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Database: PDB
Entry: 2CHB
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HEADER    TOXIN                                   03-JUN-97   2CHB              
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 OTHER_DETAILS: RECEPTOR BINDING SITE ON EACH MONOMER                 
COMPND   7 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/RECEPTOR COMPLEX, PENTASACCHARIDE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.A.MERRITT,W.G.J.HOL                                                 
REVDAT   3   28-JUL-09 2CHB    1       HET    HETATM                            
REVDAT   2   24-FEB-09 2CHB    1       VERSN                                    
REVDAT   1   03-DEC-97 2CHB    0                                                
SPRSDE     03-DEC-97 2CHB      1CHB                                             
JRNL        AUTH   E.A.MERRITT,S.SARFATY,M.G.JOBLING,T.CHANG,                   
JRNL        AUTH 2 R.K.HOLMES,T.R.HIRST,W.G.HOL                                 
JRNL        TITL   STRUCTURAL STUDIES OF RECEPTOR BINDING BY CHOLERA            
JRNL        TITL 2 TOXIN MUTANTS.                                               
JRNL        REF    PROTEIN SCI.                  V.   6  1516 1997              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   9232653                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
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.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 81.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 28828                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 52.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1863                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2710                       
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4070                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 316                                     
REMARK   3   SOLVENT ATOMS            : 388                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -8.01000                                             
REMARK   3    B22 (A**2) : 2.57000                                              
REMARK   3    B33 (A**2) : 5.44000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -3.97000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.73                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.700 ; 2.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.300 ; 4.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.700 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.300 ; 4.000                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM1.CHO                                     
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH1.CHO (MODIFIED)                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2CHB 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-93                             
REMARK 200  TEMPERATURE           (KELVIN) : 287                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN                             
REMARK 200  DATA SCALING SOFTWARE          : MACRO                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35318                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: PDB ENTRY 1CHB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM MGCL2 100 MM CACODYLATE 5%        
REMARK 280  PEG 1000 PH 7.5                                                     
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       50.95000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.79000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       50.95000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.79000            
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: 21730 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 19010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 23.0 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: 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   O5   GAL H   106     O4   BGC H   107              2.16            
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    MET G  68   CG    MET G  68   SD     -0.239                       
REMARK 500    MET H  68   CG    MET H  68   SD      0.239                       
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    LEU D  31   CA  -  CB  -  CG  ANGL. DEV. =  17.0 DEGREES          
REMARK 500    VAL E  50   N   -  CA  -  C   ANGL. DEV. = -16.8 DEGREES          
REMARK 500    LEU F  31   CA  -  CB  -  CG  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    LEU G  31   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    LEU H  31   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    VAL H  50   N   -  CA  -  C   ANGL. DEV. = -16.4 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    ARG D  35       44.19   -140.20                                   
REMARK 500    GLN D  56       14.61    -66.41                                   
REMARK 500    LYS F  34       -1.02     76.23                                   
REMARK 500    GLU F  83      -70.05    -75.48                                   
REMARK 500    LYS G  34       -1.95     76.52                                   
REMARK 500    LYS H  34       -2.32     78.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 SIA D 108                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL E 104                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGA E 105                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL E 106                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC E 107                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA E 108                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL F 104                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGA F 105                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL F 106                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA F 108                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL G 104                 
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGA G 105                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL G 106                 
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC G 107                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA G 108                 
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL H 104                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGA H 105                 
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL H 106                 
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC H 107                 
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA H 108                 
DBREF  2CHB D    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  2CHB E    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  2CHB F    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  2CHB G    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  2CHB H    1   103  UNP    P01556   CHTB_VIBCH      22    124             
SEQADV 2CHB HIS D   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 2CHB THR D   47  UNP  P01556    ILE    68 CONFLICT                       
SEQADV 2CHB HIS E   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 2CHB THR E   47  UNP  P01556    ILE    68 CONFLICT                       
SEQADV 2CHB HIS F   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 2CHB THR F   47  UNP  P01556    ILE    68 CONFLICT                       
SEQADV 2CHB HIS G   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 2CHB THR G   47  UNP  P01556    ILE    68 CONFLICT                       
SEQADV 2CHB HIS H   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 2CHB THR H   47  UNP  P01556    ILE    68 CONFLICT                       
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 HIS 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 HIS 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 HIS 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 HIS 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 HIS 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    SIA  D 108      20                                                       
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    GAL  F 104      11                                                       
HET    NGA  F 105      14                                                       
HET    GAL  F 106      11                                                       
HET    SIA  F 108      20                                                       
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    GAL  H 104      11                                                       
HET    NGA  H 105      14                                                       
HET    GAL  H 106      11                                                       
HET    BGC  H 107      12                                                       
HET    SIA  H 108      20                                                       
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETNAM     NGA N-ACETYL-D-GALACTOSAMINE                                         
HETNAM     SIA O-SIALIC ACID                                                    
HETNAM     BGC BETA-D-GLUCOSE                                                   
FORMUL   6  GAL    10(C6 H12 O6)                                                
FORMUL   6  NGA    5(C8 H15 N O6)                                               
FORMUL   6  SIA    5(C11 H19 N O9)                                              
FORMUL   7  BGC    3(C6 H12 O6)                                                 
FORMUL  11  HOH   *388(H2 O)                                                    
HELIX    1 DA1 ILE D    5  CYS D    9  1                                   5    
HELIX    2 DA2 ASP D   59  THR D   78  1                                  20    
HELIX    3 EA1 ILE E    5  CYS E    9  1                                   5    
HELIX    4 EA2 LYS E   62  THR E   78  1                                  17    
HELIX    5 FA1 ILE F    5  CYS F    9  1                                   5    
HELIX    6 FA2 ASP F   59  THR F   78  1                                  20    
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 SER H   60  THR H   78  1                                  19    
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 HIS 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 HIS 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 HIS 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 HIS 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 HIS 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  2.03  
SSBOND   2 CYS E    9    CYS E   86                          1555   1555  2.04  
SSBOND   3 CYS F    9    CYS F   86                          1555   1555  2.03  
SSBOND   4 CYS G    9    CYS G   86                          1555   1555  2.04  
SSBOND   5 CYS H    9    CYS H   86                          1555   1555  2.03  
LINK         C1  GAL D 104                 O3  NGA D 105     1555   1555  1.43  
LINK         C1  NGA D 105                 O4  GAL D 106     1555   1555  1.39  
LINK         O3  GAL D 106                 C2  SIA D 108     1555   1555  1.44  
LINK         C1  GAL E 104                 O3  NGA E 105     1555   1555  1.42  
LINK         C1  NGA E 105                 O4  GAL E 106     1555   1555  1.34  
LINK         C1  GAL E 106                 O4  BGC E 107     1555   1555  1.40  
LINK         O3  GAL E 106                 C2  SIA E 108     1555   1555  1.41  
LINK         C1  GAL F 104                 O3  NGA F 105     1555   1555  1.37  
LINK         C1  NGA F 105                 O4  GAL F 106     1555   1555  1.43  
LINK         O3  GAL F 106                 C2  SIA F 108     1555   1555  1.39  
LINK         C1  GAL G 104                 O3  NGA G 105     1555   1555  1.40  
LINK         C1  NGA G 105                 O4  GAL G 106     1555   1555  1.40  
LINK         C1  GAL G 106                 O4  BGC G 107     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  1.40  
LINK         C1  NGA H 105                 O4  GAL H 106     1555   1555  1.41  
LINK         C1  GAL H 106                 O4  BGC H 107     1555   1555  1.41  
LINK         O3  GAL H 106                 C2  SIA H 108     1555   1555  1.42  
CISPEP   1 THR D   92    PRO D   93          0        -0.32                     
CISPEP   2 THR E   92    PRO E   93          0         0.16                     
CISPEP   3 THR F   92    PRO F   93          0        -0.28                     
CISPEP   4 THR G   92    PRO G   93          0         0.55                     
CISPEP   5 THR H   92    PRO H   93          0        -1.36                     
SITE     1 AC1  8 GLU D  51  GLN D  56  GLN D  61  TRP D  88                    
SITE     2 AC1  8 ASN D  90  LYS D  91  NGA D 105  HOH D 166                    
SITE     1 AC2  5 HIS D  13  ASN D  14  GAL D 104  GAL D 106                    
SITE     2 AC2  5 SIA D 108                                                     
SITE     1 AC3  3 NGA D 105  SIA D 108  HOH H 182                               
SITE     1 AC4  9 TYR D  12  HIS D  13  ILE D  58  NGA D 105                    
SITE     2 AC4  9 GAL D 106  HOH D 151  HOH D 166  GLY E  33                    
SITE     3 AC4  9 ARG E  35                                                     
SITE     1 AC5 11 GLU E  51  GLN E  56  GLN E  61  TRP E  88                    
SITE     2 AC5 11 ASN E  90  LYS E  91  NGA E 105  HOH E 132                    
SITE     3 AC5 11 HOH E 134  HOH E 147  HOH E 153                               
SITE     1 AC6  6 GLN E  56  GAL E 104  GAL E 106  SIA E 108                    
SITE     2 AC6  6 HOH E 134  HOH E 160                                          
SITE     1 AC7  3 NGA E 105  BGC E 107  SIA E 108                               
SITE     1 AC8  7 THR D   6  ASP D   7  HOH D 160  GAL E 106                    
SITE     2 AC8  7 GLY G  54  SER G  55  HOH G 149                               
SITE     1 AC9 10 GLU E  11  TYR E  12  HIS E  13  ILE E  58                    
SITE     2 AC9 10 NGA E 105  GAL E 106  HOH E 141  HOH E 147                    
SITE     3 AC9 10 HOH E 153  HOH E 157                                          
SITE     1 BC1 10 GLU F  51  GLN F  56  GLN F  61  TRP F  88                    
SITE     2 BC1 10 ASN F  90  LYS F  91  NGA F 105  HOH F 136                    
SITE     3 BC1 10 HOH F 138  HOH F 154                                          
SITE     1 BC2  6 HIS F  13  ASN F  14  GLN F  56  GAL F 104                    
SITE     2 BC2  6 GAL F 106  SIA F 108                                          
SITE     1 BC3  3 HIS F  13  NGA F 105  SIA F 108                               
SITE     1 BC4  7 GLU F  11  TYR F  12  HIS F  13  NGA F 105                    
SITE     2 BC4  7 GAL F 106  HOH F 136  HOH F 141                               
SITE     1 BC5 12 HOH D 130  GLU G  51  GLN G  56  HIS G  57                    
SITE     2 BC5 12 GLN G  61  TRP G  88  ASN G  90  LYS G  91                    
SITE     3 BC5 12 NGA G 105  HOH G 137  HOH G 152  HOH G 166                    
SITE     1 BC6 11 HIS D  18  HOH D 129  HOH D 130  HOH D 164                    
SITE     2 BC6 11 ASN G  14  GLN G  56  ILE G  58  GAL G 104                    
SITE     3 BC6 11 GAL G 106  SIA G 108  HOH G 152                               
SITE     1 BC7  5 GLN D  16  HIS G  13  NGA G 105  BGC G 107                    
SITE     2 BC7  5 SIA G 108                                                     
SITE     1 BC8  9 HIS D  18  ALA D  46  THR D  47  HIS D  94                    
SITE     2 BC8  9 HOH D 124  HOH D 144  GAL G 106  HOH G 194                    
SITE     3 BC8  9 HOH H 192                                                     
SITE     1 BC9 11 GLU G  11  TYR G  12  HIS G  13  ILE G  58                    
SITE     2 BC9 11 NGA G 105  GAL G 106  HOH G 135  HOH G 137                    
SITE     3 BC9 11 HOH G 166  HOH G 177  LYS H  34                               
SITE     1 CC1 11 GLU H  51  GLN H  56  GLN H  61  TRP H  88                    
SITE     2 CC1 11 ASN H  90  LYS H  91  NGA H 105  HOH H 113                    
SITE     3 CC1 11 HOH H 135  HOH H 156  HOH H 157                               
SITE     1 CC2 11 HIS E  18  HIS H  13  ASN H  14  GLN H  56                    
SITE     2 CC2 11 GAL H 104  GAL H 106  SIA H 108  HOH H 113                    
SITE     3 CC2 11 HOH H 135  HOH H 136  HOH H 143                               
SITE     1 CC3  7 GLN E  16  HIS E  18  HOH E 171  NGA H 105                    
SITE     2 CC3  7 BGC H 107  SIA H 108  HOH H 168                               
SITE     1 CC4 10 HOH D 169  HIS E  18  ASN E  44  ALA E  46                    
SITE     2 CC4 10 THR E  47  HIS E  94  HOH E 117  HOH E 148                    
SITE     3 CC4 10 HIS H  13  GAL H 106                                          
SITE     1 CC5  9 GLU H  11  TYR H  12  HIS H  13  ILE H  58                    
SITE     2 CC5  9 NGA H 105  GAL H 106  HOH H 156  HOH H 157                    
SITE     3 CC5  9 HOH H 171                                                     
CRYST1  101.900   67.580   80.470  90.00 105.69  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      0.009814  0.000000  0.002757        0.00000                         
SCALE2      0.000000  0.014797  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012908        0.00000                         
MTRIX1   1  0.451348 -0.852471 -0.263775       38.12210    1                    
MTRIX2   1  0.845821  0.314495  0.430906       20.78470    1                    
MTRIX3   1 -0.284379 -0.417595  0.862985       18.81040    1                    
MTRIX1   2 -0.451209 -0.536654 -0.713031       32.37560    1                    
MTRIX2   2  0.521179 -0.807037  0.277602       67.89900    1                    
MTRIX3   2 -0.724419 -0.246360  0.643835       15.42260    1                    
MTRIX1   3 -0.448617  0.509795 -0.734065       -8.98500    1                    
MTRIX2   3 -0.532801 -0.811995 -0.238300       76.05360    1                    
MTRIX3   3 -0.717542  0.284205  0.635894       -5.77370    1                    
MTRIX1   4  0.444061  0.849074 -0.286151      -29.47840    1                    
MTRIX2   4 -0.854035  0.304509 -0.421781       34.30080    1                    
MTRIX3   4 -0.270988  0.431679  0.860360      -15.01190    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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