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Database: PDB
Entry: 5M4R
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Original site: 5M4R 
HEADER    CELL ADHESION                           19-OCT-16   5M4R              
TITLE     STRUCTURAL TUNING OF CD81LEL (SPACE GROUP C2)                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CD81 ANTIGEN;                                              
COMPND   3 CHAIN: A, B, C, D, E;                                                
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 OTHER_DETAILS: IN CHAIN E THE LAST RESIDUE HAS BEEN MODELLED AS ALA  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CD81, TAPA1, TSPAN28;                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;                                
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHLSEC                                    
KEYWDS    HUMAN CELLULAR RECEPTOR FOR HEPATITIS C VIRUS, CELL ADHESION          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.S.CUNHA,P.SFRISO,A.L.ROJAS,P.ROVERSI,A.HOSPITAL,M.OROZCO,           
AUTHOR   2 N.G.ABRESCIA                                                         
REVDAT   3   13-DEC-17 5M4R    1       AUTHOR JRNL                              
REVDAT   2   18-JAN-17 5M4R    1       JRNL                                     
REVDAT   1   14-DEC-16 5M4R    0                                                
JRNL        AUTH   E.S.CUNHA,P.SFRISO,A.L.ROJAS,P.ROVERSI,A.HOSPITAL,M.OROZCO,  
JRNL        AUTH 2 N.G.ABRESCIA                                                 
JRNL        TITL   MECHANISM OF STRUCTURAL TUNING OF THE HEPATITIS C VIRUS      
JRNL        TITL 2 HUMAN CELLULAR RECEPTOR CD81 LARGE EXTRACELLULAR LOOP.       
JRNL        REF    STRUCTURE                     V.  25    53 2017              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   27916518                                                     
JRNL        DOI    10.1016/J.STR.2016.11.003                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   K.KITADOKORO,D.BORDO,G.GALLI,R.PETRACCA,F.FALUGI,            
REMARK   1  AUTH 2 S.ABRIGNANI,G.GRANDI,M.BOLOGNESI                             
REMARK   1  TITL   CD81 EXTRACELLULAR DOMAIN 3D STRUCTURE: INSIGHT INTO THE     
REMARK   1  TITL 2 TETRASPANIN SUPERFAMILY STRUCTURAL MOTIFS.                   
REMARK   1  REF    EMBO J.                       V.  20    12 2001              
REMARK   1  REFN                   ISSN 0261-4189                               
REMARK   1  PMID   11226150                                                     
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   K.KITADOKORO,M.PONASSI,G.GALLI,R.PETRACCA,F.FALUGI,G.GRANDI, 
REMARK   1  AUTH 2 M.BOLOGNESI                                                  
REMARK   1  TITL   SUBUNIT ASSOCIATION AND CONFORMATIONAL FLEXIBILITY IN THE    
REMARK   1  TITL 2 HEAD SUBDOMAIN OF HUMAN CD81 LARGE EXTRACELLULAR LOOP.       
REMARK   1  REF    BIOL. CHEM.                   V. 383  1447 2002              
REMARK   1  REFN                   ISSN 1431-6730                               
REMARK   1  PMID   12437138                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 53.09                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.100                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 15306                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 762                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 53.1006 -  5.2996    0.97     2949   173  0.2109 0.2280        
REMARK   3     2  5.2996 -  4.2070    0.99     2961   156  0.2104 0.2402        
REMARK   3     3  4.2070 -  3.6753    0.99     2939   153  0.2300 0.2553        
REMARK   3     4  3.6753 -  3.3393    0.99     2949   143  0.2687 0.2839        
REMARK   3     5  3.3393 -  3.1000    0.93     2746   137  0.2631 0.2854        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.610           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           3358                                  
REMARK   3   ANGLE     :  0.958           4514                                  
REMARK   3   CHIRALITY :  0.031            541                                  
REMARK   3   PLANARITY :  0.003            585                                  
REMARK   3   DIHEDRAL  : 12.374           1207                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 115:157 OR RESID 189:200)           
REMARK   3    ORIGIN FOR THE GROUP (A):  17.2093  -7.6320  23.3515              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9196 T22:   0.7545                                     
REMARK   3      T33:   0.5397 T12:  -0.0435                                     
REMARK   3      T13:   0.0278 T23:  -0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5144 L22:   9.3924                                     
REMARK   3      L33:   7.6339 L12:  -0.6294                                     
REMARK   3      L13:  -0.3540 L23:   0.1273                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1640 S12:   0.2679 S13:   0.3772                       
REMARK   3      S21:  -0.4783 S22:  -0.1648 S23:   0.3351                       
REMARK   3      S31:  -0.3418 S32:  -0.3612 S33:  -0.0466                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 158:188)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0082  -7.5093  16.6151              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1203 T22:   0.9487                                     
REMARK   3      T33:   0.9609 T12:  -0.2503                                     
REMARK   3      T13:   0.1585 T23:  -0.1181                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9271 L22:   4.6224                                     
REMARK   3      L33:   4.2390 L12:   0.0855                                     
REMARK   3      L13:  -0.2577 L23:   2.7079                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0803 S12:   0.1106 S13:   0.5230                       
REMARK   3      S21:   0.5265 S22:   0.7361 S23:  -1.1052                       
REMARK   3      S31:  -1.7371 S32:   1.6101 S33:  -0.6759                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 114:157 OR RESID 189:200)           
REMARK   3    ORIGIN FOR THE GROUP (A):  34.5029   8.1534 -10.7304              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7585 T22:   0.5172                                     
REMARK   3      T33:   0.6452 T12:  -0.0683                                     
REMARK   3      T13:   0.0461 T23:  -0.0381                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2416 L22:   6.8339                                     
REMARK   3      L33:   7.0230 L12:   2.1671                                     
REMARK   3      L13:   1.1267 L23:  -0.5515                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2839 S12:   0.2201 S13:  -0.6235                       
REMARK   3      S21:  -0.6216 S22:   0.2693 S23:   0.0162                       
REMARK   3      S31:  -0.1427 S32:   0.4454 S33:  -0.0145                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 158:188)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  33.6100  -0.5041  -0.0717              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7262 T22:   0.6047                                     
REMARK   3      T33:   0.6098 T12:  -0.1381                                     
REMARK   3      T13:   0.0419 T23:   0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7416 L22:   5.5998                                     
REMARK   3      L33:   4.4936 L12:   1.3655                                     
REMARK   3      L13:  -0.3174 L23:   1.9600                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3710 S12:  -0.5070 S13:   0.2594                       
REMARK   3      S21:   0.9585 S22:  -0.4288 S23:   0.0762                       
REMARK   3      S31:   0.8212 S32:  -0.4648 S33:   0.0965                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN C AND (RESID 114:157 OR RESID 189:200)           
REMARK   3    ORIGIN FOR THE GROUP (A):   7.6481 -16.6356  -1.0368              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5142 T22:   0.3926                                     
REMARK   3      T33:   0.4834 T12:  -0.0379                                     
REMARK   3      T13:  -0.0129 T23:   0.0230                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7134 L22:   1.4525                                     
REMARK   3      L33:   6.7923 L12:  -0.2133                                     
REMARK   3      L13:  -0.3592 L23:   1.1580                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2930 S12:  -0.0595 S13:  -0.4597                       
REMARK   3      S21:  -0.1860 S22:   0.1088 S23:  -0.5498                       
REMARK   3      S31:  -0.3537 S32:   0.1915 S33:  -0.4285                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN C AND (RESID 158:188)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  16.8076  -6.3373   0.9551              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9363 T22:   0.6118                                     
REMARK   3      T33:   0.6409 T12:   0.1301                                     
REMARK   3      T13:  -0.0434 T23:   0.0582                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3229 L22:   2.8802                                     
REMARK   3      L33:   4.7838 L12:   3.4055                                     
REMARK   3      L13:   1.9745 L23:   0.3220                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2043 S12:   0.1117 S13:   0.6333                       
REMARK   3      S21:   0.0853 S22:   0.1618 S23:   1.1865                       
REMARK   3      S31:  -2.0014 S32:  -0.7025 S33:  -0.1488                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN D AND (RESID 114:157 OR RESID 189:201)           
REMARK   3    ORIGIN FOR THE GROUP (A):  14.5711 -13.4530  37.7119              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8201 T22:   0.8360                                     
REMARK   3      T33:   0.6310 T12:  -0.1066                                     
REMARK   3      T13:   0.0646 T23:   0.0048                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4791 L22:   8.2144                                     
REMARK   3      L33:   9.8475 L12:   0.3083                                     
REMARK   3      L13:   1.2541 L23:   1.3281                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4037 S12:  -0.1780 S13:  -0.4685                       
REMARK   3      S21:   1.0932 S22:  -0.3712 S23:   0.6734                       
REMARK   3      S31:   0.9620 S32:  -1.4002 S33:   0.0388                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN D AND (RESID 158:188)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  22.2650 -14.3289  49.1799              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1816 T22:   0.7025                                     
REMARK   3      T33:   0.7404 T12:  -0.0036                                     
REMARK   3      T13:   0.0817 T23:   0.0733                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6362 L22:   5.1219                                     
REMARK   3      L33:   2.6386 L12:   1.0140                                     
REMARK   3      L13:   1.0886 L23:   2.1458                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6277 S12:   0.0238 S13:  -0.1192                       
REMARK   3      S21:   0.1025 S22:  -0.1939 S23:  -0.8422                       
REMARK   3      S31:   0.2303 S32:   0.4902 S33:  -0.3096                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN E AND (RESID 114:157 OR RESID 189:203)           
REMARK   3    ORIGIN FOR THE GROUP (A):  33.5169  23.0963 -10.3706              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9852 T22:   0.6183                                     
REMARK   3      T33:   0.6723 T12:   0.0432                                     
REMARK   3      T13:   0.0692 T23:   0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2792 L22:   6.5184                                     
REMARK   3      L33:   6.8755 L12:   1.6646                                     
REMARK   3      L13:   0.4575 L23:   0.6361                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3309 S12:   0.3743 S13:   0.4107                       
REMARK   3      S21:  -1.3962 S22:  -0.3306 S23:  -0.0475                       
REMARK   3      S31:  -0.6245 S32:  -0.4990 S33:   0.0719                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN E AND (RESID 158:188)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  34.6296  32.6550  -0.6687              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9968 T22:   0.6244                                     
REMARK   3      T33:   0.7822 T12:  -0.0782                                     
REMARK   3      T13:   0.1638 T23:  -0.0690                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4839 L22:   5.2556                                     
REMARK   3      L33:   4.3310 L12:   1.0630                                     
REMARK   3      L13:  -1.2424 L23:   0.5791                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3788 S12:  -0.9537 S13:  -0.1525                       
REMARK   3      S21:   1.1921 S22:  -0.0721 S23:   0.9030                       
REMARK   3      S31:   0.5693 S32:   0.0495 S33:   0.4284                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 115:136 OR RESSEQ       
REMARK   3                          143:160 OR RESSEQ 188:200 ) AND (NOT        
REMARK   3                          ELEMENT H)                                  
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 115:136 OR RESSEQ       
REMARK   3                          143:160 OR RESSEQ 188:200 ) AND (NOT        
REMARK   3                          ELEMENT H)                                  
REMARK   3     ATOM PAIRS NUMBER  : 413                                         
REMARK   3     RMSD               : 0.025                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 115:136 OR RESSEQ       
REMARK   3                          143:160 OR RESSEQ 188:200 ) AND (NOT        
REMARK   3                          ELEMENT H)                                  
REMARK   3     SELECTION          : CHAIN D AND (RESSEQ 115:136 OR RESSEQ       
REMARK   3                          143:160 OR RESSEQ 188:200 ) AND (NOT        
REMARK   3                          ELEMENT H)                                  
REMARK   3     ATOM PAIRS NUMBER  : 413                                         
REMARK   3     RMSD               : 0.063                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 115:136 OR RESSEQ       
REMARK   3                          143:160 OR RESSEQ 188:200 ) AND (NOT        
REMARK   3                          ELEMENT H)                                  
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 115:136 OR RESSEQ       
REMARK   3                          143:160 OR RESSEQ 188:200 ) AND (NOT        
REMARK   3                          ELEMENT H)                                  
REMARK   3     ATOM PAIRS NUMBER  : 413                                         
REMARK   3     RMSD               : 0.060                                       
REMARK   3    NCS OPERATOR : 4                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 115:136 OR RESSEQ       
REMARK   3                          143:160 OR RESSEQ 188:200 ) AND (NOT        
REMARK   3                          ELEMENT H)                                  
REMARK   3     SELECTION          : CHAIN E AND (RESSEQ 115:136 OR RESSEQ       
REMARK   3                          143:160 OR RESSEQ 188:200 ) AND (NOT        
REMARK   3                          ELEMENT H)                                  
REMARK   3     ATOM PAIRS NUMBER  : 413                                         
REMARK   3     RMSD               : 0.026                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5M4R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-OCT-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001790.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15510                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 53.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
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: 1G8Q                                                 
REMARK 200                                                                      
REMARK 200 REMARK: SMALL (ABOUT 40X60X15 MICRONS) BRICK-LIKE MORPHOLOGY WEAK    
REMARK 200  DIFFRACTOR BUT REASONABLE TO 3.1 ANG                                
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: ~10MG/ML BUFFER: 0.1 M          
REMARK 280  NACITRATE PH 4.0, 0.8 M (NH4)2 SO4, VAPOR DIFFUSION, SITTING        
REMARK 280  DROP, TEMPERATURE 294.15K                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       65.06000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.48500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       65.06000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       52.48500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9090 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9120 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9030 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A   110                                                      
REMARK 465     THR A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     PHE A   113                                                      
REMARK 465     VAL A   114                                                      
REMARK 465     LYS A   201                                                      
REMARK 465     GLY A   202                                                      
REMARK 465     THR A   203                                                      
REMARK 465     LYS A   204                                                      
REMARK 465     HIS A   205                                                      
REMARK 465     HIS A   206                                                      
REMARK 465     HIS A   207                                                      
REMARK 465     HIS A   208                                                      
REMARK 465     HIS A   209                                                      
REMARK 465     HIS A   210                                                      
REMARK 465     GLU B   110                                                      
REMARK 465     THR B   111                                                      
REMARK 465     GLY B   112                                                      
REMARK 465     PHE B   113                                                      
REMARK 465     LYS B   201                                                      
REMARK 465     GLY B   202                                                      
REMARK 465     THR B   203                                                      
REMARK 465     LYS B   204                                                      
REMARK 465     HIS B   205                                                      
REMARK 465     HIS B   206                                                      
REMARK 465     HIS B   207                                                      
REMARK 465     HIS B   208                                                      
REMARK 465     HIS B   209                                                      
REMARK 465     HIS B   210                                                      
REMARK 465     GLU C   110                                                      
REMARK 465     THR C   111                                                      
REMARK 465     GLY C   112                                                      
REMARK 465     PHE C   113                                                      
REMARK 465     ASP C   139                                                      
REMARK 465     LYS C   201                                                      
REMARK 465     GLY C   202                                                      
REMARK 465     THR C   203                                                      
REMARK 465     LYS C   204                                                      
REMARK 465     HIS C   205                                                      
REMARK 465     HIS C   206                                                      
REMARK 465     HIS C   207                                                      
REMARK 465     HIS C   208                                                      
REMARK 465     HIS C   209                                                      
REMARK 465     HIS C   210                                                      
REMARK 465     GLU D   110                                                      
REMARK 465     THR D   111                                                      
REMARK 465     GLY D   112                                                      
REMARK 465     PHE D   113                                                      
REMARK 465     ASP D   139                                                      
REMARK 465     ALA D   140                                                      
REMARK 465     GLY D   202                                                      
REMARK 465     THR D   203                                                      
REMARK 465     LYS D   204                                                      
REMARK 465     HIS D   205                                                      
REMARK 465     HIS D   206                                                      
REMARK 465     HIS D   207                                                      
REMARK 465     HIS D   208                                                      
REMARK 465     HIS D   209                                                      
REMARK 465     HIS D   210                                                      
REMARK 465     GLU E   110                                                      
REMARK 465     THR E   111                                                      
REMARK 465     GLY E   112                                                      
REMARK 465     PHE E   113                                                      
REMARK 465     ASP E   139                                                      
REMARK 465     ALA E   140                                                      
REMARK 465     ASN E   141                                                      
REMARK 465     LYS E   204                                                      
REMARK 465     HIS E   205                                                      
REMARK 465     HIS E   206                                                      
REMARK 465     HIS E   207                                                      
REMARK 465     HIS E   208                                                      
REMARK 465     HIS E   209                                                      
REMARK 465     HIS E   210                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP B   138     HZ2  LYS B   144              1.53            
REMARK 500   O    ASN D   180     ND2  ASN D   184              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS C 144   CD  -  CE  -  NZ  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    LYS E 144   CD  -  CE  -  NZ  ANGL. DEV. =  15.1 DEGREES          
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    ALA A 140       81.55     57.93                                   
REMARK 500    LEU A 170      -21.00     73.58                                   
REMARK 500    LYS A 171       46.63   -147.46                                   
REMARK 500    ASP B 137     -163.13   -125.95                                   
REMARK 500    ASN B 142      -39.87    -34.13                                   
REMARK 500    LEU B 170      -73.83    -87.32                                   
REMARK 500    ILE B 181      -27.79     88.44                                   
REMARK 500    ASN C 141      177.74     58.17                                   
REMARK 500    LEU C 170      -95.09    -88.05                                   
REMARK 500    SER C 179       77.66     58.49                                   
REMARK 500    SER D 168       32.37    -90.09                                   
REMARK 500    ASN D 172       -4.48     77.65                                   
REMARK 500    LEU E 170      -73.87    -79.07                                   
REMARK 500    LYS E 171       73.11   -101.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5M2C   RELATED DB: PDB                                   
REMARK 900 SAME STUDY                                                           
REMARK 900 RELATED ID: 5M3D   RELATED DB: PDB                                   
REMARK 900 SAME STUDY                                                           
REMARK 900 RELATED ID: 5M33   RELATED DB: PDB                                   
REMARK 900 SAME STUDY                                                           
REMARK 900 RELATED ID: 5M3T   RELATED DB: PDB                                   
REMARK 900 SAME STUDY                                                           
REMARK 900 RELATED ID: 1G8Q   RELATED DB: PDB                                   
REMARK 900 KITADOKORO ET AL., 2001                                              
REMARK 900 RELATED ID: 1IV5   RELATED DB: PDB                                   
REMARK 900 KITADOKORO ET AL., 2002                                              
DBREF  5M4R A  112   201  UNP    P60033   CD81_HUMAN     112    201             
DBREF  5M4R B  112   201  UNP    P60033   CD81_HUMAN     112    201             
DBREF  5M4R C  112   201  UNP    P60033   CD81_HUMAN     112    201             
DBREF  5M4R D  112   201  UNP    P60033   CD81_HUMAN     112    201             
DBREF  5M4R E  112   201  UNP    P60033   CD81_HUMAN     112    201             
SEQADV 5M4R GLU A  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R THR A  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R GLY A  202  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R THR A  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R LYS A  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS A  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS A  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS A  207  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS A  208  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS A  209  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS A  210  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R GLU B  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R THR B  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R GLY B  202  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R THR B  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R LYS B  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS B  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS B  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS B  207  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS B  208  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS B  209  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS B  210  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R GLU C  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R THR C  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R GLY C  202  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R THR C  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R LYS C  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS C  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS C  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS C  207  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS C  208  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS C  209  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS C  210  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R GLU D  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R THR D  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R GLY D  202  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R THR D  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R LYS D  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS D  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS D  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS D  207  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS D  208  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS D  209  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS D  210  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R GLU E  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R THR E  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R GLY E  202  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R THR E  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R LYS E  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS E  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS E  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS E  207  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS E  208  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS E  209  UNP  P60033              EXPRESSION TAG                 
SEQADV 5M4R HIS E  210  UNP  P60033              EXPRESSION TAG                 
SEQRES   1 A  101  GLU THR GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 A  101  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 A  101  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 A  101  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 A  101  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 A  101  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 A  101  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 A  101  LYS GLY THR LYS HIS HIS HIS HIS HIS HIS                      
SEQRES   1 B  101  GLU THR GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 B  101  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 B  101  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 B  101  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 B  101  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 B  101  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 B  101  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 B  101  LYS GLY THR LYS HIS HIS HIS HIS HIS HIS                      
SEQRES   1 C  101  GLU THR GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 C  101  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 C  101  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 C  101  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 C  101  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 C  101  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 C  101  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 C  101  LYS GLY THR LYS HIS HIS HIS HIS HIS HIS                      
SEQRES   1 D  101  GLU THR GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 D  101  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 D  101  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 D  101  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 D  101  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 D  101  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 D  101  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 D  101  LYS GLY THR LYS HIS HIS HIS HIS HIS HIS                      
SEQRES   1 E  101  GLU THR GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 E  101  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 E  101  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 E  101  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 E  101  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 E  101  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 E  101  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 E  101  LYS GLY THR LYS HIS HIS HIS HIS HIS HIS                      
HET    SO4  B 301       5                                                       
HET    EDO  B 302      10                                                       
HET    EDO  B 303      10                                                       
HET    SO4  C 301       5                                                       
HET    EDO  C 302      10                                                       
HET    SO4  E 301       5                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   6  SO4    3(O4 S 2-)                                                   
FORMUL   7  EDO    3(C2 H6 O2)                                                  
HELIX    1 AA1 ASN A  115  ASP A  137  1                                  23    
HELIX    2 AA2 ASN A  141  ASP A  155  1                                  15    
HELIX    3 AA3 SER A  160  VAL A  169  1                                  10    
HELIX    4 AA4 LYS A  171  CYS A  175  5                                   5    
HELIX    5 AA5 ASN A  180  LEU A  185  1                                   6    
HELIX    6 AA6 ASP A  189  GLY A  200  1                                  12    
HELIX    7 AA7 ASN B  115  ASP B  137  1                                  23    
HELIX    8 AA8 ASN B  141  ASP B  155  1                                  15    
HELIX    9 AA9 SER B  160  LYS B  171  1                                  12    
HELIX   10 AB1 ASN B  172  CYS B  175  5                                   4    
HELIX   11 AB2 ASP B  189  GLY B  200  1                                  12    
HELIX   12 AB3 ASN C  115  ASP C  137  1                                  23    
HELIX   13 AB4 ASN C  141  ASP C  155  1                                  15    
HELIX   14 AB5 SER C  160  LEU C  170  1                                  11    
HELIX   15 AB6 LYS C  171  CYS C  175  5                                   5    
HELIX   16 AB7 ASN C  180  LEU C  185  1                                   6    
HELIX   17 AB8 ASP C  189  GLY C  200  1                                  12    
HELIX   18 AB9 ASN D  115  ASP D  137  1                                  23    
HELIX   19 AC1 ASN D  142  ASP D  155  1                                  14    
HELIX   20 AC2 LEU D  162  THR D  167  1                                   6    
HELIX   21 AC3 ASN D  180  LYS D  187  1                                   8    
HELIX   22 AC4 ASP D  189  GLY D  200  1                                  12    
HELIX   23 AC5 ASN E  115  ASP E  137  1                                  23    
HELIX   24 AC6 ALA E  143  ASP E  155  1                                  13    
HELIX   25 AC7 SER E  160  LEU E  170  1                                  11    
HELIX   26 AC8 LYS E  171  CYS E  175  5                                   5    
HELIX   27 AC9 ILE E  182  PHE E  186  5                                   5    
HELIX   28 AD1 ASP E  189  GLY E  200  1                                  12    
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  2.04  
SSBOND   4 CYS B  157    CYS B  175                          1555   1555  2.03  
SSBOND   5 CYS C  156    CYS C  190                          1555   1555  2.04  
SSBOND   6 CYS C  157    CYS C  175                          1555   1555  2.03  
SSBOND   7 CYS D  156    CYS D  190                          1555   1555  2.05  
SSBOND   8 CYS D  157    CYS D  175                          1555   1555  2.03  
SSBOND   9 CYS E  156    CYS E  190                          1555   1555  2.03  
SSBOND  10 CYS E  157    CYS E  175                          1555   1555  2.04  
CISPEP   1 SER B  177    GLY B  178          0        -1.97                     
CISPEP   2 ASP E  137    ASP E  138          0         0.29                     
SITE     1 AC1  2 LYS B 124  HIS B 191                                          
SITE     1 AC2  3 EDO B 303  EDO C 302  LEU D 165                               
SITE     1 AC3  3 EDO B 302  ILE D 181  VAL E 169                               
SITE     1 AC4  4 PHE C 126  GLN C 133  ASN C 142  VAL C 146                    
SITE     1 AC5  3 LEU B 165  EDO B 302  THR C 166                               
SITE     1 AC6  2 LYS E 124  HIS E 191                                          
CRYST1  130.120  104.970   65.010  90.00  99.44  90.00 C 1 2 1      20          
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      0.007685  0.000000  0.001278        0.00000                         
SCALE2      0.000000  0.009527  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015593        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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