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Database: PDB
Entry: 5J06
LinkDB: 5J06
Original site: 5J06 
HEADER    IMMUNE SYSTEM                           27-MAR-16   5J06              
TITLE     STRUCTURE OF THE IMMUNE RECEPTOR CD33 IN COMPLEX WITH 3'-SIALYLLACTOSE
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYELOID CELL SURFACE ANTIGEN CD33;                         
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 21-232;                                       
COMPND   5 SYNONYM: SIALIC ACID-BINDING IG-LIKE LECTIN 3,SIGLEC-3,GP67;         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CD33, SIGLEC3;                                                 
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK 293-F;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PHLSEC                                    
KEYWDS    IMMUNE RECEPTOR, SIGLEC, IG-LIKE, SIALIC-ACID BINDING, IMMUNE SYSTEM  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.B.DODD                                                              
REVDAT   3   29-JUL-20 5J06    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE   ATOM                              
REVDAT   2   02-OCT-19 5J06    1       REMARK                                   
REVDAT   1   05-APR-17 5J06    0                                                
JRNL        AUTH   R.B.DODD,W.MEADOWS,S.QAMAR,C.M.JOHNSON,                      
JRNL        AUTH 2 D.KRONENBERG-VERSTEEG,P.ST GEORGE-HYSLOP                     
JRNL        TITL   STRUCTURE OF LIGAND BOUND CD33 RECEPTOR ASSOCIATED WITH      
JRNL        TITL 2 ALZHEIMER'S DISEASE                                          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.66 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_2313: ???)                               
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) : 2.66                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 62.26                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 34627                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.930                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1707                            
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 62.2724 -  6.0882    0.99     2915   144  0.2014 0.2330        
REMARK   3     2  6.0882 -  4.8330    0.99     2769   164  0.1737 0.2096        
REMARK   3     3  4.8330 -  4.2222    0.99     2740   148  0.1476 0.1848        
REMARK   3     4  4.2222 -  3.8362    1.00     2723   155  0.1873 0.1971        
REMARK   3     5  3.8362 -  3.5613    1.00     2736   153  0.2164 0.2511        
REMARK   3     6  3.5613 -  3.3514    1.00     2751   125  0.2243 0.2778        
REMARK   3     7  3.3514 -  3.1835    1.00     2716   144  0.2415 0.2695        
REMARK   3     8  3.1835 -  3.0450    1.00     2734   133  0.2527 0.3339        
REMARK   3     9  3.0450 -  2.9277    1.00     2682   146  0.2831 0.3547        
REMARK   3    10  2.9277 -  2.8267    1.00     2715   141  0.2832 0.3376        
REMARK   3    11  2.8267 -  2.7383    1.00     2732   129  0.2917 0.3599        
REMARK   3    12  2.7383 -  2.6600    1.00     2707   125  0.3210 0.3517        
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)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.480           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 58.87                          
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      :  0.003           7128                                  
REMARK   3   ANGLE     :  0.603           9744                                  
REMARK   3   CHIRALITY :  0.046           1122                                  
REMARK   3   PLANARITY :  0.004           1246                                  
REMARK   3   DIHEDRAL  :  9.822           4213                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 20 THROUGH 78 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -16.1451  39.3524  16.8573              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2821 T22:   0.4109                                     
REMARK   3      T33:   0.3764 T12:   0.0161                                     
REMARK   3      T13:   0.0219 T23:  -0.0063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4613 L22:   2.0168                                     
REMARK   3      L33:   1.5185 L12:   0.3550                                     
REMARK   3      L13:   0.2102 L23:  -0.5456                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1520 S12:  -0.4522 S13:  -0.0268                       
REMARK   3      S21:   0.2857 S22:   0.0397 S23:   0.1002                       
REMARK   3      S31:  -0.2254 S32:  -0.4030 S33:  -0.0001                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 79 THROUGH 128 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -19.4402  37.0485  12.4614              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3013 T22:   0.4669                                     
REMARK   3      T33:   0.3819 T12:  -0.0201                                     
REMARK   3      T13:  -0.0059 T23:   0.0155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1237 L22:   1.5585                                     
REMARK   3      L33:   2.2928 L12:   0.3132                                     
REMARK   3      L13:  -1.3484 L23:  -0.0660                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1587 S12:  -0.2374 S13:  -0.1347                       
REMARK   3      S21:   0.0420 S22:  -0.0892 S23:   0.3059                       
REMARK   3      S31:   0.4837 S32:  -0.8883 S33:   0.0154                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 129 THROUGH 149 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1169  37.7632  -2.3487              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3371 T22:   0.3648                                     
REMARK   3      T33:   0.4368 T12:  -0.0034                                     
REMARK   3      T13:   0.0138 T23:   0.0558                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6931 L22:   0.7547                                     
REMARK   3      L33:   1.1396 L12:   0.1765                                     
REMARK   3      L13:  -0.3740 L23:   0.6971                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1369 S12:  -0.1395 S13:   0.3998                       
REMARK   3      S21:  -0.0686 S22:   0.1524 S23:  -0.1631                       
REMARK   3      S31:  -0.4709 S32:   0.2019 S33:  -0.0057                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 150 THROUGH 232 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1733  19.8931 -19.0564              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3036 T22:   0.3978                                     
REMARK   3      T33:   0.3292 T12:   0.0234                                     
REMARK   3      T13:  -0.0379 T23:  -0.0201                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2335 L22:   2.1914                                     
REMARK   3      L33:   0.7364 L12:   0.0492                                     
REMARK   3      L13:  -0.0612 L23:   0.5508                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0789 S12:   0.3824 S13:  -0.1974                       
REMARK   3      S21:  -0.0614 S22:  -0.0706 S23:  -0.0654                       
REMARK   3      S31:  -0.3610 S32:   0.0958 S33:   0.0066                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 56 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -12.3497  -3.5727   3.7356              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3718 T22:   0.1397                                     
REMARK   3      T33:   0.5018 T12:   0.0852                                     
REMARK   3      T13:  -0.0357 T23:  -0.0609                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8424 L22:   0.2627                                     
REMARK   3      L33:   0.2003 L12:  -0.4137                                     
REMARK   3      L13:   0.3121 L23:  -0.0793                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0879 S12:  -0.0894 S13:  -0.0320                       
REMARK   3      S21:  -0.1089 S22:   0.1198 S23:   0.3055                       
REMARK   3      S31:   0.0603 S32:  -0.1340 S33:   0.6466                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 57 THROUGH 92 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   1.9286  -5.0869   2.1200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4368 T22:   0.3477                                     
REMARK   3      T33:   0.5787 T12:   0.0539                                     
REMARK   3      T13:   0.0419 T23:   0.0588                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0949 L22:   2.2988                                     
REMARK   3      L33:   2.1198 L12:  -0.2235                                     
REMARK   3      L13:   2.5554 L23:  -0.0938                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0535 S12:   0.8755 S13:  -0.0060                       
REMARK   3      S21:  -0.2858 S22:  -0.3764 S23:  -0.7190                       
REMARK   3      S31:   0.2945 S32:   0.9112 S33:  -0.1882                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 93 THROUGH 149 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.5724  -9.0294  10.0874              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3241 T22:   0.2044                                     
REMARK   3      T33:   0.3592 T12:   0.0267                                     
REMARK   3      T13:  -0.0988 T23:  -0.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2566 L22:   1.4060                                     
REMARK   3      L33:   1.0154 L12:  -0.4866                                     
REMARK   3      L13:   0.2239 L23:  -0.2701                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0076 S12:  -0.2870 S13:   0.0847                       
REMARK   3      S21:   0.3133 S22:  -0.0562 S23:  -0.1525                       
REMARK   3      S31:  -0.3157 S32:  -0.0029 S33:  -0.0027                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 150 THROUGH 216 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.5251 -39.5547  21.9027              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3060 T22:   0.2664                                     
REMARK   3      T33:   0.2613 T12:   0.0286                                     
REMARK   3      T13:   0.0539 T23:   0.0872                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1774 L22:   2.2853                                     
REMARK   3      L33:   0.4614 L12:   0.5300                                     
REMARK   3      L13:  -0.1767 L23:   0.9365                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1079 S12:  -0.2655 S13:  -0.2073                       
REMARK   3      S21:  -0.0254 S22:   0.1499 S23:  -0.0231                       
REMARK   3      S31:   0.0765 S32:  -0.2456 S33:  -0.0012                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 217 THROUGH 232 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.5246 -33.7966  27.9582              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3332 T22:   0.5626                                     
REMARK   3      T33:   0.2846 T12:   0.0724                                     
REMARK   3      T13:   0.0681 T23:   0.0595                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5778 L22:   2.1351                                     
REMARK   3      L33:   4.3560 L12:   0.5565                                     
REMARK   3      L13:  -1.0558 L23:  -3.0085                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3310 S12:  -0.7115 S13:   0.1270                       
REMARK   3      S21:   0.6356 S22:  -0.5021 S23:  -0.2773                       
REMARK   3      S31:  -0.7381 S32:   0.3184 S33:  -0.6137                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 21 THROUGH 128 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -19.0535 -37.9673  14.7171              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3152 T22:   0.4984                                     
REMARK   3      T33:   0.3940 T12:  -0.0678                                     
REMARK   3      T13:   0.0311 T23:   0.0499                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3916 L22:   2.2596                                     
REMARK   3      L33:   2.1645 L12:   1.3170                                     
REMARK   3      L13:  -0.3429 L23:  -0.2811                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0831 S12:  -0.3179 S13:  -0.0206                       
REMARK   3      S21:  -0.0229 S22:   0.0047 S23:   0.4082                       
REMARK   3      S31:   0.1827 S32:  -0.6013 S33:  -0.0143                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 129 THROUGH 149 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4553 -26.0236   2.3829              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4887 T22:   0.4900                                     
REMARK   3      T33:   0.4747 T12:  -0.0218                                     
REMARK   3      T13:  -0.0469 T23:  -0.0162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7050 L22:   0.1998                                     
REMARK   3      L33:   1.2671 L12:   0.2433                                     
REMARK   3      L13:   0.5152 L23:  -0.1168                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0852 S12:  -0.4184 S13:   0.1189                       
REMARK   3      S21:   0.2247 S22:  -0.0771 S23:   0.1198                       
REMARK   3      S31:  -0.8398 S32:   0.7239 S33:  -0.0121                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 150 THROUGH 231 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.6472 -26.3978 -21.9216              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2983 T22:   0.3880                                     
REMARK   3      T33:   0.2487 T12:  -0.1190                                     
REMARK   3      T13:  -0.0459 T23:   0.0582                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7827 L22:   1.6980                                     
REMARK   3      L33:   1.8619 L12:  -0.3057                                     
REMARK   3      L13:   0.9480 L23:   1.3320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0200 S12:   0.5675 S13:   0.1527                       
REMARK   3      S21:   0.0304 S22:   0.0210 S23:  -0.1375                       
REMARK   3      S31:  -0.1508 S32:   0.6516 S33:  -0.0769                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 21 THROUGH 102 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -38.0478  10.4252  16.4224              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6488 T22:   0.4915                                     
REMARK   3      T33:   0.5623 T12:   0.1312                                     
REMARK   3      T13:   0.1929 T23:   0.1310                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8562 L22:   1.5329                                     
REMARK   3      L33:   1.3951 L12:   0.6602                                     
REMARK   3      L13:   0.2892 L23:   0.2719                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1104 S12:  -0.4095 S13:  -0.0053                       
REMARK   3      S21:   0.7211 S22:   0.1868 S23:   0.6026                       
REMARK   3      S31:   0.3641 S32:  -0.3010 S33:   0.0080                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 103 THROUGH 232 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.5925  14.7388  -9.9401              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2742 T22:   0.2505                                     
REMARK   3      T33:   0.3934 T12:   0.0399                                     
REMARK   3      T13:  -0.0456 T23:  -0.0284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7761 L22:   1.5432                                     
REMARK   3      L33:   1.5378 L12:  -0.4118                                     
REMARK   3      L13:  -0.5212 L23:  -0.3991                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0135 S12:   0.3752 S13:  -0.2970                       
REMARK   3      S21:   0.0914 S22:   0.0101 S23:   0.1578                       
REMARK   3      S31:  -0.0701 S32:  -0.1784 S33:   0.4578                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5J06 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000218873.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.920                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34631                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.660                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 62.255                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.09020                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.66                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.91900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.480                              
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 5IHB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2% PEG 20,000, 4% PEG MME 500, 100 MM    
REMARK 280  BICINE/TRIS BASE PH 8.5, 1XMORPHEUS AMINO ACIDS. CRYSTALS SOAKED    
REMARK 280  IN 20 MM 3'-SIALYLLACTOSE IN MOTHER LIQUOR FOR 10 DAYS., VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 295.15K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       32.52500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.41500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.53000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.41500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.52500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       63.53000            
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                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
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 APPLY THE FOLLOWING TO CHAINS: B, E                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -32.52500            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      -63.53000            
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    18                                                      
REMARK 465     THR A    19                                                      
REMARK 465     GLY A   233                                                      
REMARK 465     THR A   234                                                      
REMARK 465     LYS A   235                                                      
REMARK 465     HIS A   236                                                      
REMARK 465     HIS A   237                                                      
REMARK 465     HIS A   238                                                      
REMARK 465     HIS A   239                                                      
REMARK 465     HIS A   240                                                      
REMARK 465     HIS A   241                                                      
REMARK 465     GLY B   233                                                      
REMARK 465     THR B   234                                                      
REMARK 465     LYS B   235                                                      
REMARK 465     HIS B   236                                                      
REMARK 465     HIS B   237                                                      
REMARK 465     HIS B   238                                                      
REMARK 465     HIS B   239                                                      
REMARK 465     HIS B   240                                                      
REMARK 465     HIS B   241                                                      
REMARK 465     GLU C    18                                                      
REMARK 465     THR C    19                                                      
REMARK 465     GLY C    20                                                      
REMARK 465     THR C   232                                                      
REMARK 465     GLY C   233                                                      
REMARK 465     THR C   234                                                      
REMARK 465     LYS C   235                                                      
REMARK 465     HIS C   236                                                      
REMARK 465     HIS C   237                                                      
REMARK 465     HIS C   238                                                      
REMARK 465     HIS C   239                                                      
REMARK 465     HIS C   240                                                      
REMARK 465     HIS C   241                                                      
REMARK 465     GLU D    18                                                      
REMARK 465     THR D    19                                                      
REMARK 465     GLY D    20                                                      
REMARK 465     GLY D   233                                                      
REMARK 465     THR D   234                                                      
REMARK 465     LYS D   235                                                      
REMARK 465     HIS D   236                                                      
REMARK 465     HIS D   237                                                      
REMARK 465     HIS D   238                                                      
REMARK 465     HIS D   239                                                      
REMARK 465     HIS D   240                                                      
REMARK 465     HIS D   241                                                      
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  HH21  ARG B   110     OD1  ASP B   140              1.49            
REMARK 500   NH2  ARG C   110     OD1  ASP C   140              2.04            
REMARK 500   OE2  GLU D    85     NH2  ARG D    89              2.06            
REMARK 500   NH2  ARG B   110     OD1  ASP B   140              2.09            
REMARK 500   O3   GAL E     1     C1   SIA E     2              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  35     -165.64   -102.39                                   
REMARK 500    VAL A 221       70.95   -116.27                                   
REMARK 500    LEU B  35     -164.17   -103.88                                   
REMARK 500    LEU C  35     -164.25   -102.40                                   
REMARK 500    VAL C 221       68.90   -108.35                                   
REMARK 500    LEU D  35     -165.15   -103.92                                   
REMARK 500    LEU D  93      -71.88    -74.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5J06 A   21   232  UNP    P20138   CD33_HUMAN      21    232             
DBREF  5J06 B   21   232  UNP    P20138   CD33_HUMAN      21    232             
DBREF  5J06 C   21   232  UNP    P20138   CD33_HUMAN      21    232             
DBREF  5J06 D   21   232  UNP    P20138   CD33_HUMAN      21    232             
SEQADV 5J06 GLU A   18  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 THR A   19  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 GLY A   20  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 GLY A   69  UNP  P20138    ARG    69 VARIANT                        
SEQADV 5J06 GLY A  233  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 THR A  234  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 LYS A  235  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS A  236  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS A  237  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS A  238  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS A  239  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS A  240  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS A  241  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 GLU B   18  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 THR B   19  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 GLY B   20  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 GLY B   69  UNP  P20138    ARG    69 VARIANT                        
SEQADV 5J06 GLY B  233  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 THR B  234  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 LYS B  235  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS B  236  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS B  237  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS B  238  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS B  239  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS B  240  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS B  241  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 GLU C   18  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 THR C   19  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 GLY C   20  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 GLY C   69  UNP  P20138    ARG    69 VARIANT                        
SEQADV 5J06 GLY C  233  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 THR C  234  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 LYS C  235  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS C  236  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS C  237  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS C  238  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS C  239  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS C  240  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS C  241  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 GLU D   18  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 THR D   19  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 GLY D   20  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 GLY D   69  UNP  P20138    ARG    69 VARIANT                        
SEQADV 5J06 GLY D  233  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 THR D  234  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 LYS D  235  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS D  236  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS D  237  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS D  238  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS D  239  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS D  240  UNP  P20138              EXPRESSION TAG                 
SEQADV 5J06 HIS D  241  UNP  P20138              EXPRESSION TAG                 
SEQRES   1 A  224  GLU THR GLY PHE TRP LEU GLN VAL GLN GLU SER VAL THR          
SEQRES   2 A  224  VAL GLN GLU GLY LEU CYS VAL LEU VAL PRO CYS THR PHE          
SEQRES   3 A  224  PHE HIS PRO ILE PRO TYR TYR ASP LYS ASN SER PRO VAL          
SEQRES   4 A  224  HIS GLY TYR TRP PHE ARG GLU GLY ALA ILE ILE SER GLY          
SEQRES   5 A  224  ASP SER PRO VAL ALA THR ASN LYS LEU ASP GLN GLU VAL          
SEQRES   6 A  224  GLN GLU GLU THR GLN GLY ARG PHE ARG LEU LEU GLY ASP          
SEQRES   7 A  224  PRO SER ARG ASN ASN CYS SER LEU SER ILE VAL ASP ALA          
SEQRES   8 A  224  ARG ARG ARG ASP ASN GLY SER TYR PHE PHE ARG MET GLU          
SEQRES   9 A  224  ARG GLY SER THR LYS TYR SER TYR LYS SER PRO GLN LEU          
SEQRES  10 A  224  SER VAL HIS VAL THR ASP LEU THR HIS ARG PRO LYS ILE          
SEQRES  11 A  224  LEU ILE PRO GLY THR LEU GLU PRO GLY HIS SER LYS ASN          
SEQRES  12 A  224  LEU THR CYS SER VAL SER TRP ALA CYS GLU GLN GLY THR          
SEQRES  13 A  224  PRO PRO ILE PHE SER TRP LEU SER ALA ALA PRO THR SER          
SEQRES  14 A  224  LEU GLY PRO ARG THR THR HIS SER SER VAL LEU ILE ILE          
SEQRES  15 A  224  THR PRO ARG PRO GLN ASP HIS GLY THR ASN LEU THR CYS          
SEQRES  16 A  224  GLN VAL LYS PHE ALA GLY ALA GLY VAL THR THR GLU ARG          
SEQRES  17 A  224  THR ILE GLN LEU ASN VAL THR GLY THR LYS HIS HIS HIS          
SEQRES  18 A  224  HIS HIS HIS                                                  
SEQRES   1 B  224  GLU THR GLY PHE TRP LEU GLN VAL GLN GLU SER VAL THR          
SEQRES   2 B  224  VAL GLN GLU GLY LEU CYS VAL LEU VAL PRO CYS THR PHE          
SEQRES   3 B  224  PHE HIS PRO ILE PRO TYR TYR ASP LYS ASN SER PRO VAL          
SEQRES   4 B  224  HIS GLY TYR TRP PHE ARG GLU GLY ALA ILE ILE SER GLY          
SEQRES   5 B  224  ASP SER PRO VAL ALA THR ASN LYS LEU ASP GLN GLU VAL          
SEQRES   6 B  224  GLN GLU GLU THR GLN GLY ARG PHE ARG LEU LEU GLY ASP          
SEQRES   7 B  224  PRO SER ARG ASN ASN CYS SER LEU SER ILE VAL ASP ALA          
SEQRES   8 B  224  ARG ARG ARG ASP ASN GLY SER TYR PHE PHE ARG MET GLU          
SEQRES   9 B  224  ARG GLY SER THR LYS TYR SER TYR LYS SER PRO GLN LEU          
SEQRES  10 B  224  SER VAL HIS VAL THR ASP LEU THR HIS ARG PRO LYS ILE          
SEQRES  11 B  224  LEU ILE PRO GLY THR LEU GLU PRO GLY HIS SER LYS ASN          
SEQRES  12 B  224  LEU THR CYS SER VAL SER TRP ALA CYS GLU GLN GLY THR          
SEQRES  13 B  224  PRO PRO ILE PHE SER TRP LEU SER ALA ALA PRO THR SER          
SEQRES  14 B  224  LEU GLY PRO ARG THR THR HIS SER SER VAL LEU ILE ILE          
SEQRES  15 B  224  THR PRO ARG PRO GLN ASP HIS GLY THR ASN LEU THR CYS          
SEQRES  16 B  224  GLN VAL LYS PHE ALA GLY ALA GLY VAL THR THR GLU ARG          
SEQRES  17 B  224  THR ILE GLN LEU ASN VAL THR GLY THR LYS HIS HIS HIS          
SEQRES  18 B  224  HIS HIS HIS                                                  
SEQRES   1 C  224  GLU THR GLY PHE TRP LEU GLN VAL GLN GLU SER VAL THR          
SEQRES   2 C  224  VAL GLN GLU GLY LEU CYS VAL LEU VAL PRO CYS THR PHE          
SEQRES   3 C  224  PHE HIS PRO ILE PRO TYR TYR ASP LYS ASN SER PRO VAL          
SEQRES   4 C  224  HIS GLY TYR TRP PHE ARG GLU GLY ALA ILE ILE SER GLY          
SEQRES   5 C  224  ASP SER PRO VAL ALA THR ASN LYS LEU ASP GLN GLU VAL          
SEQRES   6 C  224  GLN GLU GLU THR GLN GLY ARG PHE ARG LEU LEU GLY ASP          
SEQRES   7 C  224  PRO SER ARG ASN ASN CYS SER LEU SER ILE VAL ASP ALA          
SEQRES   8 C  224  ARG ARG ARG ASP ASN GLY SER TYR PHE PHE ARG MET GLU          
SEQRES   9 C  224  ARG GLY SER THR LYS TYR SER TYR LYS SER PRO GLN LEU          
SEQRES  10 C  224  SER VAL HIS VAL THR ASP LEU THR HIS ARG PRO LYS ILE          
SEQRES  11 C  224  LEU ILE PRO GLY THR LEU GLU PRO GLY HIS SER LYS ASN          
SEQRES  12 C  224  LEU THR CYS SER VAL SER TRP ALA CYS GLU GLN GLY THR          
SEQRES  13 C  224  PRO PRO ILE PHE SER TRP LEU SER ALA ALA PRO THR SER          
SEQRES  14 C  224  LEU GLY PRO ARG THR THR HIS SER SER VAL LEU ILE ILE          
SEQRES  15 C  224  THR PRO ARG PRO GLN ASP HIS GLY THR ASN LEU THR CYS          
SEQRES  16 C  224  GLN VAL LYS PHE ALA GLY ALA GLY VAL THR THR GLU ARG          
SEQRES  17 C  224  THR ILE GLN LEU ASN VAL THR GLY THR LYS HIS HIS HIS          
SEQRES  18 C  224  HIS HIS HIS                                                  
SEQRES   1 D  224  GLU THR GLY PHE TRP LEU GLN VAL GLN GLU SER VAL THR          
SEQRES   2 D  224  VAL GLN GLU GLY LEU CYS VAL LEU VAL PRO CYS THR PHE          
SEQRES   3 D  224  PHE HIS PRO ILE PRO TYR TYR ASP LYS ASN SER PRO VAL          
SEQRES   4 D  224  HIS GLY TYR TRP PHE ARG GLU GLY ALA ILE ILE SER GLY          
SEQRES   5 D  224  ASP SER PRO VAL ALA THR ASN LYS LEU ASP GLN GLU VAL          
SEQRES   6 D  224  GLN GLU GLU THR GLN GLY ARG PHE ARG LEU LEU GLY ASP          
SEQRES   7 D  224  PRO SER ARG ASN ASN CYS SER LEU SER ILE VAL ASP ALA          
SEQRES   8 D  224  ARG ARG ARG ASP ASN GLY SER TYR PHE PHE ARG MET GLU          
SEQRES   9 D  224  ARG GLY SER THR LYS TYR SER TYR LYS SER PRO GLN LEU          
SEQRES  10 D  224  SER VAL HIS VAL THR ASP LEU THR HIS ARG PRO LYS ILE          
SEQRES  11 D  224  LEU ILE PRO GLY THR LEU GLU PRO GLY HIS SER LYS ASN          
SEQRES  12 D  224  LEU THR CYS SER VAL SER TRP ALA CYS GLU GLN GLY THR          
SEQRES  13 D  224  PRO PRO ILE PHE SER TRP LEU SER ALA ALA PRO THR SER          
SEQRES  14 D  224  LEU GLY PRO ARG THR THR HIS SER SER VAL LEU ILE ILE          
SEQRES  15 D  224  THR PRO ARG PRO GLN ASP HIS GLY THR ASN LEU THR CYS          
SEQRES  16 D  224  GLN VAL LYS PHE ALA GLY ALA GLY VAL THR THR GLU ARG          
SEQRES  17 D  224  THR ILE GLN LEU ASN VAL THR GLY THR LYS HIS HIS HIS          
SEQRES  18 D  224  HIS HIS HIS                                                  
HET    GAL  E   1      23                                                       
HET    SIA  E   2      37                                                       
HET    NAG  A 301      28                                                       
HET    NAG  A 302      27                                                       
HET    NAG  A 303      28                                                       
HET    NAG  B 301      28                                                       
HET    NAG  B 302      28                                                       
HET    NAG  B 303      27                                                       
HET    NAG  B 304      28                                                       
HET    PG0  B 307      20                                                       
HET    NAG  C 301      28                                                       
HET    NAG  C 302      27                                                       
HET    NAG  C 303      27                                                       
HET    PG0  C 304      20                                                       
HET    NAG  D 301      28                                                       
HET    NAG  D 302      27                                                       
HET    NAG  D 303      27                                                       
HET    SIA  D 304      39                                                       
HETNAM     GAL BETA-D-GALACTOPYRANOSE                                           
HETNAM     SIA N-ACETYL-ALPHA-NEURAMINIC ACID                                   
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     PG0 2-(2-METHOXYETHOXY)ETHANOL                                       
HETSYN     PG0 PEG 6000                                                         
FORMUL   5  GAL    C6 H12 O6                                                    
FORMUL   5  SIA    2(C11 H19 N O9)                                              
FORMUL   6  NAG    13(C8 H15 N O6)                                              
FORMUL  13  PG0    2(C5 H12 O3)                                                 
FORMUL  22  HOH   *36(H2 O)                                                     
HELIX    1 AA1 PRO A   48  LYS A   52  5                                   5    
HELIX    2 AA2 GLY A   64  GLY A   69  1                                   6    
HELIX    3 AA3 ASP A   95  ASN A   99  5                                   5    
HELIX    4 AA4 ARG A  109  ASN A  113  5                                   5    
HELIX    5 AA5 ARG A  202  HIS A  206  5                                   5    
HELIX    6 AA6 PRO B   48  LYS B   52  5                                   5    
HELIX    7 AA7 ASP B   95  ASN B   99  5                                   5    
HELIX    8 AA8 ARG B  109  ASN B  113  5                                   5    
HELIX    9 AA9 ARG B  202  HIS B  206  5                                   5    
HELIX   10 AB1 PRO C   48  LYS C   52  5                                   5    
HELIX   11 AB2 GLY C   64  GLY C   69  1                                   6    
HELIX   12 AB3 ASP C   95  ASN C   99  5                                   5    
HELIX   13 AB4 ARG C  109  ASN C  113  5                                   5    
HELIX   14 AB5 ARG C  202  HIS C  206  5                                   5    
HELIX   15 AB6 PRO D   48  LYS D   52  5                                   5    
HELIX   16 AB7 ASP D   95  ASN D   99  5                                   5    
HELIX   17 AB8 ARG D  109  ASN D  113  5                                   5    
HELIX   18 AB9 ARG D  202  HIS D  206  5                                   5    
SHEET    1 AA1 2 TRP A  22  VAL A  25  0                                        
SHEET    2 AA1 2 CYS A  41  PHE A  44 -1  O  THR A  42   N  GLN A  24           
SHEET    1 AA2 5 SER A  28  GLN A  32  0                                        
SHEET    2 AA2 5 LEU A 134  THR A 139  1  O  HIS A 137   N  VAL A  29           
SHEET    3 AA2 5 GLY A 114  ARG A 122 -1  N  GLY A 114   O  VAL A 136           
SHEET    4 AA2 5 VAL A  56  ARG A  62 -1  N  HIS A  57   O  GLU A 121           
SHEET    5 AA2 5 ALA A  74  THR A  75 -1  O  ALA A  74   N  TRP A  60           
SHEET    1 AA3 4 SER A  28  GLN A  32  0                                        
SHEET    2 AA3 4 LEU A 134  THR A 139  1  O  HIS A 137   N  VAL A  29           
SHEET    3 AA3 4 GLY A 114  ARG A 122 -1  N  GLY A 114   O  VAL A 136           
SHEET    4 AA3 4 THR A 125  SER A 128 -1  O  THR A 125   N  ARG A 122           
SHEET    1 AA4 3 VAL A  37  VAL A  39  0                                        
SHEET    2 AA4 3 LEU A 103  ILE A 105 -1  O  LEU A 103   N  VAL A  39           
SHEET    3 AA4 3 PHE A  90  LEU A  92 -1  N  ARG A  91   O  SER A 104           
SHEET    1 AA5 4 LYS A 146  LEU A 148  0                                        
SHEET    2 AA5 4 LYS A 159  SER A 164 -1  O  THR A 162   N  LEU A 148           
SHEET    3 AA5 4 SER A 194  ILE A 199 -1  O  LEU A 197   N  LEU A 161           
SHEET    4 AA5 4 THR A 185  THR A 191 -1  N  GLY A 188   O  VAL A 196           
SHEET    1 AA6 6 THR A 222  GLN A 228  0                                        
SHEET    2 AA6 6 ASN A 209  LYS A 215 -1  N  VAL A 214   O  THR A 223           
SHEET    3 AA6 6 ILE A 176  SER A 181 -1  N  SER A 178   O  GLN A 213           
SHEET    4 AA6 6 ILE D 176  SER D 181  1  O  TRP D 179   N  PHE A 177           
SHEET    5 AA6 6 ASN D 209  LYS D 215 -1  O  GLN D 213   N  SER D 178           
SHEET    6 AA6 6 THR D 222  GLN D 228 -1  O  THR D 223   N  VAL D 214           
SHEET    1 AA7 2 TRP B  22  VAL B  25  0                                        
SHEET    2 AA7 2 CYS B  41  PHE B  44 -1  O  THR B  42   N  GLN B  24           
SHEET    1 AA8 5 SER B  28  GLN B  32  0                                        
SHEET    2 AA8 5 THR B 125  THR B 139  1  O  HIS B 137   N  VAL B  29           
SHEET    3 AA8 5 GLY B 114  ARG B 122 -1  N  ARG B 122   O  THR B 125           
SHEET    4 AA8 5 VAL B  56  ARG B  62 -1  N  PHE B  61   O  PHE B 117           
SHEET    5 AA8 5 ALA B  74  THR B  75 -1  O  ALA B  74   N  TRP B  60           
SHEET    1 AA9 3 VAL B  37  VAL B  39  0                                        
SHEET    2 AA9 3 LEU B 103  ILE B 105 -1  O  LEU B 103   N  VAL B  39           
SHEET    3 AA9 3 PHE B  90  LEU B  92 -1  N  ARG B  91   O  SER B 104           
SHEET    1 AB1 4 LYS B 146  LEU B 148  0                                        
SHEET    2 AB1 4 LYS B 159  SER B 164 -1  O  THR B 162   N  LEU B 148           
SHEET    3 AB1 4 SER B 194  ILE B 199 -1  O  SER B 195   N  CYS B 163           
SHEET    4 AB1 4 THR B 185  ARG B 190 -1  N  SER B 186   O  ILE B 198           
SHEET    1 AB2 3 ILE B 176  SER B 181  0                                        
SHEET    2 AB2 3 ASN B 209  LYS B 215 -1  O  GLN B 213   N  SER B 178           
SHEET    3 AB2 3 THR B 222  GLN B 228 -1  O  THR B 223   N  VAL B 214           
SHEET    1 AB3 2 TRP C  22  VAL C  25  0                                        
SHEET    2 AB3 2 CYS C  41  PHE C  44 -1  O  THR C  42   N  GLN C  24           
SHEET    1 AB4 5 SER C  28  GLN C  32  0                                        
SHEET    2 AB4 5 LEU C 134  THR C 139  1  O  HIS C 137   N  VAL C  29           
SHEET    3 AB4 5 GLY C 114  ARG C 122 -1  N  GLY C 114   O  VAL C 136           
SHEET    4 AB4 5 VAL C  56  ARG C  62 -1  N  PHE C  61   O  PHE C 117           
SHEET    5 AB4 5 ALA C  74  THR C  75 -1  O  ALA C  74   N  TRP C  60           
SHEET    1 AB5 4 SER C  28  GLN C  32  0                                        
SHEET    2 AB5 4 LEU C 134  THR C 139  1  O  HIS C 137   N  VAL C  29           
SHEET    3 AB5 4 GLY C 114  ARG C 122 -1  N  GLY C 114   O  VAL C 136           
SHEET    4 AB5 4 THR C 125  SER C 128 -1  O  THR C 125   N  ARG C 122           
SHEET    1 AB6 3 VAL C  37  VAL C  39  0                                        
SHEET    2 AB6 3 LEU C 103  ILE C 105 -1  O  LEU C 103   N  VAL C  39           
SHEET    3 AB6 3 PHE C  90  LEU C  92 -1  N  ARG C  91   O  SER C 104           
SHEET    1 AB7 4 LYS C 146  LEU C 148  0                                        
SHEET    2 AB7 4 LYS C 159  SER C 164 -1  O  THR C 162   N  LEU C 148           
SHEET    3 AB7 4 SER C 194  ILE C 199 -1  O  LEU C 197   N  LEU C 161           
SHEET    4 AB7 4 THR C 185  THR C 191 -1  N  GLY C 188   O  VAL C 196           
SHEET    1 AB8 3 ILE C 176  SER C 181  0                                        
SHEET    2 AB8 3 ASN C 209  LYS C 215 -1  O  GLN C 213   N  SER C 178           
SHEET    3 AB8 3 THR C 222  GLN C 228 -1  O  THR C 223   N  VAL C 214           
SHEET    1 AB9 2 TRP D  22  GLN D  24  0                                        
SHEET    2 AB9 2 THR D  42  PHE D  44 -1  O  THR D  42   N  GLN D  24           
SHEET    1 AC1 5 SER D  28  GLN D  32  0                                        
SHEET    2 AC1 5 THR D 125  THR D 139  1  O  HIS D 137   N  VAL D  29           
SHEET    3 AC1 5 GLY D 114  ARG D 122 -1  N  ARG D 122   O  THR D 125           
SHEET    4 AC1 5 VAL D  56  ARG D  62 -1  N  TYR D  59   O  ARG D 119           
SHEET    5 AC1 5 ALA D  74  THR D  75 -1  O  ALA D  74   N  TRP D  60           
SHEET    1 AC2 3 VAL D  37  VAL D  39  0                                        
SHEET    2 AC2 3 LEU D 103  ILE D 105 -1  O  LEU D 103   N  VAL D  39           
SHEET    3 AC2 3 PHE D  90  LEU D  92 -1  N  ARG D  91   O  SER D 104           
SHEET    1 AC3 4 LYS D 146  LEU D 148  0                                        
SHEET    2 AC3 4 LYS D 159  SER D 164 -1  O  THR D 162   N  LEU D 148           
SHEET    3 AC3 4 SER D 194  ILE D 199 -1  O  LEU D 197   N  LEU D 161           
SHEET    4 AC3 4 THR D 185  ARG D 190 -1  N  SER D 186   O  ILE D 198           
SSBOND   1 CYS A   36    CYS A  169                          1555   1555  2.04  
SSBOND   2 CYS A   41    CYS A  101                          1555   1555  2.04  
SSBOND   3 CYS A  163    CYS A  212                          1555   1555  2.03  
SSBOND   4 CYS B   36    CYS B  169                          1555   1555  2.04  
SSBOND   5 CYS B   41    CYS B  101                          1555   1555  2.04  
SSBOND   6 CYS B  163    CYS B  212                          1555   1555  2.03  
SSBOND   7 CYS C   36    CYS C  169                          1555   1555  2.04  
SSBOND   8 CYS C   41    CYS C  101                          1555   1555  2.03  
SSBOND   9 CYS C  163    CYS C  212                          1555   1555  2.03  
SSBOND  10 CYS D   36    CYS D  169                          1555   1555  2.04  
SSBOND  11 CYS D   41    CYS D  101                          1555   1555  2.04  
SSBOND  12 CYS D  163    CYS D  212                          1555   1555  2.03  
LINK         ND2 ASN A 100                 C1  NAG A 301     1555   1555  1.44  
LINK         ND2 ASN A 160                 C1  NAG A 302     1555   1555  1.43  
LINK         ND2 ASN A 209                 C1  NAG A 303     1555   1555  1.44  
LINK         ND2 ASN B 100                 C1  NAG B 301     1555   1555  1.43  
LINK         ND2 ASN B 160                 C1  NAG B 302     1555   1555  1.44  
LINK         ND2 ASN B 209                 C1  NAG B 303     1555   1555  1.44  
LINK         ND2 ASN B 230                 C1  NAG B 304     1555   1555  1.43  
LINK         ND2 ASN C 100                 C1  NAG C 301     1555   1555  1.44  
LINK         ND2 ASN C 160                 C1  NAG C 302     1555   1555  1.44  
LINK         ND2 ASN C 209                 C1  NAG C 303     1555   1555  1.44  
LINK         ND2 ASN D 100                 C1  NAG D 301     1555   1555  1.44  
LINK         ND2 ASN D 160                 C1  NAG D 302     1555   1555  1.44  
LINK         ND2 ASN D 209                 C1  NAG D 303     1555   1555  1.43  
LINK         O3  GAL E   1                 C2  SIA E   2     1555   1555  1.38  
CISPEP   1 SER A  131    PRO A  132          0        -2.64                     
CISPEP   2 SER B  131    PRO B  132          0        -2.12                     
CISPEP   3 SER C  131    PRO C  132          0        -0.95                     
CISPEP   4 SER D  131    PRO D  132          0        -2.83                     
CRYST1   65.050  127.060  142.830  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015373  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007870  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007001        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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