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Database: PDB
Entry: 5ELD
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HEADER    TOXIN                                   04-NOV-15   5ELD              
TITLE     CHOLERA TOXIN CLASSICAL B-PENTAMER IN COMPLEX WITH A LEWIS-Y          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA ENTEROTOXIN B SUBUNIT;                             
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 SYNONYM: CHOLERA TOXIN B-PENTAMER, CLASSICAL VARIANT,CHOLERA         
COMPND   5 ENTEROTOXIN SUBUNIT B,CHOLERA TOXIN B PROTEIN (CTB),CHOLERA TOXIN B  
COMPND   6 SUBUNIT,CHOLERA TOXIN BETA SUBUNIT,CHOLERA TOXIN SUBUNIT B,CHOLERAE  
COMPND   7 TOXIN B SUBUNIT,CTXB;                                                
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE O1;                             
SOURCE   3 ORGANISM_TAXID: 127906;                                              
SOURCE   4 GENE: CTXB;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    CHOLERA TOXIN B-PENTAMER, A LEWIS-Y, COMPLEX, BLOOD GROUP             
KEYWDS   2 OLIGOSACCHARIDE/ANTIGEN, TOXIN                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.HEGGELUND,D.BURSCHOWSKY,U.KRENGEL                                 
REVDAT   3   11-MAY-16 5ELD    1       SOURCE                                   
REVDAT   2   27-APR-16 5ELD    1       JRNL                                     
REVDAT   1   30-MAR-16 5ELD    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.    1.40 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) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 122617                         
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) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.193                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6438                            
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) : 1.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.44                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8785                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.54                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3170                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 416                          
REMARK   3   BIN FREE R VALUE                    : 0.3170                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4070                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 345                                     
REMARK   3   SOLVENT ATOMS            : 610                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.65000                                             
REMARK   3    B22 (A**2) : 0.31000                                              
REMARK   3    B33 (A**2) : 0.34000                                              
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): 0.057         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.058         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.046         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.239         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.958                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4939 ; 0.015 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  4752 ; 0.005 ; 0.021       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6769 ; 1.806 ; 2.057       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11116 ; 1.335 ; 3.054       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   584 ; 6.848 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   195 ;40.056 ;25.333       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   860 ;12.750 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;27.755 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   890 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5042 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   993 ; 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):  2138 ; 1.382 ; 1.487       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2137 ; 1.379 ; 1.486       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2684 ; 2.202 ; 2.220       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2685 ; 2.204 ; 2.221       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2801 ; 1.801 ; 1.798       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2802 ; 1.801 ; 1.798       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4049 ; 2.836 ; 2.609       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5783 ; 5.253 ;13.461       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5784 ; 5.253 ;13.463       
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 5ELD 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_1000214976.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS NOVEMBER 3, 2014               
REMARK 200  DATA SCALING SOFTWARE          : XDS NOVEMBER 3, 2014               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 129054                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.07600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.8500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.99300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.260                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP 11.2.08; 09.12.2013                            
REMARK 200 STARTING MODEL: 3CHB                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES-IMIDAZOLE, 25% PEG4000, 5%     
REMARK 280  PGA-LM, PH 6.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       34.85000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.36750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.90300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.36750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.85000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.90300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 22230 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 78.0 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 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   NH1  ARG D    67     OD1  ASP E    70              2.08            
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    MET A 101   CG  -  SD  -  CE  ANGL. DEV. = -17.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS B  34       -1.12     66.86                                   
REMARK 500    LYS C  34       -0.40     73.43                                   
REMARK 500    LYS D  34       -0.15     69.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     MES C   201                                                      
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                              NA B 201  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B   9   O                                                      
REMARK 620 2 TYR B  12   O    88.5                                              
REMARK 620 3 THR B  15   OG1  74.8  92.4                                        
REMARK 620 4 HOH B 366   O   167.9  87.7  93.9                                  
REMARK 620 5 GLU A  79   OE1  59.0 114.9  29.7 112.6                            
REMARK 620 6 GLU A  79   OE1  58.3 113.9  29.3 113.2   1.1                      
REMARK 620 7 HOH A 399   O    84.0 172.1  88.2 100.1  63.2  64.1                
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 PEG 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 NA B 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GAL C 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE D 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GAL E 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NDG A    
REMARK 800  203 through FUC A 207                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NDG C    
REMARK 800  204 through FUC C 208                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NDG D    
REMARK 800  203 through FUC D 207                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NDG E    
REMARK 800  203 through FUC E 207                                               
DBREF  5ELD A    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
DBREF  5ELD B    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
DBREF  5ELD C    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
DBREF  5ELD D    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
DBREF  5ELD E    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              
HET    PEG  A 201       7                                                       
HET    GAL  A 202      12                                                       
HET    NDG  A 203      30                                                       
HET    GAL  A 204      22                                                       
HET    A2G  A 205      28                                                       
HET    FUC  A 206      20                                                       
HET    FUC  A 207      20                                                       
HET     NA  B 201       1                                                       
HET    MES  C 201      12                                                       
HET    PGE  C 202      10                                                       
HET    GAL  C 203      12                                                       
HET    NDG  C 204      30                                                       
HET    GAL  C 205      22                                                       
HET    A2G  C 206      28                                                       
HET    FUC  C 207      20                                                       
HET    FUC  C 208      20                                                       
HET    PEG  D 201       7                                                       
HET    PGE  D 202      10                                                       
HET    NDG  D 203      30                                                       
HET    GAL  D 204      22                                                       
HET    A2G  D 205      28                                                       
HET    FUC  D 206      20                                                       
HET    FUC  D 207      20                                                       
HET    PGE  E 201      10                                                       
HET    GAL  E 202      12                                                       
HET    GLA  E 203      12                                                       
HET    NDG  E 204      15                                                       
HET    GAL  E 205      11                                                       
HET    A2G  E 206      14                                                       
HET    FUC  E 207      10                                                       
HET    FUC  E 208      10                                                       
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
HETNAM     A2G N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE                               
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM      NA SODIUM ION                                                       
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     GLA ALPHA D-GALACTOSE                                                
FORMUL   6  PEG    2(C4 H10 O3)                                                 
FORMUL   7  GAL    7(C6 H12 O6)                                                 
FORMUL   8  NDG    4(C8 H15 N O6)                                               
FORMUL   8  A2G    4(C8 H15 N O6)                                               
FORMUL   8  FUC    8(C6 H12 O5)                                                 
FORMUL   9   NA    NA 1+                                                        
FORMUL  10  MES    C6 H13 N O4 S                                                
FORMUL  11  PGE    3(C6 H14 O4)                                                 
FORMUL  19  GLA    C6 H12 O6                                                    
FORMUL  21  HOH   *610(H2 O)                                                    
HELIX    1 AA1 ASN A    4  ALA A   10  1                                   7    
HELIX    2 AA2 SER A   60  GLU A   79  1                                  20    
HELIX    3 AA3 ASN B    4  ALA B   10  1                                   7    
HELIX    4 AA4 SER B   60  GLU B   79  1                                  20    
HELIX    5 AA5 ASN C    4  ALA C   10  1                                   7    
HELIX    6 AA6 ILE C   58  SER C   60  5                                   3    
HELIX    7 AA7 GLN C   61  GLU C   79  1                                  19    
HELIX    8 AA8 ASN D    4  GLU D   11  1                                   8    
HELIX    9 AA9 SER D   60  GLU D   79  1                                  20    
HELIX   10 AB1 ASN E    4  ALA E   10  1                                   7    
HELIX   11 AB2 ILE E   58  THR E   78  1                                  21    
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  GLU A  29  0                                        
SHEET    2   B 3 ALA A  38  THR A  41 -1                                        
SHEET    3   B 3 THR 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 THR 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 THR 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 THR 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  GLU E  29  0                                        
SHEET    2   J 3 ALA E  38  THR E  41 -1                                        
SHEET    3   J 3 THR E  47  VAL E  50 -1                                        
SSBOND   1 CYS A    9    CYS A   86                          1555   1555  2.04  
SSBOND   2 CYS B    9    CYS B   86                          1555   1555  2.03  
SSBOND   3 CYS C    9    CYS C   86                          1555   1555  2.04  
SSBOND   4 CYS D    9    CYS D   86                          1555   1555  2.05  
SSBOND   5 CYS E    9    CYS E   86                          1555   1555  2.05  
LINK         O   CYS B   9                NA    NA B 201     1555   1555  2.54  
LINK         O   TYR B  12                NA    NA B 201     1555   1555  2.30  
LINK         OG1 THR B  15                NA    NA B 201     1555   1555  2.26  
LINK         O3 ANDG A 203                 C1 AFUC A 207     1555   1555  1.46  
LINK         O3 BNDG A 203                 C1 BFUC A 207     1555   1555  1.46  
LINK         O4 ANDG A 203                 C1 AGAL A 204     1555   1555  1.45  
LINK         O4 BNDG A 203                 C1 BGAL A 204     1555   1555  1.45  
LINK         O2 AGAL A 204                 C1 AFUC A 206     1555   1555  1.42  
LINK         O2 BGAL A 204                 C1 BFUC A 206     1555   1555  1.41  
LINK         O3 AGAL A 204                 C1 AA2G A 205     1555   1555  1.42  
LINK         O3 BGAL A 204                 C1 BA2G A 205     1555   1555  1.46  
LINK        NA    NA B 201                 O   HOH B 366     1555   1555  2.36  
LINK         O3 ANDG C 204                 C1 AFUC C 208     1555   1555  1.41  
LINK         O3 BNDG C 204                 C1 BFUC C 208     1555   1555  1.49  
LINK         O4 ANDG C 204                 C1 AGAL C 205     1555   1555  1.44  
LINK         O4 BNDG C 204                 C1 BGAL C 205     1555   1555  1.43  
LINK         O2 AGAL C 205                 C1 AFUC C 207     1555   1555  1.43  
LINK         O2 BGAL C 205                 C1 BFUC C 207     1555   1555  1.45  
LINK         O3 AGAL C 205                 C1 AA2G C 206     1555   1555  1.45  
LINK         O3 BGAL C 205                 C1 BA2G C 206     1555   1555  1.47  
LINK         O3 ANDG D 203                 C1 AFUC D 207     1555   1555  1.48  
LINK         O3 BNDG D 203                 C1 BFUC D 207     1555   1555  1.48  
LINK         O4 ANDG D 203                 C1 AGAL D 204     1555   1555  1.44  
LINK         O4 BNDG D 203                 C1 BGAL D 204     1555   1555  1.44  
LINK         O2 AGAL D 204                 C1 AFUC D 206     1555   1555  1.43  
LINK         O2 BGAL D 204                 C1 BFUC D 206     1555   1555  1.44  
LINK         O3 AGAL D 204                 C1 AA2G D 205     1555   1555  1.45  
LINK         O3 BGAL D 204                 C1 BA2G D 205     1555   1555  1.43  
LINK         O3  NDG E 204                 C1  FUC E 208     1555   1555  1.49  
LINK         O4  NDG E 204                 C1  GAL E 205     1555   1555  1.46  
LINK         O2  GAL E 205                 C1  FUC E 207     1555   1555  1.46  
LINK         O3  GAL E 205                 C1  A2G E 206     1555   1555  1.47  
LINK         OE1AGLU A  79                NA    NA B 201     1555   4445  2.18  
LINK         OE1BGLU A  79                NA    NA B 201     1555   4445  2.49  
LINK        NA    NA B 201                 O   HOH A 399     1555   4545  2.42  
CISPEP   1 THR A   92    PRO A   93          0       -12.60                     
CISPEP   2 THR B   92    PRO B   93          0         1.69                     
CISPEP   3 THR B   92    PRO B   93          0       -24.45                     
CISPEP   4 THR C   92    PRO C   93          0        -8.26                     
CISPEP   5 THR D   92    PRO D   93          0       -15.19                     
CISPEP   6 THR E   92    PRO E   93          0       -11.35                     
SITE     1 AC1  6 THR A  41  PHE A  42  LYS A  43  NDG A 203                    
SITE     2 AC1  6 HOH A 383  HOH A 385                                          
SITE     1 AC2  8 GLU A  51  GLN A  56  HIS A  57  GLN A  61                    
SITE     2 AC2  8 TRP A  88  ASN A  90  LYS A  91  HOH A 361                    
SITE     1 AC3  6 GLU A  79  HOH A 399  CYS B   9  TYR B  12                    
SITE     2 AC3  6 THR B  15  HOH B 366                                          
SITE     1 AC4  4 ASN B  14  ILE B  74  LEU B  77  ASN B  89                    
SITE     1 AC5  7 PHE C  25  THR C  41  PHE C  42  LYS C  43                    
SITE     2 AC5  7 GLY C  45  NDG C 204  HOH C 387                               
SITE     1 AC6 13 GLU C  51  GLN C  56  HIS C  57  GLN C  61                    
SITE     2 AC6 13 TRP C  88  ASN C  90  LYS C  91  HOH C 304                    
SITE     3 AC6 13 HOH C 306  HOH C 362  HOH C 388  GLN D  16                    
SITE     4 AC6 13 HOH D 376                                                     
SITE     1 AC7  4 GLU D  11  TYR D  12  HOH D 395  ARG E  35                    
SITE     1 AC8  5 THR D  41  PHE D  42  NDG D 203  HOH D 365                    
SITE     2 AC8  5 HOH D 380                                                     
SITE     1 AC9  5 PHE E  25  THR E  41  PHE E  42  NDG E 204                    
SITE     2 AC9  5 HOH E 391                                                     
SITE     1 AD1 14 GLN A  16  ASN A  89  HOH A 311  HOH A 319                    
SITE     2 AD1 14 GLU E  51  GLN E  56  HIS E  57  GLN E  61                    
SITE     3 AD1 14 TRP E  88  ASN E  90  LYS E  91  HOH E 303                    
SITE     4 AD1 14 HOH E 361  HOH E 378                                          
SITE     1 AD2 36 GLN A  16  ILE A  17  HIS A  18  GLY A  33                    
SITE     2 AD2 36 LYS A  34  ASN A  44  GLY A  45  ALA A  46                    
SITE     3 AD2 36 THR A  47  PHE A  48  PRO A  93  HIS A  94                    
SITE     4 AD2 36 PEG A 201  HOH A 303  HOH A 304  HOH A 308                    
SITE     5 AD2 36 HOH A 309  HOH A 311  HOH A 312  HOH A 318                    
SITE     6 AD2 36 HOH A 320  HOH A 322  HOH A 324  HOH A 328                    
SITE     7 AD2 36 HOH A 333  HOH A 336  HOH A 350  HOH A 369                    
SITE     8 AD2 36 HOH A 387  HOH A 392  GLN E   3  SER E  55                    
SITE     9 AD2 36 GLN E  56  HIS E  57  ILE E  58  HOH E 341                    
SITE     1 AD3 68 GLN A  16  ILE A  17  HIS A  18  GLY A  33                    
SITE     2 AD3 68 LYS A  34  ASN A  44  GLY A  45  ALA A  46                    
SITE     3 AD3 68 THR A  47  PHE A  48  PRO A  93  HIS A  94                    
SITE     4 AD3 68 PEG A 201  HOH A 303  HOH A 304  HOH A 308                    
SITE     5 AD3 68 HOH A 309  HOH A 311  HOH A 312  HOH A 318                    
SITE     6 AD3 68 HOH A 320  HOH A 322  HOH A 324  HOH A 328                    
SITE     7 AD3 68 HOH A 333  HOH A 336  HOH A 350  HOH A 369                    
SITE     8 AD3 68 HOH A 387  HOH A 392  GLN B   3  GLN C  16                    
SITE     9 AD3 68 ILE C  17  HIS C  18  ASN C  44  GLY C  45                    
SITE    10 AD3 68 ALA C  46  THR C  47  PHE C  48  GLU C  51                    
SITE    11 AD3 68 GLN C  56  HIS C  57  GLN C  61  TRP C  88                    
SITE    12 AD3 68 ASN C  90  LYS C  91  THR C  92  PRO C  93                    
SITE    13 AD3 68 HIS C  94  PGE C 202  HOH C 304  HOH C 305                    
SITE    14 AD3 68 HOH C 306  HOH C 313  HOH C 315  HOH C 318                    
SITE    15 AD3 68 HOH C 362  HOH C 388  HOH C 397  GLN D  16                    
SITE    16 AD3 68 HOH D 376  GLN E   3  SER E  55  GLN E  56                    
SITE    17 AD3 68 HIS E  57  ILE E  58  A2G E 206  HOH E 341                    
SITE     1 AD4 61 GLN B   3  GLN C   3  TYR C  12  HIS C  13                    
SITE     2 AD4 61 GLN C  16  ILE C  17  HIS C  18  ASN C  44                    
SITE     3 AD4 61 GLY C  45  ALA C  46  THR C  47  GLU C  51                    
SITE     4 AD4 61 SER C  55  GLN C  56  HIS C  57  ILE C  58                    
SITE     5 AD4 61 GLN C  61  TRP C  88  ASN C  90  LYS C  91                    
SITE     6 AD4 61 HIS C  94  PGE C 202  FUC C 208  HOH C 304                    
SITE     7 AD4 61 HOH C 305  HOH C 306  HOH C 313  HOH C 315                    
SITE     8 AD4 61 HOH C 324  HOH C 362  HOH C 388  HOH C 397                    
SITE     9 AD4 61 GLN D  16  ILE D  17  HIS D  18  GLY D  33                    
SITE    10 AD4 61 LYS D  34  ASN D  44  GLY D  45  ALA D  46                    
SITE    11 AD4 61 THR D  47  PHE D  48  PRO D  93  HIS D  94                    
SITE    12 AD4 61 PGE D 202  HOH D 302  HOH D 303  HOH D 305                    
SITE    13 AD4 61 HOH D 306  HOH D 309  HOH D 313  HOH D 314                    
SITE    14 AD4 61 HOH D 316  HOH D 332  HOH D 346  HOH D 374                    
SITE    15 AD4 61 HOH D 376  HOH D 379  HOH D 390  HOH D 391                    
SITE    16 AD4 61 A2G E 206                                                     
SITE     1 AD5 54 GLN C   3  TYR C  12  HIS C  13  SER C  55                    
SITE     2 AD5 54 GLN C  56  HIS C  57  ILE C  58  A2G C 206                    
SITE     3 AD5 54 HOH C 304  HOH C 324  HOH C 362  GLN D   3                    
SITE     4 AD5 54 GLN D  16  ILE D  17  HIS D  18  GLY D  33                    
SITE     5 AD5 54 LYS D  34  ASN D  44  GLY D  45  ALA D  46                    
SITE     6 AD5 54 THR D  47  PHE D  48  PRO D  93  HIS D  94                    
SITE     7 AD5 54 PGE D 202  HOH D 302  HOH D 303  HOH D 305                    
SITE     8 AD5 54 HOH D 306  HOH D 309  HOH D 313  HOH D 314                    
SITE     9 AD5 54 HOH D 316  HOH D 332  HOH D 346  HOH D 374                    
SITE    10 AD5 54 HOH D 379  HOH D 390  HOH D 391  GLN E  16                    
SITE    11 AD5 54 ILE E  17  HIS E  18  ASN E  44  GLY E  45                    
SITE    12 AD5 54 ALA E  46  THR E  47  PHE E  48  PRO E  93                    
SITE    13 AD5 54 HIS E  94  PGE E 201  HOH E 304  HOH E 308                    
SITE    14 AD5 54 HOH E 326  HOH E 388                                          
CRYST1   69.700   69.806  134.735  90.00  90.00  90.00 P 21 21 21   20          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014347  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014325  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007422        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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