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Database: PDB
Entry: 4Z7Q
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Original site: 4Z7Q 
HEADER    MEMBRANE PROTEIN/IMMUNE SYSTEM          07-APR-15   4Z7Q              
TITLE     INTEGRIN ALPHAIIBBETA3 IN COMPLEX WITH AGDV-NH2 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 HEAVY CHAIN;                      
COMPND  15 CHAIN: E, H;                                                         
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: MONOCLONAL ANTIBODY 10E5 LIGHT CHAIN;                      
COMPND  19 CHAIN: F, L;                                                         
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 5;                                                           
COMPND  22 MOLECULE: TETRAPEPTIDE AGDV-NH2;                                     
COMPND  23 CHAIN: G, I;                                                         
COMPND  24 ENGINEERED: YES;                                                     
COMPND  25 OTHER_DETAILS: AGDV-NH2                                              
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 4Z7Q    1       JRNL                                     
REVDAT   1   16-DEC-15 4Z7Q    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.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.94                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 107750                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1078                            
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 48.9463 -  5.3978    1.00    13835   140  0.1667 0.2062        
REMARK   3     2  5.3978 -  4.2852    0.99    13401   135  0.1355 0.2081        
REMARK   3     3  4.2852 -  3.7437    0.99    13212   134  0.1598 0.1827        
REMARK   3     4  3.7437 -  3.4015    0.99    13282   134  0.1960 0.2586        
REMARK   3     5  3.4015 -  3.1578    1.00    13235   134  0.2299 0.2961        
REMARK   3     6  3.1578 -  2.9716    1.00    13253   134  0.2649 0.2927        
REMARK   3     7  2.9716 -  2.8228    1.00    13225   134  0.2906 0.3449        
REMARK   3     8  2.8228 -  2.7000    1.00    13229   133  0.3201 0.3341        
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)     : 0.360            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.570           
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      :  0.004          21749                                  
REMARK   3   ANGLE     :  0.646          29419                                  
REMARK   3   CHIRALITY :  0.028           3273                                  
REMARK   3   PLANARITY :  0.003           3824                                  
REMARK   3   DIHEDRAL  : 10.650           7831                                  
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):  48.8942  88.0669  38.7700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3372 T22:   0.2846                                     
REMARK   3      T33:   0.2589 T12:  -0.0301                                     
REMARK   3      T13:  -0.0138 T23:   0.0582                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2738 L22:   4.7657                                     
REMARK   3      L33:   5.1391 L12:  -1.4802                                     
REMARK   3      L13:  -1.8755 L23:   1.4428                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1730 S12:   0.3757 S13:  -0.0186                       
REMARK   3      S21:  -0.3678 S22:   0.1777 S23:   0.1304                       
REMARK   3      S31:   0.2345 S32:  -0.2406 S33:  -0.0264                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 45:73)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  40.5500  95.3740  38.8818              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5548 T22:   0.4910                                     
REMARK   3      T33:   0.3709 T12:   0.1327                                     
REMARK   3      T13:  -0.0257 T23:   0.0944                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1458 L22:   5.0697                                     
REMARK   3      L33:   5.4383 L12:  -0.1680                                     
REMARK   3      L13:  -1.1796 L23:   4.3527                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4110 S12:   0.2393 S13:   0.3317                       
REMARK   3      S21:  -1.1209 S22:  -0.6018 S23:   0.5370                       
REMARK   3      S31:  -0.9583 S32:  -0.6170 S33:   0.1287                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 74:274)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  42.2292  94.7801  62.5452              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4617 T22:   0.3968                                     
REMARK   3      T33:   0.3977 T12:  -0.0380                                     
REMARK   3      T13:   0.1185 T23:   0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5861 L22:   1.0499                                     
REMARK   3      L33:   1.1036 L12:  -0.1138                                     
REMARK   3      L13:   0.1449 L23:   0.2192                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0433 S12:  -0.1659 S13:  -0.0253                       
REMARK   3      S21:   0.2973 S22:  -0.1022 S23:   0.2896                       
REMARK   3      S31:   0.0687 S32:  -0.2465 S33:   0.0626                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 275:334)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  66.4805  85.6050  60.1531              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3488 T22:   0.2780                                     
REMARK   3      T33:   0.3068 T12:   0.0868                                     
REMARK   3      T13:   0.0110 T23:   0.0579                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3864 L22:   7.4044                                     
REMARK   3      L33:   5.2904 L12:   1.5795                                     
REMARK   3      L13:   0.0559 L23:   0.5300                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0850 S12:  -0.1103 S13:  -0.1950                       
REMARK   3      S21:   0.4392 S22:   0.0260 S23:  -0.3659                       
REMARK   3      S31:   0.2759 S32:   0.1422 S33:  -0.0631                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 335:448)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  62.6785  82.9249  45.5832              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4443 T22:   0.3129                                     
REMARK   3      T33:   0.3171 T12:   0.1040                                     
REMARK   3      T13:   0.0525 T23:   0.0460                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2653 L22:   1.8152                                     
REMARK   3      L33:   2.3766 L12:   0.4939                                     
REMARK   3      L13:  -0.1050 L23:   0.3247                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1066 S12:  -0.1348 S13:  -0.3556                       
REMARK   3      S21:   0.1486 S22:   0.1388 S23:  -0.1645                       
REMARK   3      S31:   0.2718 S32:  -0.0105 S33:  -0.0344                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 449:454)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  60.0769  72.8658  33.1655              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7538 T22:   0.3277                                     
REMARK   3      T33:   0.6333 T12:   0.1275                                     
REMARK   3      T13:   0.1383 T23:   0.0349                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0935 L22:   4.8775                                     
REMARK   3      L33:   6.5043 L12:  -5.4175                                     
REMARK   3      L13:   6.2585 L23:  -5.4894                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.0767 S12:   2.2193 S13:   0.9541                       
REMARK   3      S21:  -1.4685 S22:  -2.0337 S23:  -2.3299                       
REMARK   3      S31:   1.4236 S32:   0.4372 S33:   0.4985                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 1:62)                               
REMARK   3    ORIGIN FOR THE GROUP (A): 122.8597  89.0958  35.6764              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9357 T22:   2.1326                                     
REMARK   3      T33:   1.4148 T12:   0.4229                                     
REMARK   3      T13:  -0.0481 T23:  -0.1771                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2724 L22:   2.5724                                     
REMARK   3      L33:   4.1569 L12:  -3.2771                                     
REMARK   3      L13:  -3.5339 L23:   1.3903                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5469 S12:   0.2204 S13:  -0.6249                       
REMARK   3      S21:   0.1254 S22:   0.2443 S23:  -1.0490                       
REMARK   3      S31:   0.8255 S32:   2.4503 S33:   0.1827                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 63:108)                             
REMARK   3    ORIGIN FOR THE GROUP (A): 103.5060 113.3046  52.3917              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5204 T22:   1.1091                                     
REMARK   3      T33:   0.9394 T12:  -0.1068                                     
REMARK   3      T13:   0.0177 T23:  -0.1355                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3445 L22:   9.3291                                     
REMARK   3      L33:   9.0511 L12:  -1.0397                                     
REMARK   3      L13:  -2.5382 L23:   7.2375                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1392 S12:  -0.4488 S13:   1.1466                       
REMARK   3      S21:   0.2818 S22:   0.8332 S23:  -1.0199                       
REMARK   3      S31:  -0.1577 S32:   1.1855 S33:  -1.0724                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 109:349)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  67.8109 117.9883  63.5025              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5285 T22:   0.3076                                     
REMARK   3      T33:   0.4136 T12:  -0.0133                                     
REMARK   3      T13:   0.0559 T23:  -0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5236 L22:   2.7542                                     
REMARK   3      L33:   1.2531 L12:   0.7410                                     
REMARK   3      L13:   0.3278 L23:   0.5526                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0802 S12:  -0.2964 S13:   0.3200                       
REMARK   3      S21:   0.2198 S22:  -0.0014 S23:  -0.1507                       
REMARK   3      S31:  -0.3511 S32:   0.0531 S33:  -0.0696                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 350:390)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  97.2821 103.9417  60.5564              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6723 T22:   0.8103                                     
REMARK   3      T33:   0.9057 T12:   0.0948                                     
REMARK   3      T13:  -0.1024 T23:  -0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3117 L22:   7.3888                                     
REMARK   3      L33:   7.6336 L12:  -5.2275                                     
REMARK   3      L13:  -6.4690 L23:   6.0223                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2573 S12:  -0.0755 S13:  -0.1518                       
REMARK   3      S21:   0.5757 S22:   0.4128 S23:  -0.0600                       
REMARK   3      S31:   1.2105 S32:   1.0121 S33:  -0.0936                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 391:432)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 100.5001 104.3253  48.2377              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6657 T22:   0.9010                                     
REMARK   3      T33:   0.8859 T12:   0.1163                                     
REMARK   3      T13:  -0.1547 T23:  -0.0303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7860 L22:   5.0527                                     
REMARK   3      L33:   9.3592 L12:   0.1193                                     
REMARK   3      L13:  -1.4375 L23:   5.5439                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0531 S12:   0.1408 S13:   0.0152                       
REMARK   3      S21:   0.5173 S22:   0.0691 S23:  -0.2969                       
REMARK   3      S31:   0.9902 S32:   0.5913 S33:  -0.0091                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 433:466)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 116.2894  88.4727  19.2271              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8609 T22:   1.9794                                     
REMARK   3      T33:   1.0803 T12:   0.1196                                     
REMARK   3      T13:   0.1754 T23:  -0.1941                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4878 L22:   6.0948                                     
REMARK   3      L33:   4.8013 L12:   3.0060                                     
REMARK   3      L13:  -0.9333 L23:  -4.2251                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3579 S12:  -1.5707 S13:  -0.6254                       
REMARK   3      S21:  -0.7606 S22:   0.2203 S23:  -1.0087                       
REMARK   3      S31:   0.0357 S32:   1.6830 S33:   0.0946                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 1:68)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  87.9487  94.5243 131.8050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4257 T22:   0.6842                                     
REMARK   3      T33:   0.3786 T12:   0.0041                                     
REMARK   3      T13:   0.0628 T23:  -0.0922                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0906 L22:   3.3737                                     
REMARK   3      L33:   6.1077 L12:   0.3940                                     
REMARK   3      L13:  -2.0962 L23:  -0.1405                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0397 S12:  -0.2289 S13:  -0.0430                       
REMARK   3      S21:   0.0092 S22:  -0.0673 S23:  -0.4602                       
REMARK   3      S31:   0.0951 S32:   1.2976 S33:   0.1531                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 69:274)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  92.3765  89.6973 107.4968              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6129 T22:   0.8998                                     
REMARK   3      T33:   0.5107 T12:   0.0363                                     
REMARK   3      T13:   0.1849 T23:  -0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8943 L22:   0.9993                                     
REMARK   3      L33:   1.3361 L12:   0.3059                                     
REMARK   3      L13:   0.2008 L23:   0.1062                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0988 S12:   0.6674 S13:  -0.0299                       
REMARK   3      S21:  -0.3778 S22:  -0.0277 S23:  -0.2662                       
REMARK   3      S31:   0.1729 S32:   0.6212 S33:   0.1402                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 275:334)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  71.7311  75.5380 115.3055              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7720 T22:   0.5077                                     
REMARK   3      T33:   0.5254 T12:  -0.0893                                     
REMARK   3      T13:   0.1764 T23:  -0.1166                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9700 L22:   5.5095                                     
REMARK   3      L33:   5.7364 L12:  -2.4440                                     
REMARK   3      L13:  -0.4162 L23:   0.2498                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0848 S12:   0.5994 S13:  -0.8177                       
REMARK   3      S21:  -0.4893 S22:   0.0011 S23:   0.1022                       
REMARK   3      S31:   0.9028 S32:   0.0099 S33:   0.1081                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 335:399)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  73.1081  76.3000 126.1439              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6526 T22:   0.4729                                     
REMARK   3      T33:   0.4703 T12:   0.0382                                     
REMARK   3      T13:   0.2091 T23:  -0.0285                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9696 L22:   3.7755                                     
REMARK   3      L33:   3.6741 L12:  -0.4669                                     
REMARK   3      L13:   2.4065 L23:   0.0370                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2506 S12:  -0.1545 S13:  -0.6153                       
REMARK   3      S21:  -0.0246 S22:   0.3043 S23:  -0.1751                       
REMARK   3      S31:   0.7138 S32:  -0.0499 S33:   0.0022                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 400:428)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  75.7502  84.7978 132.3587              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4330 T22:   0.5150                                     
REMARK   3      T33:   0.3421 T12:   0.0357                                     
REMARK   3      T13:   0.0819 T23:   0.0134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.3371 L22:   6.3088                                     
REMARK   3      L33:   6.2393 L12:  -0.3465                                     
REMARK   3      L13:   0.8524 L23:   0.0907                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3745 S12:   0.4151 S13:  -0.5709                       
REMARK   3      S21:   0.2576 S22:   0.2141 S23:  -0.2750                       
REMARK   3      S31:   0.6995 S32:  -0.1039 S33:   0.1518                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 429:453)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  82.1768  85.6990 136.7016              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5796 T22:   0.7471                                     
REMARK   3      T33:   0.3971 T12:   0.0283                                     
REMARK   3      T13:   0.0960 T23:  -0.0882                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7859 L22:   6.4830                                     
REMARK   3      L33:   8.6929 L12:  -4.6177                                     
REMARK   3      L13:   3.4964 L23:  -7.0312                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2841 S12:  -0.9000 S13:  -0.0306                       
REMARK   3      S21:   1.0884 S22:   0.2665 S23:  -0.0680                       
REMARK   3      S31:  -0.1908 S32:  -0.0678 S33:  -0.1873                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 1:50)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  15.9507  68.8586 141.1402              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3149 T22:   1.5980                                     
REMARK   3      T33:   1.1870 T12:  -0.6896                                     
REMARK   3      T13:   0.2887 T23:  -0.2284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8122 L22:   6.3818                                     
REMARK   3      L33:   4.2736 L12:   3.7259                                     
REMARK   3      L13:  -3.9191 L23:  -1.6446                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1715 S12:   0.3314 S13:  -1.3317                       
REMARK   3      S21:  -0.3748 S22:  -0.2679 S23:   0.8987                       
REMARK   3      S31:   1.9138 S32:  -1.2549 S33:   1.2536                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 51:176)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  44.5646  97.9408 104.9548              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7325 T22:   0.9842                                     
REMARK   3      T33:   0.4881 T12:  -0.1758                                     
REMARK   3      T13:  -0.0624 T23:   0.0703                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0572 L22:   1.5094                                     
REMARK   3      L33:   2.9162 L12:   1.1876                                     
REMARK   3      L13:  -1.5428 L23:  -1.0691                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0635 S12:   0.7915 S13:   0.5509                       
REMARK   3      S21:  -0.2084 S22:   0.2745 S23:   0.4218                       
REMARK   3      S31:   0.1526 S32:  -0.9832 S33:  -0.1941                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 177:353)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  60.8319 100.3359 101.3021              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5600 T22:   0.7411                                     
REMARK   3      T33:   0.4147 T12:  -0.1104                                     
REMARK   3      T13:   0.0227 T23:   0.1019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7429 L22:   0.9247                                     
REMARK   3      L33:   3.9924 L12:  -0.0034                                     
REMARK   3      L13:   1.3086 L23:   0.1418                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1309 S12:   0.4960 S13:   0.2376                       
REMARK   3      S21:  -0.3479 S22:   0.0892 S23:   0.0073                       
REMARK   3      S31:  -0.1351 S32:  -0.2591 S33:   0.0187                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 354:440)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  33.3714  84.0688 118.3769              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8188 T22:   0.9074                                     
REMARK   3      T33:   0.6085 T12:  -0.3037                                     
REMARK   3      T13:  -0.0371 T23:   0.0789                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6910 L22:   2.1843                                     
REMARK   3      L33:   2.7442 L12:   0.2032                                     
REMARK   3      L13:  -3.4805 L23:  -1.0103                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3663 S12:   0.3671 S13:  -0.3725                       
REMARK   3      S21:  -0.1479 S22:  -0.0418 S23:   0.0321                       
REMARK   3      S31:   0.6706 S32:  -0.3444 S33:   0.4651                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 441:465)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  20.3521  78.9031 156.9720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8967 T22:   1.3564                                     
REMARK   3      T33:   0.8933 T12:  -0.2393                                     
REMARK   3      T13:   0.2793 T23:  -0.1479                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9104 L22:   5.8071                                     
REMARK   3      L33:   5.8347 L12:   4.8143                                     
REMARK   3      L13:   5.0908 L23:   4.2108                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4191 S12:  -0.5744 S13:  -0.3670                       
REMARK   3      S21:   0.0920 S22:  -0.2962 S23:   0.4519                       
REMARK   3      S31:   0.9013 S32:  -1.4720 S33:   0.7064                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 466:471)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  29.8011  72.3240 158.6919              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8615 T22:   1.5153                                     
REMARK   3      T33:   2.6346 T12:  -0.3148                                     
REMARK   3      T13:   0.0231 T23:  -0.0429                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1762 L22:   2.4991                                     
REMARK   3      L33:   2.0232 L12:   2.2989                                     
REMARK   3      L13:   2.0852 L23:   2.2424                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3078 S12:   2.1566 S13:  -3.8519                       
REMARK   3      S21:   0.2508 S22:   0.4088 S23:   3.1479                       
REMARK   3      S31:   2.6186 S32:  -2.9925 S33:   0.0041                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 1:15)                               
REMARK   3    ORIGIN FOR THE GROUP (A): 121.0726  82.5539  84.0723              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4511 T22:   1.1001                                     
REMARK   3      T33:   0.9692 T12:   0.2596                                     
REMARK   3      T13:   0.2272 T23:  -0.0698                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5677 L22:   5.5180                                     
REMARK   3      L33:   2.0311 L12:  -2.7915                                     
REMARK   3      L13:  -1.1236 L23:   3.3001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7534 S12:   0.4574 S13:  -0.6845                       
REMARK   3      S21:  -1.7266 S22:  -0.3348 S23:  -0.8155                       
REMARK   3      S31:   3.3817 S32:   2.1680 S33:   1.2060                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 16:22)                              
REMARK   3    ORIGIN FOR THE GROUP (A): 116.3781  84.8115  78.5268              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8238 T22:   1.8602                                     
REMARK   3      T33:   0.9565 T12:   0.1159                                     
REMARK   3      T13:   0.2703 T23:  -0.2648                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1207 L22:   9.1225                                     
REMARK   3      L33:   4.6432 L12:   3.2544                                     
REMARK   3      L13:  -4.0660 L23:   0.5249                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6600 S12:   0.6464 S13:  -0.0082                       
REMARK   3      S21:  -1.1280 S22:  -1.7035 S23:  -0.0478                       
REMARK   3      S31:  -0.0210 S32:   1.1124 S33:   0.9930                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 23:64)                              
REMARK   3    ORIGIN FOR THE GROUP (A): 112.7266  92.6951  88.0129              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0268 T22:   1.3217                                     
REMARK   3      T33:   0.7528 T12:  -0.1485                                     
REMARK   3      T13:   0.3327 T23:  -0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4280 L22:   4.7465                                     
REMARK   3      L33:   6.5850 L12:  -3.4882                                     
REMARK   3      L13:   2.5901 L23:   1.9916                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2638 S12:  -0.1211 S13:   0.2071                       
REMARK   3      S21:  -0.9756 S22:  -0.5007 S23:  -0.1619                       
REMARK   3      S31:   1.0504 S32:   0.1134 S33:   0.2009                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 65:119)                             
REMARK   3    ORIGIN FOR THE GROUP (A): 116.0859  89.5451  85.8281              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1970 T22:   1.5782                                     
REMARK   3      T33:   0.8566 T12:   0.0410                                     
REMARK   3      T13:   0.4728 T23:  -0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5450 L22:   2.1275                                     
REMARK   3      L33:   8.1868 L12:  -0.9337                                     
REMARK   3      L13:  -2.4425 L23:   2.6816                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1184 S12:   1.1802 S13:   0.0011                       
REMARK   3      S21:  -0.7176 S22:  -0.3881 S23:  -0.3811                       
REMARK   3      S31:   0.9267 S32:  -0.3994 S33:   0.1540                       
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 120:170)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 150.3047  83.1135  79.7670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4426 T22:   1.6661                                     
REMARK   3      T33:   1.4990 T12:   0.2233                                     
REMARK   3      T13:   0.3617 T23:   0.3646                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2217 L22:   3.5787                                     
REMARK   3      L33:   2.5348 L12:   0.1299                                     
REMARK   3      L13:   1.6633 L23:   2.7089                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2447 S12:   1.1008 S13:   0.0921                       
REMARK   3      S21:  -0.7000 S22:  -0.2219 S23:  -1.2763                       
REMARK   3      S31:  -0.1655 S32:   0.7810 S33:  -0.0044                       
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 171:219)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 152.3731  82.1353  79.7060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5826 T22:   2.2996                                     
REMARK   3      T33:   1.6142 T12:   0.6327                                     
REMARK   3      T13:   0.3946 T23:   0.0757                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9620 L22:   3.8678                                     
REMARK   3      L33:   2.8112 L12:  -0.4711                                     
REMARK   3      L13:  -1.5267 L23:   2.6625                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6985 S12:   1.0170 S13:  -0.4532                       
REMARK   3      S21:  -0.3886 S22:  -0.5437 S23:  -0.9471                       
REMARK   3      S31:   1.2165 S32:   1.3068 S33:  -0.1100                       
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 1:11)                               
REMARK   3    ORIGIN FOR THE GROUP (A): 126.9011 107.0112  95.9895              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9666 T22:   0.9956                                     
REMARK   3      T33:   1.4784 T12:  -0.2062                                     
REMARK   3      T13:   0.2230 T23:   0.2140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1040 L22:   4.3687                                     
REMARK   3      L33:   9.4072 L12:  -5.1162                                     
REMARK   3      L13:   7.3454 L23:  -5.9481                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0427 S12:   1.2516 S13:   1.0169                       
REMARK   3      S21:  -0.3583 S22:   0.0163 S23:  -2.0182                       
REMARK   3      S31:  -0.0596 S32:   0.4596 S33:   0.9309                       
REMARK   3   TLS GROUP : 32                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 12:24)                              
REMARK   3    ORIGIN FOR THE GROUP (A): 133.6846 102.5700 106.6447              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6178 T22:   2.0336                                     
REMARK   3      T33:   1.2930 T12:  -0.1252                                     
REMARK   3      T13:   0.0206 T23:   0.2092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0782 L22:   2.6769                                     
REMARK   3      L33:   7.0799 L12:  -1.4094                                     
REMARK   3      L13:   2.6988 L23:  -3.0582                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5436 S12:   0.5867 S13:   1.6762                       
REMARK   3      S21:   0.2727 S22:  -0.7993 S23:  -0.5057                       
REMARK   3      S31:   0.6809 S32:   0.4753 S33:   0.0437                       
REMARK   3   TLS GROUP : 33                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 25:102)                             
REMARK   3    ORIGIN FOR THE GROUP (A): 122.7753  98.5022 102.3556              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6086 T22:   1.4833                                     
REMARK   3      T33:   0.9947 T12:  -0.1326                                     
REMARK   3      T13:   0.2090 T23:   0.0926                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4396 L22:   2.4849                                     
REMARK   3      L33:   3.8302 L12:  -0.2532                                     
REMARK   3      L13:   0.9458 L23:  -0.6235                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2316 S12:   0.3644 S13:   0.4714                       
REMARK   3      S21:  -0.0511 S22:  -0.2265 S23:  -0.8364                       
REMARK   3      S31:   0.0712 S32:   1.1758 S33:   0.4072                       
REMARK   3   TLS GROUP : 34                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 103:118)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 150.8204  97.5551  95.0302              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9586 T22:   2.8036                                     
REMARK   3      T33:   1.8728 T12:   0.2658                                     
REMARK   3      T13:   0.5087 T23:   0.3349                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9537 L22:   3.8118                                     
REMARK   3      L33:   0.0459 L12:  -2.1549                                     
REMARK   3      L13:  -0.2135 L23:   0.4152                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0210 S12:   0.5869 S13:   0.2036                       
REMARK   3      S21:  -1.1352 S22:  -1.1260 S23:  -0.8461                       
REMARK   3      S31:   0.5678 S32:   0.8132 S33:   1.0081                       
REMARK   3   TLS GROUP : 35                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 119:164)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 152.3889  98.1611  78.8582              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5470 T22:   1.8501                                     
REMARK   3      T33:   1.6788 T12:   0.2515                                     
REMARK   3      T13:   0.7039 T23:   0.3134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1818 L22:   1.2999                                     
REMARK   3      L33:   3.6060 L12:   1.3836                                     
REMARK   3      L13:  -0.1553 L23:  -0.7209                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4043 S12:   0.2361 S13:   0.4392                       
REMARK   3      S21:  -0.7461 S22:   0.3706 S23:  -0.1174                       
REMARK   3      S31:  -0.5581 S32:   0.5957 S33:  -0.8407                       
REMARK   3   TLS GROUP : 36                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 165:214)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 156.4266  98.7437  80.0273              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3109 T22:   2.0268                                     
REMARK   3      T33:   1.9904 T12:   0.0243                                     
REMARK   3      T13:   0.5394 T23:   0.5398                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2229 L22:   1.2293                                     
REMARK   3      L33:   4.6068 L12:   1.3601                                     
REMARK   3      L13:  -3.0321 L23:   0.1655                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0620 S12:   0.2489 S13:  -0.5487                       
REMARK   3      S21:  -0.8042 S22:  -0.2352 S23:  -1.2081                       
REMARK   3      S31:  -0.3271 S32:   1.6204 S33:   0.1882                       
REMARK   3   TLS GROUP : 37                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 1:31)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  19.5756  89.8550  85.4862              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1493 T22:   1.3004                                     
REMARK   3      T33:   0.7801 T12:   0.1308                                     
REMARK   3      T13:   0.1976 T23:   0.1086                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0580 L22:   6.5969                                     
REMARK   3      L33:   5.5620 L12:  -5.6661                                     
REMARK   3      L13:  -5.2921 L23:   5.9202                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9353 S12:  -1.8589 S13:  -0.2351                       
REMARK   3      S21:   1.8337 S22:   0.8115 S23:   0.7492                       
REMARK   3      S31:   2.1600 S32:   0.3796 S33:  -0.0059                       
REMARK   3   TLS GROUP : 38                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 32:64)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  18.0444 101.6776  79.7694              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5479 T22:   0.6478                                     
REMARK   3      T33:   0.4885 T12:   0.1009                                     
REMARK   3      T13:   0.1950 T23:  -0.0152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6235 L22:   7.0642                                     
REMARK   3      L33:   6.8091 L12:   3.1675                                     
REMARK   3      L13:   3.5110 L23:   0.1873                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0087 S12:  -0.2862 S13:   0.3182                       
REMARK   3      S21:   0.3695 S22:  -0.0267 S23:   0.5615                       
REMARK   3      S31:  -0.4827 S32:  -0.3033 S33:  -0.0664                       
REMARK   3   TLS GROUP : 39                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 65:120)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  17.4144  96.0135  83.0659              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7580 T22:   0.8107                                     
REMARK   3      T33:   0.5586 T12:   0.0563                                     
REMARK   3      T13:   0.1486 T23:  -0.0890                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0493 L22:   2.0991                                     
REMARK   3      L33:   2.6296 L12:   0.6769                                     
REMARK   3      L13:  -4.1480 L23:  -0.2097                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2127 S12:  -1.1793 S13:   0.0489                       
REMARK   3      S21:   1.0753 S22:   0.0759 S23:   0.3701                       
REMARK   3      S31:   0.3668 S32:   0.1589 S33:   0.0735                       
REMARK   3   TLS GROUP : 40                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 121:151)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -17.0849  83.8549  94.3397              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9712 T22:   1.2389                                     
REMARK   3      T33:   1.8686 T12:   0.0671                                     
REMARK   3      T13:   0.1886 T23:   0.3786                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3968 L22:   4.4562                                     
REMARK   3      L33:   5.0200 L12:   5.3610                                     
REMARK   3      L13:   5.6648 L23:   4.8104                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2406 S12:  -1.0304 S13:  -1.9803                       
REMARK   3      S21:   0.8039 S22:  -0.2031 S23:   0.5487                       
REMARK   3      S31:   0.9762 S32:   0.2246 S33:  -0.0507                       
REMARK   3   TLS GROUP : 41                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 152:179)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.4839  82.5980  89.9340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6408 T22:   1.3931                                     
REMARK   3      T33:   2.1743 T12:   0.2660                                     
REMARK   3      T13:   0.3723 T23:   0.4129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5800 L22:   6.3125                                     
REMARK   3      L33:   4.0087 L12:   5.0159                                     
REMARK   3      L13:   4.5308 L23:   1.0700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3956 S12:  -0.9884 S13:  -2.4566                       
REMARK   3      S21:   0.0388 S22:   0.4453 S23:   0.3395                       
REMARK   3      S31:   0.6397 S32:   0.1377 S33:  -0.0347                       
REMARK   3   TLS GROUP : 42                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 180:219)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -15.7469  77.5696  93.8844              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8429 T22:   1.2984                                     
REMARK   3      T33:   2.6340 T12:   0.0333                                     
REMARK   3      T13:   0.3204 T23:   0.7195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2755 L22:   0.2122                                     
REMARK   3      L33:   5.3642 L12:  -0.3915                                     
REMARK   3      L13:  -0.6536 L23:   0.9598                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0584 S12:  -0.0349 S13:  -2.3000                       
REMARK   3      S21:   0.4227 S22:   0.2476 S23:   0.0441                       
REMARK   3      S31:   1.6252 S32:  -0.1118 S33:  -0.0918                       
REMARK   3   TLS GROUP : 43                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 1:27)                               
REMARK   3    ORIGIN FOR THE GROUP (A):   1.9153  99.9918  63.1919              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4997 T22:   1.1447                                     
REMARK   3      T33:   1.0792 T12:   0.1000                                     
REMARK   3      T13:   0.0903 T23:  -0.1631                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6732 L22:   9.8984                                     
REMARK   3      L33:   0.5398 L12:   3.0916                                     
REMARK   3      L13:   0.7071 L23:   1.2290                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0445 S12:   0.4202 S13:   0.7310                       
REMARK   3      S21:   0.1722 S22:  -0.0271 S23:   1.4261                       
REMARK   3      S31:   0.0591 S32:  -0.6759 S33:  -0.0121                       
REMARK   3   TLS GROUP : 44                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 28:71)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9004  93.9501  63.1506              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3735 T22:   0.8759                                     
REMARK   3      T33:   0.7402 T12:  -0.0957                                     
REMARK   3      T13:   0.0349 T23:  -0.1706                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1136 L22:   6.6377                                     
REMARK   3      L33:   4.9704 L12:   0.8160                                     
REMARK   3      L13:  -0.5058 L23:   0.1032                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0842 S12:   0.5940 S13:  -0.6421                       
REMARK   3      S21:  -0.0551 S22:   0.0901 S23:   1.0759                       
REMARK   3      S31:   0.4640 S32:  -1.1448 S33:  -0.0278                       
REMARK   3   TLS GROUP : 45                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 72:106)                             
REMARK   3    ORIGIN FOR THE GROUP (A):   5.9951  94.9766  66.4675              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4590 T22:   1.1451                                     
REMARK   3      T33:   1.0287 T12:   0.0007                                     
REMARK   3      T13:   0.1426 T23:  -0.2583                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2512 L22:   5.5497                                     
REMARK   3      L33:   3.2060 L12:   5.5641                                     
REMARK   3      L13:   1.4845 L23:   1.6263                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1871 S12:   0.4878 S13:  -0.1527                       
REMARK   3      S21:   0.4068 S22:  -0.4519 S23:   1.2472                       
REMARK   3      S31:   0.3522 S32:  -1.3181 S33:   0.2590                       
REMARK   3   TLS GROUP : 46                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 107:145)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -19.9794  89.1104  84.0805              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5409 T22:   1.1864                                     
REMARK   3      T33:   1.4085 T12:   0.0817                                     
REMARK   3      T13:   0.2867 T23:   0.1096                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2374 L22:   3.2116                                     
REMARK   3      L33:   9.6370 L12:  -0.5070                                     
REMARK   3      L13:  -3.2281 L23:   2.3463                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7076 S12:   0.1884 S13:  -1.8402                       
REMARK   3      S21:   0.2987 S22:  -0.0359 S23:   0.4883                       
REMARK   3      S31:   0.8637 S32:   0.2126 S33:   0.7001                       
REMARK   3   TLS GROUP : 47                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 146:182)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -17.6049  94.3639  84.4745              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4829 T22:   1.0548                                     
REMARK   3      T33:   1.3911 T12:  -0.0086                                     
REMARK   3      T13:   0.2318 T23:   0.3126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9368 L22:   3.2583                                     
REMARK   3      L33:   6.8572 L12:  -1.9659                                     
REMARK   3      L13:  -0.4711 L23:   1.9107                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4360 S12:  -0.6473 S13:  -1.5189                       
REMARK   3      S21:   0.1255 S22:   0.2553 S23:   0.3813                       
REMARK   3      S31:  -0.1108 S32:   0.4707 S33:   0.1731                       
REMARK   3   TLS GROUP : 48                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 183:214)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -28.8119  95.1719  89.1441              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6438 T22:   1.2525                                     
REMARK   3      T33:   1.4209 T12:   0.1956                                     
REMARK   3      T13:   0.3254 T23:   0.0568                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5916 L22:   3.9456                                     
REMARK   3      L33:   7.3881 L12:   2.3522                                     
REMARK   3      L13:  -2.9031 L23:   1.0439                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1001 S12:  -0.1992 S13:  -1.1685                       
REMARK   3      S21:   0.5737 S22:  -0.5705 S23:   0.7818                       
REMARK   3      S31:  -0.3928 S32:  -2.7476 S33:   0.5073                       
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 4Z7Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000208775.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAR-13                          
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-D                            
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   : 107768                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
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                : 2.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.0200                             
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   (%): 62.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30                     
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      129.72000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.12000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      129.72000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.12000            
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, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH H 315  LIES ON A SPECIAL POSITION.                          
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     GLY E   135                                                      
REMARK 465     ASP E   136                                                      
REMARK 465     THR E   137                                                      
REMARK 465     THR E   138                                                      
REMARK 465     GLY E   139                                                      
REMARK 465     GLY H   135                                                      
REMARK 465     ASP H   136                                                      
REMARK 465     THR H   137                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU B  174   CG   CD   OE1  OE2                                  
REMARK 480     LYS D  350   CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP I   410    MN     MN D   509              1.27            
REMARK 500   ND2  ASN D   371     H2   NAG D   507              1.49            
REMARK 500   C1   MAN C   505     O3   BMA D   506              1.57            
REMARK 500   ND2  ASN D   371     C2   NAG D   507              1.64            
REMARK 500   O    HOH D   601     O    HOH I  2101              1.78            
REMARK 500   OG   SER D   123     OD1  ASP I   410              1.92            
REMARK 500   ND2  ASN D    99     O5   NAG D   503              1.95            
REMARK 500   ND2  ASN B   371     O5   NAG B  2010              2.00            
REMARK 500   O4   NAG D   507     O5   NAG D   508              2.02            
REMARK 500   OE2  GLU C   243     O    ASP C   247              2.03            
REMARK 500   ND2  ASN B   320     O5   NAG B  2005              2.03            
REMARK 500   OG   SER D   121     O    HOH D   601              2.06            
REMARK 500   ND2  ASN B   371     C2   NAG B  2010              2.12            
REMARK 500   O4   NAG B  2010     O5   NAG B  2011              2.13            
REMARK 500   CG   ASN B   371     C1   NAG B  2010              2.16            
REMARK 500   O    HOH A   714     O    HOH A   965              2.17            
REMARK 500   OG   SER D   123     O    HOH D   601              2.17            
REMARK 500   ND2  ASN D   320     O5   NAG D   504              2.18            
REMARK 500   CG   ASN D   371     C1   NAG D   507              2.18            
REMARK 500   O    HOH D   611     O    HOH D   684              2.19            
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    SER A  81       19.99     58.06                                   
REMARK 500    SER A 101     -142.69     57.73                                   
REMARK 500    ASP A 102       38.69    -94.93                                   
REMARK 500    LYS A 118     -110.53     57.70                                   
REMARK 500    GLU A 123      133.47     73.08                                   
REMARK 500    LEU A 212      -48.24     70.69                                   
REMARK 500    TRP A 235      104.09    -58.89                                   
REMARK 500    PHE A 417      108.38    -59.31                                   
REMARK 500    PHE B  56       82.11   -151.27                                   
REMARK 500    ASP B  76      177.41     60.08                                   
REMARK 500    SER B  77       60.44   -115.54                                   
REMARK 500    VAL B 157      -85.72   -135.19                                   
REMARK 500    SER B 213     -157.01   -117.53                                   
REMARK 500    CYS B 232       71.32   -101.17                                   
REMARK 500    ASP B 241       79.93   -101.24                                   
REMARK 500    LYS B 253     -179.64    -65.34                                   
REMARK 500    HIS B 274       31.44   -145.00                                   
REMARK 500    ALA B 309       79.25   -104.18                                   
REMARK 500    LEU B 375      -95.26     55.58                                   
REMARK 500    VAL C   6      -64.25    -92.08                                   
REMARK 500    VAL C   6      -63.81    -92.08                                   
REMARK 500    PRO C  40        4.14    -69.36                                   
REMARK 500    SER C 101     -123.01     56.58                                   
REMARK 500    LYS C 118     -114.86     60.54                                   
REMARK 500    GLU C 123      140.67     74.94                                   
REMARK 500    LEU C 212      -51.24     69.19                                   
REMARK 500    PHE C 289      104.09    -58.60                                   
REMARK 500    THR C 350      -34.06   -133.81                                   
REMARK 500    PHE C 417      108.19    -50.48                                   
REMARK 500    ALA C 439       74.11   -150.51                                   
REMARK 500    ALA D  30       35.47    -92.09                                   
REMARK 500    ASP D  47       32.00    -89.57                                   
REMARK 500    ALA D  50      109.74    -51.77                                   
REMARK 500    PHE D  56       77.42   -157.23                                   
REMARK 500    LEU D  64      -60.47   -106.84                                   
REMARK 500    VAL D 157      -79.37   -133.87                                   
REMARK 500    ASN D 175       88.27   -155.69                                   
REMARK 500    LYS D 181       43.86    -82.69                                   
REMARK 500    SER D 213     -158.54   -126.14                                   
REMARK 500    ASP D 241       70.92   -107.08                                   
REMARK 500    LEU D 258       -1.41     79.30                                   
REMARK 500    CYS D 374     -125.61    -88.68                                   
REMARK 500    ASN D 376     -136.54     54.93                                   
REMARK 500    ASN E  55      -26.08   -157.28                                   
REMARK 500    PHE E  64       37.90    -97.58                                   
REMARK 500    LEU E 100      -65.62    -92.49                                   
REMARK 500    PRO E 155     -165.29   -105.47                                   
REMARK 500    SER E 192       31.37    -93.46                                   
REMARK 500    SER F  77       82.18     56.76                                   
REMARK 500    ASN F 138       81.46     49.53                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      63 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     MAN C  505                                                       
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 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 243   OE1                                                    
REMARK 620 2 GLU A 243   OE2  54.9                                              
REMARK 620 3 ASP A 245   OD1 115.7  62.1                                        
REMARK 620 4 ASP A 247   O    74.7  63.7  89.3                                  
REMARK 620 5 THR A 250   O    75.9 125.9 164.7  84.2                            
REMARK 620 6 THR A 250   OG1 147.8 133.9  87.3  83.9  78.3                      
REMARK 620 7 GLU A 252   OE1  92.9  81.4  65.5 144.0 126.1 118.0                
REMARK 620 8 GLU A 252   OE2 126.9 136.5  90.8 155.2  89.4  71.3  55.8          
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 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 297   OD1                                                    
REMARK 620 2 ASN A 299   OD1  70.8                                              
REMARK 620 3 ASP A 301   OD1  71.0  78.6                                        
REMARK 620 4 ARG A 303   O    77.6 148.1  87.1                                  
REMARK 620 5 ASP A 305   OD1 131.7 106.7 157.3  97.5                            
REMARK 620 6 ASP A 305   OD2  77.7  82.3 147.2  95.6  54.8                      
REMARK 620 7 HOH A 619   O   149.3  83.2  88.4 125.1  70.7 115.6                
REMARK 620 N                    1     2     3     4     5     6                 
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 365   OD1                                                    
REMARK 620 2 ASP A 367   OD1  88.8                                              
REMARK 620 3 ASP A 369   OD1  76.3  84.3                                        
REMARK 620 4 TYR A 371   O    83.6 171.4  89.9                                  
REMARK 620 5 ASP A 373   OD1 146.1 106.0 134.3  82.6                            
REMARK 620 6 ASP A 373   OD2  97.9  85.4 168.3  99.6  54.5                      
REMARK 620 7 HOH A 625   O   141.2  91.6  65.2  91.9  70.1 120.7                
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 426   OD1                                                    
REMARK 620 2 ASP A 428   OD1  74.2                                              
REMARK 620 3 ASN A 430   OD1  78.1  79.5                                        
REMARK 620 4 TYR A 432   O    78.2 151.2  87.0                                  
REMARK 620 5 ASP A 434   OD1 141.4 110.8 140.2  95.9                            
REMARK 620 6 ASP A 434   OD2  86.4  88.4 162.4  98.0  56.4                      
REMARK 620 7 HOH A 644   O   142.3  74.6  76.0 126.6  70.6 113.2                
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   81.2                                              
REMARK 620 3 GLU B 220   OE2  84.3 164.6                                        
REMARK 620 4 ASP G 410   OD1  85.7  83.8  89.9                                  
REMARK 620 5 HOH B2147   O   171.7 106.2  88.6  98.6                            
REMARK 620 6 HOH B2105   O    81.7  79.1 104.1 160.1  95.8                      
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  85.4                                              
REMARK 620 3 HOH B2239   O   107.9 101.8                                        
REMARK 620 4 HOH B2102   O    83.9 168.8  78.6                                  
REMARK 620 5 HOH B2104   O   120.3  89.9 131.1  98.2                            
REMARK 620 N                    1     2     3     4                             
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 106.5                                              
REMARK 620 3 ASP B 217   O   161.7  78.8                                        
REMARK 620 4 ASP B 217   OD1  95.2  81.9  67.9                                  
REMARK 620 5 PRO B 219   O    82.1 171.3  92.6  96.3                            
REMARK 620 6 GLU B 220   OE1  98.7  89.5  98.9 165.3  90.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 243   OE1                                                    
REMARK 620 2 GLU C 243   OE2  54.6                                              
REMARK 620 3 ASP C 245   OD1 113.5  66.4                                        
REMARK 620 4 ASP C 247   O    80.8  50.7  84.6                                  
REMARK 620 5 THR C 250   O    75.1 117.4 169.1  90.4                            
REMARK 620 6 THR C 250   OG1 151.3 126.2  87.7  82.2  82.0                      
REMARK 620 7 GLU C 252   OE1  84.0  91.6  69.0 141.0 119.9 123.0                
REMARK 620 8 GLU C 252   OE2 133.6 135.4  73.8 144.4 105.5  69.1  54.8          
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 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 297   OD1                                                    
REMARK 620 2 ASN C 299   OD1  70.3                                              
REMARK 620 3 ASP C 301   OD1  59.8  87.4                                        
REMARK 620 4 ASP C 301   OD2 107.6  80.0  54.3                                  
REMARK 620 5 ARG C 303   O    69.2 139.4  75.3 115.6                            
REMARK 620 6 ASP C 305   OD1 126.7 120.1 152.5 125.4  82.7                      
REMARK 620 7 ASP C 305   OD2  85.1  74.9 144.5 146.0  98.3  54.5                
REMARK 620 N                    1     2     3     4     5     6                 
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 ASP C 365   OD1                                                    
REMARK 620 2 ASP C 367   OD1  86.5                                              
REMARK 620 3 ASP C 369   OD1  71.7  73.3                                        
REMARK 620 4 TYR C 371   O    79.2 162.8  93.1                                  
REMARK 620 5 ASP C 373   OD1 142.7 114.1 142.3  83.1                            
REMARK 620 6 ASP C 373   OD2  96.2  93.7 162.4  97.2  53.7                      
REMARK 620 7 HOH C 613   O   149.1  96.2  79.6  91.4  63.1 114.2                
REMARK 620 N                    1     2     3     4     5     6                 
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 426   OD1                                                    
REMARK 620 2 ASP C 428   OD1  64.1                                              
REMARK 620 3 ASN C 430   OD1  76.0  68.4                                        
REMARK 620 4 TYR C 432   O    76.1 138.8  93.1                                  
REMARK 620 5 ASP C 434   OD1 145.2 118.5 138.7  99.9                            
REMARK 620 6 ASP C 434   OD2  90.9  92.0 159.6  98.8  55.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 509  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER D 121   OG                                                     
REMARK 620 2 SER D 123   OG   84.7                                              
REMARK 620 3 GLU D 220   OE2  80.6 125.4                                        
REMARK 620 4 ASP I 410   OD2 117.9 119.5 113.8                                  
REMARK 620 5 HOH D 601   O    57.1  60.0  68.0 174.7                            
REMARK 620 6 HOH I2101   O   105.1  69.8  64.1 136.3  48.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 501  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 126   OD1                                                    
REMARK 620 2 ASP D 126   OD2  61.0                                              
REMARK 620 3 ASP D 127   OD1  90.1 120.9                                        
REMARK 620 4 MET D 335   O   143.7  86.8  93.2                                  
REMARK 620 5 HOH D 684   O   107.9  96.2 142.8  90.8                            
REMARK 620 6 HOH D 611   O   123.3 156.1  82.9  92.9  60.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 502  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 158   OD2                                                    
REMARK 620 2 ASN D 215   OD1 112.0                                              
REMARK 620 3 ASP D 217   O   161.9  79.4                                        
REMARK 620 4 ASP D 217   OD1  93.9  84.0  72.7                                  
REMARK 620 5 PRO D 219   O    79.8 167.1  90.7 100.9                            
REMARK 620 6 GLU D 220   OE1  98.3  85.7  96.5 166.3  87.4                      
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 CA 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 SO4 A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MAN C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN D 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN D 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN D 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
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: AE8                                                 
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: AE9                                                 
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: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 503 bound   
REMARK 800  to ASN D 99                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D    
REMARK 800  504 through BMA D 506 bound to ASN D 320                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D    
REMARK 800  507 through NAG D 508 bound to ASN D 371                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide VAL G 411 and NH2 G    
REMARK 800  412                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide VAL I 411 and NH2 I    
REMARK 800  412                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4Z7O   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Z7N   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Z7S   RELATED DB: PDB                                   
DBREF  4Z7Q A    1   454  UNP    P08514   ITA2B_HUMAN     32    485             
DBREF  4Z7Q B    1   471  UNP    P05106   ITB3_HUMAN      27    497             
DBREF  4Z7Q C    1   454  UNP    P08514   ITA2B_HUMAN     32    485             
DBREF  4Z7Q D    1   471  UNP    P05106   ITB3_HUMAN      27    497             
DBREF  4Z7Q E    1   219  PDB    4Z7Q     4Z7Q             1    219             
DBREF  4Z7Q F    1   214  PDB    4Z7Q     4Z7Q             1    214             
DBREF  4Z7Q H    1   219  PDB    4Z7Q     4Z7Q             1    219             
DBREF  4Z7Q L    1   214  PDB    4Z7Q     4Z7Q             1    214             
DBREF  4Z7Q G  408   412  PDB    4Z7Q     4Z7Q           408    412             
DBREF  4Z7Q I  408   412  PDB    4Z7Q     4Z7Q           408    412             
SEQRES   1 A  454  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 A  454  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 A  454  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 A  454  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 A  454  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 A  454  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 A  454  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 A  454  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 A  454  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 A  454  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 A  454  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 A  454  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 A  454  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 A  454  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 A  454  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 A  454  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 A  454  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 A  454  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 A  454  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 A  454  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 A  454  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 A  454  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 A  454  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 A  454  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 A  454  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 A  454  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 A  454  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 A  454  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 A  454  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 A  454  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 A  454  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 A  454  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 A  454  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 A  454  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 A  454  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL              
SEQRES   1 B  471  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  471  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  471  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  471  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  471  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  471  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  471  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  471  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  471  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  471  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  471  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  471  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  471  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  471  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  471  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  471  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  471  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  471  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  471  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  471  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  471  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  471  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  471  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  471  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  471  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  471  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  471  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  471  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  471  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  471  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  471  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  471  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  471  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  471  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  471  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  471  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 B  471  SER GLN CYS                                                  
SEQRES   1 C  454  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 C  454  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 C  454  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 C  454  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 C  454  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 C  454  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 C  454  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 C  454  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 C  454  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 C  454  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 C  454  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 C  454  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 C  454  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 C  454  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 C  454  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 C  454  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 C  454  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 C  454  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 C  454  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 C  454  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 C  454  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 C  454  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 C  454  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 C  454  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 C  454  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 C  454  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 C  454  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 C  454  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 C  454  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 C  454  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 C  454  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 C  454  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 C  454  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 C  454  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 C  454  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL              
SEQRES   1 D  471  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 D  471  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 D  471  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 D  471  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 D  471  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 D  471  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 D  471  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 D  471  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 D  471  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 D  471  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 D  471  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 D  471  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 D  471  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 D  471  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 D  471  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 D  471  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 D  471  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 D  471  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 D  471  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 D  471  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 D  471  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 D  471  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 D  471  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 D  471  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 D  471  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 D  471  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 D  471  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 D  471  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 D  471  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 D  471  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 D  471  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 D  471  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 D  471  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 D  471  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 D  471  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 D  471  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 D  471  SER GLN CYS                                                  
SEQRES   1 E  219  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 E  219  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 E  219  PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN          
SEQRES   4 E  219  ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 E  219  PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 E  219  GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 E  219  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 E  219  ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR          
SEQRES   9 E  219  ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL          
SEQRES  10 E  219  SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU          
SEQRES  11 E  219  ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR          
SEQRES  12 E  219  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 E  219  THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 E  219  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 E  219  LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO          
SEQRES  16 E  219  SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 E  219  SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG                  
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  219  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 H  219  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 H  219  PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN          
SEQRES   4 H  219  ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 H  219  PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 H  219  GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 H  219  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 H  219  ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR          
SEQRES   9 H  219  ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL          
SEQRES  10 H  219  SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU          
SEQRES  11 H  219  ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR          
SEQRES  12 H  219  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 H  219  THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 H  219  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 H  219  LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO          
SEQRES  16 H  219  SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 H  219  SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG                  
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    5  ALA GLY ASP VAL NH2                                          
SEQRES   1 I    5  ALA GLY ASP VAL NH2                                          
HET    NH2  G 412       1                                                       
HET    NH2  I 412       1                                                       
HET     CA  A 501       1                                                       
HET     CA  A 502       1                                                       
HET     CA  A 503       1                                                       
HET     CA  A 504       1                                                       
HET    SO4  A 505       5                                                       
HET    SO4  A 506       5                                                       
HET    SO4  A 507       5                                                       
HET    GOL  A 508      14                                                       
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      21                                                       
HET    MAN  B2009      21                                                       
HET    NAG  B2010      27                                                       
HET    NAG  B2011      28                                                       
HET     CA  C 501       1                                                       
HET     CA  C 502       1                                                       
HET     CA  C 503       1                                                       
HET     CA  C 504       1                                                       
HET    MAN  C 505      21                                                       
HET    SO4  C 506       5                                                       
HET    SO4  C 507       5                                                       
HET    SO4  C 508       5                                                       
HET     CL  C 509       1                                                       
HET     MN  D 501       1                                                       
HET     MN  D 502       1                                                       
HET    NAG  D 503      28                                                       
HET    NAG  D 504      27                                                       
HET    NAG  D 505      27                                                       
HET    BMA  D 506      20                                                       
HET    NAG  D 507      27                                                       
HET    NAG  D 508      28                                                       
HET     MN  D 509       1                                                       
HET    SO4  L 301       5                                                       
HETNAM     NH2 AMINO GROUP                                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
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                                                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   9  NH2    2(H2 N)                                                      
FORMUL  11   CA    8(CA 2+)                                                     
FORMUL  15  SO4    7(O4 S 2-)                                                   
FORMUL  18  GOL    C3 H8 O3                                                     
FORMUL  19   MN    6(MN 2+)                                                     
FORMUL  22  NAG    10(C8 H15 N O6)                                              
FORMUL  23  BMA    2(C6 H12 O6)                                                 
FORMUL  23  MAN    3(C6 H12 O6)                                                 
FORMUL  33   CL    CL 1-                                                        
FORMUL  41  HOH   *991(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  TYR A  207  1                                   8    
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 ASN B    3  ARG B    8  1                                   6    
HELIX    7 AA7 SER B   12  SER B   20  1                                   9    
HELIX    8 AA8 LEU B   40  ASP B   47  1                                   8    
HELIX    9 AA9 ALA B   50  GLU B   52  5                                   3    
HELIX   10 AB1 SER B  121  SER B  123  5                                   3    
HELIX   11 AB2 MET B  124  ILE B  131  1                                   8    
HELIX   12 AB3 ASN B  133  ARG B  143  1                                  11    
HELIX   13 AB4 PRO B  170  ASN B  175  1                                   6    
HELIX   14 AB5 VAL B  200  LYS B  208  1                                   9    
HELIX   15 AB6 GLY B  221  CYS B  232  1                                  12    
HELIX   16 AB7 CYS B  232  GLY B  237  1                                   6    
HELIX   17 AB8 ASP B  259  GLY B  264  5                                   6    
HELIX   18 AB9 SER B  291  LYS B  302  1                                  12    
HELIX   19 AC1 VAL B  314  GLU B  323  1                                  10    
HELIX   20 AC2 ASN B  339  ARG B  352  1                                  14    
HELIX   21 AC3 CYS B  435  ALA B  441  5                                   7    
HELIX   22 AC4 LEU C  151  ASN C  158  1                                   8    
HELIX   23 AC5 GLY C  187  LEU C  192  1                                   6    
HELIX   24 AC6 VAL C  200  TYR C  207  1                                   8    
HELIX   25 AC7 THR C  259  LEU C  264  1                                   6    
HELIX   26 AC8 ASN D    3  ARG D    8  1                                   6    
HELIX   27 AC9 SER D   12  SER D   20  1                                   9    
HELIX   28 AD1 LEU D   40  ASP D   47  1                                   8    
HELIX   29 AD2 ALA D   50  GLU D   52  5                                   3    
HELIX   30 AD3 ASP D   76  VAL D   80  5                                   5    
HELIX   31 AD4 SER D  121  LYS D  125  5                                   5    
HELIX   32 AD5 ASN D  133  ARG D  143  1                                  11    
HELIX   33 AD6 PRO D  170  ASN D  175  1                                   6    
HELIX   34 AD7 VAL D  200  LYS D  209  1                                  10    
HELIX   35 AD8 GLY D  221  CYS D  232  1                                  12    
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 SER D  291  LYS D  302  1                                  12    
HELIX   39 AE3 VAL D  314  ILE D  325  1                                  12    
HELIX   40 AE4 ASN D  339  ARG D  352  1                                  14    
HELIX   41 AE5 CYS D  435  ALA D  439  5                                   5    
HELIX   42 AE6 ASN E   28  THR E   32  5                                   5    
HELIX   43 AE7 PRO E   62  GLN E   65  5                                   4    
HELIX   44 AE8 THR E   87  THR E   91  5                                   5    
HELIX   45 AE9 SER F  121  THR F  126  1                                   6    
HELIX   46 AF1 THR F  182  GLU F  187  1                                   6    
HELIX   47 AF2 ASN H   28  THR H   32  5                                   5    
HELIX   48 AF3 THR H   87  THR H   91  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  GLU L  187  1                                   5    
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 445   N  TYR A  11           
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  ARG A 422   O  ILE A 436           
SHEET    1 AA2 4 LEU A  23  LYS A  27  0                                        
SHEET    2 AA2 4 VAL A  33  GLY A  38 -1  O  ALA A  34   N  HIS A  26           
SHEET    3 AA2 4 VAL A  53  PRO A  57 -1  O  CYS A  56   N  ILE A  35           
SHEET    4 AA2 4 SER A  67  LEU A  68 -1  O  LEU A  68   N  VAL A  53           
SHEET    1 AA3 4 THR A  76  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 VAL A  97  TRP A 100  0                                        
SHEET    2 AA4 4 VAL A 103  ALA A 108 -1  O  VAL A 105   N  VAL A  98           
SHEET    3 AA4 4 SER A 129  ALA A 133 -1  O  PHE A 131   N  ALA A 106           
SHEET    4 AA4 4 ARG A 140  TYR A 143 -1  O  ALA A 141   N  LEU A 132           
SHEET    1 AA5 4 SER A 172  VAL A 175  0                                        
SHEET    2 AA5 4 GLU A 180  ALA A 185 -1  O  VAL A 182   N  VAL A 174           
SHEET    3 AA5 4 LEU A 194  PRO A 199 -1  O  ALA A 196   N  LEU A 183           
SHEET    4 AA5 4 SER A 220  LEU A 221 -1  O  SER A 220   N  GLN A 197           
SHEET    1 AA6 4 VAL A 239  GLY A 242  0                                        
SHEET    2 AA6 4 GLU A 252  ALA A 257 -1  O  VAL A 254   N  ALA A 240           
SHEET    3 AA6 4 ALA A 266  LEU A 270 -1  O  ALA A 266   N  ALA A 257           
SHEET    4 AA6 4 ARG A 276  ARG A 281 -1  O  LEU A 280   N  VAL A 267           
SHEET    1 AA7 4 VAL A 293  VAL A 295  0                                        
SHEET    2 AA7 4 LEU A 306  ALA A 310 -1  O  LEU A 307   N  ALA A 294           
SHEET    3 AA7 4 ARG A 327  PHE A 331 -1  O  PHE A 331   N  LEU A 306           
SHEET    4 AA7 4 LEU A 345  THR A 348 -1  O  LEU A 347   N  VAL A 328           
SHEET    1 AA8 2 MET A 314  SER A 316  0                                        
SHEET    2 AA8 2 LEU A 322  GLU A 324 -1  O  ALA A 323   N  GLU A 315           
SHEET    1 AA9 4 ILE A 360  GLY A 364  0                                        
SHEET    2 AA9 4 ASP A 373  ALA A 378 -1  O  ASP A 373   N  GLY A 364           
SHEET    3 AA9 4 GLN A 388  PHE A 392 -1  O  LEU A 390   N  VAL A 376           
SHEET    4 AA9 4 GLN A 405  ASP A 408 -1  O  LEU A 407   N  VAL A 389           
SHEET    1 AB1 2 GLY A 394  GLN A 395  0                                        
SHEET    2 AB1 2 GLY A 398  LEU A 399 -1  O  GLY A 398   N  GLN A 395           
SHEET    1 AB2 3 CYS B  38  ASP B  39  0                                        
SHEET    2 AB2 3 ALA B  24  CYS B  26 -1  N  ALA B  24   O  ASP B  39           
SHEET    3 AB2 3 ILE B  54  GLU B  55 -1  O  GLU B  55   N  TRP B  25           
SHEET    1 AB3 6 GLU B  60  GLU B  65  0                                        
SHEET    2 AB3 6 ARG B  87  LEU B  92 -1  O  ALA B  89   N  ARG B  62           
SHEET    3 AB3 6 LEU B 425  PHE B 431  1  O  GLN B 428   N  LEU B  90           
SHEET    4 AB3 6 GLU B 411  PRO B 418 -1  N  ILE B 416   O  LEU B 425           
SHEET    5 AB3 6 LYS B 354  ARG B 360 -1  N  GLU B 358   O  LYS B 417           
SHEET    6 AB3 6 SER B 385  MET B 387 -1  O  CYS B 386   N  VAL B 355           
SHEET    1 AB4 5 VAL B  83  SER B  84  0                                        
SHEET    2 AB4 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3 AB4 5 THR B 394  VAL B 403 -1  O  ILE B 399   N  PHE B 100           
SHEET    4 AB4 5 LEU B 366  CYS B 374 -1  N  SER B 367   O  LYS B 402           
SHEET    5 AB4 5 GLU B 378  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1 AB5 6 TYR B 190  THR B 197  0                                        
SHEET    2 AB5 6 LEU B 149  PHE B 156 -1  N  ALA B 155   O  LYS B 191           
SHEET    3 AB5 6 VAL B 112  ASP B 119  1  N  MET B 118   O  GLY B 154           
SHEET    4 AB5 6 SER B 243  THR B 250  1  O  LEU B 245   N  ASP B 113           
SHEET    5 AB5 6 ILE B 304  THR B 311  1  O  ILE B 307   N  PHE B 248           
SHEET    6 AB5 6 THR B 329  LEU B 333  1  O  LEU B 333   N  VAL B 310           
SHEET    1 AB6 3 GLU B 442  PRO B 443  0                                        
SHEET    2 AB6 3 GLY B 453  GLU B 456 -1  O  PHE B 455   N  GLU B 442           
SHEET    3 AB6 3 VAL B 459  CYS B 462 -1  O  ARG B 461   N  THR B 454           
SHEET    1 AB7 5 GLY C  62  GLY C  63  0                                        
SHEET    2 AB7 5 THR C   9  ALA C  12  1  N  ALA C  12   O  GLY C  63           
SHEET    3 AB7 5 GLN C 444  TYR C 448 -1  O  VAL C 445   N  TYR C  11           
SHEET    4 AB7 5 ASP C 434  ALA C 439 -1  N  LEU C 435   O  TYR C 448           
SHEET    5 AB7 5 LEU C 421  VAL C 425 -1  N  ARG C 422   O  ILE C 436           
SHEET    1 AB8 3 LEU C  23  LYS C  27  0                                        
SHEET    2 AB8 3 VAL C  33  ALA C  39 -1  O  ALA C  34   N  HIS C  26           
SHEET    3 AB8 3 GLY C  52  PRO C  57 -1  O  CYS C  56   N  ILE C  35           
SHEET    1 AB9 4 THR C  76  VAL C  79  0                                        
SHEET    2 AB9 4 GLN C  82  PHE C  87 -1  O  LEU C  84   N  ARG C  77           
SHEET    3 AB9 4 HIS C 112  GLU C 117 -1  O  HIS C 112   N  PHE C  87           
SHEET    4 AB9 4 GLU C 120  GLU C 121 -1  O  GLU C 120   N  GLU C 117           
SHEET    1 AC1 4 VAL C  97  TRP C 100  0                                        
SHEET    2 AC1 4 VAL C 103  ALA C 108 -1  O  VAL C 105   N  VAL C  98           
SHEET    3 AC1 4 SER C 129  ALA C 133 -1  O  PHE C 131   N  ALA C 106           
SHEET    4 AC1 4 ARG C 140  TYR C 143 -1  O  ALA C 141   N  LEU C 132           
SHEET    1 AC2 4 SER C 172  VAL C 175  0                                        
SHEET    2 AC2 4 GLU C 180  ALA C 185 -1  O  GLY C 184   N  SER C 172           
SHEET    3 AC2 4 LEU C 194  PRO C 199 -1  O  LEU C 194   N  ALA C 185           
SHEET    4 AC2 4 SER C 220  LEU C 221 -1  O  SER C 220   N  GLN C 197           
SHEET    1 AC3 4 VAL C 239  GLY C 242  0                                        
SHEET    2 AC3 4 GLU C 252  ALA C 257 -1  O  VAL C 254   N  ALA C 240           
SHEET    3 AC3 4 ALA C 266  LEU C 270 -1  O  ALA C 266   N  ALA C 257           
SHEET    4 AC3 4 ARG C 276  ARG C 281 -1  O  LEU C 280   N  VAL C 267           
SHEET    1 AC4 4 VAL C 293  THR C 296  0                                        
SHEET    2 AC4 4 ASP C 305  ALA C 310 -1  O  ASP C 305   N  THR C 296           
SHEET    3 AC4 4 ARG C 327  PHE C 331 -1  O  ARG C 327   N  ALA C 310           
SHEET    4 AC4 4 LEU C 345  THR C 348 -1  O  LEU C 347   N  VAL C 328           
SHEET    1 AC5 2 MET C 314  SER C 316  0                                        
SHEET    2 AC5 2 LEU C 322  GLU C 324 -1  O  ALA C 323   N  GLU C 315           
SHEET    1 AC6 4 ILE C 360  GLY C 364  0                                        
SHEET    2 AC6 4 ASP C 373  ALA C 378 -1  O  ASP C 373   N  GLY C 364           
SHEET    3 AC6 4 GLN C 388  PHE C 392 -1  O  LEU C 390   N  VAL C 376           
SHEET    4 AC6 4 GLN C 405  ASP C 408 -1  O  LEU C 407   N  VAL C 389           
SHEET    1 AC7 2 GLY C 394  GLN C 395  0                                        
SHEET    2 AC7 2 GLY C 398  LEU C 399 -1  O  GLY C 398   N  GLN C 395           
SHEET    1 AC8 3 CYS D  38  ASP D  39  0                                        
SHEET    2 AC8 3 ALA D  24  CYS D  26 -1  N  ALA D  24   O  ASP D  39           
SHEET    3 AC8 3 ILE D  54  GLU D  55 -1  O  GLU D  55   N  TRP D  25           
SHEET    1 AC9 6 ALA D  61  GLU D  65  0                                        
SHEET    2 AC9 6 ARG D  87  LEU D  92 -1  O  ALA D  89   N  ARG D  62           
SHEET    3 AC9 6 LEU D 425  PHE D 431  1  O  THR D 430   N  LEU D  90           
SHEET    4 AC9 6 GLU D 411  PRO D 418 -1  N  PHE D 414   O  VAL D 427           
SHEET    5 AC9 6 VAL D 355  ARG D 360 -1  N  GLU D 358   O  LYS D 417           
SHEET    6 AC9 6 SER D 385  CYS D 386 -1  O  CYS D 386   N  VAL D 355           
SHEET    1 AD1 5 VAL D  83  SER D  84  0                                        
SHEET    2 AD1 5 SER D  97  ARG D 105 -1  O  GLN D 103   N  SER D  84           
SHEET    3 AD1 5 THR D 394  VAL D 403 -1  O  ILE D 399   N  PHE D 100           
SHEET    4 AD1 5 LEU D 366  THR D 373 -1  N  ASN D 371   O  SER D 398           
SHEET    5 AD1 5 VAL D 379  PRO D 381 -1  O  ILE D 380   N  ALA D 372           
SHEET    1 AD2 6 TYR D 190  THR D 197  0                                        
SHEET    2 AD2 6 LEU D 149  PHE D 156 -1  N  ALA D 155   O  LYS D 191           
SHEET    3 AD2 6 VAL D 112  ASP D 119  1  N  TYR D 116   O  GLY D 154           
SHEET    4 AD2 6 SER D 243  THR D 250  1  O  LEU D 245   N  ASP D 113           
SHEET    5 AD2 6 ILE D 304  THR D 311  1  O  ASN D 305   N  HIS D 244           
SHEET    6 AD2 6 THR D 329  LEU D 333  1  O  LEU D 333   N  VAL D 310           
SHEET    1 AD3 3 GLU D 442  PRO D 443  0                                        
SHEET    2 AD3 3 GLY D 453  GLU D 456 -1  O  PHE D 455   N  GLU D 442           
SHEET    3 AD3 3 VAL D 459  CYS D 462 -1  O  ARG D 461   N  THR D 454           
SHEET    1 AD4 4 GLN E   3  GLN E   6  0                                        
SHEET    2 AD4 4 SER E  17  SER E  25 -1  O  THR E  23   N  GLN E   5           
SHEET    3 AD4 4 THR E  78  SER E  84 -1  O  LEU E  83   N  VAL E  18           
SHEET    4 AD4 4 ALA E  68  ASP E  73 -1  N  THR E  69   O  GLN E  82           
SHEET    1 AD5 6 GLU E  10  VAL E  12  0                                        
SHEET    2 AD5 6 THR E 113  VAL E 117  1  O  THR E 116   N  GLU E  10           
SHEET    3 AD5 6 ALA E  92  ARG E  98 -1  N  TYR E  94   O  THR E 113           
SHEET    4 AD5 6 VAL E  34  ARG E  40 -1  N  HIS E  35   O  VAL E  97           
SHEET    5 AD5 6 GLY E  44  ILE E  51 -1  O  GLU E  46   N  LYS E  38           
SHEET    6 AD5 6 THR E  58  TYR E  60 -1  O  LYS E  59   N  ARG E  50           
SHEET    1 AD6 4 GLU E  10  VAL E  12  0                                        
SHEET    2 AD6 4 THR E 113  VAL E 117  1  O  THR E 116   N  GLU E  10           
SHEET    3 AD6 4 ALA E  92  ARG E  98 -1  N  TYR E  94   O  THR E 113           
SHEET    4 AD6 4 TYR E 108  TRP E 109 -1  O  TYR E 108   N  ARG E  98           
SHEET    1 AD7 4 SER E 126  LEU E 130  0                                        
SHEET    2 AD7 4 GLY E 145  TYR E 151 -1  O  LEU E 147   N  TYR E 128           
SHEET    3 AD7 4 LEU E 180  LEU E 183 -1  O  LEU E 183   N  VAL E 148           
SHEET    4 AD7 4 VAL E 175  GLN E 177 -1  N  GLN E 177   O  LEU E 180           
SHEET    1 AD8 2 SER E 141  THR E 143  0                                        
SHEET    2 AD8 2 THR E 188  THR E 190 -1  O  VAL E 189   N  VAL E 142           
SHEET    1 AD9 3 THR E 157  TRP E 160  0                                        
SHEET    2 AD9 3 THR E 200  ALA E 204 -1  O  ALA E 204   N  THR E 157           
SHEET    3 AD9 3 ASP E 213  LYS E 215 -1  O  LYS E 214   N  CYS E 201           
SHEET    1 AE1 4 MET F   4  SER F   7  0                                        
SHEET    2 AE1 4 VAL F  19  ALA F  25 -1  O  HIS F  24   N  THR F   5           
SHEET    3 AE1 4 ASP F  70  ILE F  75 -1  O  TYR F  71   N  CYS F  23           
SHEET    4 AE1 4 PHE F  62  SER F  67 -1  N  SER F  65   O  SER F  72           
SHEET    1 AE2 6 SER F  10  VAL F  13  0                                        
SHEET    2 AE2 6 THR F 102  ILE F 106  1  O  GLU F 105   N  VAL F  13           
SHEET    3 AE2 6 ASP F  85  GLN F  90 -1  N  TYR F  86   O  THR F 102           
SHEET    4 AE2 6 ILE F  33  GLN F  38 -1  N  GLY F  34   O  VAL F  89           
SHEET    5 AE2 6 PHE F  44  TYR F  49 -1  O  LEU F  47   N  TRP F  35           
SHEET    6 AE2 6 ASN F  53  LEU F  54 -1  O  ASN F  53   N  TYR F  49           
SHEET    1 AE3 4 SER F  10  VAL F  13  0                                        
SHEET    2 AE3 4 THR F 102  ILE F 106  1  O  GLU F 105   N  VAL F  13           
SHEET    3 AE3 4 ASP F  85  GLN F  90 -1  N  TYR F  86   O  THR F 102           
SHEET    4 AE3 4 THR F  97  PHE F  98 -1  O  THR F  97   N  GLN F  90           
SHEET    1 AE4 4 THR F 114  PHE F 118  0                                        
SHEET    2 AE4 4 ALA F 130  PHE F 139 -1  O  VAL F 133   N  PHE F 118           
SHEET    3 AE4 4 TYR F 173  LEU F 181 -1  O  MET F 175   N  LEU F 136           
SHEET    4 AE4 4 VAL F 159  TRP F 163 -1  N  SER F 162   O  SER F 176           
SHEET    1 AE5 3 SER F 153  ARG F 155  0                                        
SHEET    2 AE5 3 ASN F 145  ILE F 150 -1  N  ILE F 150   O  SER F 153           
SHEET    3 AE5 3 TYR F 192  THR F 197 -1  O  THR F 193   N  LYS F 149           
SHEET    1 AE6 4 GLN H   3  GLN H   6  0                                        
SHEET    2 AE6 4 VAL H  18  SER H  25 -1  O  THR H  23   N  GLN H   5           
SHEET    3 AE6 4 THR H  78  LEU H  83 -1  O  LEU H  83   N  VAL H  18           
SHEET    4 AE6 4 ALA H  68  ASP H  73 -1  N  THR H  69   O  GLN H  82           
SHEET    1 AE7 6 GLU H  10  VAL H  12  0                                        
SHEET    2 AE7 6 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3 AE7 6 ALA H  92  ARG H  98 -1  N  TYR H  94   O  THR H 113           
SHEET    4 AE7 6 VAL H  34  ARG H  40 -1  N  HIS H  35   O  VAL H  97           
SHEET    5 AE7 6 GLY H  44  ILE H  51 -1  O  GLU H  46   N  LYS H  38           
SHEET    6 AE7 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  ARG H  50           
SHEET    1 AE8 4 GLU H  10  VAL H  12  0                                        
SHEET    2 AE8 4 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3 AE8 4 ALA H  92  ARG H  98 -1  N  TYR H  94   O  THR H 113           
SHEET    4 AE8 4 TYR H 108  TRP H 109 -1  O  TYR H 108   N  ARG H  98           
SHEET    1 AE9 4 SER H 126  LEU H 130  0                                        
SHEET    2 AE9 4 SER H 141  TYR H 151 -1  O  LYS H 149   N  SER H 126           
SHEET    3 AE9 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4 AE9 4 VAL H 169  THR H 171 -1  N  HIS H 170   O  SER H 186           
SHEET    1 AF1 4 SER H 126  LEU H 130  0                                        
SHEET    2 AF1 4 SER H 141  TYR H 151 -1  O  LYS H 149   N  SER H 126           
SHEET    3 AF1 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4 AF1 4 VAL H 175  GLN H 177 -1  N  GLN H 177   O  LEU H 180           
SHEET    1 AF2 3 THR H 157  TRP H 160  0                                        
SHEET    2 AF2 3 THR H 200  HIS H 205 -1  O  ASN H 202   N  THR H 159           
SHEET    3 AF2 3 THR H 210  LYS H 215 -1  O  THR H 210   N  HIS H 205           
SHEET    1 AF3 4 MET L   4  SER L   7  0                                        
SHEET    2 AF3 4 VAL L  19  ALA L  25 -1  O  HIS L  24   N  THR L   5           
SHEET    3 AF3 4 ASP L  70  ILE L  75 -1  O  LEU L  73   N  ILE L  21           
SHEET    4 AF3 4 PHE L  62  SER L  67 -1  N  SER L  63   O  THR L  74           
SHEET    1 AF4 6 SER L  10  VAL L  13  0                                        
SHEET    2 AF4 6 THR L 102  ILE L 106  1  O  GLU L 105   N  MET L  11           
SHEET    3 AF4 6 ASP L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4 AF4 6 ILE L  33  GLN L  38 -1  N  GLY L  34   O  VAL L  89           
SHEET    5 AF4 6 PHE L  44  TYR L  49 -1  O  LEU L  47   N  TRP L  35           
SHEET    6 AF4 6 ASN L  53  LEU L  54 -1  O  ASN L  53   N  TYR L  49           
SHEET    1 AF5 4 SER L  10  VAL L  13  0                                        
SHEET    2 AF5 4 THR L 102  ILE L 106  1  O  GLU L 105   N  MET L  11           
SHEET    3 AF5 4 ASP L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4 AF5 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1 AF6 4 THR L 114  PHE L 118  0                                        
SHEET    2 AF6 4 GLY L 129  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3 AF6 4 TYR L 173  THR L 182 -1  O  LEU L 181   N  ALA L 130           
SHEET    4 AF6 4 VAL L 159  TRP L 163 -1  N  SER L 162   O  SER L 176           
SHEET    1 AF7 4 SER L 153  ARG L 155  0                                        
SHEET    2 AF7 4 ASN L 145  ILE L 150 -1  N  ILE L 150   O  SER L 153           
SHEET    3 AF7 4 SER L 191  THR L 197 -1  O  GLU L 195   N  LYS L 147           
SHEET    4 AF7 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  2.03  
SSBOND   2 CYS A  107    CYS A  130                          1555   1555  2.03  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.03  
SSBOND   4 CYS B    5    CYS B   23                          1555   1555  2.03  
SSBOND   5 CYS B   13    CYS B  435                          1555   1555  2.03  
SSBOND   6 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND   7 CYS B   26    CYS B   49                          1555   1555  2.03  
SSBOND   8 CYS B  177    CYS B  184                          1555   1555  2.04  
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  2.03  
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  2.03  
SSBOND  15 CYS C  107    CYS C  130                          1555   1555  2.03  
SSBOND  16 CYS C  146    CYS C  167                          1555   1555  2.03  
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  2.03  
SSBOND  21 CYS D  177    CYS D  184                          1555   1555  2.03  
SSBOND  22 CYS D  232    CYS D  273                          1555   1555  2.03  
SSBOND  23 CYS D  374    CYS D  386                          1555   1555  2.03  
SSBOND  24 CYS D  406    CYS D  433                          1555   1555  2.03  
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  2.03  
SSBOND  28 CYS E   22    CYS E   96                          1555   1555  2.03  
SSBOND  29 CYS E  134    CYS F  214                          1555   1555  2.03  
SSBOND  30 CYS E  146    CYS E  201                          1555   1555  2.03  
SSBOND  31 CYS F   23    CYS F   88                          1555   1555  2.03  
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  2.03  
SSBOND  35 CYS H  146    CYS H  201                          1555   1555  2.03  
SSBOND  36 CYS L   23    CYS L   88                          1555   1555  2.03  
SSBOND  37 CYS L  134    CYS L  194                          1555   1555  2.03  
LINK         OE1 GLU A 243                CA    CA A 501     1555   1555  2.36  
LINK         OE2 GLU A 243                CA    CA A 501     1555   1555  2.41  
LINK         OD1 ASP A 245                CA    CA A 501     1555   1555  2.30  
LINK         O   ASP A 247                CA    CA A 501     1555   1555  2.34  
LINK         O   THR A 250                CA    CA A 501     1555   1555  2.33  
LINK         OG1 THR A 250                CA    CA A 501     1555   1555  2.41  
LINK         OE1 GLU A 252                CA    CA A 501     1555   1555  2.34  
LINK         OE2 GLU A 252                CA    CA A 501     1555   1555  2.36  
LINK         OD1 ASP A 297                CA    CA A 502     1555   1555  2.39  
LINK         OD1 ASN A 299                CA    CA A 502     1555   1555  2.37  
LINK         OD1 ASP A 301                CA    CA A 502     1555   1555  2.44  
LINK         O   ARG A 303                CA    CA A 502     1555   1555  2.21  
LINK         OD1 ASP A 305                CA    CA A 502     1555   1555  2.38  
LINK         OD2 ASP A 305                CA    CA A 502     1555   1555  2.38  
LINK         OD1 ASP A 365                CA    CA A 503     1555   1555  2.37  
LINK         OD1 ASP A 367                CA    CA A 503     1555   1555  2.37  
LINK         OD1 ASP A 369                CA    CA A 503     1555   1555  2.37  
LINK         O   TYR A 371                CA    CA A 503     1555   1555  2.23  
LINK         OD1 ASP A 373                CA    CA A 503     1555   1555  2.39  
LINK         OD2 ASP A 373                CA    CA A 503     1555   1555  2.41  
LINK         OD1 ASP A 426                CA    CA A 504     1555   1555  2.36  
LINK         OD1 ASP A 428                CA    CA A 504     1555   1555  2.38  
LINK         OD1 ASN A 430                CA    CA A 504     1555   1555  2.34  
LINK         O   TYR A 432                CA    CA A 504     1555   1555  2.16  
LINK         OD1 ASP A 434                CA    CA A 504     1555   1555  2.26  
LINK         OD2 ASP A 434                CA    CA A 504     1555   1555  2.38  
LINK         ND2 ASN B  99                 C1  NAG B2004     1555   1555  1.38  
LINK         OG  SER B 121                MN    MN B2001     1555   1555  2.16  
LINK         O   SER B 123                MN    MN B2002     1555   1555  2.17  
LINK         OG  SER B 123                MN    MN B2001     1555   1555  2.18  
LINK         OD2 ASP B 158                MN    MN B2003     1555   1555  2.15  
LINK         OD1 ASN B 215                MN    MN B2003     1555   1555  2.17  
LINK         O   ASP B 217                MN    MN B2003     1555   1555  2.19  
LINK         OD1 ASP B 217                MN    MN B2003     1555   1555  2.14  
LINK         O   PRO B 219                MN    MN B2003     1555   1555  2.07  
LINK         OE1 GLU B 220                MN    MN B2003     1555   1555  2.15  
LINK         OE2 GLU B 220                MN    MN B2001     1555   1555  2.14  
LINK         OD2 ASP B 251                MN    MN B2002     1555   1555  2.16  
LINK         ND2 ASN B 320                 C1  NAG B2005     1555   1555  1.37  
LINK         ND2 ASN B 371                 C1  NAG B2010     1555   1555  1.42  
LINK         OE1 GLU C 243                CA    CA C 501     1555   1555  2.40  
LINK         OE2 GLU C 243                CA    CA C 501     1555   1555  2.38  
LINK         OD1 ASP C 245                CA    CA C 501     1555   1555  2.34  
LINK         O   ASP C 247                CA    CA C 501     1555   1555  2.36  
LINK         O   THR C 250                CA    CA C 501     1555   1555  2.38  
LINK         OG1 THR C 250                CA    CA C 501     1555   1555  2.40  
LINK         OE1 GLU C 252                CA    CA C 501     1555   1555  2.37  
LINK         OE2 GLU C 252                CA    CA C 501     1555   1555  2.39  
LINK         OD1 ASP C 297                CA    CA C 502     1555   1555  2.38  
LINK         OD1 ASN C 299                CA    CA C 502     1555   1555  2.32  
LINK         OD1 ASP C 301                CA    CA C 502     1555   1555  2.40  
LINK         OD2 ASP C 301                CA    CA C 502     1555   1555  2.40  
LINK         O   ARG C 303                CA    CA C 502     1555   1555  2.51  
LINK         OD1 ASP C 305                CA    CA C 502     1555   1555  2.40  
LINK         OD2 ASP C 305                CA    CA C 502     1555   1555  2.39  
LINK         OD1 ASP C 365                CA    CA C 503     1555   1555  2.37  
LINK         OD1 ASP C 367                CA    CA C 503     1555   1555  2.34  
LINK         OD1 ASP C 369                CA    CA C 503     1555   1555  2.46  
LINK         O   TYR C 371                CA    CA C 503     1555   1555  2.23  
LINK         OD1 ASP C 373                CA    CA C 503     1555   1555  2.43  
LINK         OD2 ASP C 373                CA    CA C 503     1555   1555  2.42  
LINK         OD1 ASP C 426                CA    CA C 504     1555   1555  2.35  
LINK         OD1 ASP C 428                CA    CA C 504     1555   1555  2.41  
LINK         OD1 ASN C 430                CA    CA C 504     1555   1555  2.37  
LINK         O   TYR C 432                CA    CA C 504     1555   1555  2.23  
LINK         OD1 ASP C 434                CA    CA C 504     1555   1555  2.34  
LINK         OD2 ASP C 434                CA    CA C 504     1555   1555  2.40  
LINK         ND2 ASN D  99                 C1  NAG D 503     1555   1555  1.38  
LINK         OG  SER D 121                MN    MN D 509     1555   1555  2.20  
LINK         OG  SER D 123                MN    MN D 509     1555   1555  2.23  
LINK         OD1 ASP D 126                MN    MN D 501     1555   1555  2.15  
LINK         OD2 ASP D 126                MN    MN D 501     1555   1555  2.17  
LINK         OD1 ASP D 127                MN    MN D 501     1555   1555  2.17  
LINK         OD2 ASP D 158                MN    MN D 502     1555   1555  2.17  
LINK         OD1 ASN D 215                MN    MN D 502     1555   1555  2.18  
LINK         O   ASP D 217                MN    MN D 502     1555   1555  2.19  
LINK         OD1 ASP D 217                MN    MN D 502     1555   1555  2.16  
LINK         O   PRO D 219                MN    MN D 502     1555   1555  2.15  
LINK         OE1 GLU D 220                MN    MN D 502     1555   1555  2.18  
LINK         OE2 GLU D 220                MN    MN D 509     1555   1555  2.19  
LINK         ND2 ASN D 320                 C1  NAG D 504     1555   1555  1.43  
LINK         O   MET D 335                MN    MN D 501     1555   1555  2.29  
LINK         ND2 ASN D 371                 C1  NAG D 507     1555   1555  1.44  
LINK         OD1 ASP G 410                MN    MN B2001     1555   1555  2.14  
LINK         C   VAL G 411                 N   NH2 G 412     1555   1555  1.23  
LINK         OD2 ASP I 410                MN    MN D 509     1555   1555  2.13  
LINK         C   VAL I 411                 N   NH2 I 412     1555   1555  1.23  
LINK        CA    CA A 502                 O   HOH A 619     1555   1555  2.40  
LINK        CA    CA A 503                 O   HOH A 625     1555   1555  2.42  
LINK        CA    CA A 504                 O   HOH A 644     1555   1555  2.38  
LINK        MN    MN B2001                 O   HOH B2147     1555   1555  2.18  
LINK        MN    MN B2001                 O   HOH B2105     1555   1555  2.18  
LINK        MN    MN B2002                 O   HOH B2239     1555   1555  2.20  
LINK        MN    MN B2002                 O   HOH B2102     1555   1555  2.19  
LINK        MN    MN B2002                 O   HOH B2104     1555   1555  2.20  
LINK         O4  NAG B2005                 C1  NAG B2006     1555   1555  1.46  
LINK         O4  NAG B2006                 C1  BMA B2007     1555   1555  1.47  
LINK         O3  BMA B2007                 C1  MAN B2008     1555   1555  1.49  
LINK         O6  BMA B2007                 C1  MAN B2009     1555   1555  1.40  
LINK         O4  NAG B2010                 C1  NAG B2011     1555   1555  1.44  
LINK        CA    CA C 503                 O   HOH C 613     1555   1555  2.36  
LINK        MN    MN D 501                 O   HOH D 684     1555   1555  2.20  
LINK        MN    MN D 501                 O   HOH D 611     1555   1555  2.20  
LINK         O4  NAG D 504                 C1  NAG D 505     1555   1555  1.55  
LINK         O4  NAG D 505                 C1  BMA D 506     1555   1555  1.49  
LINK         O4  NAG D 507                 C1  NAG D 508     1555   1555  1.49  
LINK        MN    MN D 509                 O   HOH D 601     1555   1555  2.11  
LINK        MN    MN D 509                 O   HOH I2101     1555   1555  2.19  
CISPEP   1 SER B   84    PRO B   85          0        -2.76                     
CISPEP   2 SER B  162    PRO B  163          0         0.99                     
CISPEP   3 SER B  168    PRO B  169          0        -3.99                     
CISPEP   4 SER D   84    PRO D   85          0        -2.49                     
CISPEP   5 SER D  162    PRO D  163          0         1.38                     
CISPEP   6 SER D  168    PRO D  169          0        -6.09                     
CISPEP   7 PHE E  152    PRO E  153          0        -4.30                     
CISPEP   8 GLU E  154    PRO E  155          0        -4.02                     
CISPEP   9 TRP E  194    PRO E  195          0        -4.09                     
CISPEP  10 SER F    7    PRO F    8          0        -2.50                     
CISPEP  11 LEU F   94    PRO F   95          0        -0.33                     
CISPEP  12 TYR F  140    PRO F  141          0        -0.14                     
CISPEP  13 PHE H  152    PRO H  153          0        -3.30                     
CISPEP  14 GLU H  154    PRO H  155          0        -4.27                     
CISPEP  15 TRP H  194    PRO H  195          0        -2.12                     
CISPEP  16 SER L    7    PRO L    8          0        -2.20                     
CISPEP  17 LEU L   94    PRO L   95          0         0.48                     
CISPEP  18 TYR L  140    PRO L  141          0         0.15                     
SITE     1 AC1  5 GLU A 243  ASP A 245  ASP A 247  THR A 250                    
SITE     2 AC1  5 GLU A 252                                                     
SITE     1 AC2  6 ASP A 297  ASN A 299  ASP A 301  ARG A 303                    
SITE     2 AC2  6 ASP A 305  HOH A 619                                          
SITE     1 AC3  6 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC3  6 ASP A 373  HOH A 625                                          
SITE     1 AC4  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC4  6 ASP A 434  HOH A 644                                          
SITE     1 AC5  3 ILE A 154  TYR A 155  SER A 161                               
SITE     1 AC6  5 PHE A  10  PRO A 410  PHE A 411  GLN A 444                    
SITE     2 AC6  5 PRO C 383                                                     
SITE     1 AC7  4 ARG A 400  SER A 401  ARG A 402  HOH A 601                    
SITE     1 AC8  5 ASN A 227  ARG A 276  ARG A 279  HOH A 607                    
SITE     2 AC8  5 HOH A 631                                                     
SITE     1 AC9  6 SER B 121  SER B 123  GLU B 220  HOH B2105                    
SITE     2 AC9  6 HOH B2147  ASP G 410                                          
SITE     1 AD1  6 SER B 123  ASP B 127  ASP B 251  HOH B2102                    
SITE     2 AD1  6 HOH B2104  HOH B2239                                          
SITE     1 AD2  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 AD2  5 GLU B 220                                                     
SITE     1 AD3  5 GLU C 243  ASP C 245  ASP C 247  THR C 250                    
SITE     2 AD3  5 GLU C 252                                                     
SITE     1 AD4  5 ASP C 297  ASN C 299  ASP C 301  ARG C 303                    
SITE     2 AD4  5 ASP C 305                                                     
SITE     1 AD5  6 ASP C 365  ASP C 367  ASP C 369  TYR C 371                    
SITE     2 AD5  6 ASP C 373  HOH C 613                                          
SITE     1 AD6  5 ASP C 426  ASP C 428  ASN C 430  TYR C 432                    
SITE     2 AD6  5 ASP C 434                                                     
SITE     1 AD7  2 ARG C 281  BMA D 506                                          
SITE     1 AD8  3 ALA C  89  ARG C  90  HIS C 112                               
SITE     1 AD9  4 ARG C 400  SER C 401  ARG C 402  HOH C 607                    
SITE     1 AE1  3 SER C 225  ASN C 227  ARG C 276                               
SITE     1 AE2  2 HOH A 879  GLN C 444                                          
SITE     1 AE3  6 SER D 123  ASP D 126  ASP D 127  MET D 335                    
SITE     2 AE3  6 HOH D 611  HOH D 684                                          
SITE     1 AE4  5 ASP D 158  ASN D 215  ASP D 217  PRO D 219                    
SITE     2 AE4  5 GLU D 220                                                     
SITE     1 AE5  8 SER D 121  TYR D 122  SER D 123  ASN D 215                    
SITE     2 AE5  8 GLU D 220  HOH D 601  ASP I 410  HOH I2101                    
SITE     1 AE6  3 SER L  30  SER L  67  GLY L  68                               
SITE     1 AE7  4 ASN B  99  SER B 101  HOH B2152  HOH B2196                    
SITE     1 AE8  9 TRP A 262  ARG A 281  MET A 285  LEU B 317                    
SITE     2 AE8  9 ASN B 320  HOH B2142  HOH B2170  HOH B2186                    
SITE     3 AE8  9 HOH B2199                                                     
SITE     1 AE9  4 ASN B 371  SER B 398  ILE B 399  GLU B 400                    
SITE     1 AF1  4 LYS D  98  ASN D  99  SER D 101  NAG D 508                    
SITE     1 AF2  7 ARG C 281  MAN C 505  ASN D 316  LEU D 317                    
SITE     2 AF2  7 ASN D 320  HOH D 620  HOH D 652                               
SITE     1 AF3  5 ASN D 371  SER D 398  ILE D 399  GLU D 400                    
SITE     2 AF3  5 NAG D 503                                                     
SITE     1 AF4  3 SER B 123  GLY G 409  ASP G 410                               
SITE     1 AF5  2 GLY I 409  ASP I 410                                          
CRYST1  259.440  144.240  104.500  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      0.003854  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006933  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009569        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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