GenomeNet

Database: PDB
Entry: 3CHB
LinkDB: 3CHB
Original site: 3CHB 
HEADER    TOXIN                                   24-MAR-98   3CHB              
TITLE     CHOLERA TOXIN B-PENTAMER COMPLEXED WITH GM1 PENTASACCHARIDE           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA TOXIN;                                             
COMPND   3 CHAIN: D, E, F, G, H;                                                
COMPND   4 FRAGMENT: B-PENTAMER;                                                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 OTHER_DETAILS: RECEPTOR BINDING SITE ON EACH MONOMER                 
COMPND   8 OCCUPIED BY GM1 PENTASACCHARIDE                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   3 ORGANISM_TAXID: 666;                                                 
SOURCE   4 STRAIN: OGAWA 41 (CLASSICAL BIOTYPE);                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TOXIN, TOXIN/RECEPTOR COMPLEX, PENTASACCHARIDE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.A.MERRITT,W.G.J.HOL                                                 
REVDAT   3   28-JUL-09 3CHB    1       HET    HETATM                            
REVDAT   2   24-FEB-09 3CHB    1       VERSN                                    
REVDAT   1   12-AUG-98 3CHB    0                                                
JRNL        AUTH   E.A.MERRITT,P.KUHN,S.SARFATY,J.L.ERBE,R.K.HOLMES,            
JRNL        AUTH 2 W.G.HOL                                                      
JRNL        TITL   THE 1.25 A RESOLUTION REFINEMENT OF THE CHOLERA              
JRNL        TITL 2 TOXIN B-PENTAMER: EVIDENCE OF PEPTIDE BACKBONE               
JRNL        TITL 3 STRAIN AT THE RECEPTOR-BINDING SITE.                         
JRNL        REF    J.MOL.BIOL.                   V. 282  1043 1998              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   9753553                                                      
JRNL        DOI    10.1006/JMBI.1998.2076                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.A.MERRITT,S.SARFATY,M.G.JOBLING,T.CHANG,                   
REMARK   1  AUTH 2 R.K.HOLMES,T.R.HIRST,W.G.HOL                                 
REMARK   1  TITL   STRUCTURAL STUDIES OF RECEPTOR BINDING BY CHOLERA            
REMARK   1  TITL 2 TOXIN MUTANTS                                                
REMARK   1  REF    PROTEIN SCI.                  V.   6  1516 1997              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   E.A.MERRITT,S.SARFATY,F.VAN DEN AKKER,C.L'HOIR,              
REMARK   1  AUTH 2 J.A.MARTIAL,W.G.HOL                                          
REMARK   1  TITL   CRYSTAL STRUCTURE OF CHOLERA TOXIN B-PENTAMER BOUND          
REMARK   1  TITL 2 TO RECEPTOR GM1 PENTASACCHARIDE                              
REMARK   1  REF    PROTEIN SCI.                  V.   3   166 1994              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELX-96                                             
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.0                           
REMARK   3   CROSS-VALIDATION METHOD           : R-FREE                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.133                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.133                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.180                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 6491                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 123337                 
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.122                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.122                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.166                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 5458                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 104274                 
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    : 347                                           
REMARK   3   SOLVENT ATOMS      : 758                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL                    
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 12                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 46849                   
REMARK   3   NUMBER OF RESTRAINTS                     : 21203                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.013                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.031                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.016                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.423                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.065                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.073                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.070                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.004                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.037                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.046                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: BABINET                                               
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : SHELX-96                            
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3CHB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
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        : FEB-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 125                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
REMARK 200  MONOCHROMATOR                  : GE(111)                            
REMARK 200  OPTICS                         : BENT CRYSTAL + VERTICAL MIRROR     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 126728                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.03100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 2CHB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 31.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP, PH 7.0, VAPOR              
REMARK 280  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       51.06200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.08800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       51.06200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.08800            
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: 21490 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 19.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET D     0                                                      
REMARK 465     MET E     0                                                      
REMARK 465     MET F     0                                                      
REMARK 465     MET G     0                                                      
REMARK 465     MET H     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG D  35   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    PRO D  53   O   -  C   -  N   ANGL. DEV. = -11.4 DEGREES          
REMARK 500    GLY D  54   C   -  N   -  CA  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    HIS D  57   CG  -  ND1 -  CE1 ANGL. DEV. =  12.1 DEGREES          
REMARK 500    HIS D  57   ND1 -  CE1 -  NE2 ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    ARG D  67   NE  -  CZ  -  NH1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG D  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ARG D  73   NE  -  CZ  -  NH2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG D  94   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG D  94   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASN D 103   CB  -  CG  -  ND2 ANGL. DEV. =  19.2 DEGREES          
REMARK 500    ARG E  35   NE  -  CZ  -  NH1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG E  35   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    PRO E  53   O   -  C   -  N   ANGL. DEV. = -14.6 DEGREES          
REMARK 500    GLY E  54   C   -  N   -  CA  ANGL. DEV. =  18.0 DEGREES          
REMARK 500    HIS E  57   CB  -  CG  -  CD2 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    HIS E  57   CG  -  ND1 -  CE1 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ARG E  67   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG E  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    ARG E  73   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    ARG E  73   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG E  94   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    TYR F  27   CB  -  CG  -  CD2 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    HIS F  57   CG  -  ND1 -  CE1 ANGL. DEV. =   8.3 DEGREES          
REMARK 500    ARG F  67   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG F  73   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG F  73   NE  -  CZ  -  NH2 ANGL. DEV. =   8.9 DEGREES          
REMARK 500    ARG F  94   CD  -  NE  -  CZ  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    ARG F  94   NE  -  CZ  -  NH2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP G   7   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    PRO G  53   O   -  C   -  N   ANGL. DEV. = -12.8 DEGREES          
REMARK 500    GLY G  54   C   -  N   -  CA  ANGL. DEV. =  15.9 DEGREES          
REMARK 500    HIS G  57   CG  -  ND1 -  CE1 ANGL. DEV. =  11.0 DEGREES          
REMARK 500    HIS G  57   ND1 -  CE1 -  NE2 ANGL. DEV. =  -8.1 DEGREES          
REMARK 500    ARG G  67   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG G  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    ARG G  73   NE  -  CZ  -  NH2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG G  94   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    PHE H  25   CB  -  CG  -  CD1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    HIS H  57   CG  -  ND1 -  CE1 ANGL. DEV. =  11.3 DEGREES          
REMARK 500    HIS H  57   ND1 -  CE1 -  NE2 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    ARG H  67   NE  -  CZ  -  NH1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG H  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG H  73   CD  -  NE  -  CZ  ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ARG H  73   NE  -  CZ  -  NH2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG H  94   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS D  34       -0.27     74.56                                   
REMARK 500    GLU F  83      -70.63    -80.64                                   
REMARK 500    LYS H  34       -1.36     73.71                                   
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 G9456        DISTANCE =  9.36 ANGSTROMS                       
REMARK 525    HOH G9464        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH G9628        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH G9813        DISTANCE =  7.45 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     GLC D  107                                                       
REMARK 610     GLC F  107                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL D 104                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGA D 105                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL D 106                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC D 107                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA D 108                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL E 104                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGA E 105                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL E 106                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC E 107                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA E 108                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL F 104                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGA F 105                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL F 106                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC F 107                 
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA F 108                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL G 104                 
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGA G 105                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL G 106                 
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC G 107                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA G 108                 
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES G 6001                
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES G 6002                
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL H 104                 
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGA H 105                 
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL H 106                 
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC H 107                 
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA H 108                 
DBREF  3CHB D    0   103  UNP    P01556   CHTB_VIBCH       1    124             
DBREF  3CHB E    0   103  UNP    P01556   CHTB_VIBCH       1    124             
DBREF  3CHB F    0   103  UNP    P01556   CHTB_VIBCH       1    124             
DBREF  3CHB G    0   103  UNP    P01556   CHTB_VIBCH       1    124             
DBREF  3CHB H    0   103  UNP    P01556   CHTB_VIBCH       1    124             
SEQADV 3CHB     D       UNP  P01556    ILE     2 DELETION                       
SEQADV 3CHB     D       UNP  P01556    LYS     3 DELETION                       
SEQADV 3CHB     D       UNP  P01556    LEU     4 DELETION                       
SEQADV 3CHB     D       UNP  P01556    LYS     5 DELETION                       
SEQADV 3CHB     D       UNP  P01556    PHE     6 DELETION                       
SEQADV 3CHB     D       UNP  P01556    GLY     7 DELETION                       
SEQADV 3CHB     D       UNP  P01556    VAL     8 DELETION                       
SEQADV 3CHB     D       UNP  P01556    PHE     9 DELETION                       
SEQADV 3CHB     D       UNP  P01556    PHE    10 DELETION                       
SEQADV 3CHB     D       UNP  P01556    THR    11 DELETION                       
SEQADV 3CHB     D       UNP  P01556    VAL    12 DELETION                       
SEQADV 3CHB     D       UNP  P01556    LEU    13 DELETION                       
SEQADV 3CHB     D       UNP  P01556    LEU    14 DELETION                       
SEQADV 3CHB     D       UNP  P01556    SER    15 DELETION                       
SEQADV 3CHB     D       UNP  P01556    SER    16 DELETION                       
SEQADV 3CHB     D       UNP  P01556    ALA    17 DELETION                       
SEQADV 3CHB     D       UNP  P01556    TYR    18 DELETION                       
SEQADV 3CHB     D       UNP  P01556    ALA    19 DELETION                       
SEQADV 3CHB     D       UNP  P01556    HIS    20 DELETION                       
SEQADV 3CHB     D       UNP  P01556    GLY    21 DELETION                       
SEQADV 3CHB HIS D   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 3CHB THR D   47  UNP  P01556    ILE    68 CONFLICT                       
SEQADV 3CHB ARG D   94  UNP  P01556    HIS   115 CLONING ARTIFACT               
SEQADV 3CHB     E       UNP  P01556    ILE     2 DELETION                       
SEQADV 3CHB     E       UNP  P01556    LYS     3 DELETION                       
SEQADV 3CHB     E       UNP  P01556    LEU     4 DELETION                       
SEQADV 3CHB     E       UNP  P01556    LYS     5 DELETION                       
SEQADV 3CHB     E       UNP  P01556    PHE     6 DELETION                       
SEQADV 3CHB     E       UNP  P01556    GLY     7 DELETION                       
SEQADV 3CHB     E       UNP  P01556    VAL     8 DELETION                       
SEQADV 3CHB     E       UNP  P01556    PHE     9 DELETION                       
SEQADV 3CHB     E       UNP  P01556    PHE    10 DELETION                       
SEQADV 3CHB     E       UNP  P01556    THR    11 DELETION                       
SEQADV 3CHB     E       UNP  P01556    VAL    12 DELETION                       
SEQADV 3CHB     E       UNP  P01556    LEU    13 DELETION                       
SEQADV 3CHB     E       UNP  P01556    LEU    14 DELETION                       
SEQADV 3CHB     E       UNP  P01556    SER    15 DELETION                       
SEQADV 3CHB     E       UNP  P01556    SER    16 DELETION                       
SEQADV 3CHB     E       UNP  P01556    ALA    17 DELETION                       
SEQADV 3CHB     E       UNP  P01556    TYR    18 DELETION                       
SEQADV 3CHB     E       UNP  P01556    ALA    19 DELETION                       
SEQADV 3CHB     E       UNP  P01556    HIS    20 DELETION                       
SEQADV 3CHB     E       UNP  P01556    GLY    21 DELETION                       
SEQADV 3CHB HIS E   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 3CHB THR E   47  UNP  P01556    ILE    68 CONFLICT                       
SEQADV 3CHB ARG E   94  UNP  P01556    HIS   115 CLONING ARTIFACT               
SEQADV 3CHB     F       UNP  P01556    ILE     2 DELETION                       
SEQADV 3CHB     F       UNP  P01556    LYS     3 DELETION                       
SEQADV 3CHB     F       UNP  P01556    LEU     4 DELETION                       
SEQADV 3CHB     F       UNP  P01556    LYS     5 DELETION                       
SEQADV 3CHB     F       UNP  P01556    PHE     6 DELETION                       
SEQADV 3CHB     F       UNP  P01556    GLY     7 DELETION                       
SEQADV 3CHB     F       UNP  P01556    VAL     8 DELETION                       
SEQADV 3CHB     F       UNP  P01556    PHE     9 DELETION                       
SEQADV 3CHB     F       UNP  P01556    PHE    10 DELETION                       
SEQADV 3CHB     F       UNP  P01556    THR    11 DELETION                       
SEQADV 3CHB     F       UNP  P01556    VAL    12 DELETION                       
SEQADV 3CHB     F       UNP  P01556    LEU    13 DELETION                       
SEQADV 3CHB     F       UNP  P01556    LEU    14 DELETION                       
SEQADV 3CHB     F       UNP  P01556    SER    15 DELETION                       
SEQADV 3CHB     F       UNP  P01556    SER    16 DELETION                       
SEQADV 3CHB     F       UNP  P01556    ALA    17 DELETION                       
SEQADV 3CHB     F       UNP  P01556    TYR    18 DELETION                       
SEQADV 3CHB     F       UNP  P01556    ALA    19 DELETION                       
SEQADV 3CHB     F       UNP  P01556    HIS    20 DELETION                       
SEQADV 3CHB     F       UNP  P01556    GLY    21 DELETION                       
SEQADV 3CHB HIS F   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 3CHB THR F   47  UNP  P01556    ILE    68 CONFLICT                       
SEQADV 3CHB ARG F   94  UNP  P01556    HIS   115 CLONING ARTIFACT               
SEQADV 3CHB     G       UNP  P01556    ILE     2 DELETION                       
SEQADV 3CHB     G       UNP  P01556    LYS     3 DELETION                       
SEQADV 3CHB     G       UNP  P01556    LEU     4 DELETION                       
SEQADV 3CHB     G       UNP  P01556    LYS     5 DELETION                       
SEQADV 3CHB     G       UNP  P01556    PHE     6 DELETION                       
SEQADV 3CHB     G       UNP  P01556    GLY     7 DELETION                       
SEQADV 3CHB     G       UNP  P01556    VAL     8 DELETION                       
SEQADV 3CHB     G       UNP  P01556    PHE     9 DELETION                       
SEQADV 3CHB     G       UNP  P01556    PHE    10 DELETION                       
SEQADV 3CHB     G       UNP  P01556    THR    11 DELETION                       
SEQADV 3CHB     G       UNP  P01556    VAL    12 DELETION                       
SEQADV 3CHB     G       UNP  P01556    LEU    13 DELETION                       
SEQADV 3CHB     G       UNP  P01556    LEU    14 DELETION                       
SEQADV 3CHB     G       UNP  P01556    SER    15 DELETION                       
SEQADV 3CHB     G       UNP  P01556    SER    16 DELETION                       
SEQADV 3CHB     G       UNP  P01556    ALA    17 DELETION                       
SEQADV 3CHB     G       UNP  P01556    TYR    18 DELETION                       
SEQADV 3CHB     G       UNP  P01556    ALA    19 DELETION                       
SEQADV 3CHB     G       UNP  P01556    HIS    20 DELETION                       
SEQADV 3CHB     G       UNP  P01556    GLY    21 DELETION                       
SEQADV 3CHB HIS G   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 3CHB THR G   47  UNP  P01556    ILE    68 CONFLICT                       
SEQADV 3CHB ARG G   94  UNP  P01556    HIS   115 CLONING ARTIFACT               
SEQADV 3CHB     H       UNP  P01556    ILE     2 DELETION                       
SEQADV 3CHB     H       UNP  P01556    LYS     3 DELETION                       
SEQADV 3CHB     H       UNP  P01556    LEU     4 DELETION                       
SEQADV 3CHB     H       UNP  P01556    LYS     5 DELETION                       
SEQADV 3CHB     H       UNP  P01556    PHE     6 DELETION                       
SEQADV 3CHB     H       UNP  P01556    GLY     7 DELETION                       
SEQADV 3CHB     H       UNP  P01556    VAL     8 DELETION                       
SEQADV 3CHB     H       UNP  P01556    PHE     9 DELETION                       
SEQADV 3CHB     H       UNP  P01556    PHE    10 DELETION                       
SEQADV 3CHB     H       UNP  P01556    THR    11 DELETION                       
SEQADV 3CHB     H       UNP  P01556    VAL    12 DELETION                       
SEQADV 3CHB     H       UNP  P01556    LEU    13 DELETION                       
SEQADV 3CHB     H       UNP  P01556    LEU    14 DELETION                       
SEQADV 3CHB     H       UNP  P01556    SER    15 DELETION                       
SEQADV 3CHB     H       UNP  P01556    SER    16 DELETION                       
SEQADV 3CHB     H       UNP  P01556    ALA    17 DELETION                       
SEQADV 3CHB     H       UNP  P01556    TYR    18 DELETION                       
SEQADV 3CHB     H       UNP  P01556    ALA    19 DELETION                       
SEQADV 3CHB     H       UNP  P01556    HIS    20 DELETION                       
SEQADV 3CHB     H       UNP  P01556    GLY    21 DELETION                       
SEQADV 3CHB HIS H   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 3CHB THR H   47  UNP  P01556    ILE    68 CONFLICT                       
SEQADV 3CHB ARG H   94  UNP  P01556    HIS   115 CLONING ARTIFACT               
SEQRES   1 D  104  MET THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR          
SEQRES   2 D  104  HIS ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE          
SEQRES   3 D  104  SER TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA          
SEQRES   4 D  104  ILE ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU          
SEQRES   5 D  104  VAL PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA          
SEQRES   6 D  104  ILE GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU          
SEQRES   7 D  104  THR GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN          
SEQRES   8 D  104  LYS THR PRO ARG ALA ILE ALA ALA ILE SER MET ALA ASN          
SEQRES   1 E  104  MET THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR          
SEQRES   2 E  104  HIS ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE          
SEQRES   3 E  104  SER TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA          
SEQRES   4 E  104  ILE ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU          
SEQRES   5 E  104  VAL PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA          
SEQRES   6 E  104  ILE GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU          
SEQRES   7 E  104  THR GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN          
SEQRES   8 E  104  LYS THR PRO ARG ALA ILE ALA ALA ILE SER MET ALA ASN          
SEQRES   1 F  104  MET THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR          
SEQRES   2 F  104  HIS ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE          
SEQRES   3 F  104  SER TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA          
SEQRES   4 F  104  ILE ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU          
SEQRES   5 F  104  VAL PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA          
SEQRES   6 F  104  ILE GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU          
SEQRES   7 F  104  THR GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN          
SEQRES   8 F  104  LYS THR PRO ARG ALA ILE ALA ALA ILE SER MET ALA ASN          
SEQRES   1 G  104  MET THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR          
SEQRES   2 G  104  HIS ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE          
SEQRES   3 G  104  SER TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA          
SEQRES   4 G  104  ILE ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU          
SEQRES   5 G  104  VAL PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA          
SEQRES   6 G  104  ILE GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU          
SEQRES   7 G  104  THR GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN          
SEQRES   8 G  104  LYS THR PRO ARG ALA ILE ALA ALA ILE SER MET ALA ASN          
SEQRES   1 H  104  MET THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR          
SEQRES   2 H  104  HIS ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE          
SEQRES   3 H  104  SER TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA          
SEQRES   4 H  104  ILE ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU          
SEQRES   5 H  104  VAL PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA          
SEQRES   6 H  104  ILE GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU          
SEQRES   7 H  104  THR GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN          
SEQRES   8 H  104  LYS THR PRO ARG ALA ILE ALA ALA ILE SER MET ALA ASN          
HET    GAL  D 104      11                                                       
HET    NGA  D 105      14                                                       
HET    GAL  D 106      11                                                       
HET    GLC  D 107       1                                                       
HET    SIA  D 108      20                                                       
HET    UNX  D 109       1                                                       
HET    GAL  E 104      11                                                       
HET    NGA  E 105      14                                                       
HET    GAL  E 106      11                                                       
HET    BGC  E 107      12                                                       
HET    SIA  E 108      20                                                       
HET    UNX  E 109       1                                                       
HET    GAL  F 104      11                                                       
HET    NGA  F 105      14                                                       
HET    GAL  F 106      11                                                       
HET    GLC  F 107       1                                                       
HET    SIA  F 108      20                                                       
HET    UNX  F 109       1                                                       
HET    GAL  G 104      11                                                       
HET    NGA  G 105      14                                                       
HET    GAL  G 106      11                                                       
HET    BGC  G 107      12                                                       
HET    SIA  G 108      20                                                       
HET    UNX  G 109       1                                                       
HET    MES  G6001      12                                                       
HET    MES  G6002      12                                                       
HET    GAL  H 104      11                                                       
HET    NGA  H 105      14                                                       
HET    GAL  H 106      11                                                       
HET    BGC  H 107      12                                                       
HET    SIA  H 108      20                                                       
HET    UNX  H 109       1                                                       
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETNAM     NGA N-ACETYL-D-GALACTOSAMINE                                         
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     SIA O-SIALIC ACID                                                    
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
FORMUL   6  GAL    10(C6 H12 O6)                                                
FORMUL   6  NGA    5(C8 H15 N O6)                                               
FORMUL   6  GLC    2(C6 H12 O6)                                                 
FORMUL   6  SIA    5(C11 H19 N O9)                                              
FORMUL   7  UNX    5(X)                                                         
FORMUL   8  BGC    3(C6 H12 O6)                                                 
FORMUL  14  MES    2(C6 H13 N O4 S)                                             
FORMUL  18  HOH   *758(H2 O)                                                    
HELIX    1 DA1 ILE D    5  CYS D    9  1                                   5    
HELIX    2 DA2 GLN D   61  THR D   78  1                                  18    
HELIX    3 EA1 ILE E    5  CYS E    9  1                                   5    
HELIX    4 EA2 GLN E   61  THR E   78  1                                  18    
HELIX    5 FA1 ILE F    5  CYS F    9  1                                   5    
HELIX    6 FA2 GLN F   61  THR F   78  1                                  18    
HELIX    7 GA1 ILE G    5  CYS G    9  1                                   5    
HELIX    8 GA2 GLN G   61  THR G   78  1                                  18    
HELIX    9 HA1 ILE H    5  CYS H    9  1                                   5    
HELIX   10 HA2 GLN H   61  THR H   78  1                                  18    
SHEET    1 BB1 6 THR D  15  ASP D  22  0                                        
SHEET    2 BB1 6 VAL D  82  TRP D  88 -1                                        
SHEET    3 BB1 6 ARG D  94  ALA D 102 -1                                        
SHEET    4 BB1 6 SER E  26  SER E  30 -1                                        
SHEET    5 BB1 6 MET E  37  THR E  41 -1                                        
SHEET    6 BB1 6 THR E  47  VAL E  50 -1                                        
SHEET    1 BB2 6 THR E  15  ASP E  22  0                                        
SHEET    2 BB2 6 VAL E  82  TRP E  88 -1                                        
SHEET    3 BB2 6 ARG E  94  ALA E 102 -1                                        
SHEET    4 BB2 6 SER F  26  SER F  30 -1                                        
SHEET    5 BB2 6 MET F  37  THR F  41 -1                                        
SHEET    6 BB2 6 THR F  47  VAL F  50 -1                                        
SHEET    1 BB3 6 THR F  15  ASP F  22  0                                        
SHEET    2 BB3 6 VAL F  82  TRP F  88 -1                                        
SHEET    3 BB3 6 ARG F  94  ALA F 102 -1                                        
SHEET    4 BB3 6 SER G  26  SER G  30 -1                                        
SHEET    5 BB3 6 MET G  37  THR G  41 -1                                        
SHEET    6 BB3 6 THR G  47  VAL G  50 -1                                        
SHEET    1 BB4 6 THR G  15  ASP G  22  0                                        
SHEET    2 BB4 6 VAL G  82  TRP G  88 -1                                        
SHEET    3 BB4 6 ARG G  94  ALA G 102 -1                                        
SHEET    4 BB4 6 SER H  26  SER H  30 -1                                        
SHEET    5 BB4 6 MET H  37  THR H  41 -1                                        
SHEET    6 BB4 6 THR H  47  VAL H  50 -1                                        
SHEET    1 BB5 6 THR H  15  ASP H  22  0                                        
SHEET    2 BB5 6 VAL H  82  TRP H  88 -1                                        
SHEET    3 BB5 6 ARG H  94  ALA H 102 -1                                        
SHEET    4 BB5 6 SER D  26  SER D  30 -1                                        
SHEET    5 BB5 6 MET D  37  THR D  41 -1                                        
SHEET    6 BB5 6 THR D  47  VAL D  50 -1                                        
SSBOND   1 CYS D    9    CYS D   86                          1555   1555  2.08  
SSBOND   2 CYS E    9    CYS E   86                          1555   1555  2.08  
SSBOND   3 CYS F    9    CYS F   86                          1555   1555  2.06  
SSBOND   4 CYS G    9    CYS G   86                          1555   1555  2.08  
SSBOND   5 CYS H    9    CYS H   86                          1555   1555  2.07  
LINK         C1  GAL D 104                 O3  NGA D 105     1555   1555  1.42  
LINK         C1  NGA D 105                 O4  GAL D 106     1555   1555  1.42  
LINK         C1  GAL D 106                 O4  GLC D 107     1555   1555  1.44  
LINK         O3  GAL D 106                 C2  SIA D 108     1555   1555  1.41  
LINK         C1  GAL E 104                 O3  NGA E 105     1555   1555  1.42  
LINK         C1  NGA E 105                 O4  GAL E 106     1555   1555  1.44  
LINK         O3  GAL E 106                 C2  SIA E 108     1555   1555  1.42  
LINK         C1  GAL F 104                 O3  NGA F 105     1555   1555  1.43  
LINK         C1  NGA F 105                 O4  GAL F 106     1555   1555  1.43  
LINK         C1  GAL F 106                 O4  GLC F 107     1555   1555  1.44  
LINK         O3  GAL F 106                 C2  SIA F 108     1555   1555  1.42  
LINK         C1  GAL G 104                 O3  NGA G 105     1555   1555  1.40  
LINK         C1  NGA G 105                 O4  GAL G 106     1555   1555  1.42  
LINK         O3  GAL G 106                 C2  SIA G 108     1555   1555  1.43  
LINK         C1  GAL H 104                 O3  NGA H 105     1555   1555  1.41  
LINK         C1  NGA H 105                 O4  GAL H 106     1555   1555  1.42  
LINK         O3  GAL H 106                 C2  SIA H 108     1555   1555  1.41  
LINK         C1  GAL E 106                 O4  BGC E 107     1555   1555  1.42  
LINK         C1  GAL G 106                 O4  BGC G 107     1555   1555  1.43  
LINK         C1  GAL H 106                 O4  BGC H 107     1555   1555  1.43  
CISPEP   1 THR D   92    PRO D   93          0        -9.08                     
CISPEP   2 THR E   92    PRO E   93          0        -7.07                     
CISPEP   3 THR F   92    PRO F   93          0        -4.86                     
CISPEP   4 THR G   92    PRO G   93          0        -8.67                     
CISPEP   5 THR H   92    PRO H   93          0       -11.77                     
SITE     1 AC1 10 GLU D  51  GLN D  56  HIS D  57  GLN D  61                    
SITE     2 AC1 10 TRP D  88  ASN D  90  LYS D  91  NGA D 105                    
SITE     3 AC1 10 HOH D7002  HOH D7007                                          
SITE     1 AC2 11 GLN D  56  ILE D  58  GAL D 104  GAL D 106                    
SITE     2 AC2 11 SIA D 108  HOH D7001  HOH D7005  HOH D7007                    
SITE     3 AC2 11 HOH D7008  HOH D9318  HOH H9436                               
SITE     1 AC3  8 LYS D  34  NGA D 105  GLC D 107  SIA D 108                    
SITE     2 AC3  8 ILE H  58  NGA H 105  HOH H9436  HOH H9799                    
SITE     1 AC4  4 GAL D 106  NGA H 105  GAL H 106  HOH H9799                    
SITE     1 AC5 11 GLU D  11  TYR D  12  HIS D  13  ILE D  58                    
SITE     2 AC5 11 NGA D 105  GAL D 106  HOH D7002  HOH D7003                    
SITE     3 AC5 11 HOH D7005  HOH D9617  GLY E  33                               
SITE     1 AC6 11 GLU E  51  GLN E  56  GLN E  61  TRP E  88                    
SITE     2 AC6 11 ASN E  90  LYS E  91  NGA E 105  HOH E7101                    
SITE     3 AC6 11 HOH E7102  HOH E7105  HOH E7107                               
SITE     1 AC7  9 GLN E  56  ILE E  58  GAL E 104  GAL E 106                    
SITE     2 AC7  9 SIA E 108  HOH E7108  HOH E9787  HOH E9815                    
SITE     3 AC7  9 HOH F9661                                                     
SITE     1 AC8  8 NGA E 105  BGC E 107  SIA E 108  HOH E9334                    
SITE     2 AC8  8 HOH E9451  HOH E9618  HOH F9232  HOH G9410                    
SITE     1 AC9 11 ASP D   7  HOH D9402  GAL E 106  HOH E9351                    
SITE     2 AC9 11 HOH E9451  HOH F9777  GLY G  54  SER G  55                    
SITE     3 AC9 11 GLN G  56  HOH G9295  HOH G9410                               
SITE     1 BC1 13 GLU E  11  TYR E  12  HIS E  13  ILE E  58                    
SITE     2 BC1 13 NGA E 105  GAL E 106  HOH E7102  HOH E7103                    
SITE     3 BC1 13 HOH E7105  HOH E9437  HOH E9729  HOH E9815                    
SITE     4 BC1 13 GLY F  33                                                     
SITE     1 BC2 12 GLU F  51  GLN F  56  HIS F  57  GLN F  61                    
SITE     2 BC2 12 TRP F  88  ASN F  90  LYS F  91  NGA F 105                    
SITE     3 BC2 12 HOH F7201  HOH F7202  HOH F7205  HOH F7207                    
SITE     1 BC3 11 ASN F  14  GLN F  56  HIS F  57  ILE F  58                    
SITE     2 BC3 11 GAL F 104  GAL F 106  SIA F 108  HOH F7201                    
SITE     3 BC3 11 HOH F7205  HOH F7207  HOH F7208                               
SITE     1 BC4  4 HIS F  13  NGA F 105  GLC F 107  SIA F 108                    
SITE     1 BC5  1 GAL F 106                                                     
SITE     1 BC6 10 GLU F  11  TYR F  12  HIS F  13  ILE F  58                    
SITE     2 BC6 10 NGA F 105  GAL F 106  HOH F7202  HOH F7203                    
SITE     3 BC6 10 HOH F7205  GLY G  33                                          
SITE     1 BC7 12 GLU G  51  GLN G  56  HIS G  57  GLN G  61                    
SITE     2 BC7 12 TRP G  88  ASN G  90  LYS G  91  NGA G 105                    
SITE     3 BC7 12 HOH G7301  HOH G7302  HOH G7305  HOH G7307                    
SITE     1 BC8 12 HIS D  18  HOH D9194  HOH D9306  GLN G  56                    
SITE     2 BC8 12 ILE G  58  GAL G 104  GAL G 106  SIA G 108                    
SITE     3 BC8 12 HOH G7301  HOH G7305  HOH G7307  HOH G7308                    
SITE     1 BC9  8 GLN D  16  HIS D  18  HOH D9251  HIS G  13                    
SITE     2 BC9  8 NGA G 105  BGC G 107  SIA G 108  HOH G9720                    
SITE     1 CC1  9 HIS D  18  ALA D  46  THR D  47  HOH D9132                    
SITE     2 CC1  9 GAL G 106  HOH G9581  HOH G9713  HOH G9733                    
SITE     3 CC1  9 HOH H9375                                                     
SITE     1 CC2 11 GLU G  11  TYR G  12  HIS G  13  ILE G  58                    
SITE     2 CC2 11 NGA G 105  GAL G 106  HOH G7302  HOH G7303                    
SITE     3 CC2 11 HOH G7305  HOH G9552  HOH G9634                               
SITE     1 CC3 12 ASN D  21  ASP D  22  LYS D  43  LYS D  81                    
SITE     2 CC3 12 HOH D9068  HOH D9397  ASN G  89  LYS G  91                    
SITE     3 CC3 12 THR G  92  ARG G  94  LYS H  43  HOH H9781                    
SITE     1 CC4 10 ASN E  21  ASP E  22  LYS E  81  LYS G  43                    
SITE     2 CC4 10 ASN H  89  ASN H  90  LYS H  91  THR H  92                    
SITE     3 CC4 10 ARG H  94  HOH H9257                                          
SITE     1 CC5 12 GLU H  51  GLN H  56  HIS H  57  GLN H  61                    
SITE     2 CC5 12 TRP H  88  ASN H  90  LYS H  91  NGA H 105                    
SITE     3 CC5 12 HOH H7401  HOH H7402  HOH H7405  HOH H7407                    
SITE     1 CC6 11 GAL D 106  GLC D 107  HIS E  18  GLN H  56                    
SITE     2 CC6 11 GAL H 104  GAL H 106  SIA H 108  HOH H7407                    
SITE     3 CC6 11 HOH H7408  HOH H9538  HOH H9799                               
SITE     1 CC7  6 GLC D 107  GLN E  16  HIS H  13  NGA H 105                    
SITE     2 CC7  6 BGC H 107  SIA H 108                                          
SITE     1 CC8 10 HIS E  18  ALA E  46  THR E  47  ARG E  94                    
SITE     2 CC8 10 HOH E9269  HIS H  13  GAL H 106  HOH H9154                    
SITE     3 CC8 10 HOH H9361  HOH H9717                                          
SITE     1 CC9 10 GLU H  11  TYR H  12  HIS H  13  ILE H  58                    
SITE     2 CC9 10 NGA H 105  GAL H 106  HOH H7402  HOH H7403                    
SITE     3 CC9 10 HOH H7405  HOH H9814                                          
CRYST1  102.124   66.176   78.221  90.00 106.33  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      0.009792  0.000000  0.002869        0.00000                         
SCALE2      0.000000  0.015111  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013322        0.00000                         
MTRIX1   1  0.446207 -0.852405 -0.272590       37.89980    1                    
MTRIX2   1  0.852840  0.312704  0.418186       21.82120    1                    
MTRIX3   1 -0.271223 -0.419073  0.866496       18.62370    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system