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Database: PDB
Entry: 1LLR
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HEADER    TOXIN                                   30-APR-02   1LLR              
TITLE     CHOLERA TOXIN B-PENTAMER WITH LIGAND BMSC-0012                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA TOXIN B SUBUNIT;                                   
COMPND   3 CHAIN: D, E, F, G, H;                                                
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   3 ORGANISM_TAXID: 666;                                                 
SOURCE   4 GENE: CTXB;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ENTEROTOXIN, RECEPTOR, B-PENTAMER                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.A.MERRITT,W.G.J.HOL                                                 
REVDAT   3   24-FEB-09 1LLR    1       VERSN                                    
REVDAT   2   01-APR-03 1LLR    1       JRNL                                     
REVDAT   1   14-AUG-02 1LLR    0                                                
JRNL        AUTH   E.A.MERRITT,Z.ZHANG,J.C.PICKENS,M.AHN,W.G.HOL,E.FAN          
JRNL        TITL   CHARACTERIZATION AND CRYSTAL STRUCTURE OF A                  
JRNL        TITL 2 HIGH-AFFINITY PENTAVALENT RECEPTOR-BINDING                   
JRNL        TITL 3 INHIBITOR FOR CHOLERA TOXIN AND E. COLI                      
JRNL        TITL 4 HEAT-LABILE ENTEROTOXIN.                                     
JRNL        REF    J.AM.CHEM.SOC.                V. 124  8818 2002              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   12137534                                                     
JRNL        DOI    10.1021/JA0202560                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.46 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 4                                             
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.46                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 84750                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : RFREE                           
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.149                           
REMARK   3   R VALUE            (WORKING SET) : 0.149                           
REMARK   3   FREE R VALUE                     : 0.191                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4244                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4098                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 225                                     
REMARK   3   SOLVENT ATOMS            : 570                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.080         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.070         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.044         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.177         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.020 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.040 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
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) : 0.160 ; 0.150               
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) : 1.060 ; 1.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.600 ; 1.500                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.480 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.440 ; 3.000                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: PROTEIN + FNG RESIDUES REFINED WITH       
REMARK   3  ANISOTROPIC UIJ. REMAINDER OF LIGAND ATOMS IN MODEL REFINED         
REMARK   3  WITH ISOTROPIC U.                                                   
REMARK   4                                                                      
REMARK   4 1LLR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB016062.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-MAR-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM-MADE                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 84902                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.460                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.51                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 300, NACL, MGCL2, TRIS HCL, PH       
REMARK 280  7.50, VAPOR DIFFUSION, SITTING DROP                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       51.19550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.98200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       51.19550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       32.98200            
REMARK 290   SMTRY3   4  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: 17850 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 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   OE1  GLN E    16     ND2  ASN E    89              2.12            
REMARK 500   O    HOH H  1579     O    HOH H  1603              2.13            
REMARK 500   CE   LYS E    81     O    ALA E   102              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH D   170     O    HOH E   177     4445     1.87            
REMARK 500   NZ   LYS H    43     O    HOH F  1376     4546     1.88            
REMARK 500   OG   SER E    55     OD1  ASP G    59     2555     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    GLU E  29   CB    GLU E  29   CG     -0.140                       
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    THR D   1   OG1 -  CB  -  CG2 ANGL. DEV. =  16.8 DEGREES          
REMARK 500    THR D   1   CA  -  CB  -  OG1 ANGL. DEV. = -16.7 DEGREES          
REMARK 500    THR D   1   CA  -  CB  -  CG2 ANGL. DEV. = -12.9 DEGREES          
REMARK 500    TYR D  12   CZ  -  CE2 -  CD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    HIS D  13   CA  -  CB  -  CG  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    HIS D  18   CE1 -  NE2 -  CD2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ASP D  22   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG D  35   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG D  35   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG D  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    LYS D  81   CG  -  CD  -  CE  ANGL. DEV. =  19.4 DEGREES          
REMARK 500    LYS D  81   CD  -  CE  -  NZ  ANGL. DEV. =  29.3 DEGREES          
REMARK 500    HIS D  94   CE1 -  NE2 -  CD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASN D 103   CA  -  CB  -  CG  ANGL. DEV. =  16.4 DEGREES          
REMARK 500    CYS E   9   CA  -  CB  -  SG  ANGL. DEV. =  10.6 DEGREES          
REMARK 500    TYR E  12   CB  -  CG  -  CD2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    TYR E  12   CB  -  CG  -  CD1 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    GLU E  29   CA  -  CB  -  CG  ANGL. DEV. =  15.9 DEGREES          
REMARK 500    GLU E  29   OE1 -  CD  -  OE2 ANGL. DEV. =  12.3 DEGREES          
REMARK 500    GLU E  29   CG  -  CD  -  OE2 ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ARG E  35   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG E  35   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ARG E  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    GLU E  83   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    THR F   1   N   -  CA  -  CB  ANGL. DEV. = -12.1 DEGREES          
REMARK 500    ASP F   7   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    GLU F  11   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    TYR F  12   CB  -  CG  -  CD1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    LYS F  34   CB  -  CG  -  CD  ANGL. DEV. =  17.2 DEGREES          
REMARK 500    PHE F  48   CB  -  CG  -  CD1 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    LYS F  62   CB  -  CG  -  CD  ANGL. DEV. =  16.8 DEGREES          
REMARK 500    ARG F  67   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG F  73   CD  -  NE  -  CZ  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ALA F 102   O   -  C   -  N   ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ASP G   7   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    GLU G  11   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.4 DEGREES          
REMARK 500    TYR G  12   CB  -  CG  -  CD1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    HIS G  18   CE1 -  NE2 -  CD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    LYS G  34   CB  -  CG  -  CD  ANGL. DEV. =  22.6 DEGREES          
REMARK 500    ARG G  35   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG G  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG G  73   CD  -  NE  -  CZ  ANGL. DEV. =   8.7 DEGREES          
REMARK 500    CYS H   9   CA  -  CB  -  SG  ANGL. DEV. =  11.5 DEGREES          
REMARK 500    ARG H  35   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.8 DEGREES          
REMARK 500    ARG H  35   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.9 DEGREES          
REMARK 500    SER H  60   O   -  C   -  N   ANGL. DEV. = -10.3 DEGREES          
REMARK 500    LYS H  62   CD  -  CE  -  NZ  ANGL. DEV. =  22.3 DEGREES          
REMARK 500    ARG H  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    TYR H  76   CG  -  CD2 -  CE2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    TYR H  76   CZ  -  CE2 -  CD2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      51 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    GLU E  83      -71.13    -79.67                                   
REMARK 500    ARG G  35       40.52   -140.15                                   
REMARK 500    GLU G  83      -70.91    -80.62                                   
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 H1154        DISTANCE =  9.86 ANGSTROMS                       
REMARK 525    HOH H1361        DISTANCE = 10.57 ANGSTROMS                       
REMARK 525    HOH G1456        DISTANCE =  9.32 ANGSTROMS                       
REMARK 525    HOH G1464        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH E 210        DISTANCE =  5.57 ANGSTROMS                       
REMARK 525    HOH H1590        DISTANCE =  5.42 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 LIGAND BMS-0012 IS A PENTAVALENT LIGAND                              
REMARK 600 CONSISTING OF A PENTACYCLEN CORE TO WHICH                            
REMARK 600 ARE LINKED FIVE LONG ARMS, EACH CONTAINING                           
REMARK 600 TWO 'LINKER' MOITIES AND TERMINATING IN A                            
REMARK 600 'FINGER' DERIVED FROM METANITROPHENYLGALACTOSIDE.                    
REMARK 600 FOR REFINEMENT THE LIGAND WAS BROKEN INTO PIECES:                    
REMARK 600 FNG (FOR 'FINGER')  IS DERIVED FROM                                  
REMARK 600 METANITROPHENYL-ALPHA-D-GALACTOPYRANOSIDE.                           
REMARK 600 LNQ (FOR 'LINKER') IS A LINKER GROUP PRESENT IN                      
REMARK 600 TWO COPIES PER ARM, ONLY ONE OF WHICH IS INCLUDED                    
REMARK 600 IN THE MODEL.  THERE IS AN ADDITIONAL PENTANE-2-ONE                  
REMARK 600 WHICH LINKS THE LNQ TO THE CORE.                                     
REMARK 600 COR (FOR 'CORE', 1,4,7,10,13PENTAAZA-CYCLOPENTADECANE)               
REMARK 600 IS NOT PRESENT IN THIS PDB FILE BECAUSE IT WAS NOT                   
REMARK 600 SUFFICIENTLY WELL ORDERED TO BE INCLUDED IN THE                      
REMARK 600 STRUCTURAL MODEL.                                                    
REMARK 600 THE CENTRAL CORE OF THE LIGAND IS INFERRED TO                        
REMARK 600 LIE NEAR THE CENTRAL PORE OF THE PENTAMERIC PROTEIN.                 
REMARK 600                                                                      
REMARK 600 WATER NUMBERING RETAINED FROM 3CHB EXCEPT THAT                       
REMARK 600 CANONICAL SITES (FORMERLY 7000) ARE GIVEN THE                        
REMARK 600 FOLLOWING NUMBERS:                                                   
REMARK 600                                                                      
REMARK 600 001-009 CANONICAL WATERS AT BINDING SITE OF CHAIN D                  
REMARK 600 101-109 CANONICAL WATERS AT BINDING SITE OF CHAIN E                  
REMARK 600 201-209 CANONICAL WATERS AT BINDING SITE OF CHAIN F                  
REMARK 600 301-309 CANONICAL WATERS AT BINDING SITE OF CHAIN G                  
REMARK 600 401-409 CANONICAL WATERS AT BINDING SITE OF CHAIN H                  
REMARK 600                                                                      
REMARK 600 ALL OTHER WATERS (FORMERLY 9000) GIVEN RESIDUE                       
REMARK 600 NUMBERS 1001-1733.                                                   
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C SSEQI                                                      
REMARK 615     LNQ D  105                                                       
REMARK 615     LNQ E  105                                                       
REMARK 615     LNQ F  105                                                       
REMARK 615     LNQ G  105                                                       
REMARK 615     LNQ H  105                                                       
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED                                
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED                                
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNG D 104                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LNQ D 105                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNG E 104                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LNQ E 105                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNG F 104                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LNQ F 105                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNG G 104                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LNQ G 105                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNG H 104                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LNQ H 105                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3CHB   RELATED DB: PDB                                   
REMARK 900 ISOMORPHOUS COMPLEX OF CTB WITH NATIVE RECEPTOR SACCHARIDE           
REMARK 900 RELATED ID: 1EEI   RELATED DB: PDB                                   
REMARK 900 IEE1 IS CTB COMPLEXED WITH MNPG, FROM WHICH FNG IS DERIVED           
DBREF  1LLR D    1   103  GB     48890    X58785          22    124             
DBREF  1LLR E    1   103  GB     48890    X58785          22    124             
DBREF  1LLR F    1   103  GB     48890    X58785          22    124             
DBREF  1LLR G    1   103  GB     48890    X58785          22    124             
DBREF  1LLR H    1   103  GB     48890    X58785          22    124             
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              
HET    FNG  D 104      24                                                       
HET    LNQ  D 105      21                                                       
HET    FNG  E 104      24                                                       
HET    LNQ  E 105      21                                                       
HET    FNG  F 104      24                                                       
HET    LNQ  F 105      21                                                       
HET    FNG  G 104      24                                                       
HET    LNQ  G 105      21                                                       
HET    FNG  H 104      24                                                       
HET    LNQ  H 105      21                                                       
HETNAM     FNG 5-AMINOCARBONYL-3-NITROPHENYL-ALPHA-D-GALACTOPYRANOSE            
HETNAM     LNQ 3-AMINO-4-{3-[2-(2-PROPOXY-ETHOXY)-ETHOXY]-                      
HETNAM   2 LNQ  PROPYLAMINO}-CYCLOBUT-3-ENE-1,2-DIONE                           
FORMUL   6  FNG    5(C13 H16 N2 O9)                                             
FORMUL   6  LNQ    5(C14 H24 N2 O5)                                             
FORMUL  11  HOH   *570(H2 O)                                                    
HELIX    1   1 ASN D    4  ALA D   10  1                                   7    
HELIX    2   2 ILE D   58  GLU D   79  1                                  22    
HELIX    3   3 ASN E    4  ALA E   10  1                                   7    
HELIX    4   4 SER E   60  GLU E   79  1                                  20    
HELIX    5   5 ASN F    4  GLU F   11  1                                   8    
HELIX    6   6 SER F   60  GLU F   79  1                                  20    
HELIX    7   7 ASN G    4  ALA G   10  1                                   7    
HELIX    8   8 SER G   60  GLU G   79  1                                  20    
HELIX    9   9 ASN H    4  GLU H   11  1                                   8    
HELIX   10  10 SER H   60  GLU H   79  1                                  20    
SHEET    1   A39 THR D  15  ASP D  22  0                                        
SHEET    2   A39 VAL D  82  TRP D  88 -1  N  VAL D  82   O  ASP D  22           
SHEET    3   A39 HIS D  94  ALA D 102 -1  O  ALA D  95   N  TRP D  88           
SHEET    4   A39 THR D  47  VAL D  50  1  O  THR D  47   N  HIS D  94           
SHEET    5   A39 MET D  37  THR D  41 -1  O  ALA D  38   N  VAL D  50           
SHEET    6   A39 SER D  26  SER D  30 -1  O  SER D  26   N  THR D  41           
SHEET    7   A39 HIS H  94  ALA H 102 -1  N  ILE H  99   O  GLU D  29           
SHEET    8   A39 VAL H  82  TRP H  88 -1  N  GLU H  83   O  SER H 100           
SHEET    9   A39 THR H  15  ASP H  22 -1  O  GLN H  16   N  VAL H  87           
SHEET   10   A39 VAL H  82  TRP H  88 -1  N  VAL H  82   O  ASP H  22           
SHEET   11   A39 HIS H  94  ALA H 102 -1  O  ALA H  95   N  TRP H  88           
SHEET   12   A39 THR H  47  VAL H  50  1  O  THR H  47   N  HIS H  94           
SHEET   13   A39 MET H  37  THR H  41 -1  O  ALA H  38   N  VAL H  50           
SHEET   14   A39 SER H  26  SER H  30 -1  O  SER H  26   N  THR H  41           
SHEET   15   A39 HIS G  94  ALA G 102 -1  N  ILE G  99   O  GLU H  29           
SHEET   16   A39 VAL G  82  TRP G  88 -1  N  GLU G  83   O  SER G 100           
SHEET   17   A39 THR G  15  ASP G  22 -1  O  GLN G  16   N  VAL G  87           
SHEET   18   A39 VAL G  82  TRP G  88 -1  N  VAL G  82   O  ASP G  22           
SHEET   19   A39 HIS G  94  ALA G 102 -1  O  ALA G  95   N  TRP G  88           
SHEET   20   A39 THR G  47  VAL G  50  1  O  THR G  47   N  HIS G  94           
SHEET   21   A39 MET G  37  THR G  41 -1  O  ALA G  38   N  VAL G  50           
SHEET   22   A39 SER G  26  SER G  30 -1  N  SER G  26   O  THR G  41           
SHEET   23   A39 HIS F  94  ALA F 102 -1  O  ILE F  99   N  GLU G  29           
SHEET   24   A39 VAL F  82  TRP F  88 -1  N  GLU F  83   O  SER F 100           
SHEET   25   A39 THR F  15  ASP F  22 -1  O  GLN F  16   N  VAL F  87           
SHEET   26   A39 VAL F  82  TRP F  88 -1  N  VAL F  82   O  ASP F  22           
SHEET   27   A39 HIS F  94  ALA F 102 -1  O  ALA F  95   N  TRP F  88           
SHEET   28   A39 THR F  47  VAL F  50  1  O  THR F  47   N  HIS F  94           
SHEET   29   A39 MET F  37  THR F  41 -1  O  ALA F  38   N  VAL F  50           
SHEET   30   A39 SER F  26  SER F  30 -1  O  SER F  26   N  THR F  41           
SHEET   31   A39 HIS E  94  ALA E 102 -1  N  ILE E  99   O  GLU F  29           
SHEET   32   A39 VAL E  82  TRP E  88 -1  N  GLU E  83   O  SER E 100           
SHEET   33   A39 THR E  15  ASP E  22 -1  O  GLN E  16   N  VAL E  87           
SHEET   34   A39 VAL E  82  TRP E  88 -1  N  VAL E  82   O  ASP E  22           
SHEET   35   A39 HIS E  94  ALA E 102 -1  O  ALA E  95   N  TRP E  88           
SHEET   36   A39 THR E  47  VAL E  50  1  O  THR E  47   N  HIS E  94           
SHEET   37   A39 ALA E  38  THR E  41 -1  O  ALA E  38   N  VAL E  50           
SHEET   38   A39 SER E  26  SER E  30 -1  O  SER E  26   N  THR E  41           
SHEET   39   A39 HIS D  94  ALA D 102  1  O  ILE D  99   N  GLU E  29           
SSBOND   1 CYS D    9    CYS D   86                          1555   1555  2.10  
SSBOND   2 CYS E    9    CYS E   86                          1555   1555  2.02  
SSBOND   3 CYS F    9    CYS F   86                          1555   1555  2.08  
SSBOND   4 CYS G    9    CYS G   86                          1555   1555  2.05  
SSBOND   5 CYS H    9    CYS H   86                          1555   1555  2.03  
LINK         N15 FNG D 104                 C1  LNQ D 105     1555   1555  1.46  
LINK         N15 FNG E 104                 C1  LNQ E 105     1555   1555  1.49  
LINK         N15 FNG F 104                 C1  LNQ F 105     1555   1555  1.49  
LINK         N15 FNG G 104                 C1  LNQ G 105     1555   1555  1.46  
LINK         N15 FNG H 104                 C1  LNQ H 105     1555   1555  1.52  
CISPEP   1 THR D   92    PRO D   93          0       -10.02                     
CISPEP   2 THR E   92    PRO E   93          0       -17.01                     
CISPEP   3 THR F   92    PRO F   93          0       -11.93                     
CISPEP   4 THR G   92    PRO G   93          0        -9.68                     
CISPEP   5 THR H   92    PRO H   93          0       -14.76                     
SITE     1 AC1 12 TYR D  12  GLU D  51  GLN D  56  HIS D  57                    
SITE     2 AC1 12 GLN D  61  TRP D  88  ASN D  90  LYS D  91                    
SITE     3 AC1 12 LNQ D 105  HOH D 106  HOH D 110  GLY E  33                    
SITE     1 AC2  6 GLU D  11  TYR D  12  HIS D  13  FNG D 104                    
SITE     2 AC2  6 HOH D 180  HOH D 218                                          
SITE     1 AC3 13 TYR E  12  GLU E  51  GLN E  56  HIS E  57                    
SITE     2 AC3 13 GLN E  61  TRP E  88  ASN E  90  LYS E  91                    
SITE     3 AC3 13 LNQ E 105  HOH E 106  HOH E 109  HOH E 111                    
SITE     4 AC3 13 GLY F  33                                                     
SITE     1 AC4  5 GLU E  11  TYR E  12  FNG E 104  HOH E 212                    
SITE     2 AC4  5 LYS F  34                                                     
SITE     1 AC5 13 TYR F  12  GLU F  51  GLN F  56  HIS F  57                    
SITE     2 AC5 13 GLN F  61  TRP F  88  ASN F  90  LYS F  91                    
SITE     3 AC5 13 LNQ F 105  HOH F 201  HOH F 205  HOH F 207                    
SITE     4 AC5 13 GLY G  33                                                     
SITE     1 AC6  4 GLU F  11  TYR F  12  FNG F 104  HOH F1730                    
SITE     1 AC7 13 TYR G  12  GLU G  51  GLN G  56  HIS G  57                    
SITE     2 AC7 13 GLN G  61  TRP G  88  ASN G  90  LYS G  91                    
SITE     3 AC7 13 LNQ G 105  HOH G 301  HOH G 305  HOH G 307                    
SITE     4 AC7 13 GLY H  33                                                     
SITE     1 AC8  5 GLU G  11  TYR G  12  HIS G  13  FNG G 104                    
SITE     2 AC8  5 HOH G1731                                                     
SITE     1 AC9 13 GLY D  33  TYR H  12  GLU H  51  GLN H  56                    
SITE     2 AC9 13 HIS H  57  GLN H  61  TRP H  88  ASN H  90                    
SITE     3 AC9 13 LYS H  91  LNQ H 105  HOH H 401  HOH H 405                    
SITE     4 AC9 13 HOH H 407                                                     
SITE     1 BC1  4 GLU H  11  TYR H  12  FNG H 104  HOH H1732                    
CRYST1  102.391   65.964   78.146  90.00 105.97  90.00 C 1 2 1      20          
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      0.009766  0.000000  0.002795        0.00000                         
SCALE2      0.000000  0.015160  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013310        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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