 0.2530        
REMARK   3     6  2.5627 -  2.4117    0.99     1216   136  0.1929 0.2574        
REMARK   3     7  2.4117 -  2.2909    0.99     1218   135  0.2428 0.2937        
REMARK   3     8  2.2909 -  2.1912    0.95     1169   130  0.3624 0.4234        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 1.00                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.100           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.92                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           1409                                  
REMARK   3   ANGLE     :  1.054           1887                                  
REMARK   3   CHIRALITY :  0.072            207                                  
REMARK   3   PLANARITY :  0.004            244                                  
REMARK   3   DIHEDRAL  : 16.135            519                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A OR CHAIN C                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  20.0334  -9.5138   4.6275              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2600 T22:   0.3400                                     
REMARK   3      T33:   0.2728 T12:  -0.0488                                     
REMARK   3      T13:  -0.0024 T23:   0.1080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2249 L22:   1.1708                                     
REMARK   3      L33:  -0.2743 L12:   1.1108                                     
REMARK   3      L13:  -0.3059 L23:  -0.0616                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0306 S12:   0.2025 S13:   0.2165                       
REMARK   3      S21:  -0.0213 S22:   0.1085 S23:   0.2342                       
REMARK   3      S31:   0.0661 S32:  -0.0409 S33:   0.0127                       
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 4ZII COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209332.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11053                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.191                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.420                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 13.70                              
REMARK 200  R MERGE                    (I) : 0.10860                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.2900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.50                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.94700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.630                              
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: 4BD2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRI-SODIUM CITRATE, SODIUM CACODYLATE,   
REMARK 280  PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K             
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       19.00350            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       51.90050            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       51.90050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       28.50525            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       51.90050            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       51.90050            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        9.50175            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       51.90050            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       51.90050            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       28.50525            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       51.90050            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       51.90050            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        9.50175            
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       19.00350            
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: 13440 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 16960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -111.0 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   BIOMT1   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       19.00350            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     ARG A     9                                                      
REMARK 465     MET A    38                                                      
REMARK 465     GLY A    39                                                      
REMARK 465     GLY A    40                                                      
REMARK 465     GLU A    41                                                      
REMARK 465     ALA A    42                                                      
REMARK 465     PRO A    43                                                      
REMARK 465     PRO A   168                                                      
REMARK 465     THR A   169                                                      
REMARK 465     TRP A   170                                                      
REMARK 465     SER C   100                                                      
REMARK 465     ILE C   101                                                      
REMARK 465     PRO C   102                                                      
REMARK 465     PRO C   103                                                      
REMARK 465     GLY C   104                                                      
REMARK 465     LEU C   105                                                      
REMARK 465     VAL C   106                                                      
REMARK 465     ASN C   107                                                      
REMARK 465     GLY C   108                                                      
REMARK 465     LEU C   109                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ILE A  66    CG1  CG2  CD1                                       
REMARK 470     ARG C  99    CG   CD   NE   CZ   NH1  NH2                        
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    HOH A   335     O    HOH A   344              2.15            
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    THR A  85       53.20   -106.47                                   
REMARK 500    SER A  87       78.38   -110.67                                   
REMARK 500    ASP C  98      -89.35    -58.37                                   
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 EDO A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 205                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ZIE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZIF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZIG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZIH   RELATED DB: PDB                                   
DBREF  4ZII A    1   170  UNP    Q07812   BAX_HUMAN        1    170             
DBREF  4ZII C   76   109  UNP    P55957   BID_HUMAN      122    155             
SEQADV 4ZII SER A   62  UNP  Q07812    CYS    62 ENGINEERED MUTATION            
SEQADV 4ZII SER A  126  UNP  Q07812    CYS   126 ENGINEERED MUTATION            
SEQRES   1 A  170  MET ASP GLY SER GLY GLU GLN PRO ARG GLY GLY GLY PRO          
SEQRES   2 A  170  THR SER SER GLU GLN ILE MET LYS THR GLY ALA LEU LEU          
SEQRES   3 A  170  LEU GLN GLY PHE ILE GLN ASP ARG ALA GLY ARG MET GLY          
SEQRES   4 A  170  GLY GLU ALA PRO GLU LEU ALA LEU ASP PRO VAL PRO GLN          
SEQRES   5 A  170  ASP ALA SER THR LYS LYS LEU SER GLU SER LEU LYS ARG          
SEQRES   6 A  170  ILE GLY ASP GLU LEU ASP SER ASN MET GLU LEU GLN ARG          
SEQRES   7 A  170  MET ILE ALA ALA VAL ASP THR ASP SER PRO ARG GLU VAL          
SEQRES   8 A  170  PHE PHE ARG VAL ALA ALA ASP MET PHE SER ASP GLY ASN          
SEQRES   9 A  170  PHE ASN TRP GLY ARG VAL VAL ALA LEU PHE TYR PHE ALA          
SEQRES  10 A  170  SER LYS LEU VAL LEU LYS ALA LEU SER THR LYS VAL PRO          
SEQRES  11 A  170  GLU LEU ILE ARG THR ILE MET GLY TRP THR LEU ASP PHE          
SEQRES  12 A  170  LEU ARG GLU ARG LEU LEU GLY TRP ILE GLN ASP GLN GLY          
SEQRES  13 A  170  GLY TRP ASP GLY LEU LEU SER TYR PHE GLY THR PRO THR          
SEQRES  14 A  170  TRP                                                          
SEQRES   1 C   34  SER GLU SER GLN GLU ASP ILE ILE ARG ASN ILE ALA ARG          
SEQRES   2 C   34  HIS LEU ALA GLN VAL GLY ASP SER MET ASP ARG SER ILE          
SEQRES   3 C   34  PRO PRO GLY LEU VAL ASN GLY LEU                              
HET    EDO  A 201       4                                                       
HET    EDO  A 202       4                                                       
HET    EDO  A 203       4                                                       
HET    EDO  A 204       4                                                       
HET    EDO  A 205       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  EDO    5(C2 H6 O2)                                                  
FORMUL   8  HOH   *53(H2 O)                                                     
HELIX    1 AA1 SER A   15  ARG A   37  1                                  23    
HELIX    2 AA2 ASP A   53  SER A   72  1                                  20    
HELIX    3 AA3 ASN A   73  VAL A   83  1                                  11    
HELIX    4 AA4 SER A   87  PHE A  100  1                                  14    
HELIX    5 AA5 ASN A  106  LEU A  148  1                                  43    
HELIX    6 AA6 LEU A  148  GLN A  155  1                                   8    
HELIX    7 AA7 TRP A  158  GLY A  166  1                                   9    
HELIX    8 AA8 GLU C   77  MET C   97  1                                  21    
SITE     1 AC1  5 SER A  55  THR A  56  TRP A 158  ASP A 159                    
SITE     2 AC1  5 HOH A 303                                                     
SITE     1 AC2  3 MET A  20  ARG A 145  HOH A 309                               
SITE     1 AC3  1 ASP A 154                                                     
SITE     1 AC4  5 LEU A  45  ALA A  81  LYS A 123  SER A 126                    
SITE     2 AC4  5 HOH A 306                                                     
SITE     1 AC5  2 PRO A  88  TRP A 139                                          
CRYST1  103.801  103.801   38.007  90.00  90.00  90.00 P 43 21 2     8          
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      0.009634  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009634  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.026311        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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