GenomeNet

Database: PDB
Entry: 5W5X
LinkDB: 5W5X
Original site: 5W5X 
HEADER    APOPTOSIS/IMMUNE SYSTEM                 16-JUN-17   5W5X              
TITLE     CRYSTAL STRUCTURE OF BAXP168G IN COMPLEX WITH AN ACTIVATING ANTIBODY  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3C10 FAB' LIGHT CHAIN;                                     
COMPND   3 CHAIN: L;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: 3C10 FAB' HEAVY CHAIN;                                     
COMPND   6 CHAIN: H;                                                            
COMPND   7 OTHER_DETAILS: N-TERMINUS GLUTAMATE IS CONVERTED INTO A PYROGLUTAMATE
COMPND   8 RESIDUE. C-TERMINUS RESIDUES NOT SEEN IN STRUCTURE.;                 
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: APOPTOSIS REGULATOR BAX;                                   
COMPND  11 CHAIN: A;                                                            
COMPND  12 SYNONYM: BCL-2-LIKE PROTEIN 4,BCL2-L-4;                              
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_TAXID: 10116;                                               
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   6 ORGANISM_TAXID: 10116;                                               
SOURCE   7 MOL_ID: 3;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 GENE: BAX, BCL2L4;                                                   
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    FAB', BAX ACTIVATION, UNFOLDING, APOPTOSIS, APOPTOSIS-IMMUNE SYSTEM   
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.Y.ROBIN,P.M.COLMAN,P.E.CZABOTAR                                     
REVDAT   4   17-OCT-18 5W5X    1       JRNL                                     
REVDAT   3   05-SEP-18 5W5X    1       JRNL                                     
REVDAT   2   29-AUG-18 5W5X    1       JRNL                                     
REVDAT   1   27-JUN-18 5W5X    0                                                
JRNL        AUTH   A.Y.ROBIN,S.IYER,R.W.BIRKINSHAW,J.SANDOW,A.WARDAK,C.S.LUO,   
JRNL        AUTH 2 M.SHI,A.I.WEBB,P.E.CZABOTAR,R.M.KLUCK,P.M.COLMAN             
JRNL        TITL   ENSEMBLE PROPERTIES OF BAX DETERMINE ITS FUNCTION.           
JRNL        REF    STRUCTURE                     V.  26  1346 2018              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   30122452                                                     
JRNL        DOI    10.1016/J.STR.2018.07.006                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2152: ???)                              
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.64                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 24112                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1204                            
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 47.6480 -  5.2014    0.93     2643   141  0.1820 0.2300        
REMARK   3     2  5.2014 -  4.1293    0.96     2560   136  0.1467 0.1807        
REMARK   3     3  4.1293 -  3.6075    0.97     2526   130  0.1622 0.2298        
REMARK   3     4  3.6075 -  3.2778    0.98     2537   131  0.1857 0.2428        
REMARK   3     5  3.2778 -  3.0429    0.98     2546   131  0.2009 0.2711        
REMARK   3     6  3.0429 -  2.8635    0.99     2528   134  0.2208 0.2998        
REMARK   3     7  2.8635 -  2.7201    0.99     2541   136  0.2395 0.3181        
REMARK   3     8  2.7201 -  2.6017    0.99     2509   133  0.2610 0.3211        
REMARK   3     9  2.6017 -  2.5016    0.98     2518   132  0.2815 0.3445        
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)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.620           
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           4572                                  
REMARK   3   ANGLE     :  0.593           6212                                  
REMARK   3   CHIRALITY :  0.042            716                                  
REMARK   3   PLANARITY :  0.004            784                                  
REMARK   3   DIHEDRAL  : 13.958           2678                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN H AND RESID 1:117 OR CHAIN L AND RESID 1:109     
REMARK   3               OR CHAIN A AND RESID 31:45                             
REMARK   3    ORIGIN FOR THE GROUP (A): -33.4830 -22.8092 -22.6287              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2513 T22:   0.3264                                     
REMARK   3      T33:   0.3020 T12:  -0.0230                                     
REMARK   3      T13:  -0.0427 T23:   0.0087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9558 L22:   1.5638                                     
REMARK   3      L33:   1.9935 L12:   0.6779                                     
REMARK   3      L13:  -0.3995 L23:  -0.4711                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1786 S12:  -0.2559 S13:  -0.1330                       
REMARK   3      S21:   0.1627 S22:  -0.1312 S23:  -0.0011                       
REMARK   3      S31:   0.2092 S32:  -0.0243 S33:  -0.0360                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN H AND RESID 118:212 OR CHAIN L AND RESID         
REMARK   3               110:214                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -15.2007   6.1562 -12.5405              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3261 T22:   0.3672                                     
REMARK   3      T33:   0.3304 T12:  -0.0135                                     
REMARK   3      T13:  -0.0314 T23:  -0.0328                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7808 L22:   2.2441                                     
REMARK   3      L33:   4.3146 L12:   0.3612                                     
REMARK   3      L13:   0.6173 L23:   0.8585                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0762 S12:  -0.2998 S13:   0.1084                       
REMARK   3      S21:   0.0883 S22:  -0.2896 S23:   0.2046                       
REMARK   3      S31:  -0.3360 S32:  -0.6136 S33:   0.1672                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 1:30 OR CHAIN A AND RESID 46:200     
REMARK   3    ORIGIN FOR THE GROUP (A): -54.8691 -51.1524 -25.0970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3614 T22:   0.4497                                     
REMARK   3      T33:   0.4884 T12:  -0.0653                                     
REMARK   3      T13:   0.0112 T23:   0.0834                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9049 L22:   6.2397                                     
REMARK   3      L33:   3.0822 L12:   0.6820                                     
REMARK   3      L13:   0.1365 L23:   0.7235                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1781 S12:  -0.0689 S13:   0.1458                       
REMARK   3      S21:   0.0796 S22:  -0.1622 S23:  -0.5929                       
REMARK   3      S31:  -0.0019 S32:   0.4066 S33:  -0.0169                       
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 5W5X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000228421.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JUL-16                          
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24112                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.502                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.639                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.10180                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.3700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
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) : 0.91180                            
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: 1ZAN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, HEPES, VAPOR DIFFUSION,        
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
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      144.32150            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       34.15450            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       34.15450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       72.16075            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       34.15450            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       34.15450            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      216.48225            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       34.15450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       34.15450            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       72.16075            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       34.15450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       34.15450            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      216.48225            
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      144.32150            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, A                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13270 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 52010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, A                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 ZN    ZN L 307  LIES ON A SPECIAL POSITION.                          
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     CYS L   213                                                      
REMARK 465     ALA H   134                                                      
REMARK 465     LEU H   135                                                      
REMARK 465     LYS H   136                                                      
REMARK 465     SER H   137                                                      
REMARK 465     ASN H   138                                                      
REMARK 465     ARG H   218                                                      
REMARK 465     GLU H   219                                                      
REMARK 465     CYS H   220                                                      
REMARK 465     ASN H   221                                                      
REMARK 465     PRO H   222                                                      
REMARK 465     CYS H   223                                                      
REMARK 465     GLY H   224                                                      
REMARK 465     CYS H   225                                                      
REMARK 465     THR H   226                                                      
REMARK 465     GLY H   227                                                      
REMARK 465     SER H   228                                                      
REMARK 465     GLU H   229                                                      
REMARK 465     VAL H   230                                                      
REMARK 465     SER H   231                                                      
REMARK 465     SER H   232                                                      
REMARK 465     VAL H   233                                                      
REMARK 465     PHE H   234                                                      
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     GLY A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     PRO A    43                                                      
REMARK 465     GLU A    44                                                      
REMARK 465     LEU A    45                                                      
REMARK 465     ALA A    46                                                      
REMARK 465     LEU A    47                                                      
REMARK 465     ASP A    48                                                      
REMARK 465     PRO A    49                                                      
REMARK 465     VAL A    50                                                      
REMARK 465     PRO A    51                                                      
REMARK 465     GLN A    52                                                      
REMARK 465     LYS A   189                                                      
REMARK 465     LYS A   190                                                      
REMARK 465     MET A   191                                                      
REMARK 465     GLY A   192                                                      
REMARK 465     SER A   193                                                      
REMARK 465     SER A   194                                                      
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     ASP L   1    CG   OD1  OD2                                       
REMARK 470     LYS L  24    CG   CD   CE   NZ                                   
REMARK 470     LYS L  31    CE   NZ                                             
REMARK 470     GLU L 153    CG   CD   OE1  OE2                                  
REMARK 470     GLU L 212    CG   CD   OE1  OE2                                  
REMARK 470     GLN H   3    CG   CD   OE1  NE2                                  
REMARK 470     LYS H  13    CE   NZ                                             
REMARK 470     GLN H  62    CG   CD   OE1  NE2                                  
REMARK 470     LYS H  63    CG   CD   CE   NZ                                   
REMARK 470     GLN H  82    CG   CD   OE1  NE2                                  
REMARK 470     GLU H  89    CG   CD   OE1  OE2                                  
REMARK 470     THR H 133    OG1  CG2                                            
REMARK 470     LYS H 210    CG   CD   CE   NZ                                   
REMARK 470     LYS H 214    CG   CD   CE   NZ                                   
REMARK 470     GLU A  17    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  21    CG   CD   CE   NZ                                   
REMARK 470     ASP A  53    CG   OD1  OD2                                       
REMARK 470     LYS A  57    CG   CD   CE   NZ                                   
REMARK 470     LYS A  58    CE   NZ                                             
REMARK 470     ASP A  86    CG   OD1  OD2                                       
REMARK 470     LYS A 123    CG   CD   CE   NZ                                   
REMARK 470     SER A 126    OG                                                  
REMARK 470     THR A 127    OG1  CG2                                            
REMARK 470     LYS A 128    CG   CD   CE   NZ                                   
REMARK 470     VAL A 129    CG1  CG2                                            
REMARK 470     GLU A 131    CG   CD   OE1  OE2                                  
REMARK 470     TRP A 188    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 188    CZ3  CH2                                            
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    ASN L  30     -138.78     51.50                                   
REMARK 500    THR L  51      -43.43     70.89                                   
REMARK 500    ASN L  52       14.78   -149.41                                   
REMARK 500    ASN L 189      -52.64   -121.64                                   
REMARK 500    ASN L 211       38.75    -86.41                                   
REMARK 500    THR H 104     -126.42   -103.95                                   
REMARK 500    PRO H 131      104.26    -56.70                                   
REMARK 500    SER H 165      -39.32   -149.18                                   
REMARK 500    ARG A  37       -7.52   -157.04                                   
REMARK 500    ASN A 104       78.25   -111.11                                   
REMARK 500    SER A 126      126.82   -175.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN L 307  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L 188   NE2                                                    
REMARK 620 2 HIS L 188   NE2   0.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO L 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO L 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO L 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO L 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO L 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO L 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN L 307                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO H 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO H 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO H 303                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5W5Z   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5W60   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5W61   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5W62   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5W63   RELATED DB: PDB                                   
DBREF  5W5X L    1   213  PDB    5W5X     5W5X             1    213             
DBREF  5W5X H    1   234  PDB    5W5X     5W5X             1    234             
DBREF  5W5X A    1   192  UNP    Q07812   BAX_HUMAN        1    192             
SEQADV 5W5X SER A   62  UNP  Q07812    CYS    62 ENGINEERED MUTATION            
SEQADV 5W5X SER A  126  UNP  Q07812    CYS   126 ENGINEERED MUTATION            
SEQADV 5W5X GLY A  168  UNP  Q07812    PRO   168 ENGINEERED MUTATION            
SEQADV 5W5X SER A  193  UNP  Q07812              EXPRESSION TAG                 
SEQADV 5W5X SER A  194  UNP  Q07812              EXPRESSION TAG                 
SEQRES   1 L  213  ASP ILE GLN MET THR GLN SER PRO SER PHE LEU SER ALA          
SEQRES   2 L  213  SER VAL GLY ASP ARG VAL THR ILE ASN CYS LYS ALA SER          
SEQRES   3 L  213  GLN ASN VAL ASN LYS TYR LEU ASP TRP TYR GLN GLN ASN          
SEQRES   4 L  213  LEU GLY GLU PRO PRO LYS LEU LEU ILE TYR HIS THR ASN          
SEQRES   5 L  213  SER LEU PRO THR GLY ILE PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  213  GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU          
SEQRES   7 L  213  GLN VAL GLU ASP VAL ALA THR TYR PHE CYS LEU GLN HIS          
SEQRES   8 L  213  ASP SER GLY LEU THR PHE GLY SER GLY THR LYS LEU GLU          
SEQRES   9 L  213  ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE          
SEQRES  10 L  213  PRO PRO SER MET GLU GLN LEU THR SER GLY GLY ALA THR          
SEQRES  11 L  213  VAL VAL CYS PHE VAL ASN ASN PHE TYR PRO ARG ASP ILE          
SEQRES  12 L  213  SER VAL LYS TRP LYS ILE ASP GLY SER GLU GLN ARG ASP          
SEQRES  13 L  213  GLY VAL LEU ASP SER VAL THR ASP GLN ASP SER LYS ASP          
SEQRES  14 L  213  SER THR TYR SER MET SER SER THR LEU SER LEU THR LYS          
SEQRES  15 L  213  VAL GLU TYR GLU ARG HIS ASN LEU TYR THR CYS GLU VAL          
SEQRES  16 L  213  VAL HIS LYS THR SER SER SER PRO VAL VAL LYS SER PHE          
SEQRES  17 L  213  ASN ARG ASN GLU CYS                                          
SEQRES   1 H  234  PCA VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 H  234  PRO GLY SER SER VAL LYS ILE SER CYS LYS ALA SER GLY          
SEQRES   3 H  234  TYR THR PHE THR ASN TYR ASP MET HIS TRP ILE LYS GLN          
SEQRES   4 H  234  ARG PRO GLY SER GLY LEU GLU TRP ILE GLY TRP ILE TYR          
SEQRES   5 H  234  PRO GLY ASN GLY ASN THR LYS TYR ASN GLN LYS PHE ASN          
SEQRES   6 H  234  GLY LYS ALA THR LEU THR ALA ASP LYS SER SER THR THR          
SEQRES   7 H  234  ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER          
SEQRES   8 H  234  ALA VAL TYR PHE CYS VAL ARG GLU GLY LEU GLY ILE THR          
SEQRES   9 H  234  PHE GLU TYR TRP GLY GLN GLY VAL LYS VAL THR VAL SER          
SEQRES  10 H  234  SER ALA GLU THR THR ALA PRO SER VAL TYR PRO LEU ALA          
SEQRES  11 H  234  PRO GLY THR ALA LEU LYS SER ASN SER MET VAL THR LEU          
SEQRES  12 H  234  GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR          
SEQRES  13 H  234  VAL THR TRP ASN SER GLY ALA LEU SER SER GLY VAL HIS          
SEQRES  14 H  234  THR PHE PRO ALA VAL LEU GLN SER GLY LEU TYR THR LEU          
SEQRES  15 H  234  THR SER SER VAL THR VAL PRO SER SER THR TRP SER SER          
SEQRES  16 H  234  GLN ALA VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER          
SEQRES  17 H  234  THR LYS VAL ASP LYS LYS ILE VAL PRO ARG GLU CYS ASN          
SEQRES  18 H  234  PRO CYS GLY CYS THR GLY SER GLU VAL SER SER VAL PHE          
SEQRES   1 A  194  MET ASP GLY SER GLY GLU GLN PRO ARG GLY GLY GLY PRO          
SEQRES   2 A  194  THR SER SER GLU GLN ILE MET LYS THR GLY ALA LEU LEU          
SEQRES   3 A  194  LEU GLN GLY PHE ILE GLN ASP ARG ALA GLY ARG MET GLY          
SEQRES   4 A  194  GLY GLU ALA PRO GLU LEU ALA LEU ASP PRO VAL PRO GLN          
SEQRES   5 A  194  ASP ALA SER THR LYS LYS LEU SER GLU SER LEU LYS ARG          
SEQRES   6 A  194  ILE GLY ASP GLU LEU ASP SER ASN MET GLU LEU GLN ARG          
SEQRES   7 A  194  MET ILE ALA ALA VAL ASP THR ASP SER PRO ARG GLU VAL          
SEQRES   8 A  194  PHE PHE ARG VAL ALA ALA ASP MET PHE SER ASP GLY ASN          
SEQRES   9 A  194  PHE ASN TRP GLY ARG VAL VAL ALA LEU PHE TYR PHE ALA          
SEQRES  10 A  194  SER LYS LEU VAL LEU LYS ALA LEU SER THR LYS VAL PRO          
SEQRES  11 A  194  GLU LEU ILE ARG THR ILE MET GLY TRP THR LEU ASP PHE          
SEQRES  12 A  194  LEU ARG GLU ARG LEU LEU GLY TRP ILE GLN ASP GLN GLY          
SEQRES  13 A  194  GLY TRP ASP GLY LEU LEU SER TYR PHE GLY THR GLY THR          
SEQRES  14 A  194  TRP GLN THR VAL THR ILE PHE VAL ALA GLY VAL LEU THR          
SEQRES  15 A  194  ALA SER LEU THR ILE TRP LYS LYS MET GLY SER SER              
HET    PCA  H   1       8                                                       
HET    EDO  L 301       4                                                       
HET    EDO  L 302       4                                                       
HET    EDO  L 303       4                                                       
HET    EDO  L 304       4                                                       
HET    EDO  L 305       4                                                       
HET    EDO  L 306       4                                                       
HET     ZN  L 307       1                                                       
HET    EDO  H 301       4                                                       
HET    EDO  H 302       4                                                       
HET    EDO  H 303       4                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      ZN ZINC ION                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  PCA    C5 H7 N O3                                                   
FORMUL   4  EDO    9(C2 H6 O2)                                                  
FORMUL  10   ZN    ZN 2+                                                        
FORMUL  14  HOH   *98(H2 O)                                                     
HELIX    1 AA1 GLN L   79  VAL L   83  5                                   5    
HELIX    2 AA2 SER L  120  SER L  126  1                                   7    
HELIX    3 AA3 LYS L  182  GLU L  186  1                                   5    
HELIX    4 AA4 THR H   28  TYR H   32  5                                   5    
HELIX    5 AA5 GLN H   62  ASN H   65  5                                   4    
HELIX    6 AA6 THR H   87  SER H   91  5                                   5    
HELIX    7 AA7 SER H  161  ALA H  163  5                                   3    
HELIX    8 AA8 SER H  190  GLN H  196  1                                   7    
HELIX    9 AA9 PRO H  205  SER H  208  5                                   4    
HELIX   10 AB1 SER A   15  ILE A   31  1                                  17    
HELIX   11 AB2 ALA A   54  SER A   72  1                                  19    
HELIX   12 AB3 ASN A   73  ALA A   82  1                                  10    
HELIX   13 AB4 SER A   87  SER A  101  1                                  15    
HELIX   14 AB5 ASN A  106  ALA A  124  1                                  19    
HELIX   15 AB6 LYS A  128  LEU A  148  1                                  21    
HELIX   16 AB7 LEU A  148  GLN A  155  1                                   8    
HELIX   17 AB8 TRP A  158  PHE A  165  1                                   8    
HELIX   18 AB9 THR A  169  THR A  186  1                                  18    
SHEET    1 AA1 4 MET L   4  SER L   7  0                                        
SHEET    2 AA1 4 VAL L  19  ALA L  25 -1  O  LYS L  24   N  THR L   5           
SHEET    3 AA1 4 ASP L  70  ILE L  75 -1  O  ILE L  75   N  VAL L  19           
SHEET    4 AA1 4 PHE L  62  GLY L  66 -1  N  SER L  65   O  THR L  72           
SHEET    1 AA2 5 PHE L  10  ALA L  13  0                                        
SHEET    2 AA2 5 THR L 101  ILE L 105  1  O  GLU L 104   N  LEU L  11           
SHEET    3 AA2 5 THR L  85  GLN L  90 -1  N  TYR L  86   O  THR L 101           
SHEET    4 AA2 5 LEU L  33  GLN L  38 -1  N  TYR L  36   O  PHE L  87           
SHEET    5 AA2 5 LYS L  45  ILE L  48 -1  O  ILE L  48   N  TRP L  35           
SHEET    1 AA3 4 PHE L  10  ALA L  13  0                                        
SHEET    2 AA3 4 THR L 101  ILE L 105  1  O  GLU L 104   N  LEU L  11           
SHEET    3 AA3 4 THR L  85  GLN L  90 -1  N  TYR L  86   O  THR L 101           
SHEET    4 AA3 4 THR L  96  PHE L  97 -1  O  THR L  96   N  GLN L  90           
SHEET    1 AA4 4 THR L 113  PHE L 117  0                                        
SHEET    2 AA4 4 GLY L 128  PHE L 138 -1  O  VAL L 132   N  PHE L 117           
SHEET    3 AA4 4 TYR L 172  THR L 181 -1  O  MET L 174   N  VAL L 135           
SHEET    4 AA4 4 VAL L 158  VAL L 162 -1  N  SER L 161   O  SER L 175           
SHEET    1 AA5 4 SER L 152  GLN L 154  0                                        
SHEET    2 AA5 4 ILE L 143  ILE L 149 -1  N  ILE L 149   O  SER L 152           
SHEET    3 AA5 4 LEU L 190  HIS L 197 -1  O  GLU L 194   N  LYS L 146           
SHEET    4 AA5 4 VAL L 204  ASN L 209 -1  O  LYS L 206   N  CYS L 193           
SHEET    1 AA6 4 GLN H   3  GLN H   6  0                                        
SHEET    2 AA6 4 VAL H  18  SER H  25 -1  O  LYS H  23   N  GLN H   5           
SHEET    3 AA6 4 THR H  78  LEU H  83 -1  O  ALA H  79   N  CYS H  22           
SHEET    4 AA6 4 ALA H  68  ASP H  73 -1  N  THR H  71   O  TYR H  80           
SHEET    1 AA7 6 GLU H  10  VAL H  12  0                                        
SHEET    2 AA7 6 VAL H 112  VAL H 116  1  O  THR H 115   N  GLU H  10           
SHEET    3 AA7 6 ALA H  92  GLU H  99 -1  N  ALA H  92   O  VAL H 114           
SHEET    4 AA7 6 MET H  34  ARG H  40 -1  N  HIS H  35   O  VAL H  97           
SHEET    5 AA7 6 GLY H  44  ILE H  51 -1  O  GLY H  44   N  ARG H  40           
SHEET    6 AA7 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  TRP H  50           
SHEET    1 AA8 4 GLU H  10  VAL H  12  0                                        
SHEET    2 AA8 4 VAL H 112  VAL H 116  1  O  THR H 115   N  GLU H  10           
SHEET    3 AA8 4 ALA H  92  GLU H  99 -1  N  ALA H  92   O  VAL H 114           
SHEET    4 AA8 4 PHE H 105  TRP H 108 -1  O  TYR H 107   N  ARG H  98           
SHEET    1 AA9 4 SER H 125  LEU H 129  0                                        
SHEET    2 AA9 4 MET H 140  TYR H 150 -1  O  GLY H 144   N  LEU H 129           
SHEET    3 AA9 4 LEU H 179  PRO H 189 -1  O  VAL H 186   N  LEU H 143           
SHEET    4 AA9 4 VAL H 168  THR H 170 -1  N  HIS H 169   O  SER H 185           
SHEET    1 AB1 4 SER H 125  LEU H 129  0                                        
SHEET    2 AB1 4 MET H 140  TYR H 150 -1  O  GLY H 144   N  LEU H 129           
SHEET    3 AB1 4 LEU H 179  PRO H 189 -1  O  VAL H 186   N  LEU H 143           
SHEET    4 AB1 4 VAL H 174  GLN H 176 -1  N  VAL H 174   O  THR H 181           
SHEET    1 AB2 3 THR H 156  TRP H 159  0                                        
SHEET    2 AB2 3 THR H 199  HIS H 204 -1  O  ASN H 201   N  THR H 158           
SHEET    3 AB2 3 THR H 209  LYS H 214 -1  O  THR H 209   N  HIS H 204           
SSBOND   1 CYS L   23    CYS L   88                          1555   1555  2.04  
SSBOND   2 CYS L  133    CYS L  193                          1555   1555  2.03  
SSBOND   3 CYS H   22    CYS H   96                          1555   1555  2.03  
SSBOND   4 CYS H  145    CYS H  200                          1555   1555  2.04  
LINK         NE2 HIS L 188                ZN    ZN L 307     1555   1555  2.25  
LINK         C   PCA H   1                 N   VAL H   2     1555   1555  1.33  
LINK         NE2 HIS L 188                ZN    ZN L 307     1555   7555  2.25  
CISPEP   1 SER L    7    PRO L    8          0        -3.49                     
CISPEP   2 TYR L  139    PRO L  140          0         6.94                     
CISPEP   3 PHE H  151    PRO H  152          0        -5.83                     
CISPEP   4 GLU H  153    PRO H  154          0         0.62                     
SITE     1 AC1  5 SER L  12  GLU L 104  PRO L 140  ARG L 141                    
SITE     2 AC1  5 ASP L 142                                                     
SITE     1 AC2  4 ASN L  39  LEU L  40  GLY L  41  GLU L  42                    
SITE     1 AC3  3 SER L  12  THR L  56  LYS L 106                               
SITE     1 AC4  1 ASP L 150                                                     
SITE     1 AC5  3 ARG L 141  MET L 174  HOH L 405                               
SITE     1 AC6  6 GLN L  37  LYS L  45  ARG L  61  PHE L  62                    
SITE     2 AC6  6 GLU L  81  ASP L  82                                          
SITE     1 AC7  2 GLU L 184  HIS L 188                                          
SITE     1 AC8  9 PHE H 171  PRO H 172  LEU H 182  THR H 183                    
SITE     2 AC8  9 HOH H 425  LEU L 159  SER L 161  SER L 175                    
SITE     3 AC8  9 THR L 177                                                     
SITE     1 AC9  2 GLN H 110  GLY H 111                                          
SITE     1 AD1  2 ALA A  42  GLN H 196                                          
CRYST1   68.309   68.309  288.643  90.00  90.00  90.00 P 41 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      0.014639  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014639  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003464        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system