GenomeNet

Database: PDB
Entry: 4Z7O
LinkDB: 4Z7O
Original site: 4Z7O 
HEADER    MEMBRANE PROTEIN/IMMUNE SYSTEM          07-APR-15   4Z7O              
TITLE     INTEGRIN ALPHAIIBBETA3 IN COMPLEX WITH AGDV PEPTIDE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-IIB;                                        
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 32-486;                                       
COMPND   5 SYNONYM: GPALPHA IIB,GPIIB,PLATELET MEMBRANE GLYCOPROTEIN IIB;       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: INTEGRIN BETA-3;                                           
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 29-497;                                       
COMPND  11 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA,GPIIIA;                 
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: MONOCLONAL ANTIBODY 10E5 FAB HEAVY CHAIN;                  
COMPND  15 CHAIN: E, H;                                                         
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: MONOCLONAL ANTIBODY 10E5 FAB LIGHT CHAIN;                  
COMPND  19 CHAIN: F, L;                                                         
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 5;                                                           
COMPND  22 MOLECULE: TETRAPEPTIDE ALA-GLY-ASP-VAL;                              
COMPND  23 CHAIN: G, I;                                                         
COMPND  24 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: ITGA2B, GP2B, ITGAB;                                           
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: ITGB3, GP3A;                                                   
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  17 ORGANISM_TAXID: 10090;                                               
SOURCE  18 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  20 MOL_ID: 4;                                                           
SOURCE  21 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  22 ORGANISM_TAXID: 10090;                                               
SOURCE  23 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  25 MOL_ID: 5;                                                           
SOURCE  26 SYNTHETIC: YES;                                                      
SOURCE  27 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  28 ORGANISM_TAXID: 9606                                                 
KEYWDS    CELL ADHESION, PLATELET AGGREGATION, MEMBRANE PROTEIN-IMMUNE SYSTEM   
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.Y.LIN,J.ZHU,T.A.SPRINGER                                            
REVDAT   2   09-MAR-16 4Z7O    1       JRNL                                     
REVDAT   1   27-JAN-16 4Z7O    0                                                
JRNL        AUTH   F.Y.LIN,J.ZHU,E.T.ENG,N.E.HUDSON,T.A.SPRINGER                
JRNL        TITL   BETA-SUBUNIT BINDING IS SUFFICIENT FOR LIGANDS TO OPEN THE   
JRNL        TITL 2 INTEGRIN ALPHA IIB BETA 3 HEADPIECE.                         
JRNL        REF    J.BIOL.CHEM.                  V. 291  4537 2016              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   26631735                                                     
JRNL        DOI    10.1074/JBC.M115.705624                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2142: ???)                              
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) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.03                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 90699                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.170                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1966                            
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 49.0342 -  6.8629    0.99     6797   147  0.1981 0.2559        
REMARK   3     2  6.8629 -  5.4496    1.00     6609   147  0.2036 0.2374        
REMARK   3     3  5.4496 -  4.7614    1.00     6520   144  0.1647 0.1718        
REMARK   3     4  4.7614 -  4.3263    1.00     6491   144  0.1597 0.2036        
REMARK   3     5  4.3263 -  4.0164    1.00     6468   143  0.1882 0.2254        
REMARK   3     6  4.0164 -  3.7797    1.00     6486   143  0.2176 0.2420        
REMARK   3     7  3.7797 -  3.5905    1.00     6424   143  0.2474 0.2938        
REMARK   3     8  3.5905 -  3.4342    1.00     6417   142  0.2635 0.2649        
REMARK   3     9  3.4342 -  3.3020    1.00     6406   143  0.2829 0.3035        
REMARK   3    10  3.3020 -  3.1881    1.00     6415   142  0.3165 0.3354        
REMARK   3    11  3.1881 -  3.0884    1.00     6395   141  0.3461 0.3957        
REMARK   3    12  3.0884 -  3.0002    0.99     6388   140  0.3851 0.4020        
REMARK   3    13  3.0002 -  2.9212    0.92     5876   135  0.3836 0.4165        
REMARK   3    14  2.9212 -  2.8499    0.78     5041   112  0.3975 0.4176        
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)     : 0.510            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.560           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006          21635                                  
REMARK   3   ANGLE     :  0.555          29371                                  
REMARK   3   CHIRALITY :  0.043           3278                                  
REMARK   3   PLANARITY :  0.003           3806                                  
REMARK   3   DIHEDRAL  :  8.669          12890                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 48                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1:44)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  48.9374  88.3259  38.7782              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7487 T22:   0.6393                                     
REMARK   3      T33:   0.6981 T12:   0.0041                                     
REMARK   3      T13:   0.0239 T23:   0.0269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5099 L22:   2.7771                                     
REMARK   3      L33:   4.2189 L12:  -1.6390                                     
REMARK   3      L13:  -1.7827 L23:   0.1389                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1293 S12:   0.2827 S13:   0.0689                       
REMARK   3      S21:  -0.2057 S22:   0.1672 S23:   0.0801                       
REMARK   3      S31:   0.2199 S32:  -0.3505 S33:  -0.0069                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 45:73)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  40.5942  95.4273  39.0308              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9221 T22:   0.7729                                     
REMARK   3      T33:   0.8015 T12:   0.0924                                     
REMARK   3      T13:  -0.0279 T23:   0.1309                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0962 L22:   8.5792                                     
REMARK   3      L33:   4.6721 L12:  -2.7237                                     
REMARK   3      L13:  -3.2502 L23:   5.8552                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6259 S12:   0.5107 S13:   0.3045                       
REMARK   3      S21:  -1.2553 S22:  -0.7001 S23:   0.4464                       
REMARK   3      S31:  -1.0149 S32:  -0.9709 S33:  -0.1544                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 74:274)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  42.3759  94.8952  62.8020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8036 T22:   0.6059                                     
REMARK   3      T33:   0.7684 T12:  -0.0303                                     
REMARK   3      T13:   0.1566 T23:  -0.0137                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9254 L22:   1.3998                                     
REMARK   3      L33:   1.7896 L12:   0.0961                                     
REMARK   3      L13:  -0.1177 L23:   0.1513                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1103 S12:  -0.2351 S13:   0.0685                       
REMARK   3      S21:   0.3990 S22:  -0.1376 S23:   0.3226                       
REMARK   3      S31:   0.1147 S32:  -0.3360 S33:   0.0320                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 275:334)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  66.6390  85.5958  60.1820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7065 T22:   0.4786                                     
REMARK   3      T33:   0.5941 T12:   0.0947                                     
REMARK   3      T13:   0.0468 T23:   0.0908                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8266 L22:   6.3465                                     
REMARK   3      L33:   5.9508 L12:   1.6135                                     
REMARK   3      L13:  -0.6422 L23:   1.3825                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2673 S12:  -0.3186 S13:  -0.0935                       
REMARK   3      S21:   0.5557 S22:  -0.1386 S23:  -0.3967                       
REMARK   3      S31:   0.3327 S32:   0.3740 S33:  -0.1450                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 335:448)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  62.7201  82.8962  45.5798              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7841 T22:   0.4971                                     
REMARK   3      T33:   0.7131 T12:   0.0880                                     
REMARK   3      T13:   0.0802 T23:   0.0370                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4994 L22:   1.8681                                     
REMARK   3      L33:   2.9307 L12:   0.7077                                     
REMARK   3      L13:  -0.1490 L23:   0.3150                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0577 S12:  -0.0720 S13:  -0.3714                       
REMARK   3      S21:   0.2401 S22:   0.0225 S23:  -0.1419                       
REMARK   3      S31:   0.3207 S32:   0.1045 S33:   0.0129                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 449:454)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  60.0008  72.8872  33.0186              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0713 T22:   0.7435                                     
REMARK   3      T33:   0.8797 T12:   0.1756                                     
REMARK   3      T13:   0.2645 T23:  -0.0087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0125 L22:   5.8088                                     
REMARK   3      L33:   4.8155 L12:  -1.7746                                     
REMARK   3      L13:   2.2503 L23:  -4.6977                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   2.2308 S12:   2.8164 S13:   0.8473                       
REMARK   3      S21:  -2.8226 S22:  -3.4051 S23:  -2.0138                       
REMARK   3      S31:   1.5117 S32:   0.6777 S33:   0.7256                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 3:62)                               
REMARK   3    ORIGIN FOR THE GROUP (A): 122.9506  89.0619  35.4175              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2170 T22:   2.7088                                     
REMARK   3      T33:   1.7895 T12:   0.3751                                     
REMARK   3      T13:  -0.0151 T23:  -0.1641                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6895 L22:   4.8945                                     
REMARK   3      L33:   2.6585 L12:  -4.6013                                     
REMARK   3      L13:  -4.3351 L23:   2.9869                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3507 S12:  -0.0002 S13:   0.1655                       
REMARK   3      S21:   0.5118 S22:   0.7219 S23:  -1.2012                       
REMARK   3      S31:   0.6563 S32:   1.7644 S33:  -0.2579                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 63:108)                             
REMARK   3    ORIGIN FOR THE GROUP (A): 103.7106 113.2412  52.2560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0969 T22:   1.6858                                     
REMARK   3      T33:   1.5354 T12:  -0.2084                                     
REMARK   3      T13:  -0.0318 T23:  -0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0609 L22:   6.6252                                     
REMARK   3      L33:   9.3271 L12:  -2.8515                                     
REMARK   3      L13:  -2.6413 L23:   6.6626                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0375 S12:  -0.4320 S13:   1.0053                       
REMARK   3      S21:  -0.3645 S22:   0.9239 S23:  -1.1067                       
REMARK   3      S31:  -0.6313 S32:   1.4343 S33:  -1.1902                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 109:349)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  68.0224 117.8247  63.3943              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8561 T22:   0.5194                                     
REMARK   3      T33:   0.7635 T12:   0.0231                                     
REMARK   3      T13:   0.0835 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3982 L22:   3.7214                                     
REMARK   3      L33:   2.0840 L12:   0.9976                                     
REMARK   3      L13:   0.1117 L23:   0.5293                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0963 S12:  -0.3027 S13:   0.3103                       
REMARK   3      S21:   0.2071 S22:  -0.0031 S23:  -0.1197                       
REMARK   3      S31:  -0.4205 S32:   0.1188 S33:  -0.0898                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 350:390)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  97.5314 103.8837  60.4624              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0390 T22:   1.2816                                     
REMARK   3      T33:   1.3737 T12:   0.1759                                     
REMARK   3      T13:  -0.0000 T23:   0.1086                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6062 L22:   7.6125                                     
REMARK   3      L33:   6.0040 L12:  -6.0968                                     
REMARK   3      L13:  -6.7833 L23:   6.1027                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0120 S12:  -0.5583 S13:  -0.1010                       
REMARK   3      S21:   0.9136 S22:   0.7481 S23:   0.2361                       
REMARK   3      S31:   1.3488 S32:   1.4676 S33:   0.3309                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 391:432)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 100.7373 104.2683  48.2019              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9720 T22:   1.4270                                     
REMARK   3      T33:   1.3886 T12:   0.0542                                     
REMARK   3      T13:  -0.0449 T23:   0.1107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9800 L22:   3.8495                                     
REMARK   3      L33:   9.1694 L12:   0.3584                                     
REMARK   3      L13:  -2.3525 L23:   3.7957                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1239 S12:   0.0639 S13:   0.1296                       
REMARK   3      S21:   0.0384 S22:   0.0432 S23:  -0.0930                       
REMARK   3      S31:   0.6409 S32:   0.8891 S33:   0.1007                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 433:466)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 116.2241  88.5267  19.0174              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3907 T22:   2.7706                                     
REMARK   3      T33:   1.4919 T12:   0.4165                                     
REMARK   3      T13:   0.1673 T23:  -0.0361                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7908 L22:   3.9741                                     
REMARK   3      L33:   3.7140 L12:   2.0870                                     
REMARK   3      L13:  -1.6209 L23:  -2.5643                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1019 S12:  -0.6206 S13:  -0.3227                       
REMARK   3      S21:  -1.1906 S22:  -0.3009 S23:  -0.9337                       
REMARK   3      S31:   0.7554 S32:   1.1236 S33:   0.2378                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 1:68)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  88.1720  94.5747 131.7442              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8161 T22:   1.0539                                     
REMARK   3      T33:   0.7526 T12:   0.0896                                     
REMARK   3      T13:   0.0486 T23:  -0.0160                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7284 L22:   5.5966                                     
REMARK   3      L33:   5.3527 L12:   1.2466                                     
REMARK   3      L13:  -2.7228 L23:  -1.8461                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0601 S12:  -0.1016 S13:   0.1192                       
REMARK   3      S21:   0.0606 S22:   0.1309 S23:  -0.3189                       
REMARK   3      S31:   0.3219 S32:   1.0625 S33:  -0.0628                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 69:274)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  92.3802  90.0347 107.4822              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0517 T22:   1.4401                                     
REMARK   3      T33:   0.8925 T12:   0.1532                                     
REMARK   3      T13:   0.2569 T23:   0.0155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5310 L22:   1.3653                                     
REMARK   3      L33:   2.7015 L12:   0.4623                                     
REMARK   3      L13:  -0.3673 L23:  -0.3758                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2224 S12:   0.8693 S13:  -0.1291                       
REMARK   3      S21:  -0.4085 S22:  -0.0899 S23:  -0.3042                       
REMARK   3      S31:   0.3739 S32:   0.5733 S33:   0.3292                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 275:334)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  71.7494  75.7193 115.2614              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4368 T22:   1.0162                                     
REMARK   3      T33:   0.9625 T12:  -0.0831                                     
REMARK   3      T13:   0.2787 T23:  -0.2318                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0190 L22:   3.6635                                     
REMARK   3      L33:   5.6139 L12:  -2.0431                                     
REMARK   3      L13:  -1.1466 L23:   0.5681                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1672 S12:   1.0556 S13:  -0.8752                       
REMARK   3      S21:  -0.5648 S22:  -0.0695 S23:   0.0525                       
REMARK   3      S31:   1.4168 S32:  -0.3734 S33:   0.2698                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 335:399)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  73.1045  76.2788 126.1772              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1630 T22:   0.8954                                     
REMARK   3      T33:   0.9327 T12:   0.0194                                     
REMARK   3      T13:   0.2181 T23:  -0.1157                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0840 L22:   2.7434                                     
REMARK   3      L33:   4.1740 L12:  -0.7774                                     
REMARK   3      L13:   0.1942 L23:   0.1275                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2215 S12:  -0.0547 S13:  -0.8734                       
REMARK   3      S21:  -0.2762 S22:   0.2176 S23:  -0.1902                       
REMARK   3      S31:   1.0859 S32:   0.0730 S33:   0.0293                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 400:428)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  75.8320  84.7284 132.4602              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9146 T22:   0.9493                                     
REMARK   3      T33:   0.7276 T12:   0.0428                                     
REMARK   3      T13:   0.0863 T23:   0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2899 L22:   4.3433                                     
REMARK   3      L33:   4.6012 L12:  -0.0616                                     
REMARK   3      L13:  -0.1798 L23:  -0.8135                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5179 S12:   0.2448 S13:  -0.4860                       
REMARK   3      S21:  -0.0091 S22:   0.1089 S23:   0.0178                       
REMARK   3      S31:   0.8727 S32:  -0.0559 S33:   0.3949                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 429:453)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  82.2200  85.5692 136.8298              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8155 T22:   0.9804                                     
REMARK   3      T33:   0.7668 T12:   0.0263                                     
REMARK   3      T13:   0.1512 T23:  -0.0541                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4223 L22:   8.5688                                     
REMARK   3      L33:   6.0212 L12:  -3.2088                                     
REMARK   3      L13:   1.6213 L23:  -4.0844                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0072 S12:  -0.3155 S13:  -0.3244                       
REMARK   3      S21:   0.8051 S22:  -0.2198 S23:  -0.3376                       
REMARK   3      S31:   0.3826 S32:   0.3481 S33:   0.2342                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 3:50)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  15.9315  69.3059 141.4911              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6892 T22:   2.0513                                     
REMARK   3      T33:   1.7173 T12:  -0.6487                                     
REMARK   3      T13:   0.3455 T23:  -0.1245                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6891 L22:   7.1701                                     
REMARK   3      L33:   4.1725 L12:   1.2031                                     
REMARK   3      L13:  -5.5771 L23:  -1.5799                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8476 S12:   0.7972 S13:  -0.7882                       
REMARK   3      S21:  -0.2838 S22:   0.2801 S23:   1.2478                       
REMARK   3      S31:   2.0941 S32:  -1.7077 S33:   0.8749                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 51:176)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  44.5936  98.3222 105.2271              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2160 T22:   1.8919                                     
REMARK   3      T33:   0.9738 T12:  -0.2532                                     
REMARK   3      T13:  -0.0903 T23:   0.1500                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0834 L22:   1.2260                                     
REMARK   3      L33:   3.6447 L12:   1.2530                                     
REMARK   3      L13:  -2.6671 L23:  -1.2056                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1508 S12:   1.4928 S13:   0.4696                       
REMARK   3      S21:  -0.2469 S22:   0.3920 S23:   0.4210                       
REMARK   3      S31:   0.3171 S32:  -1.4256 S33:  -0.2834                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 177:353)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  60.7631 100.5633 101.5377              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0083 T22:   1.5999                                     
REMARK   3      T33:   0.7916 T12:  -0.1091                                     
REMARK   3      T13:  -0.0026 T23:   0.1755                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8559 L22:   2.1408                                     
REMARK   3      L33:   4.4439 L12:   0.2564                                     
REMARK   3      L13:   0.2249 L23:  -0.5416                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2309 S12:   1.1665 S13:   0.4322                       
REMARK   3      S21:  -0.4716 S22:   0.2717 S23:   0.0860                       
REMARK   3      S31:   0.0166 S32:  -0.7994 S33:  -0.0269                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 354:440)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  33.4174  84.3047 118.6267              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3582 T22:   1.8400                                     
REMARK   3      T33:   1.0637 T12:  -0.4231                                     
REMARK   3      T13:   0.0435 T23:  -0.0832                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5722 L22:   2.8166                                     
REMARK   3      L33:   6.0355 L12:   0.4082                                     
REMARK   3      L13:  -1.1189 L23:  -0.1842                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5044 S12:   1.1612 S13:  -0.4202                       
REMARK   3      S21:  -0.0557 S22:  -0.1224 S23:   0.1520                       
REMARK   3      S31:   1.1218 S32:  -0.7831 S33:   0.5455                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 441:465)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  20.4284  79.1396 157.2602              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6548 T22:   1.6562                                     
REMARK   3      T33:   1.4067 T12:  -0.2487                                     
REMARK   3      T13:   0.2952 T23:   0.0159                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.7149 L22:   9.7292                                     
REMARK   3      L33:   2.8445 L12:   2.8152                                     
REMARK   3      L13:   3.9134 L23:   4.0014                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7303 S12:   0.0159 S13:  -0.2701                       
REMARK   3      S21:   0.5765 S22:  -0.5336 S23:   0.1315                       
REMARK   3      S31:   2.2165 S32:  -2.1547 S33:   1.2148                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 466:471)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  29.6408  72.5271 159.1869              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3396 T22:   1.6910                                     
REMARK   3      T33:   2.8710 T12:  -0.4590                                     
REMARK   3      T13:   0.0667 T23:   0.5742                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2675 L22:   4.8204                                     
REMARK   3      L33:   4.9444 L12:   0.7616                                     
REMARK   3      L13:   0.3322 L23:  -4.7963                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6614 S12:   0.4854 S13:  -4.2319                       
REMARK   3      S21:   1.3894 S22:   1.4078 S23:   0.8177                       
REMARK   3      S31:   2.6138 S32:  -2.5311 S33:  -1.6809                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 1:15)                               
REMARK   3    ORIGIN FOR THE GROUP (A): 120.8016  82.6384  83.8939              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6152 T22:   1.8781                                     
REMARK   3      T33:   1.6952 T12:   0.2319                                     
REMARK   3      T13:   0.4594 T23:   0.0557                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2672 L22:   5.9726                                     
REMARK   3      L33:   1.4749 L12:  -2.2036                                     
REMARK   3      L13:   2.2381 L23:   0.1046                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1326 S12:   0.8066 S13:  -1.2157                       
REMARK   3      S21:  -0.9698 S22:  -0.6884 S23:   0.3381                       
REMARK   3      S31:   1.4809 S32:   1.5288 S33:   0.8262                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 16:22)                              
REMARK   3    ORIGIN FOR THE GROUP (A): 116.1168  84.8955  78.5010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.5975 T22:   2.8629                                     
REMARK   3      T33:   1.1813 T12:   0.0504                                     
REMARK   3      T13:   0.0740 T23:  -0.1986                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0852 L22:   6.8412                                     
REMARK   3      L33:   0.7910 L12:  -0.2404                                     
REMARK   3      L13:  -0.9049 L23:   1.7602                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0860 S12:   2.7721 S13:   0.4585                       
REMARK   3      S21:  -2.6441 S22:  -0.2754 S23:   0.5720                       
REMARK   3      S31:   0.9742 S32:  -0.2865 S33:   0.4309                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 23:64)                              
REMARK   3    ORIGIN FOR THE GROUP (A): 112.6598  93.0149  87.9964              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3673 T22:   2.2690                                     
REMARK   3      T33:   1.2580 T12:   0.0542                                     
REMARK   3      T13:   0.3738 T23:   0.3036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4748 L22:   2.2410                                     
REMARK   3      L33:   3.2350 L12:  -2.2980                                     
REMARK   3      L13:  -0.7507 L23:   2.2487                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5970 S12:   0.4396 S13:   0.7234                       
REMARK   3      S21:  -1.0441 S22:  -0.5681 S23:  -0.0751                       
REMARK   3      S31:   0.8028 S32:   0.0137 S33:   0.0475                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 65:119)                             
REMARK   3    ORIGIN FOR THE GROUP (A): 115.9600  89.7214  85.7789              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3933 T22:   2.3121                                     
REMARK   3      T33:   1.2743 T12:   0.1601                                     
REMARK   3      T13:   0.4350 T23:   0.1312                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8859 L22:   3.7144                                     
REMARK   3      L33:   4.7928 L12:  -0.5473                                     
REMARK   3      L13:  -1.9271 L23:   0.5348                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1050 S12:   1.2843 S13:   0.0074                       
REMARK   3      S21:  -0.7048 S22:  -0.2955 S23:  -0.2824                       
REMARK   3      S31:   1.0760 S32:   0.1071 S33:   0.1819                       
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 120:170)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 150.0155  82.5792  79.9806              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9573 T22:   3.0458                                     
REMARK   3      T33:   2.0499 T12:   0.4669                                     
REMARK   3      T13:   0.3634 T23:   0.2187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3974 L22:   6.5645                                     
REMARK   3      L33:   2.4874 L12:  -1.6836                                     
REMARK   3      L13:  -1.9600 L23:  -0.0852                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3744 S12:   0.7438 S13:   0.1209                       
REMARK   3      S21:  -0.8466 S22:  -0.0381 S23:  -1.8607                       
REMARK   3      S31:   0.6961 S32:   0.4370 S33:   0.4584                       
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 171:219)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 151.1082  81.2789  79.6530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9781 T22:   3.5632                                     
REMARK   3      T33:   2.0222 T12:   1.0641                                     
REMARK   3      T13:   0.2778 T23:   0.1126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3255 L22:   3.0953                                     
REMARK   3      L33:   3.3141 L12:  -0.4988                                     
REMARK   3      L13:   2.1762 L23:   1.2834                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.5828 S12:   2.3077 S13:   0.3082                       
REMARK   3      S21:   0.1912 S22:  -0.6442 S23:  -0.1447                       
REMARK   3      S31:   0.8339 S32:   1.3631 S33:  -1.0075                       
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 1:11)                               
REMARK   3    ORIGIN FOR THE GROUP (A): 126.9072 107.2520  96.1477              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3162 T22:   1.9273                                     
REMARK   3      T33:   1.9070 T12:  -0.0654                                     
REMARK   3      T13:   0.2994 T23:   0.2375                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2861 L22:   4.9357                                     
REMARK   3      L33:   5.9850 L12:  -1.5067                                     
REMARK   3      L13:   2.5581 L23:  -1.6544                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1850 S12:   0.6104 S13:   1.4654                       
REMARK   3      S21:   0.1934 S22:  -0.8065 S23:  -1.1908                       
REMARK   3      S31:  -0.5962 S32:   1.1430 S33:   0.4904                       
REMARK   3   TLS GROUP : 32                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 12:24)                              
REMARK   3    ORIGIN FOR THE GROUP (A): 133.7464 102.6526 106.7312              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9236 T22:   2.1082                                     
REMARK   3      T33:   2.0024 T12:   0.0056                                     
REMARK   3      T13:  -0.0916 T23:   0.1301                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2952 L22:   2.4198                                     
REMARK   3      L33:   6.3806 L12:  -3.4141                                     
REMARK   3      L13:  -0.1128 L23:  -1.1836                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0487 S12:   0.0558 S13:   2.5665                       
REMARK   3      S21:   0.6852 S22:  -0.0908 S23:  -1.0977                       
REMARK   3      S31:   0.4775 S32:   0.7869 S33:  -0.0174                       
REMARK   3   TLS GROUP : 33                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 25:102)                             
REMARK   3    ORIGIN FOR THE GROUP (A): 122.7921  98.6756 102.4199              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1689 T22:   2.2258                                     
REMARK   3      T33:   1.3891 T12:  -0.0178                                     
REMARK   3      T13:   0.2475 T23:   0.1238                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4945 L22:   3.2705                                     
REMARK   3      L33:   2.2996 L12:  -2.6281                                     
REMARK   3      L13:   0.9684 L23:  -0.0313                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2402 S12:  -0.2512 S13:   0.8494                       
REMARK   3      S21:   0.1413 S22:   0.0056 S23:  -0.8483                       
REMARK   3      S31:   0.2688 S32:   0.8629 S33:   0.2731                       
REMARK   3   TLS GROUP : 34                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 103:118)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 150.7355  97.2598  94.9214              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2406 T22:   3.8343                                     
REMARK   3      T33:   2.1269 T12:   0.3312                                     
REMARK   3      T13:   0.3453 T23:   0.2470                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6706 L22:   0.2208                                     
REMARK   3      L33:   4.0403 L12:   0.8629                                     
REMARK   3      L13:  -4.3035 L23:  -0.8577                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6700 S12:   0.6040 S13:   0.6243                       
REMARK   3      S21:  -0.3938 S22:  -1.0144 S23:  -0.3979                       
REMARK   3      S31:   0.5344 S32:   2.4456 S33:   1.3280                       
REMARK   3   TLS GROUP : 35                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 119:164)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 152.4169  97.7387  78.7008              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0869 T22:   3.1699                                     
REMARK   3      T33:   2.0937 T12:   0.3191                                     
REMARK   3      T13:   0.5672 T23:   0.4210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1604 L22:   4.4030                                     
REMARK   3      L33:   4.0454 L12:   0.0993                                     
REMARK   3      L13:  -0.0305 L23:   0.9013                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2337 S12:   0.9092 S13:   0.2267                       
REMARK   3      S21:  -0.9757 S22:  -0.2152 S23:  -0.4400                       
REMARK   3      S31:  -0.3921 S32:   2.2039 S33:  -0.1325                       
REMARK   3   TLS GROUP : 36                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 165:214)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 156.4609  98.5031  80.1195              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6535 T22:   3.7361                                     
REMARK   3      T33:   2.4767 T12:   0.0617                                     
REMARK   3      T13:   0.6491 T23:   0.4510                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4204 L22:   1.4747                                     
REMARK   3      L33:   4.0118 L12:   1.1836                                     
REMARK   3      L13:  -0.7988 L23:   0.4144                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0682 S12:   1.2088 S13:   0.1010                       
REMARK   3      S21:  -0.8777 S22:   0.3790 S23:  -0.9929                       
REMARK   3      S31:  -0.2820 S32:   0.6132 S33:  -0.3948                       
REMARK   3   TLS GROUP : 37                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 1:31)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  19.3688  89.9102  85.8022              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4628 T22:   1.5409                                     
REMARK   3      T33:   1.1701 T12:  -0.0495                                     
REMARK   3      T13:   0.2039 T23:   0.0194                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8291 L22:   2.5032                                     
REMARK   3      L33:   8.9208 L12:  -3.8024                                     
REMARK   3      L13:  -5.9631 L23:   3.2376                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4446 S12:  -0.9331 S13:  -0.1833                       
REMARK   3      S21:   1.2895 S22:   0.3664 S23:  -0.0540                       
REMARK   3      S31:   1.3435 S32:   0.4170 S33:   0.3546                       
REMARK   3   TLS GROUP : 38                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 32:64)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  18.0113 101.7299  80.0463              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9569 T22:   1.1970                                     
REMARK   3      T33:   1.0959 T12:   0.0381                                     
REMARK   3      T13:   0.1750 T23:  -0.1541                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0281 L22:   4.4218                                     
REMARK   3      L33:   3.8761 L12:   2.9752                                     
REMARK   3      L13:   2.1957 L23:  -0.3024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0723 S12:  -0.7724 S13:   0.7394                       
REMARK   3      S21:   0.2854 S22:   0.1527 S23:   0.4312                       
REMARK   3      S31:  -0.2449 S32:   0.0535 S33:  -0.1308                       
REMARK   3   TLS GROUP : 39                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 65:120)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3618  96.0626  83.3068              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0660 T22:   1.2588                                     
REMARK   3      T33:   1.0051 T12:   0.0308                                     
REMARK   3      T13:   0.2647 T23:  -0.0364                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2424 L22:   2.2074                                     
REMARK   3      L33:   4.5458 L12:  -0.1900                                     
REMARK   3      L13:  -3.8754 L23:  -0.6445                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0592 S12:  -0.9705 S13:   0.1743                       
REMARK   3      S21:   0.9496 S22:   0.0925 S23:   0.4381                       
REMARK   3      S31:  -0.1128 S32:  -0.3056 S33:  -0.1477                       
REMARK   3   TLS GROUP : 40                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 121:151)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -17.4120  83.8975  94.1014              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3207 T22:   1.5113                                     
REMARK   3      T33:   2.2243 T12:   0.0478                                     
REMARK   3      T13:   0.2294 T23:   0.5768                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5587 L22:   4.0977                                     
REMARK   3      L33:   5.2709 L12:   1.6477                                     
REMARK   3      L13:   2.9376 L23:   2.8495                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0462 S12:  -1.1426 S13:  -1.7729                       
REMARK   3      S21:   0.7474 S22:   0.0721 S23:   0.6813                       
REMARK   3      S31:   0.8805 S32:  -0.0098 S33:  -0.0026                       
REMARK   3   TLS GROUP : 41                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 152:179)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.6880  82.7066  89.8095              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0031 T22:   1.6352                                     
REMARK   3      T33:   2.5531 T12:   0.2450                                     
REMARK   3      T13:   0.3024 T23:   0.2261                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3709 L22:   6.4741                                     
REMARK   3      L33:   4.8653 L12:   7.5564                                     
REMARK   3      L13:   3.9604 L23:   2.0203                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2169 S12:  -0.1389 S13:  -2.8408                       
REMARK   3      S21:   0.1283 S22:   0.3952 S23:  -0.6430                       
REMARK   3      S31:   0.7110 S32:   0.6057 S33:  -0.2762                       
REMARK   3   TLS GROUP : 42                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 180:219)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -16.0378  77.6315  93.5091              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4433 T22:   1.4992                                     
REMARK   3      T33:   2.9166 T12:  -0.0060                                     
REMARK   3      T13:   0.1880 T23:   0.6250                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2875 L22:   0.9668                                     
REMARK   3      L33:   6.6502 L12:   2.0889                                     
REMARK   3      L13:   2.0418 L23:   1.7950                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2950 S12:  -0.2148 S13:  -2.4112                       
REMARK   3      S21:   0.2924 S22:  -0.0714 S23:   0.0021                       
REMARK   3      S31:   1.4916 S32:  -0.3743 S33:  -0.2382                       
REMARK   3   TLS GROUP : 43                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 1:27)                               
REMARK   3    ORIGIN FOR THE GROUP (A):   2.0820 100.2039  63.2242              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9134 T22:   1.6300                                     
REMARK   3      T33:   1.6731 T12:   0.0640                                     
REMARK   3      T13:   0.1719 T23:  -0.2562                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2996 L22:   6.8336                                     
REMARK   3      L33:   1.0255 L12:   2.8495                                     
REMARK   3      L13:   0.6856 L23:   0.6106                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0702 S12:   0.8001 S13:   1.2414                       
REMARK   3      S21:   0.0106 S22:  -0.1955 S23:   1.9892                       
REMARK   3      S31:   0.0104 S32:  -0.7644 S33:   0.1539                       
REMARK   3   TLS GROUP : 44                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 28:71)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  12.0009  94.0769  63.2313              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8388 T22:   1.2758                                     
REMARK   3      T33:   1.1489 T12:  -0.0750                                     
REMARK   3      T13:   0.0927 T23:  -0.1747                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4983 L22:   3.9054                                     
REMARK   3      L33:   3.5344 L12:   0.5199                                     
REMARK   3      L13:  -0.6845 L23:   0.1856                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0859 S12:   0.4685 S13:  -0.6128                       
REMARK   3      S21:  -0.0873 S22:  -0.1130 S23:   0.7599                       
REMARK   3      S31:   0.2321 S32:  -0.9072 S33:   0.2566                       
REMARK   3   TLS GROUP : 45                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 72:106)                             
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0155  95.1871  66.5149              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8320 T22:   1.4781                                     
REMARK   3      T33:   1.3497 T12:  -0.0241                                     
REMARK   3      T13:   0.1617 T23:  -0.1421                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6096 L22:   5.2362                                     
REMARK   3      L33:   3.6421 L12:   2.4500                                     
REMARK   3      L13:   1.3317 L23:   1.3829                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0615 S12:   0.1952 S13:  -0.2786                       
REMARK   3      S21:   0.1393 S22:  -0.2504 S23:   1.1521                       
REMARK   3      S31:   0.3000 S32:  -1.1886 S33:   0.3567                       
REMARK   3   TLS GROUP : 46                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 107:145)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -20.1456  89.2818  83.8499              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9687 T22:   1.5037                                     
REMARK   3      T33:   2.0041 T12:  -0.0054                                     
REMARK   3      T13:   0.2359 T23:   0.1376                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4889 L22:   1.7597                                     
REMARK   3      L33:   4.8353 L12:  -0.1169                                     
REMARK   3      L13:   1.0503 L23:   1.7889                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3971 S12:  -0.0870 S13:  -1.5310                       
REMARK   3      S21:   0.2698 S22:   0.0549 S23:   0.4103                       
REMARK   3      S31:   0.6123 S32:   0.1935 S33:   0.4482                       
REMARK   3   TLS GROUP : 47                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 146:182)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -17.7713  94.4507  84.3208              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8631 T22:   1.3749                                     
REMARK   3      T33:   1.7642 T12:  -0.0976                                     
REMARK   3      T13:   0.1888 T23:   0.3808                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6583 L22:   1.6606                                     
REMARK   3      L33:   4.4468 L12:  -1.7693                                     
REMARK   3      L13:  -0.1548 L23:   0.7830                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1295 S12:  -1.1536 S13:  -1.7664                       
REMARK   3      S21:  -0.3665 S22:   0.4682 S23:   0.1912                       
REMARK   3      S31:  -0.4910 S32:   0.5233 S33:  -0.2015                       
REMARK   3   TLS GROUP : 48                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 183:214)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -29.0762  95.2805  88.9322              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0085 T22:   1.6955                                     
REMARK   3      T33:   1.8995 T12:   0.0965                                     
REMARK   3      T13:   0.3381 T23:   0.1862                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8216 L22:   3.1605                                     
REMARK   3      L33:   6.0317 L12:   0.9378                                     
REMARK   3      L13:  -0.5808 L23:   2.1835                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0080 S12:  -0.4472 S13:  -0.9429                       
REMARK   3      S21:   0.5693 S22:  -0.3513 S23:   0.8483                       
REMARK   3      S31:   0.1995 S32:  -1.5976 S33:   0.4070                       
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 4Z7O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000208768.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 92354                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
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     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 2.6800                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 8000, 0.2 M AMMONIUM SULFATE,    
REMARK 280  0.1 M TRIS-HCL, PH 8.9, VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000      129.95900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.26200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      129.95900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.26200            
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L, G                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F, I                         
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     LEU B   467                                                      
REMARK 465     GLY B   468                                                      
REMARK 465     SER B   469                                                      
REMARK 465     GLN B   470                                                      
REMARK 465     CYS B   471                                                      
REMARK 465     VAL C   454                                                      
REMARK 465     LYS C   455                                                      
REMARK 465     GLY E   135                                                      
REMARK 465     ASP E   136                                                      
REMARK 465     THR E   137                                                      
REMARK 465     GLY E   220                                                      
REMARK 465     PRO E   221                                                      
REMARK 465     GLY H   135                                                      
REMARK 465     ASP H   136                                                      
REMARK 465     THR H   137                                                      
REMARK 465     GLY H   220                                                      
REMARK 465     PRO H   221                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU B 128    CG   CD1  CD2                                       
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   HG   CYS H   134     SG   CYS L   214              1.40            
REMARK 500   HG   SER B   130     O    ASP B   336              1.53            
REMARK 500   O    HOH A   748     O    HOH A   829              1.92            
REMARK 500   O    HOH A   767     O    HOH A   849              1.96            
REMARK 500   O    HOH A   693     O    HOH A   749              2.02            
REMARK 500   O    HOH A   805     O    HOH B  2182              2.02            
REMARK 500   O    HOH L   401     O    HOH L   410              2.02            
REMARK 500   O    HOH A   838     O    HOH A   852              2.04            
REMARK 500   O    HOH A   702     O    HOH A   809              2.05            
REMARK 500   OD1  ASP A   245     OE1  GLU A   252              2.06            
REMARK 500   O    HOH A   749     O    HOH A   864              2.06            
REMARK 500   O    HOH A   674     O    HOH A   829              2.07            
REMARK 500   O    HOH A   819     O    HOH B  2156              2.07            
REMARK 500   O    HOH B  2117     O    HOH B  2130              2.07            
REMARK 500   O    HOH A   677     O    HOH A   730              2.10            
REMARK 500   OE2  GLU C   243     O    ASP C   247              2.12            
REMARK 500   OE1  GLN A   351     O    HOH A   601              2.13            
REMARK 500   O    HOH A   669     O    HOH A   733              2.14            
REMARK 500   O    HOH A   812     O    HOH A   841              2.14            
REMARK 500   O    HOH C   669     O    HOH C   681              2.14            
REMARK 500   OD1  ASN L   157     O    HOH L   401              2.14            
REMARK 500   O    HOH A   776     O    HOH A   863              2.15            
REMARK 500   OD1  ASN A    15     O    HOH A   602              2.15            
REMARK 500   O    HOH C   637     O    HOH C   651              2.15            
REMARK 500   O    HOH B  2125     O    HOH B  2138              2.16            
REMARK 500   ND2  ASN B    99     O5   NAG B  2004              2.16            
REMARK 500   O    HOH B  2169     O    HOH B  2181              2.17            
REMARK 500   O    HOH A   693     O    HOH A   864              2.17            
REMARK 500   O    HOH A   744     O    HOH A   796              2.18            
REMARK 500   O    HOH B  2180     O    HOH B  2202              2.18            
REMARK 500   OE1  GLU A   142     O    HOH A   603              2.18            
REMARK 500   O    HOH A   725     O    HOH A   859              2.18            
REMARK 500   OE2  GLU A   243     OD1  ASP A   245              2.18            
REMARK 500   O2   SO4 A   501     O    HOH A   604              2.19            
REMARK 500   OD2  ASP C   428     O    HOH C   601              2.19            
REMARK 500   O    HOH A   661     O    HOH A   763              2.19            
REMARK 500   O    HOH A   683     O    HOH B  2211              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   833     O    HOH C   650     1554     2.14            
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    ASN A   2       43.48   -108.62                                   
REMARK 500    SER A 101     -133.93     56.15                                   
REMARK 500    LYS A 118     -113.95     64.65                                   
REMARK 500    GLU A 123      138.65     75.42                                   
REMARK 500    ALA A 198      135.90   -174.86                                   
REMARK 500    LEU A 212      -49.12     71.35                                   
REMARK 500    SER A 220      105.16   -163.75                                   
REMARK 500    GLN A 388      141.86   -175.56                                   
REMARK 500    ARG A 422      131.01   -172.34                                   
REMARK 500    ILE B   4      -30.68   -139.64                                   
REMARK 500    PRO B  32      176.45    -56.69                                   
REMARK 500    ALA B  61       76.76   -166.16                                   
REMARK 500    ASP B  76      166.35     65.15                                   
REMARK 500    GLN B  79       36.30    -89.39                                   
REMARK 500    ILE B 131       35.66    -93.81                                   
REMARK 500    LEU B 138      -78.97    -69.81                                   
REMARK 500    ALA B 139      -34.29    -35.55                                   
REMARK 500    VAL B 157      -88.30   -133.76                                   
REMARK 500    PRO B 160       73.81    -65.80                                   
REMARK 500    THR B 182     -166.33   -114.50                                   
REMARK 500    SER B 213     -161.64   -117.04                                   
REMARK 500    ASP B 241       77.88   -117.31                                   
REMARK 500    LEU B 258       -2.41     71.85                                   
REMARK 500    SER B 334       67.27    -68.89                                   
REMARK 500    MET B 335      -65.48     66.92                                   
REMARK 500    LEU B 375     -129.19     58.77                                   
REMARK 500    ASN B 450       67.09     60.07                                   
REMARK 500    VAL C   6      -60.18    -99.52                                   
REMARK 500    SER C  81       16.87     58.80                                   
REMARK 500    SER C 101     -130.57     54.82                                   
REMARK 500    LYS C 118     -105.32     58.92                                   
REMARK 500    GLU C 123      143.35     73.29                                   
REMARK 500    TYR C 143      107.10   -164.50                                   
REMARK 500    ALA C 198      128.18   -174.08                                   
REMARK 500    LEU C 212      -32.81     72.90                                   
REMARK 500    TRP C 262       71.17     58.58                                   
REMARK 500    PHE C 289      108.03    -51.24                                   
REMARK 500    VAL C 325      -30.55   -131.21                                   
REMARK 500    PRO C 412     -175.34    -68.14                                   
REMARK 500    ARG C 422      137.60   -170.64                                   
REMARK 500    ALA C 439       73.89   -153.69                                   
REMARK 500    THR D   7       35.88    -85.96                                   
REMARK 500    PHE D  56       79.83   -153.79                                   
REMARK 500    LEU D  64      -76.14   -105.41                                   
REMARK 500    ASP D  66       79.61   -150.45                                   
REMARK 500    VAL D 157      -79.86   -131.89                                   
REMARK 500    PRO D 160       71.18    -68.68                                   
REMARK 500    CYS D 177       42.23    -90.69                                   
REMARK 500    LYS D 181       39.70    -93.64                                   
REMARK 500    TYR D 190      130.69   -170.34                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      85 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 243   OE1                                                    
REMARK 620 2 GLU A 243   OE2  55.8                                              
REMARK 620 3 ASP A 245   OD1 110.8  56.2                                        
REMARK 620 4 ASP A 247   O    77.5  66.4  87.2                                  
REMARK 620 5 THR A 250   O    73.8 128.0 175.4  93.1                            
REMARK 620 6 THR A 250   OG1 147.0 133.1  91.9  80.1  83.6                      
REMARK 620 7 GLU A 252   OE1  95.9  72.8  52.6 134.4 128.8 117.0                
REMARK 620 8 GLU A 252   OE2 122.8 128.0  90.1 158.8  88.0  79.0  55.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 297   OD1                                                    
REMARK 620 2 ASN A 299   OD1  75.6                                              
REMARK 620 3 ASP A 301   OD1  69.1  70.8                                        
REMARK 620 4 ARG A 303   O    74.6 149.8  93.7                                  
REMARK 620 5 ASP A 305   OD1 141.2 101.2 147.4 105.1                            
REMARK 620 6 ASP A 305   OD2  85.7  86.6 149.3  96.2  55.6                      
REMARK 620 7 HOH A 611   O   140.6  75.8  76.2 126.8  71.2 118.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 365   OD1                                                    
REMARK 620 2 ASP A 367   OD1  92.9                                              
REMARK 620 3 ASP A 369   OD1  77.1  76.5                                        
REMARK 620 4 TYR A 371   O    67.1 157.8  89.0                                  
REMARK 620 5 ASP A 373   OD1 143.4 107.0 136.7  95.1                            
REMARK 620 6 ASP A 373   OD2  92.6  98.1 167.9  92.7  55.1                      
REMARK 620 7 HOH A 656   O   143.0  91.4  68.3  98.8  68.4 123.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 505  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 426   OD1                                                    
REMARK 620 2 ASP A 428   OD1  71.4                                              
REMARK 620 3 ASN A 430   OD1  83.4  70.2                                        
REMARK 620 4 TYR A 432   O    78.4 148.1  96.6                                  
REMARK 620 5 ASP A 434   OD1 142.5 122.2 133.4  88.3                            
REMARK 620 6 ASP A 434   OD2  92.3  86.4 156.4 105.3  57.4                      
REMARK 620 7 HOH A 619   O   142.5  82.9  62.1 117.3  74.5 113.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B2001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 121   OG                                                     
REMARK 620 2 SER B 123   OG   82.5                                              
REMARK 620 3 GLU B 220   OE2  79.7 161.8                                        
REMARK 620 4 ASP G 410   OD1  84.2  91.0  84.0                                  
REMARK 620 5 HOH B2108   O   165.8 111.7  86.1  93.9                            
REMARK 620 6 HOH B2116   O    73.3  77.3 100.5 155.7 110.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B2002  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 123   O                                                      
REMARK 620 2 ASP B 251   OD2  75.7                                              
REMARK 620 3 HOH B2172   O    91.5  98.4                                        
REMARK 620 4 HOH B2129   O   131.3 104.4 135.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B2003  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 158   OD2                                                    
REMARK 620 2 ASN B 215   OD1 104.4                                              
REMARK 620 3 ASP B 217   O   158.5  86.1                                        
REMARK 620 4 ASP B 217   OD1  94.2  89.4  66.9                                  
REMARK 620 5 PRO B 219   O    89.6 159.1  86.2 105.3                            
REMARK 620 6 GLU B 220   OE1  96.5  82.6 103.5 168.0  80.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 243   OE1                                                    
REMARK 620 2 GLU C 243   OE2  55.5                                              
REMARK 620 3 ASP C 245   OD1 109.4  58.9                                        
REMARK 620 4 ASP C 247   O    80.2  53.2  80.9                                  
REMARK 620 5 THR C 250   O    70.9 116.3 169.2  88.6                            
REMARK 620 6 THR C 250   OG1 148.8 123.3  89.2  78.3  86.1                      
REMARK 620 7 GLU C 252   OE1  86.2  82.0  61.6 132.8 128.8 125.1                
REMARK 620 8 GLU C 252   OE2 128.1 133.6  83.3 151.1 105.2  77.5  55.2          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 297   OD1                                                    
REMARK 620 2 ASN C 299   OD1  70.4                                              
REMARK 620 3 ASP C 301   OD1  60.8  62.6                                        
REMARK 620 4 ARG C 303   O    74.3 144.3  95.8                                  
REMARK 620 5 ASP C 305   OD1 141.2 110.3 156.0 100.2                            
REMARK 620 6 ASP C 305   OD2  86.2  86.0 139.7  96.6  55.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 505  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 365   OD1                                                    
REMARK 620 2 ASP C 367   OD1  89.9                                              
REMARK 620 3 ASP C 369   OD1  62.8  72.5                                        
REMARK 620 4 TYR C 371   O    63.5 152.4  87.7                                  
REMARK 620 5 ASP C 373   OD1 138.8 123.3 144.5  84.0                            
REMARK 620 6 ASP C 373   OD2 109.3  88.5 159.0 106.6  54.6                      
REMARK 620 7 HOH C 608   O   132.2  94.6  73.3  98.0  73.8 118.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 506  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 426   OD1                                                    
REMARK 620 2 ASP C 428   OD1  62.8                                              
REMARK 620 3 ASN C 430   OD1  76.3  81.9                                        
REMARK 620 4 TYR C 432   O    80.5 143.2  90.0                                  
REMARK 620 5 ASP C 434   OD1 142.2 114.6 141.3  94.0                            
REMARK 620 6 ASP C 434   OD2  91.7  71.0 152.9 112.2  55.7                      
REMARK 620 7 HOH C 601   O   132.6  71.1  87.7 144.7  67.5  82.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D2001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER D 121   OG                                                     
REMARK 620 2 SER D 123   OG   91.1                                              
REMARK 620 3 GLU D 220   OE2  90.8 170.4                                        
REMARK 620 4 ASP I 410   OD2  91.3  96.3  93.0                                  
REMARK 620 5 HOH D2115   O    85.7  80.9  89.8 175.9                            
REMARK 620 6 HOH D2130   O   173.4  90.6  86.6  94.9  88.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D2002  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER D 123   O                                                      
REMARK 620 2 ASP D 251   OD2  94.3                                              
REMARK 620 3 HOH D2101   O   116.3 109.4                                        
REMARK 620 4 HOH D2145   O   170.5  90.7  69.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D2003  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 158   OD2                                                    
REMARK 620 2 ASN D 215   OD1  99.2                                              
REMARK 620 3 ASP D 217   O   162.0  86.1                                        
REMARK 620 4 ASP D 217   OD1  88.0  75.7  76.5                                  
REMARK 620 5 PRO D 219   O    86.1 171.7  90.9 111.1                            
REMARK 620 6 GLU D 220   OE1  92.2 109.9 102.3 174.2  63.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN D 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN D 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN D 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 2004        
REMARK 800  bound to ASN B 99                                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  2005 through MAN B 2009 bound to ASN B 320                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  2010 through NAG B 2011 bound to ASN B 371                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 2004        
REMARK 800  bound to ASN D 99                                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D    
REMARK 800  2005 through MAN D 2008 bound to ASN D 320                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D    
REMARK 800  2009 through NAG D 2010 bound to ASN D 371                          
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4Z7N   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Z7Q   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Z7S   RELATED DB: PDB                                   
DBREF  4Z7O A    1   455  UNP    P08514   ITA2B_HUMAN     32    486             
DBREF  4Z7O B    3   471  UNP    P05106   ITB3_HUMAN      29    497             
DBREF  4Z7O C    1   455  UNP    P08514   ITA2B_HUMAN     32    486             
DBREF  4Z7O D    3   471  UNP    P05106   ITB3_HUMAN      29    497             
DBREF  4Z7O E    1   221  PDB    4Z7O     4Z7O             1    221             
DBREF  4Z7O F    1   214  PDB    4Z7O     4Z7O             1    214             
DBREF  4Z7O H    1   221  PDB    4Z7O     4Z7O             1    221             
DBREF  4Z7O L    1   214  PDB    4Z7O     4Z7O             1    214             
DBREF  4Z7O G  408   411  PDB    4Z7O     4Z7O           408    411             
DBREF  4Z7O I  408   411  PDB    4Z7O     4Z7O           408    411             
SEQRES   1 A  455  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 A  455  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 A  455  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 A  455  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 A  455  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 A  455  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 A  455  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 A  455  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 A  455  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 A  455  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 A  455  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 A  455  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 A  455  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 A  455  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 A  455  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 A  455  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 A  455  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 A  455  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 A  455  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 A  455  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 A  455  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 A  455  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 A  455  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 A  455  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 A  455  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 A  455  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 A  455  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 A  455  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 A  455  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 A  455  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 A  455  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 A  455  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 A  455  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 A  455  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 A  455  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES   1 B  469  ASN ILE CYS THR THR ARG GLY VAL SER SER CYS GLN GLN          
SEQRES   2 B  469  CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS SER ASP          
SEQRES   3 B  469  GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP LEU LYS          
SEQRES   4 B  469  GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU SER ILE          
SEQRES   5 B  469  GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU ASP ARG          
SEQRES   6 B  469  PRO LEU SER ASP LYS GLY SER GLY ASP SER SER GLN VAL          
SEQRES   7 B  469  THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG LEU ARG          
SEQRES   8 B  469  PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL ARG GLN          
SEQRES   9 B  469  VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU MET ASP          
SEQRES  10 B  469  LEU SER TYR SER MET LYS ASP ASP LEU TRP SER ILE GLN          
SEQRES  11 B  469  ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG LYS LEU          
SEQRES  12 B  469  THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE VAL ASP          
SEQRES  13 B  469  LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO PRO GLU          
SEQRES  14 B  469  ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR THR CYS          
SEQRES  15 B  469  LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR LEU THR          
SEQRES  16 B  469  ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS LYS GLN          
SEQRES  17 B  469  SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY GLY PHE          
SEQRES  18 B  469  ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU LYS ILE          
SEQRES  19 B  469  GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL PHE THR          
SEQRES  20 B  469  THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY ARG LEU          
SEQRES  21 B  469  ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS HIS VAL          
SEQRES  22 B  469  GLY SER ASP ASN HIS TYR SER ALA SER THR THR MET ASP          
SEQRES  23 B  469  TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU SER GLN          
SEQRES  24 B  469  LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU ASN VAL          
SEQRES  25 B  469  VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE PRO GLY          
SEQRES  26 B  469  THR THR VAL GLY VAL LEU SER MET ASP SER SER ASN VAL          
SEQRES  27 B  469  LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE ARG SER          
SEQRES  28 B  469  LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU GLU LEU          
SEQRES  29 B  469  SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN GLU VAL          
SEQRES  30 B  469  ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS ILE GLY          
SEQRES  31 B  469  ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL ARG GLY          
SEQRES  32 B  469  CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE LYS PRO          
SEQRES  33 B  469  VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL THR PHE          
SEQRES  34 B  469  ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU PRO ASN          
SEQRES  35 B  469  SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE GLU CYS          
SEQRES  36 B  469  GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY SER GLN          
SEQRES  37 B  469  CYS                                                          
SEQRES   1 C  455  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 C  455  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 C  455  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 C  455  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 C  455  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 C  455  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 C  455  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 C  455  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 C  455  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 C  455  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 C  455  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 C  455  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 C  455  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 C  455  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 C  455  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 C  455  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 C  455  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 C  455  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 C  455  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 C  455  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 C  455  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 C  455  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 C  455  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 C  455  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 C  455  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 C  455  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 C  455  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 C  455  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 C  455  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 C  455  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 C  455  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 C  455  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 C  455  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 C  455  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 C  455  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES   1 D  469  ASN ILE CYS THR THR ARG GLY VAL SER SER CYS GLN GLN          
SEQRES   2 D  469  CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS SER ASP          
SEQRES   3 D  469  GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP LEU LYS          
SEQRES   4 D  469  GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU SER ILE          
SEQRES   5 D  469  GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU ASP ARG          
SEQRES   6 D  469  PRO LEU SER ASP LYS GLY SER GLY ASP SER SER GLN VAL          
SEQRES   7 D  469  THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG LEU ARG          
SEQRES   8 D  469  PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL ARG GLN          
SEQRES   9 D  469  VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU MET ASP          
SEQRES  10 D  469  LEU SER TYR SER MET LYS ASP ASP LEU TRP SER ILE GLN          
SEQRES  11 D  469  ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG LYS LEU          
SEQRES  12 D  469  THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE VAL ASP          
SEQRES  13 D  469  LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO PRO GLU          
SEQRES  14 D  469  ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR THR CYS          
SEQRES  15 D  469  LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR LEU THR          
SEQRES  16 D  469  ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS LYS GLN          
SEQRES  17 D  469  SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY GLY PHE          
SEQRES  18 D  469  ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU LYS ILE          
SEQRES  19 D  469  GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL PHE THR          
SEQRES  20 D  469  THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY ARG LEU          
SEQRES  21 D  469  ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS HIS VAL          
SEQRES  22 D  469  GLY SER ASP ASN HIS TYR SER ALA SER THR THR MET ASP          
SEQRES  23 D  469  TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU SER GLN          
SEQRES  24 D  469  LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU ASN VAL          
SEQRES  25 D  469  VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE PRO GLY          
SEQRES  26 D  469  THR THR VAL GLY VAL LEU SER MET ASP SER SER ASN VAL          
SEQRES  27 D  469  LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE ARG SER          
SEQRES  28 D  469  LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU GLU LEU          
SEQRES  29 D  469  SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN GLU VAL          
SEQRES  30 D  469  ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS ILE GLY          
SEQRES  31 D  469  ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL ARG GLY          
SEQRES  32 D  469  CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE LYS PRO          
SEQRES  33 D  469  VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL THR PHE          
SEQRES  34 D  469  ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU PRO ASN          
SEQRES  35 D  469  SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE GLU CYS          
SEQRES  36 D  469  GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY SER GLN          
SEQRES  37 D  469  CYS                                                          
SEQRES   1 E  221  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 E  221  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 E  221  PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN          
SEQRES   4 E  221  ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 E  221  PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 E  221  GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 E  221  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 E  221  ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR          
SEQRES   9 E  221  ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL          
SEQRES  10 E  221  SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU          
SEQRES  11 E  221  ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR          
SEQRES  12 E  221  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 E  221  THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 E  221  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 E  221  LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO          
SEQRES  16 E  221  SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 E  221  SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO          
SEQRES   1 F  214  ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL          
SEQRES   2 F  214  SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER          
SEQRES   3 F  214  GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS          
SEQRES   4 F  214  PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR          
SEQRES   5 F  214  ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 F  214  GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU          
SEQRES   7 F  214  ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR          
SEQRES   8 F  214  ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 F  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 F  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 F  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 F  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 F  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 F  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 F  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 F  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 F  214  PHE ASN ARG ASN GLU CYS                                      
SEQRES   1 H  221  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 H  221  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 H  221  PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN          
SEQRES   4 H  221  ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 H  221  PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 H  221  GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 H  221  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 H  221  ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR          
SEQRES   9 H  221  ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL          
SEQRES  10 H  221  SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU          
SEQRES  11 H  221  ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR          
SEQRES  12 H  221  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 H  221  THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 H  221  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 H  221  LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO          
SEQRES  16 H  221  SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 H  221  SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO          
SEQRES   1 L  214  ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL          
SEQRES   2 L  214  SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER          
SEQRES   3 L  214  GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS          
SEQRES   4 L  214  PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR          
SEQRES   5 L  214  ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU          
SEQRES   7 L  214  ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR          
SEQRES   8 L  214  ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 L  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 L  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 L  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 L  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 L  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 L  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 L  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 L  214  PHE ASN ARG ASN GLU CYS                                      
SEQRES   1 G    4  ALA GLY ASP VAL                                              
SEQRES   1 I    4  ALA GLY ASP VAL                                              
HET    SO4  A 501       5                                                       
HET     CA  A 502       1                                                       
HET     CA  A 503       1                                                       
HET     CA  A 504       1                                                       
HET     CA  A 505       1                                                       
HET     MN  B2001       1                                                       
HET     MN  B2002       1                                                       
HET     MN  B2003       1                                                       
HET    NAG  B2004      28                                                       
HET    NAG  B2005      27                                                       
HET    NAG  B2006      27                                                       
HET    BMA  B2007      20                                                       
HET    MAN  B2008      22                                                       
HET    MAN  B2009      22                                                       
HET    NAG  B2010      27                                                       
HET    NAG  B2011      28                                                       
HET    SO4  C 501       5                                                       
HET     CL  C 502       1                                                       
HET     CA  C 503       1                                                       
HET     CA  C 504       1                                                       
HET     CA  C 505       1                                                       
HET     CA  C 506       1                                                       
HET     MN  D2001       1                                                       
HET     MN  D2002       1                                                       
HET     MN  D2003       1                                                       
HET    NAG  D2004      28                                                       
HET    NAG  D2005      27                                                       
HET    NAG  D2006      27                                                       
HET    BMA  D2007      21                                                       
HET    MAN  D2008      22                                                       
HET    NAG  D2009      27                                                       
HET    NAG  D2010      28                                                       
HET    SO4  L 301       5                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      CL CHLORIDE ION                                                     
FORMUL  11  SO4    3(O4 S 2-)                                                   
FORMUL  12   CA    8(CA 2+)                                                     
FORMUL  16   MN    6(MN 2+)                                                     
FORMUL  19  NAG    10(C8 H15 N O6)                                              
FORMUL  20  BMA    2(C6 H12 O6)                                                 
FORMUL  20  MAN    3(C6 H12 O6)                                                 
FORMUL  23   CL    CL 1-                                                        
FORMUL  35  HOH   *584(H2 O)                                                    
HELIX    1 AA1 LEU A  151  ASN A  158  1                                   8    
HELIX    2 AA2 GLY A  187  LEU A  192  1                                   6    
HELIX    3 AA3 VAL A  200  SER A  206  1                                   7    
HELIX    4 AA4 ASN A  227  PHE A  231  5                                   5    
HELIX    5 AA5 THR A  259  LEU A  264  1                                   6    
HELIX    6 AA6 SER B   12  SER B   20  1                                   9    
HELIX    7 AA7 LEU B   40  LYS B   46  1                                   7    
HELIX    8 AA8 ALA B   50  GLU B   52  5                                   3    
HELIX    9 AA9 SER B  121  LYS B  125  5                                   5    
HELIX   10 AB1 ASP B  126  ILE B  131  1                                   6    
HELIX   11 AB2 ASN B  133  ARG B  143  1                                  11    
HELIX   12 AB3 PRO B  170  ASN B  175  1                                   6    
HELIX   13 AB4 VAL B  200  LYS B  208  1                                   9    
HELIX   14 AB5 GLY B  221  CYS B  232  1                                  12    
HELIX   15 AB6 CYS B  232  GLY B  237  1                                   6    
HELIX   16 AB7 LEU B  258  GLY B  264  5                                   7    
HELIX   17 AB8 SER B  291  LYS B  302  1                                  12    
HELIX   18 AB9 VAL B  314  SER B  322  1                                   9    
HELIX   19 AC1 ASN B  339  ARG B  352  1                                  14    
HELIX   20 AC2 CYS B  435  ALA B  441  5                                   7    
HELIX   21 AC3 LEU C  151  ASN C  158  1                                   8    
HELIX   22 AC4 GLY C  187  LEU C  192  1                                   6    
HELIX   23 AC5 VAL C  200  SER C  206  1                                   7    
HELIX   24 AC6 THR C  259  LEU C  264  1                                   6    
HELIX   25 AC7 CYS D    5  GLY D    9  5                                   5    
HELIX   26 AC8 SER D   12  ALA D   18  1                                   7    
HELIX   27 AC9 LEU D   40  ASP D   47  1                                   8    
HELIX   28 AD1 ALA D   50  GLU D   52  5                                   3    
HELIX   29 AD2 ASP D   76  VAL D   80  5                                   5    
HELIX   30 AD3 SER D  121  LYS D  125  5                                   5    
HELIX   31 AD4 ASP D  126  ILE D  131  1                                   6    
HELIX   32 AD5 ASN D  133  LYS D  144  1                                  12    
HELIX   33 AD6 PRO D  169  ASN D  175  1                                   7    
HELIX   34 AD7 GLN D  199  LYS D  208  1                                  10    
HELIX   35 AD8 GLY D  222  CYS D  232  1                                  11    
HELIX   36 AD9 CYS D  232  GLY D  237  1                                   6    
HELIX   37 AE1 ASP D  259  GLY D  264  5                                   6    
HELIX   38 AE2 TYR D  281  THR D  285  5                                   5    
HELIX   39 AE3 SER D  291  ASN D  303  1                                  13    
HELIX   40 AE4 VAL D  314  ILE D  325  1                                  12    
HELIX   41 AE5 ASN D  339  ARG D  352  1                                  14    
HELIX   42 AE6 CYS D  435  ALA D  441  5                                   7    
HELIX   43 AE7 ASN E   28  THR E   32  5                                   5    
HELIX   44 AE8 PRO E   62  GLN E   65  5                                   4    
HELIX   45 AE9 SER E  162  SER E  164  5                                   3    
HELIX   46 AF1 SER F  121  THR F  126  1                                   6    
HELIX   47 AF2 LYS F  183  GLU F  187  1                                   5    
HELIX   48 AF3 ASN H   28  THR H   32  5                                   5    
HELIX   49 AF4 ASP L   79  PHE L   83  5                                   5    
HELIX   50 AF5 SER L  121  THR L  126  1                                   6    
HELIX   51 AF6 LYS L  183  ARG L  188  1                                   6    
SHEET    1 AA1 5 GLY A  63  GLN A  64  0                                        
SHEET    2 AA1 5 THR A   9  ALA A  12  1  N  PHE A  10   O  GLY A  63           
SHEET    3 AA1 5 GLN A 444  TYR A 448 -1  O  VAL A 447   N  THR A   9           
SHEET    4 AA1 5 ASP A 434  ALA A 439 -1  N  LEU A 435   O  TYR A 448           
SHEET    5 AA1 5 SER A 420  VAL A 425 -1  N  VAL A 425   O  ASP A 434           
SHEET    1 AA2 4 LEU A  23  LYS A  27  0                                        
SHEET    2 AA2 4 VAL A  33  ALA A  39 -1  O  ALA A  34   N  HIS A  26           
SHEET    3 AA2 4 GLY A  52  PRO A  57 -1  O  GLY A  52   N  ALA A  39           
SHEET    4 AA2 4 SER A  67  LEU A  68 -1  O  LEU A  68   N  VAL A  53           
SHEET    1 AA3 4 GLU A  75  VAL A  79  0                                        
SHEET    2 AA3 4 GLN A  82  PHE A  87 -1  O  LEU A  84   N  ARG A  77           
SHEET    3 AA3 4 HIS A 112  GLU A 117 -1  O  LEU A 116   N  THR A  83           
SHEET    4 AA3 4 GLU A 120  GLU A 121 -1  O  GLU A 120   N  GLU A 117           
SHEET    1 AA4 4 GLU A  75  VAL A  79  0                                        
SHEET    2 AA4 4 GLN A  82  PHE A  87 -1  O  LEU A  84   N  ARG A  77           
SHEET    3 AA4 4 HIS A 112  GLU A 117 -1  O  LEU A 116   N  THR A  83           
SHEET    4 AA4 4 THR A 125  PRO A 126 -1  O  THR A 125   N  TRP A 113           
SHEET    1 AA5 4 VAL A  97  TRP A 100  0                                        
SHEET    2 AA5 4 VAL A 103  ALA A 108 -1  O  VAL A 105   N  VAL A  98           
SHEET    3 AA5 4 SER A 129  ALA A 133 -1  O  PHE A 131   N  ALA A 106           
SHEET    4 AA5 4 ARG A 140  TYR A 143 -1  O  ALA A 141   N  LEU A 132           
SHEET    1 AA6 4 SER A 173  VAL A 175  0                                        
SHEET    2 AA6 4 GLU A 180  ALA A 185 -1  O  VAL A 182   N  VAL A 174           
SHEET    3 AA6 4 LEU A 194  PRO A 199 -1  O  ALA A 196   N  LEU A 183           
SHEET    4 AA6 4 SER A 220  LEU A 221 -1  O  SER A 220   N  GLN A 197           
SHEET    1 AA7 4 VAL A 239  GLY A 242  0                                        
SHEET    2 AA7 4 GLU A 252  ALA A 257 -1  O  VAL A 254   N  ALA A 240           
SHEET    3 AA7 4 ALA A 266  LEU A 270 -1  O  ALA A 266   N  ALA A 257           
SHEET    4 AA7 4 ARG A 276  ARG A 281 -1  O  LEU A 277   N  ILE A 269           
SHEET    1 AA8 4 VAL A 293  THR A 296  0                                        
SHEET    2 AA8 4 ASP A 305  ALA A 310 -1  O  ASP A 305   N  THR A 296           
SHEET    3 AA8 4 ARG A 327  PHE A 331 -1  O  ARG A 327   N  ALA A 310           
SHEET    4 AA8 4 LEU A 345  THR A 348 -1  O  LEU A 347   N  VAL A 328           
SHEET    1 AA9 2 MET A 314  ARG A 317  0                                        
SHEET    2 AA9 2 LYS A 321  GLU A 324 -1  O  LYS A 321   N  ARG A 317           
SHEET    1 AB1 4 ILE A 360  GLY A 364  0                                        
SHEET    2 AB1 4 ASP A 373  ALA A 377 -1  O  ASP A 373   N  GLY A 364           
SHEET    3 AB1 4 GLN A 388  PHE A 392 -1  O  LEU A 390   N  VAL A 376           
SHEET    4 AB1 4 GLN A 405  ASP A 408 -1  O  LEU A 407   N  VAL A 389           
SHEET    1 AB2 2 GLY A 394  GLN A 395  0                                        
SHEET    2 AB2 2 GLY A 398  LEU A 399 -1  O  GLY A 398   N  GLN A 395           
SHEET    1 AB3 3 CYS B  38  ASP B  39  0                                        
SHEET    2 AB3 3 ALA B  24  CYS B  26 -1  N  ALA B  24   O  ASP B  39           
SHEET    3 AB3 3 ILE B  54  GLU B  55 -1  O  GLU B  55   N  TRP B  25           
SHEET    1 AB4 6 ALA B  61  GLU B  65  0                                        
SHEET    2 AB4 6 ARG B  87  LEU B  92 -1  O  ARG B  87   N  LEU B  64           
SHEET    3 AB4 6 LEU B 425  PHE B 431  1  O  GLN B 428   N  LEU B  90           
SHEET    4 AB4 6 GLU B 411  PRO B 418 -1  N  ILE B 416   O  LEU B 425           
SHEET    5 AB4 6 LYS B 354  ARG B 360 -1  N  GLU B 358   O  LYS B 417           
SHEET    6 AB4 6 SER B 385  MET B 387 -1  O  CYS B 386   N  VAL B 355           
SHEET    1 AB5 5 VAL B  83  SER B  84  0                                        
SHEET    2 AB5 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3 AB5 5 THR B 394  VAL B 403 -1  O  ILE B 399   N  PHE B 100           
SHEET    4 AB5 5 LEU B 366  CYS B 374 -1  N  SER B 367   O  LYS B 402           
SHEET    5 AB5 5 GLU B 378  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1 AB6 6 TYR B 190  THR B 197  0                                        
SHEET    2 AB6 6 LEU B 149  PHE B 156 -1  N  ILE B 151   O  THR B 197           
SHEET    3 AB6 6 VAL B 112  ASP B 119  1  N  MET B 118   O  GLY B 154           
SHEET    4 AB6 6 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    5 AB6 6 ILE B 304  THR B 311  1  O  ILE B 307   N  PHE B 248           
SHEET    6 AB6 6 THR B 329  LEU B 333  1  O  LEU B 333   N  VAL B 310           
SHEET    1 AB7 3 GLU B 442  PRO B 443  0                                        
SHEET    2 AB7 3 GLY B 453  GLU B 456 -1  O  PHE B 455   N  GLU B 442           
SHEET    3 AB7 3 VAL B 459  CYS B 462 -1  O  ARG B 461   N  THR B 454           
SHEET    1 AB8 4 THR C   9  ALA C  12  0                                        
SHEET    2 AB8 4 GLN C 444  TYR C 448 -1  O  VAL C 445   N  TYR C  11           
SHEET    3 AB8 4 ASP C 434  ALA C 439 -1  N  LEU C 435   O  TYR C 448           
SHEET    4 AB8 4 LEU C 421  VAL C 425 -1  N  VAL C 425   O  ASP C 434           
SHEET    1 AB9 4 LEU C  23  LYS C  27  0                                        
SHEET    2 AB9 4 VAL C  33  GLY C  38 -1  O  VAL C  36   N  ASP C  24           
SHEET    3 AB9 4 VAL C  53  PRO C  57 -1  O  PHE C  54   N  VAL C  37           
SHEET    4 AB9 4 SER C  67  LEU C  68 -1  O  LEU C  68   N  VAL C  53           
SHEET    1 AC1 4 THR C  76  VAL C  79  0                                        
SHEET    2 AC1 4 GLN C  82  PHE C  87 -1  O  LEU C  84   N  ARG C  77           
SHEET    3 AC1 4 HIS C 112  GLU C 117 -1  O  LEU C 116   N  THR C  83           
SHEET    4 AC1 4 GLU C 120  GLU C 121 -1  O  GLU C 120   N  GLU C 117           
SHEET    1 AC2 4 THR C  76  VAL C  79  0                                        
SHEET    2 AC2 4 GLN C  82  PHE C  87 -1  O  LEU C  84   N  ARG C  77           
SHEET    3 AC2 4 HIS C 112  GLU C 117 -1  O  LEU C 116   N  THR C  83           
SHEET    4 AC2 4 THR C 125  PRO C 126 -1  O  THR C 125   N  TRP C 113           
SHEET    1 AC3 4 VAL C  97  TRP C 100  0                                        
SHEET    2 AC3 4 VAL C 103  ALA C 108 -1  O  VAL C 103   N  TRP C 100           
SHEET    3 AC3 4 SER C 129  GLN C 134 -1  O  PHE C 131   N  ALA C 106           
SHEET    4 AC3 4 ARG C 139  TYR C 143 -1  O  ALA C 141   N  LEU C 132           
SHEET    1 AC4 4 SER C 172  VAL C 175  0                                        
SHEET    2 AC4 4 GLU C 180  ALA C 185 -1  O  VAL C 182   N  VAL C 174           
SHEET    3 AC4 4 LEU C 194  PRO C 199 -1  O  LEU C 194   N  ALA C 185           
SHEET    4 AC4 4 SER C 220  LEU C 221 -1  O  SER C 220   N  GLN C 197           
SHEET    1 AC5 4 VAL C 239  GLY C 242  0                                        
SHEET    2 AC5 4 GLU C 252  ALA C 257 -1  O  VAL C 254   N  ALA C 240           
SHEET    3 AC5 4 ALA C 266  LEU C 270 -1  O  ALA C 266   N  ALA C 257           
SHEET    4 AC5 4 HIS C 278  ARG C 281 -1  O  LEU C 280   N  VAL C 267           
SHEET    1 AC6 4 VAL C 293  THR C 296  0                                        
SHEET    2 AC6 4 ASP C 305  ALA C 310 -1  O  LEU C 307   N  ALA C 294           
SHEET    3 AC6 4 ARG C 327  PHE C 331 -1  O  TYR C 329   N  VAL C 308           
SHEET    4 AC6 4 LEU C 345  THR C 348 -1  O  LEU C 347   N  VAL C 328           
SHEET    1 AC7 2 MET C 314  ARG C 317  0                                        
SHEET    2 AC7 2 LYS C 321  GLU C 324 -1  O  ALA C 323   N  GLU C 315           
SHEET    1 AC8 4 ILE C 360  GLY C 364  0                                        
SHEET    2 AC8 4 ASP C 373  ALA C 377 -1  O  ASP C 373   N  GLY C 364           
SHEET    3 AC8 4 GLN C 388  PHE C 392 -1  O  LEU C 390   N  VAL C 376           
SHEET    4 AC8 4 GLN C 405  ASP C 408 -1  O  LEU C 407   N  VAL C 389           
SHEET    1 AC9 2 GLY C 394  GLN C 395  0                                        
SHEET    2 AC9 2 GLY C 398  LEU C 399 -1  O  GLY C 398   N  GLN C 395           
SHEET    1 AD1 3 CYS D  38  ASP D  39  0                                        
SHEET    2 AD1 3 ALA D  24  CYS D  26 -1  N  ALA D  24   O  ASP D  39           
SHEET    3 AD1 3 ILE D  54  GLU D  55 -1  O  GLU D  55   N  TRP D  25           
SHEET    1 AD2 6 ALA D  61  GLU D  65  0                                        
SHEET    2 AD2 6 ARG D  87  LEU D  92 -1  O  ALA D  89   N  ARG D  62           
SHEET    3 AD2 6 LEU D 425  PHE D 431  1  O  GLN D 428   N  LEU D  90           
SHEET    4 AD2 6 GLU D 411  PRO D 418 -1  N  ILE D 416   O  LEU D 425           
SHEET    5 AD2 6 LYS D 354  ARG D 360 -1  N  ARG D 360   O  THR D 415           
SHEET    6 AD2 6 SER D 385  MET D 387 -1  O  CYS D 386   N  VAL D 355           
SHEET    1 AD3 5 VAL D  83  SER D  84  0                                        
SHEET    2 AD3 5 SER D  97  ARG D 105 -1  O  GLN D 103   N  SER D  84           
SHEET    3 AD3 5 THR D 394  VAL D 403 -1  O  ILE D 399   N  PHE D 100           
SHEET    4 AD3 5 LEU D 366  THR D 373 -1  N  ASN D 371   O  SER D 398           
SHEET    5 AD3 5 VAL D 379  PRO D 381 -1  O  ILE D 380   N  ALA D 372           
SHEET    1 AD4 6 TYR D 190  THR D 197  0                                        
SHEET    2 AD4 6 LEU D 149  PHE D 156 -1  N  ILE D 151   O  THR D 197           
SHEET    3 AD4 6 VAL D 112  ASP D 119  1  N  TYR D 116   O  GLY D 154           
SHEET    4 AD4 6 SER D 243  THR D 250  1  O  SER D 243   N  ASP D 113           
SHEET    5 AD4 6 ASN D 305  THR D 311  1  O  ALA D 309   N  PHE D 248           
SHEET    6 AD4 6 THR D 329  LEU D 333  1  O  THR D 329   N  PHE D 308           
SHEET    1 AD5 2 GLY D 453  GLU D 456  0                                        
SHEET    2 AD5 2 VAL D 459  CYS D 462 -1  O  ARG D 461   N  THR D 454           
SHEET    1 AD6 4 GLN E   3  GLN E   6  0                                        
SHEET    2 AD6 4 SER E  17  SER E  25 -1  O  THR E  23   N  GLN E   5           
SHEET    3 AD6 4 THR E  78  SER E  84 -1  O  LEU E  81   N  LEU E  20           
SHEET    4 AD6 4 ALA E  68  ASP E  73 -1  N  THR E  69   O  GLN E  82           
SHEET    1 AD7 6 GLU E  10  VAL E  12  0                                        
SHEET    2 AD7 6 THR E 113  VAL E 117  1  O  THR E 116   N  GLU E  10           
SHEET    3 AD7 6 ALA E  92  ARG E  98 -1  N  ALA E  92   O  VAL E 115           
SHEET    4 AD7 6 VAL E  34  ARG E  40 -1  N  HIS E  35   O  VAL E  97           
SHEET    5 AD7 6 GLY E  44  ILE E  51 -1  O  GLU E  46   N  LYS E  38           
SHEET    6 AD7 6 THR E  58  TYR E  60 -1  O  LYS E  59   N  ARG E  50           
SHEET    1 AD8 4 GLU E  10  VAL E  12  0                                        
SHEET    2 AD8 4 THR E 113  VAL E 117  1  O  THR E 116   N  GLU E  10           
SHEET    3 AD8 4 ALA E  92  ARG E  98 -1  N  ALA E  92   O  VAL E 115           
SHEET    4 AD8 4 TYR E 108  TRP E 109 -1  O  TYR E 108   N  ARG E  98           
SHEET    1 AD9 4 SER E 126  LEU E 130  0                                        
SHEET    2 AD9 4 SER E 141  TYR E 151 -1  O  LYS E 149   N  SER E 126           
SHEET    3 AD9 4 LEU E 180  THR E 190 -1  O  LEU E 183   N  VAL E 148           
SHEET    4 AD9 4 VAL E 169  THR E 171 -1  N  HIS E 170   O  SER E 186           
SHEET    1 AE1 4 SER E 126  LEU E 130  0                                        
SHEET    2 AE1 4 SER E 141  TYR E 151 -1  O  LYS E 149   N  SER E 126           
SHEET    3 AE1 4 LEU E 180  THR E 190 -1  O  LEU E 183   N  VAL E 148           
SHEET    4 AE1 4 VAL E 175  GLN E 177 -1  N  GLN E 177   O  LEU E 180           
SHEET    1 AE2 3 THR E 157  TRP E 160  0                                        
SHEET    2 AE2 3 THR E 200  HIS E 205 -1  O  ASN E 202   N  THR E 159           
SHEET    3 AE2 3 THR E 210  LYS E 215 -1  O  VAL E 212   N  VAL E 203           
SHEET    1 AE3 4 MET F   4  SER F   7  0                                        
SHEET    2 AE3 4 VAL F  19  ALA F  25 -1  O  HIS F  24   N  THR F   5           
SHEET    3 AE3 4 ASP F  70  ILE F  75 -1  O  LEU F  73   N  ILE F  21           
SHEET    4 AE3 4 PHE F  62  SER F  67 -1  N  SER F  63   O  THR F  74           
SHEET    1 AE4 6 SER F  10  VAL F  13  0                                        
SHEET    2 AE4 6 THR F 102  ILE F 106  1  O  GLU F 105   N  MET F  11           
SHEET    3 AE4 6 ASP F  85  GLN F  90 -1  N  TYR F  86   O  THR F 102           
SHEET    4 AE4 6 ILE F  33  GLN F  38 -1  N  GLY F  34   O  VAL F  89           
SHEET    5 AE4 6 PHE F  44  TYR F  49 -1  O  LEU F  47   N  TRP F  35           
SHEET    6 AE4 6 ASN F  53  LEU F  54 -1  O  ASN F  53   N  TYR F  49           
SHEET    1 AE5 4 SER F  10  VAL F  13  0                                        
SHEET    2 AE5 4 THR F 102  ILE F 106  1  O  GLU F 105   N  MET F  11           
SHEET    3 AE5 4 ASP F  85  GLN F  90 -1  N  TYR F  86   O  THR F 102           
SHEET    4 AE5 4 THR F  97  PHE F  98 -1  O  THR F  97   N  GLN F  90           
SHEET    1 AE6 4 THR F 114  PHE F 118  0                                        
SHEET    2 AE6 4 GLY F 129  PHE F 139 -1  O  VAL F 133   N  PHE F 118           
SHEET    3 AE6 4 TYR F 173  THR F 182 -1  O  LEU F 181   N  ALA F 130           
SHEET    4 AE6 4 VAL F 159  TRP F 163 -1  N  SER F 162   O  SER F 176           
SHEET    1 AE7 4 SER F 153  ARG F 155  0                                        
SHEET    2 AE7 4 ASN F 145  ILE F 150 -1  N  ILE F 150   O  SER F 153           
SHEET    3 AE7 4 SER F 191  THR F 197 -1  O  THR F 197   N  ASN F 145           
SHEET    4 AE7 4 SER F 208  ASN F 210 -1  O  PHE F 209   N  TYR F 192           
SHEET    1 AE8 4 GLN H   3  GLN H   6  0                                        
SHEET    2 AE8 4 VAL H  18  SER H  25 -1  O  THR H  23   N  GLN H   5           
SHEET    3 AE8 4 THR H  78  LEU H  83 -1  O  LEU H  81   N  LEU H  20           
SHEET    4 AE8 4 ALA H  68  ASP H  73 -1  N  THR H  69   O  GLN H  82           
SHEET    1 AE9 6 GLU H  10  VAL H  12  0                                        
SHEET    2 AE9 6 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3 AE9 6 ALA H  92  ARG H  98 -1  N  TYR H  94   O  THR H 113           
SHEET    4 AE9 6 VAL H  34  ARG H  40 -1  N  HIS H  35   O  VAL H  97           
SHEET    5 AE9 6 GLY H  44  ILE H  51 -1  O  GLU H  46   N  LYS H  38           
SHEET    6 AE9 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  ARG H  50           
SHEET    1 AF1 4 GLU H  10  VAL H  12  0                                        
SHEET    2 AF1 4 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3 AF1 4 ALA H  92  ARG H  98 -1  N  TYR H  94   O  THR H 113           
SHEET    4 AF1 4 TYR H 108  TRP H 109 -1  O  TYR H 108   N  ARG H  98           
SHEET    1 AF2 4 SER H 126  LEU H 130  0                                        
SHEET    2 AF2 4 SER H 141  TYR H 151 -1  O  LYS H 149   N  SER H 126           
SHEET    3 AF2 4 TYR H 181  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4 AF2 4 VAL H 169  THR H 171 -1  N  HIS H 170   O  SER H 186           
SHEET    1 AF3 4 SER H 126  LEU H 130  0                                        
SHEET    2 AF3 4 SER H 141  TYR H 151 -1  O  LYS H 149   N  SER H 126           
SHEET    3 AF3 4 TYR H 181  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4 AF3 4 VAL H 175  LEU H 176 -1  N  VAL H 175   O  THR H 182           
SHEET    1 AF4 3 THR H 157  TRP H 160  0                                        
SHEET    2 AF4 3 THR H 200  ALA H 204 -1  O  ASN H 202   N  THR H 159           
SHEET    3 AF4 3 ASP H 213  LYS H 215 -1  O  LYS H 214   N  CYS H 201           
SHEET    1 AF5 4 MET L   4  SER L   7  0                                        
SHEET    2 AF5 4 VAL L  19  ALA L  25 -1  O  HIS L  24   N  THR L   5           
SHEET    3 AF5 4 ASP L  70  ILE L  75 -1  O  LEU L  73   N  ILE L  21           
SHEET    4 AF5 4 PHE L  62  SER L  67 -1  N  SER L  63   O  THR L  74           
SHEET    1 AF6 6 SER L  10  VAL L  13  0                                        
SHEET    2 AF6 6 THR L 102  ILE L 106  1  O  GLU L 105   N  VAL L  13           
SHEET    3 AF6 6 ASP L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4 AF6 6 ILE L  33  GLN L  38 -1  N  LEU L  36   O  TYR L  87           
SHEET    5 AF6 6 PHE L  44  TYR L  49 -1  O  LEU L  47   N  TRP L  35           
SHEET    6 AF6 6 ASN L  53  LEU L  54 -1  O  ASN L  53   N  TYR L  49           
SHEET    1 AF7 4 SER L  10  VAL L  13  0                                        
SHEET    2 AF7 4 THR L 102  ILE L 106  1  O  GLU L 105   N  VAL L  13           
SHEET    3 AF7 4 ASP L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4 AF7 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1 AF8 4 THR L 114  PHE L 118  0                                        
SHEET    2 AF8 4 GLY L 129  PHE L 139 -1  O  PHE L 135   N  SER L 116           
SHEET    3 AF8 4 TYR L 173  THR L 182 -1  O  LEU L 181   N  ALA L 130           
SHEET    4 AF8 4 VAL L 159  TRP L 163 -1  N  LEU L 160   O  THR L 178           
SHEET    1 AF9 4 SER L 153  ARG L 155  0                                        
SHEET    2 AF9 4 ASN L 145  ILE L 150 -1  N  ILE L 150   O  SER L 153           
SHEET    3 AF9 4 SER L 191  THR L 197 -1  O  GLU L 195   N  LYS L 147           
SHEET    4 AF9 4 ILE L 205  ASN L 210 -1  O  ILE L 205   N  ALA L 196           
SSBOND   1 CYS A   56    CYS A   65                          1555   1555  2.02  
SSBOND   2 CYS A  107    CYS A  130                          1555   1555  2.04  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.02  
SSBOND   4 CYS B    5    CYS B   23                          1555   1555  2.04  
SSBOND   5 CYS B   13    CYS B  435                          1555   1555  2.04  
SSBOND   6 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND   7 CYS B   26    CYS B   49                          1555   1555  2.04  
SSBOND   8 CYS B  177    CYS B  184                          1555   1555  2.03  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.04  
SSBOND  10 CYS B  374    CYS B  386                          1555   1555  2.03  
SSBOND  11 CYS B  406    CYS B  433                          1555   1555  2.04  
SSBOND  12 CYS B  437    CYS B  457                          1555   1555  2.03  
SSBOND  13 CYS B  448    CYS B  460                          1555   1555  2.03  
SSBOND  14 CYS C   56    CYS C   65                          1555   1555  2.02  
SSBOND  15 CYS C  107    CYS C  130                          1555   1555  2.04  
SSBOND  16 CYS C  146    CYS C  167                          1555   1555  2.02  
SSBOND  17 CYS D    5    CYS D   23                          1555   1555  2.03  
SSBOND  18 CYS D   13    CYS D  435                          1555   1555  2.03  
SSBOND  19 CYS D   16    CYS D   38                          1555   1555  2.03  
SSBOND  20 CYS D   26    CYS D   49                          1555   1555  2.04  
SSBOND  21 CYS D  177    CYS D  184                          1555   1555  2.04  
SSBOND  22 CYS D  232    CYS D  273                          1555   1555  2.04  
SSBOND  23 CYS D  374    CYS D  386                          1555   1555  2.03  
SSBOND  24 CYS D  406    CYS D  433                          1555   1555  2.04  
SSBOND  25 CYS D  437    CYS D  457                          1555   1555  2.03  
SSBOND  26 CYS D  448    CYS D  460                          1555   1555  2.03  
SSBOND  27 CYS D  462    CYS D  471                          1555   1555  2.04  
SSBOND  28 CYS E   22    CYS E   96                          1555   1555  2.03  
SSBOND  29 CYS E  134    CYS F  214                          1555   1555  2.04  
SSBOND  30 CYS E  146    CYS E  201                          1555   1555  2.03  
SSBOND  31 CYS F   23    CYS F   88                          1555   1555  2.04  
SSBOND  32 CYS F  134    CYS F  194                          1555   1555  2.03  
SSBOND  33 CYS H   22    CYS H   96                          1555   1555  2.03  
SSBOND  34 CYS H  134    CYS L  214                          1555   1555  2.04  
SSBOND  35 CYS H  146    CYS H  201                          1555   1555  2.03  
SSBOND  36 CYS L   23    CYS L   88                          1555   1555  2.05  
SSBOND  37 CYS L  134    CYS L  194                          1555   1555  2.04  
LINK         OE1 GLU A 243                CA    CA A 502     1555   1555  2.35  
LINK         OE2 GLU A 243                CA    CA A 502     1555   1555  2.34  
LINK         OD1 ASP A 245                CA    CA A 502     1555   1555  2.29  
LINK         O   ASP A 247                CA    CA A 502     1555   1555  2.34  
LINK         O   THR A 250                CA    CA A 502     1555   1555  2.32  
LINK         OG1 THR A 250                CA    CA A 502     1555   1555  2.33  
LINK         OE1 GLU A 252                CA    CA A 502     1555   1555  2.36  
LINK         OE2 GLU A 252                CA    CA A 502     1555   1555  2.37  
LINK         OD1 ASP A 297                CA    CA A 503     1555   1555  2.36  
LINK         OD1 ASN A 299                CA    CA A 503     1555   1555  2.29  
LINK         OD1 ASP A 301                CA    CA A 503     1555   1555  2.40  
LINK         O   ARG A 303                CA    CA A 503     1555   1555  2.20  
LINK         OD1 ASP A 305                CA    CA A 503     1555   1555  2.39  
LINK         OD2 ASP A 305                CA    CA A 503     1555   1555  2.30  
LINK         OD1 ASP A 365                CA    CA A 504     1555   1555  2.31  
LINK         OD1 ASP A 367                CA    CA A 504     1555   1555  2.40  
LINK         OD1 ASP A 369                CA    CA A 504     1555   1555  2.37  
LINK         O   TYR A 371                CA    CA A 504     1555   1555  2.25  
LINK         OD1 ASP A 373                CA    CA A 504     1555   1555  2.36  
LINK         OD2 ASP A 373                CA    CA A 504     1555   1555  2.38  
LINK         OD1 ASP A 426                CA    CA A 505     1555   1555  2.27  
LINK         OD1 ASP A 428                CA    CA A 505     1555   1555  2.31  
LINK         OD1 ASN A 430                CA    CA A 505     1555   1555  2.31  
LINK         O   TYR A 432                CA    CA A 505     1555   1555  2.24  
LINK         OD1 ASP A 434                CA    CA A 505     1555   1555  2.27  
LINK         OD2 ASP A 434                CA    CA A 505     1555   1555  2.31  
LINK         ND2 ASN B  99                 C1  NAG B2004     1555   1555  1.42  
LINK         OG  SER B 121                MN    MN B2001     1555   1555  2.15  
LINK         O   SER B 123                MN    MN B2002     1555   1555  2.17  
LINK         OG  SER B 123                MN    MN B2001     1555   1555  2.16  
LINK         OD2 ASP B 158                MN    MN B2003     1555   1555  2.18  
LINK         OD1 ASN B 215                MN    MN B2003     1555   1555  2.14  
LINK         O   ASP B 217                MN    MN B2003     1555   1555  2.21  
LINK         OD1 ASP B 217                MN    MN B2003     1555   1555  2.13  
LINK         O   PRO B 219                MN    MN B2003     1555   1555  1.85  
LINK         OE1 GLU B 220                MN    MN B2003     1555   1555  2.15  
LINK         OE2 GLU B 220                MN    MN B2001     1555   1555  2.15  
LINK         OD2 ASP B 251                MN    MN B2002     1555   1555  2.16  
LINK         ND2 ASN B 320                 C1  NAG B2005     1555   1555  1.44  
LINK         ND2 ASN B 371                 C1  NAG B2010     1555   1555  1.43  
LINK         OE1 GLU C 243                CA    CA C 503     1555   1555  2.37  
LINK         OE2 GLU C 243                CA    CA C 503     1555   1555  2.35  
LINK         OD1 ASP C 245                CA    CA C 503     1555   1555  2.34  
LINK         O   ASP C 247                CA    CA C 503     1555   1555  2.40  
LINK         O   THR C 250                CA    CA C 503     1555   1555  2.36  
LINK         OG1 THR C 250                CA    CA C 503     1555   1555  2.34  
LINK         OE1 GLU C 252                CA    CA C 503     1555   1555  2.38  
LINK         OE2 GLU C 252                CA    CA C 503     1555   1555  2.36  
LINK         OD1 ASP C 297                CA    CA C 504     1555   1555  2.37  
LINK         OD1 ASN C 299                CA    CA C 504     1555   1555  2.36  
LINK         OD1 ASP C 301                CA    CA C 504     1555   1555  2.33  
LINK         O   ARG C 303                CA    CA C 504     1555   1555  2.22  
LINK         OD1 ASP C 305                CA    CA C 504     1555   1555  2.35  
LINK         OD2 ASP C 305                CA    CA C 504     1555   1555  2.35  
LINK         OD1 ASP C 365                CA    CA C 505     1555   1555  2.34  
LINK         OD1 ASP C 367                CA    CA C 505     1555   1555  2.39  
LINK         OD1 ASP C 369                CA    CA C 505     1555   1555  2.41  
LINK         O   TYR C 371                CA    CA C 505     1555   1555  2.26  
LINK         OD1 ASP C 373                CA    CA C 505     1555   1555  2.40  
LINK         OD2 ASP C 373                CA    CA C 505     1555   1555  2.38  
LINK         OD1 ASP C 426                CA    CA C 506     1555   1555  2.31  
LINK         OD1 ASP C 428                CA    CA C 506     1555   1555  2.32  
LINK         OD1 ASN C 430                CA    CA C 506     1555   1555  2.33  
LINK         O   TYR C 432                CA    CA C 506     1555   1555  2.24  
LINK         OD1 ASP C 434                CA    CA C 506     1555   1555  2.31  
LINK         OD2 ASP C 434                CA    CA C 506     1555   1555  2.38  
LINK         ND2 ASN D  99                 C1  NAG D2004     1555   1555  1.44  
LINK         OG  SER D 121                MN    MN D2001     1555   1555  2.15  
LINK         O   SER D 123                MN    MN D2002     1555   1555  2.16  
LINK         OG  SER D 123                MN    MN D2001     1555   1555  2.19  
LINK         OD2 ASP D 158                MN    MN D2003     1555   1555  2.18  
LINK         OD1 ASN D 215                MN    MN D2003     1555   1555  2.17  
LINK         O   ASP D 217                MN    MN D2003     1555   1555  2.18  
LINK         OD1 ASP D 217                MN    MN D2003     1555   1555  2.14  
LINK         O   PRO D 219                MN    MN D2003     1555   1555  1.95  
LINK         OE1 GLU D 220                MN    MN D2003     1555   1555  2.15  
LINK         OE2 GLU D 220                MN    MN D2001     1555   1555  2.15  
LINK         OD2 ASP D 251                MN    MN D2002     1555   1555  2.15  
LINK         ND2 ASN D 320                 C1  NAG D2005     1555   1555  1.43  
LINK         ND2 ASN D 371                 C1  NAG D2009     1555   1555  1.42  
LINK         OD1 ASP G 410                MN    MN B2001     1555   1555  2.10  
LINK         OD2 ASP I 410                MN    MN D2001     1555   1555  2.14  
LINK        CA    CA A 503                 O   HOH A 611     1555   1555  2.24  
LINK        CA    CA A 504                 O   HOH A 656     1555   1555  2.24  
LINK        CA    CA A 505                 O   HOH A 619     1555   1555  2.39  
LINK        MN    MN B2001                 O   HOH B2108     1555   1555  2.02  
LINK        MN    MN B2001                 O   HOH B2116     1555   1555  1.99  
LINK        MN    MN B2002                 O   HOH B2172     1555   1555  2.13  
LINK        MN    MN B2002                 O   HOH B2129     1555   1555  2.18  
LINK         O4  NAG B2005                 C1  NAG B2006     1555   1555  1.44  
LINK         O4  NAG B2006                 C1  BMA B2007     1555   1555  1.45  
LINK         O3  BMA B2007                 C1  MAN B2008     1555   1555  1.44  
LINK         O6  BMA B2007                 C1  MAN B2009     1555   1555  1.45  
LINK         O4  NAG B2010                 C1  NAG B2011     1555   1555  1.44  
LINK        CA    CA C 505                 O   HOH C 608     1555   1555  2.32  
LINK        CA    CA C 506                 O   HOH C 601     1555   1555  2.38  
LINK        MN    MN D2001                 O   HOH D2115     1555   1555  1.99  
LINK        MN    MN D2001                 O   HOH D2130     1555   1555  1.90  
LINK        MN    MN D2002                 O   HOH D2101     1555   1555  2.18  
LINK        MN    MN D2002                 O   HOH D2145     1555   1555  2.19  
LINK         O4  NAG D2005                 C1  NAG D2006     1555   1555  1.44  
LINK         O4  NAG D2006                 C1  BMA D2007     1555   1555  1.45  
LINK         O3  BMA D2007                 C1  MAN D2008     1555   1555  1.45  
LINK         O4  NAG D2009                 C1  NAG D2010     1555   1555  1.43  
CISPEP   1 SER B   84    PRO B   85          0        -2.98                     
CISPEP   2 SER B  162    PRO B  163          0         1.08                     
CISPEP   3 SER B  168    PRO B  169          0        -3.20                     
CISPEP   4 SER D   84    PRO D   85          0        -0.69                     
CISPEP   5 SER D  162    PRO D  163          0         1.89                     
CISPEP   6 SER D  168    PRO D  169          0        -3.03                     
CISPEP   7 PHE E  152    PRO E  153          0        -3.60                     
CISPEP   8 GLU E  154    PRO E  155          0        -4.79                     
CISPEP   9 TRP E  194    PRO E  195          0        -0.42                     
CISPEP  10 SER F    7    PRO F    8          0        -2.32                     
CISPEP  11 LEU F   94    PRO F   95          0         0.66                     
CISPEP  12 TYR F  140    PRO F  141          0         1.04                     
CISPEP  13 PHE H  152    PRO H  153          0        -5.33                     
CISPEP  14 GLU H  154    PRO H  155          0        -3.54                     
CISPEP  15 TRP H  194    PRO H  195          0        -0.15                     
CISPEP  16 SER L    7    PRO L    8          0        -2.11                     
CISPEP  17 LEU L   94    PRO L   95          0         0.84                     
CISPEP  18 TYR L  140    PRO L  141          0         0.87                     
SITE     1 AC1  6 ARG A 386  HOH A 604  HOH A 613  ARG C 386                    
SITE     2 AC1  6 PRO C 412  THR C 413                                          
SITE     1 AC2  5 GLU A 243  ASP A 245  ASP A 247  THR A 250                    
SITE     2 AC2  5 GLU A 252                                                     
SITE     1 AC3  6 ASP A 297  ASN A 299  ASP A 301  ARG A 303                    
SITE     2 AC3  6 ASP A 305  HOH A 611                                          
SITE     1 AC4  6 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC4  6 ASP A 373  HOH A 656                                          
SITE     1 AC5  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC5  6 ASP A 434  HOH A 619                                          
SITE     1 AC6  6 SER B 121  SER B 123  GLU B 220  HOH B2108                    
SITE     2 AC6  6 HOH B2116  ASP G 410                                          
SITE     1 AC7  6 SER B 123  ASP B 126  ASP B 127  ASP B 251                    
SITE     2 AC7  6 HOH B2129  HOH B2172                                          
SITE     1 AC8  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 AC8  5 GLU B 220                                                     
SITE     1 AC9  3 ALA C  89  HIS C 112  HOH C 631                               
SITE     1 AD1  6 GLU C 243  ASP C 245  ASP C 247  THR C 250                    
SITE     2 AD1  6 THR C 251  GLU C 252                                          
SITE     1 AD2  5 ASP C 297  ASN C 299  ASP C 301  ARG C 303                    
SITE     2 AD2  5 ASP C 305                                                     
SITE     1 AD3  6 ASP C 365  ASP C 367  ASP C 369  TYR C 371                    
SITE     2 AD3  6 ASP C 373  HOH C 608                                          
SITE     1 AD4  6 ASP C 426  ASP C 428  ASN C 430  TYR C 432                    
SITE     2 AD4  6 ASP C 434  HOH C 601                                          
SITE     1 AD5  6 SER D 121  SER D 123  GLU D 220  HOH D2115                    
SITE     2 AD5  6 HOH D2130  ASP I 410                                          
SITE     1 AD6  4 SER D 123  ASP D 251  HOH D2101  HOH D2145                    
SITE     1 AD7  5 ASP D 158  ASN D 215  ASP D 217  PRO D 219                    
SITE     2 AD7  5 GLU D 220                                                     
SITE     1 AD8  4 SER L  30  SER L  67  GLY L  68  HOH L 403                    
SITE     1 AD9  1 ASN B  99                                                     
SITE     1 AE1  6 MET A 285  ASN B 320  HOH B2117  HOH B2130                    
SITE     2 AE1  6 HOH B2147  HOH B2173                                          
SITE     1 AE2  5 ASN B 371  PRO B 381  SER B 398  ILE B 399                    
SITE     2 AE2  5 GLU B 400                                                     
SITE     1 AE3  3 ASN D  99  SER D 101  NAG D2010                               
SITE     1 AE4  8 ARG C 281  ASN D 316  ASN D 320  HOH D2123                    
SITE     2 AE4  8 HOH D2124  HOH D2128  HOH D2138  HOH D2143                    
SITE     1 AE5  4 ASN D 371  SER D 398  ILE D 399  NAG D2004                    
CRYST1  259.918  144.524  104.650  90.00  90.00  90.00 P 21 21 2     8          
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      0.003847  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006919  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009556        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system