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Database: PDB
Entry: 5JSN
LinkDB: 5JSN
Original site: 5JSN 
HEADER    VIRAL PROTEIN/INHIBITOR                 09-MAY-16   5JSN              
TITLE     BCL2-INHIBITOR COMPLEX                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APOPTOSIS REGULATOR BCL-2;                                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: BCL2 INHIBITOR;                                            
COMPND   7 CHAIN: B, D;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BCL2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET29B;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: UNIDENTIFIED;                                   
SOURCE  12 ORGANISM_TAXID: 32644;                                               
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PET29B                                    
KEYWDS    BCL-2, ANTIBCL2, COMPLEX, VIRAL PROTEIN-INHIBITOR COMPLEX             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.W.SHEN,B.L.STODDARD                                                 
REVDAT   1   16-NOV-16 5JSN    0                                                
JRNL        AUTH   S.BERGER,E.PROCKO,D.MARGINEANTU,E.F.LEE,B.W.SHEN,A.ZELTER,   
JRNL        AUTH 2 D.A.SILVA,K.CHAWLA,M.J.HEROLD,J.M.GARNIER,R.JOHNSON,         
JRNL        AUTH 3 M.J.MACCOSS,G.LESSENE,T.N.DAVIS,P.S.STAYTON,B.L.STODDARD,    
JRNL        AUTH 4 W.D.FAIRLIE,D.M.HOCKENBERY,D.BAKER                           
JRNL        TITL   COMPUTATIONALLY DESIGNED HIGH SPECIFICITY INHIBITORS         
JRNL        TITL 2 DELINEATE THE ROLES OF BCL2 FAMILY PROTEINS IN CANCER.       
JRNL        REF    ELIFE                         V.   5       2016              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   27805565                                                     
JRNL        DOI    10.7554/ELIFE.20352                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 30512                          
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) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
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      : 1605                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2108                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.41                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 123                          
REMARK   3   BIN FREE R VALUE                    : 0.3330                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4374                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 152                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 17.56000                                             
REMARK   3    B22 (A**2) : 17.56000                                             
REMARK   3    B33 (A**2) : -35.11000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.044         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.036         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.107         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.627         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4470 ; 0.019 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4316 ; 0.008 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6008 ; 2.010 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9880 ; 1.734 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   526 ; 6.454 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   247 ;34.429 ;23.036       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   838 ;18.695 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    55 ;19.549 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   630 ; 0.126 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5034 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1097 ; 0.006 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  2113 ; 2.452 ; 3.298       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2112 ; 2.452 ; 3.298       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2633 ; 3.520 ; 4.923       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2634 ; 3.519 ; 4.923       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2357 ; 2.744 ; 3.686       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2358 ; 2.743 ; 3.686       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3375 ; 4.179 ; 5.401       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5319 ; 6.602 ;26.514       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5292 ; 6.577 ;26.393       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 2                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     7    209       C     7    209   15744  0.14  0.05     
REMARK   3    2     B     3    117       D     3    117   13106  0.16  0.05     
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.692                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : -H, K, -L                                       
REMARK   3      TWIN FRACTION : 0.308                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
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     7        A   209                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5849  -5.6482  58.2767              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0190 T22:   0.0499                                     
REMARK   3      T33:   0.2169 T12:  -0.0117                                     
REMARK   3      T13:  -0.0235 T23:  -0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6993 L22:   2.9680                                     
REMARK   3      L33:   3.8507 L12:   0.3465                                     
REMARK   3      L13:   0.1616 L23:   0.7157                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0310 S12:   0.2036 S13:  -0.0792                       
REMARK   3      S21:  -0.1102 S22:  -0.0159 S23:   0.1523                       
REMARK   3      S31:   0.1937 S32:  -0.2935 S33:  -0.0151                       
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     3        B   117                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.3315  10.5232  58.8693              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0768 T22:   0.0309                                     
REMARK   3      T33:   0.2508 T12:  -0.0358                                     
REMARK   3      T13:   0.0058 T23:   0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8921 L22:   2.2664                                     
REMARK   3      L33:   3.6527 L12:  -1.2923                                     
REMARK   3      L13:  -1.6137 L23:   0.8614                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2251 S12:   0.1255 S13:   0.3492                       
REMARK   3      S21:  -0.1739 S22:  -0.0076 S23:  -0.2213                       
REMARK   3      S31:  -0.2828 S32:   0.0827 S33:  -0.2175                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     7        C   209                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.2254  37.2449  72.6643              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0361 T22:   0.0655                                     
REMARK   3      T33:   0.1700 T12:  -0.0134                                     
REMARK   3      T13:   0.0429 T23:  -0.0316                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2028 L22:   1.9796                                     
REMARK   3      L33:   4.3307 L12:   0.6088                                     
REMARK   3      L13:   0.9704 L23:   0.1984                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0922 S12:  -0.1762 S13:   0.1390                       
REMARK   3      S21:   0.1243 S22:  -0.0236 S23:  -0.0347                       
REMARK   3      S31:  -0.1187 S32:   0.3290 S33:  -0.0686                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     3        D   117                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.4555  23.4038  70.2064              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0927 T22:   0.0455                                     
REMARK   3      T33:   0.2138 T12:  -0.0338                                     
REMARK   3      T13:   0.0319 T23:  -0.0159                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9751 L22:   3.2358                                     
REMARK   3      L33:   3.8876 L12:  -0.9577                                     
REMARK   3      L13:   1.3394 L23:  -2.0137                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0989 S12:  -0.2512 S13:  -0.2689                       
REMARK   3      S21:   0.1059 S22:   0.0916 S23:   0.2737                       
REMARK   3      S31:   0.1483 S32:  -0.0180 S33:  -0.1905                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 5JSN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000221159.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRROR                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000 708                       
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000 708                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : 0.05000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 69.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.680                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.7                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% JEFFAMINE ED-2001, PH7.0/100 MM      
REMARK 280  HEPES PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
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,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
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       67.15700            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       33.57850            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      100.73550            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 2850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     ASP A    34                                                      
REMARK 465     VAL A    35                                                      
REMARK 465     GLY A    36                                                      
REMARK 465     ALA A    37                                                      
REMARK 465     ALA A    38                                                      
REMARK 465     PRO A    39                                                      
REMARK 465     PRO A    40                                                      
REMARK 465     GLY A    41                                                      
REMARK 465     ALA A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     PRO A    44                                                      
REMARK 465     ALA A    45                                                      
REMARK 465     PRO A    46                                                      
REMARK 465     GLY A    47                                                      
REMARK 465     ILE A    48                                                      
REMARK 465     PHE A    49                                                      
REMARK 465     SER A    50                                                      
REMARK 465     SER A    51                                                      
REMARK 465     GLN A    52                                                      
REMARK 465     PRO A    53                                                      
REMARK 465     GLY A    54                                                      
REMARK 465     HIS A    55                                                      
REMARK 465     THR A    56                                                      
REMARK 465     PRO A    57                                                      
REMARK 465     HIS A    58                                                      
REMARK 465     PRO A    59                                                      
REMARK 465     ALA A    60                                                      
REMARK 465     ALA A    61                                                      
REMARK 465     SER A    62                                                      
REMARK 465     ARG A    63                                                      
REMARK 465     ASP A    64                                                      
REMARK 465     PRO A    65                                                      
REMARK 465     VAL A    66                                                      
REMARK 465     ALA A    67                                                      
REMARK 465     ARG A    68                                                      
REMARK 465     THR A    69                                                      
REMARK 465     SER A    70                                                      
REMARK 465     PRO A    71                                                      
REMARK 465     LEU A    72                                                      
REMARK 465     GLN A    73                                                      
REMARK 465     THR A    74                                                      
REMARK 465     PRO A    75                                                      
REMARK 465     ALA A    76                                                      
REMARK 465     ALA A    77                                                      
REMARK 465     PRO A    78                                                      
REMARK 465     GLY A    79                                                      
REMARK 465     ALA A    80                                                      
REMARK 465     ALA A    81                                                      
REMARK 465     ALA A    82                                                      
REMARK 465     GLY A    83                                                      
REMARK 465     PRO A    84                                                      
REMARK 465     ALA A    85                                                      
REMARK 465     LEU A    86                                                      
REMARK 465     HIS A   210                                                      
REMARK 465     HIS A   211                                                      
REMARK 465     HIS A   212                                                      
REMARK 465     HIS A   213                                                      
REMARK 465     HIS A   214                                                      
REMARK 465     HIS A   215                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     GLY B   118                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     ALA C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     ARG C     6                                                      
REMARK 465     GLY C    33                                                      
REMARK 465     ASP C    34                                                      
REMARK 465     VAL C    35                                                      
REMARK 465     GLY C    36                                                      
REMARK 465     ALA C    37                                                      
REMARK 465     ALA C    38                                                      
REMARK 465     PRO C    39                                                      
REMARK 465     PRO C    40                                                      
REMARK 465     GLY C    41                                                      
REMARK 465     ALA C    42                                                      
REMARK 465     ALA C    43                                                      
REMARK 465     PRO C    44                                                      
REMARK 465     ALA C    45                                                      
REMARK 465     PRO C    46                                                      
REMARK 465     GLY C    47                                                      
REMARK 465     ILE C    48                                                      
REMARK 465     PHE C    49                                                      
REMARK 465     SER C    50                                                      
REMARK 465     SER C    51                                                      
REMARK 465     GLN C    52                                                      
REMARK 465     PRO C    53                                                      
REMARK 465     GLY C    54                                                      
REMARK 465     HIS C    55                                                      
REMARK 465     THR C    56                                                      
REMARK 465     PRO C    57                                                      
REMARK 465     HIS C    58                                                      
REMARK 465     PRO C    59                                                      
REMARK 465     ALA C    60                                                      
REMARK 465     ALA C    61                                                      
REMARK 465     SER C    62                                                      
REMARK 465     ARG C    63                                                      
REMARK 465     ASP C    64                                                      
REMARK 465     PRO C    65                                                      
REMARK 465     VAL C    66                                                      
REMARK 465     ALA C    67                                                      
REMARK 465     ARG C    68                                                      
REMARK 465     THR C    69                                                      
REMARK 465     SER C    70                                                      
REMARK 465     PRO C    71                                                      
REMARK 465     LEU C    72                                                      
REMARK 465     GLN C    73                                                      
REMARK 465     THR C    74                                                      
REMARK 465     PRO C    75                                                      
REMARK 465     ALA C    76                                                      
REMARK 465     ALA C    77                                                      
REMARK 465     PRO C    78                                                      
REMARK 465     GLY C    79                                                      
REMARK 465     ALA C    80                                                      
REMARK 465     ALA C    81                                                      
REMARK 465     ALA C    82                                                      
REMARK 465     GLY C    83                                                      
REMARK 465     PRO C    84                                                      
REMARK 465     ALA C    85                                                      
REMARK 465     LEU C    86                                                      
REMARK 465     HIS C   210                                                      
REMARK 465     HIS C   211                                                      
REMARK 465     HIS C   212                                                      
REMARK 465     HIS C   213                                                      
REMARK 465     HIS C   214                                                      
REMARK 465     HIS C   215                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     GLY D   118                                                      
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 C   344     O    HOH D   223              2.15            
REMARK 500   OE1  GLN B    24     NH1  ARG D    20              2.17            
REMARK 500   O    HOH B   203     O    HOH B   210              2.19            
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    TYR B  63   CB    TYR B  63   CG     -0.093                       
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    ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 127   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 146   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    LEU A 181   CA  -  CB  -  CG  ANGL. DEV. =  16.8 DEGREES          
REMARK 500    ARG B  18   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG B  67   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG B  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG B  92   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B 112   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG C 106   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG C 107   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG C 146   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    LEU D  38   CA  -  CB  -  CG  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    ARG D  51   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG D 101   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG D 101   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 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    GLN A 118       42.14    -86.47                                   
REMARK 500    GLU A 165       32.81     70.62                                   
REMARK 500    GLN C 118       44.48    -89.12                                   
REMARK 500    LEU D  38       49.03    -99.41                                   
REMARK 500    LEU D 115      -70.31    -61.40                                   
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 ASP B   37     LEU B   38                 -149.65                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5JSB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OYD   RELATED DB: PDB                                   
DBREF  5JSN A    1   207  UNP    P10415   BCL2_HUMAN       1    207             
DBREF  5JSN B    1   118  PDB    5JSN     5JSN             1    118             
DBREF  5JSN C    1   207  UNP    P10415   BCL2_HUMAN       1    207             
DBREF  5JSN D    1   118  PDB    5JSN     5JSN             1    118             
SEQADV 5JSN LEU A  208  UNP  P10415              EXPRESSION TAG                 
SEQADV 5JSN GLU A  209  UNP  P10415              EXPRESSION TAG                 
SEQADV 5JSN HIS A  210  UNP  P10415              EXPRESSION TAG                 
SEQADV 5JSN HIS A  211  UNP  P10415              EXPRESSION TAG                 
SEQADV 5JSN HIS A  212  UNP  P10415              EXPRESSION TAG                 
SEQADV 5JSN HIS A  213  UNP  P10415              EXPRESSION TAG                 
SEQADV 5JSN HIS A  214  UNP  P10415              EXPRESSION TAG                 
SEQADV 5JSN HIS A  215  UNP  P10415              EXPRESSION TAG                 
SEQADV 5JSN LEU C  208  UNP  P10415              EXPRESSION TAG                 
SEQADV 5JSN GLU C  209  UNP  P10415              EXPRESSION TAG                 
SEQADV 5JSN HIS C  210  UNP  P10415              EXPRESSION TAG                 
SEQADV 5JSN HIS C  211  UNP  P10415              EXPRESSION TAG                 
SEQADV 5JSN HIS C  212  UNP  P10415              EXPRESSION TAG                 
SEQADV 5JSN HIS C  213  UNP  P10415              EXPRESSION TAG                 
SEQADV 5JSN HIS C  214  UNP  P10415              EXPRESSION TAG                 
SEQADV 5JSN HIS C  215  UNP  P10415              EXPRESSION TAG                 
SEQRES   1 A  215  MET ALA HIS ALA GLY ARG THR GLY TYR ASP ASN ARG GLU          
SEQRES   2 A  215  ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER GLN ARG          
SEQRES   3 A  215  GLY TYR GLU TRP ASP ALA GLY ASP VAL GLY ALA ALA PRO          
SEQRES   4 A  215  PRO GLY ALA ALA PRO ALA PRO GLY ILE PHE SER SER GLN          
SEQRES   5 A  215  PRO GLY HIS THR PRO HIS PRO ALA ALA SER ARG ASP PRO          
SEQRES   6 A  215  VAL ALA ARG THR SER PRO LEU GLN THR PRO ALA ALA PRO          
SEQRES   7 A  215  GLY ALA ALA ALA GLY PRO ALA LEU SER PRO VAL PRO PRO          
SEQRES   8 A  215  VAL VAL HIS LEU THR LEU ARG GLN ALA GLY ASP ASP PHE          
SEQRES   9 A  215  SER ARG ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER          
SEQRES  10 A  215  GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE          
SEQRES  11 A  215  ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN          
SEQRES  12 A  215  TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL          
SEQRES  13 A  215  MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU          
SEQRES  14 A  215  VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN          
SEQRES  15 A  215  ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP          
SEQRES  16 A  215  ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG LEU          
SEQRES  17 A  215  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 B  118  MET ALA ASP PRO LYS LYS VAL LEU ASP LYS ALA LYS ASP          
SEQRES   2 B  118  GLU ALA GLU ASN ARG VAL ARG GLU LEU LYS GLN ARG LEU          
SEQRES   3 B  118  GLU GLU LEU TYR LYS GLU ALA ARG LYS LEU ASP LEU THR          
SEQRES   4 B  118  GLN GLU MET ARG GLN GLU LEU VAL ASP LYS ALA ARG ALA          
SEQRES   5 B  118  ALA SER LEU GLN ALA ASN GLY ASP ILE PHE TYR ALA ILE          
SEQRES   6 B  118  LEU ARG ALA LEU ALA GLU ALA GLU LYS LEU LYS LYS ALA          
SEQRES   7 B  118  GLY LEU VAL ASN SER GLN GLN LEU ASP GLU LEU LYS ARG          
SEQRES   8 B  118  ARG LEU GLU GLU LEU ALA GLU GLU ALA ARG ARG LYS ALA          
SEQRES   9 B  118  GLU LYS LEU ARG ASP GLU PHE ARG LEU LYS LEU GLU TYR          
SEQRES  10 B  118  GLY                                                          
SEQRES   1 C  215  MET ALA HIS ALA GLY ARG THR GLY TYR ASP ASN ARG GLU          
SEQRES   2 C  215  ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER GLN ARG          
SEQRES   3 C  215  GLY TYR GLU TRP ASP ALA GLY ASP VAL GLY ALA ALA PRO          
SEQRES   4 C  215  PRO GLY ALA ALA PRO ALA PRO GLY ILE PHE SER SER GLN          
SEQRES   5 C  215  PRO GLY HIS THR PRO HIS PRO ALA ALA SER ARG ASP PRO          
SEQRES   6 C  215  VAL ALA ARG THR SER PRO LEU GLN THR PRO ALA ALA PRO          
SEQRES   7 C  215  GLY ALA ALA ALA GLY PRO ALA LEU SER PRO VAL PRO PRO          
SEQRES   8 C  215  VAL VAL HIS LEU THR LEU ARG GLN ALA GLY ASP ASP PHE          
SEQRES   9 C  215  SER ARG ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER          
SEQRES  10 C  215  GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE          
SEQRES  11 C  215  ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN          
SEQRES  12 C  215  TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL          
SEQRES  13 C  215  MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU          
SEQRES  14 C  215  VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN          
SEQRES  15 C  215  ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP          
SEQRES  16 C  215  ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG LEU          
SEQRES  17 C  215  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 D  118  MET ALA ASP PRO LYS LYS VAL LEU ASP LYS ALA LYS ASP          
SEQRES   2 D  118  GLU ALA GLU ASN ARG VAL ARG GLU LEU LYS GLN ARG LEU          
SEQRES   3 D  118  GLU GLU LEU TYR LYS GLU ALA ARG LYS LEU ASP LEU THR          
SEQRES   4 D  118  GLN GLU MET ARG GLN GLU LEU VAL ASP LYS ALA ARG ALA          
SEQRES   5 D  118  ALA SER LEU GLN ALA ASN GLY ASP ILE PHE TYR ALA ILE          
SEQRES   6 D  118  LEU ARG ALA LEU ALA GLU ALA GLU LYS LEU LYS LYS ALA          
SEQRES   7 D  118  GLY LEU VAL ASN SER GLN GLN LEU ASP GLU LEU LYS ARG          
SEQRES   8 D  118  ARG LEU GLU GLU LEU ALA GLU GLU ALA ARG ARG LYS ALA          
SEQRES   9 D  118  GLU LYS LEU ARG ASP GLU PHE ARG LEU LYS LEU GLU TYR          
SEQRES  10 D  118  GLY                                                          
FORMUL   5  HOH   *152(H2 O)                                                    
HELIX    1 AA1 ASP A   10  GLN A   25  1                                  16    
HELIX    2 AA2 PRO A   90  GLN A  118  1                                  29    
HELIX    3 AA3 THR A  125  PHE A  138  1                                  14    
HELIX    4 AA4 ASN A  143  ARG A  164  1                                  22    
HELIX    5 AA5 PRO A  168  LEU A  185  1                                  18    
HELIX    6 AA6 LEU A  185  ASN A  192  1                                   8    
HELIX    7 AA7 GLY A  193  ARG A  207  1                                  15    
HELIX    8 AA8 LEU A  208  GLU A  209  5                                   2    
HELIX    9 AA9 ASP B    3  ASP B    3  5                                   1    
HELIX   10 AB1 PRO B    4  LYS B   35  1                                  32    
HELIX   11 AB2 THR B   39  ALA B   78  1                                  40    
HELIX   12 AB3 ASN B   82  TYR B  117  1                                  36    
HELIX   13 AB4 ASP C   10  GLN C   25  1                                  16    
HELIX   14 AB5 PRO C   90  TYR C  108  1                                  19    
HELIX   15 AB6 TYR C  108  GLN C  118  1                                  11    
HELIX   16 AB7 PHE C  124  PHE C  138  1                                  15    
HELIX   17 AB8 ASN C  143  ARG C  164  1                                  22    
HELIX   18 AB9 PRO C  168  LEU C  185  1                                  18    
HELIX   19 AC1 LEU C  185  ASN C  192  1                                   8    
HELIX   20 AC2 GLY C  193  ARG C  207  1                                  15    
HELIX   21 AC3 PRO D    4  LYS D   35  1                                  32    
HELIX   22 AC4 THR D   39  ALA D   78  1                                  40    
HELIX   23 AC5 ASN D   82  TYR D  117  1                                  36    
CRYST1   65.005   65.005  134.314  90.00  90.00  90.00 P 41          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      0.015383  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015383  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007445        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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