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Database: PDB
Entry: 5ELB
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Original site: 5ELB 
HEADER    TOXIN                                   04-NOV-15   5ELB              
TITLE     CHOLERA TOXIN CLASSICAL B-PENTAMER IN COMPLEX WITH LEWIS-Y            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA ENTEROTOXIN B SUBUNIT;                             
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J;                                 
COMPND   4 SYNONYM: CHOLERA ENTEROTOXIN SUBUNIT B,CHOLERA TOXIN B PROTEIN (CTB),
COMPND   5 CHOLERA TOXIN B SUBUNIT,CHOLERA TOXIN BETA SUBUNIT,CHOLERA TOXIN     
COMPND   6 SUBUNIT B,CHOLERAE TOXIN B SUBUNIT,CTXB;                             
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   3 ORGANISM_TAXID: 666;                                                 
SOURCE   4 GENE: CTXB, EN12_07055, ERS013160_03498, ERS013165_03981,            
SOURCE   5 ERS013197_06217, ERS013202_03762, ERS013206_03003, ERS013207_03244,  
SOURCE   6 ERS013212_03447;                                                     
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008                                      
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   3   11-OCT-17 5ELB    1       REMARK                                   
REVDAT   2   27-APR-16 5ELB    1       JRNL                                     
REVDAT   1   30-MAR-16 5ELB    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.    1.08 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) : 1.08                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.49                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 79.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 351626                         
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) : 0.122                           
REMARK   3   R VALUE            (WORKING SET) : 0.121                           
REMARK   3   FREE R VALUE                     : 0.155                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 18334                           
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) : 1.08                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3376                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 10.29                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3440                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 165                          
REMARK   3   BIN FREE R VALUE                    : 0.3150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8140                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 857                                     
REMARK   3   SOLVENT ATOMS            : 1550                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.54000                                              
REMARK   3    B22 (A**2) : 0.91000                                              
REMARK   3    B33 (A**2) : -1.45000                                             
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): 0.031         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.033         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.026         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.311         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.984                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.976                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10284 ; 0.021 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  9758 ; 0.005 ; 0.021       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14142 ; 2.218 ; 2.062       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 22897 ; 1.295 ; 3.056       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1217 ; 7.173 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   403 ;41.333 ;25.360       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1768 ;11.614 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;30.642 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1872 ; 0.192 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10575 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2061 ; 0.003 ; 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):  4438 ; 1.634 ; 1.127       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4437 ; 1.603 ; 1.126       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5632 ; 1.881 ; 1.691       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  5633 ; 1.882 ; 1.691       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5846 ; 2.680 ; 1.468       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  5847 ; 2.680 ; 1.468       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  8452 ; 3.193 ; 2.137       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 12720 ; 5.915 ;12.313       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 12721 ; 5.915 ;12.313       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2): 20042 ; 3.535 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   321 ;38.855 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2): 21012 ;12.706 ; 5.000       
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 5ELB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-NOV-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214992.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAY-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 JANUARY 10, 2014               
REMARK 200  DATA SCALING SOFTWARE          : XDS JANUARY 10, 2014               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 369957                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.080                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 78.9                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.08                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 19.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.6                                          
REMARK 200 STARTING MODEL: 3CHB                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINE-TRIS, 10% PEG1000, 10%      
REMARK 280  PEG3350, 10% MPD, 0.03 M CALCIUM CHLORIDE, 0.03 M MAGNESIUM         
REMARK 280  CHLORIDE. MICROSEEDING., 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 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       36.16650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       76.00950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.49200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       76.00950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.16650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.49200            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19860 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 21460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19260 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 22800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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   O1   GAL J  1201     O    HOH J  1301              2.12            
REMARK 500   O    HOH A   334     O    HOH G   358              2.15            
REMARK 500   O    HOH C   406     O    HOH C   429              2.15            
REMARK 500   O    HOH H  1441     O    HOH H  1451              2.17            
REMARK 500   O    HOH G   346     O    HOH G   418              2.17            
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 B   310     O    HOH J  1408     3545     2.03            
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  29   CD    GLU B  29   OE1    -0.073                       
REMARK 500    GLU E  11   CD    GLU E  11   OE1    -0.075                       
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 A  35   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A  35   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A  67   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B  35   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    LYS B  63   CD  -  CE  -  NZ  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    GLU C  29   CG  -  CD  -  OE1 ANGL. DEV. = -12.5 DEGREES          
REMARK 500    ARG C  67   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    LYS C  81   CD  -  CE  -  NZ  ANGL. DEV. =  20.9 DEGREES          
REMARK 500    ARG D  67   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG D  67   NE  -  CZ  -  NH2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    LYS D  81   CD  -  CE  -  NZ  ANGL. DEV. =  18.3 DEGREES          
REMARK 500    ARG E  35   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG E  35   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP E  59   CB  -  CG  -  OD1 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ARG E  67   NE  -  CZ  -  NH1 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    ARG F  67   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG F  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    LYS G  34   CD  -  CE  -  NZ  ANGL. DEV. =  17.7 DEGREES          
REMARK 500    ARG G  35   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG G  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG G  73   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG I  67   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    LYS J  23   CD  -  CE  -  NZ  ANGL. DEV. =  23.6 DEGREES          
REMARK 500    LYS J  43   CD  -  CE  -  NZ  ANGL. DEV. =  14.3 DEGREES          
REMARK 500    ARG J  67   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    LYS J  81   CD  -  CE  -  NZ  ANGL. DEV. =  16.1 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    GLU C  83      -70.28    -78.73                                   
REMARK 500    LYS H  34       -6.94     77.69                                   
REMARK 500    LYS H  34       -0.63     73.04                                   
REMARK 500    GLU I  83      -70.20    -78.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA B  102     ASN B  103                  148.82                    
REMARK 500 ALA G  102     ASN G  103                  148.56                    
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 B 463        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH B 464        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH E 440        DISTANCE =  6.47 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  49.5                                              
REMARK 620 3 GLU H  79   OE2 121.1  72.0                                        
REMARK 620 4 BCN A 204   O22  78.4 126.3 159.9                                  
REMARK 620 5 BCN A 204   O4  154.6 141.9  78.4  81.5                            
REMARK 620 6 HOH A 406   O    79.1  80.5  99.9  77.6  81.5                      
REMARK 620 7 BCN A 204   O6   79.7  81.0  85.7 104.2 120.5 157.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 205  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  79   OE2                                                    
REMARK 620 2 GLU H  79   OE1 121.1                                              
REMARK 620 3 GLU H  79   OE2  71.9  50.2                                        
REMARK 620 4 HOH A 411   O    97.8  82.1  78.2                                  
REMARK 620 5 BCN A 206   O6   80.1 152.3 139.4  77.1                            
REMARK 620 6 BCN A 206   O21 160.0  78.8 127.2  82.4  80.5                      
REMARK 620 7 BCN A 206   O4   82.9  78.8  81.1 158.0 124.4 104.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  79   OE1                                                    
REMARK 620 2 GLU B  79   OE2  50.9                                              
REMARK 620 3 GLU G  79   OE2 121.8  71.4                                        
REMARK 620 4 BCN B 202   O6  152.1 139.4  78.7                                  
REMARK 620 5 HOH F1363   O    80.4  80.5  99.0  77.6                            
REMARK 620 6 BCN B 202   O4   81.1  81.4  83.9 122.5 159.7                      
REMARK 620 7 BCN B 202   O22  76.6 126.4 161.5  83.2  80.8 102.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 205  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  79   OE2                                                    
REMARK 620 2 GLU G  79   OE1 120.0                                              
REMARK 620 3 GLU G  79   OE2  71.2  50.2                                        
REMARK 620 4 BCN B 206   O21 162.1  77.8 126.4                                  
REMARK 620 5 BCN B 206   O6   80.8 154.9 141.3  82.2                            
REMARK 620 6 HOH B 410   O   105.3  77.2  78.4  78.2  84.0                      
REMARK 620 7 BCN B 206   O4   81.3  79.8  82.4 102.6 119.7 156.2                
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  50.6                                              
REMARK 620 3 GLU F  79   OE1  71.4 121.2                                        
REMARK 620 4 BCN C 206   O22 126.8  77.5 161.2                                  
REMARK 620 5 BCN C 206   O4   81.4  79.1  84.5 101.6                            
REMARK 620 6 BCN C 206   O6  140.8 153.8  79.3  82.4 121.7                      
REMARK 620 7 HOH J1325   O    83.8  85.7  98.0  81.3 163.4  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 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  79   OE1                                                    
REMARK 620 2 GLU F  79   OE1  71.2                                              
REMARK 620 3 GLU F  79   OE2 121.1  50.1                                        
REMARK 620 4 BCN C 205   O6   80.9  80.1  84.1                                  
REMARK 620 5 BCN C 205   O21 161.1 125.7  76.9 108.5                            
REMARK 620 6 HOH C 418   O    94.6  82.0  83.5 162.1  81.2                      
REMARK 620 7 BCN C 205   O4   79.2 142.7 153.7 117.6  81.9  78.1                
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  50.7                                              
REMARK 620 3 GLU J  79   OE2 119.5  70.0                                        
REMARK 620 4 BCN D 203   O22  77.7 126.2 162.6                                  
REMARK 620 5 BCN D 203   O4   80.2  83.8  83.4 103.5                            
REMARK 620 6 BCN D 203   O6  153.7 137.4  79.7  83.1 122.2                      
REMARK 620 7 HOH D 397   O    83.9  78.6  96.1  82.4 161.4  75.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 206  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D  79   OE2                                                    
REMARK 620 2 GLU J  79   OE1 120.6                                              
REMARK 620 3 GLU J  79   OE2  69.3  51.7                                        
REMARK 620 4 BCN D 201   O21 160.5  77.5 127.0                                  
REMARK 620 5 BCN D 201   O4   85.3  80.8  82.0 106.4                            
REMARK 620 6 BCN D 201   O6   79.6 153.0 139.6  81.0 121.3                      
REMARK 620 7 HOH C 355   O    92.4  81.7  76.9  82.4 158.1  79.5                
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  50.7                                              
REMARK 620 3 GLU I  79   OE2 120.0  69.8                                        
REMARK 620 4 BCN E 203   O22  78.7 127.2 160.0                                  
REMARK 620 5 BCN E 203   O4   80.1  79.5  82.9 109.0                            
REMARK 620 6 BCN E 203   O6  155.6 141.0  79.0  81.1 119.9                      
REMARK 620 7 HOH E 306   O    85.3  79.9  91.9  82.1 159.3  78.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 206  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E  79   OE2                                                    
REMARK 620 2 GLU I  79   OE1 119.4                                              
REMARK 620 3 GLU I  79   OE2  69.6  50.4                                        
REMARK 620 4 BCN E 201   O21 162.6  77.4 125.9                                  
REMARK 620 5 BCN E 201   O4   84.4  79.7  81.9 104.4                            
REMARK 620 6 BCN E 201   O6   80.3 153.7 139.8  82.3 121.9                      
REMARK 620 7 HOH D 357   O    92.6  84.2  78.1  84.3 159.5  77.3                
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 GAL A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GLA 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 CA A 205                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN A 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GAL B 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GLA B 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 205                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN B 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GAL C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GLA C 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN C 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN C 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN D 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GAL D 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GLA D 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN E 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GAL E 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GLA E 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GLA F 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GAL F 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG G 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GLA G 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GAL G 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GAL H 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GLA H 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GAL I 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GLA I 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG I 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GAL J 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GLA J 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG J 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL A    
REMARK 800  207 through FUC A 210                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL B    
REMARK 800  207 through FUC B 210                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL C    
REMARK 800  207 through FUC C 210                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL D    
REMARK 800  207 through FUC D 210                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL E    
REMARK 800  207 through FUC E 210                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL F    
REMARK 800  1203 through FUC F 1206                                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL G    
REMARK 800  204 through FUC G 207                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL H    
REMARK 800  1203 through FUC H 1206                                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL I    
REMARK 800  1203 through NDG I 1207                                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL J    
REMARK 800  1203 through NDG J 1207                                             
DBREF  5ELB A    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
DBREF  5ELB B    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
DBREF  5ELB C    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
DBREF  5ELB D    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
DBREF  5ELB E    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
DBREF  5ELB F    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
DBREF  5ELB G    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
DBREF  5ELB H    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
DBREF  5ELB I    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
DBREF  5ELB J    1   103  UNP    Q57193   Q57193_VIBCL    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 HIS 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 THR 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 HIS 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 THR 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 HIS 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 THR 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 HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 D  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 D  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 D  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 D  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 D  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 D  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 E  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 E  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 E  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 E  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 E  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 E  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 E  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 E  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 F  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 F  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 F  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 F  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 F  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 F  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 F  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 F  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 G  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 G  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 G  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 G  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 G  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 G  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 G  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 G  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 H  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 H  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 H  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 H  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 H  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 H  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 H  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 H  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
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 HIS 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 THR 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 HIS 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 THR 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    GAL  A 202      12                                                       
HET    GLA  A 203      12                                                       
HET    BCN  A 204      11                                                       
HET     CA  A 205       1                                                       
HET    BCN  A 206      11                                                       
HET    GAL  A 207      22                                                       
HET    NDG  A 208      30                                                       
HET    FUC  A 209      20                                                       
HET    FUC  A 210      20                                                       
HET     CA  B 201       1                                                       
HET    BCN  B 202      11                                                       
HET    GAL  B 203      12                                                       
HET    GLA  B 204      12                                                       
HET     CA  B 205       1                                                       
HET    BCN  B 206      11                                                       
HET    GAL  B 207      22                                                       
HET    NDG  B 208      30                                                       
HET    FUC  B 209      20                                                       
HET    FUC  B 210      20                                                       
HET     CA  C 201       1                                                       
HET    GAL  C 202      12                                                       
HET    GLA  C 203      12                                                       
HET     CA  C 204       1                                                       
HET    BCN  C 205      11                                                       
HET    BCN  C 206      11                                                       
HET    GAL  C 207      22                                                       
HET    NDG  C 208      30                                                       
HET    FUC  C 209      20                                                       
HET    FUC  C 210      20                                                       
HET    BCN  D 201      11                                                       
HET     CA  D 202       1                                                       
HET    BCN  D 203      11                                                       
HET    GAL  D 204      12                                                       
HET    GLA  D 205      12                                                       
HET     CA  D 206       1                                                       
HET    GAL  D 207      22                                                       
HET    NDG  D 208      30                                                       
HET    FUC  D 209      20                                                       
HET    FUC  D 210      20                                                       
HET    BCN  E 201      11                                                       
HET     CA  E 202       1                                                       
HET    BCN  E 203      11                                                       
HET    GAL  E 204      12                                                       
HET    GLA  E 205      12                                                       
HET     CA  E 206       1                                                       
HET    GAL  E 207      11                                                       
HET    NDG  E 208      15                                                       
HET    FUC  E 209      10                                                       
HET    FUC  E 210      10                                                       
HET    GLA  F1201      12                                                       
HET    GAL  F1202      12                                                       
HET    GAL  F1203      11                                                       
HET    NDG  F1204      15                                                       
HET    FUC  F1205      10                                                       
HET    FUC  F1206      10                                                       
HET    PEG  G 201       7                                                       
HET    GLA  G 202      12                                                       
HET    GAL  G 203      12                                                       
HET    GAL  G 204      22                                                       
HET    NDG  G 205      30                                                       
HET    FUC  G 206      20                                                       
HET    FUC  G 207      20                                                       
HET    GAL  H1201      12                                                       
HET    GLA  H1202      12                                                       
HET    GAL  H1203      11                                                       
HET    NDG  H1204      15                                                       
HET    FUC  H1205      10                                                       
HET    FUC  H1206      10                                                       
HET    GAL  I1201      12                                                       
HET    GLA  I1202      12                                                       
HET    GAL  I1203      22                                                       
HET    NAG  I1204      15                                                       
HET    FUC  I1205      20                                                       
HET    FUC  I1206      20                                                       
HET    NDG  I1207      15                                                       
HET    GAL  J1201      12                                                       
HET    GLA  J1202      12                                                       
HET    GAL  J1203      22                                                       
HET    NAG  J1204      15                                                       
HET    FUC  J1205      20                                                       
HET    FUC  J1206      20                                                       
HET    NDG  J1207      15                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETNAM     GLA ALPHA D-GALACTOSE                                                
HETNAM     BCN BICINE                                                           
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL  11   CA    10(CA 2+)                                                    
FORMUL  12  GAL    20(C6 H12 O6)                                                
FORMUL  13  GLA    10(C6 H12 O6)                                                
FORMUL  14  BCN    10(C6 H13 N O4)                                              
FORMUL  17  NDG    10(C8 H15 N O6)                                              
FORMUL  17  FUC    20(C6 H12 O5)                                                
FORMUL  49  PEG    C4 H10 O3                                                    
FORMUL  58  NAG    2(C8 H15 N O6)                                               
FORMUL  62  HOH   *1550(H2 O)                                                   
HELIX    1 AA1 ASN A    4  ALA A   10  1                                   7    
HELIX    2 AA2 ILE A   58  SER A   60  5                                   3    
HELIX    3 AA3 GLN A   61  GLU A   79  1                                  19    
HELIX    4 AA4 ASN B    4  ALA B   10  1                                   7    
HELIX    5 AA5 SER B   60  GLU B   79  1                                  20    
HELIX    6 AA6 ASN C    4  ALA C   10  1                                   7    
HELIX    7 AA7 SER C   60  THR C   78  1                                  19    
HELIX    8 AA8 ASN D    4  GLU D   11  1                                   8    
HELIX    9 AA9 ILE D   58  SER D   60  5                                   3    
HELIX   10 AB1 GLN D   61  LEU D   77  1                                  17    
HELIX   11 AB2 ASN E    4  ALA E   10  1                                   7    
HELIX   12 AB3 SER E   60  THR E   78  1                                  19    
HELIX   13 AB4 ASN F    4  ALA F   10  1                                   7    
HELIX   14 AB5 SER F   60  THR F   78  1                                  19    
HELIX   15 AB6 ASN G    4  GLU G   11  1                                   8    
HELIX   16 AB7 ILE G   58  SER G   60  5                                   3    
HELIX   17 AB8 GLN G   61  GLU G   79  1                                  19    
HELIX   18 AB9 ASN H    4  ALA H   10  1                                   7    
HELIX   19 AC1 SER H   60  GLU H   79  1                                  20    
HELIX   20 AC2 ASN I    4  GLU I   11  1                                   8    
HELIX   21 AC3 SER I   60  GLU I   79  1                                  20    
HELIX   22 AC4 ASN J    4  ALA J   10  1                                   7    
HELIX   23 AC5 ILE J   58  SER J   60  5                                   3    
HELIX   24 AC6 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 THR A  47  VAL A  50  1                                        
SHEET    5  AA 7 MET A  37  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  ASP F  22  0                                        
SHEET    2  FA 7 VAL F  82  TRP F  88  1                                        
SHEET    3  FA 7 HIS F  94  ALA F 102  1                                        
SHEET    4  FA 7 THR 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  ASP F  22  0                                        
SHEET    2  FB 3 HIS F  94  ALA F 102  1                                        
SSBOND   1 CYS A    9    CYS A   86                          1555   1555  2.06  
SSBOND   2 CYS B    9    CYS B   86                          1555   1555  2.07  
SSBOND   3 CYS C    9    CYS C   86                          1555   1555  2.08  
SSBOND   4 CYS D    9    CYS D   86                          1555   1555  2.07  
SSBOND   5 CYS E    9    CYS E   86                          1555   1555  2.07  
SSBOND   6 CYS F    9    CYS F   86                          1555   1555  2.11  
SSBOND   7 CYS G    9    CYS G   86                          1555   1555  2.10  
SSBOND   8 CYS H    9    CYS H   86                          1555   1555  2.05  
SSBOND   9 CYS I    9    CYS I   86                          1555   1555  2.12  
SSBOND  10 CYS J    9    CYS J   86                          1555   1555  2.03  
LINK         OE1 GLU A  79                CA    CA A 201     1555   1555  2.44  
LINK         OE2 GLU A  79                CA    CA A 201     1555   1555  2.58  
LINK         OE2 GLU A  79                CA    CA A 205     1555   1555  2.37  
LINK         OE1 GLU B  79                CA    CA B 201     1555   1555  2.44  
LINK         OE2 GLU B  79                CA    CA B 201     1555   1555  2.56  
LINK         OE2 GLU B  79                CA    CA B 205     1555   1555  2.37  
LINK         OE1 GLU C  79                CA    CA C 201     1555   1555  2.52  
LINK         OE1 GLU C  79                CA    CA C 204     1555   1555  2.35  
LINK         OE2 GLU C  79                CA    CA C 201     1555   1555  2.46  
LINK         OE1 GLU D  79                CA    CA D 202     1555   1555  2.47  
LINK         OE2 GLU D  79                CA    CA D 202     1555   1555  2.56  
LINK         OE2 GLU D  79                CA    CA D 206     1555   1555  2.36  
LINK         OE1 GLU E  79                CA    CA E 202     1555   1555  2.45  
LINK         OE2 GLU E  79                CA    CA E 202     1555   1555  2.56  
LINK         OE2 GLU E  79                CA    CA E 206     1555   1555  2.39  
LINK         OE1 GLU F  79                CA    CA C 201     1555   1555  2.39  
LINK         OE1 GLU F  79                CA    CA C 204     1555   1555  2.57  
LINK         OE2 GLU F  79                CA    CA C 204     1555   1555  2.43  
LINK         OE1 GLU G  79                CA    CA B 205     1555   1555  2.44  
LINK         OE2 GLU G  79                CA    CA B 201     1555   1555  2.35  
LINK         OE2 GLU G  79                CA    CA B 205     1555   1555  2.55  
LINK         OE1 GLU H  79                CA    CA A 205     1555   1555  2.48  
LINK         OE2 GLU H  79                CA    CA A 201     1555   1555  2.36  
LINK         OE2 GLU H  79                CA    CA A 205     1555   1555  2.57  
LINK         OE1 GLU I  79                CA    CA E 206     1555   1555  2.46  
LINK         OE2 GLU I  79                CA    CA E 202     1555   1555  2.39  
LINK         OE2 GLU I  79                CA    CA E 206     1555   1555  2.57  
LINK         OE1 GLU J  79                CA    CA D 206     1555   1555  2.44  
LINK         OE2 GLU J  79                CA    CA D 202     1555   1555  2.35  
LINK         OE2 GLU J  79                CA    CA D 206     1555   1555  2.59  
LINK        CA    CA A 201                 O22 BCN A 204     1555   1555  2.32  
LINK        CA    CA A 201                 O4  BCN A 204     1555   1555  2.36  
LINK        CA    CA A 201                 O   HOH A 406     1555   1555  2.44  
LINK        CA    CA A 201                 O6  BCN A 204     1555   1555  2.30  
LINK        CA    CA A 205                 O   HOH A 411     1555   1555  2.39  
LINK        CA    CA A 205                 O6  BCN A 206     1555   1555  2.42  
LINK        CA    CA A 205                 O21 BCN A 206     1555   1555  2.33  
LINK        CA    CA A 205                 O4  BCN A 206     1555   1555  2.28  
LINK         C1 AGAL A 207                 O4 ANDG A 208     1555   1555  1.40  
LINK         C1 BGAL A 207                 O4 BNDG A 208     1555   1555  1.36  
LINK         O2 AGAL A 207                 C1 AFUC A 210     1555   1555  1.43  
LINK         O2 BGAL A 207                 C1 BFUC A 210     1555   1555  1.41  
LINK         O3 ANDG A 208                 C1 AFUC A 209     1555   1555  1.43  
LINK         O3 BNDG A 208                 C1 BFUC A 209     1555   1555  1.43  
LINK        CA    CA B 201                 O6  BCN B 202     1555   1555  2.38  
LINK        CA    CA B 201                 O   HOH F1363     1555   1555  2.36  
LINK        CA    CA B 201                 O4  BCN B 202     1555   1555  2.36  
LINK        CA    CA B 201                 O22 BCN B 202     1555   1555  2.34  
LINK        CA    CA B 205                 O21 BCN B 206     1555   1555  2.30  
LINK        CA    CA B 205                 O6  BCN B 206     1555   1555  2.33  
LINK        CA    CA B 205                 O   HOH B 410     1555   1555  2.43  
LINK        CA    CA B 205                 O4  BCN B 206     1555   1555  2.23  
LINK         C1 AGAL B 207                 O4 ANDG B 208     1555   1555  1.45  
LINK         C1 BGAL B 207                 O4 BNDG B 208     1555   1555  1.43  
LINK         O2 AGAL B 207                 C1 AFUC B 210     1555   1555  1.43  
LINK         O2 BGAL B 207                 C1 BFUC B 210     1555   1555  1.42  
LINK         O3 ANDG B 208                 C1 AFUC B 209     1555   1555  1.44  
LINK         O3 BNDG B 208                 C1 BFUC B 209     1555   1555  1.42  
LINK        CA    CA C 201                 O22 BCN C 206     1555   1555  2.33  
LINK        CA    CA C 201                 O4  BCN C 206     1555   1555  2.30  
LINK        CA    CA C 201                 O6  BCN C 206     1555   1555  2.32  
LINK        CA    CA C 201                 O   HOH J1325     1555   1555  2.44  
LINK        CA    CA C 204                 O6  BCN C 205     1555   1555  2.19  
LINK        CA    CA C 204                 O21 BCN C 205     1555   1555  2.32  
LINK        CA    CA C 204                 O   HOH C 418     1555   1555  2.51  
LINK        CA    CA C 204                 O4  BCN C 205     1555   1555  2.39  
LINK         C1 AGAL C 207                 O4 ANDG C 208     1555   1555  1.49  
LINK         C1 BGAL C 207                 O4 BNDG C 208     1555   1555  1.45  
LINK         O2 AGAL C 207                 C1 AFUC C 210     1555   1555  1.47  
LINK         O2 BGAL C 207                 C1 BFUC C 210     1555   1555  1.42  
LINK         O3 ANDG C 208                 C1 AFUC C 209     1555   1555  1.40  
LINK         O3 BNDG C 208                 C1 BFUC C 209     1555   1555  1.38  
LINK         O21 BCN D 201                CA    CA D 206     1555   1555  2.35  
LINK         O4  BCN D 201                CA    CA D 206     1555   1555  2.35  
LINK         O6  BCN D 201                CA    CA D 206     1555   1555  2.39  
LINK        CA    CA D 202                 O22 BCN D 203     1555   1555  2.35  
LINK        CA    CA D 202                 O4  BCN D 203     1555   1555  2.37  
LINK        CA    CA D 202                 O6  BCN D 203     1555   1555  2.39  
LINK        CA    CA D 202                 O   HOH D 397     1555   1555  2.44  
LINK        CA    CA D 206                 O   HOH C 355     1555   1555  2.40  
LINK         C1 AGAL D 207                 O4 ANDG D 208     1555   1555  1.44  
LINK         C1 BGAL D 207                 O4 BNDG D 208     1555   1555  1.33  
LINK         O2 AGAL D 207                 C1 AFUC D 210     1555   1555  1.47  
LINK         O2 BGAL D 207                 C1 BFUC D 210     1555   1555  1.41  
LINK         O3 ANDG D 208                 C1 AFUC D 209     1555   1555  1.41  
LINK         O3 BNDG D 208                 C1 BFUC D 209     1555   1555  1.44  
LINK         O21 BCN E 201                CA    CA E 206     1555   1555  2.36  
LINK         O4  BCN E 201                CA    CA E 206     1555   1555  2.29  
LINK         O6  BCN E 201                CA    CA E 206     1555   1555  2.44  
LINK        CA    CA E 202                 O22 BCN E 203     1555   1555  2.36  
LINK        CA    CA E 202                 O4  BCN E 203     1555   1555  2.30  
LINK        CA    CA E 202                 O6  BCN E 203     1555   1555  2.41  
LINK        CA    CA E 202                 O   HOH E 306     1555   1555  2.40  
LINK        CA    CA E 206                 O   HOH D 357     1555   1555  2.37  
LINK         C1  GAL E 207                 O4  NDG E 208     1555   1555  1.45  
LINK         O2  GAL E 207                 C1  FUC E 210     1555   1555  1.47  
LINK         O3  NDG E 208                 C1  FUC E 209     1555   1555  1.46  
LINK         C1  GAL F1203                 O4  NDG F1204     1555   1555  1.40  
LINK         O2  GAL F1203                 C1  FUC F1206     1555   1555  1.48  
LINK         O3  NDG F1204                 C1  FUC F1205     1555   1555  1.43  
LINK         C1 AGAL G 204                 O4 ANDG G 205     1555   1555  1.45  
LINK         C1 BGAL G 204                 O4 BNDG G 205     1555   1555  1.42  
LINK         O2 AGAL G 204                 C1 AFUC G 207     1555   1555  1.36  
LINK         O2 BGAL G 204                 C1 BFUC G 207     1555   1555  1.45  
LINK         O3 ANDG G 205                 C1 AFUC G 206     1555   1555  1.44  
LINK         O3 BNDG G 205                 C1 BFUC G 206     1555   1555  1.46  
LINK         C1  GAL H1203                 O4  NDG H1204     1555   1555  1.43  
LINK         O2  GAL H1203                 C1  FUC H1206     1555   1555  1.46  
LINK         O3  NDG H1204                 C1  FUC H1205     1555   1555  1.43  
LINK         C1 AGAL I1203                 O4 ANDG I1207     1555   1555  1.40  
LINK         C1 BGAL I1203                 O4 BNAG I1204     1555   1555  1.43  
LINK         O2 AGAL I1203                 C1 AFUC I1206     1555   1555  1.42  
LINK         O2 BGAL I1203                 C1 BFUC I1206     1555   1555  1.43  
LINK         O3 BNAG I1204                 C1 BFUC I1205     1555   1555  1.40  
LINK         C1 AFUC I1205                 O3 ANDG I1207     1555   1555  1.41  
LINK         C1 AGAL J1203                 O4 ANDG J1207     1555   1555  1.47  
LINK         C1 BGAL J1203                 O4 BNAG J1204     1555   1555  1.44  
LINK         O2 AGAL J1203                 C1 AFUC J1206     1555   1555  1.43  
LINK         O2 BGAL J1203                 C1 BFUC J1206     1555   1555  1.45  
LINK         O3 BNAG J1204                 C1 BFUC J1205     1555   1555  1.44  
LINK         C1 AFUC J1205                 O3 ANDG J1207     1555   1555  1.43  
CISPEP   1 THR A   92    PRO A   93          0       -13.30                     
CISPEP   2 THR B   92    PRO B   93          0       -11.58                     
CISPEP   3 THR B   92    PRO B   93          0       -12.60                     
CISPEP   4 THR C   92    PRO C   93          0       -12.37                     
CISPEP   5 THR D   92    PRO D   93          0       -10.44                     
CISPEP   6 THR E   92    PRO E   93          0        -6.96                     
CISPEP   7 THR F   92    PRO F   93          0        -6.71                     
CISPEP   8 THR G   92    PRO G   93          0        -9.92                     
CISPEP   9 THR H   92    PRO H   93          0       -13.45                     
CISPEP  10 THR I   92    PRO I   93          0       -13.89                     
CISPEP  11 THR J   92    PRO J   93          0        -8.93                     
SITE     1 AC1  4 GLU A  79  BCN A 204  HOH A 406  GLU H  79                    
SITE     1 AC2 12 GLU A  51  GLN A  56  HIS A  57  GLN A  61                    
SITE     2 AC2 12 TRP A  88  ASN A  90  LYS A  91  GLA A 203                    
SITE     3 AC2 12 HOH A 319  HOH A 324  HOH A 343  HOH A 349                    
SITE     1 AC3 12 GLU A  51  GLN A  56  HIS A  57  GLN A  61                    
SITE     2 AC3 12 TRP A  88  ASN A  90  LYS A  91  GAL A 202                    
SITE     3 AC3 12 HOH A 319  HOH A 324  HOH A 343  HOH A 349                    
SITE     1 AC4 13 GLU A  79   CA A 201  HOH A 309  HOH A 322                    
SITE     2 AC4 13 HOH A 334  HOH A 406  ALA G  80  LYS G  81                    
SITE     3 AC4 13 ASN G 103  TYR H  76  LEU H  77  GLU H  79                    
SITE     4 AC4 13 HOH H1309                                                     
SITE     1 AC5  4 GLU A  79  BCN A 206  HOH A 411  GLU H  79                    
SITE     1 AC6 13 TYR A  76  LEU A  77  GLU A  79   CA A 205                    
SITE     2 AC6 13 HOH A 314  HOH A 322  HOH A 374  HOH A 411                    
SITE     3 AC6 13 ALA E  80  LYS E  81  ASN E 103  LYS H  23                    
SITE     4 AC6 13 GLU H  79                                                     
SITE     1 AC7  4 GLU B  79  BCN B 202  HOH F1363  GLU G  79                    
SITE     1 AC8 13 LYS B  23  GLU B  79   CA B 201  HOH B 307                    
SITE     2 AC8 13 HOH B 388  ALA F  80  LYS F  81  ASN F 103                    
SITE     3 AC8 13 HOH F1363  TYR G  76  LEU G  77  GLU G  79                    
SITE     4 AC8 13 HOH G 327                                                     
SITE     1 AC9 12 GLU B  51  GLN B  56  HIS B  57  GLN B  61                    
SITE     2 AC9 12 TRP B  88  ASN B  90  LYS B  91  GLA B 204                    
SITE     3 AC9 12 HOH B 312  HOH B 316  HOH B 324  HOH B 381                    
SITE     1 AD1 13 GLU B  51  GLN B  56  HIS B  57  GLN B  61                    
SITE     2 AD1 13 TRP B  88  ASN B  90  LYS B  91  GAL B 203                    
SITE     3 AD1 13 HOH B 312  HOH B 316  HOH B 324  HOH B 381                    
SITE     4 AD1 13 HOH B 403                                                     
SITE     1 AD2  4 GLU B  79  BCN B 206  HOH B 410  GLU G  79                    
SITE     1 AD3 13 ALA A  80  LYS A  81  ASN A 103  TYR B  76                    
SITE     2 AD3 13 LEU B  77  GLU B  79   CA B 205  HOH B 307                    
SITE     3 AD3 13 HOH B 315  HOH B 320  HOH B 410  LYS G  23                    
SITE     4 AD3 13 GLU G  79                                                     
SITE     1 AD4  4 GLU C  79  BCN C 206  GLU F  79  HOH J1325                    
SITE     1 AD5 13 GLU C  51  GLN C  56  HIS C  57  GLN C  61                    
SITE     2 AD5 13 TRP C  88  ASN C  90  LYS C  91  GLA C 203                    
SITE     3 AD5 13 HOH C 307  HOH C 327  HOH C 337  HOH C 356                    
SITE     4 AD5 13 HOH D 376                                                     
SITE     1 AD6 13 GLU C  51  GLN C  56  HIS C  57  GLN C  61                    
SITE     2 AD6 13 TRP C  88  ASN C  90  LYS C  91  GAL C 202                    
SITE     3 AD6 13 HOH C 307  HOH C 327  HOH C 337  HOH C 356                    
SITE     4 AD6 13 HOH D 376                                                     
SITE     1 AD7  4 GLU C  79  BCN C 205  HOH C 418  GLU F  79                    
SITE     1 AD8 13 ALA B  80  LYS B  81  ASN B 103  TYR C  76                    
SITE     2 AD8 13 LEU C  77  GLU C  79   CA C 204  HOH C 306                    
SITE     3 AD8 13 HOH C 315  HOH C 318  HOH C 418  LYS F  23                    
SITE     4 AD8 13 GLU F  79                                                     
SITE     1 AD9 12 GLU C  79   CA C 201  HOH C 318  HOH C 413                    
SITE     2 AD9 12 TYR F  76  LEU F  77  GLU F  79  HOH F1315                    
SITE     3 AD9 12 ALA J  80  LYS J  81  ASN J 103  HOH J1325                    
SITE     1 AE1 11 LYS C  81  ASN C 103  HOH C 355  TYR D  76                    
SITE     2 AE1 11 LEU D  77  GLU D  79   CA D 206  HOH D 307                    
SITE     3 AE1 11 HOH D 312  HOH D 318  GLU J  79                               
SITE     1 AE2  4 GLU D  79  BCN D 203  HOH D 397  GLU J  79                    
SITE     1 AE3 13 LYS D  23  GLU D  79   CA D 202  HOH D 307                    
SITE     2 AE3 13 HOH D 331  HOH D 397  ALA I  80  LYS I  81                    
SITE     3 AE3 13 ASN I 103  TYR J  76  LEU J  77  GLU J  79                    
SITE     4 AE3 13 HOH J1321                                                     
SITE     1 AE4 13 GLU D  51  GLN D  56  HIS D  57  GLN D  61                    
SITE     2 AE4 13 TRP D  88  ASN D  90  LYS D  91  GLA D 205                    
SITE     3 AE4 13 HOH D 323  HOH D 340  HOH D 354  HOH D 373                    
SITE     4 AE4 13 HOH D 392                                                     
SITE     1 AE5 12 GLU D  51  GLN D  56  HIS D  57  GLN D  61                    
SITE     2 AE5 12 TRP D  88  ASN D  90  LYS D  91  GAL D 204                    
SITE     3 AE5 12 HOH D 323  HOH D 340  HOH D 354  HOH D 373                    
SITE     1 AE6  4 HOH C 355  GLU D  79  BCN D 201  GLU J  79                    
SITE     1 AE7 14 ALA D  80  LYS D  81  ASN D 103  HOH D 301                    
SITE     2 AE7 14 HOH D 357  TYR E  76  LEU E  77  GLU E  79                    
SITE     3 AE7 14  CA E 206  HOH E 309  HOH E 315  LYS I  23                    
SITE     4 AE7 14 GLU I  79  HOH I1389                                          
SITE     1 AE8  4 GLU E  79  BCN E 203  HOH E 306  GLU I  79                    
SITE     1 AE9 13 GLU E  79   CA E 202  HOH E 306  HOH E 309                    
SITE     2 AE9 13 HOH E 312  HOH E 330  ALA H  80  LYS H  81                    
SITE     3 AE9 13 ASN H 103  TYR I  76  LEU I  77  GLU I  79                    
SITE     4 AE9 13 HOH I1319                                                     
SITE     1 AF1 13 HOH A 378  GLU E  51  GLN E  56  HIS E  57                    
SITE     2 AF1 13 GLN E  61  TRP E  88  ASN E  90  LYS E  91                    
SITE     3 AF1 13 GLA E 205  HOH E 311  HOH E 321  HOH E 345                    
SITE     4 AF1 13 HOH E 378                                                     
SITE     1 AF2 13 HOH A 378  GLU E  51  GLN E  56  HIS E  57                    
SITE     2 AF2 13 GLN E  61  TRP E  88  ASN E  90  LYS E  91                    
SITE     3 AF2 13 GAL E 204  HOH E 311  HOH E 321  HOH E 345                    
SITE     4 AF2 13 HOH E 378                                                     
SITE     1 AF3  4 HOH D 357  GLU E  79  BCN E 201  GLU I  79                    
SITE     1 AF4 13 ASN F  14  GLU F  51  GLN F  56  GLN F  61                    
SITE     2 AF4 13 TRP F  88  ASN F  90  LYS F  91  GAL F1202                    
SITE     3 AF4 13 HOH F1313  HOH F1319  HOH F1330  HOH F1386                    
SITE     4 AF4 13 HIS G  13                                                     
SITE     1 AF5 13 ASN F  14  GLU F  51  GLN F  56  GLN F  61                    
SITE     2 AF5 13 TRP F  88  ASN F  90  LYS F  91  GLA F1201                    
SITE     3 AF5 13 HOH F1313  HOH F1314  HOH F1319  HOH F1330                    
SITE     4 AF5 13 HOH F1386                                                     
SITE     1 AF6 11 ALA D  10  GLU D  11  TYR D  12  HIS D  13                    
SITE     2 AF6 11 HOH D 308  HOH D 368  HOH D 435  THR G   6                    
SITE     3 AF6 11 GLU G  83  LYS G  84  HOH G 383                               
SITE     1 AF7 13 GLU G  51  GLN G  56  GLN G  61  TRP G  88                    
SITE     2 AF7 13 ASN G  90  LYS G  91  GAL G 203  HOH G 318                    
SITE     3 AF7 13 HOH G 324  HOH G 352  HOH G 367  HOH G 369                    
SITE     4 AF7 13 HOH G 396                                                     
SITE     1 AF8 13 GLU G  51  GLN G  56  GLN G  61  TRP G  88                    
SITE     2 AF8 13 ASN G  90  LYS G  91  GLA G 202  HOH G 318                    
SITE     3 AF8 13 HOH G 324  HOH G 367  HOH G 369  HOH G 396                    
SITE     4 AF8 13 HOH G 410                                                     
SITE     1 AF9 14 GLU H  51  GLN H  56  HIS H  57  GLN H  61                    
SITE     2 AF9 14 TRP H  88  ASN H  90  LYS H  91  GLA H1202                    
SITE     3 AF9 14 HOH H1304  HOH H1316  HOH H1317  HOH H1341                    
SITE     4 AF9 14 HOH H1347  HOH H1362                                          
SITE     1 AG1 13 GLU H  51  GLN H  56  HIS H  57  GLN H  61                    
SITE     2 AG1 13 TRP H  88  ASN H  90  LYS H  91  GAL H1201                    
SITE     3 AG1 13 HOH H1304  HOH H1316  HOH H1317  HOH H1341                    
SITE     4 AG1 13 HOH H1347                                                     
SITE     1 AG2 13 GLU I  51  GLN I  56  HIS I  57  GLN I  61                    
SITE     2 AG2 13 TRP I  88  ASN I  90  LYS I  91  GLA I1202                    
SITE     3 AG2 13 HOH I1308  HOH I1322  HOH I1375  HOH I1388                    
SITE     4 AG2 13 HOH I1395                                                     
SITE     1 AG3 12 GLU I  51  GLN I  56  GLN I  61  TRP I  88                    
SITE     2 AG3 12 ASN I  90  LYS I  91  GAL I1201  HOH I1308                    
SITE     3 AG3 12 HOH I1322  HOH I1375  HOH I1388  HOH I1395                    
SITE     1 AG4 12 ASN A  90  LYS A  91  GLY I  45  THR I  47                    
SITE     2 AG4 12 GAL I1203  FUC I1205  FUC I1206  NDG I1207                    
SITE     3 AG4 12 HOH I1304  HOH I1351  HOH I1353  HOH I1355                    
SITE     1 AG5 13 HOH F1379  GLU J  51  GLN J  56  HIS J  57                    
SITE     2 AG5 13 GLN J  61  TRP J  88  ASN J  90  LYS J  91                    
SITE     3 AG5 13 GLA J1202  HOH J1301  HOH J1308  HOH J1314                    
SITE     4 AG5 13 HOH J1425                                                     
SITE     1 AG6 13 HOH F1379  GLU J  51  GLN J  56  HIS J  57                    
SITE     2 AG6 13 GLN J  61  TRP J  88  ASN J  90  LYS J  91                    
SITE     3 AG6 13 GAL J1201  HOH J1301  HOH J1308  HOH J1314                    
SITE     4 AG6 13 HOH J1425                                                     
SITE     1 AG7 13 ASN B  90  LYS B  91  GLN I   3  GLY J  45                    
SITE     2 AG7 13 THR J  47  GAL J1203  FUC J1205  FUC J1206                    
SITE     3 AG7 13 NDG J1207  HOH J1322  HOH J1340  HOH J1398                    
SITE     4 AG7 13 HOH J1410                                                     
SITE     1 AG8 20 HIS A  18  ASN A  44  GLY A  45  ALA A  46                    
SITE     2 AG8 20 THR A  47  PRO A  93  HIS A  94  HOH A 308                    
SITE     3 AG8 20 HOH A 311  HOH A 313  HOH A 317  HOH A 320                    
SITE     4 AG8 20 HOH A 354  HOH A 372  HOH A 382  HOH A 386                    
SITE     5 AG8 20 THR D  19  LYS D  84  HOH D 403  GLN E   3                    
SITE     1 AG9 45 GLN A   3  HIS A  18  ASN A  44  GLY A  45                    
SITE     2 AG9 45 ALA A  46  THR A  47  PRO A  93  HIS A  94                    
SITE     3 AG9 45 HOH A 308  HOH A 311  HOH A 313  HOH A 317                    
SITE     4 AG9 45 HOH A 320  HOH A 354  HOH A 372  HOH A 382                    
SITE     5 AG9 45 HOH A 386  GLN B  16  HIS B  18  ASN B  44                    
SITE     6 AG9 45 GLY B  45  ALA B  46  THR B  47  THR B  92                    
SITE     7 AG9 45 PRO B  93  HIS B  94  HOH B 302  HOH B 313                    
SITE     8 AG9 45 HOH B 321  HOH B 322  HOH B 326  HOH B 334                    
SITE     9 AG9 45 HOH B 339  HOH B 340  HOH B 371  HOH B 382                    
SITE    10 AG9 45 HOH B 400  HOH B 414  THR C  19  LYS C  84                    
SITE    11 AG9 45 THR D  19  LYS D  84  HOH D 403  GLN E   3                    
SITE    12 AG9 45 HOH J1431                                                     
SITE     1 AH1 45 GLN A   3  GLN B   3  GLN B  16  HIS B  18                    
SITE     2 AH1 45 ASN B  44  GLY B  45  ALA B  46  THR B  47                    
SITE     3 AH1 45 THR B  92  PRO B  93  HIS B  94  HOH B 302                    
SITE     4 AH1 45 HOH B 313  HOH B 321  HOH B 322  HOH B 326                    
SITE     5 AH1 45 HOH B 334  HOH B 339  HOH B 340  HOH B 371                    
SITE     6 AH1 45 HOH B 382  HOH B 400  HOH B 414  GLN C  16                    
SITE     7 AH1 45 HIS C  18  THR C  19  ASN C  44  GLY C  45                    
SITE     8 AH1 45 ALA C  46  THR C  47  PHE C  48  LYS C  84                    
SITE     9 AH1 45 THR C  92  PRO C  93  HIS C  94  HOH C 302                    
SITE    10 AH1 45 HOH C 303  HOH C 310  HOH C 311  HOH C 324                    
SITE    11 AH1 45 HOH C 336  HOH C 368  HOH C 411  HOH C 415                    
SITE    12 AH1 45 HOH J1431                                                     
SITE     1 AH2 36 GLN B   3  GLN C   3  GLN C  16  HIS C  18                    
SITE     2 AH2 36 ASN C  44  GLY C  45  ALA C  46  THR C  47                    
SITE     3 AH2 36 PHE C  48  THR C  92  PRO C  93  HIS C  94                    
SITE     4 AH2 36 HOH C 302  HOH C 303  HOH C 310  HOH C 311                    
SITE     5 AH2 36 HOH C 324  HOH C 336  HOH C 368  HOH C 411                    
SITE     6 AH2 36 HOH C 415  ASN D  44  GLY D  45  ALA D  46                    
SITE     7 AH2 36 THR D  47  THR D  92  PRO D  93  HIS D  94                    
SITE     8 AH2 36 HOH D 304  HOH D 305  HOH D 315  THR E   6                    
SITE     9 AH2 36 LYS E  84  HOH E 326  HOH E 387  HOH E 436                    
SITE     1 AH3 31 GLN C   3  GLN D   3  ASN D  44  GLY D  45                    
SITE     2 AH3 31 ALA D  46  THR D  47  THR D  92  PRO D  93                    
SITE     3 AH3 31 HIS D  94  HOH D 304  HOH D 305  HOH D 315                    
SITE     4 AH3 31 THR E   6  GLN E  16  HIS E  18  ASN E  44                    
SITE     5 AH3 31 GLY E  45  ALA E  46  THR E  47  PHE E  48                    
SITE     6 AH3 31 LYS E  84  PRO E  93  HIS E  94  HOH E 320                    
SITE     7 AH3 31 HOH E 326  HOH E 344  HOH E 379  HOH E 387                    
SITE     8 AH3 31 HOH E 390  HOH E 407  HOH E 436                               
SITE     1 AH4 27 GLN D   3  GLN E  16  HIS E  18  ASN E  44                    
SITE     2 AH4 27 GLY E  45  ALA E  46  THR E  47  PHE E  48                    
SITE     3 AH4 27 PRO E  93  HIS E  94  HOH E 320  HOH E 344                    
SITE     4 AH4 27 HOH E 379  HOH E 390  HOH E 407  HIS F  18                    
SITE     5 AH4 27 ASN F  44  GLY F  45  ALA F  46  THR F  47                    
SITE     6 AH4 27 PRO F  93  HIS F  94  HOH F1316  HOH F1340                    
SITE     7 AH4 27 HOH F1380  HOH F1395  GLN J   3                               
SITE     1 AH5 32 ASN C  90  HOH C 387  GLN F   3  HIS F  18                    
SITE     2 AH5 32 ASN F  44  GLY F  45  ALA F  46  THR F  47                    
SITE     3 AH5 32 PRO F  93  HIS F  94  FUC F1206  HOH F1316                    
SITE     4 AH5 32 HOH F1395  GLN G  16  HIS G  18  ASN G  44                    
SITE     5 AH5 32 GLY G  45  ALA G  46  THR G  47  PRO G  93                    
SITE     6 AH5 32 HIS G  94  HOH G 302  HOH G 310  HOH G 316                    
SITE     7 AH5 32 HOH G 317  HOH G 321  HOH G 331  HOH G 355                    
SITE     8 AH5 32 HOH G 356  HOH G 361  HOH G 402  GLN J   3                    
SITE     1 AH6 36 ASN C  90  HOH C 387  ASN D  14  ASN D  90                    
SITE     2 AH6 36 HOH D 340  GLN F   3  GLN G   3  HIS G  18                    
SITE     3 AH6 36 ASN G  44  GLY G  45  ALA G  46  THR G  47                    
SITE     4 AH6 36 PRO G  93  HIS G  94  FUC G 207  HOH G 310                    
SITE     5 AH6 36 HOH G 316  HOH G 317  HOH G 331  HOH G 355                    
SITE     6 AH6 36 HOH G 356  HOH G 361  HOH G 402  GLN H  16                    
SITE     7 AH6 36 HIS H  18  ASN H  44  GLY H  45  ALA H  46                    
SITE     8 AH6 36 THR H  47  PHE H  48  PRO H  93  HIS H  94                    
SITE     9 AH6 36 HOH H1303  HOH H1321  HOH H1363  HOH H1384                    
SITE     1 AH7 45 ASN A  90  LYS A  91  THR A  92  HOH A 301                    
SITE     2 AH7 45 HOH A 437  ASN D  14  ASN D  90  HOH D 340                    
SITE     3 AH7 45 HOH E 394  GLN G   3  GLN H   3  GLN H  16                    
SITE     4 AH7 45 HIS H  18  ASN H  44  GLY H  45  ALA H  46                    
SITE     5 AH7 45 THR H  47  PHE H  48  PRO H  93  HIS H  94                    
SITE     6 AH7 45 HOH H1303  HOH H1321  HOH H1363  HOH H1384                    
SITE     7 AH7 45 HIS I  18  ASN I  44  GLY I  45  ALA I  46                    
SITE     8 AH7 45 THR I  47  PHE I  48  PRO I  93  HIS I  94                    
SITE     9 AH7 45 HOH I1304  HOH I1323  HOH I1326  HOH I1330                    
SITE    10 AH7 45 HOH I1331  HOH I1332  HOH I1351  HOH I1353                    
SITE    11 AH7 45 HOH I1355  HOH I1392  HOH I1402  HOH I1409                    
SITE    12 AH7 45 HOH I1415                                                     
SITE     1 AH8 58 ASN A  90  LYS A  91  THR A  92  HOH A 301                    
SITE     2 AH8 58 HOH A 348  HOH A 416  HOH A 437  ASN B  90                    
SITE     3 AH8 58 LYS B  91  THR B  92  HOH B 301  HOH E 394                    
SITE     4 AH8 58 GLN H   3  GLN I   3  HIS I  18  ASN I  44                    
SITE     5 AH8 58 GLY I  45  ALA I  46  THR I  47  PHE I  48                    
SITE     6 AH8 58 PRO I  93  HIS I  94  NAG I1204  HOH I1304                    
SITE     7 AH8 58 HOH I1323  HOH I1326  HOH I1330  HOH I1331                    
SITE     8 AH8 58 HOH I1332  HOH I1351  HOH I1353  HOH I1355                    
SITE     9 AH8 58 HOH I1392  HOH I1402  HOH I1409  HOH I1415                    
SITE    10 AH8 58 GLN J  16  HIS J  18  ASN J  44  GLY J  45                    
SITE    11 AH8 58 ALA J  46  THR J  47  PHE J  48  PRO J  93                    
SITE    12 AH8 58 HIS J  94  NAG J1204  HOH J1305  HOH J1306                    
SITE    13 AH8 58 HOH J1307  HOH J1309  HOH J1311  HOH J1322                    
SITE    14 AH8 58 HOH J1340  HOH J1358  HOH J1385  HOH J1391                    
SITE    15 AH8 58 HOH J1396  HOH J1398                                          
CRYST1   72.333   98.984  152.019  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      0.013825  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010103  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006578        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system