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Database: PDB
Entry: 5ELF
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Original site: 5ELF 
HEADER    TOXIN                                   04-NOV-15   5ELF              
TITLE     CHOLERA TOXIN EL TOR B-PENTAMER IN COMPLEX WITH A-PENTASACCHARIDE     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA ENTEROTOXIN SUBUNIT B;                             
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J;                                 
COMPND   4 SYNONYM: CHOLERA ENTEROTOXIN B CHAIN,CHOLERA ENTEROTOXIN GAMMA CHAIN,
COMPND   5 CHOLERAGENOID;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE SEROTYPE O1 (STRAIN ATCC 39315  
SOURCE   3 / EL TOR INABA N16961);                                              
SOURCE   4 ORGANISM_TAXID: 243277;                                              
SOURCE   5 STRAIN: ATCC 39315 / EL TOR INABA N16961;                            
SOURCE   6 GENE: CTXB, TOXB, VC_1456;                                           
SOURCE   7 EXPRESSION_SYSTEM: VIBRIO;                                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 662;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SP. 60                                     
KEYWDS    CHOLERA TOXIN B-PENTAMER, HUMAN MILK OLIGOSACCHARIDE, COMPLEX, BLOOD  
KEYWDS   2 GROUP OLIGOSACCHARIDE/ANTIGEN, TOXIN                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.HEGGELUND,D.BURSCHOWSKY,U.KRENGEL                                 
REVDAT   2   27-APR-16 5ELF    1       JRNL                                     
REVDAT   1   30-MAR-16 5ELF    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.    1.55 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) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 145899                         
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7664                            
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) : 1.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10549                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 530                          
REMARK   3   BIN FREE R VALUE                    : 0.3610                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8170                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 578                                     
REMARK   3   SOLVENT ATOMS            : 1194                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.25000                                             
REMARK   3    B22 (A**2) : 2.12000                                              
REMARK   3    B33 (A**2) : -0.88000                                             
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): 0.088         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.092         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.089         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.761         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9171 ; 0.017 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  8775 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12470 ; 1.902 ; 2.029       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20418 ; 1.231 ; 3.035       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1048 ; 7.154 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   373 ;40.446 ;25.416       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1586 ;12.505 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;26.310 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1585 ; 0.153 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9515 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1873 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4147 ; 1.479 ; 1.799       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4146 ; 1.476 ; 1.798       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5177 ; 2.178 ; 2.684       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  5178 ; 2.179 ; 2.685       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5024 ; 2.054 ; 2.103       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  5024 ; 2.052 ; 2.103       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  7283 ; 3.130 ; 3.071       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 11232 ; 5.641 ;16.584       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 11233 ; 5.642 ;16.586       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5ELF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-NOV-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214994.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-OCT-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
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   : 153547                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.920                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 3CHB                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINE-TRIS, 9% PEG1000, 9%        
REMARK 280  PEG3350, 9% MPD, 0.03 M CALCIUM CHLORIDE, 0.03 M MAGNESIUM          
REMARK 280  CHLORIDE. MICROSEEDING., PH 8.5, VAPOR DIFFUSION, SITTING 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       31.81300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       97.84000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.36000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       97.84000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.81300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.36000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G, H, I, J                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NZ   LYS C    23     O    HOH C   301              2.10            
REMARK 500   O6   A2G G   203     O    HOH G   301              2.14            
REMARK 500   NE2  HIS D    13     O    HOH D   302              2.18            
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 A  83      -70.51    -78.66                                   
REMARK 500    PRO A  93      157.34    -48.02                                   
REMARK 500    LYS B  34       -6.66     72.86                                   
REMARK 500    GLU B  83      -71.76    -78.59                                   
REMARK 500    LYS C  34       -0.81     73.27                                   
REMARK 500    LYS C  34       -0.36     72.80                                   
REMARK 500    ASN C  44        0.72    -68.58                                   
REMARK 500    GLU C  83      -70.12    -83.15                                   
REMARK 500    LYS D  34       -0.72     76.15                                   
REMARK 500    GLU D  83      -71.48    -81.77                                   
REMARK 500    LYS F  34       -0.06     76.22                                   
REMARK 500    GLU F  83      -72.84    -77.39                                   
REMARK 500    ASN G  21       53.30     39.51                                   
REMARK 500    GLU J  83      -70.92    -80.81                                   
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 A 406        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH C 411        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH E 426        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH I 427        DISTANCE =  5.85 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  52.5                                              
REMARK 620 3 GLU F  79   OE2 121.2  69.4                                        
REMARK 620 4 BCN A 202   O22  77.1 127.8 161.1                                  
REMARK 620 5 BCN A 202   O4   79.3  81.6  85.2 103.8                            
REMARK 620 6 BCN A 202   O6  153.9 136.7  77.4  83.8 123.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  79   OE2                                                    
REMARK 620 2 GLU F  79   OE1 118.4                                              
REMARK 620 3 GLU F  79   OE2  69.4  51.1                                        
REMARK 620 4 BCN A 204   O6   81.1  79.9  85.3                                  
REMARK 620 5 BCN A 204   O4   78.8 156.8 135.6 120.1                            
REMARK 620 6 BCN A 204   O21 163.0  78.5 127.4 101.4  85.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  79   OE1                                                    
REMARK 620 2 GLU B  79   OE2  51.3                                              
REMARK 620 3 GLU J  79   OE2 119.4  68.6                                        
REMARK 620 4 BCN B 204   O22  77.0 126.5 162.6                                  
REMARK 620 5 BCN B 204   O6  153.3 142.0  81.7  80.9                            
REMARK 620 6 HOH I 327   O    86.9  80.3  89.9  85.1  76.3                      
REMARK 620 7 BCN B 204   O4   78.3  79.0  84.8 105.5 122.5 159.2                
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 J  79   OE1 121.5                                              
REMARK 620 3 GLU J  79   OE2  69.0  52.5                                        
REMARK 620 4 BCN B 201   O21 159.4  77.4 129.0                                  
REMARK 620 5 BCN B 201   O4   78.9 154.1 143.2  80.7                            
REMARK 620 6 BCN B 201   O6   88.8  78.8  77.5 104.0 120.3                      
REMARK 620 7 HOH J 367   O    85.0  91.9  86.5  86.4  72.8 164.0                
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  51.6                                              
REMARK 620 3 GLU I  79   OE2 117.6  66.8                                        
REMARK 620 4 BCN C 203   O22  78.1 127.9 164.0                                  
REMARK 620 5 BCN C 203   O6  155.0 137.9  80.7  83.4                            
REMARK 620 6 HOH C 345   O    85.0  80.7  95.0  82.8  76.1                      
REMARK 620 7 BCN C 203   O4   80.3  81.3  82.2 104.8 121.1 161.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  79   OE2                                                    
REMARK 620 2 GLU I  79   OE1 123.5                                              
REMARK 620 3 GLU I  79   OE2  72.7  51.7                                        
REMARK 620 4 BCN C 202   O21 165.7  70.8 121.0                                  
REMARK 620 5 BCN C 202   O4   82.7  79.2  80.2 102.9                            
REMARK 620 6 BCN C 202   O6   81.2 151.5 143.6  84.7 121.6                      
REMARK 620 7 HOH B 341   O    96.7  83.9  79.7  82.7 159.1  78.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D  79   OE1                                                    
REMARK 620 2 GLU D  79   OE2  52.0                                              
REMARK 620 3 GLU H  79   OE2 120.3  69.0                                        
REMARK 620 4 BCN D 203   O6  155.7 138.4  78.1                                  
REMARK 620 5 BCN D 203   O4   79.8  80.7  83.0 120.5                            
REMARK 620 6 HOH C 370   O    87.2  78.3  89.5  76.6 159.0                      
REMARK 620 7 BCN D 203   O22  78.5 128.2 160.5  82.4 107.1  86.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D  79   OE2                                                    
REMARK 620 2 GLU H  79   OE1 117.6                                              
REMARK 620 3 GLU H  79   OE2  68.0  50.5                                        
REMARK 620 4 BCN D 202   O21 164.5  77.6 126.2                                  
REMARK 620 5 BCN D 202   O4   80.8  82.3  83.0 105.8                            
REMARK 620 6 BCN D 202   O6   79.7 152.3 134.3  85.1 123.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E  79   OE1                                                    
REMARK 620 2 GLU E  79   OE2  52.1                                              
REMARK 620 3 GLU G  79   OE2 120.4  68.9                                        
REMARK 620 4 BCN E 203   O4  152.9 137.9  79.3                                  
REMARK 620 5 BCN E 203   O21  77.9 128.7 161.5  82.6                            
REMARK 620 6 BCN E 203   O6   78.9  80.5  84.5 124.1 102.8                      
REMARK 620 7 HOH E 303   O    83.1  85.1 101.2  74.3  77.3 161.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E  79   OE2                                                    
REMARK 620 2 GLU G  79   OE1 117.0                                              
REMARK 620 3 GLU G  79   OE2  66.8  50.8                                        
REMARK 620 4 BCN E 201   O21 165.7  77.2 126.9                                  
REMARK 620 5 BCN E 201   O4   81.3 154.5 138.7  84.6                            
REMARK 620 6 BCN E 201   O6   74.2  81.3  74.3 111.8 122.5                      
REMARK 620 7 HOH G 304   O    99.2  83.4  83.8  79.8  75.8 158.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FUC B 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN B 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 205                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN C 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN D 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN D 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GLC D 210                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN E 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 F 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BGC G 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FUC H 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GLC A    
REMARK 800  205 through FUC A 209                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues BGC D    
REMARK 800  205 through FUC D 209                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GLC E    
REMARK 800  205 through FUC E 209                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues BGC F    
REMARK 800  202 through FUC F 206                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL G    
REMARK 800  202 through GLC G 206                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GLC I    
REMARK 800  201 through FUC I 205                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GLC J    
REMARK 800  201 through FUC J 205                                               
DBREF  5ELF A    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELF B    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELF C    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELF D    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELF E    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELF F    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELF G    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELF H    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELF I    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5ELF J    1   103  UNP    P01556   CHTB_VIBCH      22    124             
SEQRES   1 A  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 A  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 A  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 A  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 A  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 A  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 A  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 A  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 B  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 B  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 B  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 B  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 B  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 B  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 B  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 B  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 C  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 C  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 C  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 C  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 C  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 C  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 C  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 C  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 D  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 D  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 D  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 D  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 D  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 D  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 D  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 D  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 E  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 E  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 E  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 E  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 E  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 E  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 E  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 E  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 F  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 F  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 F  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 F  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 F  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 F  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 F  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 F  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 G  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 G  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 G  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 G  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 G  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 G  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 G  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 G  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 H  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 H  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 H  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 H  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 H  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 H  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 H  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 H  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 I  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 I  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 I  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 I  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 I  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 I  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 I  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 I  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 J  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 J  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 J  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 J  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 J  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 J  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 J  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 J  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
HET     CA  A 201       1                                                       
HET    BCN  A 202      11                                                       
HET     CA  A 203       1                                                       
HET    BCN  A 204      11                                                       
HET    GLC  A 205      12                                                       
HET    GAL  A 206      11                                                       
HET    A2G  A 207      14                                                       
HET    FUC  A 208      10                                                       
HET    FUC  A 209      10                                                       
HET    BCN  B 201      11                                                       
HET     CA  B 202       1                                                       
HET    FUC  B 203      11                                                       
HET    BCN  B 204      11                                                       
HET     CA  B 205       1                                                       
HET     CA  C 201       1                                                       
HET    BCN  C 202      11                                                       
HET    BCN  C 203      11                                                       
HET     CA  C 204       1                                                       
HET     CA  D 201       1                                                       
HET    BCN  D 202      11                                                       
HET    BCN  D 203      11                                                       
HET     CA  D 204       1                                                       
HET    BGC  D 205      12                                                       
HET    GAL  D 206      22                                                       
HET    A2G  D 207      28                                                       
HET    FUC  D 208      20                                                       
HET    FUC  D 209      20                                                       
HET    GLC  D 210      12                                                       
HET    BCN  E 201      11                                                       
HET     CA  E 202       1                                                       
HET    BCN  E 203      11                                                       
HET     CA  E 204       1                                                       
HET    GLC  E 205      12                                                       
HET    GAL  E 206      11                                                       
HET    A2G  E 207      14                                                       
HET    FUC  E 208      10                                                       
HET    FUC  E 209      10                                                       
HET    PG4  F 201      13                                                       
HET    BGC  F 202      12                                                       
HET    GAL  F 203      11                                                       
HET    A2G  F 204      14                                                       
HET    FUC  F 205      10                                                       
HET    FUC  F 206      10                                                       
HET    BGC  G 201      12                                                       
HET    GAL  G 202      22                                                       
HET    A2G  G 203      28                                                       
HET    FUC  G 204      20                                                       
HET    FUC  G 205      20                                                       
HET    GLC  G 206      12                                                       
HET    FUC  H 201      11                                                       
HET    GLC  I 201      12                                                       
HET    GAL  I 202      11                                                       
HET    A2G  I 203      14                                                       
HET    FUC  I 204      10                                                       
HET    FUC  I 205      10                                                       
HET    GLC  J 201      24                                                       
HET    GAL  J 202      22                                                       
HET    A2G  J 203      28                                                       
HET    FUC  J 204      20                                                       
HET    FUC  J 205      20                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     BCN BICINE                                                           
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETNAM     A2G N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE                               
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
FORMUL  11   CA    10(CA 2+)                                                    
FORMUL  12  BCN    10(C6 H13 N O4)                                              
FORMUL  15  GLC    6(C6 H12 O6)                                                 
FORMUL  15  GAL    7(C6 H12 O6)                                                 
FORMUL  15  A2G    7(C8 H15 N O6)                                               
FORMUL  15  FUC    16(C6 H12 O5)                                                
FORMUL  29  BGC    3(C6 H12 O6)                                                 
FORMUL  35  PG4    C8 H18 O5                                                    
FORMUL  41  HOH   *1194(H2 O)                                                   
HELIX    1 AA1 ASN A    4  GLU A   11  1                                   8    
HELIX    2 AA2 SER A   60  THR A   78  1                                  19    
HELIX    3 AA3 ASN B    4  GLU B   11  1                                   8    
HELIX    4 AA4 SER B   60  THR B   78  1                                  19    
HELIX    5 AA5 ASN C    4  GLU C   11  1                                   8    
HELIX    6 AA6 ILE C   58  GLU C   79  1                                  22    
HELIX    7 AA7 ASN D    4  ALA D   10  1                                   7    
HELIX    8 AA8 ILE D   58  THR D   78  1                                  21    
HELIX    9 AA9 ASN E    4  GLU E   11  1                                   8    
HELIX   10 AB1 ILE E   58  SER E   60  5                                   3    
HELIX   11 AB2 GLN E   61  THR E   78  1                                  18    
HELIX   12 AB3 ASN F    4  GLU F   11  1                                   8    
HELIX   13 AB4 SER F   60  GLU F   79  1                                  20    
HELIX   14 AB5 ASN G    4  ALA G   10  1                                   7    
HELIX   15 AB6 ILE G   58  THR G   78  1                                  21    
HELIX   16 AB7 ASN H    4  ALA H   10  1                                   7    
HELIX   17 AB8 SER H   60  THR H   78  1                                  19    
HELIX   18 AB9 ASN I    4  ALA I   10  1                                   7    
HELIX   19 AC1 SER I   60  THR I   78  1                                  19    
HELIX   20 AC2 ASN J    4  ALA J   10  1                                   7    
HELIX   21 AC3 SER J   60  THR J   78  1                                  19    
SHEET    1   A 3 THR A  15  THR A  19  0                                        
SHEET    2   A 3 VAL A  82  TRP A  88 -1                                        
SHEET    3   A 3 ALA A  98  MET A 101 -1                                        
SHEET    1   B 3 SER A  26  SER A  30  0                                        
SHEET    2   B 3 MET A  37  THR A  41 -1                                        
SHEET    3   B 3 ILE A  47  VAL A  50 -1                                        
SHEET    1   C 3 THR B  15  THR B  19  0                                        
SHEET    2   C 3 VAL B  82  TRP B  88 -1                                        
SHEET    3   C 3 ALA B  98  MET B 101 -1                                        
SHEET    1   D 3 SER B  26  SER B  30  0                                        
SHEET    2   D 3 MET B  37  THR B  41 -1                                        
SHEET    3   D 3 ILE B  47  VAL B  50 -1                                        
SHEET    1   E 3 THR C  15  THR C  19  0                                        
SHEET    2   E 3 VAL C  82  TRP C  88 -1                                        
SHEET    3   E 3 ALA C  98  MET C 101 -1                                        
SHEET    1   F 3 SER C  26  SER C  30  0                                        
SHEET    2   F 3 MET C  37  THR C  41 -1                                        
SHEET    3   F 3 ILE C  47  VAL C  50 -1                                        
SHEET    1   G 3 THR D  15  THR D  19  0                                        
SHEET    2   G 3 VAL D  82  TRP D  88 -1                                        
SHEET    3   G 3 ALA D  98  MET D 101 -1                                        
SHEET    1   H 3 SER D  26  SER D  30  0                                        
SHEET    2   H 3 MET D  37  THR D  41 -1                                        
SHEET    3   H 3 ILE D  47  VAL D  50 -1                                        
SHEET    1   I 3 THR E  15  THR E  19  0                                        
SHEET    2   I 3 VAL E  82  TRP E  88 -1                                        
SHEET    3   I 3 ALA E  98  MET E 101 -1                                        
SHEET    1   J 3 SER E  26  SER E  30  0                                        
SHEET    2   J 3 MET E  37  THR E  41 -1                                        
SHEET    3   J 3 ILE E  47  VAL E  50 -1                                        
SHEET    1   K 3 THR F  15  THR F  19  0                                        
SHEET    2   K 3 VAL F  82  TRP F  88 -1                                        
SHEET    3   K 3 ALA F  98  MET F 101 -1                                        
SHEET    1   L 3 SER F  26  SER F  30  0                                        
SHEET    2   L 3 MET F  37  THR F  41 -1                                        
SHEET    3   L 3 ILE F  47  VAL F  50 -1                                        
SHEET    1   M 3 THR G  15  THR G  19  0                                        
SHEET    2   M 3 VAL G  82  TRP G  88 -1                                        
SHEET    3   M 3 ALA G  98  MET G 101 -1                                        
SHEET    1   N 3 SER G  26  SER G  30  0                                        
SHEET    2   N 3 MET G  37  THR G  41 -1                                        
SHEET    3   N 3 ILE G  47  VAL G  50 -1                                        
SHEET    1   O 3 THR H  15  THR H  19  0                                        
SHEET    2   O 3 VAL H  82  TRP H  88 -1                                        
SHEET    3   O 3 ALA H  98  MET H 101 -1                                        
SHEET    1   P 3 SER H  26  SER H  30  0                                        
SHEET    2   P 3 MET H  37  THR H  41 -1                                        
SHEET    3   P 3 ILE H  47  VAL H  50 -1                                        
SHEET    1   Q 3 THR I  15  THR I  19  0                                        
SHEET    2   Q 3 VAL I  82  TRP I  88 -1                                        
SHEET    3   Q 3 ALA I  98  MET I 101 -1                                        
SHEET    1   R 3 SER I  26  SER I  30  0                                        
SHEET    2   R 3 MET I  37  THR I  41 -1                                        
SHEET    3   R 3 ILE I  47  VAL I  50 -1                                        
SHEET    1   S 3 THR J  15  THR J  19  0                                        
SHEET    2   S 3 VAL J  82  TRP J  88 -1                                        
SHEET    3   S 3 ALA J  98  MET J 101 -1                                        
SHEET    1   T 3 SER J  26  SER J  30  0                                        
SHEET    2   T 3 MET J  37  THR J  41 -1                                        
SHEET    3   T 3 ILE J  47  VAL J  50 -1                                        
SSBOND   1 CYS A    9    CYS A   86                          1555   1555  2.14  
SSBOND   2 CYS B    9    CYS B   86                          1555   1555  2.04  
SSBOND   3 CYS C    9    CYS C   86                          1555   1555  2.08  
SSBOND   4 CYS D    9    CYS D   86                          1555   1555  2.12  
SSBOND   5 CYS E    9    CYS E   86                          1555   1555  2.11  
SSBOND   6 CYS F    9    CYS F   86                          1555   1555  2.08  
SSBOND   7 CYS G    9    CYS G   86                          1555   1555  2.12  
SSBOND   8 CYS H    9    CYS H   86                          1555   1555  2.10  
SSBOND   9 CYS I    9    CYS I   86                          1555   1555  2.10  
SSBOND  10 CYS J    9    CYS J   86                          1555   1555  2.10  
LINK         OE1 GLU A  79                CA    CA A 201     1555   1555  2.31  
LINK         OE2 GLU A  79                CA    CA A 201     1555   1555  2.55  
LINK         OE2 GLU A  79                CA    CA A 203     1555   1555  2.29  
LINK         OE1 GLU B  79                CA    CA B 202     1555   1555  2.42  
LINK         OE2 GLU B  79                CA    CA B 202     1555   1555  2.56  
LINK         OE2 GLU B  79                CA    CA B 205     1555   1555  2.31  
LINK         OE1 GLU C  79                CA    CA C 201     1555   1555  2.42  
LINK         OE2 GLU C  79                CA    CA C 201     1555   1555  2.62  
LINK         OE2 GLU C  79                CA    CA C 204     1555   1555  2.26  
LINK         OE1 GLU D  79                CA    CA D 201     1555   1555  2.51  
LINK         OE2 GLU D  79                CA    CA D 201     1555   1555  2.54  
LINK         OE2 GLU D  79                CA    CA D 204     1555   1555  2.31  
LINK         OE1 GLU E  79                CA    CA E 202     1555   1555  2.43  
LINK         OE2 GLU E  79                CA    CA E 204     1555   1555  2.38  
LINK         OE2 GLU E  79                CA    CA E 202     1555   1555  2.49  
LINK         OE1 GLU F  79                CA    CA A 203     1555   1555  2.43  
LINK         OE2 GLU F  79                CA    CA A 201     1555   1555  2.35  
LINK         OE2 GLU F  79                CA    CA A 203     1555   1555  2.59  
LINK         OE1 GLU G  79                CA    CA E 204     1555   1555  2.44  
LINK         OE2 GLU G  79                CA    CA E 204     1555   1555  2.57  
LINK         OE2 GLU G  79                CA    CA E 202     1555   1555  2.33  
LINK         OE1 GLU H  79                CA    CA D 204     1555   1555  2.45  
LINK         OE2 GLU H  79                CA    CA D 201     1555   1555  2.32  
LINK         OE2 GLU H  79                CA    CA D 204     1555   1555  2.60  
LINK         OE1 GLU I  79                CA    CA C 204     1555   1555  2.48  
LINK         OE2 GLU I  79                CA    CA C 201     1555   1555  2.50  
LINK         OE2 GLU I  79                CA    CA C 204     1555   1555  2.50  
LINK         OE1 GLU J  79                CA    CA B 205     1555   1555  2.34  
LINK         OE2 GLU J  79                CA    CA B 202     1555   1555  2.29  
LINK         OE2 GLU J  79                CA    CA B 205     1555   1555  2.52  
LINK        CA    CA A 201                 O22 BCN A 202     1555   1555  2.39  
LINK        CA    CA A 201                 O4  BCN A 202     1555   1555  2.09  
LINK        CA    CA A 201                 O6  BCN A 202     1555   1555  2.16  
LINK        CA    CA A 203                 O6  BCN A 204     1555   1555  2.24  
LINK        CA    CA A 203                 O4  BCN A 204     1555   1555  2.53  
LINK        CA    CA A 203                 O21 BCN A 204     1555   1555  2.38  
LINK         O3  GLC A 205                 C1  FUC A 209     1555   1555  1.41  
LINK         O4  GLC A 205                 C1  GAL A 206     1555   1555  1.45  
LINK         O2  GAL A 206                 C1  FUC A 208     1555   1555  1.45  
LINK         O3  GAL A 206                 C1  A2G A 207     1555   1555  1.46  
LINK         O21 BCN B 201                CA    CA B 205     1555   1555  2.37  
LINK         O4  BCN B 201                CA    CA B 205     1555   1555  2.35  
LINK         O6  BCN B 201                CA    CA B 205     1555   1555  2.15  
LINK        CA    CA B 202                 O22 BCN B 204     1555   1555  2.35  
LINK        CA    CA B 202                 O6  BCN B 204     1555   1555  2.34  
LINK        CA    CA B 202                 O   HOH I 327     1555   1555  2.40  
LINK        CA    CA B 202                 O4  BCN B 204     1555   1555  2.30  
LINK        CA    CA B 205                 O   HOH J 367     1555   1555  2.57  
LINK        CA    CA C 201                 O22 BCN C 203     1555   1555  2.33  
LINK        CA    CA C 201                 O6  BCN C 203     1555   1555  2.33  
LINK        CA    CA C 201                 O   HOH C 345     1555   1555  2.35  
LINK        CA    CA C 201                 O4  BCN C 203     1555   1555  2.05  
LINK         O21 BCN C 202                CA    CA C 204     1555   1555  2.39  
LINK         O4  BCN C 202                CA    CA C 204     1555   1555  2.13  
LINK         O6  BCN C 202                CA    CA C 204     1555   1555  2.37  
LINK        CA    CA C 204                 O   HOH B 341     1555   1555  2.37  
LINK        CA    CA D 201                 O6  BCN D 203     1555   1555  2.48  
LINK        CA    CA D 201                 O4  BCN D 203     1555   1555  2.23  
LINK        CA    CA D 201                 O   HOH C 370     1555   1555  2.36  
LINK        CA    CA D 201                 O22 BCN D 203     1555   1555  2.42  
LINK         O21 BCN D 202                CA    CA D 204     1555   1555  2.34  
LINK         O4  BCN D 202                CA    CA D 204     1555   1555  2.28  
LINK         O6  BCN D 202                CA    CA D 204     1555   1555  2.38  
LINK         O3 ABGC D 205                 C1 AFUC D 209     1555   1555  1.43  
LINK         O4 ABGC D 205                 C1 AGAL D 206     1555   1555  1.43  
LINK         C1 BGAL D 206                 O4 BGLC D 210     1555   1555  1.38  
LINK         O2 AGAL D 206                 C1 AFUC D 208     1555   1555  1.41  
LINK         O2 BGAL D 206                 C1 BFUC D 208     1555   1555  1.43  
LINK         O3 AGAL D 206                 C1 AA2G D 207     1555   1555  1.43  
LINK         O3 BGAL D 206                 C1 BA2G D 207     1555   1555  1.44  
LINK         C1 BFUC D 209                 O3 BGLC D 210     1555   1555  1.43  
LINK         O21 BCN E 201                CA    CA E 204     1555   1555  2.30  
LINK         O4  BCN E 201                CA    CA E 204     1555   1555  2.52  
LINK         O6  BCN E 201                CA    CA E 204     1555   1555  1.93  
LINK        CA    CA E 202                 O4  BCN E 203     1555   1555  2.33  
LINK        CA    CA E 202                 O21 BCN E 203     1555   1555  2.31  
LINK        CA    CA E 202                 O6  BCN E 203     1555   1555  2.39  
LINK        CA    CA E 202                 O   HOH E 303     1555   1555  2.32  
LINK        CA    CA E 204                 O   HOH G 304     1555   1555  2.36  
LINK         O3  GLC E 205                 C1  FUC E 209     1555   1555  1.40  
LINK         O4  GLC E 205                 C1  GAL E 206     1555   1555  1.44  
LINK         O2  GAL E 206                 C1  FUC E 208     1555   1555  1.46  
LINK         O3  GAL E 206                 C1  A2G E 207     1555   1555  1.46  
LINK         O3  BGC F 202                 C1  FUC F 206     1555   1555  1.46  
LINK         O4  BGC F 202                 C1  GAL F 203     1555   1555  1.43  
LINK         O2  GAL F 203                 C1  FUC F 205     1555   1555  1.46  
LINK         O3  GAL F 203                 C1  A2G F 204     1555   1555  1.48  
LINK         O3 BBGC G 201                 C1 BFUC G 205     1555   1555  1.43  
LINK         O4 BBGC G 201                 C1 BGAL G 202     1555   1555  1.39  
LINK         C1 AGAL G 202                 O4 AGLC G 206     1555   1555  1.41  
LINK         O2 AGAL G 202                 C1 AFUC G 204     1555   1555  1.46  
LINK         O2 BGAL G 202                 C1 BFUC G 204     1555   1555  1.43  
LINK         O3 AGAL G 202                 C1 AA2G G 203     1555   1555  1.50  
LINK         O3 BGAL G 202                 C1 BA2G G 203     1555   1555  1.45  
LINK         C1 AFUC G 205                 O3 AGLC G 206     1555   1555  1.46  
LINK         O3  GLC I 201                 C1  FUC I 205     1555   1555  1.45  
LINK         O4  GLC I 201                 C1  GAL I 202     1555   1555  1.39  
LINK         O2  GAL I 202                 C1  FUC I 204     1555   1555  1.43  
LINK         O3  GAL I 202                 C1  A2G I 203     1555   1555  1.46  
LINK         O3 AGLC J 201                 C1 AFUC J 205     1555   1555  1.43  
LINK         O3 BGLC J 201                 C1 BFUC J 205     1555   1555  1.50  
LINK         O4 AGLC J 201                 C1 AGAL J 202     1555   1555  1.45  
LINK         O4 BGLC J 201                 C1 BGAL J 202     1555   1555  1.41  
LINK         O2 AGAL J 202                 C1 AFUC J 204     1555   1555  1.46  
LINK         O2 BGAL J 202                 C1 BFUC J 204     1555   1555  1.47  
LINK         O3 AGAL J 202                 C1 AA2G J 203     1555   1555  1.47  
LINK         O3 BGAL J 202                 C1 BA2G J 203     1555   1555  1.46  
CISPEP   1 THR A   92    PRO A   93          0       -20.22                     
CISPEP   2 THR B   92    PRO B   93          0       -17.65                     
CISPEP   3 THR C   92    PRO C   93          0       -14.11                     
CISPEP   4 THR D   92    PRO D   93          0       -11.48                     
CISPEP   5 THR E   92    PRO E   93          0        -4.62                     
CISPEP   6 THR F   92    PRO F   93          0       -10.48                     
CISPEP   7 THR G   92    PRO G   93          0       -12.79                     
CISPEP   8 THR H   92    PRO H   93          0       -13.39                     
CISPEP   9 THR I   92    PRO I   93          0       -13.39                     
CISPEP  10 THR J   92    PRO J   93          0        -7.03                     
SITE     1 AC1  4 GLU A  79  BCN A 202  GLU F  79  ASN J 103                    
SITE     1 AC2 11 GLU A  79   CA A 201  HOH A 321  HOH A 342                    
SITE     2 AC2 11 TYR F  76  LEU F  77  GLU F  79  HOH F 324                    
SITE     3 AC2 11 ALA J  80  LYS J  81  ASN J 103                               
SITE     1 AC3  4 GLU A  79  BCN A 204  ASN E 103  GLU F  79                    
SITE     1 AC4 14 TYR A  76  LEU A  77  GLU A  79   CA A 203                    
SITE     2 AC4 14 HOH A 311  HOH A 321  HOH A 329  HOH A 363                    
SITE     3 AC4 14 HOH A 367  ALA E  80  LYS E  81  ASN E 103                    
SITE     4 AC4 14 LYS F  23  GLU F  79                                          
SITE     1 AC5 12 ALA A  80  LYS A  81  ASN A 103  TYR B  76                    
SITE     2 AC5 12 LEU B  77  GLU B  79   CA B 205  HOH B 303                    
SITE     3 AC5 12 HOH B 305  HOH B 372  GLU J  79  HOH J 367                    
SITE     1 AC6  4 GLU B  79  BCN B 204  HOH I 327  GLU J  79                    
SITE     1 AC7  8 GLN A   3  TYR B  18  ILE B  47  PHE B  48                    
SITE     2 AC7  8 PRO B  93  HIS B  94  HOH B 308  HOH B 352                    
SITE     1 AC8 13 GLU B  79   CA B 202  HOH B 322  HOH B 365                    
SITE     2 AC8 13 HOH B 372  ALA I  80  LYS I  81  ASN I 103                    
SITE     3 AC8 13 HOH I 327  TYR J  76  LEU J  77  GLU J  79                    
SITE     4 AC8 13 HOH J 319                                                     
SITE     1 AC9  4 GLU B  79  BCN B 201  GLU J  79  HOH J 367                    
SITE     1 AD1  4 GLU C  79  BCN C 203  HOH C 345  GLU I  79                    
SITE     1 AD2 14 ALA B  80  LYS B  81  ASN B 103  HOH B 317                    
SITE     2 AD2 14 HOH B 341  LYS C  23  TYR C  76  LEU C  77                    
SITE     3 AD2 14 GLU C  79   CA C 204  HOH C 301  HOH C 304                    
SITE     4 AD2 14 HOH C 311  GLU I  79                                          
SITE     1 AD3 12 GLU C  79   CA C 201  HOH C 304  HOH C 313                    
SITE     2 AD3 12 HOH C 345  ALA H  80  LYS H  81  ASN H 103                    
SITE     3 AD3 12 TYR I  76  LEU I  77  GLU I  79  HOH I 317                    
SITE     1 AD4  4 HOH B 341  GLU C  79  BCN C 202  GLU I  79                    
SITE     1 AD5  4 HOH C 370  GLU D  79  BCN D 203  GLU H  79                    
SITE     1 AD6 12 ALA C  80  LYS C  81  ASN C 103  HOH C 364                    
SITE     2 AD6 12 TYR D  76  LEU D  77  GLU D  79   CA D 204                    
SITE     3 AD6 12 HOH D 317  HOH D 341  LYS H  23  GLU H  79                    
SITE     1 AD7 11 HOH C 370  LYS D  23  GLU D  79   CA D 201                    
SITE     2 AD7 11 ALA G  80  LYS G  81  ASN G 103  TYR H  76                    
SITE     3 AD7 11 LEU H  77  GLU H  79  HOH H 328                               
SITE     1 AD8  4 ASN C 103  GLU D  79  BCN D 202  GLU H  79                    
SITE     1 AD9  8 GLY D  45  BGC D 205  GAL D 206  FUC D 208                    
SITE     2 AD9  8 FUC D 209  HOH D 305  HOH D 323  HOH D 350                    
SITE     1 AE1 11 LYS D  81  ASN D 103  TYR E  76  LEU E  77                    
SITE     2 AE1 11 GLU E  79   CA E 204  HOH E 304  HOH E 310                    
SITE     3 AE1 11 LYS G  23  GLU G  79  HOH G 304                               
SITE     1 AE2  4 GLU E  79  BCN E 203  HOH E 303  GLU G  79                    
SITE     1 AE3 11 GLU E  79   CA E 202  HOH E 303  ALA F  80                    
SITE     2 AE3 11 LYS F  81  ASN F 103  TYR G  76  LEU G  77                    
SITE     3 AE3 11 GLU G  79  HOH G 312  HOH G 340                               
SITE     1 AE4  4 GLU E  79  BCN E 201  GLU G  79  HOH G 304                    
SITE     1 AE5  8 LYS F  34  HOH F 367  ALA H  10  GLU H  11                    
SITE     2 AE5  8 TYR H  12  HIS H  13  GLU J  11  TYR J  12                    
SITE     1 AE6 11 GLY G  45  GAL G 202  FUC G 204  FUC G 205                    
SITE     2 AE6 11 GLC G 206  HOH G 301  HOH G 303  HOH G 331                    
SITE     3 AE6 11 HOH G 386  HOH G 395  ASN J  90                               
SITE     1 AE7  8 GLN G   3  ILE H  47  PHE H  48  PRO H  93                    
SITE     2 AE7  8 HIS H  94  HOH H 302  HOH H 305  HOH H 349                    
SITE     1 AE8 13 GLN A  16  ILE A  17  TYR A  18  ASN A  44                    
SITE     2 AE8 13 GLY A  45  ALA A  46  ILE A  47  PHE A  48                    
SITE     3 AE8 13 PRO A  93  HIS A  94  HOH A 366  GLN E   3                    
SITE     4 AE8 13 FUC E 208                                                     
SITE     1 AE9 46 GLN A  16  ILE A  17  TYR A  18  ASN A  44                    
SITE     2 AE9 46 GLY A  45  ALA A  46  ILE A  47  PHE A  48                    
SITE     3 AE9 46 PRO A  93  HIS A  94  HOH A 366  GLN C   3                    
SITE     4 AE9 46 GLN D  16  ILE D  17  TYR D  18  ASN D  44                    
SITE     5 AE9 46 GLY D  45  ALA D  46  ILE D  47  PHE D  48                    
SITE     6 AE9 46 PRO D  93  HIS D  94  GLC D 210  HOH D 301                    
SITE     7 AE9 46 HOH D 304  HOH D 305  HOH D 306  HOH D 308                    
SITE     8 AE9 46 HOH D 313  HOH D 315  HOH D 320  HOH D 321                    
SITE     9 AE9 46 HOH D 322  HOH D 333  HOH D 337  HOH D 350                    
SITE    10 AE9 46 HOH D 357  HOH D 366  HOH D 386  GLN E   3                    
SITE    11 AE9 46 FUC E 208  THR I   6  ASN I  21  GLU I  83                    
SITE    12 AE9 46 LYS I  84  HOH I 301                                          
SITE     1 AF1 50 LYS A  43  ASN A  44  GLY A  45  GLC A 205                    
SITE     2 AF1 50 GLN C   3  GLN D   3  GLN D  16  ILE D  17                    
SITE     3 AF1 50 TYR D  18  ASN D  44  GLY D  45  ALA D  46                    
SITE     4 AF1 50 ILE D  47  PHE D  48  PRO D  93  HIS D  94                    
SITE     5 AF1 50 GLC D 210  HOH D 301  HOH D 304  HOH D 305                    
SITE     6 AF1 50 HOH D 306  HOH D 308  HOH D 313  HOH D 315                    
SITE     7 AF1 50 HOH D 320  HOH D 321  HOH D 322  HOH D 333                    
SITE     8 AF1 50 HOH D 337  HOH D 350  HOH D 357  HOH D 366                    
SITE     9 AF1 50 HOH D 386  GLN E  16  ILE E  17  TYR E  18                    
SITE    10 AF1 50 ASN E  44  GLY E  45  ALA E  46  ILE E  47                    
SITE    11 AF1 50 PHE E  48  PRO E  93  HIS E  94  HOH E 315                    
SITE    12 AF1 50 HOH E 375  THR I   6  ASN I  21  GLU I  83                    
SITE    13 AF1 50 LYS I  84  HOH I 301                                          
SITE     1 AF2 46 LYS A  43  ASN A  44  GLY A  45  GLC A 205                    
SITE     2 AF2 46 GLN E  16  ILE E  17  TYR E  18  ASN E  44                    
SITE     3 AF2 46 GLY E  45  ALA E  46  ILE E  47  GLU E  79                    
SITE     4 AF2 46 HIS E  94  BCN E 201  FUC E 209  HOH E 303                    
SITE     5 AF2 46 HOH E 315  HOH E 375  GLN F  16  ILE F  17                    
SITE     6 AF2 46 TYR F  18  ASN F  44  GLY F  45  ALA F  46                    
SITE     7 AF2 46 ILE F  47  PHE F  48  ALA F  80  LYS F  81                    
SITE     8 AF2 46 PRO F  93  HIS F  94  ASN F 103  HOH F 302                    
SITE     9 AF2 46 HOH F 310  HOH F 316  HOH F 317  HOH F 318                    
SITE    10 AF2 46 HOH F 326  HOH F 385  HOH F 391  TYR G  76                    
SITE    11 AF2 46 LEU G  77  GLU G  79  HOH G 304  HOH G 312                    
SITE    12 AF2 46 HOH G 340  GLN J   3                                          
SITE     1 AF3 50 GLN F   3  GLN F  16  ILE F  17  TYR F  18                    
SITE     2 AF3 50 ASN F  44  GLY F  45  ALA F  46  ILE F  47                    
SITE     3 AF3 50 PHE F  48  PRO F  93  HIS F  94  HOH F 302                    
SITE     4 AF3 50 HOH F 310  HOH F 316  HOH F 317  HOH F 318                    
SITE     5 AF3 50 HOH F 326  HOH F 385  HOH F 391  GLN G  16                    
SITE     6 AF3 50 ILE G  17  TYR G  18  ASN G  44  GLY G  45                    
SITE     7 AF3 50 ALA G  46  ILE G  47  PHE G  48  THR G  92                    
SITE     8 AF3 50 PRO G  93  HIS G  94  BGC G 201  HOH G 301                    
SITE     9 AF3 50 HOH G 302  HOH G 303  HOH G 308  HOH G 321                    
SITE    10 AF3 50 HOH G 345  HOH G 356  HOH G 386  HOH G 389                    
SITE    11 AF3 50 HOH G 392  HOH G 395  THR I   1  GLN J   3                    
SITE    12 AF3 50 SER J  55  GLN J  56  ASN J  90  LYS J  91                    
SITE    13 AF3 50 THR J  92  HOH J 327                                          
SITE     1 AF4 53 GLN F   3  ASP F  59  LYS F  63  GLN G  16                    
SITE     2 AF4 53 ILE G  17  TYR G  18  ASN G  44  GLY G  45                    
SITE     3 AF4 53 ALA G  46  ILE G  47  PHE G  48  ASP G  59                    
SITE     4 AF4 53 THR G  92  PRO G  93  HIS G  94  HOH G 301                    
SITE     5 AF4 53 HOH G 302  HOH G 303  HOH G 308  HOH G 321                    
SITE     6 AF4 53 HOH G 331  HOH G 345  HOH G 356  HOH G 386                    
SITE     7 AF4 53 HOH G 389  HOH G 392  HOH G 395  GLN H   3                    
SITE     8 AF4 53 THR I   1  GLN I  16  TYR I  18  ASN I  44                    
SITE     9 AF4 53 GLY I  45  ALA I  46  ILE I  47  PRO I  93                    
SITE    10 AF4 53 HIS I  94  HOH I 303  HOH I 305  HOH I 320                    
SITE    11 AF4 53 HOH I 322  HOH I 358  HOH I 362  HOH I 363                    
SITE    12 AF4 53 HOH I 385  HOH I 389  HOH I 396  SER J  55                    
SITE    13 AF4 53 GLN J  56  ASN J  90  LYS J  91  THR J  92                    
SITE    14 AF4 53 HOH J 327                                                     
SITE     1 AF5 50 LYS D  84  HOH D 332  ASP F  59  LYS F  63                    
SITE     2 AF5 50 ASP G  59  GLN H   3  GLN I   3  GLN I  16                    
SITE     3 AF5 50 TYR I  18  ASN I  44  GLY I  45  ALA I  46                    
SITE     4 AF5 50 ILE I  47  PRO I  93  HIS I  94  HOH I 303                    
SITE     5 AF5 50 HOH I 305  HOH I 320  HOH I 322  HOH I 358                    
SITE     6 AF5 50 HOH I 362  HOH I 363  HOH I 385  HOH I 389                    
SITE     7 AF5 50 HOH I 396  GLN J  16  ILE J  17  TYR J  18                    
SITE     8 AF5 50 ASN J  44  GLY J  45  ALA J  46  ILE J  47                    
SITE     9 AF5 50 PHE J  48  THR J  92  PRO J  93  HIS J  94                    
SITE    10 AF5 50 HOH J 302  HOH J 303  HOH J 304  HOH J 305                    
SITE    11 AF5 50 HOH J 306  HOH J 309  HOH J 312  HOH J 329                    
SITE    12 AF5 50 HOH J 372  HOH J 376  HOH J 377  HOH J 379                    
SITE    13 AF5 50 HOH J 396  HOH J 403                                          
CRYST1   63.626   84.720  195.680  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      0.015717  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011804  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005110        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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