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Database: PDB
Entry: 3O8E
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HEADER    CELL ADHESION/IMMUNE SYSTEM             03-AUG-10   3O8E              
TITLE     STRUCTURE OF EXTRACELLLAR PORTION OF CD46 IN COMPLEX WITH ADENOVIRUS  
TITLE    2 TYPE 11 KNOB                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBER 36.1 KDA PROTEIN;                                    
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: ADENOVIRUS 11 KNOB (UNP RESIDUES 117-325);                 
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: MEMBRANE COFACTOR PROTEIN;                                 
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 FRAGMENT: CD46 SCR1-SCR4 (UNP RESIDUES 35-286);                      
COMPND  10 SYNONYM: TROPHOBLAST LEUKOCYTE COMMON ANTIGEN, TLX;                  
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN ADENOVIRUS 11;                            
SOURCE   3 ORGANISM_TAXID: 10541;                                               
SOURCE   4 GENE: CD46, MCP, MIC10;                                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET-15B;                                  
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  16 EXPRESSION_SYSTEM_CELL_LINE: CHINESE HAMSTER OVARY (CHO) CELLS       
KEYWDS    SHORT CONSENSUS REPEAT, COMPLEMENT CONTROL PROTEIN, FIBER KNOB,       
KEYWDS   2 VIRUS-RECEPTOR INTERACTION, CELL ADHESION-IMMUNITY COMPLEX,          
KEYWDS   3 ADENOVIRUS, CD46, CELL ADHESION - IMMUNE SYSTEM COMPLEX, CELL        
KEYWDS   4 ADHESION-IMMUNE SYSTEM COMPLEX                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.D.PERSSON,N.B.SCHMITZ,J.M.CASASNOVAS,T.STEHLE                       
REVDAT   7   29-JUL-20 3O8E    1       COMPND REMARK SEQADV HETNAM              
REVDAT   7 2                   1       LINK   SITE   ATOM                       
REVDAT   6   08-NOV-17 3O8E    1       REMARK                                   
REVDAT   5   05-OCT-11 3O8E    1       JRNL                                     
REVDAT   4   07-SEP-11 3O8E    1       JRNL                                     
REVDAT   3   24-AUG-11 3O8E    1       JRNL   VERSN                             
REVDAT   2   02-FEB-11 3O8E    1       JRNL                                     
REVDAT   1   13-OCT-10 3O8E    0                                                
JRNL        AUTH   B.D.PERSSON,N.B.SCHMITZ,C.SANTIAGO,G.ZOCHER,M.LARVIE,        
JRNL        AUTH 2 U.SCHEU,J.M.CASASNOVAS,T.STEHLE                              
JRNL        TITL   STRUCTURE OF THE EXTRACELLULAR PORTION OF CD46 PROVIDES      
JRNL        TITL 2 INSIGHTS INTO ITS INTERACTIONS WITH COMPLEMENT PROTEINS AND  
JRNL        TITL 3 PATHOGENS.                                                   
JRNL        REF    PLOS PATHOG.                  V.   6 01122 2010              
JRNL        REFN                   ISSN 1553-7366                               
JRNL        PMID   20941397                                                     
JRNL        DOI    10.1371/JOURNAL.PPAT.1001122                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.84 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.8.0                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.84                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 33537                          
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)  : 0.210                          
REMARK   3   R VALUE            (WORKING SET)  : 0.210                          
REMARK   3   FREE R VALUE                      : 0.229                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.020                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1682                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 17                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.84                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.94                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2861                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2631                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2721                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2591                   
REMARK   3   BIN FREE R VALUE                        : 0.3413                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.89                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 140                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7053                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 100                                     
REMARK   3   SOLVENT ATOMS            : 378                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.82                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.99980                                             
REMARK   3    B22 (A**2) : -7.99980                                             
REMARK   3    B33 (A**2) : 15.99950                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.416               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.884                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.872                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 7369   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 10061  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2386   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 182    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1058   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 7369   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1001   ; 5.000  ; NULL                
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7773   ; 4.000  ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.007                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.91                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.00                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.33                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: {A|129 - 179}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   36.2665  -31.0490   22.2765           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0935 T22:   -0.0575                                    
REMARK   3     T33:   -0.0471 T12:    0.0168                                    
REMARK   3     T13:   -0.0014 T23:    0.0366                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4103 L22:    0.3579                                    
REMARK   3     L33:    0.1363 L12:    0.3383                                    
REMARK   3     L13:   -0.5156 L23:    0.0287                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0017 S12:    0.0181 S13:    0.0058                     
REMARK   3     S21:   -0.0129 S22:   -0.0094 S23:    0.0492                     
REMARK   3     S31:   -0.0108 S32:   -0.0349 S33:    0.0077                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: {A|180 - 208}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   32.3465  -25.5507   13.8915           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0476 T22:   -0.0118                                    
REMARK   3     T33:   -0.0045 T12:    0.0182                                    
REMARK   3     T13:    0.0170 T23:    0.0293                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2228 L22:   -0.1639                                    
REMARK   3     L33:    0.0015 L12:   -0.1387                                    
REMARK   3     L13:    0.0686 L23:    0.6388                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0047 S12:    0.0121 S13:   -0.0125                     
REMARK   3     S21:   -0.0118 S22:   -0.0045 S23:    0.0236                     
REMARK   3     S31:    0.0096 S32:   -0.0021 S33:   -0.0002                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: {A|209 - 294}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   41.0554  -22.4762   19.3417           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1430 T22:   -0.1258                                    
REMARK   3     T33:   -0.0779 T12:    0.0197                                    
REMARK   3     T13:    0.0446 T23:    0.0222                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2414 L22:    1.0505                                    
REMARK   3     L33:    0.2843 L12:   -0.1267                                    
REMARK   3     L13:    0.7363 L23:   -0.1637                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0178 S12:   -0.0107 S13:    0.0200                     
REMARK   3     S21:   -0.0029 S22:    0.0005 S23:    0.0369                     
REMARK   3     S31:   -0.0216 S32:   -0.0152 S33:   -0.0183                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: {A|295 - 306}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   36.1728  -35.5076   -1.5381           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0019 T22:   -0.0061                                    
REMARK   3     T33:   -0.0114 T12:   -0.0046                                    
REMARK   3     T13:   -0.0066 T23:    0.0063                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   -0.1171 L22:    0.1171                                    
REMARK   3     L33:    0.1505 L12:    0.0676                                    
REMARK   3     L13:    0.1351 L23:   -0.0435                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0007 S12:    0.0042 S13:   -0.0013                     
REMARK   3     S21:   -0.0042 S22:   -0.0016 S23:    0.0044                     
REMARK   3     S31:    0.0014 S32:   -0.0061 S33:    0.0009                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: {A|307 - 325}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   43.8822  -28.6046   19.0047           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0396 T22:   -0.0268                                    
REMARK   3     T33:   -0.0305 T12:    0.0093                                    
REMARK   3     T13:    0.0036 T23:    0.0039                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.1169 L22:    0.1211                                    
REMARK   3     L33:    0.0000 L12:   -0.0281                                    
REMARK   3     L13:    0.2565 L23:    0.1591                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0023 S12:   -0.0055 S13:    0.0065                     
REMARK   3     S21:    0.0109 S22:   -0.0023 S23:   -0.0008                     
REMARK   3     S31:   -0.0071 S32:    0.0003 S33:    0.0046                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: {C|129 - 179}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   36.2590   31.1302  -23.6099           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0775 T22:   -0.0438                                    
REMARK   3     T33:   -0.0425 T12:    0.0003                                    
REMARK   3     T13:    0.0075 T23:    0.0187                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8367 L22:   -0.1460                                    
REMARK   3     L33:    0.0534 L12:   -0.4617                                    
REMARK   3     L13:    0.6175 L23:    0.4552                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0032 S12:   -0.0123 S13:   -0.0016                     
REMARK   3     S21:    0.0085 S22:   -0.0036 S23:    0.0536                     
REMARK   3     S31:    0.0097 S32:   -0.0348 S33:    0.0004                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: {C|180 - 208}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   32.3433   25.6080  -15.2521           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0318 T22:   -0.0086                                    
REMARK   3     T33:   -0.0116 T12:    0.0010                                    
REMARK   3     T13:   -0.0124 T23:   -0.0113                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4072 L22:   -0.1750                                    
REMARK   3     L33:    0.0204 L12:   -0.1411                                    
REMARK   3     L13:    0.1377 L23:    0.5182                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0032 S12:   -0.0212 S13:    0.0100                     
REMARK   3     S21:    0.0113 S22:    0.0008 S23:    0.0201                     
REMARK   3     S31:   -0.0023 S32:   -0.0073 S33:   -0.0040                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: {C|209 - 265}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   41.6851   23.0457  -23.2305           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1035 T22:   -0.0826                                    
REMARK   3     T33:   -0.0777 T12:   -0.0100                                    
REMARK   3     T13:   -0.0299 T23:    0.0108                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2032 L22:    0.6304                                    
REMARK   3     L33:    0.0784 L12:    0.3022                                    
REMARK   3     L13:   -0.0754 L23:    0.0490                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0143 S12:    0.0044 S13:    0.0078                     
REMARK   3     S21:   -0.0118 S22:   -0.0058 S23:    0.0051                     
REMARK   3     S31:   -0.0043 S32:   -0.0173 S33:   -0.0086                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: {C|266 - 303}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   39.6092   24.0408  -12.5728           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0590 T22:   -0.0641                                    
REMARK   3     T33:   -0.0339 T12:   -0.0059                                    
REMARK   3     T13:   -0.0175 T23:    0.0047                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.1664 L22:    0.3754                                    
REMARK   3     L33:    0.0318 L12:    0.0578                                    
REMARK   3     L13:    1.0440 L23:    0.8100                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0020 S12:   -0.0257 S13:    0.0113                     
REMARK   3     S21:    0.0205 S22:    0.0082 S23:    0.0083                     
REMARK   3     S31:   -0.0092 S32:   -0.0100 S33:   -0.0062                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: {C|304 - 325}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   41.9401   30.3586  -17.6825           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0420 T22:   -0.0256                                    
REMARK   3     T33:   -0.0334 T12:    0.0021                                    
REMARK   3     T13:   -0.0006 T23:    0.0082                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3309 L22:    0.0782                                    
REMARK   3     L33:    0.0732 L12:   -0.1189                                    
REMARK   3     L13:    0.0486 L23:   -0.1147                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0028 S12:   -0.0088 S13:   -0.0015                     
REMARK   3     S21:    0.0053 S22:   -0.0032 S23:    0.0118                     
REMARK   3     S31:   -0.0032 S32:   -0.0131 S33:    0.0004                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: {B|1 - 62}                                             
REMARK   3    ORIGIN FOR THE GROUP (A):   20.7271   -5.3289   21.8865           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0078 T22:    0.0774                                    
REMARK   3     T33:    0.1050 T12:    0.0380                                    
REMARK   3     T13:    0.0451 T23:    0.0366                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.7888 L22:    2.4276                                    
REMARK   3     L33:    0.9046 L12:   -0.4264                                    
REMARK   3     L13:    0.8612 L23:   -0.8834                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0011 S12:   -0.0178 S13:    0.0028                     
REMARK   3     S21:    0.0187 S22:   -0.0061 S23:    0.0674                     
REMARK   3     S31:   -0.0171 S32:   -0.0587 S33:    0.0050                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: {B|63 - 126}                                           
REMARK   3    ORIGIN FOR THE GROUP (A):   41.0215   -7.7149   -8.4517           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0369 T22:    0.0253                                    
REMARK   3     T33:    0.0145 T12:   -0.0033                                    
REMARK   3     T13:    0.0049 T23:    0.0354                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8070 L22:    1.3804                                    
REMARK   3     L33:    0.7306 L12:    0.1731                                    
REMARK   3     L13:    0.5705 L23:   -0.1029                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0035 S12:   -0.0046 S13:   -0.0095                     
REMARK   3     S21:    0.0035 S22:   -0.0012 S23:    0.0336                     
REMARK   3     S31:    0.0087 S32:   -0.0125 S33:   -0.0023                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: {B|127 - 187}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   47.7659   -5.8193  -45.3700           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1167 T22:    0.0878                                    
REMARK   3     T33:    0.0257 T12:   -0.0016                                    
REMARK   3     T13:    0.0224 T23:   -0.0132                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6960 L22:    2.7602                                    
REMARK   3     L33:    1.4378 L12:    0.4677                                    
REMARK   3     L13:   -0.1760 L23:    0.3223                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0080 S12:    0.0052 S13:    0.0014                     
REMARK   3     S21:    0.0064 S22:    0.0111 S23:    0.0136                     
REMARK   3     S31:    0.0111 S32:   -0.0030 S33:   -0.0031                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: {B|188 - 252}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   27.5821    8.5260  -66.2485           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1194 T22:    0.1471                                    
REMARK   3     T33:    0.1199 T12:   -0.0116                                    
REMARK   3     T13:   -0.0027 T23:    0.0223                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.2112 L22:    2.5271                                    
REMARK   3     L33:    2.8740 L12:    1.1317                                    
REMARK   3     L13:   -1.0821 L23:    0.5280                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0035 S12:   -0.0096 S13:    0.0021                     
REMARK   3     S21:    0.0053 S22:   -0.0005 S23:    0.0175                     
REMARK   3     S31:    0.0026 S32:   -0.0119 S33:   -0.0030                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: {D|1 - 62}                                             
REMARK   3    ORIGIN FOR THE GROUP (A):   20.7145    5.3811  -23.2574           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0468 T22:    0.0515                                    
REMARK   3     T33:    0.1030 T12:   -0.0187                                    
REMARK   3     T13:   -0.0351 T23:    0.0493                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2053 L22:    3.0245                                    
REMARK   3     L33:    1.1019 L12:    0.7168                                    
REMARK   3     L13:   -0.8589 L23:   -0.5481                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0034 S12:    0.0240 S13:    0.0081                     
REMARK   3     S21:   -0.0188 S22:    0.0035 S23:    0.0635                     
REMARK   3     S31:    0.0096 S32:   -0.0605 S33:   -0.0001                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: {D|63 - 125}                                           
REMARK   3    ORIGIN FOR THE GROUP (A):   41.1792    8.0437    7.2476           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0435 T22:    0.0108                                    
REMARK   3     T33:    0.0035 T12:   -0.0009                                    
REMARK   3     T13:    0.0223 T23:    0.0293                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4725 L22:    1.7572                                    
REMARK   3     L33:    0.7511 L12:   -0.1439                                    
REMARK   3     L13:   -0.2671 L23:    0.4580                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0049 S12:    0.0077 S13:    0.0150                     
REMARK   3     S21:   -0.0022 S22:    0.0117 S23:    0.0306                     
REMARK   3     S31:   -0.0096 S32:   -0.0200 S33:   -0.0067                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: {D|126 - 191}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   47.3351    5.8950   44.5954           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1262 T22:    0.0920                                    
REMARK   3     T33:    0.0292 T12:   -0.0028                                    
REMARK   3     T13:   -0.0262 T23:   -0.0041                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.1272 L22:    2.4989                                    
REMARK   3     L33:    1.5405 L12:   -0.2702                                    
REMARK   3     L13:    0.5711 L23:    0.0636                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0054 S12:   -0.0101 S13:   -0.0046                     
REMARK   3     S21:   -0.0035 S22:    0.0117 S23:    0.0153                     
REMARK   3     S31:   -0.0142 S32:    0.0014 S33:   -0.0063                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: {D|192 - 252}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   26.8210   -9.4451   65.5006           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1192 T22:    0.1474                                    
REMARK   3     T33:    0.1303 T12:    0.0074                                    
REMARK   3     T13:    0.0121 T23:    0.0192                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.5555 L22:    2.1967                                    
REMARK   3     L33:    3.0018 L12:   -0.8493                                    
REMARK   3     L13:    0.9017 L23:    0.3016                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0002 S12:    0.0009 S13:    0.0026                     
REMARK   3     S21:   -0.0004 S22:    0.0016 S23:    0.0104                     
REMARK   3     S31:   -0.0027 S32:   -0.0104 S33:   -0.0017                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3O8E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000060794.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : YES                                
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33537                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.840                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.12800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.84                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.99                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53100                            
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: PDB ENTRY 1CKL AND 3EXV                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MICROSEEDING, PH 8.0, VAPOR DIFFUSION,   
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      111.49500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      111.49500            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      111.49500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL MOLECULE CAN BE DESCRIBED AS COMPOSED OF A    
REMARK 300 THREEFOLD ARRANGEMENT OF THE TWO POLYMERIC CHAINS                    
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: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F                            
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 -0.500000 -0.866025  0.000000       54.08000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      -93.66931            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000      108.16000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G                               
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 -0.500000 -0.866025  0.000000      108.16000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000       54.08000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000       93.66931            
REMARK 350   BIOMT3   3  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   113                                                      
REMARK 465     SER A   114                                                      
REMARK 465     HIS A   115                                                      
REMARK 465     MET A   116                                                      
REMARK 465     GLY A   117                                                      
REMARK 465     LEU A   118                                                      
REMARK 465     THR A   119                                                      
REMARK 465     PHE A   120                                                      
REMARK 465     ASN A   121                                                      
REMARK 465     SER A   122                                                      
REMARK 465     ASN A   123                                                      
REMARK 465     ASN A   124                                                      
REMARK 465     ILE A   125                                                      
REMARK 465     CYS A   126                                                      
REMARK 465     ILE A   127                                                      
REMARK 465     ASP A   128                                                      
REMARK 465     GLY C   113                                                      
REMARK 465     SER C   114                                                      
REMARK 465     HIS C   115                                                      
REMARK 465     MET C   116                                                      
REMARK 465     GLY C   117                                                      
REMARK 465     LEU C   118                                                      
REMARK 465     THR C   119                                                      
REMARK 465     PHE C   120                                                      
REMARK 465     ASN C   121                                                      
REMARK 465     SER C   122                                                      
REMARK 465     ASN C   123                                                      
REMARK 465     ASN C   124                                                      
REMARK 465     ILE C   125                                                      
REMARK 465     CYS C   126                                                      
REMARK 465     ILE C   127                                                      
REMARK 465     ASP C   128                                                      
REMARK 465     GLY D    81                                                      
REMARK 465     THR D    82                                                      
REMARK 465     TYR D    83                                                      
REMARK 465     GLU D    84                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU B  84    CB   CG   CD   OE1  OE2                             
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    ASN A 139       75.97     39.97                                   
REMARK 500    VAL A 178      -59.13   -121.59                                   
REMARK 500    ASN A 278     -105.87     57.43                                   
REMARK 500    ARG A 279      -66.05     53.22                                   
REMARK 500    THR A 286       98.79    -69.12                                   
REMARK 500    THR A 309      -70.10   -128.63                                   
REMARK 500    GLU B   2     -177.40     62.49                                   
REMARK 500    THR B  82     -166.54   -113.77                                   
REMARK 500    TYR B 213     -160.91   -106.19                                   
REMARK 500    ASN C 130      -33.02     63.89                                   
REMARK 500    ASN C 139       78.68     38.08                                   
REMARK 500    VAL C 178      -60.46   -124.34                                   
REMARK 500    ASN C 278     -106.52     57.60                                   
REMARK 500    ARG C 279      -64.64     53.18                                   
REMARK 500    THR C 309      -76.77   -127.27                                   
REMARK 500    GLU D   2     -151.96    -95.32                                   
REMARK 500    GLU D 143       -5.81     67.62                                   
REMARK 500    ALA D 160      121.41    -38.22                                   
REMARK 500    TYR D 213     -166.55   -106.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3O8E A  117   325  UNP    Q772X2   Q772X2_9ADEN   117    325             
DBREF  3O8E B    1   252  UNP    P15529   MCP_HUMAN       35    286             
DBREF  3O8E C  117   325  UNP    Q772X2   Q772X2_9ADEN   117    325             
DBREF  3O8E D    1   252  UNP    P15529   MCP_HUMAN       35    286             
SEQADV 3O8E GLY A  113  UNP  Q772X2              EXPRESSION TAG                 
SEQADV 3O8E SER A  114  UNP  Q772X2              EXPRESSION TAG                 
SEQADV 3O8E HIS A  115  UNP  Q772X2              EXPRESSION TAG                 
SEQADV 3O8E MET A  116  UNP  Q772X2              EXPRESSION TAG                 
SEQADV 3O8E GLY C  113  UNP  Q772X2              EXPRESSION TAG                 
SEQADV 3O8E SER C  114  UNP  Q772X2              EXPRESSION TAG                 
SEQADV 3O8E HIS C  115  UNP  Q772X2              EXPRESSION TAG                 
SEQADV 3O8E MET C  116  UNP  Q772X2              EXPRESSION TAG                 
SEQRES   1 A  213  GLY SER HIS MET GLY LEU THR PHE ASN SER ASN ASN ILE          
SEQRES   2 A  213  CYS ILE ASP ASP ASN ILE ASN THR LEU TRP THR GLY VAL          
SEQRES   3 A  213  ASN PRO THR GLU ALA ASN CYS GLN ILE MET ASN SER SER          
SEQRES   4 A  213  GLU SER ASN ASP CYS LYS LEU ILE LEU THR LEU VAL LYS          
SEQRES   5 A  213  THR GLY ALA LEU VAL THR ALA PHE VAL TYR VAL ILE GLY          
SEQRES   6 A  213  VAL SER ASN ASN PHE ASN MET LEU THR THR HIS ARG ASN          
SEQRES   7 A  213  ILE ASN PHE THR ALA GLU LEU PHE PHE ASP SER THR GLY          
SEQRES   8 A  213  ASN LEU LEU THR ARG LEU SER SER LEU LYS THR PRO LEU          
SEQRES   9 A  213  ASN HIS LYS SER GLY GLN ASN MET ALA THR GLY ALA ILE          
SEQRES  10 A  213  THR ASN ALA LYS GLY PHE MET PRO SER THR THR ALA TYR          
SEQRES  11 A  213  PRO PHE ASN ASP ASN SER ARG GLU LYS GLU ASN TYR ILE          
SEQRES  12 A  213  TYR GLY THR CYS TYR TYR THR ALA SER ASP ARG THR ALA          
SEQRES  13 A  213  PHE PRO ILE ASP ILE SER VAL MET LEU ASN ARG ARG ALA          
SEQRES  14 A  213  ILE ASN ASP GLU THR SER TYR CYS ILE ARG ILE THR TRP          
SEQRES  15 A  213  SER TRP ASN THR GLY ASP ALA PRO GLU VAL GLN THR SER          
SEQRES  16 A  213  ALA THR THR LEU VAL THR SER PRO PHE THR PHE TYR TYR          
SEQRES  17 A  213  ILE ARG GLU ASP ASP                                          
SEQRES   1 B  252  CYS GLU GLU PRO PRO THR PHE GLU ALA MET GLU LEU ILE          
SEQRES   2 B  252  GLY LYS PRO LYS PRO TYR TYR GLU ILE GLY GLU ARG VAL          
SEQRES   3 B  252  ASP TYR LYS CYS LYS LYS GLY TYR PHE TYR ILE PRO PRO          
SEQRES   4 B  252  LEU ALA THR HIS THR ILE CYS ASP ARG ASN HIS THR TRP          
SEQRES   5 B  252  LEU PRO VAL SER ASP ASP ALA CYS TYR ARG GLU THR CYS          
SEQRES   6 B  252  PRO TYR ILE ARG ASP PRO LEU ASN GLY GLN ALA VAL PRO          
SEQRES   7 B  252  ALA ASN GLY THR TYR GLU PHE GLY TYR GLN MET HIS PHE          
SEQRES   8 B  252  ILE CYS ASN GLU GLY TYR TYR LEU ILE GLY GLU GLU ILE          
SEQRES   9 B  252  LEU TYR CYS GLU LEU LYS GLY SER VAL ALA ILE TRP SER          
SEQRES  10 B  252  GLY LYS PRO PRO ILE CYS GLU LYS VAL LEU CYS THR PRO          
SEQRES  11 B  252  PRO PRO LYS ILE LYS ASN GLY LYS HIS THR PHE SER GLU          
SEQRES  12 B  252  VAL GLU VAL PHE GLU TYR LEU ASP ALA VAL THR TYR SER          
SEQRES  13 B  252  CYS ASP PRO ALA PRO GLY PRO ASP PRO PHE SER LEU ILE          
SEQRES  14 B  252  GLY GLU SER THR ILE TYR CYS GLY ASP ASN SER VAL TRP          
SEQRES  15 B  252  SER ARG ALA ALA PRO GLU CYS LYS VAL VAL LYS CYS ARG          
SEQRES  16 B  252  PHE PRO VAL VAL GLU ASN GLY LYS GLN ILE SER GLY PHE          
SEQRES  17 B  252  GLY LYS LYS PHE TYR TYR LYS ALA THR VAL MET PHE GLU          
SEQRES  18 B  252  CYS ASP LYS GLY PHE TYR LEU ASP GLY SER ASP THR ILE          
SEQRES  19 B  252  VAL CYS ASP SER ASN SER THR TRP ASP PRO PRO VAL PRO          
SEQRES  20 B  252  LYS CYS LEU LYS VAL                                          
SEQRES   1 C  213  GLY SER HIS MET GLY LEU THR PHE ASN SER ASN ASN ILE          
SEQRES   2 C  213  CYS ILE ASP ASP ASN ILE ASN THR LEU TRP THR GLY VAL          
SEQRES   3 C  213  ASN PRO THR GLU ALA ASN CYS GLN ILE MET ASN SER SER          
SEQRES   4 C  213  GLU SER ASN ASP CYS LYS LEU ILE LEU THR LEU VAL LYS          
SEQRES   5 C  213  THR GLY ALA LEU VAL THR ALA PHE VAL TYR VAL ILE GLY          
SEQRES   6 C  213  VAL SER ASN ASN PHE ASN MET LEU THR THR HIS ARG ASN          
SEQRES   7 C  213  ILE ASN PHE THR ALA GLU LEU PHE PHE ASP SER THR GLY          
SEQRES   8 C  213  ASN LEU LEU THR ARG LEU SER SER LEU LYS THR PRO LEU          
SEQRES   9 C  213  ASN HIS LYS SER GLY GLN ASN MET ALA THR GLY ALA ILE          
SEQRES  10 C  213  THR ASN ALA LYS GLY PHE MET PRO SER THR THR ALA TYR          
SEQRES  11 C  213  PRO PHE ASN ASP ASN SER ARG GLU LYS GLU ASN TYR ILE          
SEQRES  12 C  213  TYR GLY THR CYS TYR TYR THR ALA SER ASP ARG THR ALA          
SEQRES  13 C  213  PHE PRO ILE ASP ILE SER VAL MET LEU ASN ARG ARG ALA          
SEQRES  14 C  213  ILE ASN ASP GLU THR SER TYR CYS ILE ARG ILE THR TRP          
SEQRES  15 C  213  SER TRP ASN THR GLY ASP ALA PRO GLU VAL GLN THR SER          
SEQRES  16 C  213  ALA THR THR LEU VAL THR SER PRO PHE THR PHE TYR TYR          
SEQRES  17 C  213  ILE ARG GLU ASP ASP                                          
SEQRES   1 D  252  CYS GLU GLU PRO PRO THR PHE GLU ALA MET GLU LEU ILE          
SEQRES   2 D  252  GLY LYS PRO LYS PRO TYR TYR GLU ILE GLY GLU ARG VAL          
SEQRES   3 D  252  ASP TYR LYS CYS LYS LYS GLY TYR PHE TYR ILE PRO PRO          
SEQRES   4 D  252  LEU ALA THR HIS THR ILE CYS ASP ARG ASN HIS THR TRP          
SEQRES   5 D  252  LEU PRO VAL SER ASP ASP ALA CYS TYR ARG GLU THR CYS          
SEQRES   6 D  252  PRO TYR ILE ARG ASP PRO LEU ASN GLY GLN ALA VAL PRO          
SEQRES   7 D  252  ALA ASN GLY THR TYR GLU PHE GLY TYR GLN MET HIS PHE          
SEQRES   8 D  252  ILE CYS ASN GLU GLY TYR TYR LEU ILE GLY GLU GLU ILE          
SEQRES   9 D  252  LEU TYR CYS GLU LEU LYS GLY SER VAL ALA ILE TRP SER          
SEQRES  10 D  252  GLY LYS PRO PRO ILE CYS GLU LYS VAL LEU CYS THR PRO          
SEQRES  11 D  252  PRO PRO LYS ILE LYS ASN GLY LYS HIS THR PHE SER GLU          
SEQRES  12 D  252  VAL GLU VAL PHE GLU TYR LEU ASP ALA VAL THR TYR SER          
SEQRES  13 D  252  CYS ASP PRO ALA PRO GLY PRO ASP PRO PHE SER LEU ILE          
SEQRES  14 D  252  GLY GLU SER THR ILE TYR CYS GLY ASP ASN SER VAL TRP          
SEQRES  15 D  252  SER ARG ALA ALA PRO GLU CYS LYS VAL VAL LYS CYS ARG          
SEQRES  16 D  252  PHE PRO VAL VAL GLU ASN GLY LYS GLN ILE SER GLY PHE          
SEQRES  17 D  252  GLY LYS LYS PHE TYR TYR LYS ALA THR VAL MET PHE GLU          
SEQRES  18 D  252  CYS ASP LYS GLY PHE TYR LEU ASP GLY SER ASP THR ILE          
SEQRES  19 D  252  VAL CYS ASP SER ASN SER THR TRP ASP PRO PRO VAL PRO          
SEQRES  20 D  252  LYS CYS LEU LYS VAL                                          
MODRES 3O8E ASN D   80  ASN  GLYCOSYLATION SITE                                 
MODRES 3O8E ASN B   80  ASN  GLYCOSYLATION SITE                                 
MODRES 3O8E ASN B   49  ASN  GLYCOSYLATION SITE                                 
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    DTD  A2816       8                                                       
HET    DTD  C2815       8                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     DTD DITHIANE DIOL                                                    
FORMUL   5  NAG    6(C8 H15 N O6)                                               
FORMUL   8  DTD    2(C4 H8 O2 S2)                                               
FORMUL  10  HOH   *378(H2 O)                                                    
HELIX    1   1 ASP A  129  ILE A  131  5                                   3    
HELIX    2   2 SER A  179  MET A  184  1                                   6    
HELIX    3   3 LEU A  185  HIS A  188  5                                   4    
HELIX    4   4 ASN A  231  MET A  236  5                                   6    
HELIX    5   5 ARG A  249  GLU A  252  5                                   4    
HELIX    6   6 SER C  179  MET C  184  1                                   6    
HELIX    7   7 LEU C  185  HIS C  188  5                                   4    
HELIX    8   8 ASN C  231  MET C  236  5                                   6    
HELIX    9   9 ASP C  246  GLU C  252  5                                   7    
HELIX   10  10 SER D   56  ASP D   58  5                                   3    
HELIX   11  11 GLY D  177  VAL D  181  5                                   5    
SHEET    1   A 4 THR A 133  TRP A 135  0                                        
SHEET    2   A 4 CYS A 156  THR A 165 -1  O  LEU A 162   N  LEU A 134           
SHEET    3   A 4 LEU A 168  GLY A 177 -1  O  ILE A 176   N  LYS A 157           
SHEET    4   A 4 PHE A 316  ILE A 321 -1  O  PHE A 316   N  VAL A 173           
SHEET    1   B 4 ASN A 190  PHE A 199  0                                        
SHEET    2   B 4 TYR A 288  ASN A 297 -1  O  ILE A 292   N  ALA A 195           
SHEET    3   B 4 ALA A 268  LEU A 277 -1  N  ASP A 272   O  SER A 295           
SHEET    4   B 4 TYR A 254  THR A 262 -1  N  ILE A 255   O  VAL A 275           
SHEET    1   C 2 LYS A 219  SER A 220  0                                        
SHEET    2   C 2 ASN A 223  MET A 224 -1  O  ASN A 223   N  SER A 220           
SHEET    1   D 3 MET B  10  LEU B  12  0                                        
SHEET    2   D 3 ARG B  25  CYS B  30 -1  O  LYS B  29   N  GLU B  11           
SHEET    3   D 3 HIS B  43  ILE B  45 -1  O  THR B  44   N  VAL B  26           
SHEET    1   E 2 TYR B  34  TYR B  36  0                                        
SHEET    2   E 2 CYS B  60  ARG B  62 -1  O  TYR B  61   N  PHE B  35           
SHEET    1   F 4 GLY B  74  PRO B  78  0                                        
SHEET    2   F 4 GLN B  88  CYS B  93 -1  O  HIS B  90   N  VAL B  77           
SHEET    3   F 4 ILE B 104  LEU B 109 -1  O  LEU B 105   N  MET B  89           
SHEET    4   F 4 ALA B 114  TRP B 116 -1  O  ILE B 115   N  GLU B 108           
SHEET    1   G 2 TYR B  97  ILE B 100  0                                        
SHEET    2   G 2 ILE B 122  LYS B 125 -1  O  GLU B 124   N  TYR B  98           
SHEET    1   H 2 LEU B 127  CYS B 128  0                                        
SHEET    2   H 2 PHE B 147  GLU B 148 -1  O  PHE B 147   N  CYS B 128           
SHEET    1   I 3 GLY B 137  HIS B 139  0                                        
SHEET    2   I 3 ALA B 152  CYS B 157 -1  O  SER B 156   N  LYS B 138           
SHEET    3   I 3 THR B 173  TYR B 175 -1  O  ILE B 174   N  VAL B 153           
SHEET    1   J 2 SER B 167  ILE B 169  0                                        
SHEET    2   J 2 GLU B 188  LYS B 190 -1  O  LYS B 190   N  SER B 167           
SHEET    1   K 4 GLY B 202  SER B 206  0                                        
SHEET    2   K 4 THR B 217  CYS B 222 -1  O  GLU B 221   N  LYS B 203           
SHEET    3   K 4 THR B 233  CYS B 236 -1  O  ILE B 234   N  VAL B 218           
SHEET    4   K 4 TRP B 242  ASP B 243 -1  O  ASP B 243   N  VAL B 235           
SHEET    1   L 2 PHE B 226  ASP B 229  0                                        
SHEET    2   L 2 LYS B 248  LYS B 251 -1  O  LEU B 250   N  TYR B 227           
SHEET    1   M 4 THR C 133  TRP C 135  0                                        
SHEET    2   M 4 CYS C 156  THR C 165 -1  O  LEU C 162   N  LEU C 134           
SHEET    3   M 4 LEU C 168  GLY C 177 -1  O  ILE C 176   N  LYS C 157           
SHEET    4   M 4 PHE C 316  ILE C 321 -1  O  PHE C 318   N  ALA C 171           
SHEET    1   N 4 ASN C 190  PHE C 199  0                                        
SHEET    2   N 4 TYR C 288  ASN C 297 -1  O  ILE C 292   N  ALA C 195           
SHEET    3   N 4 ALA C 268  LEU C 277 -1  N  SER C 274   O  THR C 293           
SHEET    4   N 4 TYR C 254  THR C 262 -1  N  ILE C 255   O  VAL C 275           
SHEET    1   O 2 LYS C 219  SER C 220  0                                        
SHEET    2   O 2 ASN C 223  MET C 224 -1  O  ASN C 223   N  SER C 220           
SHEET    1   P 3 MET D  10  LEU D  12  0                                        
SHEET    2   P 3 ARG D  25  CYS D  30 -1  O  LYS D  29   N  GLU D  11           
SHEET    3   P 3 HIS D  43  ILE D  45 -1  O  THR D  44   N  VAL D  26           
SHEET    1   Q 2 TYR D  34  TYR D  36  0                                        
SHEET    2   Q 2 CYS D  60  ARG D  62 -1  O  TYR D  61   N  PHE D  35           
SHEET    1   R 4 GLY D  74  PRO D  78  0                                        
SHEET    2   R 4 GLN D  88  CYS D  93 -1  O  HIS D  90   N  VAL D  77           
SHEET    3   R 4 ILE D 104  LEU D 109 -1  O  LEU D 105   N  MET D  89           
SHEET    4   R 4 ALA D 114  TRP D 116 -1  O  ILE D 115   N  GLU D 108           
SHEET    1   S 2 TYR D  97  ILE D 100  0                                        
SHEET    2   S 2 ILE D 122  LYS D 125 -1  O  GLU D 124   N  TYR D  98           
SHEET    1   T 2 LEU D 127  CYS D 128  0                                        
SHEET    2   T 2 PHE D 147  GLU D 148 -1  O  PHE D 147   N  CYS D 128           
SHEET    1   U 3 GLY D 137  HIS D 139  0                                        
SHEET    2   U 3 ALA D 152  CYS D 157 -1  O  SER D 156   N  LYS D 138           
SHEET    3   U 3 THR D 173  TYR D 175 -1  O  ILE D 174   N  VAL D 153           
SHEET    1   V 2 SER D 167  ILE D 169  0                                        
SHEET    2   V 2 GLU D 188  LYS D 190 -1  O  LYS D 190   N  SER D 167           
SHEET    1   W 4 GLY D 202  SER D 206  0                                        
SHEET    2   W 4 THR D 217  CYS D 222 -1  O  GLU D 221   N  LYS D 203           
SHEET    3   W 4 THR D 233  CYS D 236 -1  O  ILE D 234   N  VAL D 218           
SHEET    4   W 4 TRP D 242  ASP D 243 -1  O  ASP D 243   N  VAL D 235           
SHEET    1   X 2 PHE D 226  ASP D 229  0                                        
SHEET    2   X 2 LYS D 248  LYS D 251 -1  O  LEU D 250   N  TYR D 227           
SSBOND   1 CYS B    1    CYS B   46                          1555   1555  2.03  
SSBOND   2 CYS B   30    CYS B   60                          1555   1555  2.04  
SSBOND   3 CYS B   65    CYS B  107                          1555   1555  2.03  
SSBOND   4 CYS B   93    CYS B  123                          1555   1555  2.04  
SSBOND   5 CYS B  128    CYS B  176                          1555   1555  2.04  
SSBOND   6 CYS B  157    CYS B  189                          1555   1555  2.04  
SSBOND   7 CYS B  194    CYS B  236                          1555   1555  2.03  
SSBOND   8 CYS B  222    CYS B  249                          1555   1555  2.04  
SSBOND   9 CYS D    1    CYS D   46                          1555   1555  2.03  
SSBOND  10 CYS D   30    CYS D   60                          1555   1555  2.04  
SSBOND  11 CYS D   65    CYS D  107                          1555   1555  2.04  
SSBOND  12 CYS D   93    CYS D  123                          1555   1555  2.04  
SSBOND  13 CYS D  128    CYS D  176                          1555   1555  2.03  
SSBOND  14 CYS D  157    CYS D  189                          1555   1555  2.04  
SSBOND  15 CYS D  194    CYS D  236                          1555   1555  2.03  
SSBOND  16 CYS D  222    CYS D  249                          1555   1555  2.04  
LINK         ND2 ASN B  49                 C1  NAG E   1     1555   1555  1.45  
LINK         ND2 ASN B  80                 C1  NAG F   1     1555   1555  1.45  
LINK         ND2 ASN D  80                 C1  NAG G   1     1555   1555  1.45  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.44  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.44  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.44  
CISPEP   1 PRO B   38    PRO B   39          0         5.59                     
CISPEP   2 ASP B  243    PRO B  244          0         0.73                     
CISPEP   3 PRO D   38    PRO D   39          0         4.88                     
CISPEP   4 ASP D  243    PRO D  244          0         1.01                     
CRYST1  108.160  108.160  222.990  90.00  90.00 120.00 P 63         12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009246  0.005338  0.000000        0.00000                         
SCALE2      0.000000  0.010676  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004485        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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