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Database: PDB
Entry: 2WH6
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Original site: 2WH6 
HEADER    APOPTOSIS                               01-MAY-09   2WH6              
TITLE     CRYSTAL STRUCTURE OF ANTI-APOPTOTIC BHRF1 IN COMPLEX WITH THE BIM BH3 
TITLE    2 DOMAIN                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EARLY ANTIGEN PROTEIN R;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: BCL-2, RESIDUES 1-160;                                     
COMPND   5 SYNONYM: NUCLEAR ANTIGEN, EA-R, BHRF1;                               
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: BCL-2-LIKE PROTEIN 11;                                     
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: BH3, RESIDUES 51-72;                                       
COMPND  11 SYNONYM: BCL2-L-11, BCL2-INTERACTING MEDIATOR OF CELL DEATH, BIM;    
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: EPSTEIN-BARR VIRUS STRAIN AG876;                
SOURCE   3 ORGANISM_TAXID: 82830;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_PLASMID: PDUET;                                    
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 SYNTHETIC: YES;                                                      
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606                                                 
KEYWDS    MITOCHONDRION, EARLY PROTEIN, TRANSMEMBRANE, VIRAL PROTEIN, APOPTOSIS 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.KVANSAKUL,D.C.S.HUANG,P.M.COLMAN                                    
REVDAT   4   28-MAR-18 2WH6    1       SOURCE JRNL   REMARK                     
REVDAT   3   13-JUL-11 2WH6    1       VERSN                                    
REVDAT   2   16-FEB-11 2WH6    1       JRNL   REMARK                            
REVDAT   1   26-MAY-10 2WH6    0                                                
JRNL        AUTH   M.KVANSAKUL,A.H.WEI,J.I.FLETCHER,S.N.WILLIS,L.CHEN,          
JRNL        AUTH 2 A.W.ROBERTS,D.C.HUANG,P.M.COLMAN                             
JRNL        TITL   STRUCTURAL BASIS FOR APOPTOSIS INHIBITION BY EPSTEIN-BARR    
JRNL        TITL 2 VIRUS BHRF1.                                                 
JRNL        REF    PLOS PATHOG.                  V.   6 01236 2010              
JRNL        REFN                   ESSN 1553-7374                               
JRNL        PMID   21203485                                                     
JRNL        DOI    10.1371/JOURNAL.PPAT.1001236                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 32170                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1705                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2169                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 104                          
REMARK   3   BIN FREE R VALUE                    : 0.3360                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1457                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 115                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.02                          
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.076         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.070         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.049         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.875         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.953                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1504 ; 0.015 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2046 ; 1.685 ; 1.942       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   183 ;11.678 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    75 ;29.789 ;23.067       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   246 ;15.402 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;22.297 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   228 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1145 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   810 ; 0.253 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1040 ; 0.313 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    91 ; 0.262 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    48 ; 0.201 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    18 ; 0.324 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   918 ; 1.430 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1455 ; 2.371 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   670 ; 3.404 ; 5.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   588 ; 4.668 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   159                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.2863  10.8281   4.9905              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0182 T22:  -0.0602                                     
REMARK   3      T33:  -0.0487 T12:  -0.0351                                     
REMARK   3      T13:  -0.0121 T23:   0.0172                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3053 L22:   1.0312                                     
REMARK   3      L33:   1.5152 L12:   0.3420                                     
REMARK   3      L13:  -0.2875 L23:  -0.5980                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0555 S12:   0.0472 S13:  -0.0333                       
REMARK   3      S21:  -0.0507 S22:   0.0960 S23:   0.0569                       
REMARK   3      S31:  -0.1177 S32:  -0.0378 S33:  -0.0404                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    51        B    76                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.1692  24.9296   9.2571              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1921 T22:  -0.1638                                     
REMARK   3      T33:  -0.0635 T12:  -0.0904                                     
REMARK   3      T13:   0.1041 T23:  -0.0042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5978 L22:   3.2718                                     
REMARK   3      L33:   3.3341 L12:   0.6473                                     
REMARK   3      L13:   2.5020 L23:   1.2713                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0839 S12:  -0.2723 S13:   0.5385                       
REMARK   3      S21:  -0.4480 S22:   0.2327 S23:   0.0050                       
REMARK   3      S31:  -0.4916 S32:   0.3781 S33:  -0.3166                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  2001        A  2099                          
REMARK   3    RESIDUE RANGE :   B  2001        B  2016                          
REMARK   3    RESIDUE RANGE :   A  1159        A  1167                          
REMARK   3    RESIDUE RANGE :   A  1168        A  1169                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.6051  12.5791   5.2648              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0402 T22:   0.0284                                     
REMARK   3      T33:   0.0625 T12:  -0.0183                                     
REMARK   3      T13:  -0.0006 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5328 L22:   1.2257                                     
REMARK   3      L33:   2.4635 L12:   0.2994                                     
REMARK   3      L13:  -0.3345 L23:  -0.6295                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0016 S12:  -0.0351 S13:   0.0229                       
REMARK   3      S21:   0.0583 S22:   0.0496 S23:  -0.0564                       
REMARK   3      S31:  -0.1638 S32:  -0.0246 S33:  -0.0512                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2WH6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-MAY-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290036537.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-SEP-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.987                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32170                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
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     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 9.600                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 40.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
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 2V6Q                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MALIC ACID PH 4 1.25 M NABR, PH    
REMARK 280  4.0                                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.58867            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       30.79433            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       30.79433            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       61.58867            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8880 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     GLN A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     PRO A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     PRO A   159                                                      
REMARK 465     GLY A   160                                                      
REMARK 465     TYR B    73                                                      
REMARK 465     ALA B    74                                                      
REMARK 465     ARG B    75                                                      
REMARK 465     ARG B    76                                                      
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     HIS A   92   ND1  CE1  NE2                                       
REMARK 480     ASP A   95   CG   OD1  OD2                                       
REMARK 480     GLN A  146   OE1  NE2                                            
REMARK 480     ARG B   53   CD   NE   CZ   NH1  NH2                             
REMARK 480     ARG B   64   NH1                                                 
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  2054     O    HOH A  2080              1.95            
REMARK 500   O    HOH B  2012     O    HOH B  2013              1.97            
REMARK 500   O    ILE A   158     O    HOH A  2097              2.03            
REMARK 500   O    HOH A  2030     O    HOH A  2031              2.10            
REMARK 500   NE2  HIS A    92     O    HOH A  2062              2.13            
REMARK 500   O    GLY A    94     O    HOH A  2067              2.14            
REMARK 500   O    HOH B  2008     O    HOH B  2009              2.14            
REMARK 500   O    GLU A   155     O    HOH A  2095              2.16            
REMARK 500   NH1  ARG A    60    BR     BR A  1166              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2021     O    HOH A  2055     5555     2.07            
REMARK 500   OE1  GLU A    59     ND2  ASN A    84     2564     2.08            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  55   CD    GLU A  55   OE2     0.071                       
REMARK 500    HIS A  92   NE2   HIS A  92   CD2    -0.076                       
REMARK 500    GLN A 146   CD    GLN A 146   OE1     0.200                       
REMARK 500    ARG B  53   CG    ARG B  53   CD     -0.245                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    HIS A  92   ND1 -  CG  -  CD2 ANGL. DEV. = -11.5 DEGREES          
REMARK 500    HIS A  92   CB  -  CG  -  ND1 ANGL. DEV. =  -8.8 DEGREES          
REMARK 500    ASP A  95   CA  -  CB  -  CG  ANGL. DEV. = -22.4 DEGREES          
REMARK 500    ASP A  95   CB  -  CG  -  OD1 ANGL. DEV. =  35.0 DEGREES          
REMARK 500    ASP A  95   CB  -  CG  -  OD2 ANGL. DEV. = -31.9 DEGREES          
REMARK 500    ARG B  53   CB  -  CG  -  CD  ANGL. DEV. =  19.7 DEGREES          
REMARK 500    ARG B  64   NH1 -  CZ  -  NH2 ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    ARG B  64   NE  -  CZ  -  NH1 ANGL. DEV. =   9.5 DEGREES          
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  36      -75.52    -60.70                                   
REMARK 500    HIS A  78       89.76   -158.60                                   
REMARK 500    ARG A  93       67.48   -112.78                                   
REMARK 500    ASN B  70       -7.16    -51.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR A   36     PRO A   37                   35.54                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    HIS A  92         0.17    SIDE CHAIN                              
REMARK 500    GLN A 146         0.11    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    THR A  36         12.36                                           
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 BR A 1159                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 1160                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 1161                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 1162                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 1163                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 1164                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 1165                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 1166                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1168                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1169                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VM6   RELATED DB: PDB                                   
REMARK 900 HUMAN BCL-2A1 IN COMPLEX WITH BIM                                    
REMARK 900 RELATED ID: 1Q59   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF THE BHRF1 PROTEIN FROM EPSTEIN-BARRVIRUS, A    
REMARK 900 HOMOLOG OF HUMAN BCL -2                                              
REMARK 900 RELATED ID: 2V6Q   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A BHRF-1 : BIM BH3 COMPLEX                      
DBREF  2WH6 A    1   160  UNP    P03182   EAR_EBV          1    160             
DBREF  2WH6 B   51    76  UNP    O43521   B2L11_HUMAN     51     76             
SEQADV 2WH6 MET A  -12  UNP  P03182              EXPRESSION TAG                 
SEQADV 2WH6 GLY A  -11  UNP  P03182              EXPRESSION TAG                 
SEQADV 2WH6 SER A  -10  UNP  P03182              EXPRESSION TAG                 
SEQADV 2WH6 HIS A   -9  UNP  P03182              EXPRESSION TAG                 
SEQADV 2WH6 HIS A   -8  UNP  P03182              EXPRESSION TAG                 
SEQADV 2WH6 HIS A   -7  UNP  P03182              EXPRESSION TAG                 
SEQADV 2WH6 HIS A   -6  UNP  P03182              EXPRESSION TAG                 
SEQADV 2WH6 HIS A   -5  UNP  P03182              EXPRESSION TAG                 
SEQADV 2WH6 HIS A   -4  UNP  P03182              EXPRESSION TAG                 
SEQADV 2WH6 SER A   -3  UNP  P03182              EXPRESSION TAG                 
SEQADV 2WH6 GLN A   -2  UNP  P03182              EXPRESSION TAG                 
SEQADV 2WH6 ASP A   -1  UNP  P03182              EXPRESSION TAG                 
SEQADV 2WH6 PRO A    0  UNP  P03182              EXPRESSION TAG                 
SEQRES   1 A  173  MET GLY SER HIS HIS HIS HIS HIS HIS SER GLN ASP PRO          
SEQRES   2 A  173  MET ALA TYR SER THR ARG GLU ILE LEU LEU ALA LEU CYS          
SEQRES   3 A  173  ILE ARG ASP SER ARG VAL HIS GLY ASN GLY THR LEU HIS          
SEQRES   4 A  173  PRO VAL LEU GLU LEU ALA ALA ARG GLU THR PRO LEU ARG          
SEQRES   5 A  173  LEU SER PRO GLU ASP THR VAL VAL LEU ARG TYR HIS VAL          
SEQRES   6 A  173  LEU LEU GLU GLU ILE ILE GLU ARG ASN SER GLU THR PHE          
SEQRES   7 A  173  THR GLU THR TRP ASN ARG PHE ILE THR HIS THR GLU HIS          
SEQRES   8 A  173  VAL ASP LEU ASP PHE ASN SER VAL PHE LEU GLU ILE PHE          
SEQRES   9 A  173  HIS ARG GLY ASP PRO SER LEU GLY ARG ALA LEU ALA TRP          
SEQRES  10 A  173  MET ALA TRP CYS MET HIS ALA CYS ARG THR LEU CYS CYS          
SEQRES  11 A  173  ASN GLN SER THR PRO TYR TYR VAL VAL ASP LEU SER VAL          
SEQRES  12 A  173  ARG GLY MET LEU GLU ALA SER GLU GLY LEU ASP GLY TRP          
SEQRES  13 A  173  ILE HIS GLN GLN GLY GLY TRP SER THR LEU ILE GLU ASP          
SEQRES  14 A  173  ASN ILE PRO GLY                                              
SEQRES   1 B   26  ASP MET ARG PRO GLU ILE TRP ILE ALA GLN GLU LEU ARG          
SEQRES   2 B   26  ARG ILE GLY ASP GLU PHE ASN ALA TYR TYR ALA ARG ARG          
HET     BR  A1159       1                                                       
HET     BR  A1160       1                                                       
HET     BR  A1161       1                                                       
HET     BR  A1162       1                                                       
HET     BR  A1163       1                                                       
HET     BR  A1164       1                                                       
HET     BR  A1165       1                                                       
HET     BR  A1166       1                                                       
HET     BR  A1167       1                                                       
HET    GOL  A1168       6                                                       
HET    GOL  A1169       6                                                       
HETNAM      BR BROMIDE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   BR    9(BR 1-)                                                     
FORMUL  12  GOL    2(C3 H8 O3)                                                  
FORMUL  14  HOH   *115(H2 O)                                                    
HELIX    1   1 SER A    4  VAL A   19  1                                  16    
HELIX    2   2 HIS A   26  THR A   36  1                                  11    
HELIX    3   3 ASP A   44  ASN A   61  1                                  18    
HELIX    4   4 ASN A   61  THR A   76  1                                  16    
HELIX    5   5 HIS A   78  HIS A   92  1                                  15    
HELIX    6   6 SER A   97  ASN A  118  1                                  22    
HELIX    7   7 PRO A  122  GLU A  138  1                                  17    
HELIX    8   8 LEU A  140  GLN A  147  1                                   8    
HELIX    9   9 GLY A  148  ASN A  157  1                                  10    
HELIX   10  10 MET B   52  ASN B   70  1                                  19    
SITE     1 AC1  2 VAL A  79   BR A1163                                          
SITE     1 AC2  2 SER A  41  ASN A  70                                          
SITE     1 AC3  1 SER A  62                                                     
SITE     1 AC4  2 TRP A  69  LEU A 115                                          
SITE     1 AC5  3 TYR A 123  TYR A 124   BR A1159                               
SITE     1 AC6  2 ARG A  49  GLU A 155                                          
SITE     1 AC7  4 ARG A  93  ILE B  56  GLN B  60  ARG B  63                    
SITE     1 AC8  2 ARG A  60  ASN A  61                                          
SITE     1 AC9  5 ARG A   6  THR A  36  ARG A 131  GLU A 135                    
SITE     2 AC9  5 HOH A2081                                                     
SITE     1 BC1  6 ALA A  33  LEU A  38  SER A  62  GLU A  63                    
SITE     2 BC1  6 THR A  66  HOH A2043                                          
CRYST1   62.747   62.747   92.383  90.00  90.00 120.00 P 32 2 1      6          
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      0.015937  0.009201  0.000000        0.00000                         
SCALE2      0.000000  0.018402  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010825        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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