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Database: PDB
Entry: 5M3D
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Original site: 5M3D 
HEADER    CELL ADHESION                           14-OCT-16   5M3D              
TITLE     STRUCTURAL TUNING OF CD81LEL (SPACE GROUP P31)                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CD81 ANTIGEN;                                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 112-201;                                      
COMPND   5 SYNONYM: 26 KDA CELL SURFACE PROTEIN TAPA-1,TARGET OF THE            
COMPND   6 ANTIPROLIFERATIVE ANTIBODY 1,TETRASPANIN-28,TSPAN-28;                
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CD81, TAPA1, TSPAN28;                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;                                
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHLSEC                                    
KEYWDS    HUMAN CELLULAR RECEPTOR FOR HEPATITIS C VIRUS, CELL ADHESION          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.S.CUNHA,P.SFRISO,A.L.ROJAS,P.ROVERSI,A.HOSPITAL,M.OROZCO,           
AUTHOR   2 N.G.ABRESCIA                                                         
REVDAT   3   13-DEC-17 5M3D    1       AUTHOR JRNL                              
REVDAT   2   18-JAN-17 5M3D    1       JRNL                                     
REVDAT   1   14-DEC-16 5M3D    0                                                
JRNL        AUTH   E.S.CUNHA,P.SFRISO,A.L.ROJAS,P.ROVERSI,A.HOSPITAL,M.OROZCO,  
JRNL        AUTH 2 N.G.ABRESCIA                                                 
JRNL        TITL   MECHANISM OF STRUCTURAL TUNING OF THE HEPATITIS C VIRUS      
JRNL        TITL 2 HUMAN CELLULAR RECEPTOR CD81 LARGE EXTRACELLULAR LOOP.       
JRNL        REF    STRUCTURE                     V.  25    53 2017              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   27916518                                                     
JRNL        DOI    10.1016/J.STR.2016.11.003                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   K.KITADOKORO,D.BORDO,G.GALLI,R.PETRACCA,F.FALUGI,            
REMARK   1  AUTH 2 S.ABRIGNANI,G.GRANDI,M.BOLOGNESI                             
REMARK   1  TITL   CD81 EXTRACELLULAR DOMAIN 3D STRUCTURE: INSIGHT INTO THE     
REMARK   1  TITL 2 TETRASPANIN SUPERFAMILY STRUCTURAL MOTIFS.                   
REMARK   1  REF    EMBO J.                       V.  20    12 2001              
REMARK   1  REFN                   ISSN 0261-4189                               
REMARK   1  PMID   11226150                                                     
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   K.KITADOKORO,M.PONASSI,G.GALLI,R.PETRACCA,F.FALUGI,G.GRANDI, 
REMARK   1  AUTH 2 M.BOLOGNESI                                                  
REMARK   1  TITL   SUBUNIT ASSOCIATION AND CONFORMATIONAL FLEXIBILITY IN THE    
REMARK   1  TITL 2 HEAD SUBDOMAIN OF HUMAN CD81 LARGE EXTRACELLULAR LOOP.       
REMARK   1  REF    BIOL. CHEM.                   V. 383  1447 2002              
REMARK   1  REFN                   ISSN 1431-6730                               
REMARK   1  PMID   12437138                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.38 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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.38                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.97                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.250                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 14539                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 740                             
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 48.9843 -  4.0693    0.96     2707   135  0.1636 0.2060        
REMARK   3     2  4.0693 -  3.2301    0.98     2738   164  0.1628 0.2079        
REMARK   3     3  3.2301 -  2.8219    0.99     2782   139  0.1909 0.2547        
REMARK   3     4  2.8219 -  2.5639    0.99     2793   156  0.1940 0.2648        
REMARK   3     5  2.5639 -  2.3801    0.99     2779   146  0.2350 0.2895        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.040           
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      :  0.009           2810                                  
REMARK   3   ANGLE     :  1.009           3773                                  
REMARK   3   CHIRALITY :  0.036            442                                  
REMARK   3   PLANARITY :  0.004            489                                  
REMARK   3   DIHEDRAL  : 14.737           1005                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 113:157 OR RESID 189:202)           
REMARK   3    ORIGIN FOR THE GROUP (A): -22.9456 -21.0892   4.1491              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5959 T22:   0.4945                                     
REMARK   3      T33:   0.6228 T12:   0.0932                                     
REMARK   3      T13:   0.0273 T23:   0.0895                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7332 L22:   7.4793                                     
REMARK   3      L33:   5.5403 L12:  -2.3676                                     
REMARK   3      L13:   0.0508 L23:  -1.6865                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0434 S12:   0.2340 S13:   0.4144                       
REMARK   3      S21:  -0.4586 S22:  -0.3078 S23:  -0.9503                       
REMARK   3      S31:  -0.0918 S32:   0.6288 S33:   0.2395                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 158:188)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -25.5098 -32.8942  10.9578              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7139 T22:   0.6223                                     
REMARK   3      T33:   0.6973 T12:   0.1339                                     
REMARK   3      T13:   0.0890 T23:   0.1913                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5292 L22:   3.7022                                     
REMARK   3      L33:   3.4252 L12:   0.5987                                     
REMARK   3      L13:  -1.2299 L23:  -1.9372                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4684 S12:  -0.7745 S13:  -1.0698                       
REMARK   3      S21:   0.1258 S22:  -0.1079 S23:  -0.3008                       
REMARK   3      S31:   0.6533 S32:   0.0833 S33:   0.5647                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 113:157 OR RESID 189:202)           
REMARK   3    ORIGIN FOR THE GROUP (A):   6.8504 -30.3073  -7.2844              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3232 T22:   0.5171                                     
REMARK   3      T33:   0.5005 T12:  -0.0199                                     
REMARK   3      T13:  -0.0640 T23:   0.0687                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.0603 L22:   5.9552                                     
REMARK   3      L33:   6.5206 L12:   0.5761                                     
REMARK   3      L13:   0.8577 L23:   0.1926                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1845 S12:   0.6224 S13:   0.9159                       
REMARK   3      S21:  -0.1268 S22:  -0.3069 S23:  -0.0525                       
REMARK   3      S31:  -0.5465 S32:   0.3256 S33:   0.4396                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 158:188)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  15.7333 -38.5764  -0.5159              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5074 T22:   0.7335                                     
REMARK   3      T33:   0.6532 T12:  -0.0110                                     
REMARK   3      T13:  -0.1135 T23:   0.1568                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7777 L22:   2.9545                                     
REMARK   3      L33:   4.5977 L12:   0.3327                                     
REMARK   3      L13:   0.2902 L23:  -2.4907                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0572 S12:  -0.5891 S13:  -0.0735                       
REMARK   3      S21:   0.2083 S22:  -0.7031 S23:  -0.6949                       
REMARK   3      S31:   0.2573 S32:   0.8147 S33:   0.5643                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN C AND (RESID 114:157 OR RESID 189:202)           
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.4606 -33.0810 -13.2174              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3910 T22:   0.6501                                     
REMARK   3      T33:   0.5192 T12:   0.1169                                     
REMARK   3      T13:  -0.0893 T23:   0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1886 L22:   6.1499                                     
REMARK   3      L33:   5.4794 L12:   0.2392                                     
REMARK   3      L13:   1.0105 L23:  -0.1717                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0150 S12:   0.4284 S13:   0.6121                       
REMARK   3      S21:  -0.3264 S22:  -0.1896 S23:  -0.0217                       
REMARK   3      S31:  -0.1538 S32:  -0.0068 S33:   0.2796                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN C AND (RESID 158:188)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -16.6337 -41.9077  -9.3696              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6312 T22:   0.7207                                     
REMARK   3      T33:   0.8526 T12:   0.0692                                     
REMARK   3      T13:  -0.0996 T23:  -0.1040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4225 L22:   4.3894                                     
REMARK   3      L33:   4.0116 L12:   1.4232                                     
REMARK   3      L13:   0.9808 L23:  -0.8909                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0846 S12:  -0.5780 S13:  -0.4462                       
REMARK   3      S21:   0.0814 S22:  -0.4686 S23:   0.8238                       
REMARK   3      S31:   0.6795 S32:  -0.3344 S33:   0.2900                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN D AND (RESID 114:157 OR RESID 189:202)           
REMARK   3    ORIGIN FOR THE GROUP (A): -31.9047 -10.9892  -1.7281              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6623 T22:   0.3819                                     
REMARK   3      T33:   0.5349 T12:   0.0131                                     
REMARK   3      T13:  -0.0262 T23:   0.0796                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5627 L22:   7.0008                                     
REMARK   3      L33:   5.7007 L12:  -1.5939                                     
REMARK   3      L13:   0.1050 L23:  -0.0081                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1422 S12:   0.3115 S13:   0.2562                       
REMARK   3      S21:  -0.5756 S22:   0.0207 S23:  -0.5069                       
REMARK   3      S31:  -0.1300 S32:   0.1879 S33:   0.1600                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN D AND (RESID 158:188)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -44.5872  -6.5503   2.0753              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6622 T22:   0.4958                                     
REMARK   3      T33:   0.7157 T12:   0.0111                                     
REMARK   3      T13:  -0.1361 T23:  -0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9927 L22:   3.5831                                     
REMARK   3      L33:   4.8902 L12:  -0.7752                                     
REMARK   3      L13:   0.4391 L23:  -0.6653                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4602 S12:  -0.4947 S13:   0.1338                       
REMARK   3      S21:   0.2125 S22:   0.0435 S23:   0.5862                       
REMARK   3      S31:  -0.0166 S32:  -0.5277 S33:   0.3563                       
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 5M3D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-OCT-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001789.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14545                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.380                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.970                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.38                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.51                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.71200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1G8Q                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 10 MG/ML BUFFER: 40% ETOH,      
REMARK 280  0.097 M CITRATE PH 2.2, 0.113 M NA2HPO4 PH 9.3, (PH ~6) 2.5% PEG    
REMARK 280  1000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294.15K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       11.46967            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       22.93933            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8690 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
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: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8980 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
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     GLU A   110                                                      
REMARK 465     THR A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     THR A   203                                                      
REMARK 465     LYS A   204                                                      
REMARK 465     HIS A   205                                                      
REMARK 465     HIS A   206                                                      
REMARK 465     HIS A   207                                                      
REMARK 465     HIS A   208                                                      
REMARK 465     HIS A   209                                                      
REMARK 465     HIS A   210                                                      
REMARK 465     GLU B   110                                                      
REMARK 465     THR B   111                                                      
REMARK 465     THR B   203                                                      
REMARK 465     LYS B   204                                                      
REMARK 465     HIS B   205                                                      
REMARK 465     HIS B   206                                                      
REMARK 465     HIS B   207                                                      
REMARK 465     HIS B   208                                                      
REMARK 465     HIS B   209                                                      
REMARK 465     HIS B   210                                                      
REMARK 465     GLU C   110                                                      
REMARK 465     THR C   111                                                      
REMARK 465     GLY C   112                                                      
REMARK 465     PHE C   113                                                      
REMARK 465     THR C   203                                                      
REMARK 465     LYS C   204                                                      
REMARK 465     HIS C   205                                                      
REMARK 465     HIS C   206                                                      
REMARK 465     HIS C   207                                                      
REMARK 465     HIS C   208                                                      
REMARK 465     HIS C   209                                                      
REMARK 465     HIS C   210                                                      
REMARK 465     GLU D   110                                                      
REMARK 465     THR D   111                                                      
REMARK 465     GLY D   112                                                      
REMARK 465     PHE D   113                                                      
REMARK 465     THR D   203                                                      
REMARK 465     LYS D   204                                                      
REMARK 465     HIS D   205                                                      
REMARK 465     HIS D   206                                                      
REMARK 465     HIS D   207                                                      
REMARK 465     HIS D   208                                                      
REMARK 465     HIS D   209                                                      
REMARK 465     HIS D   210                                                      
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    PRO C   176     OG   SER C   179              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS B 157       17.29   -144.73                                   
REMARK 500    LYS C 171       58.66   -140.19                                   
REMARK 500    ASP D 139       26.97   -143.47                                   
REMARK 500    CYS D 157       18.36   -146.79                                   
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 EDO A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 604                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5M2C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5M33   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5M4R   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5M3T   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1G8Q   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1IV5   RELATED DB: PDB                                   
DBREF  5M3D A  112   201  UNP    P60033   CD81_HUMAN     112    201             
DBREF  5M3D B  112   201  UNP    P60033   CD81_HUMAN     112    201             
DBREF  5M3D C  112   201  UNP    P60033   CD81_HUMAN     112    201             
DBREF  5M3D D  112   201  UNP    P60033   CD81_HUMAN     112    201             
SEQADV 5M3D GLU A  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D THR A  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D GLY A  202  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D THR A  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D LYS A  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS A  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS A  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS A  207  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS A  208  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS A  209  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS A  210  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D GLU B  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D THR B  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D GLY B  202  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D THR B  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D LYS B  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS B  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS B  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS B  207  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS B  208  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS B  209  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS B  210  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D GLU C  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D THR C  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D GLY C  202  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D THR C  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D LYS C  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS C  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS C  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS C  207  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS C  208  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS C  209  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS C  210  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D GLU D  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D THR D  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D GLY D  202  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D THR D  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D LYS D  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS D  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS D  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS D  207  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS D  208  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS D  209  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M3D HIS D  210  UNP  P60033              EXPRESSION TAG                 
SEQRES   1 A  101  GLU THR GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 A  101  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 A  101  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 A  101  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 A  101  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 A  101  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 A  101  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 A  101  LYS GLY THR LYS HIS HIS HIS HIS HIS HIS                      
SEQRES   1 B  101  GLU THR GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 B  101  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 B  101  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 B  101  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 B  101  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 B  101  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 B  101  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 B  101  LYS GLY THR LYS HIS HIS HIS HIS HIS HIS                      
SEQRES   1 C  101  GLU THR GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 C  101  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 C  101  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 C  101  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 C  101  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 C  101  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 C  101  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 C  101  LYS GLY THR LYS HIS HIS HIS HIS HIS HIS                      
SEQRES   1 D  101  GLU THR GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 D  101  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 D  101  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 D  101  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 D  101  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 D  101  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 D  101  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 D  101  LYS GLY THR LYS HIS HIS HIS HIS HIS HIS                      
HET    EDO  A 301      10                                                       
HET    EDO  A 302      10                                                       
HET    PO4  B 301       5                                                       
HET    PO4  B 302       5                                                       
HET    EDO  B 303      10                                                       
HET    PO4  C 301       5                                                       
HET    PO4  C 302       5                                                       
HET    EDO  C 303      10                                                       
HET    PO4  D 601       5                                                       
HET    PO4  D 602       5                                                       
HET    EDO  D 603      10                                                       
HET    EDO  D 604      10                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5  EDO    6(C2 H6 O2)                                                  
FORMUL   7  PO4    6(O4 P 3-)                                                   
FORMUL  17  HOH   *10(H2 O)                                                     
HELIX    1 AA1 ASN A  115  ASP A  137  1                                  23    
HELIX    2 AA2 ALA A  140  ASP A  155  1                                  16    
HELIX    3 AA3 SER A  160  LYS A  171  1                                  12    
HELIX    4 AA4 ASN A  172  CYS A  175  5                                   4    
HELIX    5 AA5 ASN A  180  PHE A  186  5                                   7    
HELIX    6 AA6 ASP A  189  GLY A  200  1                                  12    
HELIX    7 AA7 ASN B  115  ASP B  137  1                                  23    
HELIX    8 AA8 ALA B  140  ASP B  155  1                                  16    
HELIX    9 AA9 SER B  160  LYS B  171  1                                  12    
HELIX   10 AB1 ASN B  172  CYS B  175  5                                   4    
HELIX   11 AB2 ILE B  182  LYS B  187  1                                   6    
HELIX   12 AB3 ASP B  189  GLY B  200  1                                  12    
HELIX   13 AB4 ASN C  115  VAL C  135  1                                  21    
HELIX   14 AB5 ASN C  142  ASP C  155  1                                  14    
HELIX   15 AB6 SER C  160  LYS C  171  1                                  12    
HELIX   16 AB7 ASN C  172  CYS C  175  5                                   4    
HELIX   17 AB8 ILE C  181  PHE C  186  5                                   6    
HELIX   18 AB9 ASP C  189  GLY C  200  1                                  12    
HELIX   19 AC1 ASN D  115  VAL D  136  1                                  22    
HELIX   20 AC2 ASN D  142  ASP D  155  1                                  14    
HELIX   21 AC3 SER D  160  LYS D  171  1                                  12    
HELIX   22 AC4 ASN D  172  CYS D  175  5                                   4    
HELIX   23 AC5 ILE D  181  PHE D  186  5                                   6    
HELIX   24 AC6 ASP D  189  GLY D  200  1                                  12    
SSBOND   1 CYS A  156    CYS A  190                          1555   1555  2.02  
SSBOND   2 CYS A  157    CYS A  175                          1555   1555  2.01  
SSBOND   3 CYS B  156    CYS B  190                          1555   1555  2.01  
SSBOND   4 CYS B  157    CYS B  175                          1555   1555  2.00  
SSBOND   5 CYS C  156    CYS C  190                          1555   1555  2.03  
SSBOND   6 CYS C  157    CYS C  175                          1555   1555  2.03  
SSBOND   7 CYS D  156    CYS D  190                          1555   1555  2.02  
SSBOND   8 CYS D  157    CYS D  175                          1555   1555  2.02  
CISPEP   1 GLY B  112    PHE B  113          0         4.45                     
SITE     1 AC1  5 ASN A 172  CYS A 175  PRO A 176  SER A 177                    
SITE     2 AC1  5 GLY A 178                                                     
SITE     1 AC2  4 GLN A 129  ALA A 130  GLN A 133  ASN A 142                    
SITE     1 AC3  5 SER B 159  SER B 160  ASP B 189  HIS B 191                    
SITE     2 AC3  5 THR D 161                                                     
SITE     1 AC4  6 ASN B 172  CYS B 175  PRO B 176  SER B 177                    
SITE     2 AC4  6 GLY B 178  SER B 179                                          
SITE     1 AC5  1 GLN B 129                                                     
SITE     1 AC6  3 LYS A 121  LYS C 124  HIS C 191                               
SITE     1 AC7  2 ASP C 139  LYS C 144                                          
SITE     1 AC8  5 ASN C 172  CYS C 175  PRO C 176  GLY C 178                    
SITE     2 AC8  5 SER C 179                                                     
SITE     1 AC9  4 LYS B 121  ASP B 138  LYS D 124  HIS D 191                    
SITE     1 AD1  2 ASP D 139  LYS D 144                                          
SITE     1 AD2  4 ASN D 172  CYS D 175  PRO D 176  SER D 179                    
SITE     1 AD3  4 PHE D 126  GLN D 129  ALA D 130  ASN D 141                    
CRYST1   97.948   97.948   34.409  90.00  90.00 120.00 P 31         12          
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      0.010209  0.005894  0.000000        0.00000                         
SCALE2      0.000000  0.011789  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.029062        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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