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Database: PDB
Entry: 5K6K
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Original site: 5K6K 
HEADER    VIRAL PROTEIN                           24-MAY-16   5K6K              
TITLE     ZIKA VIRUS NON-STRUCTURAL PROTEIN 1 (NS1)                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ZIKA VIRUS PROTEIN;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ZIKA VIRUS;                                     
SOURCE   3 ORGANISM_COMMON: ZIKV;                                               
SOURCE   4 ORGANISM_TAXID: 64320;                                               
SOURCE   5 STRAIN: MR 766;                                                      
SOURCE   6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469                                       
KEYWDS    VIRAL PROTEIN                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.L.AKEY,W.C.BROWN,J.L.SMITH                                          
REVDAT   5   22-NOV-17 5K6K    1       REMARK                                   
REVDAT   4   21-SEP-16 5K6K    1       JRNL                                     
REVDAT   3   10-AUG-16 5K6K    1       JRNL                                     
REVDAT   2   13-JUL-16 5K6K    1       AUTHOR JRNL                              
REVDAT   1   06-JUL-16 5K6K    0                                                
JRNL        AUTH   W.C.BROWN,D.L.AKEY,J.R.KONWERSKI,J.T.TARRASCH,G.SKINIOTIS,   
JRNL        AUTH 2 R.J.KUHN,J.L.SMITH                                           
JRNL        TITL   EXTENDED SURFACE FOR MEMBRANE ASSOCIATION IN ZIKA VIRUS NS1  
JRNL        TITL 2 STRUCTURE.                                                   
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  23   865 2016              
JRNL        REFN                   ESSN 1545-9985                               
JRNL        PMID   27455458                                                     
JRNL        DOI    10.1038/NSMB.3268                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.89 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 1.89                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.08                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 74473                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.150                           
REMARK   3   R VALUE            (WORKING SET) : 0.149                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.810                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2089                            
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 48.0955 -  4.6600    1.00     5072   146  0.1456 0.1641        
REMARK   3     2  4.6600 -  3.6992    1.00     4893   141  0.1127 0.1592        
REMARK   3     3  3.6992 -  3.2317    1.00     4852   142  0.1291 0.1756        
REMARK   3     4  3.2317 -  2.9363    1.00     4867   140  0.1381 0.1826        
REMARK   3     5  2.9363 -  2.7258    1.00     4799   141  0.1466 0.1890        
REMARK   3     6  2.7258 -  2.5651    1.00     4828   137  0.1532 0.1890        
REMARK   3     7  2.5651 -  2.4367    1.00     4802   138  0.1537 0.2055        
REMARK   3     8  2.4367 -  2.3306    1.00     4799   137  0.1579 0.2276        
REMARK   3     9  2.3306 -  2.2409    1.00     4779   139  0.1697 0.1883        
REMARK   3    10  2.2409 -  2.1636    1.00     4828   139  0.1704 0.1839        
REMARK   3    11  2.1636 -  2.0959    1.00     4781   134  0.1743 0.2341        
REMARK   3    12  2.0959 -  2.0360    1.00     4772   137  0.1872 0.2359        
REMARK   3    13  2.0360 -  1.9824    1.00     4780   142  0.2129 0.2549        
REMARK   3    14  1.9824 -  1.9340    1.00     4763   140  0.2557 0.3156        
REMARK   3    15  1.9340 -  1.8901    1.00     4769   136  0.3050 0.3598        
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)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.920           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.05                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.61                          
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      :  0.007           5933                                  
REMARK   3   ANGLE     :  0.838           8069                                  
REMARK   3   CHIRALITY :  0.055            850                                  
REMARK   3   PLANARITY :  0.005           1035                                  
REMARK   3   DIHEDRAL  : 18.003           3539                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID -5 THROUGH 180 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.2237 -38.7751 -14.1706              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2155 T22:   0.2311                                     
REMARK   3      T33:   0.2535 T12:   0.0236                                     
REMARK   3      T13:  -0.0313 T23:   0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8188 L22:   1.1370                                     
REMARK   3      L33:   0.8099 L12:   1.3907                                     
REMARK   3      L13:   0.3973 L23:   0.0046                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0568 S12:  -0.0841 S13:  -0.2635                       
REMARK   3      S21:   0.0821 S22:  -0.0306 S23:  -0.2343                       
REMARK   3      S31:   0.0204 S32:   0.1330 S33:  -0.0199                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 181 THROUGH 352 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.1421 -23.9272 -11.8706              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1858 T22:   0.2159                                     
REMARK   3      T33:   0.1965 T12:  -0.0099                                     
REMARK   3      T13:  -0.0162 T23:   0.0228                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4647 L22:   2.1046                                     
REMARK   3      L33:   2.0336 L12:  -0.3311                                     
REMARK   3      L13:  -0.3112 L23:   1.3083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0044 S12:  -0.0692 S13:   0.0685                       
REMARK   3      S21:   0.0009 S22:   0.0025 S23:   0.0532                       
REMARK   3      S31:  -0.1672 S32:  -0.0659 S33:  -0.0006                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 31 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -26.1711 -55.0785 -17.5835              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2462 T22:   0.1855                                     
REMARK   3      T33:   0.2511 T12:  -0.0321                                     
REMARK   3      T13:  -0.0328 T23:   0.0708                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3246 L22:   2.5628                                     
REMARK   3      L33:   4.2982 L12:   0.2773                                     
REMARK   3      L13:   1.3754 L23:   1.0164                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2611 S12:  -0.2718 S13:  -0.2838                       
REMARK   3      S21:   0.1708 S22:  -0.0963 S23:  -0.1454                       
REMARK   3      S31:   0.3299 S32:  -0.3158 S33:  -0.1400                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 32 THROUGH 180 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -56.8414 -51.5902 -31.0621              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1900 T22:   0.2118                                     
REMARK   3      T33:   0.2252 T12:  -0.0172                                     
REMARK   3      T13:   0.0024 T23:   0.0206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9633 L22:   2.5514                                     
REMARK   3      L33:   1.7238 L12:   0.9270                                     
REMARK   3      L13:  -0.3927 L23:  -0.5591                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0845 S12:  -0.2606 S13:  -0.1545                       
REMARK   3      S21:   0.1607 S22:  -0.0678 S23:   0.2528                       
REMARK   3      S31:   0.1387 S32:  -0.1060 S33:  -0.0162                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 181 THROUGH 352 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -26.2940 -51.0775 -44.0288              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2217 T22:   0.1904                                     
REMARK   3      T33:   0.2229 T12:   0.0008                                     
REMARK   3      T13:  -0.0060 T23:   0.0227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4988 L22:   1.0594                                     
REMARK   3      L33:   3.6290 L12:  -0.1204                                     
REMARK   3      L13:  -0.4783 L23:   0.9921                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0150 S12:   0.0514 S13:  -0.0827                       
REMARK   3      S21:  -0.1250 S22:  -0.0131 S23:  -0.0415                       
REMARK   3      S31:   0.1519 S32:   0.1342 S33:   0.0338                       
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 5K6K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000221837.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-APR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE, XDS                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 74493                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.890                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.080                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.50                              
REMARK 200  R MERGE                    (I) : 0.12500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.2200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.30                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.61300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.330                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.6.0                                          
REMARK 200 STARTING MODEL: 4O6D                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350 150 MM NH3SO4 100 MM TRIS   
REMARK 280  8.5, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       48.08000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       65.22000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       73.97500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       48.08000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       65.22000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       73.97500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       48.08000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       65.22000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       73.97500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       48.08000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       65.22000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       73.97500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL                        
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18120 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 60510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -133.0 KCAL/MOL                       
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   BIOMT1   2 -1.000000  0.000000  0.000000      -96.16000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000     -130.44000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17800 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 60830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -117.0 KCAL/MOL                       
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 563  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 950  LIES ON A SPECIAL POSITION.                          
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     ALA A   -23                                                      
REMARK 465     HIS A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     GLY A   -14                                                      
REMARK 465     VAL A   -13                                                      
REMARK 465     ASP A   -12                                                      
REMARK 465     LEU A   -11                                                      
REMARK 465     GLY A   -10                                                      
REMARK 465     THR A    -9                                                      
REMARK 465     GLU A    -8                                                      
REMARK 465     ASN A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     HIS A   113                                                      
REMARK 465     GLY A   114                                                      
REMARK 465     TRP A   115                                                      
REMARK 465     LYS A   116                                                      
REMARK 465     ALA A   117                                                      
REMARK 465     TRP A   118                                                      
REMARK 465     GLY A   119                                                      
REMARK 465     LYS A   120                                                      
REMARK 465     ALA B   -23                                                      
REMARK 465     HIS B   -22                                                      
REMARK 465     HIS B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     GLY B   -14                                                      
REMARK 465     VAL B   -13                                                      
REMARK 465     ASP B   -12                                                      
REMARK 465     LEU B   -11                                                      
REMARK 465     GLY B   -10                                                      
REMARK 465     THR B    -9                                                      
REMARK 465     GLU B    -8                                                      
REMARK 465     ASN B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     TYR B    -5                                                      
REMARK 465     PHE B    -4                                                      
REMARK 465     GLN B    -3                                                      
REMARK 465     SER B    -2                                                      
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     TYR A  -5    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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   538     O    HOH B   899              2.08            
REMARK 500   O    HOH A   895     O    HOH A   940              2.08            
REMARK 500   O    HOH B   650     O    HOH B   897              2.14            
REMARK 500   O    HOH B   829     O    HOH B   938              2.14            
REMARK 500   O    HOH B   509     O    HOH B   914              2.15            
REMARK 500   O    HOH B   738     O    HOH B   947              2.15            
REMARK 500   O    LEU A   145     O    HOH A   501              2.16            
REMARK 500   OD2  ASP B    24     O    HOH B   501              2.17            
REMARK 500   O    HOH A   514     O    HOH A   846              2.17            
REMARK 500   O    HOH B   871     O    HOH B   916              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   539     O    HOH B   947     8544     2.11            
REMARK 500   O    HOH B   713     O    HOH B   938     2445     2.17            
REMARK 500   O    HOH B   665     O    HOH B   895     2445     2.17            
REMARK 500   O    HOH B   842     O    HOH B   876     2445     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    ASP A 136     -147.97     56.99                                   
REMARK 500    ASP A 197     -157.67   -143.92                                   
REMARK 500    ASN A 207     -121.36    -96.54                                   
REMARK 500    TRP A 232       76.42     48.98                                   
REMARK 500    ASN A 255       45.98   -100.57                                   
REMARK 500    GLU A 278      140.81   -175.72                                   
REMARK 500    GLU A 315       28.17   -157.89                                   
REMARK 500    ASP B 136     -142.39     48.05                                   
REMARK 500    ASP B 197     -155.30   -147.81                                   
REMARK 500    ASN B 207     -128.32    -98.29                                   
REMARK 500    TRP B 232       74.97     52.02                                   
REMARK 500    ASN B 255       41.89    -98.44                                   
REMARK 500    GLU B 278      140.70   -171.03                                   
REMARK 500    GLU B 315       34.58   -157.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1006        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH B1041        DISTANCE =  6.69 ANGSTROMS                       
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 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 401 bound   
REMARK 800  to ASN A 130                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 402 bound   
REMARK 800  to ASN A 207                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 401 bound   
REMARK 800  to ASN B 130                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 402 bound   
REMARK 800  to ASN B 207                                                        
DBREF  5K6K A    0   352  UNP    Q32ZE1   POLG_ZIKV      790   1142             
DBREF  5K6K B    0   352  UNP    Q32ZE1   POLG_ZIKV      790   1142             
SEQADV 5K6K ALA A  -23  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS A  -22  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS A  -21  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS A  -20  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS A  -19  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS A  -18  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS A  -17  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K SER A  -16  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K SER A  -15  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K GLY A  -14  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K VAL A  -13  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K ASP A  -12  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K LEU A  -11  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K GLY A  -10  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K THR A   -9  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K GLU A   -8  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K ASN A   -7  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K LEU A   -6  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K TYR A   -5  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K PHE A   -4  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K GLN A   -3  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K SER A   -2  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K ASN A   -1  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K ALA B  -23  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS B  -22  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS B  -21  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS B  -20  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS B  -19  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS B  -18  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS B  -17  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K SER B  -16  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K SER B  -15  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K GLY B  -14  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K VAL B  -13  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K ASP B  -12  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K LEU B  -11  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K GLY B  -10  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K THR B   -9  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K GLU B   -8  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K ASN B   -7  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K LEU B   -6  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K TYR B   -5  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K PHE B   -4  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K GLN B   -3  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K SER B   -2  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K ASN B   -1  UNP  Q32ZE1              EXPRESSION TAG                 
SEQRES   1 A  376  ALA HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  376  GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA ASP VAL          
SEQRES   3 A  376  GLY CYS SER VAL ASP PHE SER LYS LYS GLU THR ARG CYS          
SEQRES   4 A  376  GLY THR GLY VAL PHE ILE TYR ASN ASP VAL GLU ALA TRP          
SEQRES   5 A  376  ARG ASP ARG TYR LYS TYR HIS PRO ASP SER PRO ARG ARG          
SEQRES   6 A  376  LEU ALA ALA ALA VAL LYS GLN ALA TRP GLU GLU GLY ILE          
SEQRES   7 A  376  CYS GLY ILE SER SER VAL SER ARG MET GLU ASN ILE MET          
SEQRES   8 A  376  TRP LYS SER VAL GLU GLY GLU LEU ASN ALA ILE LEU GLU          
SEQRES   9 A  376  GLU ASN GLY VAL GLN LEU THR VAL VAL VAL GLY SER VAL          
SEQRES  10 A  376  LYS ASN PRO MET TRP ARG GLY PRO GLN ARG LEU PRO VAL          
SEQRES  11 A  376  PRO VAL ASN GLU LEU PRO HIS GLY TRP LYS ALA TRP GLY          
SEQRES  12 A  376  LYS SER TYR PHE VAL ARG ALA ALA LYS THR ASN ASN SER          
SEQRES  13 A  376  PHE VAL VAL ASP GLY ASP THR LEU LYS GLU CYS PRO LEU          
SEQRES  14 A  376  GLU HIS ARG ALA TRP ASN SER PHE LEU VAL GLU ASP HIS          
SEQRES  15 A  376  GLY PHE GLY VAL PHE HIS THR SER VAL TRP LEU LYS VAL          
SEQRES  16 A  376  ARG GLU ASP TYR SER LEU GLU CYS ASP PRO ALA VAL ILE          
SEQRES  17 A  376  GLY THR ALA VAL LYS GLY ARG GLU ALA ALA HIS SER ASP          
SEQRES  18 A  376  LEU GLY TYR TRP ILE GLU SER GLU LYS ASN ASP THR TRP          
SEQRES  19 A  376  ARG LEU LYS ARG ALA HIS LEU ILE GLU MET LYS THR CYS          
SEQRES  20 A  376  GLU TRP PRO LYS SER HIS THR LEU TRP THR ASP GLY VAL          
SEQRES  21 A  376  GLU GLU SER ASP LEU ILE ILE PRO LYS SER LEU ALA GLY          
SEQRES  22 A  376  PRO LEU SER HIS HIS ASN THR ARG GLU GLY TYR ARG THR          
SEQRES  23 A  376  GLN VAL LYS GLY PRO TRP HIS SER GLU GLU LEU GLU ILE          
SEQRES  24 A  376  ARG PHE GLU GLU CYS PRO GLY THR LYS VAL TYR VAL GLU          
SEQRES  25 A  376  GLU THR CYS GLY THR ARG GLY PRO SER LEU ARG SER THR          
SEQRES  26 A  376  THR ALA SER GLY ARG VAL ILE GLU GLU TRP CYS CYS ARG          
SEQRES  27 A  376  GLU CYS THR MET PRO PRO LEU SER PHE ARG ALA LYS ASP          
SEQRES  28 A  376  GLY CYS TRP TYR GLY MET GLU ILE ARG PRO ARG LYS GLU          
SEQRES  29 A  376  PRO GLU SER ASN LEU VAL ARG SER MET VAL THR ALA              
SEQRES   1 B  376  ALA HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  376  GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA ASP VAL          
SEQRES   3 B  376  GLY CYS SER VAL ASP PHE SER LYS LYS GLU THR ARG CYS          
SEQRES   4 B  376  GLY THR GLY VAL PHE ILE TYR ASN ASP VAL GLU ALA TRP          
SEQRES   5 B  376  ARG ASP ARG TYR LYS TYR HIS PRO ASP SER PRO ARG ARG          
SEQRES   6 B  376  LEU ALA ALA ALA VAL LYS GLN ALA TRP GLU GLU GLY ILE          
SEQRES   7 B  376  CYS GLY ILE SER SER VAL SER ARG MET GLU ASN ILE MET          
SEQRES   8 B  376  TRP LYS SER VAL GLU GLY GLU LEU ASN ALA ILE LEU GLU          
SEQRES   9 B  376  GLU ASN GLY VAL GLN LEU THR VAL VAL VAL GLY SER VAL          
SEQRES  10 B  376  LYS ASN PRO MET TRP ARG GLY PRO GLN ARG LEU PRO VAL          
SEQRES  11 B  376  PRO VAL ASN GLU LEU PRO HIS GLY TRP LYS ALA TRP GLY          
SEQRES  12 B  376  LYS SER TYR PHE VAL ARG ALA ALA LYS THR ASN ASN SER          
SEQRES  13 B  376  PHE VAL VAL ASP GLY ASP THR LEU LYS GLU CYS PRO LEU          
SEQRES  14 B  376  GLU HIS ARG ALA TRP ASN SER PHE LEU VAL GLU ASP HIS          
SEQRES  15 B  376  GLY PHE GLY VAL PHE HIS THR SER VAL TRP LEU LYS VAL          
SEQRES  16 B  376  ARG GLU ASP TYR SER LEU GLU CYS ASP PRO ALA VAL ILE          
SEQRES  17 B  376  GLY THR ALA VAL LYS GLY ARG GLU ALA ALA HIS SER ASP          
SEQRES  18 B  376  LEU GLY TYR TRP ILE GLU SER GLU LYS ASN ASP THR TRP          
SEQRES  19 B  376  ARG LEU LYS ARG ALA HIS LEU ILE GLU MET LYS THR CYS          
SEQRES  20 B  376  GLU TRP PRO LYS SER HIS THR LEU TRP THR ASP GLY VAL          
SEQRES  21 B  376  GLU GLU SER ASP LEU ILE ILE PRO LYS SER LEU ALA GLY          
SEQRES  22 B  376  PRO LEU SER HIS HIS ASN THR ARG GLU GLY TYR ARG THR          
SEQRES  23 B  376  GLN VAL LYS GLY PRO TRP HIS SER GLU GLU LEU GLU ILE          
SEQRES  24 B  376  ARG PHE GLU GLU CYS PRO GLY THR LYS VAL TYR VAL GLU          
SEQRES  25 B  376  GLU THR CYS GLY THR ARG GLY PRO SER LEU ARG SER THR          
SEQRES  26 B  376  THR ALA SER GLY ARG VAL ILE GLU GLU TRP CYS CYS ARG          
SEQRES  27 B  376  GLU CYS THR MET PRO PRO LEU SER PHE ARG ALA LYS ASP          
SEQRES  28 B  376  GLY CYS TRP TYR GLY MET GLU ILE ARG PRO ARG LYS GLU          
SEQRES  29 B  376  PRO GLU SER ASN LEU VAL ARG SER MET VAL THR ALA              
HET    NAG  A 401      14                                                       
HET    NAG  A 402      14                                                       
HET    SO4  A 403       5                                                       
HET    NAG  B 401      14                                                       
HET    NAG  B 402      14                                                       
HET    SO4  B 403       5                                                       
HET    SO4  B 404       5                                                       
HET    SO4  B 405       5                                                       
HET    SO4  B 406       5                                                       
HET    GOL  B 407       6                                                       
HET    GOL  B 408       6                                                       
HET    GOL  B 409       6                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   5  SO4    5(O4 S 2-)                                                   
FORMUL  12  GOL    3(C3 H8 O3)                                                  
FORMUL  15  HOH   *1047(H2 O)                                                   
HELIX    1 AA1 SER A   38  GLU A   52  1                                  15    
HELIX    2 AA2 SER A   61  ASN A   82  1                                  22    
HELIX    3 AA3 PRO A  144  GLU A  146  5                                   3    
HELIX    4 AA4 ASP A  180  VAL A  183  5                                   4    
HELIX    5 AA5 PRO A  226  THR A  230  5                                   5    
HELIX    6 AA6 GLU A  237  LEU A  241  5                                   5    
HELIX    7 AA7 PRO A  244  ALA A  248  5                                   5    
HELIX    8 AA8 SER A  252  THR A  256  5                                   5    
HELIX    9 AA9 PRO A  341  LEU A  345  5                                   5    
HELIX   10 AB1 SER B   38  GLU B   52  1                                  15    
HELIX   11 AB2 SER B   61  ASN B   82  1                                  22    
HELIX   12 AB3 GLY B  119  PHE B  123  5                                   5    
HELIX   13 AB4 PRO B  144  GLU B  146  5                                   3    
HELIX   14 AB5 ASP B  180  VAL B  183  5                                   4    
HELIX   15 AB6 PRO B  226  THR B  230  5                                   5    
HELIX   16 AB7 GLU B  237  LEU B  241  5                                   5    
HELIX   17 AB8 PRO B  244  ALA B  248  5                                   5    
HELIX   18 AB9 SER B  252  THR B  256  5                                   5    
HELIX   19 AC1 PRO B  341  LEU B  345  5                                   5    
SHEET    1 AA1 5 ASP A   1  ASP A   7  0                                        
SHEET    2 AA1 5 GLU A  12  TYR A  22 -1  O  GLU A  12   N  ASP A   7           
SHEET    3 AA1 5 GLU B  12  TYR B  22 -1  O  ILE B  21   N  VAL A  19           
SHEET    4 AA1 5 ASP B   1  ASP B   7 -1  N  ASP B   7   O  GLU B  12           
SHEET    5 AA1 5 ASP A   1  ASP A   7 -1  N  VAL A   6   O  VAL B   2           
SHEET    1 AA2 3 TYR A  32  PRO A  36  0                                        
SHEET    2 AA2 3 THR A 165  VAL A 171  1  O  VAL A 167   N  HIS A  35           
SHEET    3 AA2 3 PHE A 153  GLY A 159 -1  N  GLU A 156   O  TRP A 168           
SHEET    1 AA3 4 THR A  87  VAL A  90  0                                        
SHEET    2 AA3 4 SER A 132  VAL A 135  1  O  PHE A 133   N  THR A  87           
SHEET    3 AA3 4 GLY A  56  ILE A  57  1  N  ILE A  57   O  VAL A 134           
SHEET    4 AA3 4 ARG A 148  ALA A 149  1  O  ALA A 149   N  GLY A  56           
SHEET    1 AA414 GLY A 328  TYR A 331  0                                        
SHEET    2 AA414 LEU A 321  ALA A 325 -1  N  PHE A 323   O  TRP A 330           
SHEET    3 AA414 LEU A 273  PHE A 277 -1  N  GLU A 274   O  ARG A 324           
SHEET    4 AA414 TRP A 210  LEU A 217 -1  N  LEU A 217   O  LEU A 273           
SHEET    5 AA414 TYR A 200  LYS A 206 -1  N  GLU A 203   O  LYS A 213           
SHEET    6 AA414 GLU A 192  SER A 196 -1  N  HIS A 195   O  ILE A 202           
SHEET    7 AA414 GLY A 185  LYS A 189 -1  N  ALA A 187   O  ALA A 194           
SHEET    8 AA414 GLY B 185  LYS B 189 -1  O  VAL B 188   N  THR A 186           
SHEET    9 AA414 GLU B 192  SER B 196 -1  O  ALA B 194   N  ALA B 187           
SHEET   10 AA414 TYR B 200  LYS B 206 -1  O  ILE B 202   N  HIS B 195           
SHEET   11 AA414 TRP B 210  LEU B 217 -1  O  LYS B 213   N  GLU B 203           
SHEET   12 AA414 LEU B 273  PHE B 277 -1  O  ILE B 275   N  ALA B 215           
SHEET   13 AA414 LEU B 321  ALA B 325 -1  O  ARG B 324   N  GLU B 274           
SHEET   14 AA414 GLY B 328  TYR B 331 -1  O  GLY B 328   N  ALA B 325           
SHEET    1 AA5 3 LYS A 284  VAL A 287  0                                        
SHEET    2 AA5 3 GLU A 310  CYS A 313  1  O  TRP A 311   N  LYS A 284           
SHEET    3 AA5 3 ARG A 336  PRO A 337 -1  O  ARG A 336   N  CYS A 312           
SHEET    1 AA6 3 TYR B  32  PRO B  36  0                                        
SHEET    2 AA6 3 THR B 165  VAL B 171  1  O  LEU B 169   N  HIS B  35           
SHEET    3 AA6 3 PHE B 153  GLY B 159 -1  N  GLU B 156   O  TRP B 168           
SHEET    1 AA7 4 THR B  87  VAL B  90  0                                        
SHEET    2 AA7 4 SER B 132  VAL B 135  1  O  VAL B 135   N  VAL B  89           
SHEET    3 AA7 4 GLY B  56  ILE B  57  1  N  ILE B  57   O  VAL B 134           
SHEET    4 AA7 4 ARG B 148  ALA B 149  1  O  ALA B 149   N  GLY B  56           
SHEET    1 AA8 3 LYS B 284  VAL B 287  0                                        
SHEET    2 AA8 3 GLU B 310  CYS B 313  1  O  TRP B 311   N  LYS B 284           
SHEET    3 AA8 3 ARG B 336  PRO B 337 -1  O  ARG B 336   N  CYS B 312           
SSBOND   1 CYS A    4    CYS A   15                          1555   1555  2.05  
SSBOND   2 CYS A   55    CYS A  143                          1555   1555  2.04  
SSBOND   3 CYS A  179    CYS A  223                          1555   1555  2.06  
SSBOND   4 CYS A  280    CYS A  329                          1555   1555  2.05  
SSBOND   5 CYS A  291    CYS A  312                          1555   1555  2.08  
SSBOND   6 CYS A  313    CYS A  316                          1555   1555  2.05  
SSBOND   7 CYS B    4    CYS B   15                          1555   1555  2.03  
SSBOND   8 CYS B   55    CYS B  143                          1555   1555  2.03  
SSBOND   9 CYS B  179    CYS B  223                          1555   1555  2.07  
SSBOND  10 CYS B  280    CYS B  329                          1555   1555  2.06  
SSBOND  11 CYS B  291    CYS B  312                          1555   1555  2.07  
SSBOND  12 CYS B  313    CYS B  316                          1555   1555  2.05  
LINK         ND2 ASN A 130                 C1  NAG A 401     1555   1555  1.43  
LINK         ND2 ASN A 207                 C1  NAG A 402     1555   1555  1.44  
LINK         ND2 ASN B 130                 C1  NAG B 401     1555   1555  1.44  
LINK         ND2 ASN B 207                 C1  NAG B 402     1555   1555  1.44  
CISPEP   1 ASN A   95    PRO A   96          0        -5.82                     
CISPEP   2 MET A  318    PRO A  319          0        -4.47                     
CISPEP   3 ASN B   95    PRO B   96          0        -6.85                     
CISPEP   4 MET B  318    PRO B  319          0        -2.59                     
SITE     1 AC1  4 ARG A 261  ARG A 294  HOH A 507  HOH A 509                    
SITE     1 AC2 10 ALA A 303  SER A 304  PRO B 341  GLU B 342                    
SITE     2 AC2 10 SER B 343  HOH B 544  HOH B 584  HOH B 603                    
SITE     3 AC2 10 HOH B 643  HOH B 660                                          
SITE     1 AC3  5 THR B 302  SER B 304  ARG B 306  HOH B 524                    
SITE     2 AC3  5 HOH B 540                                                     
SITE     1 AC4  5 ARG B 261  ARG B 294  HOH B 507  HOH B 563                    
SITE     2 AC4  5 HOH B 853                                                     
SITE     1 AC5  6 ARG B 261  THR B 293  ARG B 294  ARG B 314                    
SITE     2 AC5  6 HOH B 507  HOH B 734                                          
SITE     1 AC6  6 GLU A 224  LYS A 245  GLU B  52  GLY B  53                    
SITE     2 AC6  6 GLN B 102  HIS B 147                                          
SITE     1 AC7  6 GLY A  53  LYS B 265  THR B 351  HOH B 504                    
SITE     2 AC7  6 HOH B 688  HOH B 861                                          
SITE     1 AC8  4 SER B  92  GLY B 137  ASP B 138  HOH B 666                    
SITE     1 AC9 12 ASN A 130  ARG A 299  ALA A 303  ASP A 327                    
SITE     2 AC9 12 HOH A 520  HOH A 584  HOH A 686  HOH A 706                    
SITE     3 AC9 12 HOH A 714  HOH A 775  HOH A 801  HOH A 940                    
SITE     1 AD1  6 ARG A 191  ASN A 207  ASP A 208  ARG A 211                    
SITE     2 AD1  6 HOH A 526  HOH A 850                                          
SITE     1 AD2  2 ASN B 130  HOH B 838                                          
SITE     1 AD3  4 ASN B 207  ARG B 211  HOH B 502  HOH B 602                    
CRYST1   96.160  130.440  147.950  90.00  90.00  90.00 I 2 2 2      16          
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      0.010399  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007666  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006759        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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