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Database: PDB
Entry: 5ELC
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Original site: 5ELC 
HEADER    TOXIN                                   04-NOV-15   5ELC              
TITLE     CHOLERA TOXIN EL TOR B-PENTAMER IN COMPLEX WITH LEWIS-Y               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA ENTEROTOXIN SUBUNIT B;                             
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J;                                 
COMPND   4 SYNONYM: CHOLERA ENTEROTOXIN B CHAIN,CHOLERA ENTEROTOXIN GAMMA CHAIN,
COMPND   5 CHOLERAGENOID;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE SEROTYPE O1 (STRAIN ATCC 39315  
SOURCE   3 / EL TOR INABA N16961);                                              
SOURCE   4 ORGANISM_TAXID: 243277;                                              
SOURCE   5 GENE: CTXB, TOXB, VC_1456;                                           
SOURCE   6 EXPRESSION_SYSTEM: VIBRIO;                                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 662;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SP. 60                                     
KEYWDS    CHOLERA TOXIN B-PENTAMER, LEWIS-Y, COMPLEX, BLOOD GROUP               
KEYWDS   2 OLIGOSACCHARIDE/ANTIGEN, TOXIN                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.HEGGELUND,D.BURSCHOWSKY,U.KRENGEL                                 
REVDAT   2   27-APR-16 5ELC    1       JRNL                                     
REVDAT   1   30-MAR-16 5ELC    0                                                
JRNL        AUTH   J.E.HEGGELUND,D.BURSCHOWSKY,V.A.BJRNESTAD,V.HODNIK,          
JRNL        AUTH 2 G.ANDERLUH,U.KRENGEL                                         
JRNL        TITL   HIGH-RESOLUTION CRYSTAL STRUCTURES ELUCIDATE THE MOLECULAR   
JRNL        TITL 2 BASIS OF CHOLERA BLOOD GROUP DEPENDENCE.                     
JRNL        REF    PLOS PATHOG.                  V.  12 05567 2016              
JRNL        REFN                   ESSN 1553-7374                               
JRNL        PMID   27082955                                                     
JRNL        DOI    10.1371/JOURNAL.PPAT.1005567                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.62                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 138740                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7329                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8501                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.61                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3170                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 453                          
REMARK   3   BIN FREE R VALUE                    : 0.3640                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8170                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 590                                     
REMARK   3   SOLVENT ATOMS            : 654                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -8.77000                                             
REMARK   3    B22 (A**2) : -0.74000                                             
REMARK   3    B33 (A**2) : 9.51000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.63000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.022         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.022         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.061         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.539         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9052 ; 0.015 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  8644 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12306 ; 1.956 ; 2.023       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20074 ; 1.181 ; 3.035       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1035 ; 9.340 ; 5.043       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   370 ;39.852 ;25.405       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1549 ;13.862 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;24.784 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1563 ; 0.151 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9438 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1860 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4122 ; 1.385 ; 1.772       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4121 ; 1.385 ; 1.771       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5138 ; 2.081 ; 2.652       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  5139 ; 2.081 ; 2.652       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4930 ; 1.653 ; 2.019       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4930 ; 1.653 ; 2.019       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  7163 ; 2.508 ; 2.968       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 10505 ; 4.231 ;15.281       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 10506 ; 4.231 ;15.281       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5ELC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-NOV-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214989.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-OCT-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-1                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.965                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 2M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS JANUARY 10, 2014               
REMARK 200  DATA SCALING SOFTWARE          : XDS JANUARY 10, 2014               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 146071                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.620                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.340                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP 11.2.08; 09.12.2013                            
REMARK 200 STARTING MODEL: 3CHB                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINE-TRIS, 12.5% PEG1000,        
REMARK 280  12.5% PEG3350, 12.5% MPD, 0.03 M CALCIUM CHLORIDE, 0.03 M           
REMARK 280  MAGNESIUM CHLORIDE, PH 8.5, VAPOR DIFFUSION, HANGING DROP,          
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       40.45800            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 20150 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 21120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19180 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 21300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G, H, I, J                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG1  THR E    92     O    HOH E   301              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B  79   CD    GLU B  79   OE1     0.074                       
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    ARG B  73   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG C  73   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG C  73   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG I  73   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG I  73   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ASP J  70   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG J  73   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  35       40.57   -141.79                                   
REMARK 500    GLN A  56        4.68    -63.93                                   
REMARK 500    LYS B  34       -1.83     70.01                                   
REMARK 500    ASN C  21       51.98     39.34                                   
REMARK 500    GLU D  83      -73.16    -73.63                                   
REMARK 500    LYS E  34       -2.14     69.37                                   
REMARK 500    GLU F  83      -73.94    -76.66                                   
REMARK 500    ASN H  21       49.71     37.89                                   
REMARK 500    ASN I  21       51.11     36.95                                   
REMARK 500    ASN I  44        0.87    -69.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  79   OE1                                                    
REMARK 620 2 GLU A  79   OE2  51.1                                              
REMARK 620 3 GLU F  79   OE2  72.3 121.8                                        
REMARK 620 4 ASN J 103   OD1  82.4  81.1 106.2                                  
REMARK 620 5 BCN A 204   O4  131.4 144.4  81.9  66.0                            
REMARK 620 6 BCN A 204   O6   89.2  84.5  82.1 165.6 127.7                      
REMARK 620 7 BCN A 204   O22 125.1  76.2 162.1  74.9  82.4 100.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  79   OE1                                                    
REMARK 620 2 GLU F  79   OE1 122.4                                              
REMARK 620 3 GLU F  79   OE2  72.4  50.1                                        
REMARK 620 4 BCN A 202   O21 162.3  75.0 124.6                                  
REMARK 620 5 BCN A 202   O4   82.5  76.3  70.4 107.1                            
REMARK 620 6 BCN A 202   O6   76.7 157.6 145.2  85.6 121.0                      
REMARK 620 7 HOH F 332   O    92.4  76.5  73.9  88.3 143.8  92.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  79   OE1                                                    
REMARK 620 2 GLU B  79   OE2  56.8                                              
REMARK 620 3 GLU J  79   OE2 123.1  67.8                                        
REMARK 620 4 BCN B 203   O21  74.1 128.4 162.8                                  
REMARK 620 5 BCN B 203   O4  158.2 141.0  78.2  84.7                            
REMARK 620 6 BCN B 203   O6   84.8  75.5  68.9 117.4 110.0                      
REMARK 620 7 HOH B 312   O    95.1  86.6  94.0  82.6  77.0 158.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  79   OE2                                                    
REMARK 620 2 GLU J  79   OE1 120.9                                              
REMARK 620 3 GLU J  79   OE2  67.1  54.1                                        
REMARK 620 4 BCN B 201   O22 166.1  73.0 126.6                                  
REMARK 620 5 BCN B 201   O4   79.5  78.9  73.5 105.0                            
REMARK 620 6 BCN B 201   O6   80.4 154.2 141.1  86.2 122.1                      
REMARK 620 7 HOH J 301   O    87.2  90.9  82.6  92.7 155.7  74.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  79   OE1                                                    
REMARK 620 2 GLU C  79   OE2  48.1                                              
REMARK 620 3 GLU I  79   OE2 117.2  70.2                                        
REMARK 620 4 BCN C 202   O22  75.5 121.9 167.2                                  
REMARK 620 5 BCN C 202   O4  155.4 135.1  77.6  89.9                            
REMARK 620 6 BCN C 202   O6   79.2  80.9  80.9 104.3 124.2                      
REMARK 620 7 HOH C 355   O    76.3  75.6 101.7  78.9  81.5 153.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  79   OE2                                                    
REMARK 620 2 GLU I  79   OE1 120.9                                              
REMARK 620 3 GLU I  79   OE2  71.6  51.2                                        
REMARK 620 4 HOH C 339   O   103.5  85.4  83.2                                  
REMARK 620 5 BCN C 204   O4   72.7 157.2 130.5  73.0                            
REMARK 620 6 BCN C 204   O6   75.3  82.0  81.6 164.3 120.5                      
REMARK 620 7 BCN C 204   O21 166.1  72.9 122.2  78.5  95.2 106.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D  79   OE1                                                    
REMARK 620 2 GLU D  79   OE2  52.7                                              
REMARK 620 3 GLU H  79   OE2 121.7  69.0                                        
REMARK 620 4 BCN D 203   O6   78.9  72.4  83.5                                  
REMARK 620 5 BCN D 203   O22  78.4 129.8 157.6 112.1                            
REMARK 620 6 BCN D 203   O4  153.0 143.1  79.4 123.3  78.6                      
REMARK 620 7 HOH D 355   O    90.2  88.9  89.7 161.3  79.9  71.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D  79   OE2                                                    
REMARK 620 2 GLU H  79   OE1 117.6                                              
REMARK 620 3 GLU H  79   OE2  68.7  51.5                                        
REMARK 620 4 BCN D 201   O21 168.7  73.5 122.5                                  
REMARK 620 5 BCN D 201   O4   75.6  81.9  84.4 105.5                            
REMARK 620 6 BCN D 201   O6   82.9 151.5 133.3  87.4 124.4                      
REMARK 620 7 HOH H 303   O    96.3  83.4  73.0  86.5 157.3  74.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E  79   OE1                                                    
REMARK 620 2 GLU E  79   OE2  48.9                                              
REMARK 620 3 GLU G  79   OE2 120.0  71.5                                        
REMARK 620 4 BCN E 204   O22  81.2 128.8 158.3                                  
REMARK 620 5 BCN E 204   O4  155.7 143.8  79.5  78.9                            
REMARK 620 6 BCN E 204   O6   83.1  78.0  78.1 110.9 117.0                      
REMARK 620 7 HOH E 359   O    83.1  77.5  91.1  87.1  82.1 155.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E  79   OE2                                                    
REMARK 620 2 GLU G  79   OE1 120.7                                              
REMARK 620 3 GLU G  79   OE2  70.8  51.8                                        
REMARK 620 4 BCN E 202   O21 158.9  80.4 129.2                                  
REMARK 620 5 BCN E 202   O4   82.2 153.4 140.8  77.1                            
REMARK 620 6 BCN E 202   O6   78.2  85.4  87.8 106.4 114.4                      
REMARK 620 7 HOH E 357   O    99.2  83.8  78.0  81.2  78.9 165.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN B 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN C 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN D 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN E 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN E 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FUC F 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL A    
REMARK 800  205 through FUC A 208                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL B    
REMARK 800  205 through FUC B 208                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL C    
REMARK 800  205 through FUC C 208                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL D    
REMARK 800  205 through FUC D 208                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL E    
REMARK 800  205 through FUC E 208                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL G    
REMARK 800  201 through FUC G 204                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL H    
REMARK 800  201 through FUC H 204                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL I    
REMARK 800  201 through FUC I 204                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL J    
REMARK 800  201 through FUC J 204                                               
DBREF  5ELC A    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELC B    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELC C    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELC D    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELC E    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELC F    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELC G    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELC H    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELC I    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELC J    1   103  UNP    P01556   CHTB_VIBCH      22    124             
SEQRES   1 A  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 A  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 A  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 A  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 A  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 A  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 A  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 A  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 B  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 B  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 B  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 B  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 B  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 B  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 B  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 B  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 C  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 C  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 C  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 C  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 C  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 C  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 C  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 C  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 D  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 D  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 D  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 D  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 D  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 D  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 D  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 D  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 E  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 E  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 E  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 E  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 E  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 E  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 E  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 E  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 F  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 F  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 F  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 F  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 F  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 F  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 F  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 F  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 G  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 G  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 G  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 G  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 G  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 G  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 G  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 G  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 H  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 H  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 H  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 H  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 H  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 H  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 H  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 H  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 I  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 I  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 I  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 I  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 I  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 I  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 I  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 I  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 J  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 J  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 J  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 J  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 J  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 J  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 J  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 J  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
HET     CA  A 201       1                                                       
HET    BCN  A 202      11                                                       
HET     CA  A 203       1                                                       
HET    BCN  A 204      11                                                       
HET    GAL  A 205      11                                                       
HET    NDG  A 206      15                                                       
HET    FUC  A 207      10                                                       
HET    FUC  A 208      10                                                       
HET    BCN  B 201      11                                                       
HET     CA  B 202       1                                                       
HET    BCN  B 203      11                                                       
HET     CA  B 204       1                                                       
HET    GAL  B 205      22                                                       
HET    NDG  B 206      15                                                       
HET    FUC  B 207      20                                                       
HET    FUC  B 208      20                                                       
HET    NAG  B 209      15                                                       
HET     CA  C 201       1                                                       
HET    BCN  C 202      11                                                       
HET     CA  C 203       1                                                       
HET    BCN  C 204      11                                                       
HET    GAL  C 205      22                                                       
HET    NDG  C 206      15                                                       
HET    FUC  C 207      20                                                       
HET    FUC  C 208      20                                                       
HET    NAG  C 209      15                                                       
HET    BCN  D 201      11                                                       
HET     CA  D 202       1                                                       
HET    BCN  D 203      11                                                       
HET     CA  D 204       1                                                       
HET    GAL  D 205      11                                                       
HET    NAG  D 206      15                                                       
HET    FUC  D 207      10                                                       
HET    FUC  D 208      10                                                       
HET     CA  E 201       1                                                       
HET    BCN  E 202      11                                                       
HET     CA  E 203       1                                                       
HET    BCN  E 204      11                                                       
HET    GAL  E 205      11                                                       
HET    NDG  E 206      15                                                       
HET    FUC  E 207      10                                                       
HET    FUC  E 208      10                                                       
HET    FUC  F 201      11                                                       
HET    GAL  G 201      11                                                       
HET    NAG  G 202      15                                                       
HET    FUC  G 203      10                                                       
HET    FUC  G 204      10                                                       
HET    GAL  H 201      11                                                       
HET    NDG  H 202      15                                                       
HET    FUC  H 203      10                                                       
HET    FUC  H 204      10                                                       
HET    GAL  I 201      22                                                       
HET    NDG  I 202      15                                                       
HET    FUC  I 203      20                                                       
HET    FUC  I 204      20                                                       
HET    NAG  I 205      15                                                       
HET    GAL  J 201      11                                                       
HET    NDG  J 202      15                                                       
HET    FUC  J 203      10                                                       
HET    FUC  J 204      10                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     BCN BICINE                                                           
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL  11   CA    10(CA 2+)                                                    
FORMUL  12  BCN    10(C6 H13 N O4)                                              
FORMUL  15  GAL    9(C6 H12 O6)                                                 
FORMUL  15  NDG    7(C8 H15 N O6)                                               
FORMUL  15  FUC    19(C6 H12 O5)                                                
FORMUL  20  NAG    5(C8 H15 N O6)                                               
FORMUL  41  HOH   *654(H2 O)                                                    
HELIX    1 AA1 ASN A    4  GLU A   11  1                                   8    
HELIX    2 AA2 ILE A   58  THR A   78  1                                  21    
HELIX    3 AA3 ASN B    4  GLU B   11  1                                   8    
HELIX    4 AA4 ILE B   58  SER B   60  5                                   3    
HELIX    5 AA5 GLN B   61  GLU B   79  1                                  19    
HELIX    6 AA6 ASN C    4  ALA C   10  1                                   7    
HELIX    7 AA7 SER C   60  GLU C   79  1                                  20    
HELIX    8 AA8 ASN D    4  ALA D   10  1                                   7    
HELIX    9 AA9 SER D   60  GLU D   79  1                                  20    
HELIX   10 AB1 ASN E    4  ALA E   10  1                                   7    
HELIX   11 AB2 SER E   60  GLU E   79  1                                  20    
HELIX   12 AB3 ASN F    4  ALA F   10  1                                   7    
HELIX   13 AB4 SER F   60  THR F   78  1                                  19    
HELIX   14 AB5 ASN G    4  ALA G   10  1                                   7    
HELIX   15 AB6 ILE G   58  THR G   78  1                                  21    
HELIX   16 AB7 ASN H    4  ALA H   10  1                                   7    
HELIX   17 AB8 ILE H   58  SER H   60  5                                   3    
HELIX   18 AB9 GLN H   61  GLU H   79  1                                  19    
HELIX   19 AC1 ASN I    4  ALA I   10  1                                   7    
HELIX   20 AC2 ILE I   58  GLU I   79  1                                  22    
HELIX   21 AC3 ASN J    4  ALA J   10  1                                   7    
HELIX   22 AC4 ILE J   58  SER J   60  5                                   3    
HELIX   23 AC5 GLN J   61  GLU J   79  1                                  19    
SHEET    1  AA 7 THR A  15  LYS A  23  0                                        
SHEET    2  AA 7 LYS A  81  TRP A  88 -1                                        
SHEET    3  AA 7 HIS A  94  ALA A 102 -1                                        
SHEET    4  AA 7 ILE A  47  VAL A  50  1                                        
SHEET    5  AA 7 ALA A  38  THR A  41 -1                                        
SHEET    6  AA 7 SER A  26  SER A  30 -1                                        
SHEET    7  AA 7 HIS E  94  ALA E 102 -1                                        
SHEET    1  AB 3 THR A  15  LYS A  23  0                                        
SHEET    2  AB 3 HIS A  94  ALA A 102 -1                                        
SHEET    1  FA 7 THR F  15  LYS F  23  0                                        
SHEET    2  FA 7 LYS F  81  TRP F  88 -1                                        
SHEET    3  FA 7 HIS F  94  ALA F 102 -1                                        
SHEET    4  FA 7 ILE F  47  VAL F  50  1                                        
SHEET    5  FA 7 MET F  37  THR F  41 -1                                        
SHEET    6  FA 7 SER F  26  SER F  30 -1                                        
SHEET    7  FA 7 HIS J  94  ALA J 102 -1                                        
SHEET    1  FB 3 THR F  15  LYS F  23  0                                        
SHEET    2  FB 3 HIS F  94  ALA F 102 -1                                        
SSBOND   1 CYS A    9    CYS A   86                          1555   1555  2.09  
SSBOND   2 CYS B    9    CYS B   86                          1555   1555  2.10  
SSBOND   3 CYS C    9    CYS C   86                          1555   1555  2.06  
SSBOND   4 CYS D    9    CYS D   86                          1555   1555  2.06  
SSBOND   5 CYS E    9    CYS E   86                          1555   1555  2.05  
SSBOND   6 CYS F    9    CYS F   86                          1555   1555  2.05  
SSBOND   7 CYS G    9    CYS G   86                          1555   1555  2.08  
SSBOND   8 CYS H    9    CYS H   86                          1555   1555  2.04  
SSBOND   9 CYS I    9    CYS I   86                          1555   1555  2.05  
SSBOND  10 CYS J    9    CYS J   86                          1555   1555  2.07  
LINK         OE1 GLU A  79                CA    CA A 201     1555   1555  2.54  
LINK         OE1 GLU A  79                CA    CA A 203     1555   1555  2.33  
LINK         OE2 GLU A  79                CA    CA A 201     1555   1555  2.55  
LINK         OE1 GLU B  79                CA    CA B 202     1555   1555  2.13  
LINK         OE2 GLU B  79                CA    CA B 202     1555   1555  2.49  
LINK         OE2 GLU B  79                CA    CA B 204     1555   1555  2.33  
LINK         OE1 GLU C  79                CA    CA C 201     1555   1555  2.58  
LINK         OE2 GLU C  79                CA    CA C 201     1555   1555  2.60  
LINK         OE2 GLU C  79                CA    CA C 203     1555   1555  2.41  
LINK         OE1 GLU D  79                CA    CA D 202     1555   1555  2.54  
LINK         OE2 GLU D  79                CA    CA D 202     1555   1555  2.48  
LINK         OE2 GLU D  79                CA    CA D 204     1555   1555  2.37  
LINK         OE1 GLU E  79                CA    CA E 201     1555   1555  2.47  
LINK         OE2 GLU E  79                CA    CA E 201     1555   1555  2.64  
LINK         OE2 GLU E  79                CA    CA E 203     1555   1555  2.42  
LINK         OE1 GLU F  79                CA    CA A 203     1555   1555  2.52  
LINK         OE2 GLU F  79                CA    CA A 201     1555   1555  2.41  
LINK         OE2 GLU F  79                CA    CA A 203     1555   1555  2.60  
LINK         OE1 GLU G  79                CA    CA E 203     1555   1555  2.40  
LINK         OE2 GLU G  79                CA    CA E 201     1555   1555  2.29  
LINK         OE2 GLU G  79                CA    CA E 203     1555   1555  2.57  
LINK         OE1 GLU H  79                CA    CA D 204     1555   1555  2.54  
LINK         OE2 GLU H  79                CA    CA D 202     1555   1555  2.35  
LINK         OE2 GLU H  79                CA    CA D 204     1555   1555  2.48  
LINK         OE1 GLU I  79                CA    CA C 203     1555   1555  2.33  
LINK         OE2 GLU I  79                CA    CA C 201     1555   1555  2.40  
LINK         OE2 GLU I  79                CA    CA C 203     1555   1555  2.51  
LINK         OE1 GLU J  79                CA    CA B 204     1555   1555  2.26  
LINK         OE2 GLU J  79                CA    CA B 202     1555   1555  2.31  
LINK         OE2 GLU J  79                CA    CA B 204     1555   1555  2.51  
LINK         OD1 ASN J 103                CA    CA A 201     1555   1555  2.63  
LINK        CA    CA A 201                 O4  BCN A 204     1555   1555  2.29  
LINK        CA    CA A 201                 O6  BCN A 204     1555   1555  2.29  
LINK        CA    CA A 201                 O22 BCN A 204     1555   1555  2.34  
LINK         O21 BCN A 202                CA    CA A 203     1555   1555  2.31  
LINK         O4  BCN A 202                CA    CA A 203     1555   1555  2.48  
LINK         O6  BCN A 202                CA    CA A 203     1555   1555  2.50  
LINK        CA    CA A 203                 O   HOH F 332     1555   1555  2.17  
LINK         C1  GAL A 205                 O4  NDG A 206     1555   1555  1.42  
LINK         O2  GAL A 205                 C1  FUC A 208     1555   1555  1.48  
LINK         O3  NDG A 206                 C1  FUC A 207     1555   1555  1.44  
LINK         O22 BCN B 201                CA    CA B 204     1555   1555  2.34  
LINK         O4  BCN B 201                CA    CA B 204     1555   1555  2.58  
LINK         O6  BCN B 201                CA    CA B 204     1555   1555  2.39  
LINK        CA    CA B 202                 O21 BCN B 203     1555   1555  2.37  
LINK        CA    CA B 202                 O4  BCN B 203     1555   1555  2.20  
LINK        CA    CA B 202                 O6  BCN B 203     1555   1555  2.56  
LINK        CA    CA B 202                 O   HOH B 312     1555   1555  2.40  
LINK        CA    CA B 204                 O   HOH J 301     1555   1555  2.51  
LINK         C1 AGAL B 205                 O4 ANDG B 206     1555   1555  1.42  
LINK         C1 BGAL B 205                 O4 BNAG B 209     1555   1555  1.43  
LINK         O2 AGAL B 205                 C1 AFUC B 208     1555   1555  1.44  
LINK         O2 BGAL B 205                 C1 BFUC B 208     1555   1555  1.43  
LINK         O3 ANDG B 206                 C1 AFUC B 207     1555   1555  1.45  
LINK         C1 BFUC B 207                 O3 BNAG B 209     1555   1555  1.44  
LINK        CA    CA C 201                 O22 BCN C 202     1555   1555  2.36  
LINK        CA    CA C 201                 O4  BCN C 202     1555   1555  2.35  
LINK        CA    CA C 201                 O6  BCN C 202     1555   1555  2.42  
LINK        CA    CA C 201                 O   HOH C 355     1555   1555  2.26  
LINK        CA    CA C 203                 O   HOH C 339     1555   1555  2.40  
LINK        CA    CA C 203                 O4  BCN C 204     1555   1555  2.32  
LINK        CA    CA C 203                 O6  BCN C 204     1555   1555  2.30  
LINK        CA    CA C 203                 O21 BCN C 204     1555   1555  2.38  
LINK         C1 AGAL C 205                 O4 ANDG C 206     1555   1555  1.40  
LINK         C1 BGAL C 205                 O4 BNAG C 209     1555   1555  1.42  
LINK         O2 AGAL C 205                 C1 AFUC C 208     1555   1555  1.44  
LINK         O2 BGAL C 205                 C1 BFUC C 208     1555   1555  1.42  
LINK         O3 ANDG C 206                 C1 AFUC C 207     1555   1555  1.40  
LINK         C1 BFUC C 207                 O3 BNAG C 209     1555   1555  1.42  
LINK         O21 BCN D 201                CA    CA D 204     1555   1555  2.27  
LINK         O4  BCN D 201                CA    CA D 204     1555   1555  2.51  
LINK         O6  BCN D 201                CA    CA D 204     1555   1555  2.48  
LINK        CA    CA D 202                 O6  BCN D 203     1555   1555  2.46  
LINK        CA    CA D 202                 O22 BCN D 203     1555   1555  2.32  
LINK        CA    CA D 202                 O4  BCN D 203     1555   1555  2.47  
LINK        CA    CA D 202                 O   HOH D 355     1555   1555  2.54  
LINK        CA    CA D 204                 O   HOH H 303     1555   1555  2.29  
LINK         C1  GAL D 205                 O4  NAG D 206     1555   1555  1.40  
LINK         O2  GAL D 205                 C1  FUC D 208     1555   1555  1.46  
LINK         O3  NAG D 206                 C1  FUC D 207     1555   1555  1.49  
LINK        CA    CA E 201                 O22 BCN E 204     1555   1555  2.28  
LINK        CA    CA E 201                 O4  BCN E 204     1555   1555  2.39  
LINK        CA    CA E 201                 O6  BCN E 204     1555   1555  2.59  
LINK        CA    CA E 201                 O   HOH E 359     1555   1555  2.50  
LINK         O21 BCN E 202                CA    CA E 203     1555   1555  2.37  
LINK         O4  BCN E 202                CA    CA E 203     1555   1555  2.41  
LINK         O6  BCN E 202                CA    CA E 203     1555   1555  2.31  
LINK        CA    CA E 203                 O   HOH E 357     1555   1555  2.54  
LINK         C1  GAL E 205                 O4  NDG E 206     1555   1555  1.43  
LINK         O2  GAL E 205                 C1  FUC E 208     1555   1555  1.43  
LINK         O3  NDG E 206                 C1  FUC E 207     1555   1555  1.46  
LINK         C1  GAL G 201                 O4  NAG G 202     1555   1555  1.41  
LINK         O2  GAL G 201                 C1  FUC G 204     1555   1555  1.42  
LINK         O3  NAG G 202                 C1  FUC G 203     1555   1555  1.48  
LINK         C1  GAL H 201                 O4  NDG H 202     1555   1555  1.42  
LINK         O2  GAL H 201                 C1  FUC H 204     1555   1555  1.43  
LINK         O3  NDG H 202                 C1  FUC H 203     1555   1555  1.50  
LINK         C1 AGAL I 201                 O4 ANDG I 202     1555   1555  1.43  
LINK         C1 BGAL I 201                 O4 BNAG I 205     1555   1555  1.46  
LINK         O2 AGAL I 201                 C1 AFUC I 204     1555   1555  1.44  
LINK         O2 BGAL I 201                 C1 BFUC I 204     1555   1555  1.47  
LINK         O3 ANDG I 202                 C1 AFUC I 203     1555   1555  1.42  
LINK         C1 BFUC I 203                 O3 BNAG I 205     1555   1555  1.48  
LINK         C1  GAL J 201                 O4  NDG J 202     1555   1555  1.43  
LINK         O2  GAL J 201                 C1  FUC J 204     1555   1555  1.47  
LINK         O3  NDG J 202                 C1  FUC J 203     1555   1555  1.43  
CISPEP   1 THR A   92    PRO A   93          0        -6.16                     
CISPEP   2 THR B   92    PRO B   93          0       -10.49                     
CISPEP   3 THR C   92    PRO C   93          0       -19.73                     
CISPEP   4 THR D   92    PRO D   93          0        -9.19                     
CISPEP   5 THR E   92    PRO E   93          0       -10.99                     
CISPEP   6 THR F   92    PRO F   93          0        -0.93                     
CISPEP   7 THR G   92    PRO G   93          0       -10.05                     
CISPEP   8 THR H   92    PRO H   93          0        -6.72                     
CISPEP   9 THR I   92    PRO I   93          0        -8.47                     
CISPEP  10 THR J   92    PRO J   93          0       -15.33                     
SITE     1 AC1  4 GLU A  79  BCN A 204  GLU F  79  ASN J 103                    
SITE     1 AC2  9 TYR A  76  LEU A  77  GLU A  79   CA A 203                    
SITE     2 AC2  9 HOH A 304  ALA E  80  LYS E  81  ASN E 103                    
SITE     3 AC2  9 GLU F  79                                                     
SITE     1 AC3  4 GLU A  79  BCN A 202  GLU F  79  HOH F 332                    
SITE     1 AC4 10 LYS A  23  GLU A  79   CA A 201  TYR F  76                    
SITE     2 AC4 10 LEU F  77  GLU F  79  ALA J  80  LYS J  81                    
SITE     3 AC4 10 ASN J 103  HOH J 312                                          
SITE     1 AC5 12 ALA A  80  LYS A  81  ASN A 103  TYR B  76                    
SITE     2 AC5 12 LEU B  77  GLU B  79  BCN B 203   CA B 204                    
SITE     3 AC5 12 HOH B 304  HOH B 314  GLU J  79  HOH J 301                    
SITE     1 AC6  4 GLU B  79  BCN B 203  HOH B 312  GLU J  79                    
SITE     1 AC7 12 GLU B  79  BCN B 201   CA B 202  HOH B 312                    
SITE     2 AC7 12 HOH B 319  ALA I  80  LYS I  81  ASN I 103                    
SITE     3 AC7 12 TYR J  76  LEU J  77  GLU J  79  HOH J 321                    
SITE     1 AC8  4 GLU B  79  BCN B 201  GLU J  79  HOH J 301                    
SITE     1 AC9  4 GLU C  79  BCN C 202  HOH C 355  GLU I  79                    
SITE     1 AD1 12 LYS C  23  GLU C  79   CA C 201  HOH C 331                    
SITE     2 AD1 12 HOH C 355  ALA H  80  LYS H  81  ASN H 103                    
SITE     3 AD1 12 TYR I  76  LEU I  77  GLU I  79  HOH I 308                    
SITE     1 AD2  4 GLU C  79  BCN C 204  HOH C 339  GLU I  79                    
SITE     1 AD3 11 ALA B  80  LYS B  81  TYR C  76  LEU C  77                    
SITE     2 AD3 11 GLU C  79   CA C 203  HOH C 301  HOH C 315                    
SITE     3 AD3 11 HOH C 339  LYS I  23  GLU I  79                               
SITE     1 AD4 12 ALA C  80  LYS C  81  ASN C 103  LYS D  23                    
SITE     2 AD4 12 TYR D  76  LEU D  77  GLU D  79  BCN D 203                    
SITE     3 AD4 12  CA D 204  HOH D 305  GLU H  79  HOH H 303                    
SITE     1 AD5  4 GLU D  79  BCN D 203  HOH D 355  GLU H  79                    
SITE     1 AD6 11 GLU D  79  BCN D 201   CA D 202  HOH D 355                    
SITE     2 AD6 11 ALA G  80  LYS G  81  ASN G 103  TYR H  76                    
SITE     3 AD6 11 LEU H  77  GLU H  79  HOH H 304                               
SITE     1 AD7  4 GLU D  79  BCN D 201  GLU H  79  HOH H 303                    
SITE     1 AD8  4 GLU E  79  BCN E 204  HOH E 359  GLU G  79                    
SITE     1 AD9  9 ALA D  80  LYS D  81  TYR E  76  LEU E  77                    
SITE     2 AD9  9 GLU E  79   CA E 203  HOH E 303  HOH E 327                    
SITE     3 AD9  9 GLU G  79                                                     
SITE     1 AE1  4 GLU E  79  BCN E 202  HOH E 357  GLU G  79                    
SITE     1 AE2  9 GLU E  79   CA E 201  HOH E 346  ALA F  80                    
SITE     2 AE2  9 LYS F  81  TYR G  76  LEU G  77  GLU G  79                    
SITE     3 AE2  9 HOH G 306                                                     
SITE     1 AE3  8 TYR F  18  ALA F  46  ILE F  47  THR F  92                    
SITE     2 AE3  8 PRO F  93  HIS F  94  HOH F 333  GLN J   3                    
SITE     1 AE4 11 GLN A  16  TYR A  18  GLY A  45  ALA A  46                    
SITE     2 AE4 11 ILE A  47  PHE A  48  PRO A  93  HIS A  94                    
SITE     3 AE4 11 HOH A 306  HOH A 310  GLN E   3                               
SITE     1 AE5 32 GLN A   3  GLN A  16  TYR A  18  GLY A  45                    
SITE     2 AE5 32 ALA A  46  ILE A  47  PHE A  48  PRO A  93                    
SITE     3 AE5 32 HIS A  94  HOH A 306  HOH A 310  HOH A 343                    
SITE     4 AE5 32 TYR B  18  ASN B  44  GLY B  45  ALA B  46                    
SITE     5 AE5 32 ILE B  47  PHE B  48  PRO B  93  HIS B  94                    
SITE     6 AE5 32 HOH B 301  HOH B 302  HOH B 323  HOH B 338                    
SITE     7 AE5 32 HOH B 351  HOH B 356  HOH B 362  GLN E   3                    
SITE     8 AE5 32 ASN E  90  LYS E  91  THR E  92  HOH E 301                    
SITE     1 AE6 39 GLN A   3  HOH A 343  GLN B   3  TYR B  18                    
SITE     2 AE6 39 ASN B  44  GLY B  45  ALA B  46  ILE B  47                    
SITE     3 AE6 39 PHE B  48  PRO B  93  HIS B  94  HOH B 301                    
SITE     4 AE6 39 HOH B 302  HOH B 323  HOH B 338  HOH B 351                    
SITE     5 AE6 39 HOH B 356  HOH B 362  TYR C  18  ASN C  44                    
SITE     6 AE6 39 GLY C  45  ALA C  46  ILE C  47  PHE C  48                    
SITE     7 AE6 39 THR C  92  PRO C  93  HIS C  94  HOH C 303                    
SITE     8 AE6 39 HOH C 307  HOH C 311  HOH C 312  HOH C 321                    
SITE     9 AE6 39 HOH C 328  HOH C 345  HOH C 349  ASN E  90                    
SITE    10 AE6 39 LYS E  91  THR E  92  HOH E 301                               
SITE     1 AE7 29 GLN B   3  GLN C   3  TYR C  18  ASN C  44                    
SITE     2 AE7 29 GLY C  45  ALA C  46  ILE C  47  PHE C  48                    
SITE     3 AE7 29 THR C  92  PRO C  93  HIS C  94  HOH C 303                    
SITE     4 AE7 29 HOH C 307  HOH C 311  HOH C 312  HOH C 321                    
SITE     5 AE7 29 HOH C 328  HOH C 345  HOH C 349  TYR D  18                    
SITE     6 AE7 29 ASN D  44  GLY D  45  ALA D  46  ILE D  47                    
SITE     7 AE7 29 PRO D  93  HIS D  94  HOH D 310  HOH D 328                    
SITE     8 AE7 29 HOH D 345                                                     
SITE     1 AE8 23 GLN C   3  GLN D   3  TYR D  18  ASN D  44                    
SITE     2 AE8 23 GLY D  45  ALA D  46  ILE D  47  PRO D  93                    
SITE     3 AE8 23 HIS D  94  HOH D 310  HOH D 328  HOH D 345                    
SITE     4 AE8 23 TYR E  18  ASN E  44  GLY E  45  ALA E  46                    
SITE     5 AE8 23 ILE E  47  PRO E  93  HIS E  94  HOH E 309                    
SITE     6 AE8 23 HOH E 335  THR I  19  LYS I  84                               
SITE     1 AE9 44 GLN D   3  ALA D  80  LYS D  81  TYR E  18                    
SITE     2 AE9 44 ASN E  44  GLY E  45  ALA E  46  ILE E  47                    
SITE     3 AE9 44 TYR E  76  LEU E  77  GLU E  79  PRO E  93                    
SITE     4 AE9 44 HIS E  94  HOH E 303  HOH E 309  HOH E 327                    
SITE     5 AE9 44 HOH E 335  HOH E 346  HOH E 357  HOH E 359                    
SITE     6 AE9 44 GLN F   3  ALA F  80  LYS F  81  GLN G  16                    
SITE     7 AE9 44 TYR G  18  ASN G  44  GLY G  45  ALA G  46                    
SITE     8 AE9 44 ILE G  47  PHE G  48  TYR G  76  LEU G  77                    
SITE     9 AE9 44 GLU G  79  THR G  92  PRO G  93  HIS G  94                    
SITE    10 AE9 44 HOH G 303  HOH G 306  HOH G 316  HOH G 336                    
SITE    11 AE9 44 HOH G 345  THR I  19  LYS I  84  ASN I  90                    
SITE     1 AF1 25 GLN F   3  GLN G   3  GLN G  16  TYR G  18                    
SITE     2 AF1 25 ASN G  44  GLY G  45  ALA G  46  ILE G  47                    
SITE     3 AF1 25 PHE G  48  THR G  92  PRO G  93  HIS G  94                    
SITE     4 AF1 25 HOH G 303  HOH G 316  HOH G 336  HOH G 345                    
SITE     5 AF1 25 TYR H  18  ASN H  44  GLY H  45  ALA H  46                    
SITE     6 AF1 25 ILE H  47  PRO H  93  HIS H  94  HOH H 327                    
SITE     7 AF1 25 ASN I  90                                                     
SITE     1 AF2 28 LYS D  84  HOH D 302  GLN G   3  GLN H   3                    
SITE     2 AF2 28 TYR H  18  ASN H  44  GLY H  45  ALA H  46                    
SITE     3 AF2 28 ILE H  47  PRO H  93  HIS H  94  HOH H 327                    
SITE     4 AF2 28 TYR I  18  ASN I  44  GLY I  45  ALA I  46                    
SITE     5 AF2 28 ILE I  47  PHE I  48  PRO I  93  HIS I  94                    
SITE     6 AF2 28 HOH I 302  HOH I 311  HOH I 318  HOH I 325                    
SITE     7 AF2 28 HOH I 328  HOH I 342  HOH I 349  HOH I 363                    
SITE     1 AF3 30 LYS D  84  HOH D 302  GLN H   3  GLN I   3                    
SITE     2 AF3 30 TYR I  18  ASN I  44  GLY I  45  ALA I  46                    
SITE     3 AF3 30 ILE I  47  PHE I  48  PRO I  93  HIS I  94                    
SITE     4 AF3 30 HOH I 302  HOH I 311  HOH I 318  HOH I 325                    
SITE     5 AF3 30 HOH I 328  HOH I 342  HOH I 349  HOH I 363                    
SITE     6 AF3 30 TYR J  18  ASN J  44  GLY J  45  ALA J  46                    
SITE     7 AF3 30 ILE J  47  THR J  92  PRO J  93  HIS J  94                    
SITE     8 AF3 30 HOH J 306  HOH J 351                                          
CRYST1   63.667   80.916   95.770  90.00  96.07  90.00 P 1 21 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      0.015707  0.000000  0.001671        0.00000                         
SCALE2      0.000000  0.012358  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010501        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system