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Entry: 1KBA
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HEADER    TOXIN                                   13-JUL-94   1KBA              
TITLE     CRYSTAL STRUCTURE OF KAPPA-BUNGAROTOXIN AT 2.3-ANGSTROM RESOLUTION    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KAPPA-BUNGAROTOXIN;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BUNGARUS MULTICINCTUS;                          
SOURCE   3 ORGANISM_COMMON: MANY-BANDED KRAIT;                                  
SOURCE   4 ORGANISM_TAXID: 8616                                                 
KEYWDS    TOXIN                                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.C.DEWAN,G.A.GRANT,J.C.SACCHETTINI                                   
REVDAT   5   14-AUG-19 1KBA    1       REMARK                                   
REVDAT   4   17-JUL-19 1KBA    1       REMARK                                   
REVDAT   3   24-FEB-09 1KBA    1       VERSN                                    
REVDAT   2   30-SEP-03 1KBA    1       JRNL   DBREF                             
REVDAT   1   20-DEC-94 1KBA    0                                                
JRNL        AUTH   J.C.DEWAN,G.A.GRANT,J.C.SACCHETTINI                          
JRNL        TITL   CRYSTAL STRUCTURE OF KAPPA-BUNGAROTOXIN AT 2.3-A RESOLUTION. 
JRNL        REF    BIOCHEMISTRY                  V.  33 13147 1994              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   7947721                                                      
JRNL        DOI    10.1021/BI00248A026                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 13.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 5354                           
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1002                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 56                                      
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : NULL  ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : NULL                                             
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1KBA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000174399.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6602                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z                                                
REMARK 290       6555   X-Y,X,Z                                                 
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
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        0.00000            
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: DODECAMERIC                       
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   BIOMT1   2  0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   4 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   5 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   5  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000  1.000000        0.00000            
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    PRO A   7   C   -  N   -  CD  ANGL. DEV. = -14.1 DEGREES          
REMARK 500    PRO A  15   C   -  N   -  CD  ANGL. DEV. = -47.5 DEGREES          
REMARK 500    LEU A  23   CB  -  CG  -  CD2 ANGL. DEV. = -12.0 DEGREES          
REMARK 500    PRO A  36   C   -  N   -  CD  ANGL. DEV. = -13.3 DEGREES          
REMARK 500    LEU A  57   CB  -  CG  -  CD2 ANGL. DEV. =  10.9 DEGREES          
REMARK 500    LEU B   4   CA  -  CB  -  CG  ANGL. DEV. = -18.9 DEGREES          
REMARK 500    SER B   6   N   -  CA  -  C   ANGL. DEV. =  18.8 DEGREES          
REMARK 500    PRO B  15   C   -  N   -  CD  ANGL. DEV. = -16.8 DEGREES          
REMARK 500    PRO B  47   C   -  N   -  CD  ANGL. DEV. = -13.2 DEGREES          
REMARK 500    CYS B  59   CA  -  CB  -  SG  ANGL. DEV. = -14.5 DEGREES          
REMARK 500    ASP B  62   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 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    SER A   6     -108.12     -7.35                                   
REMARK 500    PHE A  49       95.00    -66.64                                   
REMARK 500    SER A  55      148.35    160.13                                   
REMARK 500    THR A  61      145.46   -177.78                                   
REMARK 500    SER B   6      -69.62    -20.11                                   
REMARK 500    ASN B  16      119.83    -32.02                                   
REMARK 500    ALA B  25      118.82   -160.65                                   
REMARK 500    ASP B  28     -169.97   -126.79                                   
REMARK 500    CYS B  31        5.36    -67.82                                   
REMARK 500    ARG B  34      -36.04   -139.51                                   
REMARK 500    ASN B  52       34.24    -70.45                                   
REMARK 500    LEU B  56      111.35   -162.32                                   
REMARK 500    THR B  60       75.58   -116.98                                   
REMARK 500    ASN B  63       45.11     33.64                                   
REMARK 500    ASN B  65       74.89    -56.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1NBT   RELATED DB: PDB                                   
REMARK 900 1NBT REPORTS AN NMR STRUCTURE DETERMINATION FOR KAPPA-BUNGAROTOXIN.  
REMARK 900 SEE THE FOLLOWING TWO REFERENCES: M.J.SUTCLIFFE, C.M.DOBSON,         
REMARK 900 R.E.OSWALD, "SOLUTION STRUCTURE OF NEURONAL BUNGAROTOXIN DETERMINED  
REMARK 900 BY TWO-DIMENSIONAL NMR SPECTROSCOPY: CALCULATION OF TERTIARY         
REMARK 900 STRUCTURE USING SYSTEMATIC HOMOLOGOUS MODEL BUILDING, DYNAMICAL      
REMARK 900 SIMULATED ANNEALING, AND RESTRAINED MOLECULAR DYNAMICS".             
REMARK 900 BIOCHEMISTRY (1992) V. 31, 2962-2970. R.E.OSWALD, M.J.SUTCLIFFE,     
REMARK 900 M.BAMBERGER, R.H.LORING, E.BRASWELL, C.M.DOBSON, "SOLUTION           
REMARK 900 STRUCTURE OF NEURONAL BUNGAROTOXIN DETERMINED BY TWO-DIMENSIONAL     
REMARK 900 NMR SPECTROSCOPY: SEQUENCE-SPECIFIC ASSIGNMENTS, SECONDARY           
REMARK 900 STRUCTURE, AND DIMER FORMATION". BIOCHEMISTRY (1991) V. 30, 4901-    
REMARK 900 4909.                                                                
DBREF  1KBA A    1    66  UNP    P01398   NXL1_BUNMU      22     87             
DBREF  1KBA B    1    66  UNP    P01398   NXL1_BUNMU      22     87             
SEQRES   1 A   66  ARG THR CYS LEU ILE SER PRO SER SER THR PRO GLN THR          
SEQRES   2 A   66  CYS PRO ASN GLY GLN ASP ILE CYS PHE LEU LYS ALA GLN          
SEQRES   3 A   66  CYS ASP LYS PHE CYS SER ILE ARG GLY PRO VAL ILE GLU          
SEQRES   4 A   66  GLN GLY CYS VAL ALA THR CYS PRO GLN PHE ARG SER ASN          
SEQRES   5 A   66  TYR ARG SER LEU LEU CYS CYS THR THR ASP ASN CYS ASN          
SEQRES   6 A   66  HIS                                                          
SEQRES   1 B   66  ARG THR CYS LEU ILE SER PRO SER SER THR PRO GLN THR          
SEQRES   2 B   66  CYS PRO ASN GLY GLN ASP ILE CYS PHE LEU LYS ALA GLN          
SEQRES   3 B   66  CYS ASP LYS PHE CYS SER ILE ARG GLY PRO VAL ILE GLU          
SEQRES   4 B   66  GLN GLY CYS VAL ALA THR CYS PRO GLN PHE ARG SER ASN          
SEQRES   5 B   66  TYR ARG SER LEU LEU CYS CYS THR THR ASP ASN CYS ASN          
SEQRES   6 B   66  HIS                                                          
FORMUL   3  HOH   *56(H2 O)                                                     
HELIX    1   1 PHE A   30  GLY A   35  1                                   6    
SHEET    1  SA 5 ARG A   1  ILE A   5  0                                        
SHEET    2  SA 5 THR A  10  CYS A  14  1                                        
SHEET    3  SA 5 ILE A  20  GLN A  26  1                                        
SHEET    4  SA 5 VAL A  37  VAL A  43  1                                        
SHEET    5  SA 5 ARG A  54  THR A  60  1                                        
SHEET    1  SB 5 ARG B   1  ILE B   5  0                                        
SHEET    2  SB 5 THR B  10  CYS B  14  1                                        
SHEET    3  SB 5 ILE B  20  GLN B  26  1                                        
SHEET    4  SB 5 VAL B  37  VAL B  43  1                                        
SHEET    5  SB 5 ARG B  54  THR B  60  1                                        
SSBOND   1 CYS A    3    CYS A   21                          1555   1555  2.03  
SSBOND   2 CYS A   14    CYS A   42                          1555   1555  2.04  
SSBOND   3 CYS A   27    CYS A   31                          1555   1555  2.02  
SSBOND   4 CYS A   46    CYS A   58                          1555   1555  2.03  
SSBOND   5 CYS A   59    CYS A   64                          1555   1555  2.04  
SSBOND   6 CYS B    3    CYS B   21                          1555   1555  2.02  
SSBOND   7 CYS B   14    CYS B   42                          1555   1555  2.02  
SSBOND   8 CYS B   27    CYS B   31                          1555   1555  2.02  
SSBOND   9 CYS B   46    CYS B   58                          1555   1555  2.03  
SSBOND  10 CYS B   59    CYS B   64                          1555   1555  2.04  
CRYST1   80.200   80.200   39.600  90.00  90.00 120.00 P 6          12          
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      0.012469  0.007199  0.000000        0.00000                         
SCALE2      0.000000  0.014398  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.025253        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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