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Database: PDB
Entry: 6EK2
LinkDB: 6EK2
Original site: 6EK2 
HEADER    CELL ADHESION                           25-SEP-17   6EK2              
TITLE     CRYSTAL STRUCTURE OF HUMAN CD81 LARGE EXTRACELLULAR LOOP IN COMPLEX   
TITLE    2 WITH SINGLE CHAIN FV FRAGMENT 10                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CD81 ANTIGEN;                                              
COMPND   3 CHAIN: A, B;                                                         
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;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: SINGLE CHAIN FV FRAGMENT;                                  
COMPND  10 CHAIN: H, I;                                                         
COMPND  11 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: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  10 ORGANISM_COMMON: MOUSE;                                              
SOURCE  11 ORGANISM_TAXID: 10090;                                               
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HELICAL BUNDLE, ANTIBODY-ANTIGEN COMPLEX, CELL ADHESION               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.F.HARRIS,A.VILLASENOR,A.KUGLSTATTER                                 
REVDAT   2   20-JUN-18 6EK2    1       JRNL                                     
REVDAT   1   30-MAY-18 6EK2    0                                                
JRNL        AUTH   B.NELSON,J.ADAMS,A.KUGLSTATTER,Z.LI,S.F.HARRIS,Y.LIU,        
JRNL        AUTH 2 S.BOHINI,H.MA,K.KLUMPP,J.GAO,S.S.SIDHU                       
JRNL        TITL   STRUCTURE-GUIDED COMBINATORIAL ENGINEERING FACILITATES       
JRNL        TITL 2 AFFINITY AND SPECIFICITY OPTIMIZATION OF ANTI-CD81           
JRNL        TITL 3 ANTIBODIES.                                                  
JRNL        REF    J. MOL. BIOL.                 V. 430  2139 2018              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   29778602                                                     
JRNL        DOI    10.1016/J.JMB.2018.05.018                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.9.2                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.72                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 72.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 17650                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.182                          
REMARK   3   R VALUE            (WORKING SET)  : 0.179                          
REMARK   3   FREE R VALUE                      : 0.247                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.290                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 933                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 9                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.65                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.81                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 390                      
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2318                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 364                      
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2280                   
REMARK   3   BIN FREE R VALUE                        : 0.2771                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 6.67                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 26                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4905                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 257                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 47.28                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.20040                                              
REMARK   3    B22 (A**2) : -8.42490                                             
REMARK   3    B33 (A**2) : 2.22460                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.322               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.885                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5016   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 6788   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1708   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 122    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 723    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5016   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 654    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 5797   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.24                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.98                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 22.24                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6EK2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200006706.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97945                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17696                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.720                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 72.8                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.17700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 5.9                                
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.33500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.1 M BIS-TRIS, 0.2 M       
REMARK 280  AMMONIUM ACETATE, PH 6.5, VAPOR DIFFUSION, SITTING DROP,            
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.15850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.06500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.03000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.06500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.15850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.03000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, I                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   110                                                      
REMARK 465     SER A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     HIS A   203                                                      
REMARK 465     HIS A   204                                                      
REMARK 465     HIS A   205                                                      
REMARK 465     HIS A   206                                                      
REMARK 465     HIS A   207                                                      
REMARK 465     GLY B   110                                                      
REMARK 465     SER B   111                                                      
REMARK 465     GLY B   112                                                      
REMARK 465     HIS B   202                                                      
REMARK 465     HIS B   203                                                      
REMARK 465     HIS B   204                                                      
REMARK 465     HIS B   205                                                      
REMARK 465     HIS B   206                                                      
REMARK 465     HIS B   207                                                      
REMARK 465     GLY H   319                                                      
REMARK 465     GLY H   320                                                      
REMARK 465     GLY H   321                                                      
REMARK 465     GLY H   322                                                      
REMARK 465     SER H   323                                                      
REMARK 465     GLY H   324                                                      
REMARK 465     GLY H   325                                                      
REMARK 465     GLY H   326                                                      
REMARK 465     GLY H   327                                                      
REMARK 465     SER H   328                                                      
REMARK 465     GLY H   329                                                      
REMARK 465     GLY H   330                                                      
REMARK 465     GLY H   331                                                      
REMARK 465     GLY H   332                                                      
REMARK 465     SER H   333                                                      
REMARK 465     GLY H   334                                                      
REMARK 465     GLY H   335                                                      
REMARK 465     GLY H   336                                                      
REMARK 465     GLY H   337                                                      
REMARK 465     SER H   338                                                      
REMARK 465     ALA I   318                                                      
REMARK 465     GLY I   319                                                      
REMARK 465     GLY I   320                                                      
REMARK 465     GLY I   321                                                      
REMARK 465     GLY I   322                                                      
REMARK 465     SER I   323                                                      
REMARK 465     GLY I   324                                                      
REMARK 465     GLY I   325                                                      
REMARK 465     GLY I   326                                                      
REMARK 465     GLY I   327                                                      
REMARK 465     SER I   328                                                      
REMARK 465     GLY I   329                                                      
REMARK 465     GLY I   330                                                      
REMARK 465     GLY I   331                                                      
REMARK 465     GLY I   332                                                      
REMARK 465     SER I   333                                                      
REMARK 465     GLY I   334                                                      
REMARK 465     GLY I   335                                                      
REMARK 465     GLY I   336                                                      
REMARK 465     GLY I   337                                                      
REMARK 465     SER I   338                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG H   236     OD2  ASP H   259              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 139       58.86    -90.91                                   
REMARK 500    ALA A 140       58.52   -153.07                                   
REMARK 500    LEU A 162       47.45   -103.89                                   
REMARK 500    SER A 183     -128.44     66.36                                   
REMARK 500    ASP B 138     -150.07   -179.27                                   
REMARK 500    ALA B 140       37.31    -71.33                                   
REMARK 500    LEU B 162       46.96   -104.72                                   
REMARK 500    SER B 183      -91.50     70.65                                   
REMARK 500    ASN B 184       21.86   -143.47                                   
REMARK 500    ASN H 270     -151.64   -120.77                                   
REMARK 500    TYR H 272       81.42   -151.74                                   
REMARK 500    SER H 345      -59.72    -23.23                                   
REMARK 500    ASP H 355     -176.27    -68.41                                   
REMARK 500    ASN H 369       10.78     58.05                                   
REMARK 500    LEU H 385      -62.21    -98.44                                   
REMARK 500    ALA H 389      -34.84     62.74                                   
REMARK 500    TRP H 434       94.67    -68.79                                   
REMARK 500    ASN I 270     -154.13   -121.89                                   
REMARK 500    TYR I 272       81.02   -153.28                                   
REMARK 500    SER I 345      -63.86    -26.46                                   
REMARK 500    ASP I 355     -176.68    -68.14                                   
REMARK 500    TYR I 368       47.56     37.87                                   
REMARK 500    LEU I 385      -61.78    -99.09                                   
REMARK 500    ALA I 389      -35.00     61.97                                   
REMARK 500    TRP I 430      -60.43    -95.32                                   
REMARK 500    TRP I 434       93.68    -67.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 335        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH A 336        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH A 337        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH A 338        DISTANCE =  9.61 ANGSTROMS                       
REMARK 525    HOH A 339        DISTANCE = 10.10 ANGSTROMS                       
REMARK 525    HOH B 328        DISTANCE =  6.03 ANGSTROMS                       
REMARK 525    HOH B 329        DISTANCE =  6.85 ANGSTROMS                       
REMARK 525    HOH H 603        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH H 604        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH H 605        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH H 606        DISTANCE =  6.62 ANGSTROMS                       
REMARK 525    HOH H 607        DISTANCE =  7.72 ANGSTROMS                       
REMARK 525    HOH H 608        DISTANCE =  7.83 ANGSTROMS                       
REMARK 525    HOH H 609        DISTANCE =  7.96 ANGSTROMS                       
REMARK 525    HOH H 610        DISTANCE =  7.98 ANGSTROMS                       
REMARK 525    HOH H 611        DISTANCE =  8.63 ANGSTROMS                       
REMARK 525    HOH H 612        DISTANCE =  8.66 ANGSTROMS                       
REMARK 525    HOH H 613        DISTANCE =  9.36 ANGSTROMS                       
REMARK 525    HOH H 614        DISTANCE =  9.48 ANGSTROMS                       
REMARK 525    HOH H 615        DISTANCE = 10.93 ANGSTROMS                       
REMARK 525    HOH H 616        DISTANCE = 12.98 ANGSTROMS                       
REMARK 525    HOH H 617        DISTANCE = 15.32 ANGSTROMS                       
REMARK 525    HOH H 618        DISTANCE = 17.98 ANGSTROMS                       
REMARK 525    HOH I 570        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH I 571        DISTANCE =  6.95 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5DFW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6EJG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6EJM   RELATED DB: PDB                                   
DBREF  6EK2 A  112   201  UNP    P60033   CD81_HUMAN     112    201             
DBREF  6EK2 B  112   201  UNP    P60033   CD81_HUMAN     112    201             
DBREF  6EK2 H  170   445  PDB    6EK2     6EK2           170    445             
DBREF  6EK2 I  170   445  PDB    6EK2     6EK2           170    445             
SEQADV 6EK2 GLY A  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EK2 SER A  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EK2 HIS A  202  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EK2 HIS A  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EK2 HIS A  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EK2 HIS A  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EK2 HIS A  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EK2 HIS A  207  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EK2 GLY B  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EK2 SER B  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EK2 HIS B  202  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EK2 HIS B  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EK2 HIS B  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EK2 HIS B  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EK2 HIS B  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EK2 HIS B  207  UNP  P60033              EXPRESSION TAG                 
SEQRES   1 A   98  GLY SER GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 A   98  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 A   98  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 A   98  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 A   98  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 A   98  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 A   98  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 A   98  LYS HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 B   98  GLY SER GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 B   98  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 B   98  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 B   98  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 B   98  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 B   98  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 B   98  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 B   98  LYS HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 H  247  GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS          
SEQRES   2 H  247  PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY          
SEQRES   3 H  247  PHE THR PHE SER ASP TYR TYR MET HIS TRP VAL ARG GLN          
SEQRES   4 H  247  THR PRO LYS LYS ARG LEU GLU TRP VAL ALA THR ILE SER          
SEQRES   5 H  247  ASP GLY GLY SER TYR THR TYR PHE LEU ASP SER VAL LYS          
SEQRES   6 H  247  GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN LYS          
SEQRES   7 H  247  LEU ASP LEU GLN MET SER SER LEU LYS SER GLU ASP THR          
SEQRES   8 H  247  GLY MET TYR TYR CYS ALA ARG ASP GLY ASN LYS TYR SER          
SEQRES   9 H  247  ALA TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR          
SEQRES  10 H  247  VAL SER ALA GLY GLY GLY GLY SER GLY GLY GLY GLY SER          
SEQRES  11 H  247  GLY GLY GLY GLY SER GLY GLY GLY GLY SER ASP ILE GLN          
SEQRES  12 H  247  MET THR GLN SER SER SER SER PHE SER VAL SER LEU GLY          
SEQRES  13 H  247  ASP ARG VAL THR ILE THR CYS LYS ALA SER GLU ASP ILE          
SEQRES  14 H  247  TYR ASN ARG LEU ALA TRP TYR GLN GLN LYS PRO GLY ASN          
SEQRES  15 H  247  ALA PRO ARG LEU LEU ILE SER GLY ALA THR SER LEU GLU          
SEQRES  16 H  247  THR GLY VAL PRO SER ARG PHE SER GLY SER GLY SER GLY          
SEQRES  17 H  247  LYS ASP TYR THR LEU SER ILE THR SER LEU GLN THR GLU          
SEQRES  18 H  247  ASP PHE ALA THR TYR TYR CYS GLN GLN TYR TRP SER PRO          
SEQRES  19 H  247  PRO TRP THR PHE GLY GLY GLY THR LYS LEU GLU ILE LYS          
SEQRES   1 I  247  GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS          
SEQRES   2 I  247  PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY          
SEQRES   3 I  247  PHE THR PHE SER ASP TYR TYR MET HIS TRP VAL ARG GLN          
SEQRES   4 I  247  THR PRO LYS LYS ARG LEU GLU TRP VAL ALA THR ILE SER          
SEQRES   5 I  247  ASP GLY GLY SER TYR THR TYR PHE LEU ASP SER VAL LYS          
SEQRES   6 I  247  GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN LYS          
SEQRES   7 I  247  LEU ASP LEU GLN MET SER SER LEU LYS SER GLU ASP THR          
SEQRES   8 I  247  GLY MET TYR TYR CYS ALA ARG ASP GLY ASN LYS TYR SER          
SEQRES   9 I  247  ALA TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR          
SEQRES  10 I  247  VAL SER ALA GLY GLY GLY GLY SER GLY GLY GLY GLY SER          
SEQRES  11 I  247  GLY GLY GLY GLY SER GLY GLY GLY GLY SER ASP ILE GLN          
SEQRES  12 I  247  MET THR GLN SER SER SER SER PHE SER VAL SER LEU GLY          
SEQRES  13 I  247  ASP ARG VAL THR ILE THR CYS LYS ALA SER GLU ASP ILE          
SEQRES  14 I  247  TYR ASN ARG LEU ALA TRP TYR GLN GLN LYS PRO GLY ASN          
SEQRES  15 I  247  ALA PRO ARG LEU LEU ILE SER GLY ALA THR SER LEU GLU          
SEQRES  16 I  247  THR GLY VAL PRO SER ARG PHE SER GLY SER GLY SER GLY          
SEQRES  17 I  247  LYS ASP TYR THR LEU SER ILE THR SER LEU GLN THR GLU          
SEQRES  18 I  247  ASP PHE ALA THR TYR TYR CYS GLN GLN TYR TRP SER PRO          
SEQRES  19 I  247  PRO TRP THR PHE GLY GLY GLY THR LYS LEU GLU ILE LYS          
FORMUL   5  HOH   *257(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 LEU A  162  ALA A  164  5                                   3    
HELIX    4 AA4 LEU A  165  ASN A  172  1                                   8    
HELIX    5 AA5 ASP A  189  GLY A  200  1                                  12    
HELIX    6 AA6 ASN B  115  VAL B  136  1                                  22    
HELIX    7 AA7 ALA B  140  ASP B  155  1                                  16    
HELIX    8 AA8 LEU B  162  ALA B  164  5                                   3    
HELIX    9 AA9 LEU B  165  ASN B  172  1                                   8    
HELIX   10 AB1 ASP B  189  GLY B  200  1                                  12    
HELIX   11 AB2 THR H  197  TYR H  201  5                                   5    
HELIX   12 AB3 LYS H  256  THR H  260  5                                   5    
HELIX   13 AB4 GLN H  417  PHE H  421  5                                   5    
HELIX   14 AB5 THR I  197  TYR I  201  5                                   5    
HELIX   15 AB6 LYS I  256  THR I  260  5                                   5    
HELIX   16 AB7 GLN I  417  PHE I  421  5                                   5    
SHEET    1 AA1 2 ILE A 181  ILE A 182  0                                        
SHEET    2 AA1 2 LEU A 185  PHE A 186 -1  O  LEU A 185   N  ILE A 182           
SHEET    1 AA2 2 ILE B 181  ILE B 182  0                                        
SHEET    2 AA2 2 LEU B 185  PHE B 186 -1  O  LEU B 185   N  ILE B 182           
SHEET    1 AA3 4 GLN H 172  SER H 176  0                                        
SHEET    2 AA3 4 LEU H 187  SER H 194 -1  O  SER H 194   N  GLN H 172           
SHEET    3 AA3 4 LYS H 247  MET H 252 -1  O  LEU H 248   N  CYS H 191           
SHEET    4 AA3 4 PHE H 237  ASP H 242 -1  N  THR H 238   O  GLN H 251           
SHEET    1 AA4 6 LEU H 180  VAL H 181  0                                        
SHEET    2 AA4 6 THR H 283  VAL H 287  1  O  THR H 286   N  VAL H 181           
SHEET    3 AA4 6 GLY H 261  ASP H 268 -1  N  TYR H 263   O  THR H 283           
SHEET    4 AA4 6 MET H 203  GLN H 208 -1  N  VAL H 206   O  TYR H 264           
SHEET    5 AA4 6 LEU H 214  ILE H 220 -1  O  VAL H 217   N  TRP H 205           
SHEET    6 AA4 6 THR H 227  PHE H 229 -1  O  TYR H 228   N  THR H 219           
SHEET    1 AA5 4 LEU H 180  VAL H 181  0                                        
SHEET    2 AA5 4 THR H 283  VAL H 287  1  O  THR H 286   N  VAL H 181           
SHEET    3 AA5 4 GLY H 261  ASP H 268 -1  N  TYR H 263   O  THR H 283           
SHEET    4 AA5 4 PHE H 276  TRP H 279 -1  O  TYR H 278   N  ARG H 267           
SHEET    1 AA6 4 MET H 342  THR H 343  0                                        
SHEET    2 AA6 4 VAL H 357  ALA H 363 -1  O  LYS H 362   N  THR H 343           
SHEET    3 AA6 4 ASP H 408  ILE H 413 -1  O  LEU H 411   N  ILE H 359           
SHEET    4 AA6 4 PHE H 400  SER H 405 -1  N  SER H 401   O  SER H 412           
SHEET    1 AA7 6 SER H 348  SER H 350  0                                        
SHEET    2 AA7 6 THR H 440  GLU H 443  1  O  GLU H 443   N  PHE H 349           
SHEET    3 AA7 6 THR H 423  GLN H 428 -1  N  TYR H 424   O  THR H 440           
SHEET    4 AA7 6 LEU H 371  GLN H 376 -1  N  TYR H 374   O  TYR H 425           
SHEET    5 AA7 6 ARG H 383  SER H 387 -1  O  ARG H 383   N  GLN H 375           
SHEET    6 AA7 6 SER H 391  LEU H 392 -1  O  SER H 391   N  SER H 387           
SHEET    1 AA8 4 GLN I 172  SER I 176  0                                        
SHEET    2 AA8 4 LEU I 187  SER I 194 -1  O  SER I 190   N  SER I 176           
SHEET    3 AA8 4 LYS I 247  MET I 252 -1  O  LEU I 248   N  CYS I 191           
SHEET    4 AA8 4 PHE I 237  ASP I 242 -1  N  THR I 238   O  GLN I 251           
SHEET    1 AA9 5 THR I 227  PHE I 229  0                                        
SHEET    2 AA9 5 LEU I 214  ILE I 220 -1  N  THR I 219   O  TYR I 228           
SHEET    3 AA9 5 MET I 203  GLN I 208 -1  N  TRP I 205   O  VAL I 217           
SHEET    4 AA9 5 GLY I 261  ASP I 268 -1  O  TYR I 264   N  VAL I 206           
SHEET    5 AA9 5 PHE I 276  TRP I 279 -1  O  TYR I 278   N  ARG I 267           
SHEET    1 AB1 5 THR I 227  PHE I 229  0                                        
SHEET    2 AB1 5 LEU I 214  ILE I 220 -1  N  THR I 219   O  TYR I 228           
SHEET    3 AB1 5 MET I 203  GLN I 208 -1  N  TRP I 205   O  VAL I 217           
SHEET    4 AB1 5 GLY I 261  ASP I 268 -1  O  TYR I 264   N  VAL I 206           
SHEET    5 AB1 5 THR I 283  VAL I 285 -1  O  THR I 283   N  TYR I 263           
SHEET    1 AB2 4 MET I 342  THR I 343  0                                        
SHEET    2 AB2 4 VAL I 357  ALA I 363 -1  O  LYS I 362   N  THR I 343           
SHEET    3 AB2 4 ASP I 408  ILE I 413 -1  O  LEU I 411   N  ILE I 359           
SHEET    4 AB2 4 PHE I 400  SER I 405 -1  N  SER I 401   O  SER I 412           
SHEET    1 AB3 6 SER I 348  SER I 350  0                                        
SHEET    2 AB3 6 THR I 440  GLU I 443  1  O  GLU I 443   N  PHE I 349           
SHEET    3 AB3 6 THR I 423  GLN I 428 -1  N  TYR I 424   O  THR I 440           
SHEET    4 AB3 6 LEU I 371  GLN I 376 -1  N  TYR I 374   O  TYR I 425           
SHEET    5 AB3 6 ARG I 383  SER I 387 -1  O  LEU I 385   N  TRP I 373           
SHEET    6 AB3 6 SER I 391  LEU I 392 -1  O  SER I 391   N  SER I 387           
SSBOND   1 CYS A  156    CYS A  190                          1555   1555  2.04  
SSBOND   2 CYS A  157    CYS A  175                          1555   1555  2.03  
SSBOND   3 CYS B  156    CYS B  190                          1555   1555  2.03  
SSBOND   4 CYS B  157    CYS B  175                          1555   1555  2.03  
SSBOND   5 CYS H  191    CYS H  265                          1555   1555  2.03  
SSBOND   6 CYS H  361    CYS H  426                          1555   1555  2.04  
SSBOND   7 CYS I  191    CYS I  265                          1555   1555  2.02  
SSBOND   8 CYS I  361    CYS I  426                          1555   1555  2.04  
CISPEP   1 PRO H  432    PRO H  433          0        -0.54                     
CISPEP   2 GLY I  178    GLY I  179          0         0.91                     
CISPEP   3 PRO I  432    PRO I  433          0         3.36                     
CRYST1   52.317  118.060  130.130  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019114  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008470  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007685        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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