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Entry: 6EPK
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HEADER    VIRAL PROTEIN                           11-OCT-17   6EPK              
TITLE     CRYSTAL STRUCTURE OF THE PRECURSOR MEMBRANE PROTEIN-ENVELOPE PROTEIN  
TITLE    2 HETERODIMER FROM THE YELLOW FEVER VIRUS                              
CAVEAT     6EPK    FUC B 704 HAS WRONG CHIRALITY AT ATOM C1 FUC E 705 HAS WRONG 
CAVEAT   2 6EPK    CHIRALITY AT ATOM C1                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENVELOPE PROTEIN E;                                        
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 EC: 3.4.21.91,3.6.1.15,3.6.4.13,2.1.1.56,2.1.1.57,2.7.7.48;          
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PRECURSOR MEMBRANE PROTEIN;                                
COMPND   8 CHAIN: B, E;                                                         
COMPND   9 EC: 3.4.21.91,3.6.1.15,3.6.4.13,2.1.1.56,2.1.1.57,2.7.7.48;          
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: YELLOW FEVER VIRUS;                             
SOURCE   3 ORGANISM_TAXID: 11089;                                               
SOURCE   4 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   5 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER S2;                           
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: YELLOW FEVER VIRUS;                             
SOURCE  10 ORGANISM_TAXID: 11089;                                               
SOURCE  11 GENE: PRM;                                                           
SOURCE  12 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE  13 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE  15 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER S2                            
KEYWDS    PRM-E PROTEIN COMPLEX, VIRAL PROTEIN, HETERODIMER, MATURATION         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.A.REY,S.DUQUERROY,E.CRAMPON,G.BARBA-SPAETH                          
REVDAT   1   31-OCT-18 6EPK    0                                                
JRNL        AUTH   F.A.REY,S.DUQUERROY,E.CRAMPON,G.BARBA-SPAETH                 
JRNL        TITL   CRYSTAL STRUCTURE OF THE PRECURSOR MEMBRANE PROTEIN-ENVELOPE 
JRNL        TITL 2 PROTEIN HETERODIMER FROM THE YELLOW FEVER VIRUS              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.72                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 63742                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.186                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3182                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 28.1727 -  7.2891    0.94     3045   163  0.1448 0.1917        
REMARK   3     2  7.2891 -  5.8021    0.95     3044   160  0.1426 0.1767        
REMARK   3     3  5.8021 -  5.0736    0.95     3041   145  0.1300 0.1510        
REMARK   3     4  5.0736 -  4.6119    0.95     3046   155  0.1219 0.1288        
REMARK   3     5  4.6119 -  4.2825    0.95     3020   160  0.1154 0.1302        
REMARK   3     6  4.2825 -  4.0308    0.95     3019   170  0.1321 0.1455        
REMARK   3     7  4.0308 -  3.8295    0.95     3055   165  0.1491 0.1704        
REMARK   3     8  3.8295 -  3.6631    0.96     3044   138  0.1528 0.1868        
REMARK   3     9  3.6631 -  3.5224    0.95     3019   173  0.1587 0.1613        
REMARK   3    10  3.5224 -  3.4010    0.95     3012   164  0.1686 0.2028        
REMARK   3    11  3.4010 -  3.2949    0.95     3017   166  0.1786 0.1956        
REMARK   3    12  3.2949 -  3.2008    0.95     3014   167  0.1925 0.1973        
REMARK   3    13  3.2008 -  3.1167    0.95     3013   157  0.2053 0.2207        
REMARK   3    14  3.1167 -  3.0407    0.95     3063   152  0.2261 0.2622        
REMARK   3    15  3.0407 -  2.9717    0.95     3027   170  0.2510 0.2740        
REMARK   3    16  2.9717 -  2.9085    0.95     3032   159  0.2464 0.2802        
REMARK   3    17  2.9085 -  2.8504    0.95     3003   148  0.2590 0.2916        
REMARK   3    18  2.8504 -  2.7966    0.95     3051   155  0.2851 0.3274        
REMARK   3    19  2.7966 -  2.7467    0.95     3023   154  0.3135 0.4003        
REMARK   3    20  2.7467 -  2.7002    0.95     2962   160  0.3427 0.3731        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.690           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           8055                                  
REMARK   3   ANGLE     :  0.672          10935                                  
REMARK   3   CHIRALITY :  0.028           1249                                  
REMARK   3   PLANARITY :  0.002           1358                                  
REMARK   3   DIHEDRAL  : 12.237           2906                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND ( (RESID 1:45) OR (RESID 139:183) OR      
REMARK   3               (RESID 280:407) ) )                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  20.3105  79.0059 -18.9543              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4319 T22:   0.4040                                     
REMARK   3      T33:   0.4564 T12:   0.0781                                     
REMARK   3      T13:   0.0333 T23:   0.0868                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0003 L22:   3.9462                                     
REMARK   3      L33:   6.3344 L12:  -0.6429                                     
REMARK   3      L13:   1.8364 L23:  -1.1763                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1364 S12:   0.3313 S13:  -0.1000                       
REMARK   3      S21:   0.0440 S22:  -0.0660 S23:  -0.3729                       
REMARK   3      S31:   0.3254 S32:   0.2533 S33:  -0.0369                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND ( (RESID 64:120) OR (RESID 231:247) ) )   
REMARK   3               OR (CHAIN B)                                           
REMARK   3    ORIGIN FOR THE GROUP (A):  11.3749   0.0616   7.0174              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4233 T22:   0.4055                                     
REMARK   3      T33:   0.3419 T12:  -0.0305                                     
REMARK   3      T13:  -0.0587 T23:   0.0759                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5964 L22:   3.8924                                     
REMARK   3      L33:   3.2599 L12:   0.0670                                     
REMARK   3      L13:  -0.3392 L23:   1.0318                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0100 S12:  -0.0167 S13:  -0.0555                       
REMARK   3      S21:   0.1790 S22:  -0.2470 S23:  -0.1868                       
REMARK   3      S31:   0.1081 S32:   0.0142 S33:   0.2587                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND ( (RESID 46:63) OR (RESID 121:138) OR     
REMARK   3               (RESID 184:230) OR (RESID 248:279) ) )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  16.4025  41.3734   0.8662              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1630 T22:   0.5036                                     
REMARK   3      T33:   0.6863 T12:  -0.0269                                     
REMARK   3      T13:  -0.0656 T23:   0.1359                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1815 L22:   3.4571                                     
REMARK   3      L33:   0.9885 L12:   1.8929                                     
REMARK   3      L13:  -0.2083 L23:  -0.8635                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2360 S12:   0.0526 S13:   0.3989                       
REMARK   3      S21:   0.0620 S22:  -0.3766 S23:  -0.5427                       
REMARK   3      S31:  -0.4261 S32:   0.0045 S33:   0.2364                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN D AND ( (RESID 1:45) OR (RESID 139:183) OR      
REMARK   3               (RESID 280:407) ) )                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -21.2355  82.3961  18.4318              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5528 T22:   0.5771                                     
REMARK   3      T33:   0.5100 T12:  -0.0574                                     
REMARK   3      T13:  -0.0764 T23:  -0.1502                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0996 L22:   4.7232                                     
REMARK   3      L33:   6.1156 L12:  -0.6245                                     
REMARK   3      L13:   1.2221 L23:   1.8244                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2380 S12:  -0.0140 S13:  -0.2097                       
REMARK   3      S21:  -0.6376 S22:  -0.3956 S23:   0.6220                       
REMARK   3      S31:  -0.1483 S32:  -0.1835 S33:   0.1851                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN D AND ( (RESID 64:120) OR (RESID 231:247) ) )   
REMARK   3               OR (CHAIN E)                                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.7604   2.4355  -6.8541              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4112 T22:   0.3933                                     
REMARK   3      T33:   0.3513 T12:   0.0730                                     
REMARK   3      T13:  -0.0723 T23:  -0.0917                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7794 L22:   3.8599                                     
REMARK   3      L33:   4.2282 L12:   0.5230                                     
REMARK   3      L13:  -0.0737 L23:  -1.2933                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0729 S12:  -0.0510 S13:  -0.1310                       
REMARK   3      S21:  -0.1664 S22:  -0.2637 S23:   0.1957                       
REMARK   3      S31:  -0.0861 S32:  -0.1944 S33:   0.3233                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN D AND ( (RESID 46:63) OR (RESID 121:138) OR     
REMARK   3               (RESID 184:230) OR (RESID 248:279) ) )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -12.7819  44.0830   0.4712              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1489 T22:   0.5363                                     
REMARK   3      T33:   0.7536 T12:   0.1025                                     
REMARK   3      T13:  -0.1105 T23:  -0.1370                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4156 L22:   3.5604                                     
REMARK   3      L33:   1.4244 L12:  -2.7994                                     
REMARK   3      L13:  -0.3610 L23:   1.0125                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1962 S12:  -0.0914 S13:   0.5008                       
REMARK   3      S21:  -0.3907 S22:  -0.3851 S23:   0.4045                       
REMARK   3      S31:  -0.4067 S32:  -0.0948 S33:   0.2685                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6EPK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-OCT-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200007024.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-SEP-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.                                 
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63786                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.12300                            
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: AMORE                                                 
REMARK 200 STARTING MODEL: 3C5X                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M LI2SO4, 100MM TRISHCL PH8, PH      
REMARK 280  8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      119.41200            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       59.70600            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      179.11800            
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   408                                                      
REMARK 465     GLY A   409                                                      
REMARK 465     GLY A   410                                                      
REMARK 465     SER A   411                                                      
REMARK 465     GLY A   412                                                      
REMARK 465     GLY A   413                                                      
REMARK 465     GLY A   414                                                      
REMARK 465     SER A   415                                                      
REMARK 465     GLY A   416                                                      
REMARK 465     GLY A   417                                                      
REMARK 465     GLY A   418                                                      
REMARK 465     SER A   419                                                      
REMARK 465     TRP A   420                                                      
REMARK 465     SER A   421                                                      
REMARK 465     HIS A   422                                                      
REMARK 465     PRO A   423                                                      
REMARK 465     GLN A   424                                                      
REMARK 465     PHE A   425                                                      
REMARK 465     GLU A   426                                                      
REMARK 465     LYS A   427                                                      
REMARK 465     ALA B   581                                                      
REMARK 465     GLY B   582                                                      
REMARK 465     ARG B   583                                                      
REMARK 465     SER B   584                                                      
REMARK 465     ARG B   585                                                      
REMARK 465     ARG B   586                                                      
REMARK 465     SER B   587                                                      
REMARK 465     ARG B   588                                                      
REMARK 465     ARG B   589                                                      
REMARK 465     GLY D   408                                                      
REMARK 465     GLY D   409                                                      
REMARK 465     GLY D   410                                                      
REMARK 465     SER D   411                                                      
REMARK 465     GLY D   412                                                      
REMARK 465     GLY D   413                                                      
REMARK 465     GLY D   414                                                      
REMARK 465     SER D   415                                                      
REMARK 465     GLY D   416                                                      
REMARK 465     GLY D   417                                                      
REMARK 465     GLY D   418                                                      
REMARK 465     SER D   419                                                      
REMARK 465     TRP D   420                                                      
REMARK 465     SER D   421                                                      
REMARK 465     HIS D   422                                                      
REMARK 465     PRO D   423                                                      
REMARK 465     GLN D   424                                                      
REMARK 465     PHE D   425                                                      
REMARK 465     GLU D   426                                                      
REMARK 465     LYS D   427                                                      
REMARK 465     ALA E   581                                                      
REMARK 465     GLY E   582                                                      
REMARK 465     ARG E   583                                                      
REMARK 465     SER E   584                                                      
REMARK 465     ARG E   585                                                      
REMARK 465     ARG E   586                                                      
REMARK 465     SER E   587                                                      
REMARK 465     ARG E   588                                                      
REMARK 465     ARG E   589                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 407    CG   CD   CE   NZ                                   
REMARK 470     LYS D 407    CG   CD   CE   NZ                                   
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   O    HOH B   826     O    HOH B   840              1.90            
REMARK 500   O    HOH A   656     O    HOH A   683              1.98            
REMARK 500   OE1  GLU A    79     O    HOH A   601              2.02            
REMARK 500   O    HOH B   825     O    HOH B   831              2.02            
REMARK 500   O    HOH A   672     O    HOH A   677              2.06            
REMARK 500   O    THR A    24     O    HOH A   602              2.07            
REMARK 500   O    SER A   401     O    HOH A   603              2.08            
REMARK 500   O    ASP E   560     O    HOH E   801              2.10            
REMARK 500   NH1  ARG A   284     OE1  GLU A   406              2.10            
REMARK 500   O    HOH A   605     O    HOH A   629              2.13            
REMARK 500   O2   MAN E   709     O    HOH E   802              2.13            
REMARK 500   O    ALA D   240     O    HOH D   601              2.14            
REMARK 500   O    GLY A    78     O    HOH A   604              2.14            
REMARK 500   O    HOH A   665     O    HOH A   678              2.14            
REMARK 500   O    HOH E   812     O    HOH E   821              2.17            
REMARK 500   O    HOH B   829     O    HOH B   841              2.18            
REMARK 500   O    HOH D   641     O    HOH D   645              2.19            
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  46      -71.17    -78.92                                   
REMARK 500    HIS A  67       78.99     50.21                                   
REMARK 500    GLU A 199     -127.15     50.11                                   
REMARK 500    SER A 221      -19.54     75.85                                   
REMARK 500    ASP A 360       19.62     58.98                                   
REMARK 500    ASP A 393       -0.79     90.89                                   
REMARK 500    ASN B 507     -120.84     57.14                                   
REMARK 500    LYS B 538     -124.83   -129.21                                   
REMARK 500    GLU D  46      -71.17    -79.44                                   
REMARK 500    HIS D  67       80.20     50.89                                   
REMARK 500    GLU D 199     -127.80     48.00                                   
REMARK 500    SER D 219        3.21    -67.82                                   
REMARK 500    ASP D 360       18.87     57.97                                   
REMARK 500    ASN E 507     -121.67     57.64                                   
REMARK 500    LYS E 538     -124.03   -128.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 709                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 711                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 712                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 710                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  701 through NAG B 702 bound to ASN B 513                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  703 through MAN B 708 bound to ASN B 529                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG E    
REMARK 800  701 through BMA E 703 bound to ASN E 513                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG E    
REMARK 800  704 through MAN E 709 bound to ASN E 529                            
DBREF  6EPK A    1   392  UNP    Q6DV88   POLG_YEFVA     286    677             
DBREF  6EPK B  501   589  UNP    Q6DV88   POLG_YEFVA     122    210             
DBREF  6EPK D    1   392  UNP    Q6DV88   POLG_YEFVA     286    677             
DBREF  6EPK E  501   589  UNP    Q6DV88   POLG_YEFVA     122    210             
SEQADV 6EPK ASP A  393  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK ASP A  394  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK ASP A  395  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK ASP A  396  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK LYS A  397  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK ALA A  398  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY A  399  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK TRP A  400  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK SER A  401  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK HIS A  402  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK PRO A  403  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLN A  404  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK PHE A  405  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLU A  406  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK LYS A  407  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY A  408  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY A  409  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY A  410  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK SER A  411  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY A  412  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY A  413  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY A  414  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK SER A  415  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY A  416  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY A  417  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY A  418  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK SER A  419  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK TRP A  420  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK SER A  421  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK HIS A  422  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK PRO A  423  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLN A  424  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK PHE A  425  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLU A  426  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK LYS A  427  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK ASP D  393  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK ASP D  394  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK ASP D  395  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK ASP D  396  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK LYS D  397  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK ALA D  398  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY D  399  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK TRP D  400  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK SER D  401  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK HIS D  402  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK PRO D  403  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLN D  404  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK PHE D  405  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLU D  406  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK LYS D  407  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY D  408  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY D  409  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY D  410  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK SER D  411  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY D  412  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY D  413  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY D  414  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK SER D  415  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY D  416  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY D  417  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLY D  418  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK SER D  419  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK TRP D  420  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK SER D  421  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK HIS D  422  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK PRO D  423  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLN D  424  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK PHE D  425  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK GLU D  426  UNP  Q6DV88              EXPRESSION TAG                 
SEQADV 6EPK LYS D  427  UNP  Q6DV88              EXPRESSION TAG                 
SEQRES   1 A  427  ALA HIS CYS ILE GLY ILE THR ASP ARG ASP PHE ILE GLU          
SEQRES   2 A  427  GLY VAL HIS GLY GLY THR TRP VAL SER ALA THR LEU GLU          
SEQRES   3 A  427  GLN ASP LYS CYS VAL THR VAL MET ALA PRO ASP LYS PRO          
SEQRES   4 A  427  SER LEU ASP ILE SER LEU GLU THR VAL ALA ILE ASP GLY          
SEQRES   5 A  427  PRO ALA GLU ALA ARG LYS VAL CYS TYR ASN ALA VAL LEU          
SEQRES   6 A  427  THR HIS VAL LYS ILE ASN ASP LYS CYS PRO SER THR GLY          
SEQRES   7 A  427  GLU ALA HIS LEU ALA GLU GLU ASN GLU GLY ASP ASN ALA          
SEQRES   8 A  427  CYS LYS ARG THR TYR SER ASP ARG GLY TRP GLY ASN GLY          
SEQRES   9 A  427  CYS GLY LEU PHE GLY LYS GLY SER ILE VAL ALA CYS ALA          
SEQRES  10 A  427  LYS PHE THR CYS ALA LYS SER MET SER LEU PHE GLU VAL          
SEQRES  11 A  427  ASP GLN THR LYS ILE GLN TYR VAL ILE ARG ALA GLN LEU          
SEQRES  12 A  427  HIS VAL GLY ALA LYS GLN GLU ASN TRP ASN THR ASP ILE          
SEQRES  13 A  427  LYS THR LEU LYS PHE ASP ALA LEU SER GLY SER GLN GLU          
SEQRES  14 A  427  ALA GLU PHE THR GLY TYR GLY LYS ALA THR LEU GLU CYS          
SEQRES  15 A  427  GLN VAL GLN THR ALA VAL ASP PHE GLY ASN SER TYR ILE          
SEQRES  16 A  427  ALA GLU MET GLU LYS GLU SER TRP ILE VAL ASP ARG GLN          
SEQRES  17 A  427  TRP ALA GLN ASP LEU THR LEU PRO TRP GLN SER GLY SER          
SEQRES  18 A  427  GLY GLY VAL TRP ARG GLU MET HIS HIS LEU VAL GLU PHE          
SEQRES  19 A  427  GLU PRO PRO HIS ALA ALA THR ILE ARG VAL LEU ALA LEU          
SEQRES  20 A  427  GLY ASN GLN GLU GLY SER LEU LYS THR ALA LEU THR GLY          
SEQRES  21 A  427  ALA MET ARG VAL THR LYS ASP THR ASN ASP ASN ASN LEU          
SEQRES  22 A  427  TYR LYS LEU HIS GLY GLY HIS VAL SER CYS ARG VAL LYS          
SEQRES  23 A  427  LEU SER ALA LEU THR LEU LYS GLY THR SER TYR LYS MET          
SEQRES  24 A  427  CYS THR ASP LYS MET SER PHE VAL LYS ASN PRO THR ASP          
SEQRES  25 A  427  THR GLY HIS GLY THR VAL VAL MET GLN VAL LYS VAL PRO          
SEQRES  26 A  427  LYS GLY ALA PRO CYS LYS ILE PRO VAL ILE VAL ALA ASP          
SEQRES  27 A  427  ASP LEU THR ALA ALA ILE ASN LYS GLY ILE LEU VAL THR          
SEQRES  28 A  427  VAL ASN PRO ILE ALA SER THR ASN ASP ASP GLU VAL LEU          
SEQRES  29 A  427  ILE GLU VAL ASN PRO PRO PHE GLY ASP SER TYR ILE ILE          
SEQRES  30 A  427  VAL GLY THR GLY ASP SER ARG LEU THR TYR GLN TRP HIS          
SEQRES  31 A  427  LYS GLU ASP ASP ASP ASP LYS ALA GLY TRP SER HIS PRO          
SEQRES  32 A  427  GLN PHE GLU LYS GLY GLY GLY SER GLY GLY GLY SER GLY          
SEQRES  33 A  427  GLY GLY SER TRP SER HIS PRO GLN PHE GLU LYS                  
SEQRES   1 B   89  VAL THR LEU VAL ARG LYS ASN ARG TRP LEU LEU LEU ASN          
SEQRES   2 B   89  VAL THR SER GLU ASP LEU GLY LYS THR PHE SER VAL GLY          
SEQRES   3 B   89  THR GLY ASN CYS THR THR ASN ILE LEU GLU ALA LYS TYR          
SEQRES   4 B   89  TRP CYS PRO ASP SER MET GLU TYR ASN CYS PRO ASN LEU          
SEQRES   5 B   89  SER PRO ARG GLU GLU PRO ASP ASP ILE ASP CYS TRP CYS          
SEQRES   6 B   89  TYR GLY VAL GLU ASN VAL ARG VAL ALA TYR GLY LYS CYS          
SEQRES   7 B   89  ASP SER ALA GLY ARG SER ARG ARG SER ARG ARG                  
SEQRES   1 D  427  ALA HIS CYS ILE GLY ILE THR ASP ARG ASP PHE ILE GLU          
SEQRES   2 D  427  GLY VAL HIS GLY GLY THR TRP VAL SER ALA THR LEU GLU          
SEQRES   3 D  427  GLN ASP LYS CYS VAL THR VAL MET ALA PRO ASP LYS PRO          
SEQRES   4 D  427  SER LEU ASP ILE SER LEU GLU THR VAL ALA ILE ASP GLY          
SEQRES   5 D  427  PRO ALA GLU ALA ARG LYS VAL CYS TYR ASN ALA VAL LEU          
SEQRES   6 D  427  THR HIS VAL LYS ILE ASN ASP LYS CYS PRO SER THR GLY          
SEQRES   7 D  427  GLU ALA HIS LEU ALA GLU GLU ASN GLU GLY ASP ASN ALA          
SEQRES   8 D  427  CYS LYS ARG THR TYR SER ASP ARG GLY TRP GLY ASN GLY          
SEQRES   9 D  427  CYS GLY LEU PHE GLY LYS GLY SER ILE VAL ALA CYS ALA          
SEQRES  10 D  427  LYS PHE THR CYS ALA LYS SER MET SER LEU PHE GLU VAL          
SEQRES  11 D  427  ASP GLN THR LYS ILE GLN TYR VAL ILE ARG ALA GLN LEU          
SEQRES  12 D  427  HIS VAL GLY ALA LYS GLN GLU ASN TRP ASN THR ASP ILE          
SEQRES  13 D  427  LYS THR LEU LYS PHE ASP ALA LEU SER GLY SER GLN GLU          
SEQRES  14 D  427  ALA GLU PHE THR GLY TYR GLY LYS ALA THR LEU GLU CYS          
SEQRES  15 D  427  GLN VAL GLN THR ALA VAL ASP PHE GLY ASN SER TYR ILE          
SEQRES  16 D  427  ALA GLU MET GLU LYS GLU SER TRP ILE VAL ASP ARG GLN          
SEQRES  17 D  427  TRP ALA GLN ASP LEU THR LEU PRO TRP GLN SER GLY SER          
SEQRES  18 D  427  GLY GLY VAL TRP ARG GLU MET HIS HIS LEU VAL GLU PHE          
SEQRES  19 D  427  GLU PRO PRO HIS ALA ALA THR ILE ARG VAL LEU ALA LEU          
SEQRES  20 D  427  GLY ASN GLN GLU GLY SER LEU LYS THR ALA LEU THR GLY          
SEQRES  21 D  427  ALA MET ARG VAL THR LYS ASP THR ASN ASP ASN ASN LEU          
SEQRES  22 D  427  TYR LYS LEU HIS GLY GLY HIS VAL SER CYS ARG VAL LYS          
SEQRES  23 D  427  LEU SER ALA LEU THR LEU LYS GLY THR SER TYR LYS MET          
SEQRES  24 D  427  CYS THR ASP LYS MET SER PHE VAL LYS ASN PRO THR ASP          
SEQRES  25 D  427  THR GLY HIS GLY THR VAL VAL MET GLN VAL LYS VAL PRO          
SEQRES  26 D  427  LYS GLY ALA PRO CYS LYS ILE PRO VAL ILE VAL ALA ASP          
SEQRES  27 D  427  ASP LEU THR ALA ALA ILE ASN LYS GLY ILE LEU VAL THR          
SEQRES  28 D  427  VAL ASN PRO ILE ALA SER THR ASN ASP ASP GLU VAL LEU          
SEQRES  29 D  427  ILE GLU VAL ASN PRO PRO PHE GLY ASP SER TYR ILE ILE          
SEQRES  30 D  427  VAL GLY THR GLY ASP SER ARG LEU THR TYR GLN TRP HIS          
SEQRES  31 D  427  LYS GLU ASP ASP ASP ASP LYS ALA GLY TRP SER HIS PRO          
SEQRES  32 D  427  GLN PHE GLU LYS GLY GLY GLY SER GLY GLY GLY SER GLY          
SEQRES  33 D  427  GLY GLY SER TRP SER HIS PRO GLN PHE GLU LYS                  
SEQRES   1 E   89  VAL THR LEU VAL ARG LYS ASN ARG TRP LEU LEU LEU ASN          
SEQRES   2 E   89  VAL THR SER GLU ASP LEU GLY LYS THR PHE SER VAL GLY          
SEQRES   3 E   89  THR GLY ASN CYS THR THR ASN ILE LEU GLU ALA LYS TYR          
SEQRES   4 E   89  TRP CYS PRO ASP SER MET GLU TYR ASN CYS PRO ASN LEU          
SEQRES   5 E   89  SER PRO ARG GLU GLU PRO ASP ASP ILE ASP CYS TRP CYS          
SEQRES   6 E   89  TYR GLY VAL GLU ASN VAL ARG VAL ALA TYR GLY LYS CYS          
SEQRES   7 E   89  ASP SER ALA GLY ARG SER ARG ARG SER ARG ARG                  
HET    SO4  A 501       5                                                       
HET    SO4  A 502       5                                                       
HET    SO4  A 503       5                                                       
HET    SO4  A 504       5                                                       
HET    SO4  A 505       5                                                       
HET    SO4  A 506       5                                                       
HET    SO4  A 507       5                                                       
HET    SO4  A 508       5                                                       
HET    SO4  A 509       5                                                       
HET    GOL  A 510       6                                                       
HET    GOL  A 511       6                                                       
HET    GOL  A 512       6                                                       
HET    GOL  A 513       6                                                       
HET    GOL  A 514       6                                                       
HET    NAG  B 701      14                                                       
HET    NAG  B 702      14                                                       
HET    NAG  B 703      14                                                       
HET    FUC  B 704      10                                                       
HET    NAG  B 705      14                                                       
HET    BMA  B 706      11                                                       
HET    MAN  B 707      11                                                       
HET    MAN  B 708      11                                                       
HET    SO4  B 709       5                                                       
HET    SO4  B 710       5                                                       
HET    GOL  B 711       6                                                       
HET    GOL  B 712       6                                                       
HET    SO4  D 501       5                                                       
HET    SO4  D 502       5                                                       
HET    SO4  D 503       5                                                       
HET    SO4  D 504       5                                                       
HET    SO4  D 505       5                                                       
HET    SO4  D 506       5                                                       
HET    SO4  D 507       5                                                       
HET    SO4  D 508       5                                                       
HET    SO4  D 509       5                                                       
HET    SO4  D 510       5                                                       
HET    SO4  D 511       5                                                       
HET    GOL  D 512       6                                                       
HET    GOL  D 513       6                                                       
HET    GOL  D 514       6                                                       
HET    GOL  D 515       6                                                       
HET    GOL  D 516       6                                                       
HET    GOL  D 517       6                                                       
HET    NAG  E 701      14                                                       
HET    NAG  E 702      14                                                       
HET    BMA  E 703      11                                                       
HET    NAG  E 704      14                                                       
HET    FUC  E 705      10                                                       
HET    NAG  E 706      14                                                       
HET    BMA  E 707      11                                                       
HET    MAN  E 708      11                                                       
HET    MAN  E 709      11                                                       
HET    SO4  E 710       5                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  SO4    23(O4 S 2-)                                                  
FORMUL  14  GOL    13(C3 H8 O3)                                                 
FORMUL  19  NAG    8(C8 H15 N O6)                                               
FORMUL  20  FUC    2(C6 H12 O5)                                                 
FORMUL  20  BMA    3(C6 H12 O6)                                                 
FORMUL  20  MAN    4(C6 H12 O6)                                                 
FORMUL  45  HOH   *205(H2 O)                                                    
HELIX    1 AA1 ALA A    1  ILE A    6  5                                   6    
HELIX    2 AA2 LEU A   82  GLU A   87  5                                   6    
HELIX    3 AA3 LYS A  148  GLU A  150  5                                   3    
HELIX    4 AA4 ASN A  151  ILE A  156  1                                   6    
HELIX    5 AA5 ARG A  207  ASP A  212  1                                   6    
HELIX    6 AA6 GLU A  227  HIS A  230  5                                   4    
HELIX    7 AA7 GLN A  250  THR A  259  1                                  10    
HELIX    8 AA8 THR B  515  LEU B  519  5                                   5    
HELIX    9 AA9 ALA D    1  ILE D    6  5                                   6    
HELIX   10 AB1 LEU D   82  ASN D   86  5                                   5    
HELIX   11 AB2 LYS D  148  GLU D  150  5                                   3    
HELIX   12 AB3 ASN D  151  ILE D  156  1                                   6    
HELIX   13 AB4 ARG D  207  ASP D  212  1                                   6    
HELIX   14 AB5 GLU D  227  HIS D  230  5                                   4    
HELIX   15 AB6 GLN D  250  GLY D  260  1                                  11    
HELIX   16 AB7 THR E  515  LEU E  519  5                                   5    
SHEET    1   A 6 ALA A 398  TRP A 400  0                                        
SHEET    2   A 6 ARG A   9  GLU A  13  1  N  ARG A   9   O  GLY A 399           
SHEET    3   A 6 CYS A  30  MET A  34  1  N  CYS A  30   O  ASP A  10           
SHEET    4   A 6 LEU A  41  ILE A  50 -1  N  ILE A  43   O  VAL A  31           
SHEET    5   A 6 ILE A 135  LEU A 143 -1  N  GLN A 142   O  ASP A  42           
SHEET    6   A 6 LYS A 157  ASP A 162 -1  N  PHE A 161   O  TYR A 137           
SHEET    1   B 4 TRP A  20  GLU A  26  0                                        
SHEET    2   B 4 HIS A 280  LYS A 286 -1  N  VAL A 285   O  VAL A  21           
SHEET    3   B 4 GLY A 176  GLN A 185 -1  N  GLN A 185   O  HIS A 280           
SHEET    4   B 4 GLN A 168  PHE A 172 -1  N  PHE A 172   O  GLY A 176           
SHEET    1   C 2 ALA A  49  ASP A  51  0                                        
SHEET    2   C 2 LEU A 273  LYS A 275 -1  N  TYR A 274   O  ILE A  50           
SHEET    1   D 3 VAL A  68  LYS A  73  0                                        
SHEET    2   D 3 GLY A 109  LYS A 118 -1  N  CYS A 116   O  LYS A  69           
SHEET    3   D 3 ASN A  90  ARG A  99 -1  N  ARG A  99   O  GLY A 109           
SHEET    1   E 5 MET A 262  VAL A 264  0                                        
SHEET    2   E 5 GLU A 201  ASP A 206 -1  N  ILE A 204   O  MET A 262           
SHEET    3   E 5 SER A 193  MET A 198 -1  N  MET A 198   O  GLU A 201           
SHEET    4   E 5 SER A 124  GLU A 129 -1  N  PHE A 128   O  ILE A 195           
SHEET    5   E 5 GLU A  55  CYS A  60 -1  N  VAL A  59   O  MET A 125           
SHEET    1   F 2 VAL A 232  PHE A 234  0                                        
SHEET    2   F 2 VAL A 244  ALA A 246 -1  N  LEU A 245   O  GLU A 233           
SHEET    1   G 3 ASP A 361  VAL A 367  0                                        
SHEET    2   G 3 VAL A 318  VAL A 324 -1  N  VAL A 324   O  ASP A 361           
SHEET    3   G 3 SER A 305  LYS A 308 -1  N  LYS A 308   O  GLN A 321           
SHEET    1   H 3 VAL A 334  ALA A 337  0                                        
SHEET    2   H 3 GLY A 372  VAL A 378 -1  N  ILE A 377   O  ILE A 335           
SHEET    3   H 3 LEU A 385  LYS A 391 -1  N  LYS A 391   O  GLY A 372           
SHEET    1   I 2 ASN A  62  THR A  66  0                                        
SHEET    2   I 2 LYS A 118  LYS A 123 -1  N  LYS A 123   O  ASN A  62           
SHEET    1   J 4 THR B 502  LYS B 506  0                                        
SHEET    2   J 4 TRP B 509  ASN B 513 -1  N  ASN B 513   O  THR B 502           
SHEET    3   J 4 VAL B 571  GLY B 576  1  N  ARG B 572   O  LEU B 510           
SHEET    4   J 4 SER B 544  ASN B 548 -1  N  TYR B 547   O  VAL B 573           
SHEET    1   K 4 THR B 522  VAL B 525  0                                        
SHEET    2   K 4 GLY B 528  THR B 532 -1  N  CYS B 530   O  PHE B 523           
SHEET    3   K 4 CYS B 563  TYR B 566 -1  N  TYR B 566   O  ASN B 529           
SHEET    4   K 4 PRO B 550  LEU B 552  1  N  PRO B 550   O  CYS B 565           
SHEET    1   L 6 ALA D 398  TRP D 400  0                                        
SHEET    2   L 6 ARG D   9  GLY D  14  1  N  ARG D   9   O  GLY D 399           
SHEET    3   L 6 CYS D  30  ALA D  35  1  N  CYS D  30   O  ASP D  10           
SHEET    4   L 6 LEU D  41  ILE D  50 -1  N  ILE D  43   O  VAL D  31           
SHEET    5   L 6 ILE D 135  LEU D 143 -1  N  GLN D 142   O  ASP D  42           
SHEET    6   L 6 LYS D 157  ASP D 162 -1  N  PHE D 161   O  TYR D 137           
SHEET    1   M 4 TRP D  20  GLU D  26  0                                        
SHEET    2   M 4 HIS D 280  LYS D 286 -1  N  VAL D 285   O  VAL D  21           
SHEET    3   M 4 GLY D 176  GLN D 185 -1  N  GLN D 185   O  HIS D 280           
SHEET    4   M 4 GLN D 168  PHE D 172 -1  N  PHE D 172   O  GLY D 176           
SHEET    1   N 2 ALA D  49  ASP D  51  0                                        
SHEET    2   N 2 LEU D 273  LYS D 275 -1  N  TYR D 274   O  ILE D  50           
SHEET    1   O 3 VAL D  68  LYS D  73  0                                        
SHEET    2   O 3 GLY D 109  LYS D 118 -1  N  CYS D 116   O  LYS D  69           
SHEET    3   O 3 ASN D  90  ARG D  99 -1  N  ARG D  99   O  GLY D 109           
SHEET    1   P 5 MET D 262  VAL D 264  0                                        
SHEET    2   P 5 GLU D 201  ASP D 206 -1  N  ILE D 204   O  MET D 262           
SHEET    3   P 5 SER D 193  MET D 198 -1  N  MET D 198   O  GLU D 201           
SHEET    4   P 5 SER D 124  GLU D 129 -1  N  PHE D 128   O  ILE D 195           
SHEET    5   P 5 GLU D  55  CYS D  60 -1  N  VAL D  59   O  MET D 125           
SHEET    1   Q 2 VAL D 232  PHE D 234  0                                        
SHEET    2   Q 2 VAL D 244  ALA D 246 -1  N  LEU D 245   O  GLU D 233           
SHEET    1   R 3 ASP D 361  VAL D 367  0                                        
SHEET    2   R 3 VAL D 318  VAL D 324 -1  N  VAL D 324   O  ASP D 361           
SHEET    3   R 3 SER D 305  LYS D 308 -1  N  LYS D 308   O  GLN D 321           
SHEET    1   S 3 VAL D 334  ALA D 337  0                                        
SHEET    2   S 3 GLY D 372  VAL D 378 -1  N  ILE D 377   O  ILE D 335           
SHEET    3   S 3 LEU D 385  LYS D 391 -1  N  LYS D 391   O  GLY D 372           
SHEET    1   T 2 ASN D  62  THR D  66  0                                        
SHEET    2   T 2 LYS D 118  LYS D 123 -1  N  LYS D 123   O  ASN D  62           
SHEET    1   U 4 THR E 502  LYS E 506  0                                        
SHEET    2   U 4 TRP E 509  ASN E 513 -1  N  ASN E 513   O  THR E 502           
SHEET    3   U 4 VAL E 571  GLY E 576  1  N  ARG E 572   O  LEU E 510           
SHEET    4   U 4 SER E 544  CYS E 549 -1  N  CYS E 549   O  VAL E 571           
SHEET    1   V 4 THR E 522  VAL E 525  0                                        
SHEET    2   V 4 GLY E 528  THR E 532 -1  N  CYS E 530   O  PHE E 523           
SHEET    3   V 4 CYS E 563  TYR E 566 -1  N  TYR E 566   O  ASN E 529           
SHEET    4   V 4 PRO E 550  LEU E 552  1  N  PRO E 550   O  CYS E 565           
SSBOND   1 CYS A    3    CYS A   30                          1555   1555  2.03  
SSBOND   2 CYS A   60    CYS A  121                          1555   1555  2.03  
SSBOND   3 CYS A   74    CYS A  105                          1555   1555  2.03  
SSBOND   4 CYS A   92    CYS A  116                          1555   1555  2.03  
SSBOND   5 CYS A  182    CYS A  283                          1555   1555  2.03  
SSBOND   6 CYS A  300    CYS A  330                          1555   1555  2.03  
SSBOND   7 CYS B  530    CYS B  565                          1555   1555  2.03  
SSBOND   8 CYS B  541    CYS B  578                          1555   1555  2.03  
SSBOND   9 CYS B  549    CYS B  563                          1555   1555  2.03  
SSBOND  10 CYS D    3    CYS D   30                          1555   1555  2.03  
SSBOND  11 CYS D   60    CYS D  121                          1555   1555  2.03  
SSBOND  12 CYS D   74    CYS D  105                          1555   1555  2.04  
SSBOND  13 CYS D   92    CYS D  116                          1555   1555  2.03  
SSBOND  14 CYS D  182    CYS D  283                          1555   1555  2.03  
SSBOND  15 CYS D  300    CYS D  330                          1555   1555  2.03  
SSBOND  16 CYS E  530    CYS E  565                          1555   1555  2.03  
SSBOND  17 CYS E  541    CYS E  578                          1555   1555  2.04  
SSBOND  18 CYS E  549    CYS E  563                          1555   1555  2.03  
LINK         ND2 ASN B 513                 C1  NAG B 701     1555   1555  1.43  
LINK         ND2 ASN B 529                 C1  NAG B 703     1555   1555  1.44  
LINK         ND2 ASN E 513                 C1  NAG E 701     1555   1555  1.43  
LINK         ND2 ASN E 529                 C1  NAG E 704     1555   1555  1.45  
LINK         O4  NAG B 701                 C1  NAG B 702     1555   1555  1.44  
LINK         O4  NAG B 703                 C1  NAG B 705     1555   1555  1.44  
LINK         O6  NAG B 703                 C1  FUC B 704     1555   1555  1.44  
LINK         O4  NAG B 705                 C1  BMA B 706     1555   1555  1.44  
LINK         O3  BMA B 706                 C1  MAN B 708     1555   1555  1.44  
LINK         O6  BMA B 706                 C1  MAN B 707     1555   1555  1.44  
LINK         O4  NAG E 701                 C1  NAG E 702     1555   1555  1.44  
LINK         O4  NAG E 702                 C1  BMA E 703     1555   1555  1.44  
LINK         O4  NAG E 704                 C1  NAG E 706     1555   1555  1.44  
LINK         O6  NAG E 704                 C1  FUC E 705     1555   1555  1.44  
LINK         O4  NAG E 706                 C1  BMA E 707     1555   1555  1.44  
LINK         O3  BMA E 707                 C1  MAN E 709     1555   1555  1.44  
LINK         O6  BMA E 707                 C1  MAN E 708     1555   1555  1.44  
CISPEP   1 ALA A  328    PRO A  329          0        -1.11                     
CISPEP   2 ALA D  328    PRO D  329          0        -1.27                     
SITE     1 AC1  4 PHE A 172  THR A 173  GLY A 174  GLY A 176                    
SITE     1 AC2  5 GLU A 227  MET A 228  HIS A 229  GOL A 512                    
SITE     2 AC2  5 HOH A 609                                                     
SITE     1 AC3  2 ARG A 207  GLN A 211                                          
SITE     1 AC4  2 LYS A 326  ASN A 359                                          
SITE     1 AC5  6 CYS A  92  LYS A  93  ARG A  94  LYS A 303                    
SITE     2 AC5  6 HOH A 606  HOH A 633                                          
SITE     1 AC6  3 HIS A  67  HOH A 605  HOH A 627                               
SITE     1 AC7  4 LYS A 293  GLY A 294  THR A 295  SER A 296                    
SITE     1 AC8  3 LYS A  93  THR A  95  PRO A 237                               
SITE     1 AC9  3 ASN A 249  HOH A 613  HOH A 631                               
SITE     1 AD1  8 ALA A   1  HIS A 144  VAL A 145  GLY A 146                    
SITE     2 AD1  8 ALA A 147  THR A 351  LEU A 364  GLU A 366                    
SITE     1 AD2  5 GLY A 109  LYS A 110  ASP A 339  LEU A 340                    
SITE     2 AD2  5 TYR A 375                                                     
SITE     1 AD3  4 ARG A 226  GLU A 227  LYS A 323  SO4 A 502                    
SITE     1 AD4  3 ASP A  72  ARG A  99  ASN B 551                               
SITE     1 AD5  5 ARG A 243  HOH A 607  GLU B 536  HOH B 827                    
SITE     2 AD5  5 HOH B 830                                                     
SITE     1 AD6  3 LYS A  73  ARG B 508  HOH B 823                               
SITE     1 AD7  2 CYS B 578  ASP B 579                                          
SITE     1 AD8  1 ARG B 508                                                     
SITE     1 AD9  5 GLU D 227  MET D 228  HIS D 229  LYS D 303                    
SITE     2 AD9  5 GOL D 514                                                     
SITE     1 AE1  4 PHE D 172  THR D 173  GLY D 174  GLY D 176                    
SITE     1 AE2  2 ASP D  72  ARG D  99                                          
SITE     1 AE3  3 TYR D 194  ARG D 207  GLN D 211                               
SITE     1 AE4  3 ASP D 206  ALA D 257  GLY D 260                               
SITE     1 AE5  2 LYS D  93  PHE D 234                                          
SITE     1 AE6  3 LYS D  73  GOL D 517  ARG E 508                               
SITE     1 AE7  3 ASN D  62  ASN D 249  HOH D 614                               
SITE     1 AE8  3 LYS D  93  THR D  95  PRO D 237                               
SITE     1 AE9  5 LEU D 292  LYS D 293  GLY D 294  THR D 295                    
SITE     2 AE9  5 SER D 296                                                     
SITE     1 AF1  3 LYS D 326  GLY D 327  ASN D 359                               
SITE     1 AF2  8 ALA D   1  HIS D 144  VAL D 145  GLY D 146                    
SITE     2 AF2  8 ALA D 147  THR D 351  LEU D 364  GLU D 366                    
SITE     1 AF3  1 ASN D 345                                                     
SITE     1 AF4  3 ARG D 226  GLU D 227  SO4 D 501                               
SITE     1 AF5  2 CYS D 121  TRP D 225                                          
SITE     1 AF6  2 ILE D  12  THR D  24                                          
SITE     1 AF7  7 ASN D  71  LYS D  73  ALA D  80  HIS D  81                    
SITE     2 AF7  7 SO4 D 507  ARG E 508  TRP E 509                               
SITE     1 AF8  2 ASP E 579  HOH E 807                                          
SITE     1 AF9  6 LYS B 506  LEU B 511  ASN B 513  TRP B 540                    
SITE     2 AF9  6 HOH B 811  HOH B 813                                          
SITE     1 AG1 11 HIS A 402  THR B 522  ASN B 529  PRO B 554                    
SITE     2 AG1 11 ARG B 555  TYR B 566  HOH B 826  ASP D   8                    
SITE     3 AG1 11 ASP D  10  ASP D 396  LYS D 397                               
SITE     1 AG2  5 LYS E 506  LEU E 511  ASN E 513  TRP E 540                    
SITE     2 AG2  5 HOH E 813                                                     
SITE     1 AG3 14 PHE A 371  ASP A 395  ASP A 396  TRP A 400                    
SITE     2 AG3 14 THR E 522  ASN E 529  PRO E 554  ARG E 555                    
SITE     3 AG3 14 GLU E 557  TYR E 566  HOH E 802  HOH E 806                    
SITE     4 AG3 14 HOH E 818  HOH E 820                                          
CRYST1   99.880   99.880  238.824  90.00  90.00  90.00 P 41          8          
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      0.010012  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010012  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004187        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system