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Database: PDB
Entry: 5ELE
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HEADER    TOXIN                                   04-NOV-15   5ELE              
TITLE     CHOLERA TOXIN EL TOR B-PENTAMER IN COMPLEX WITH A 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 TOXIN B-PENTAMER, EL TOR VARIANT, CHOLERA           
COMPND   5 ENTEROTOXIN B CHAIN,CHOLERA ENTEROTOXIN GAMMA CHAIN,CHOLERAGENOID;   
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE O1;                             
SOURCE   3 ORGANISM_TAXID: 127906;                                              
SOURCE   4 GENE: CTXB, TOXB, VC_1456;                                           
SOURCE   5 EXPRESSION_SYSTEM: VIBRIO SP.;                                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 678;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: 60                                         
KEYWDS    CHOLERA TOXIN B-PENTAMER, A 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 5ELE    1       JRNL                                     
REVDAT   1   30-MAR-16 5ELE    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.    1.60 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) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 129701                         
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) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6822                            
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) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9264                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.18                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3530                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 499                          
REMARK   3   BIN FREE R VALUE                    : 0.3510                       
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          : 375                                     
REMARK   3   SOLVENT ATOMS            : 950                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.13000                                             
REMARK   3    B22 (A**2) : 1.32000                                              
REMARK   3    B33 (A**2) : -1.18000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.098         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.101         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.096         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.065         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8950 ; 0.014 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  8707 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12156 ; 1.809 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20186 ; 1.100 ; 3.017       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1094 ; 6.796 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   377 ;39.706 ;25.464       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1623 ;13.075 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;25.584 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1471 ; 0.168 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9663 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1893 ; 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):  4184 ; 1.552 ; 1.927       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4183 ; 1.546 ; 1.926       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5231 ; 2.366 ; 2.878       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  5232 ; 2.368 ; 2.879       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4766 ; 2.044 ; 2.237       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4766 ; 2.042 ; 2.237       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  6889 ; 3.177 ; 3.265       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 10989 ; 5.410 ;16.947       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 10990 ; 5.410 ;16.949       
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 5ELE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-NOV-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214971.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUL-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                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS NOVEMBER 3, 2014               
REMARK 200  DATA SCALING SOFTWARE          : XDS NOVEMBER 3, 2014               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 136523                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.140                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.12600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.03500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.490                              
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   (%): 44.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINE-TRIS, 9% PEG1000, 9%        
REMARK 280  PEG3350, 9% MPD, 0.03 M CALCIUM CHLORIDE, 0.03 M MAGNESIUM          
REMARK 280  CHLORIDE, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       31.77150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       98.27750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.48650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       98.27750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.77150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.48650            
REMARK 290   SMTRY3   4  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 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
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 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
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   NE2  HIS D    13     O    HOH D   301              1.80            
REMARK 500   CE1  HIS D    13     O    HOH D   301              1.98            
REMARK 500   OD1  ASN F    14     O    HOH F   301              1.98            
REMARK 500   O1L  NDG G   201     O    HOH G   301              2.07            
REMARK 500   OE2  GLU G    51     O    HOH G   302              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH F   383     O    HOH H   323     3454     2.17            
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 F  35   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG I  35   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  34       -3.95     72.97                                   
REMARK 500    GLU B  83      -70.27    -78.65                                   
REMARK 500    ASN B  90       31.68    -99.33                                   
REMARK 500    GLU C  83      -72.09    -79.88                                   
REMARK 500    ASN D  21       53.11     37.64                                   
REMARK 500    GLU D  83      -70.25    -75.93                                   
REMARK 500    GLU F  83      -70.87    -78.20                                   
REMARK 500    GLU G  83      -70.42    -78.61                                   
REMARK 500    LYS I  34       -1.44     72.44                                   
REMARK 500    LYS J  34       -1.33     70.14                                   
REMARK 500    GLU J  83      -71.88    -79.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH F 421        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH H 404        DISTANCE =  5.87 ANGSTROMS                       
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  51.3                                              
REMARK 620 3 GLU F  79   OE2 118.9  67.8                                        
REMARK 620 4 BCN A 205   O22  76.7 127.2 163.8                                  
REMARK 620 5 BCN A 205   O4  155.3 140.2  79.1  84.7                            
REMARK 620 6 BCN A 205   O6   84.1  74.3  75.1 113.0 118.6                      
REMARK 620 7 HOH A 302   O    82.6  82.6  94.9  82.2  78.8 156.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  79   OE2                                                    
REMARK 620 2 GLU F  79   OE1 120.8                                              
REMARK 620 3 GLU F  79   OE2  70.5  51.7                                        
REMARK 620 4 BCN A 203   O21 164.8  74.2 124.7                                  
REMARK 620 5 BCN A 203   O4   85.8 149.5 143.4  80.5                            
REMARK 620 6 BCN A 203   O6   78.9  80.1  80.6 103.0 122.8                      
REMARK 620 7 HOH F 302   O   101.7  83.1  81.4  81.6  76.5 160.6                
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  52.0                                              
REMARK 620 3 GLU J  79   OE2 120.6  68.9                                        
REMARK 620 4 BCN B 203   O22  74.9 125.7 163.7                                  
REMARK 620 5 HOH B 303   O    83.2  81.3  94.4  82.1                            
REMARK 620 6 BCN B 203   O6   72.2  78.7  92.9  97.1 154.6                      
REMARK 620 7 BCN B 203   O4  154.9 135.5  75.4  88.4  75.9 129.6                
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 118.0                                              
REMARK 620 3 GLU J  79   OE2  69.1  50.5                                        
REMARK 620 4 BCN B 201   O21 165.0  76.7 124.4                                  
REMARK 620 5 BCN B 201   O4   81.5 155.5 139.5  83.6                            
REMARK 620 6 BCN B 201   O6   73.0  83.9  80.2 113.5 117.7                      
REMARK 620 7 HOH A 334   O    96.7  90.2  84.2  79.6  72.0 163.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  79   OE1                                                    
REMARK 620 2 GLU C  79   OE2  51.0                                              
REMARK 620 3 GLU I  79   OE2 119.7  69.2                                        
REMARK 620 4 BCN C 203   O22  77.3 127.3 162.8                                  
REMARK 620 5 BCN C 203   O6  155.2 143.3  80.9  82.0                            
REMARK 620 6 HOH C 301   O    89.1  82.7  90.3  87.7  76.4                      
REMARK 620 7 BCN C 203   O4   77.3  78.8  85.5 101.5 120.6 161.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  79   OE2                                                    
REMARK 620 2 GLU I  79   OE1 120.3                                              
REMARK 620 3 GLU I  79   OE2  70.5  50.0                                        
REMARK 620 4 BCN C 201   O21 159.5  79.0 127.8                                  
REMARK 620 5 BCN C 201   O4   79.9  83.5  77.5 111.0                            
REMARK 620 6 BCN C 201   O6   80.2 152.6 142.8  79.3 120.0                      
REMARK 620 7 HOH C 361   O    88.5  88.1  82.8  85.4 159.5  73.8                
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  53.0                                              
REMARK 620 3 GLU H  79   OE2 120.4  68.0                                        
REMARK 620 4 BCN D 203   O6  151.2 136.8  80.2                                  
REMARK 620 5 HOH G 333   O    83.3  79.9  95.0  74.4                            
REMARK 620 6 BCN D 203   O22  77.3 128.8 162.1  82.2  83.5                      
REMARK 620 7 BCN D 203   O4   84.4  82.3  80.2 121.0 162.1 106.3                
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 119.4                                              
REMARK 620 3 GLU H  79   OE2  67.8  52.4                                        
REMARK 620 4 BCN D 201   O21 163.8  76.7 127.7                                  
REMARK 620 5 BCN D 201   O4   83.9 148.0 136.9  80.7                            
REMARK 620 6 BCN D 201   O6   78.4  81.6  79.4 107.4 127.2                      
REMARK 620 7 HOH D 352   O    96.4  85.7  82.3  82.5  69.0 161.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E  79   OE1                                                    
REMARK 620 2 GLU E  79   OE2  52.5                                              
REMARK 620 3 GLU G  79   OE2 120.6  68.3                                        
REMARK 620 4 BCN E 203   O6  151.9 139.2  79.8                                  
REMARK 620 5 BCN E 203   O21  75.9 127.9 163.5  84.2                            
REMARK 620 6 BCN E 203   O4   84.6  76.4  76.7 121.0 108.5                      
REMARK 620 7 HOH F 332   O    84.3  81.4  92.3  75.0  87.6 157.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E  79   OE2                                                    
REMARK 620 2 GLU G  79   OE1 119.2                                              
REMARK 620 3 GLU G  79   OE2  67.9  51.9                                        
REMARK 620 4 BCN E 201   O22 162.1  78.3 128.4                                  
REMARK 620 5 BCN E 201   O4   82.4 152.7 140.9  79.7                            
REMARK 620 6 BCN E 201   O6   82.8  78.0  78.3 106.3 123.9                      
REMARK 620 7 HOH E 363   O    93.1  87.0  82.0  83.3  74.5 159.9                
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 FUC A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN A 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN B 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN C 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN D 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN E 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FUC F 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE F 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FUC H 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FUC I 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NDG D    
REMARK 800  205 through FUC D 209                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NDG G    
REMARK 800  201 through FUC G 205                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NDG J    
REMARK 800  201 through FUC J 205                                               
DBREF  5ELE A    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELE B    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELE C    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELE D    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELE E    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELE F    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELE G    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELE H    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELE I    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELE 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    FUC  A 202      11                                                       
HET    BCN  A 203      11                                                       
HET     CA  A 204       1                                                       
HET    BCN  A 205      11                                                       
HET    BCN  B 201      11                                                       
HET     CA  B 202       1                                                       
HET    BCN  B 203      11                                                       
HET     CA  B 204       1                                                       
HET    BCN  C 201      11                                                       
HET     CA  C 202       1                                                       
HET    BCN  C 203      11                                                       
HET     CA  C 204       1                                                       
HET    BCN  D 201      11                                                       
HET     CA  D 202       1                                                       
HET    BCN  D 203      11                                                       
HET     CA  D 204       1                                                       
HET    NDG  D 205      15                                                       
HET    GAL  D 206      11                                                       
HET    A2G  D 207      14                                                       
HET    FUC  D 208      10                                                       
HET    FUC  D 209      10                                                       
HET    BCN  E 201      11                                                       
HET     CA  E 202       1                                                       
HET    BCN  E 203      11                                                       
HET     CA  E 204       1                                                       
HET    FUC  F 201      11                                                       
HET    1PE  F 202      16                                                       
HET    NDG  G 201      15                                                       
HET    GAL  G 202      22                                                       
HET    A2G  G 203      28                                                       
HET    FUC  G 204      20                                                       
HET    FUC  G 205      20                                                       
HET    NAG  G 206      15                                                       
HET    FUC  H 201      11                                                       
HET    FUC  I 201      11                                                       
HET    NDG  J 201      15                                                       
HET    GAL  J 202      11                                                       
HET    A2G  J 203      14                                                       
HET    FUC  J 204      10                                                       
HET    FUC  J 205      10                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     BCN BICINE                                                           
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETNAM     A2G N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE                               
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETSYN     1PE PEG400                                                           
FORMUL  11   CA    10(CA 2+)                                                    
FORMUL  12  FUC    10(C6 H12 O5)                                                
FORMUL  13  BCN    10(C6 H13 N O4)                                              
FORMUL  28  NDG    3(C8 H15 N O6)                                               
FORMUL  28  GAL    3(C6 H12 O6)                                                 
FORMUL  28  A2G    3(C8 H15 N O6)                                               
FORMUL  34  1PE    C10 H22 O6                                                   
FORMUL  35  NAG    C8 H15 N O6                                                  
FORMUL  39  HOH   *950(H2 O)                                                    
HELIX    1 AA1 ASN A    4  ALA A   10  1                                   7    
HELIX    2 AA2 SER A   60  THR A   78  1                                  19    
HELIX    3 AA3 ASN B    4  ALA B   10  1                                   7    
HELIX    4 AA4 ILE B   58  THR B   78  1                                  21    
HELIX    5 AA5 ASN C    4  ALA C   10  1                                   7    
HELIX    6 AA6 SER C   60  THR C   78  1                                  19    
HELIX    7 AA7 ASN D    4  ALA D   10  1                                   7    
HELIX    8 AA8 SER D   60  THR D   78  1                                  19    
HELIX    9 AA9 ASN E    4  GLU E   11  1                                   8    
HELIX   10 AB1 SER E   60  THR E   78  1                                  19    
HELIX   11 AB2 ASN F    4  GLU F   11  1                                   8    
HELIX   12 AB3 SER F   60  THR F   78  1                                  19    
HELIX   13 AB4 ASN G    4  GLU G   11  1                                   8    
HELIX   14 AB5 ILE G   58  GLU G   79  1                                  22    
HELIX   15 AB6 ASN H    4  ALA H   10  1                                   7    
HELIX   16 AB7 SER H   60  GLU H   79  1                                  20    
HELIX   17 AB8 ASN I    4  ALA I   10  1                                   7    
HELIX   18 AB9 ILE I   58  SER I   60  5                                   3    
HELIX   19 AC1 GLN I   61  THR I   78  1                                  18    
HELIX   20 AC2 ASN J    4  ALA J   10  1                                   7    
HELIX   21 AC3 SER J   60  GLU J   79  1                                  20    
SHEET    1   A 3 THR A  15  THR A  19  0                                        
SHEET    2   A 3 VAL A  82  TRP A  88 -1                                        
SHEET    3   A 3 ALA A  98  MET A 101 -1                                        
SHEET    1   B 3 SER A  26  SER A  30  0                                        
SHEET    2   B 3 MET A  37  THR A  41 -1                                        
SHEET    3   B 3 ILE A  47  VAL A  50 -1                                        
SHEET    1   C 3 THR B  15  THR B  19  0                                        
SHEET    2   C 3 VAL B  82  TRP B  88 -1                                        
SHEET    3   C 3 ALA B  98  MET B 101 -1                                        
SHEET    1   D 3 SER B  26  SER B  30  0                                        
SHEET    2   D 3 MET B  37  THR B  41 -1                                        
SHEET    3   D 3 ILE B  47  VAL B  50 -1                                        
SHEET    1   E 3 THR C  15  THR C  19  0                                        
SHEET    2   E 3 VAL C  82  TRP C  88 -1                                        
SHEET    3   E 3 ALA C  98  MET C 101 -1                                        
SHEET    1   F 3 SER C  26  SER C  30  0                                        
SHEET    2   F 3 MET C  37  THR C  41 -1                                        
SHEET    3   F 3 ILE C  47  VAL C  50 -1                                        
SHEET    1   G 3 THR D  15  THR D  19  0                                        
SHEET    2   G 3 VAL D  82  TRP D  88 -1                                        
SHEET    3   G 3 ALA D  98  MET D 101 -1                                        
SHEET    1   H 3 SER D  26  SER D  30  0                                        
SHEET    2   H 3 MET D  37  THR D  41 -1                                        
SHEET    3   H 3 ILE D  47  VAL D  50 -1                                        
SHEET    1   I 3 THR E  15  THR E  19  0                                        
SHEET    2   I 3 VAL E  82  TRP E  88 -1                                        
SHEET    3   I 3 ALA E  98  MET E 101 -1                                        
SHEET    1   J 3 SER E  26  ALA E  32  0                                        
SHEET    2   J 3 ARG E  35  THR E  41 -1                                        
SHEET    3   J 3 ILE E  47  VAL E  50 -1                                        
SHEET    1   K 3 THR F  15  THR F  19  0                                        
SHEET    2   K 3 VAL F  82  TRP F  88 -1                                        
SHEET    3   K 3 ALA F  98  MET F 101 -1                                        
SHEET    1   L 3 SER F  26  SER F  30  0                                        
SHEET    2   L 3 MET F  37  THR F  41 -1                                        
SHEET    3   L 3 ILE F  47  VAL F  50 -1                                        
SHEET    1   M 3 THR G  15  THR G  19  0                                        
SHEET    2   M 3 VAL G  82  TRP G  88 -1                                        
SHEET    3   M 3 ALA G  98  MET G 101 -1                                        
SHEET    1   N 3 SER G  26  SER G  30  0                                        
SHEET    2   N 3 MET G  37  THR G  41 -1                                        
SHEET    3   N 3 ILE G  47  VAL G  50 -1                                        
SHEET    1   O 3 THR H  15  THR H  19  0                                        
SHEET    2   O 3 VAL H  82  TRP H  88 -1                                        
SHEET    3   O 3 ALA H  98  MET H 101 -1                                        
SHEET    1   P 3 SER H  26  SER H  30  0                                        
SHEET    2   P 3 MET H  37  THR H  41 -1                                        
SHEET    3   P 3 ILE H  47  VAL H  50 -1                                        
SHEET    1   Q 3 THR I  15  THR I  19  0                                        
SHEET    2   Q 3 VAL I  82  TRP I  88 -1                                        
SHEET    3   Q 3 ALA I  98  MET I 101 -1                                        
SHEET    1   R 3 SER I  26  SER I  30  0                                        
SHEET    2   R 3 MET I  37  THR I  41 -1                                        
SHEET    3   R 3 ILE I  47  VAL I  50 -1                                        
SHEET    1   S 3 THR J  15  THR J  19  0                                        
SHEET    2   S 3 VAL J  82  TRP J  88 -1                                        
SHEET    3   S 3 ALA J  98  MET J 101 -1                                        
SHEET    1   T 3 SER J  26  SER J  30  0                                        
SHEET    2   T 3 MET J  37  THR J  41 -1                                        
SHEET    3   T 3 ILE J  47  VAL J  50 -1                                        
SSBOND   1 CYS A    9    CYS A   86                          1555   1555  2.02  
SSBOND   2 CYS B    9    CYS B   86                          1555   1555  2.02  
SSBOND   3 CYS C    9    CYS C   86                          1555   1555  2.02  
SSBOND   4 CYS D    9    CYS D   86                          1555   1555  2.03  
SSBOND   5 CYS E    9    CYS E   86                          1555   1555  1.98  
SSBOND   6 CYS F    9    CYS F   86                          1555   1555  2.01  
SSBOND   7 CYS G    9    CYS G   86                          1555   1555  2.04  
SSBOND   8 CYS H    9    CYS H   86                          1555   1555  2.01  
SSBOND   9 CYS I    9    CYS I   86                          1555   1555  2.05  
SSBOND  10 CYS J    9    CYS J   86                          1555   1555  2.01  
LINK         OE1 GLU A  79                CA    CA A 201     1555   1555  2.38  
LINK         OE2 GLU A  79                CA    CA A 201     1555   1555  2.57  
LINK         OE2 GLU A  79                CA    CA A 204     1555   1555  2.29  
LINK         OE1 GLU B  79                CA    CA B 202     1555   1555  2.43  
LINK         OE2 GLU B  79                CA    CA B 202     1555   1555  2.52  
LINK         OE2 GLU B  79                CA    CA B 204     1555   1555  2.32  
LINK         OE1 GLU C  79                CA    CA C 202     1555   1555  2.46  
LINK         OE2 GLU C  79                CA    CA C 202     1555   1555  2.60  
LINK         OE2 GLU C  79                CA    CA C 204     1555   1555  2.31  
LINK         OE1 GLU D  79                CA    CA D 202     1555   1555  2.50  
LINK         OE2 GLU D  79                CA    CA D 202     1555   1555  2.52  
LINK         OE2 GLU D  79                CA    CA D 204     1555   1555  2.35  
LINK         OE1 GLU E  79                CA    CA E 202     1555   1555  2.40  
LINK         OE2 GLU E  79                CA    CA E 204     1555   1555  2.27  
LINK         OE2 GLU E  79                CA    CA E 202     1555   1555  2.54  
LINK         OE1 GLU F  79                CA    CA A 204     1555   1555  2.49  
LINK         OE2 GLU F  79                CA    CA A 201     1555   1555  2.39  
LINK         OE2 GLU F  79                CA    CA A 204     1555   1555  2.50  
LINK         OE1 GLU G  79                CA    CA E 204     1555   1555  2.47  
LINK         OE2 GLU G  79                CA    CA E 204     1555   1555  2.56  
LINK         OE2 GLU G  79                CA    CA E 202     1555   1555  2.26  
LINK         OE1 GLU H  79                CA    CA D 204     1555   1555  2.40  
LINK         OE2 GLU H  79                CA    CA D 202     1555   1555  2.35  
LINK         OE2 GLU H  79                CA    CA D 204     1555   1555  2.54  
LINK         OE1 GLU I  79                CA    CA C 204     1555   1555  2.54  
LINK         OE2 GLU I  79                CA    CA C 202     1555   1555  2.35  
LINK         OE2 GLU I  79                CA    CA C 204     1555   1555  2.57  
LINK         OE1 GLU J  79                CA    CA B 204     1555   1555  2.46  
LINK         OE2 GLU J  79                CA    CA B 202     1555   1555  2.35  
LINK         OE2 GLU J  79                CA    CA B 204     1555   1555  2.54  
LINK        CA    CA A 201                 O22 BCN A 205     1555   1555  2.33  
LINK        CA    CA A 201                 O4  BCN A 205     1555   1555  2.30  
LINK        CA    CA A 201                 O6  BCN A 205     1555   1555  1.95  
LINK        CA    CA A 201                 O   HOH A 302     1555   1555  2.40  
LINK         O21 BCN A 203                CA    CA A 204     1555   1555  2.42  
LINK         O4  BCN A 203                CA    CA A 204     1555   1555  2.39  
LINK         O6  BCN A 203                CA    CA A 204     1555   1555  2.25  
LINK        CA    CA A 204                 O   HOH F 302     1555   1555  2.26  
LINK         O21 BCN B 201                CA    CA B 204     1555   1555  2.37  
LINK         O4  BCN B 201                CA    CA B 204     1555   1555  2.47  
LINK         O6  BCN B 201                CA    CA B 204     1555   1555  2.26  
LINK        CA    CA B 202                 O22 BCN B 203     1555   1555  2.30  
LINK        CA    CA B 202                 O   HOH B 303     1555   1555  2.38  
LINK        CA    CA B 202                 O6  BCN B 203     1555   1555  2.14  
LINK        CA    CA B 202                 O4  BCN B 203     1555   1555  2.46  
LINK        CA    CA B 204                 O   HOH A 334     1555   1555  2.40  
LINK         O21 BCN C 201                CA    CA C 204     1555   1555  2.42  
LINK         O4  BCN C 201                CA    CA C 204     1555   1555  2.17  
LINK         O6  BCN C 201                CA    CA C 204     1555   1555  2.40  
LINK        CA    CA C 202                 O22 BCN C 203     1555   1555  2.33  
LINK        CA    CA C 202                 O6  BCN C 203     1555   1555  2.29  
LINK        CA    CA C 202                 O   HOH C 301     1555   1555  2.29  
LINK        CA    CA C 202                 O4  BCN C 203     1555   1555  2.21  
LINK        CA    CA C 204                 O   HOH C 361     1555   1555  2.38  
LINK         O21 BCN D 201                CA    CA D 204     1555   1555  2.26  
LINK         O4  BCN D 201                CA    CA D 204     1555   1555  2.42  
LINK         O6  BCN D 201                CA    CA D 204     1555   1555  2.24  
LINK        CA    CA D 202                 O6  BCN D 203     1555   1555  2.37  
LINK        CA    CA D 202                 O   HOH G 333     1555   1555  2.40  
LINK        CA    CA D 202                 O22 BCN D 203     1555   1555  2.39  
LINK        CA    CA D 202                 O4  BCN D 203     1555   1555  2.33  
LINK        CA    CA D 204                 O   HOH D 352     1555   1555  2.48  
LINK         O3  NDG D 205                 C1  FUC D 209     1555   1555  1.48  
LINK         O4  NDG D 205                 C1  GAL D 206     1555   1555  1.43  
LINK         O2  GAL D 206                 C1  FUC D 208     1555   1555  1.46  
LINK         O3  GAL D 206                 C1  A2G D 207     1555   1555  1.47  
LINK         O22 BCN E 201                CA    CA E 204     1555   1555  2.32  
LINK         O4  BCN E 201                CA    CA E 204     1555   1555  2.39  
LINK         O6  BCN E 201                CA    CA E 204     1555   1555  1.89  
LINK        CA    CA E 202                 O6  BCN E 203     1555   1555  2.37  
LINK        CA    CA E 202                 O21 BCN E 203     1555   1555  2.36  
LINK        CA    CA E 202                 O4  BCN E 203     1555   1555  2.24  
LINK        CA    CA E 202                 O   HOH F 332     1555   1555  2.42  
LINK        CA    CA E 204                 O   HOH E 363     1555   1555  2.37  
LINK         O3 ANDG G 201                 C1 AFUC G 205     1555   1555  1.43  
LINK         O4 ANDG G 201                 C1 AGAL G 202     1555   1555  1.40  
LINK         C1 BGAL G 202                 O4 BNAG G 206     1555   1555  1.40  
LINK         O2 AGAL G 202                 C1 AFUC G 204     1555   1555  1.45  
LINK         O2 BGAL G 202                 C1 BFUC G 204     1555   1555  1.43  
LINK         O3 AGAL G 202                 C1 AA2G G 203     1555   1555  1.50  
LINK         O3 BGAL G 202                 C1 BA2G G 203     1555   1555  1.45  
LINK         C1 BFUC G 205                 O3 BNAG G 206     1555   1555  1.42  
LINK         O3  NDG J 201                 C1  FUC J 205     1555   1555  1.47  
LINK         O4  NDG J 201                 C1  GAL J 202     1555   1555  1.46  
LINK         O2  GAL J 202                 C1  FUC J 204     1555   1555  1.47  
LINK         O3  GAL J 202                 C1  A2G J 203     1555   1555  1.46  
CISPEP   1 THR A   92    PRO A   93          0        -4.08                     
CISPEP   2 THR B   92    PRO B   93          0       -18.15                     
CISPEP   3 THR C   92    PRO C   93          0        -9.01                     
CISPEP   4 THR D   92    PRO D   93          0        -7.84                     
CISPEP   5 THR D   92    PRO D   93          0        -7.64                     
CISPEP   6 THR E   92    PRO E   93          0       -15.60                     
CISPEP   7 THR F   92    PRO F   93          0       -12.70                     
CISPEP   8 THR G   92    PRO G   93          0       -16.71                     
CISPEP   9 THR H   92    PRO H   93          0       -11.06                     
CISPEP  10 THR I   92    PRO I   93          0       -11.42                     
CISPEP  11 THR J   92    PRO J   93          0       -12.74                     
SITE     1 AC1  4 GLU A  79  BCN A 205  HOH A 302  GLU F  79                    
SITE     1 AC2  6 TYR A  18  ALA A  46  ILE A  47  PRO A  93                    
SITE     2 AC2  6 HIS A  94  GLN E   3                                          
SITE     1 AC3 12 TYR A  76  LEU A  77  GLU A  79   CA A 204                    
SITE     2 AC3 12 HOH A 309  HOH A 325  HOH A 367  ALA E  80                    
SITE     3 AC3 12 LYS E  81  ASN E 103  GLU F  79  HOH F 302                    
SITE     1 AC4  4 GLU A  79  BCN A 203  GLU F  79  HOH F 302                    
SITE     1 AC5 12 GLU A  79   CA A 201  HOH A 302  HOH A 306                    
SITE     2 AC5 12 HOH A 309  HOH A 333  TYR F  76  LEU F  77                    
SITE     3 AC5 12 GLU F  79  ALA J  80  LYS J  81  ASN J 103                    
SITE     1 AC6 13 ALA A  80  LYS A  81  ASN A 103  HOH A 334                    
SITE     2 AC6 13 TYR B  76  LEU B  77  GLU B  79   CA B 204                    
SITE     3 AC6 13 HOH B 304  HOH B 308  HOH B 312  GLU J  79                    
SITE     4 AC6 13 HOH J 307                                                     
SITE     1 AC7  4 GLU B  79  BCN B 203  HOH B 303  GLU J  79                    
SITE     1 AC8 12 GLU B  79   CA B 202  HOH B 303  HOH B 304                    
SITE     2 AC8 12 ALA I  80  LYS I  81  ASN I 103  TYR J  76                    
SITE     3 AC8 12 LEU J  77  GLU J  79  HOH J 302  HOH J 305                    
SITE     1 AC9  4 HOH A 334  GLU B  79  BCN B 201  GLU J  79                    
SITE     1 AD1 11 ALA B  80  LYS B  81  ASN B 103  TYR C  76                    
SITE     2 AD1 11 LEU C  77  GLU C  79   CA C 204  HOH C 302                    
SITE     3 AD1 11 HOH C 317  HOH C 361  GLU I  79                               
SITE     1 AD2  5 LYS C  23  GLU C  79  BCN C 203  HOH C 301                    
SITE     2 AD2  5 GLU I  79                                                     
SITE     1 AD3 12 GLU C  79   CA C 202  HOH C 301  ALA H  80                    
SITE     2 AD3 12 LYS H  81  ASN H 103  HOH H 324  LYS I  23                    
SITE     3 AD3 12 TYR I  76  LEU I  77  GLU I  79  HOH I 302                    
SITE     1 AD4  4 GLU C  79  BCN C 201  HOH C 361  GLU I  79                    
SITE     1 AD5 14 ALA C  80  LYS C  81  ASN C 103  HOH C 351                    
SITE     2 AD5 14 TYR D  76  LEU D  77  GLU D  79   CA D 204                    
SITE     3 AD5 14 HOH D 303  HOH D 311  HOH D 326  HOH D 352                    
SITE     4 AD5 14 HOH D 380  GLU H  79                                          
SITE     1 AD6  4 GLU D  79  BCN D 203  HOH G 333  GLU H  79                    
SITE     1 AD7 12 GLU D  79   CA D 202  HOH D 303  ALA G  80                    
SITE     2 AD7 12 LYS G  81  ASN G 103  HOH G 333  TYR H  76                    
SITE     3 AD7 12 LEU H  77  GLU H  79  HOH H 303  HOH H 313                    
SITE     1 AD8  4 GLU D  79  BCN D 201  HOH D 352  GLU H  79                    
SITE     1 AD9 10 ALA D  80  LYS D  81  ASN D 103  TYR E  76                    
SITE     2 AD9 10 LEU E  77  GLU E  79   CA E 204  HOH E 301                    
SITE     3 AD9 10 HOH E 363  GLU G  79                                          
SITE     1 AE1  4 GLU E  79  BCN E 203  HOH F 332  GLU G  79                    
SITE     1 AE2 11 GLU E  79   CA E 202  HOH E 303  ALA F  80                    
SITE     2 AE2 11 LYS F  81  ASN F 103  HOH F 332  TYR G  76                    
SITE     3 AE2 11 LEU G  77  GLU G  79  HOH G 325                               
SITE     1 AE3  4 GLU E  79  BCN E 201  HOH E 363  GLU G  79                    
SITE     1 AE4  6 ALA F  46  ILE F  47  PHE F  48  PRO F  93                    
SITE     2 AE4  6 HIS F  94  GLN J   3                                          
SITE     1 AE5  8 LYS F  34  ARG F  35  HOH F 341  GLU H  11                    
SITE     2 AE5  8 TYR H  12  HIS H  13  GLU J  11  TYR J  12                    
SITE     1 AE6  6 GLN G   3  ALA H  46  ILE H  47  PHE H  48                    
SITE     2 AE6  6 PRO H  93  HIS H  94                                          
SITE     1 AE7  7 ASP F  59  GLN H   3  ALA I  46  ILE I  47                    
SITE     2 AE7  7 PHE I  48  PRO I  93  HIS I  94                               
SITE     1 AE8 22 LYS B  43  GLN C   3  GLN D  16  TYR D  18                    
SITE     2 AE8 22 ASN D  44  GLY D  45  ALA D  46  ILE D  47                    
SITE     3 AE8 22 THR D  92  PRO D  93  HIS D  94  HOH D 322                    
SITE     4 AE8 22 HOH D 329  HOH D 335  HOH D 365  HOH D 378                    
SITE     5 AE8 22 ASN I  21  GLU I  83  LYS I  84  HOH I 307                    
SITE     6 AE8 22 HOH I 335  HOH I 345                                          
SITE     1 AE9 65 LYS B  43  ALA C  80  LYS C  81  ASN C 103                    
SITE     2 AE9 65 HOH C 351  GLN D  16  TYR D  18  ASN D  44                    
SITE     3 AE9 65 GLY D  45  ALA D  46  ILE D  47  TYR D  76                    
SITE     4 AE9 65 LEU D  77  GLU D  79  HIS D  94  FUC D 209                    
SITE     5 AE9 65 HOH D 303  HOH D 311  HOH D 322  HOH D 326                    
SITE     6 AE9 65 HOH D 329  HOH D 335  HOH D 352  HOH D 378                    
SITE     7 AE9 65 HOH D 380  GLN F   3  GLN G  16  ILE G  17                    
SITE     8 AE9 65 TYR G  18  ASN G  44  GLY G  45  ALA G  46                    
SITE     9 AE9 65 ILE G  47  ALA G  80  LYS G  81  THR G  92                    
SITE    10 AE9 65 PRO G  93  HIS G  94  ASN G 103  HOH G 301                    
SITE    11 AE9 65 HOH G 307  HOH G 323  HOH G 333  HOH G 350                    
SITE    12 AE9 65 HOH G 362  HOH G 372  TYR H  76  LEU H  77                    
SITE    13 AE9 65 GLU H  79  HOH H 303  HOH H 313  THR I   1                    
SITE    14 AE9 65 ASN I  21  GLU I  83  LYS I  84  HOH I 307                    
SITE    15 AE9 65 HOH I 319  HOH I 335  HOH I 345  SER J  55                    
SITE    16 AE9 65 GLN J  56  ASN J  90  LYS J  91  THR J  92                    
SITE    17 AE9 65 HOH J 314                                                     
SITE     1 AF1 41 THR D  19  LYS D  84  GLN F   3  GLN G  16                    
SITE     2 AF1 41 ILE G  17  TYR G  18  ASN G  44  GLY G  45                    
SITE     3 AF1 41 ALA G  46  ILE G  47  THR G  92  PRO G  93                    
SITE     4 AF1 41 HIS G  94  HOH G 301  HOH G 307  HOH G 323                    
SITE     5 AF1 41 HOH G 350  HOH G 362  HOH G 372  THR I   1                    
SITE     6 AF1 41 GLN I   3  HOH I 319  GLN J  16  ILE J  17                    
SITE     7 AF1 41 TYR J  18  ASN J  44  GLY J  45  ALA J  46                    
SITE     8 AF1 41 ILE J  47  PHE J  48  SER J  55  GLN J  56                    
SITE     9 AF1 41 ASN J  90  LYS J  91  THR J  92  PRO J  93                    
SITE    10 AF1 41 HIS J  94  HOH J 306  HOH J 314  HOH J 318                    
SITE    11 AF1 41 HOH J 356                                                     
CRYST1   63.543   82.973  196.555  90.00  90.00  90.00 P 21 21 21   40          
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      0.015737  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012052  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005088        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system