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Database: PDB
Entry: 1FGB
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HEADER    ENTEROTOXIN                             21-FEB-96   1FGB              
TITLE     TOXIN                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA TOXIN B SUBUNIT PENTAMER;                          
COMPND   3 CHAIN: D, E, F, G, H;                                                
COMPND   4 SYNONYM: CHOLERAGENOID                                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   3 ORGANISM_TAXID: 44104;                                               
SOURCE   4 STRAIN: 569B                                                         
KEYWDS    CHOLERA TOXIN, CHOLERAGENOID, ENTEROTOXIN, ADP-RIBOSYLATION           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.-G.ZHANG,E.WESTBROOK                                                
REVDAT   3   13-JUL-11 1FGB    1       VERSN                                    
REVDAT   2   24-FEB-09 1FGB    1       VERSN                                    
REVDAT   1   23-DEC-96 1FGB    0                                                
JRNL        AUTH   R.G.ZHANG,M.L.WESTBROOK,E.M.WESTBROOK,D.L.SCOTT,             
JRNL        AUTH 2 Z.OTWINOWSKI,P.R.MAULIK,R.A.REED,G.G.SHIPLEY                 
JRNL        TITL   THE 2.4 A CRYSTAL STRUCTURE OF CHOLERA TOXIN B SUBUNIT       
JRNL        TITL 2 PENTAMER: CHOLERAGENOID.                                     
JRNL        REF    J.MOL.BIOL.                   V. 251   550 1995              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   7658472                                                      
JRNL        DOI    10.1006/JMBI.1995.0455                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.G.ZHANG,D.L.SCOTT,M.L.WESTBROOK,S.NANCE,B.D.SPANGLER,      
REMARK   1  AUTH 2 G.G.SHIPLEY,E.M.WESTBROOK                                    
REMARK   1  TITL   THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF CHOLERA TOXIN     
REMARK   1  REF    J.MOL.BIOL.                   V. 251   563 1995              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROFFT, X-PLOR                                       
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON,FINZEL,BRUNGER                   
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.500                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 16703                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
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  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
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            : 4070                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 204                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.37                          
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.019 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.037 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.038 ; 0.060               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1FGB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-89                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN                             
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
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     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.04800                            
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   (%): 42.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       47.25000            
REMARK 290   SMTRY3   2  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: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12270 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, G, H                         
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 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    SER E    55     N    GLN E    56              1.68            
REMARK 500   O    HOH E   116     O    HOH E   157              1.69            
REMARK 500   OE2  GLU D    11     O    HOH D   108              1.74            
REMARK 500   OG1  THR E    28     O    HOH E   116              1.97            
REMARK 500   O    SER D    55     N    HIS D    57              2.03            
REMARK 500   NH2  ARG H    35     O    HOH D   108              2.12            
REMARK 500   O    VAL E    52     O    HOH E   156              2.15            
REMARK 500   OD1  ASP H    22     O    HOH H   130              2.16            
REMARK 500   OE2  GLU G    29     O    HOH G   105              2.16            
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   NZ   LYS F    43     O    SER F    55     1455     1.81            
REMARK 500   CE   LYS F    43     O    SER F    55     1455     2.10            
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    VAL D  52   C     PRO D  53   N       0.132                       
REMARK 500    GLY E  54   C     SER E  55   N       0.239                       
REMARK 500    GLY F  54   C     SER F  55   N       0.285                       
REMARK 500    SER F  55   C     GLN F  56   N       0.234                       
REMARK 500    GLN F  56   C     HIS F  57   N      -0.329                       
REMARK 500    SER F 100   CB    SER F 100   OG     -0.083                       
REMARK 500    ALA G  64   C     ILE G  65   N       0.147                       
REMARK 500    ALA H  64   C     ILE H  65   N       0.171                       
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    GLN D   3   CA  -  CB  -  CG  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    CYS D   9   CB  -  CA  -  C   ANGL. DEV. =   7.8 DEGREES          
REMARK 500    HIS D  18   CA  -  C   -  N   ANGL. DEV. = -14.5 DEGREES          
REMARK 500    HIS D  18   O   -  C   -  N   ANGL. DEV. =  12.0 DEGREES          
REMARK 500    LYS D  34   CB  -  CG  -  CD  ANGL. DEV. =  18.1 DEGREES          
REMARK 500    ARG D  35   CD  -  NE  -  CZ  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    MET D  37   N   -  CA  -  CB  ANGL. DEV. = -11.3 DEGREES          
REMARK 500    PHE D  42   CB  -  CG  -  CD1 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ILE D  58   O   -  C   -  N   ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    ALA D  64   CA  -  C   -  N   ANGL. DEV. =  16.6 DEGREES          
REMARK 500    ALA D  64   O   -  C   -  N   ANGL. DEV. = -18.4 DEGREES          
REMARK 500    ARG D  67   NE  -  CZ  -  NH1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG D  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASP D  70   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP D  70   CB  -  CG  -  OD2 ANGL. DEV. = -10.4 DEGREES          
REMARK 500    ASP D  70   O   -  C   -  N   ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ARG D  73   CD  -  NE  -  CZ  ANGL. DEV. =  22.0 DEGREES          
REMARK 500    ARG D  73   NE  -  CZ  -  NH1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG D  73   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    THR D  78   N   -  CA  -  CB  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    GLU D  79   N   -  CA  -  CB  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    LYS D  81   N   -  CA  -  CB  ANGL. DEV. =  17.8 DEGREES          
REMARK 500    GLU D  83   OE1 -  CD  -  OE2 ANGL. DEV. =  -9.0 DEGREES          
REMARK 500    LEU D  85   CA  -  CB  -  CG  ANGL. DEV. =  28.4 DEGREES          
REMARK 500    LYS D  91   N   -  CA  -  CB  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    ASP E   7   CB  -  CG  -  OD1 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    ASP E   7   CB  -  CG  -  OD2 ANGL. DEV. =   8.6 DEGREES          
REMARK 500    HIS E  13   CA  -  CB  -  CG  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    HIS E  13   C   -  N   -  CA  ANGL. DEV. =  17.9 DEGREES          
REMARK 500    ASN E  21   N   -  CA  -  CB  ANGL. DEV. =  11.1 DEGREES          
REMARK 500    ARG E  35   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES          
REMARK 500    ALA E  38   CB  -  CA  -  C   ANGL. DEV. =   9.3 DEGREES          
REMARK 500    THR E  41   C   -  N   -  CA  ANGL. DEV. =  16.8 DEGREES          
REMARK 500    SER E  55   C   -  N   -  CA  ANGL. DEV. = -17.8 DEGREES          
REMARK 500    SER E  55   CA  -  C   -  N   ANGL. DEV. =  38.0 DEGREES          
REMARK 500    SER E  55   O   -  C   -  N   ANGL. DEV. = -40.2 DEGREES          
REMARK 500    GLN E  56   C   -  N   -  CA  ANGL. DEV. =  32.2 DEGREES          
REMARK 500    GLN E  56   CA  -  C   -  N   ANGL. DEV. =  21.0 DEGREES          
REMARK 500    GLN E  56   O   -  C   -  N   ANGL. DEV. = -24.1 DEGREES          
REMARK 500    ARG E  67   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG E  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP E  70   CB  -  CG  -  OD2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    ARG E  73   CD  -  NE  -  CZ  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ASN E  89   CB  -  CA  -  C   ANGL. DEV. =  13.8 DEGREES          
REMARK 500    ASP F   7   CB  -  CA  -  C   ANGL. DEV. =  13.2 DEGREES          
REMARK 500    ASP F   7   CB  -  CG  -  OD1 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    ASP F   7   CB  -  CG  -  OD2 ANGL. DEV. =  -9.5 DEGREES          
REMARK 500    ALA F  10   C   -  N   -  CA  ANGL. DEV. =  16.8 DEGREES          
REMARK 500    THR F  15   N   -  CA  -  CB  ANGL. DEV. = -14.5 DEGREES          
REMARK 500    THR F  15   OG1 -  CB  -  CG2 ANGL. DEV. =  16.0 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     114 ANGLE DEVIATIONS.                             
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    PRO D   2      153.86    -49.42                                   
REMARK 500    ASN D  14       57.78    -95.74                                   
REMARK 500    GLN D  16      143.41   -170.15                                   
REMARK 500    ARG D  35       41.19   -140.96                                   
REMARK 500    LYS D  43        0.87    -66.60                                   
REMARK 500    SER D  55      -76.58    -47.73                                   
REMARK 500    GLN D  56       64.44    -55.44                                   
REMARK 500    HIS D  57       89.91   -154.52                                   
REMARK 500    ALA D  80     -126.31     24.14                                   
REMARK 500    LYS D  81       92.82     99.56                                   
REMARK 500    ASN E  14       53.32   -118.30                                   
REMARK 500    GLN E  16      146.70   -179.77                                   
REMARK 500    LYS E  34       -4.02     77.53                                   
REMARK 500    GLU E  36       93.49    -64.43                                   
REMARK 500    SER E  55     -106.09    -56.86                                   
REMARK 500    GLN E  56       13.40     28.88                                   
REMARK 500    GLU E  79       30.97     73.08                                   
REMARK 500    GLU E  83      -71.60    -77.85                                   
REMARK 500    GLN F  16      144.69   -176.14                                   
REMARK 500    ARG F  35       47.61   -140.31                                   
REMARK 500    GLN F  56      -13.69    -44.69                                   
REMARK 500    ASP F  59      -53.26    111.61                                   
REMARK 500    ALA F  80      -79.62    -34.44                                   
REMARK 500    LYS F  81       94.96     97.34                                   
REMARK 500    ASN F  90       30.89    -83.19                                   
REMARK 500    PRO F  93     -177.11    -68.41                                   
REMARK 500    ASN G  14       45.11   -103.17                                   
REMARK 500    ARG G  35       26.03   -145.35                                   
REMARK 500    PRO G  53       86.32    -60.84                                   
REMARK 500    ALA G  80      -81.78    -19.43                                   
REMARK 500    LYS G  81       94.88     87.28                                   
REMARK 500    ASN G  90       30.77    -73.45                                   
REMARK 500    GLN H   3      -24.87     71.90                                   
REMARK 500    ASN H  14       47.41    -94.73                                   
REMARK 500    GLN H  16      140.94    176.09                                   
REMARK 500    GLU H  79       60.26     68.50                                   
REMARK 500    ALA H  80      -80.23    -13.05                                   
REMARK 500    LYS H  81       90.57     74.71                                   
REMARK 500    GLU H  83      -67.85    -95.08                                   
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 SER F   55     GLN F   56                  133.97                    
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 D  18         0.10    SIDE CHAIN                              
REMARK 500    HIS E  18         0.09    SIDE CHAIN                              
REMARK 500    ARG E  67         0.15    SIDE CHAIN                              
REMARK 500    HIS F  18         0.10    SIDE CHAIN                              
REMARK 500    ARG F  35         0.12    SIDE CHAIN                              
REMARK 500    ARG F  67         0.11    SIDE CHAIN                              
REMARK 500    HIS G  18         0.10    SIDE CHAIN                              
REMARK 500    HIS H  18         0.10    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    VAL D  87         13.19                                           
REMARK 500    VAL E  50         11.47                                           
REMARK 500    SER E  55         43.08                                           
REMARK 500    GLN E  56        -18.83                                           
REMARK 500    GLY F  54         26.17                                           
REMARK 500    SER F  55        -11.41                                           
REMARK 500    TYR G  12        -11.40                                           
REMARK 500    ALA G  64         22.09                                           
REMARK 500    LEU H  20         10.36                                           
REMARK 500    VAL H  87         13.73                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    HIS D  13        22.2      L          L   OUTSIDE RANGE           
REMARK 500    GLU D  79        23.6      L          L   OUTSIDE RANGE           
REMARK 500    LYS D  81        24.8      L          L   OUTSIDE RANGE           
REMARK 500    LYS D  84        21.3      L          L   OUTSIDE RANGE           
REMARK 500    ASP E  70        22.7      L          L   OUTSIDE RANGE           
REMARK 500    ASN E  89        24.2      L          L   OUTSIDE RANGE           
REMARK 500    HIS F  13        21.8      L          L   OUTSIDE RANGE           
REMARK 500    LYS F  43        23.4      L          L   OUTSIDE RANGE           
REMARK 500    ILE F  58        18.6      L          L   OUTSIDE RANGE           
REMARK 500    THR F  92        24.4      L          L   OUTSIDE RANGE           
REMARK 500    LYS G  84        24.8      L          L   OUTSIDE RANGE           
REMARK 500    GLU H  51        24.4      L          L   OUTSIDE RANGE           
REMARK 500    GLU H  79        24.2      L          L   OUTSIDE RANGE           
REMARK 500    ASN H 103        17.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 119        DISTANCE =  7.24 ANGSTROMS                       
REMARK 525    HOH E 147        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH E 148        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH E 149        DISTANCE =  5.18 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: GAN                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: EACH B SUBUNIT HAS A BINDING SITE, 5 BINDING       
REMARK 800  SITES IN TOTAL.                                                     
DBREF  1FGB D    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1FGB E    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1FGB F    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1FGB G    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1FGB H    1   103  UNP    P01556   CHTB_VIBCH      22    124             
SEQADV 1FGB HIS D   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 1FGB THR D   47  UNP  P01556    ILE    68 CONFLICT                       
SEQADV 1FGB HIS E   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 1FGB THR E   47  UNP  P01556    ILE    68 CONFLICT                       
SEQADV 1FGB HIS F   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 1FGB THR F   47  UNP  P01556    ILE    68 CONFLICT                       
SEQADV 1FGB HIS G   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 1FGB THR G   47  UNP  P01556    ILE    68 CONFLICT                       
SEQADV 1FGB HIS H   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 1FGB THR H   47  UNP  P01556    ILE    68 CONFLICT                       
SEQRES   1 D  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 D  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 D  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 D  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 D  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 D  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 D  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 D  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 E  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 E  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 E  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 E  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 E  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 E  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 E  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 E  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 F  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 F  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 F  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 F  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 F  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 F  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 F  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 F  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 G  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 G  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 G  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 G  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 G  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 G  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 G  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 G  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 H  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 H  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 H  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 H  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 H  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 H  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 H  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 H  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
FORMUL   6  HOH   *204(H2 O)                                                    
HELIX    1   1 ILE D    5  GLU D   11  1                                   7    
HELIX    2   2 LYS D   63  LEU D   77  1                                  15    
HELIX    3   3 ILE E    5  GLU E   11  1                                   7    
HELIX    4   4 ASP E   59  THR E   78  1                                  20    
HELIX    5   5 ILE F    5  GLU F   11  1                                   7    
HELIX    6   6 LYS F   62  LEU F   77  1                                  16    
HELIX    7   7 ILE G    5  GLU G   11  1                                   7    
HELIX    8   8 SER G   60  THR G   78  1                                  19    
HELIX    9   9 ILE H    5  GLU H   11  1                                   7    
HELIX   10  10 LYS H   63  THR H   78  1                                  16    
SHEET    1   A 6 THR D  15  THR D  19  0                                        
SHEET    2   A 6 VAL D  82  TRP D  88 -1  N  VAL D  87   O  GLN D  16           
SHEET    3   A 6 ALA D  98  ALA D 102 -1  N  SER D 100   O  GLU D  83           
SHEET    4   A 6 SER H  26  SER H  30 -1  N  GLU H  29   O  ILE D  99           
SHEET    5   A 6 ALA H  38  THR H  41 -1  N  THR H  41   O  SER H  26           
SHEET    6   A 6 THR H  47  VAL H  50 -1  N  VAL H  50   O  ALA H  38           
SHEET    1   B 6 THR E  15  THR E  19  0                                        
SHEET    2   B 6 LYS E  84  TRP E  88 -1  N  VAL E  87   O  GLN E  16           
SHEET    3   B 6 ALA E  95  ALA E 102 -1  N  SER E 100   O  LYS E  84           
SHEET    4   B 6 SER D  26  SER D  30 -1  N  GLU D  29   O  ILE E  99           
SHEET    5   B 6 ALA D  38  THR D  41 -1  N  THR D  41   O  SER D  26           
SHEET    6   B 6 THR D  47  VAL D  50 -1  N  VAL D  50   O  ALA D  38           
SHEET    1   C 6 THR F  15  THR F  19  0                                        
SHEET    2   C 6 VAL F  82  TRP F  88 -1  N  VAL F  87   O  GLN F  16           
SHEET    3   C 6 ALA F  98  ALA F 102 -1  N  SER F 100   O  GLU F  83           
SHEET    4   C 6 SER E  26  SER E  30 -1  N  GLU E  29   O  ILE F  99           
SHEET    5   C 6 MET E  37  THR E  41 -1  N  THR E  41   O  SER E  26           
SHEET    6   C 6 THR E  47  VAL E  50 -1  N  VAL E  50   O  ALA E  38           
SHEET    1   D 6 THR G  15  THR G  19  0                                        
SHEET    2   D 6 LYS G  84  TRP G  88 -1  N  VAL G  87   O  GLN G  16           
SHEET    3   D 6 ALA G  95  ALA G 102 -1  N  SER G 100   O  LYS G  84           
SHEET    4   D 6 SER F  26  SER F  30 -1  N  GLU F  29   O  ILE G  99           
SHEET    5   D 6 MET F  37  THR F  41 -1  N  THR F  41   O  SER F  26           
SHEET    6   D 6 THR F  47  VAL F  50 -1  N  VAL F  50   O  ALA F  38           
SHEET    1   E 6 THR H  15  THR H  19  0                                        
SHEET    2   E 6 VAL H  82  TRP H  88 -1  N  VAL H  87   O  GLN H  16           
SHEET    3   E 6 ALA H  98  ALA H 102 -1  N  SER H 100   O  GLU H  83           
SHEET    4   E 6 SER G  26  SER G  30 -1  N  GLU G  29   O  ILE H  99           
SHEET    5   E 6 MET G  37  THR G  41 -1  N  THR G  41   O  SER G  26           
SHEET    6   E 6 THR G  47  VAL G  50 -1  N  VAL G  50   O  ALA G  38           
SSBOND   1 CYS D    9    CYS D   86                          1555   1555  2.03  
SSBOND   2 CYS E    9    CYS E   86                          1555   1555  2.14  
SSBOND   3 CYS F    9    CYS F   86                          1555   1555  2.05  
SSBOND   4 CYS G    9    CYS G   86                          1555   1555  2.06  
SSBOND   5 CYS H    9    CYS H   86                          1555   1555  2.09  
CISPEP   1 THR D   92    PRO D   93          0        -2.70                     
CISPEP   2 THR E   92    PRO E   93          0        -0.87                     
CISPEP   3 THR F   92    PRO F   93          0        -3.57                     
CISPEP   4 THR G   92    PRO G   93          0        -0.69                     
CISPEP   5 THR H   92    PRO H   93          0         1.25                     
SITE     1 GAN 35 ALA D  46  GLU D  51  GLN D  56  GLN D  61                    
SITE     2 GAN 35 TRP D  88  ASN D  90  LYS D  91  ALA E  46                    
SITE     3 GAN 35 GLU E  51  GLN E  56  GLN E  61  TRP E  88                    
SITE     4 GAN 35 ASN E  90  LYS E  91  ALA F  46  GLU F  51                    
SITE     5 GAN 35 GLN F  56  GLN F  61  TRP F  88  ASN F  90                    
SITE     6 GAN 35 LYS F  91  ALA G  46  GLU G  51  GLN G  56                    
SITE     7 GAN 35 GLN G  61  TRP G  88  ASN G  90  LYS G  91                    
SITE     8 GAN 35 ALA H  46  GLU H  51  GLN H  56  GLN H  61                    
SITE     9 GAN 35 TRP H  88  ASN H  90  LYS H  91                               
CRYST1   39.100   94.500   67.600  90.00  96.10  90.00 P 1 21 1     10          
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      0.025575  0.000000  0.002733        0.00000                         
SCALE2      0.000000  0.010582  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014877        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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