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Database: PDB
Entry: 4JZJ
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HEADER    CYTOKINE RECEPTOR/IMMUNE SYSTEM         03-APR-13   4JZJ              
TITLE     CRYSTAL STRUCTURE OF RECEPTOR-FAB COMPLEX                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-3 RECEPTOR SUBUNIT ALPHA;                      
COMPND   3 CHAIN: C, D;                                                         
COMPND   4 FRAGMENT: DOMAIN 2, DOMAIN 3, UNP RESIDUES 20-307;                   
COMPND   5 SYNONYM: IL-3 RECEPTOR SUBUNIT ALPHA, IL-3R SUBUNIT ALPHA, IL-3R-    
COMPND   6 ALPHA, IL-3RA;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: FAB HEAVY CHAIN;                                           
COMPND  11 CHAIN: A, H;                                                         
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: FAB LIGHT CHAIN;                                           
COMPND  14 CHAIN: B, L                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: IL3RA;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1;                                
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  14 ORGANISM_COMMON: MOUSE;                                              
SOURCE  15 ORGANISM_TAXID: 10090;                                               
SOURCE  16 OTHER_DETAILS: THE FAB FRAGMENT WAS PREPARED BY PAPAIN DIGESTION OF  
SOURCE  17 MAB AND PROTEIN A REMOVAL OF UNDIGESTED IMMUNOGLOBULIN AND FC        
SOURCE  18 FRAGMENT.;                                                           
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  21 ORGANISM_COMMON: MOUSE;                                              
SOURCE  22 ORGANISM_TAXID: 10090;                                               
SOURCE  23 OTHER_DETAILS: THE FAB FRAGMENT WAS PREPARED BY PAPAIN DIGESTION OF  
SOURCE  24 MAB AND PROTEIN A REMOVAL OF UNDIGESTED IMMUNOGLOBULIN AND FC        
SOURCE  25 FRAGMENT.                                                            
KEYWDS    RECEPTOR-FAB COMPLEX, CYTOKINE RECEPTOR-IMMUNE SYSTEM COMPLEX         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.E.BROUGHTON,M.W.PARKER                                              
REVDAT   3   15-NOV-17 4JZJ    1       REMARK                                   
REVDAT   2   16-MAR-16 4JZJ    1       JRNL                                     
REVDAT   1   09-APR-14 4JZJ    0                                                
JRNL        AUTH   S.E.BROUGHTON,T.R.HERCUS,M.P.HARDY,B.J.MCCLURE,T.L.NERO,     
JRNL        AUTH 2 M.DOTTORE,H.HUYNH,H.BRALEY,E.F.BARRY,W.L.KAN,U.DHAGAT,       
JRNL        AUTH 3 P.SCOTNEY,D.HARTMAN,S.J.BUSFIELD,C.M.OWCZAREK,A.D.NASH,      
JRNL        AUTH 4 N.J.WILSON,M.W.PARKER,A.F.LOPEZ                              
JRNL        TITL   DUAL MECHANISM OF INTERLEUKIN-3 RECEPTOR BLOCKADE BY AN      
JRNL        TITL 2 ANTI-CANCER ANTIBODY                                         
JRNL        REF    CELL REP                      V.   8   410 2014              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   25043189                                                     
JRNL        DOI    10.1016/J.CELREP.2014.06.038                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_1218                                      
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.68                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 47185                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2379                            
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 49.6826 -  7.1958    0.97     2638   136  0.1816 0.2219        
REMARK   3     2  7.1958 -  5.7142    0.99     2677   127  0.1876 0.2537        
REMARK   3     3  5.7142 -  4.9927    0.99     2656   130  0.1502 0.1832        
REMARK   3     4  4.9927 -  4.5365    0.99     2639   135  0.1322 0.1908        
REMARK   3     5  4.5365 -  4.2115    0.99     2620   132  0.1420 0.1908        
REMARK   3     6  4.2115 -  3.9633    0.99     2653   148  0.1677 0.2098        
REMARK   3     7  3.9633 -  3.7649    1.00     2648   139  0.1808 0.2490        
REMARK   3     8  3.7649 -  3.6011    0.99     2626   148  0.1882 0.2539        
REMARK   3     9  3.6011 -  3.4625    1.00     2626   154  0.1988 0.2788        
REMARK   3    10  3.4625 -  3.3430    1.00     2656   133  0.2147 0.3054        
REMARK   3    11  3.3430 -  3.2385    1.00     2630   138  0.2292 0.3042        
REMARK   3    12  3.2385 -  3.1460    1.00     2656   126  0.2410 0.2849        
REMARK   3    13  3.1460 -  3.0632    1.00     2633   157  0.2548 0.3452        
REMARK   3    14  3.0632 -  2.9884    1.00     2613   150  0.2513 0.3884        
REMARK   3    15  2.9884 -  2.9205    1.00     2622   152  0.2593 0.3292        
REMARK   3    16  2.9205 -  2.8584    1.00     2664   146  0.2767 0.3479        
REMARK   3    17  2.8584 -  2.8012    0.96     2549   128  0.2934 0.3677        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.300           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 50.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.31                          
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      :  0.011          11222                                  
REMARK   3   ANGLE     :  1.456          15220                                  
REMARK   3   CHIRALITY :  0.087           1685                                  
REMARK   3   PLANARITY :  0.006           1915                                  
REMARK   3   DIHEDRAL  : 17.060           4161                                  
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 1:133)                              
REMARK   3    ORIGIN FOR THE GROUP (A):   5.5246  30.6333 -32.4702              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2608 T22:   0.7175                                     
REMARK   3      T33:   0.5916 T12:   0.0697                                     
REMARK   3      T13:   0.1705 T23:  -0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4690 L22:   1.5669                                     
REMARK   3      L33:   2.8911 L12:   0.9441                                     
REMARK   3      L13:   1.6416 L23:   1.4446                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1651 S12:   0.9791 S13:   0.1014                       
REMARK   3      S21:  -0.0649 S22:   0.0632 S23:  -0.4089                       
REMARK   3      S31:   0.0314 S32:   0.8011 S33:  -0.0150                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 141:221)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  11.8675  39.0804  -1.5771              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2825 T22:   0.3287                                     
REMARK   3      T33:   0.7578 T12:   0.0721                                     
REMARK   3      T13:  -0.0731 T23:  -0.1009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3481 L22:   3.1708                                     
REMARK   3      L33:   7.2325 L12:   0.9083                                     
REMARK   3      L13:   0.7937 L23:  -2.9362                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0053 S12:  -0.1746 S13:   0.6345                       
REMARK   3      S21:   0.1660 S22:  -0.1589 S23:  -0.4496                       
REMARK   3      S31:  -0.0827 S32:   0.8150 S33:   0.1869                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 1:112)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.0775  12.6118 -23.8501              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3535 T22:   0.2358                                     
REMARK   3      T33:   0.5867 T12:   0.1376                                     
REMARK   3      T13:   0.0185 T23:  -0.1432                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9531 L22:   1.3977                                     
REMARK   3      L33:   2.4872 L12:   0.5288                                     
REMARK   3      L13:   0.0913 L23:  -0.1288                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1973 S12:   0.3790 S13:  -0.7050                       
REMARK   3      S21:  -0.1833 S22:   0.1417 S23:  -0.4821                       
REMARK   3      S31:   0.5379 S32:   0.3438 S33:  -0.0987                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 113:219)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.4019  36.8695   4.9507              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3505 T22:   0.6834                                     
REMARK   3      T33:   0.5820 T12:   0.2551                                     
REMARK   3      T13:  -0.0075 T23:  -0.1002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4069 L22:   6.1522                                     
REMARK   3      L33:   2.0814 L12:   0.5069                                     
REMARK   3      L13:   0.1316 L23:  -0.8950                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0414 S12:  -0.7213 S13:   0.5829                       
REMARK   3      S21:   0.5873 S22:   0.0480 S23:   0.7176                       
REMARK   3      S31:  -0.3466 S32:  -0.6062 S33:  -0.0696                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN C AND RESID 25:97)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  65.3050  11.5029  -9.6055              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2427 T22:   0.2201                                     
REMARK   3      T33:   0.2867 T12:  -0.0504                                     
REMARK   3      T13:  -0.0098 T23:   0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6926 L22:   2.7785                                     
REMARK   3      L33:   8.6301 L12:   0.6138                                     
REMARK   3      L13:  -0.7021 L23:   0.2155                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1414 S12:  -0.1179 S13:  -0.4868                       
REMARK   3      S21:  -0.0494 S22:  -0.0607 S23:  -0.0046                       
REMARK   3      S31:   0.5068 S32:  -0.1899 S33:  -0.0577                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN C AND RESID 98:211)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  67.0413  36.3649 -27.3895              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2966 T22:   0.2763                                     
REMARK   3      T33:   0.1910 T12:   0.0677                                     
REMARK   3      T13:   0.0133 T23:  -0.0592                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6380 L22:   3.0675                                     
REMARK   3      L33:   3.0713 L12:   0.6397                                     
REMARK   3      L13:   1.7517 L23:   1.2809                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3265 S12:  -0.2574 S13:   0.1987                       
REMARK   3      S21:  -0.1212 S22:   0.2013 S23:  -0.1274                       
REMARK   3      S31:  -0.0778 S32:  -0.0794 S33:   0.1423                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN C AND RESID 212:289)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  43.2888  49.5700 -44.6499              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8840 T22:   0.6205                                     
REMARK   3      T33:   0.9551 T12:   0.1425                                     
REMARK   3      T13:  -0.3375 T23:   0.0444                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7823 L22:   3.5467                                     
REMARK   3      L33:   4.6687 L12:  -2.2496                                     
REMARK   3      L13:   2.6201 L23:  -3.4470                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3725 S12:  -0.4011 S13:   0.5221                       
REMARK   3      S21:  -0.3386 S22:   0.5211 S23:   1.0869                       
REMARK   3      S31:  -0.7591 S32:  -0.6815 S33:   0.0147                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN D AND RESID 25:100)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.5676  16.6503 -52.5413              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7530 T22:   0.8705                                     
REMARK   3      T33:   0.4031 T12:   0.1252                                     
REMARK   3      T13:   0.1030 T23:  -0.2072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2608 L22:   3.6483                                     
REMARK   3      L33:   1.9654 L12:   1.0993                                     
REMARK   3      L13:  -0.9565 L23:   1.7050                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1159 S12:   1.1630 S13:  -0.8068                       
REMARK   3      S21:  -0.5515 S22:  -0.0152 S23:  -0.2107                       
REMARK   3      S31:   0.7572 S32:   0.8625 S33:   0.0379                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN D AND RESID 101:205)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -36.0522  26.4687 -53.9123              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6672 T22:   0.2713                                     
REMARK   3      T33:   0.3129 T12:  -0.0911                                     
REMARK   3      T13:  -0.1023 T23:  -0.0495                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2791 L22:   0.9007                                     
REMARK   3      L33:   8.0451 L12:   0.2069                                     
REMARK   3      L13:   0.8330 L23:  -0.1412                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1915 S12:   0.2804 S13:  -0.1239                       
REMARK   3      S21:  -0.3282 S22:   0.1778 S23:   0.0820                       
REMARK   3      S31:  -0.0488 S32:  -0.2339 S33:   0.0926                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 206:290)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -44.5616  24.6844 -22.9009              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5053 T22:   0.9008                                     
REMARK   3      T33:   0.4025 T12:  -0.0238                                     
REMARK   3      T13:   0.0494 T23:   0.0653                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4905 L22:   4.6936                                     
REMARK   3      L33:   3.7949 L12:   1.1943                                     
REMARK   3      L13:  -2.9784 L23:  -0.2273                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0189 S12:  -0.6745 S13:   0.1345                       
REMARK   3      S21:   0.7024 S22:   0.1541 S23:   0.7249                       
REMARK   3      S31:   0.5211 S32:  -1.1787 S33:   0.0277                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 1:120)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  50.4857  10.6151  11.7990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4208 T22:   0.2452                                     
REMARK   3      T33:   0.2760 T12:  -0.1396                                     
REMARK   3      T13:  -0.0656 T23:   0.1216                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1969 L22:   1.9770                                     
REMARK   3      L33:   4.0612 L12:   0.8890                                     
REMARK   3      L13:  -1.3515 L23:   0.8311                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1907 S12:  -0.2147 S13:  -0.2351                       
REMARK   3      S21:   0.3029 S22:  -0.2713 S23:  -0.0791                       
REMARK   3      S31:   0.0807 S32:   0.3495 S33:   0.3762                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 121:221)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  19.1616   6.3143  27.6707              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4112 T22:   0.4507                                     
REMARK   3      T33:   0.2063 T12:  -0.1006                                     
REMARK   3      T13:  -0.0628 T23:   0.0303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1408 L22:   3.5154                                     
REMARK   3      L33:   2.4658 L12:   0.5903                                     
REMARK   3      L13:   0.1608 L23:  -0.2101                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2727 S12:  -1.1669 S13:  -0.4645                       
REMARK   3      S21:   0.4686 S22:  -0.2352 S23:  -0.2751                       
REMARK   3      S31:  -0.2252 S32:  -0.0420 S33:  -0.0452                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 1:113)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  39.7511  -0.6935  -4.4200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3226 T22:   0.5154                                     
REMARK   3      T33:   0.3655 T12:  -0.0408                                     
REMARK   3      T13:   0.0136 T23:  -0.1284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8048 L22:   3.5196                                     
REMARK   3      L33:   4.2590 L12:   2.4545                                     
REMARK   3      L13:  -0.1540 L23:   0.5877                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3456 S12:   1.0468 S13:  -0.6318                       
REMARK   3      S21:  -0.3186 S22:   0.2251 S23:  -0.0401                       
REMARK   3      S31:   0.2178 S32:   0.2806 S33:   0.1282                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 114:219)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   9.1106  10.2724  15.2145              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2834 T22:   0.3829                                     
REMARK   3      T33:   0.2029 T12:   0.0141                                     
REMARK   3      T13:   0.0042 T23:   0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3100 L22:   5.6958                                     
REMARK   3      L33:   4.0106 L12:  -1.3595                                     
REMARK   3      L13:  -1.2483 L23:   2.4796                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1529 S12:  -0.0748 S13:   0.0483                       
REMARK   3      S21:   0.0257 S22:  -0.1459 S23:   0.2874                       
REMARK   3      S31:  -0.3372 S32:  -0.5241 S33:  -0.0293                       
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 4JZJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-APR-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000078701.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.954                              
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, SCALA                   
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47194                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.3.0                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 3350, 200MM SODIUM MALONATE,     
REMARK 280  100MM CITRATE BUFFER, PH 6.4, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       60.32400            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, A, B, H, L                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS C    20                                                      
REMARK 465     GLU C    21                                                      
REMARK 465     ASP C    22                                                      
REMARK 465     PRO C    23                                                      
REMARK 465     SER C   100                                                      
REMARK 465     GLY C   101                                                      
REMARK 465     LYS C   102                                                      
REMARK 465     CYS C   216                                                      
REMARK 465     ASN C   217                                                      
REMARK 465     LYS C   218                                                      
REMARK 465     THR C   219                                                      
REMARK 465     HIS C   220                                                      
REMARK 465     LYS C   243                                                      
REMARK 465     ARG C   244                                                      
REMARK 465     MET C   245                                                      
REMARK 465     GLN C   246                                                      
REMARK 465     PRO C   247                                                      
REMARK 465     GLY C   265                                                      
REMARK 465     THR C   266                                                      
REMARK 465     TYR C   267                                                      
REMARK 465     PHE C   290                                                      
REMARK 465     GLU C   291                                                      
REMARK 465     CYS C   292                                                      
REMARK 465     ASP C   293                                                      
REMARK 465     GLN C   294                                                      
REMARK 465     GLU C   295                                                      
REMARK 465     GLU C   296                                                      
REMARK 465     GLY C   297                                                      
REMARK 465     VAL C   298                                                      
REMARK 465     ASN C   299                                                      
REMARK 465     THR C   300                                                      
REMARK 465     ARG C   301                                                      
REMARK 465     ALA C   302                                                      
REMARK 465     TRP C   303                                                      
REMARK 465     ARG C   304                                                      
REMARK 465     THR C   305                                                      
REMARK 465     SER C   306                                                      
REMARK 465     LYS D    20                                                      
REMARK 465     GLU D    21                                                      
REMARK 465     ASP D    22                                                      
REMARK 465     PRO D    23                                                      
REMARK 465     ASN D    24                                                      
REMARK 465     CYS D   216                                                      
REMARK 465     ASN D   217                                                      
REMARK 465     LYS D   218                                                      
REMARK 465     THR D   219                                                      
REMARK 465     HIS D   220                                                      
REMARK 465     LYS D   243                                                      
REMARK 465     ARG D   244                                                      
REMARK 465     MET D   245                                                      
REMARK 465     GLN D   246                                                      
REMARK 465     PRO D   247                                                      
REMARK 465     LEU D   262                                                      
REMARK 465     ASN D   263                                                      
REMARK 465     PRO D   264                                                      
REMARK 465     GLY D   265                                                      
REMARK 465     THR D   266                                                      
REMARK 465     GLU D   291                                                      
REMARK 465     CYS D   292                                                      
REMARK 465     ASP D   293                                                      
REMARK 465     GLN D   294                                                      
REMARK 465     GLU D   295                                                      
REMARK 465     GLU D   296                                                      
REMARK 465     GLY D   297                                                      
REMARK 465     VAL D   298                                                      
REMARK 465     ASN D   299                                                      
REMARK 465     THR D   300                                                      
REMARK 465     ARG D   301                                                      
REMARK 465     ALA D   302                                                      
REMARK 465     TRP D   303                                                      
REMARK 465     ARG D   304                                                      
REMARK 465     THR D   305                                                      
REMARK 465     SER D   306                                                      
REMARK 465     SER A   134                                                      
REMARK 465     SER A   135                                                      
REMARK 465     LYS A   136                                                      
REMARK 465     SER A   137                                                      
REMARK 465     THR A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     GLY A   140                                                      
REMARK 465     CYS B   220                                                      
REMARK 465     SER H   135                                                      
REMARK 465     LYS H   136                                                      
REMARK 465     SER H   137                                                      
REMARK 465     THR H   138                                                      
REMARK 465     SER H   139                                                      
REMARK 465     GLY H   140                                                      
REMARK 465     CYS L   220                                                      
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   C6   NAG D   401     O5   FUL D   404              1.66            
REMARK 500   O4   NAG D   401     O5   NAG D   402              1.77            
REMARK 500   O6   NAG D   401     O5   FUL D   404              1.84            
REMARK 500   O6   NAG C   401     O5   FUL C   402              1.90            
REMARK 500   OE2  GLU C    51     OH   TYR L   102              2.05            
REMARK 500   C6   NAG D   401     O7   NAG D   402              2.09            
REMARK 500   C5   NAG D   401     O7   NAG D   402              2.09            
REMARK 500   C6   NAG D   401     C1   FUL D   404              2.11            
REMARK 500   O4   NAG C   401     O5   NAG C   403              2.13            
REMARK 500   O6   NAG C   401     C2   FUL C   402              2.14            
REMARK 500   O4   NAG D   401     O2   FUL D   405              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU D 281   CA  -  CB  -  CG  ANGL. DEV. =  16.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP C  57      -57.08   -130.58                                   
REMARK 500    ASN C  65       16.83     47.03                                   
REMARK 500    ALA C  72       66.00   -155.45                                   
REMARK 500    ILE C  73      148.27    -38.80                                   
REMARK 500    ASP C 116     -139.93     50.17                                   
REMARK 500    LYS C 144       16.82     57.82                                   
REMARK 500    HIS C 152       75.52   -104.25                                   
REMARK 500    ASP C 156     -178.50    -69.40                                   
REMARK 500    ARG C 254      -82.52    -47.87                                   
REMARK 500    PRO C 287      147.83    -37.17                                   
REMARK 500    LYS D  35      -77.83    -40.51                                   
REMARK 500    THR D  48      -80.84    -63.76                                   
REMARK 500    ASP D  57      -63.86   -108.89                                   
REMARK 500    ASN D  64       17.19     54.32                                   
REMARK 500    ALA D  72       95.13   -161.97                                   
REMARK 500    CYS D  76      -68.50   -122.65                                   
REMARK 500    ALA D  86      -71.43    -58.89                                   
REMARK 500    TRP D 104       56.89   -111.91                                   
REMARK 500    ASP D 116     -131.58     39.79                                   
REMARK 500    ASP D 156     -159.74    -75.24                                   
REMARK 500    ASP D 255      -61.88   -153.41                                   
REMARK 500    PRO D 287       98.74    -46.45                                   
REMARK 500    ALA A  92      175.00    179.42                                   
REMARK 500    SER A  99     -174.31    -67.58                                   
REMARK 500    ASP A 151       63.64     63.17                                   
REMARK 500    PRO A 154     -166.09   -102.59                                   
REMARK 500    THR A 198      -40.74   -131.19                                   
REMARK 500    ASN A 211       70.41     47.66                                   
REMARK 500    PRO A 220     -162.45    -74.35                                   
REMARK 500    ALA B  57      -36.65     65.36                                   
REMARK 500    SER B  83      106.36   -161.11                                   
REMARK 500    ASN B  96      109.64    -59.06                                   
REMARK 500    PRO B 101       31.59    -95.99                                   
REMARK 500    HIS B 204      147.31   -175.42                                   
REMARK 500    ARG B 217        7.42    -65.18                                   
REMARK 500    SER H   7      151.55    -42.06                                   
REMARK 500    ASP H 151       73.02     52.42                                   
REMARK 500    PRO H 154     -159.90    -89.77                                   
REMARK 500    THR H 167      -35.13   -130.79                                   
REMARK 500    SER H 180        3.30    -68.29                                   
REMARK 500    PRO H 220     -167.47    -58.07                                   
REMARK 500    ALA L  57      -35.32     66.02                                   
REMARK 500    ASN L 158       -2.23     72.27                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG D  409                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG C 408 BOUND   
REMARK 800  TO ASN C 46                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF SUGAR BOUND TO ASN C   
REMARK 800  80 RESIDUES 401 TO 407                                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF SUGAR BOUND TO ASN D   
REMARK 800  80 RESIDUES 401 TO 405                                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF SUGAR BOUND TO ASN D   
REMARK 800  109 RESIDUES 406 TO 408                                             
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THIS SEQUENCE IS A RESULT OF POLYMORPHIC VARIATION                   
DBREF  4JZJ C   20   306  UNP    P26951   IL3RA_HUMAN     20    307             
DBREF  4JZJ D   20   306  UNP    P26951   IL3RA_HUMAN     20    307             
DBREF  4JZJ A    1   221  PDB    4JZJ     4JZJ             1    221             
DBREF  4JZJ H    1   221  PDB    4JZJ     4JZJ             1    221             
DBREF  4JZJ B    1   220  PDB    4JZJ     4JZJ             1    220             
DBREF  4JZJ L    1   220  PDB    4JZJ     4JZJ             1    220             
SEQADV 4JZJ LYS C  144  UNP  P26951    ASN   144 SEE REMARK 999                 
SEQADV 4JZJ     C       UNP  P26951    ARG   145 DELETION                       
SEQADV 4JZJ VAL C  298  UNP  P26951    ALA   299 ENGINEERED MUTATION            
SEQADV 4JZJ LYS D  144  UNP  P26951    ASN   144 SEE REMARK 999                 
SEQADV 4JZJ     D       UNP  P26951    ARG   145 DELETION                       
SEQADV 4JZJ VAL D  298  UNP  P26951    ALA   299 ENGINEERED MUTATION            
SEQRES   1 C  287  LYS GLU ASP PRO ASN PRO PRO ILE THR ASN LEU ARG MET          
SEQRES   2 C  287  LYS ALA LYS ALA GLN GLN LEU THR TRP ASP LEU ASN ARG          
SEQRES   3 C  287  ASN VAL THR ASP ILE GLU CYS VAL LYS ASP ALA ASP TYR          
SEQRES   4 C  287  SER MET PRO ALA VAL ASN ASN SER TYR CYS GLN PHE GLY          
SEQRES   5 C  287  ALA ILE SER LEU CYS GLU VAL THR ASN TYR THR VAL ARG          
SEQRES   6 C  287  VAL ALA ASN PRO PRO PHE SER THR TRP ILE LEU PHE PRO          
SEQRES   7 C  287  GLU ASN SER GLY LYS PRO TRP ALA GLY ALA GLU ASN LEU          
SEQRES   8 C  287  THR CYS TRP ILE HIS ASP VAL ASP PHE LEU SER CYS SER          
SEQRES   9 C  287  TRP ALA VAL GLY PRO GLY ALA PRO ALA ASP VAL GLN TYR          
SEQRES  10 C  287  ASP LEU TYR LEU ASN VAL ALA LYS ARG GLN GLN TYR GLU          
SEQRES  11 C  287  CYS LEU HIS TYR LYS THR ASP ALA GLN GLY THR ARG ILE          
SEQRES  12 C  287  GLY CYS ARG PHE ASP ASP ILE SER ARG LEU SER SER GLY          
SEQRES  13 C  287  SER GLN SER SER HIS ILE LEU VAL ARG GLY ARG SER ALA          
SEQRES  14 C  287  ALA PHE GLY ILE PRO CYS THR ASP LYS PHE VAL VAL PHE          
SEQRES  15 C  287  SER GLN ILE GLU ILE LEU THR PRO PRO ASN MET THR ALA          
SEQRES  16 C  287  LYS CYS ASN LYS THR HIS SER PHE MET HIS TRP LYS MET          
SEQRES  17 C  287  ARG SER HIS PHE ASN ARG LYS PHE ARG TYR GLU LEU GLN          
SEQRES  18 C  287  ILE GLN LYS ARG MET GLN PRO VAL ILE THR GLU GLN VAL          
SEQRES  19 C  287  ARG ASP ARG THR SER PHE GLN LEU LEU ASN PRO GLY THR          
SEQRES  20 C  287  TYR THR VAL GLN ILE ARG ALA ARG GLU ARG VAL TYR GLU          
SEQRES  21 C  287  PHE LEU SER ALA TRP SER THR PRO GLN ARG PHE GLU CYS          
SEQRES  22 C  287  ASP GLN GLU GLU GLY VAL ASN THR ARG ALA TRP ARG THR          
SEQRES  23 C  287  SER                                                          
SEQRES   1 D  287  LYS GLU ASP PRO ASN PRO PRO ILE THR ASN LEU ARG MET          
SEQRES   2 D  287  LYS ALA LYS ALA GLN GLN LEU THR TRP ASP LEU ASN ARG          
SEQRES   3 D  287  ASN VAL THR ASP ILE GLU CYS VAL LYS ASP ALA ASP TYR          
SEQRES   4 D  287  SER MET PRO ALA VAL ASN ASN SER TYR CYS GLN PHE GLY          
SEQRES   5 D  287  ALA ILE SER LEU CYS GLU VAL THR ASN TYR THR VAL ARG          
SEQRES   6 D  287  VAL ALA ASN PRO PRO PHE SER THR TRP ILE LEU PHE PRO          
SEQRES   7 D  287  GLU ASN SER GLY LYS PRO TRP ALA GLY ALA GLU ASN LEU          
SEQRES   8 D  287  THR CYS TRP ILE HIS ASP VAL ASP PHE LEU SER CYS SER          
SEQRES   9 D  287  TRP ALA VAL GLY PRO GLY ALA PRO ALA ASP VAL GLN TYR          
SEQRES  10 D  287  ASP LEU TYR LEU ASN VAL ALA LYS ARG GLN GLN TYR GLU          
SEQRES  11 D  287  CYS LEU HIS TYR LYS THR ASP ALA GLN GLY THR ARG ILE          
SEQRES  12 D  287  GLY CYS ARG PHE ASP ASP ILE SER ARG LEU SER SER GLY          
SEQRES  13 D  287  SER GLN SER SER HIS ILE LEU VAL ARG GLY ARG SER ALA          
SEQRES  14 D  287  ALA PHE GLY ILE PRO CYS THR ASP LYS PHE VAL VAL PHE          
SEQRES  15 D  287  SER GLN ILE GLU ILE LEU THR PRO PRO ASN MET THR ALA          
SEQRES  16 D  287  LYS CYS ASN LYS THR HIS SER PHE MET HIS TRP LYS MET          
SEQRES  17 D  287  ARG SER HIS PHE ASN ARG LYS PHE ARG TYR GLU LEU GLN          
SEQRES  18 D  287  ILE GLN LYS ARG MET GLN PRO VAL ILE THR GLU GLN VAL          
SEQRES  19 D  287  ARG ASP ARG THR SER PHE GLN LEU LEU ASN PRO GLY THR          
SEQRES  20 D  287  TYR THR VAL GLN ILE ARG ALA ARG GLU ARG VAL TYR GLU          
SEQRES  21 D  287  PHE LEU SER ALA TRP SER THR PRO GLN ARG PHE GLU CYS          
SEQRES  22 D  287  ASP GLN GLU GLU GLY VAL ASN THR ARG ALA TRP ARG THR          
SEQRES  23 D  287  SER                                                          
SEQRES   1 A  221  GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 A  221  PRO GLY GLU SER LEU LYS ILE SER CYS LYS GLY SER GLY          
SEQRES   3 A  221  TYR SER PHE THR ASP TYR TYR MET LYS TRP ALA ARG GLN          
SEQRES   4 A  221  MET PRO GLY LYS GLY LEU GLU TRP MET GLY ASP ILE ILE          
SEQRES   5 A  221  PRO SER ASN GLY ALA THR PHE TYR ASN GLN LYS PHE LYS          
SEQRES   6 A  221  GLY GLN VAL THR ILE SER ALA ASP LYS SER ILE SER THR          
SEQRES   7 A  221  THR TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR          
SEQRES   8 A  221  ALA MET TYR TYR CYS ALA ARG SER HIS LEU LEU ARG ALA          
SEQRES   9 A  221  SER TRP PHE ALA TYR TRP GLY GLN GLY THR MET VAL THR          
SEQRES  10 A  221  VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO          
SEQRES  11 A  221  LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA          
SEQRES  12 A  221  ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO          
SEQRES  13 A  221  VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY          
SEQRES  14 A  221  VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU          
SEQRES  15 A  221  TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER          
SEQRES  16 A  221  LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS          
SEQRES  17 A  221  PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS          
SEQRES   1 B  220  ASP ILE VAL MET THR GLN SER PRO ASP SER LEU ALA VAL          
SEQRES   2 B  220  SER LEU GLY GLU ARG ALA THR ILE ASN CYS GLU SER SER          
SEQRES   3 B  220  GLN SER LEU LEU ASN SER GLY ASN GLN LYS ASN TYR LEU          
SEQRES   4 B  220  THR TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS PRO          
SEQRES   5 B  220  LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO          
SEQRES   6 B  220  ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR          
SEQRES   7 B  220  LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL          
SEQRES   8 B  220  TYR TYR CYS GLN ASN ASP TYR SER TYR PRO TYR THR PHE          
SEQRES   9 B  220  GLY GLN GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA          
SEQRES  10 B  220  ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN          
SEQRES  11 B  220  LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN          
SEQRES  12 B  220  ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL          
SEQRES  13 B  220  ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL          
SEQRES  14 B  220  THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER          
SEQRES  15 B  220  SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS          
SEQRES  16 B  220  LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER          
SEQRES  17 B  220  SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS              
SEQRES   1 H  221  GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 H  221  PRO GLY GLU SER LEU LYS ILE SER CYS LYS GLY SER GLY          
SEQRES   3 H  221  TYR SER PHE THR ASP TYR TYR MET LYS TRP ALA ARG GLN          
SEQRES   4 H  221  MET PRO GLY LYS GLY LEU GLU TRP MET GLY ASP ILE ILE          
SEQRES   5 H  221  PRO SER ASN GLY ALA THR PHE TYR ASN GLN LYS PHE LYS          
SEQRES   6 H  221  GLY GLN VAL THR ILE SER ALA ASP LYS SER ILE SER THR          
SEQRES   7 H  221  THR TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR          
SEQRES   8 H  221  ALA MET TYR TYR CYS ALA ARG SER HIS LEU LEU ARG ALA          
SEQRES   9 H  221  SER TRP PHE ALA TYR TRP GLY GLN GLY THR MET VAL THR          
SEQRES  10 H  221  VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO          
SEQRES  11 H  221  LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA          
SEQRES  12 H  221  ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO          
SEQRES  13 H  221  VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY          
SEQRES  14 H  221  VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU          
SEQRES  15 H  221  TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER          
SEQRES  16 H  221  LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS          
SEQRES  17 H  221  PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS          
SEQRES   1 L  220  ASP ILE VAL MET THR GLN SER PRO ASP SER LEU ALA VAL          
SEQRES   2 L  220  SER LEU GLY GLU ARG ALA THR ILE ASN CYS GLU SER SER          
SEQRES   3 L  220  GLN SER LEU LEU ASN SER GLY ASN GLN LYS ASN TYR LEU          
SEQRES   4 L  220  THR TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS PRO          
SEQRES   5 L  220  LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO          
SEQRES   6 L  220  ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR          
SEQRES   7 L  220  LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL          
SEQRES   8 L  220  TYR TYR CYS GLN ASN ASP TYR SER TYR PRO TYR THR PHE          
SEQRES   9 L  220  GLY GLN GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA          
SEQRES  10 L  220  ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN          
SEQRES  11 L  220  LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN          
SEQRES  12 L  220  ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL          
SEQRES  13 L  220  ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL          
SEQRES  14 L  220  THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER          
SEQRES  15 L  220  SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS          
SEQRES  16 L  220  LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER          
SEQRES  17 L  220  SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS              
MODRES 4JZJ ASN C   80  ASN  GLYCOSYLATION SITE                                 
MODRES 4JZJ ASN C   46  ASN  GLYCOSYLATION SITE                                 
MODRES 4JZJ ASN D   80  ASN  GLYCOSYLATION SITE                                 
MODRES 4JZJ ASN D  109  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C 401      14                                                       
HET    FUL  C 402      10                                                       
HET    NAG  C 403      14                                                       
HET    BMA  C 404      11                                                       
HET    MAN  C 405      11                                                       
HET    MAN  C 406      11                                                       
HET    FUL  C 407      10                                                       
HET    NAG  C 408      14                                                       
HET    NAG  D 401      14                                                       
HET    NAG  D 402      14                                                       
HET    BMA  D 403      11                                                       
HET    FUL  D 404      10                                                       
HET    FUL  D 405      10                                                       
HET    FUL  D 406      10                                                       
HET    NAG  D 407      14                                                       
HET    FUC  D 408      10                                                       
HET    NAG  D 409      14                                                       
HET    GOL  D 410       6                                                       
HET    GOL  H 301       6                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUL BETA-L-FUCOSE                                                    
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     GOL GLYCEROL                                                         
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   7  NAG    7(C8 H15 N O6)                                               
FORMUL   7  FUL    5(C6 H12 O5)                                                 
FORMUL   7  BMA    2(C6 H12 O6)                                                 
FORMUL   7  MAN    2(C6 H12 O6)                                                 
FORMUL  10  FUC    C6 H12 O5                                                    
FORMUL  12  GOL    2(C3 H8 O3)                                                  
FORMUL  14  HOH   *39(H2 O)                                                     
HELIX    1   1 ASP C  168  SER C  173  1                                   6    
HELIX    2   2 PHE C  201  GLU C  205  1                                   5    
HELIX    3   3 ASP D  168  SER D  174  1                                   7    
HELIX    4   4 PHE D  201  GLU D  205  1                                   5    
HELIX    5   5 GLN A   62  LYS A   65  5                                   4    
HELIX    6   6 LYS A   87  THR A   91  5                                   5    
HELIX    7   7 SER A  163  ALA A  165  5                                   3    
HELIX    8   8 SER A  194  THR A  198  5                                   5    
HELIX    9   9 LYS A  208  ASN A  211  5                                   4    
HELIX   10  10 GLN B   85  VAL B   89  5                                   5    
HELIX   11  11 SER B  127  SER B  133  1                                   7    
HELIX   12  12 LYS B  189  GLU B  193  1                                   5    
HELIX   13  13 SER H   28  TYR H   32  5                                   5    
HELIX   14  14 ASN H   61  GLY H   66  1                                   6    
HELIX   15  15 LYS H   87  THR H   91  5                                   5    
HELIX   16  16 SER H  163  ALA H  165  5                                   3    
HELIX   17  17 SER H  194  LEU H  196  5                                   3    
HELIX   18  18 LYS H  208  ASN H  211  5                                   4    
HELIX   19  19 GLN L   85  VAL L   89  5                                   5    
HELIX   20  20 SER L  127  SER L  133  1                                   7    
HELIX   21  21 LYS L  189  GLU L  193  1                                   5    
SHEET    1   A 3 ILE C  27  LYS C  33  0                                        
SHEET    2   A 3 GLN C  38  LEU C  43 -1  O  ASP C  42   N  THR C  28           
SHEET    3   A 3 TYR C  67  GLN C  69 -1  O  CYS C  68   N  LEU C  39           
SHEET    1   B 4 TYR C  58  PRO C  61  0                                        
SHEET    2   B 4 ILE C  50  LYS C  54 -1  N  LYS C  54   O  TYR C  58           
SHEET    3   B 4 THR C  79  VAL C  85 -1  O  THR C  82   N  VAL C  53           
SHEET    4   B 4 PHE C  90  PHE C  96 -1  O  PHE C  90   N  VAL C  85           
SHEET    1   C 4 ALA C 107  HIS C 115  0                                        
SHEET    2   C 4 PHE C 119  VAL C 126 -1  O  ALA C 125   N  GLU C 108           
SHEET    3   C 4 ARG C 161  PHE C 166 -1  O  PHE C 166   N  LEU C 120           
SHEET    4   C 4 HIS C 152  THR C 155 -1  N  LYS C 154   O  ILE C 162           
SHEET    1   D 4 GLN C 146  GLU C 149  0                                        
SHEET    2   D 4 GLN C 135  VAL C 142 -1  N  LEU C 140   O  TYR C 148           
SHEET    3   D 4 SER C 178  ARG C 186 -1  O  LEU C 182   N  TYR C 139           
SHEET    4   D 4 THR C 195  VAL C 200 -1  O  THR C 195   N  VAL C 183           
SHEET    1   E 3 ASN C 211  THR C 213  0                                        
SHEET    2   E 3 PHE C 222  LYS C 226 -1  O  HIS C 224   N  THR C 213           
SHEET    3   E 3 SER C 258  GLN C 260 -1  O  PHE C 259   N  MET C 223           
SHEET    1   F 3 ILE C 249  VAL C 253  0                                        
SHEET    2   F 3 PHE C 235  ILE C 241 -1  N  LEU C 239   O  GLU C 251           
SHEET    3   F 3 VAL C 269  GLU C 275 -1  O  ARG C 272   N  GLU C 238           
SHEET    1   G 3 ILE D  27  LYS D  33  0                                        
SHEET    2   G 3 GLN D  38  LEU D  43 -1  O  GLN D  38   N  LYS D  33           
SHEET    3   G 3 TYR D  67  GLN D  69 -1  O  CYS D  68   N  LEU D  39           
SHEET    1   H 4 TYR D  58  PRO D  61  0                                        
SHEET    2   H 4 ILE D  50  LYS D  54 -1  N  CYS D  52   O  MET D  60           
SHEET    3   H 4 THR D  79  VAL D  85 -1  O  THR D  82   N  VAL D  53           
SHEET    4   H 4 PHE D  90  PHE D  96 -1  O  THR D  92   N  VAL D  83           
SHEET    1   I 4 GLU D 108  HIS D 115  0                                        
SHEET    2   I 4 PHE D 119  ALA D 125 -1  O  SER D 123   N  THR D 111           
SHEET    3   I 4 ARG D 161  PHE D 166 -1  O  PHE D 166   N  LEU D 120           
SHEET    4   I 4 TYR D 153  THR D 155 -1  N  LYS D 154   O  GLY D 163           
SHEET    1   J 3 GLN D 135  ASN D 141  0                                        
SHEET    2   J 3 SER D 178  ARG D 186 -1  O  HIS D 180   N  ASN D 141           
SHEET    3   J 3 GLY D 191  VAL D 200 -1  O  THR D 195   N  VAL D 183           
SHEET    1   K 3 ASN D 211  THR D 213  0                                        
SHEET    2   K 3 PHE D 222  LYS D 226 -1  O  HIS D 224   N  THR D 213           
SHEET    3   K 3 SER D 258  GLN D 260 -1  O  PHE D 259   N  MET D 223           
SHEET    1   L 3 ILE D 249  VAL D 253  0                                        
SHEET    2   L 3 PHE D 235  ILE D 241 -1  N  ILE D 241   O  ILE D 249           
SHEET    3   L 3 ALA D 273  GLU D 275 -1  O  ARG D 274   N  ARG D 236           
SHEET    1   M 4 ILE D 249  VAL D 253  0                                        
SHEET    2   M 4 PHE D 235  ILE D 241 -1  N  ILE D 241   O  ILE D 249           
SHEET    3   M 4 THR D 268  GLN D 270 -1  O  GLN D 270   N  GLN D 240           
SHEET    4   M 4 GLN D 288  ARG D 289 -1  O  GLN D 288   N  VAL D 269           
SHEET    1   N 4 GLN A   3  GLN A   6  0                                        
SHEET    2   N 4 LEU A  18  SER A  25 -1  O  LYS A  23   N  VAL A   5           
SHEET    3   N 4 THR A  78  TRP A  83 -1  O  TRP A  83   N  LEU A  18           
SHEET    4   N 4 THR A  69  ASP A  73 -1  N  THR A  69   O  GLN A  82           
SHEET    1   O 6 GLU A  10  LYS A  12  0                                        
SHEET    2   O 6 THR A 114  VAL A 118  1  O  THR A 117   N  LYS A  12           
SHEET    3   O 6 ALA A  92  ARG A  98 -1  N  ALA A  92   O  VAL A 116           
SHEET    4   O 6 MET A  34  GLN A  39 -1  N  LYS A  35   O  ALA A  97           
SHEET    5   O 6 LEU A  45  ILE A  51 -1  O  MET A  48   N  TRP A  36           
SHEET    6   O 6 THR A  58  TYR A  60 -1  O  PHE A  59   N  ASP A  50           
SHEET    1   P 4 GLU A  10  LYS A  12  0                                        
SHEET    2   P 4 THR A 114  VAL A 118  1  O  THR A 117   N  LYS A  12           
SHEET    3   P 4 ALA A  92  ARG A  98 -1  N  ALA A  92   O  VAL A 116           
SHEET    4   P 4 TYR A 109  TRP A 110 -1  O  TYR A 109   N  ARG A  98           
SHEET    1   Q 4 SER A 127  LEU A 131  0                                        
SHEET    2   Q 4 THR A 142  TYR A 152 -1  O  LEU A 148   N  PHE A 129           
SHEET    3   Q 4 TYR A 183  PRO A 192 -1  O  TYR A 183   N  TYR A 152           
SHEET    4   Q 4 VAL A 170  THR A 172 -1  N  HIS A 171   O  VAL A 188           
SHEET    1   R 4 SER A 127  LEU A 131  0                                        
SHEET    2   R 4 THR A 142  TYR A 152 -1  O  LEU A 148   N  PHE A 129           
SHEET    3   R 4 TYR A 183  PRO A 192 -1  O  TYR A 183   N  TYR A 152           
SHEET    4   R 4 VAL A 176  LEU A 177 -1  N  VAL A 176   O  SER A 184           
SHEET    1   S 3 THR A 158  TRP A 161  0                                        
SHEET    2   S 3 TYR A 201  HIS A 207 -1  O  ASN A 204   N  SER A 160           
SHEET    3   S 3 THR A 212  VAL A 218 -1  O  THR A 212   N  HIS A 207           
SHEET    1   T 4 MET B   4  SER B   7  0                                        
SHEET    2   T 4 ALA B  19  SER B  25 -1  O  ASN B  22   N  SER B   7           
SHEET    3   T 4 ASP B  76  ILE B  81 -1  O  PHE B  77   N  CYS B  23           
SHEET    4   T 4 PHE B  68  SER B  73 -1  N  SER B  69   O  THR B  80           
SHEET    1   U 6 SER B  10  VAL B  13  0                                        
SHEET    2   U 6 THR B 108  ILE B 112  1  O  GLU B 111   N  VAL B  13           
SHEET    3   U 6 ALA B  90  ASN B  96 -1  N  ALA B  90   O  LEU B 110           
SHEET    4   U 6 LEU B  39  GLN B  44 -1  N  THR B  40   O  GLN B  95           
SHEET    5   U 6 LYS B  51  TYR B  55 -1  O  LEU B  53   N  TRP B  41           
SHEET    6   U 6 THR B  59  ARG B  60 -1  O  THR B  59   N  TYR B  55           
SHEET    1   V 4 SER B 120  PHE B 124  0                                        
SHEET    2   V 4 THR B 135  PHE B 145 -1  O  VAL B 139   N  PHE B 124           
SHEET    3   V 4 TYR B 179  SER B 188 -1  O  LEU B 187   N  ALA B 136           
SHEET    4   V 4 SER B 165  VAL B 169 -1  N  GLN B 166   O  THR B 184           
SHEET    1   W 4 ALA B 159  LEU B 160  0                                        
SHEET    2   W 4 LYS B 151  VAL B 156 -1  N  VAL B 156   O  ALA B 159           
SHEET    3   W 4 VAL B 197  THR B 203 -1  O  GLU B 201   N  GLN B 153           
SHEET    4   W 4 VAL B 211  ASN B 216 -1  O  VAL B 211   N  VAL B 202           
SHEET    1   X 4 GLN H   3  GLN H   6  0                                        
SHEET    2   X 4 LEU H  18  SER H  25 -1  O  SER H  25   N  GLN H   3           
SHEET    3   X 4 THR H  78  TRP H  83 -1  O  THR H  79   N  CYS H  22           
SHEET    4   X 4 THR H  69  ASP H  73 -1  N  ASP H  73   O  THR H  78           
SHEET    1   Y 6 GLU H  10  LYS H  12  0                                        
SHEET    2   Y 6 THR H 114  VAL H 118  1  O  MET H 115   N  GLU H  10           
SHEET    3   Y 6 ALA H  92  ARG H  98 -1  N  ALA H  92   O  VAL H 116           
SHEET    4   Y 6 MET H  34  GLN H  39 -1  N  ALA H  37   O  TYR H  95           
SHEET    5   Y 6 LEU H  45  ILE H  51 -1  O  MET H  48   N  TRP H  36           
SHEET    6   Y 6 THR H  58  TYR H  60 -1  O  PHE H  59   N  ASP H  50           
SHEET    1   Z 4 GLU H  10  LYS H  12  0                                        
SHEET    2   Z 4 THR H 114  VAL H 118  1  O  MET H 115   N  GLU H  10           
SHEET    3   Z 4 ALA H  92  ARG H  98 -1  N  ALA H  92   O  VAL H 116           
SHEET    4   Z 4 TYR H 109  TRP H 110 -1  O  TYR H 109   N  ARG H  98           
SHEET    1  AA 4 SER H 127  LEU H 131  0                                        
SHEET    2  AA 4 THR H 142  TYR H 152 -1  O  GLY H 146   N  LEU H 131           
SHEET    3  AA 4 TYR H 183  PRO H 192 -1  O  TYR H 183   N  TYR H 152           
SHEET    4  AA 4 VAL H 170  THR H 172 -1  N  HIS H 171   O  VAL H 188           
SHEET    1  AB 4 SER H 127  LEU H 131  0                                        
SHEET    2  AB 4 THR H 142  TYR H 152 -1  O  GLY H 146   N  LEU H 131           
SHEET    3  AB 4 TYR H 183  PRO H 192 -1  O  TYR H 183   N  TYR H 152           
SHEET    4  AB 4 VAL H 176  LEU H 177 -1  N  VAL H 176   O  SER H 184           
SHEET    1  AC 3 THR H 158  TRP H 161  0                                        
SHEET    2  AC 3 ILE H 202  HIS H 207 -1  O  ASN H 204   N  SER H 160           
SHEET    3  AC 3 THR H 212  LYS H 217 -1  O  VAL H 214   N  VAL H 205           
SHEET    1  AD 4 MET L   4  SER L   7  0                                        
SHEET    2  AD 4 ALA L  19  SER L  25 -1  O  ASN L  22   N  SER L   7           
SHEET    3  AD 4 ASP L  76  ILE L  81 -1  O  ILE L  81   N  ALA L  19           
SHEET    4  AD 4 PHE L  68  SER L  73 -1  N  SER L  69   O  THR L  80           
SHEET    1  AE 6 SER L  10  SER L  14  0                                        
SHEET    2  AE 6 THR L 108  LYS L 113  1  O  GLU L 111   N  LEU L  11           
SHEET    3  AE 6 ALA L  90  ASN L  96 -1  N  ALA L  90   O  LEU L 110           
SHEET    4  AE 6 LEU L  39  GLN L  44 -1  N  TYR L  42   O  TYR L  93           
SHEET    5  AE 6 LYS L  51  TYR L  55 -1  O  LEU L  53   N  TRP L  41           
SHEET    6  AE 6 THR L  59  ARG L  60 -1  O  THR L  59   N  TYR L  55           
SHEET    1  AF 2 LEU L  30  ASN L  31  0                                        
SHEET    2  AF 2 LYS L  36  ASN L  37 -1  O  LYS L  36   N  ASN L  31           
SHEET    1  AG 4 SER L 120  PHE L 124  0                                        
SHEET    2  AG 4 THR L 135  PHE L 145 -1  O  ASN L 143   N  SER L 120           
SHEET    3  AG 4 TYR L 179  SER L 188 -1  O  LEU L 187   N  ALA L 136           
SHEET    4  AG 4 SER L 165  VAL L 169 -1  N  GLN L 166   O  THR L 184           
SHEET    1  AH 4 ALA L 159  LEU L 160  0                                        
SHEET    2  AH 4 LYS L 151  VAL L 156 -1  N  VAL L 156   O  ALA L 159           
SHEET    3  AH 4 VAL L 197  THR L 203 -1  O  GLU L 201   N  GLN L 153           
SHEET    4  AH 4 VAL L 211  ASN L 216 -1  O  VAL L 211   N  VAL L 202           
SSBOND   1 CYS C   52    CYS C   68                          1555   1555  2.04  
SSBOND   2 CYS C   76    CYS C  194                          1555   1555  2.07  
SSBOND   3 CYS C  112    CYS C  122                          1555   1555  2.07  
SSBOND   4 CYS C  150    CYS C  164                          1555   1555  2.02  
SSBOND   5 CYS D   52    CYS D   68                          1555   1555  2.04  
SSBOND   6 CYS D   76    CYS D  194                          1555   1555  2.07  
SSBOND   7 CYS D  112    CYS D  122                          1555   1555  2.06  
SSBOND   8 CYS D  150    CYS D  164                          1555   1555  2.05  
SSBOND   9 CYS A   22    CYS A   96                          1555   1555  2.04  
SSBOND  10 CYS A  147    CYS A  203                          1555   1555  2.03  
SSBOND  11 CYS B   23    CYS B   94                          1555   1555  2.05  
SSBOND  12 CYS B  140    CYS B  200                          1555   1555  2.04  
SSBOND  13 CYS H   22    CYS H   96                          1555   1555  2.04  
SSBOND  14 CYS H  147    CYS H  203                          1555   1555  2.03  
SSBOND  15 CYS L   23    CYS L   94                          1555   1555  2.07  
SSBOND  16 CYS L  140    CYS L  200                          1555   1555  2.03  
LINK         ND2 ASN C  80                 C1  NAG C 401     1555   1555  1.72  
LINK         O3  NAG C 401                 C1  FUL C 407     1555   1555  1.55  
LINK         O4  NAG C 401                 C1  NAG C 403     1555   1555  1.21  
LINK         O6  NAG C 401                 C1  FUL C 402     1555   1555  1.30  
LINK         O4  NAG C 403                 C1  BMA C 404     1555   1555  1.43  
LINK         O3  BMA C 404                 C1  MAN C 406     1555   1555  1.45  
LINK         O6  BMA C 404                 C1  MAN C 405     1555   1555  1.45  
LINK         ND2 ASN C  46                 C1  NAG C 408     1555   1555  1.72  
LINK         ND2 ASN D  80                 C1  NAG D 401     1555   1555  1.43  
LINK         O4  NAG D 401                 C1  NAG D 402     1555   1555  1.37  
LINK         O3  NAG D 401                 C1  FUL D 405     1555   1555  1.43  
LINK         O6  NAG D 401                 C1  FUL D 404     1555   1555  1.49  
LINK         ND2 ASN D 109                 C1  NAG D 407     1555   1555  2.00  
LINK         O3  NAG D 407                 C1  FUC D 408     1555   1555  1.35  
LINK         O4  NAG D 402                 C1  BMA D 403     1555   1555  1.44  
LINK         C1  FUL D 406                 O6  NAG D 407     1555   1555  1.45  
CISPEP   1 ASN C   87    PRO C   88          0       -10.40                     
CISPEP   2 PHE C   96    PRO C   97          0        -9.42                     
CISPEP   3 PRO C  103    TRP C  104          0        -6.14                     
CISPEP   4 LEU C  262    ASN C  263          0         9.45                     
CISPEP   5 ASN C  263    PRO C  264          0         0.04                     
CISPEP   6 ASN D   87    PRO D   88          0        -4.09                     
CISPEP   7 PHE D   96    PRO D   97          0       -10.16                     
CISPEP   8 PRO D  103    TRP D  104          0        -1.22                     
CISPEP   9 LYS D  144    ARG D  145          0        -0.72                     
CISPEP  10 PHE A  153    PRO A  154          0        -4.39                     
CISPEP  11 GLU A  155    PRO A  156          0        -0.65                     
CISPEP  12 SER B    7    PRO B    8          0         2.30                     
CISPEP  13 TYR B  100    PRO B  101          0        -1.68                     
CISPEP  14 TYR B  146    PRO B  147          0         8.40                     
CISPEP  15 PHE H  153    PRO H  154          0        -3.93                     
CISPEP  16 GLU H  155    PRO H  156          0         3.37                     
CISPEP  17 SER L    7    PRO L    8          0        -6.21                     
CISPEP  18 TYR L  100    PRO L  101          0       -15.07                     
CISPEP  19 TYR L  146    PRO L  147          0        -5.02                     
SITE     1 AC1  2 FUL D 406  NAG D 407                                          
SITE     1 AC2  1 ARG D 184                                                     
SITE     1 AC3  9 PRO H 174  VAL H 176  SER H 184  LEU H 185                    
SITE     2 AC3  9 SER H 186  HOH H 409  SER L 168  SER L 182                    
SITE     3 AC3  9 THR L 184                                                     
SITE     1 AC4  2 ASN C  46  THR C  48                                          
SITE     1 AC5 14 ALA C  56  ASN C  80  THR C  82  SER C  91                    
SITE     2 AC5 14 TRP C  93  LEU C  95  HOH C 501  ASN H  55                    
SITE     3 AC5 14 ALA H  57  THR H  58  PHE H  59  TYR H  60                    
SITE     4 AC5 14 GLN H  62  LYS H  65                                          
SITE     1 AC6  6 ALA A  57  THR A  58  PHE A  59  ASN D  80                    
SITE     2 AC6  6 THR D  82  TRP D  93                                          
SITE     1 AC7  7 ASP C 118  ARG C 171  ARG C 228  GLU D 108                    
SITE     2 AC7  7 ASN D 109  ALA D 125  NAG D 409                               
CRYST1   88.300  120.648   92.968  90.00  97.45  90.00 P 1 21 1      4          
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      0.011325  0.000000  0.001482        0.00000                         
SCALE2      0.000000  0.008289  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010848        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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