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Database: PDB
Entry: 6EJG
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Original site: 6EJG 
HEADER    CELL ADHESION                           21-SEP-17   6EJG              
TITLE     CRYSTAL STRUCTURE OF HUMAN CD81 LARGE EXTRACELLULAR LOOP IN COMPLEX   
TITLE    2 WITH SINGLE CHAIN FV FRAGMENT 4                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CD81 ANTIGEN;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: 26 KDA CELL SURFACE PROTEIN TAPA-1,TARGET OF THE            
COMPND   5 ANTIPROLIFERATIVE ANTIBODY 1,TETRASPANIN-28,TSPAN-28;                
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SINGLE CHAIN FV FRAGMENT;                                  
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 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: HOUSE 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.WONG,A.KUGLSTATTER                                       
REVDAT   2   20-JUN-18 6EJG    1       JRNL                                     
REVDAT   1   30-MAY-18 6EJG    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.    2.82 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.83                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 25664                          
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) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1348                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.82                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.89                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 686                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 32.64                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 39                           
REMARK   3   BIN FREE R VALUE                    : 0.3940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4902                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 57                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.60000                                              
REMARK   3    B22 (A**2) : -0.49000                                             
REMARK   3    B33 (A**2) : -0.11000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.630         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.346         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.231         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.326        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.905                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.873                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5022 ; 0.005 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3396 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6794 ; 0.990 ; 1.951       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8308 ; 0.760 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   638 ; 6.105 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   206 ;34.855 ;24.951       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   860 ;15.939 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;16.939 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   752 ; 0.059 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5590 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   984 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1009 ; 0.187 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3409 ; 0.176 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2397 ; 0.174 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2729 ; 0.083 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   146 ; 0.114 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.025 ; 0.200       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    15 ; 0.290 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    25 ; 0.145 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.164 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4102 ; 0.312 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1310 ; 0.024 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5102 ; 0.341 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2219 ; 0.354 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1692 ; 0.589 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6EJG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200006704.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAY-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
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) : 0.97946                            
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   : 27051                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.820                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.830                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.3                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.17000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.82                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 37.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.49400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
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   (%): 70.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE, 20% PEG 6000,     
REMARK 280  PH 5.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       92.98000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       92.98000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       39.31750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       85.45250            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       39.31750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       85.45250            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       92.98000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       39.31750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       85.45250            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       92.98000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       39.31750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       85.45250            
REMARK 290   SMTRY3   8  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: 5410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 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     LEU A   202                                                      
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     HIS A   208                                                      
REMARK 465     GLY B   110                                                      
REMARK 465     SER B   111                                                      
REMARK 465     GLY B   112                                                      
REMARK 465     LEU 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     HIS B   208                                                      
REMARK 465     GLY C   150                                                      
REMARK 465     GLY C   151                                                      
REMARK 465     GLY C   152                                                      
REMARK 465     GLY C   153                                                      
REMARK 465     SER C   154                                                      
REMARK 465     GLY C   155                                                      
REMARK 465     GLY C   156                                                      
REMARK 465     GLY C   157                                                      
REMARK 465     GLY C   158                                                      
REMARK 465     SER C   159                                                      
REMARK 465     GLY C   160                                                      
REMARK 465     GLY C   161                                                      
REMARK 465     GLY C   162                                                      
REMARK 465     GLY C   163                                                      
REMARK 465     SER C   164                                                      
REMARK 465     GLY C   165                                                      
REMARK 465     GLY C   166                                                      
REMARK 465     GLY C   167                                                      
REMARK 465     GLY C   168                                                      
REMARK 465     SER C   169                                                      
REMARK 465     GLY D   150                                                      
REMARK 465     GLY D   151                                                      
REMARK 465     GLY D   152                                                      
REMARK 465     GLY D   153                                                      
REMARK 465     SER D   154                                                      
REMARK 465     GLY D   155                                                      
REMARK 465     GLY D   156                                                      
REMARK 465     GLY D   157                                                      
REMARK 465     GLY D   158                                                      
REMARK 465     SER D   159                                                      
REMARK 465     GLY D   160                                                      
REMARK 465     GLY D   161                                                      
REMARK 465     GLY D   162                                                      
REMARK 465     GLY D   163                                                      
REMARK 465     SER D   164                                                      
REMARK 465     GLY D   165                                                      
REMARK 465     GLY D   166                                                      
REMARK 465     GLY D   167                                                      
REMARK 465     GLY D   168                                                      
REMARK 465     SER D   169                                                      
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       50.82   -119.03                                   
REMARK 500    ASP A 155       72.45     51.28                                   
REMARK 500    LEU A 162       50.75   -143.88                                   
REMARK 500    ILE A 181      124.82    172.97                                   
REMARK 500    ASP B 137      103.06   -165.50                                   
REMARK 500    ALA B 140       84.14    -66.30                                   
REMARK 500    ASN B 173       20.92     80.63                                   
REMARK 500    PRO B 176      -75.11    -57.61                                   
REMARK 500    SER B 177      169.96    173.84                                   
REMARK 500    SER B 179      -84.42    -71.79                                   
REMARK 500    GLN C  55      128.63    165.54                                   
REMARK 500    TYR C  74       -0.40     84.68                                   
REMARK 500    ALA C  93      -51.94     74.03                                   
REMARK 500    LEU C 274       40.63    -79.62                                   
REMARK 500    LEU D  53       98.27    -60.56                                   
REMARK 500    GLN D  55      147.02    163.93                                   
REMARK 500    TYR D  74        2.03     80.55                                   
REMARK 500    ALA D  93      -55.50     73.30                                   
REMARK 500    HIS D 118      116.43   -167.72                                   
REMARK 500    ALA D 125       98.04    -63.56                                   
REMARK 500    LEU D 173       86.40     62.18                                   
REMARK 500    TYR D 196      -44.36     96.07                                   
REMARK 500    LEU D 274       42.18    -69.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5DFW   RELATED DB: PDB                                   
DBREF  6EJG A  112   202  UNP    P60033   CD81_HUMAN     112    202             
DBREF  6EJG B  112   202  UNP    P60033   CD81_HUMAN     112    202             
DBREF  6EJG C   39   289  PDB    6EJG     6EJG            39    289             
DBREF  6EJG D   39   289  PDB    6EJG     6EJG            39    289             
SEQADV 6EJG GLY A  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJG SER A  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJG HIS A  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJG HIS A  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJG HIS A  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJG HIS A  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJG HIS A  207  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJG HIS A  208  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJG GLY B  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJG SER B  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJG HIS B  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJG HIS B  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJG HIS B  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJG HIS B  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJG HIS B  207  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJG HIS B  208  UNP  P60033              EXPRESSION TAG                 
SEQRES   1 A   99  GLY SER GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 A   99  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 A   99  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 A   99  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 A   99  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 A   99  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 A   99  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 A   99  LYS LEU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B   99  GLY SER GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 B   99  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 B   99  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 B   99  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 B   99  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 B   99  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 B   99  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 B   99  LYS LEU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 C  251  ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU SER VAL          
SEQRES   2 C  251  SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER          
SEQRES   3 C  251  LYS SER VAL SER THR SER ILE TYR SER TYR MET HIS TRP          
SEQRES   4 C  251  TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE          
SEQRES   5 C  251  LYS TYR ALA SER TYR LEU GLU SER GLY VAL PRO ALA ARG          
SEQRES   6 C  251  PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU ASN          
SEQRES   7 C  251  ILE HIS PRO VAL GLU GLU GLU ASP ALA ALA THR TYR TYR          
SEQRES   8 C  251  CYS GLU HIS SER ARG GLU PHE PRO PHE THR PHE GLY THR          
SEQRES   9 C  251  GLY THR LYS LEU GLU ILE LYS GLY GLY GLY GLY SER GLY          
SEQRES  10 C  251  GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY          
SEQRES  11 C  251  SER GLN VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL          
SEQRES  12 C  251  LYS PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER          
SEQRES  13 C  251  GLY TYR THR PHE SER SER SER TRP MET ASN TRP VAL LYS          
SEQRES  14 C  251  GLN ARG PRO GLY LYS GLY LEU GLU TRP ILE GLY ARG ILE          
SEQRES  15 C  251  TYR SER GLY ASP GLY ASP ALA ILE TYR ASN GLY LYS PHE          
SEQRES  16 C  251  LYS GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER          
SEQRES  17 C  251  THR ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP          
SEQRES  18 C  251  SER ALA VAL TYR PHE CYS ALA ARG GLU GLY LYS THR GLY          
SEQRES  19 C  251  ASP LEU LEU LEU ARG SER TRP GLY GLN GLY SER ALA LEU          
SEQRES  20 C  251  THR VAL SER SER                                              
SEQRES   1 D  251  ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU SER VAL          
SEQRES   2 D  251  SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER          
SEQRES   3 D  251  LYS SER VAL SER THR SER ILE TYR SER TYR MET HIS TRP          
SEQRES   4 D  251  TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE          
SEQRES   5 D  251  LYS TYR ALA SER TYR LEU GLU SER GLY VAL PRO ALA ARG          
SEQRES   6 D  251  PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU ASN          
SEQRES   7 D  251  ILE HIS PRO VAL GLU GLU GLU ASP ALA ALA THR TYR TYR          
SEQRES   8 D  251  CYS GLU HIS SER ARG GLU PHE PRO PHE THR PHE GLY THR          
SEQRES   9 D  251  GLY THR LYS LEU GLU ILE LYS GLY GLY GLY GLY SER GLY          
SEQRES  10 D  251  GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY          
SEQRES  11 D  251  SER GLN VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL          
SEQRES  12 D  251  LYS PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER          
SEQRES  13 D  251  GLY TYR THR PHE SER SER SER TRP MET ASN TRP VAL LYS          
SEQRES  14 D  251  GLN ARG PRO GLY LYS GLY LEU GLU TRP ILE GLY ARG ILE          
SEQRES  15 D  251  TYR SER GLY ASP GLY ASP ALA ILE TYR ASN GLY LYS PHE          
SEQRES  16 D  251  LYS GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER          
SEQRES  17 D  251  THR ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP          
SEQRES  18 D  251  SER ALA VAL TYR PHE CYS ALA ARG GLU GLY LYS THR GLY          
SEQRES  19 D  251  ASP LEU LEU LEU ARG SER TRP GLY GLN GLY SER ALA LEU          
SEQRES  20 D  251  THR VAL SER SER                                              
FORMUL   5  HOH   *57(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  159  THR A  161  5                                   3    
HELIX    4 AA4 LEU A  162  ASN A  172  1                                  11    
HELIX    5 AA5 ILE A  181  GLU A  188  5                                   8    
HELIX    6 AA6 ASP A  189  SER A  199  1                                  11    
HELIX    7 AA7 ASN B  115  VAL B  136  1                                  22    
HELIX    8 AA8 ALA B  140  LEU B  154  1                                  15    
HELIX    9 AA9 LEU B  162  ASN B  172  1                                  11    
HELIX   10 AB1 ILE B  181  GLU B  188  5                                   8    
HELIX   11 AB2 ASP B  189  GLY B  200  1                                  12    
HELIX   12 AB3 GLU C  121  ALA C  125  5                                   5    
HELIX   13 AB4 THR C  197  SER C  200  5                                   4    
HELIX   14 AB5 THR C  256  SER C  260  5                                   5    
HELIX   15 AB6 GLU D  121  ALA D  125  5                                   5    
HELIX   16 AB7 THR D  256  SER D  260  5                                   5    
SHEET    1 AA1 4 LEU C  42  SER C  45  0                                        
SHEET    2 AA1 4 ALA C  57  ALA C  63 -1  O  ARG C  62   N  THR C  43           
SHEET    3 AA1 4 ASP C 112  ILE C 117 -1  O  LEU C 115   N  ILE C  59           
SHEET    4 AA1 4 PHE C 104  SER C 109 -1  N  SER C 105   O  ASN C 116           
SHEET    1 AA2 6 SER C  48  SER C  52  0                                        
SHEET    2 AA2 6 THR C 144  LYS C 149  1  O  LYS C 145   N  LEU C  49           
SHEET    3 AA2 6 THR C 127  HIS C 132 -1  N  TYR C 128   O  THR C 144           
SHEET    4 AA2 6 MET C  75  GLN C  80 -1  N  TYR C  78   O  TYR C 129           
SHEET    5 AA2 6 LYS C  87  LYS C  91 -1  O  LYS C  87   N  GLN C  79           
SHEET    6 AA2 6 TYR C  95  LEU C  96 -1  O  TYR C  95   N  LYS C  91           
SHEET    1 AA3 4 GLN C 172  GLN C 175  0                                        
SHEET    2 AA3 4 VAL C 187  SER C 194 -1  O  LYS C 192   N  GLN C 174           
SHEET    3 AA3 4 THR C 247  LEU C 252 -1  O  MET C 250   N  ILE C 189           
SHEET    4 AA3 4 ALA C 237  ASP C 242 -1  N  THR C 240   O  TYR C 249           
SHEET    1 AA4 6 GLU C 179  VAL C 181  0                                        
SHEET    2 AA4 6 SER C 283  VAL C 287  1  O  THR C 286   N  GLU C 179           
SHEET    3 AA4 6 ALA C 261  ARG C 267 -1  N  ALA C 261   O  LEU C 285           
SHEET    4 AA4 6 TRP C 202  GLN C 208 -1  N  ASN C 204   O  ALA C 266           
SHEET    5 AA4 6 GLU C 215  TYR C 221 -1  O  GLU C 215   N  LYS C 207           
SHEET    6 AA4 6 ALA C 227  TYR C 229 -1  O  ILE C 228   N  ARG C 219           
SHEET    1 AA5 4 LEU D  42  SER D  45  0                                        
SHEET    2 AA5 4 ALA D  57  ALA D  63 -1  O  ARG D  62   N  THR D  43           
SHEET    3 AA5 4 ASP D 112  ILE D 117 -1  O  LEU D 115   N  ILE D  59           
SHEET    4 AA5 4 PHE D 104  SER D 109 -1  N  SER D 107   O  THR D 114           
SHEET    1 AA6 6 SER D  48  VAL D  51  0                                        
SHEET    2 AA6 6 THR D 144  ILE D 148  1  O  LYS D 145   N  LEU D  49           
SHEET    3 AA6 6 THR D 127  HIS D 132 -1  N  TYR D 128   O  THR D 144           
SHEET    4 AA6 6 MET D  75  GLN D  80 -1  N  TYR D  78   O  TYR D 129           
SHEET    5 AA6 6 LYS D  87  LYS D  91 -1  O  LYS D  87   N  GLN D  79           
SHEET    6 AA6 6 TYR D  95  LEU D  96 -1  O  TYR D  95   N  LYS D  91           
SHEET    1 AA7 4 GLN D 174  GLN D 175  0                                        
SHEET    2 AA7 4 VAL D 187  LYS D 192 -1  O  LYS D 192   N  GLN D 174           
SHEET    3 AA7 4 THR D 247  LEU D 252 -1  O  LEU D 252   N  VAL D 187           
SHEET    4 AA7 4 ALA D 237  ASP D 242 -1  N  THR D 240   O  TYR D 249           
SHEET    1 AA8 6 GLU D 179  VAL D 181  0                                        
SHEET    2 AA8 6 SER D 283  VAL D 287  1  O  THR D 286   N  GLU D 179           
SHEET    3 AA8 6 ALA D 261  ARG D 267 -1  N  TYR D 263   O  SER D 283           
SHEET    4 AA8 6 TRP D 202  GLN D 208 -1  N  ASN D 204   O  ALA D 266           
SHEET    5 AA8 6 GLU D 215  TYR D 221 -1  O  ILE D 220   N  MET D 203           
SHEET    6 AA8 6 ALA D 227  TYR D 229 -1  O  ILE D 228   N  ARG D 219           
SSBOND   1 CYS A  156    CYS A  190                          1555   1555  2.03  
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 C   61    CYS C  130                          1555   1555  2.69  
SSBOND   6 CYS C  191    CYS C  265                          1555   1555  2.04  
SSBOND   7 CYS D   61    CYS D  130                          1555   1555  2.64  
SSBOND   8 CYS D  191    CYS D  265                          1555   1555  2.04  
CISPEP   1 SER C   45    PRO C   46          0         1.38                     
CISPEP   2 GLY C   54    GLN C   55          0       -22.12                     
CISPEP   3 SER C   73    TYR C   74          0        26.07                     
CISPEP   4 HIS C  118    PRO C  119          0         0.92                     
CISPEP   5 PHE C  136    PRO C  137          0        -3.86                     
CISPEP   6 SER D   45    PRO D   46          0         0.98                     
CISPEP   7 GLY D   54    GLN D   55          0       -17.43                     
CISPEP   8 SER D   73    TYR D   74          0        25.62                     
CISPEP   9 HIS D  118    PRO D  119          0         2.54                     
CISPEP  10 PHE D  136    PRO D  137          0        -1.80                     
CRYST1   78.635  170.905  185.960  90.00  90.00  90.00 C 2 2 21     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012717  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005851  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005378        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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