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Database: PDB
Entry: 4Z7N
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HEADER    MEMBRANE PROTEIN/IMMUNE SYSTEM          07-APR-15   4Z7N              
TITLE     INTEGRIN ALPHAIIBBETA3 IN COMPLEX WITH AGDV PEPTIDE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-IIB;                                        
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 32-486;                                       
COMPND   5 SYNONYM: GPALPHA IIB,GPIIB,PLATELET MEMBRANE GLYCOPROTEIN IIB;       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: INTEGRIN BETA-3;                                           
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 29-497;                                       
COMPND  11 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA,GPIIIA;                 
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: MONOCLONAL ANTIBODY 10E5 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 ALA-GLY-ASP-VAL;                              
COMPND  23 CHAIN: G, J;                                                         
COMPND  24 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ITGA2B, GP2B, ITGAB;                                           
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: ITGB3, GP3A;                                                   
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  17 ORGANISM_TAXID: 10090;                                               
SOURCE  18 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  20 MOL_ID: 4;                                                           
SOURCE  21 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  22 ORGANISM_TAXID: 10090;                                               
SOURCE  23 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  25 MOL_ID: 5;                                                           
SOURCE  26 SYNTHETIC: YES;                                                      
SOURCE  27 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  28 ORGANISM_TAXID: 9606                                                 
KEYWDS    CELL ADHESION, PLATELET AGGREGATION, MEMBRANE PROTEIN-IMMUNE SYSTEM   
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.-Y.LIN,J.ZHU,T.A.SPRINGER                                           
REVDAT   3   13-SEP-17 4Z7N    1       JRNL   REMARK                            
REVDAT   2   09-MAR-16 4Z7N    1       JRNL                                     
REVDAT   1   16-DEC-15 4Z7N    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.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10PRE_2104: ???)                           
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.19                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 115448                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1960                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.1980 -  6.2589    1.00     8860   154  0.1953 0.2361        
REMARK   3     2  6.2589 -  4.9694    1.00     8576   150  0.1989 0.2324        
REMARK   3     3  4.9694 -  4.3416    1.00     8497   147  0.1721 0.1773        
REMARK   3     4  4.3416 -  3.9449    1.00     8492   147  0.1900 0.2085        
REMARK   3     5  3.9449 -  3.6622    1.00     8452   147  0.2208 0.2232        
REMARK   3     6  3.6622 -  3.4464    1.00     8406   145  0.2426 0.2854        
REMARK   3     7  3.4464 -  3.2738    1.00     8372   146  0.2605 0.2716        
REMARK   3     8  3.2738 -  3.1313    1.00     8413   146  0.2848 0.3004        
REMARK   3     9  3.1313 -  3.0108    1.00     8348   144  0.3069 0.3392        
REMARK   3    10  3.0108 -  2.9069    1.00     8389   146  0.3334 0.3627        
REMARK   3    11  2.9069 -  2.8160    1.00     8387   146  0.3425 0.3402        
REMARK   3    12  2.8160 -  2.7355    0.97     8118   139  0.3532 0.3578        
REMARK   3    13  2.7355 -  2.6635    0.84     6999   121  0.3818 0.3928        
REMARK   3    14  2.6635 -  2.5985    0.62     5179    82  0.3887 0.4678        
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)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.450           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006          21628                                  
REMARK   3   ANGLE     :  0.493          29304                                  
REMARK   3   CHIRALITY :  0.042           3258                                  
REMARK   3   PLANARITY :  0.003           3791                                  
REMARK   3   DIHEDRAL  :  8.327          12861                                  
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):  48.3647  88.4523  38.5242              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6367 T22:   0.4813                                     
REMARK   3      T33:   0.5467 T12:  -0.0147                                     
REMARK   3      T13:  -0.0118 T23:   0.0625                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.3659 L22:   3.0627                                     
REMARK   3      L33:   7.0365 L12:  -2.0035                                     
REMARK   3      L13:  -3.6573 L23:   1.3118                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1799 S12:   0.0955 S13:  -0.0932                       
REMARK   3      S21:  -0.1108 S22:   0.1184 S23:  -0.0112                       
REMARK   3      S31:   0.6129 S32:  -0.3602 S33:   0.0002                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 45:73)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  39.9540  95.4421  38.7268              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8590 T22:   0.7264                                     
REMARK   3      T33:   0.7182 T12:   0.0432                                     
REMARK   3      T13:   0.0029 T23:   0.1089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6098 L22:   7.3343                                     
REMARK   3      L33:   4.9665 L12:  -2.8126                                     
REMARK   3      L13:  -3.1886 L23:   5.8670                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7025 S12:   0.3244 S13:   0.4377                       
REMARK   3      S21:  -1.4897 S22:  -0.5683 S23:   0.4046                       
REMARK   3      S31:  -1.2621 S32:  -0.8331 S33:  -0.1405                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 74:274)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  41.6039  94.9124  62.5264              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7595 T22:   0.5984                                     
REMARK   3      T33:   0.6565 T12:  -0.0306                                     
REMARK   3      T13:   0.1497 T23:   0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4148 L22:   1.5276                                     
REMARK   3      L33:   1.0951 L12:   0.0228                                     
REMARK   3      L13:   0.1335 L23:   0.1993                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0633 S12:  -0.1055 S13:   0.0303                       
REMARK   3      S21:   0.2801 S22:  -0.0888 S23:   0.3178                       
REMARK   3      S31:   0.1566 S32:  -0.3140 S33:   0.0180                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 275:334)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  66.0915  86.0129  59.8919              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6612 T22:   0.5301                                     
REMARK   3      T33:   0.5835 T12:   0.1328                                     
REMARK   3      T13:   0.0066 T23:   0.0536                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3512 L22:   7.5308                                     
REMARK   3      L33:   4.5130 L12:   2.6919                                     
REMARK   3      L13:  -1.0787 L23:   0.2270                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0176 S12:  -0.2811 S13:  -0.2423                       
REMARK   3      S21:   0.5583 S22:   0.1527 S23:  -0.5164                       
REMARK   3      S31:   0.2751 S32:   0.3606 S33:  -0.1448                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 335:448)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  62.1654  83.1580  45.4439              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6821 T22:   0.5024                                     
REMARK   3      T33:   0.6036 T12:   0.0861                                     
REMARK   3      T13:   0.0924 T23:   0.0145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0069 L22:   2.3787                                     
REMARK   3      L33:   2.7457 L12:   0.7508                                     
REMARK   3      L13:   0.2620 L23:   0.5178                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0719 S12:  -0.0339 S13:  -0.2271                       
REMARK   3      S21:   0.2017 S22:   0.1081 S23:  -0.1559                       
REMARK   3      S31:   0.4693 S32:   0.0396 S33:  -0.0418                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 449:454)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  59.5587  73.0347  32.9653              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0776 T22:   0.9116                                     
REMARK   3      T33:   0.7669 T12:   0.2697                                     
REMARK   3      T13:   0.1925 T23:   0.0545                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5366 L22:   5.3771                                     
REMARK   3      L33:   2.3287 L12:  -2.5775                                     
REMARK   3      L13:   2.6666 L23:   1.5890                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   3.2724 S12:   3.3307 S13:   1.2080                       
REMARK   3      S21:  -3.1397 S22:  -3.4761 S23:  -1.9509                       
REMARK   3      S31:   1.3498 S32:   1.6454 S33:   0.1134                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 3:62)                               
REMARK   3    ORIGIN FOR THE GROUP (A): 122.2456  89.8033  35.1705              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1554 T22:   2.3603                                     
REMARK   3      T33:   1.4076 T12:   0.3488                                     
REMARK   3      T13:  -0.1254 T23:  -0.2307                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9352 L22:   7.4238                                     
REMARK   3      L33:   3.4526 L12:  -3.9003                                     
REMARK   3      L13:  -4.6956 L23:   2.5647                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0115 S12:   0.1761 S13:  -0.2641                       
REMARK   3      S21:  -0.0575 S22:   0.1023 S23:  -1.2937                       
REMARK   3      S31:   0.2513 S32:   1.6436 S33:  -0.0361                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 63:108)                             
REMARK   3    ORIGIN FOR THE GROUP (A): 102.8648 113.7066  52.1048              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9524 T22:   1.4552                                     
REMARK   3      T33:   1.4003 T12:  -0.1741                                     
REMARK   3      T13:  -0.0142 T23:  -0.1540                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4405 L22:   3.5724                                     
REMARK   3      L33:   7.6990 L12:  -1.3757                                     
REMARK   3      L13:  -1.9242 L23:   3.9734                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0289 S12:  -0.1089 S13:   1.0202                       
REMARK   3      S21:   0.1024 S22:   0.6515 S23:  -0.3108                       
REMARK   3      S31:  -0.3415 S32:   1.2642 S33:  -0.8352                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 109:349)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  67.2580 117.9831  63.2586              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8284 T22:   0.5455                                     
REMARK   3      T33:   0.6447 T12:   0.0184                                     
REMARK   3      T13:   0.0660 T23:   0.0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7445 L22:   3.1800                                     
REMARK   3      L33:   1.6262 L12:   0.9118                                     
REMARK   3      L13:  -0.1782 L23:   0.3882                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0715 S12:  -0.3203 S13:   0.3191                       
REMARK   3      S21:   0.3366 S22:  -0.0037 S23:  -0.1502                       
REMARK   3      S31:  -0.3769 S32:   0.1873 S33:  -0.0692                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 350:390)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  96.8425 104.3014  60.2563              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0293 T22:   1.3291                                     
REMARK   3      T33:   1.2516 T12:   0.0940                                     
REMARK   3      T13:  -0.0825 T23:   0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1523 L22:   5.0405                                     
REMARK   3      L33:   8.9748 L12:  -5.1158                                     
REMARK   3      L13:  -7.2734 L23:   6.4581                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8075 S12:  -0.8159 S13:  -0.1500                       
REMARK   3      S21:   0.7667 S22:   0.4042 S23:   0.3957                       
REMARK   3      S31:   0.9972 S32:   1.0879 S33:   0.1545                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 391:432)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  99.9749 104.7315  48.0217              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8002 T22:   1.4002                                     
REMARK   3      T33:   1.1606 T12:   0.0810                                     
REMARK   3      T13:  -0.1151 T23:  -0.0620                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8130 L22:   5.3791                                     
REMARK   3      L33:   8.6851 L12:  -2.0266                                     
REMARK   3      L13:  -4.1158 L23:   4.3328                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3057 S12:   0.0018 S13:   0.0917                       
REMARK   3      S21:   0.0821 S22:   0.0093 S23:  -0.3469                       
REMARK   3      S31:   0.3365 S32:   0.8292 S33:   0.2377                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 433:466)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 115.5868  89.1675  18.7668              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2204 T22:   2.2256                                     
REMARK   3      T33:   1.3537 T12:   0.3171                                     
REMARK   3      T13:   0.1399 T23:   0.0348                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7023 L22:   6.7572                                     
REMARK   3      L33:   7.7263 L12:   0.0300                                     
REMARK   3      L13:  -3.4474 L23:   1.0609                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1553 S12:  -0.7893 S13:  -0.0151                       
REMARK   3      S21:  -0.8637 S22:   0.1663 S23:  -1.2444                       
REMARK   3      S31:   0.4831 S32:   1.4536 S33:  -0.4527                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 1:68)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  87.4892  94.9516 131.4955              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6454 T22:   0.8702                                     
REMARK   3      T33:   0.6735 T12:   0.0336                                     
REMARK   3      T13:   0.0307 T23:  -0.0886                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1428 L22:   6.5890                                     
REMARK   3      L33:   5.7985 L12:   1.2880                                     
REMARK   3      L13:  -1.7045 L23:  -2.0512                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0092 S12:  -0.1102 S13:   0.1116                       
REMARK   3      S21:   0.1912 S22:  -0.0502 S23:  -0.4967                       
REMARK   3      S31:  -0.0377 S32:   0.8130 S33:   0.0242                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 69:274)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  91.7231  90.2413 107.2335              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8828 T22:   1.0982                                     
REMARK   3      T33:   0.8102 T12:   0.0892                                     
REMARK   3      T13:   0.2259 T23:  -0.0258                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6541 L22:   1.5870                                     
REMARK   3      L33:   2.0666 L12:   0.6136                                     
REMARK   3      L13:  -0.0030 L23:  -0.7726                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1558 S12:   0.4681 S13:  -0.0854                       
REMARK   3      S21:  -0.4756 S22:  -0.0576 S23:  -0.4418                       
REMARK   3      S31:   0.4217 S32:   0.6650 S33:   0.1891                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 275:334)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  71.0290  76.0558 115.1831              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0495 T22:   0.6874                                     
REMARK   3      T33:   0.7613 T12:  -0.1306                                     
REMARK   3      T13:   0.1535 T23:  -0.1052                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1907 L22:   4.4262                                     
REMARK   3      L33:   6.4621 L12:  -3.9795                                     
REMARK   3      L13:  -0.7461 L23:   0.5975                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0562 S12:   0.5655 S13:  -0.8124                       
REMARK   3      S21:  -0.4633 S22:   0.0146 S23:   0.2710                       
REMARK   3      S31:   1.0349 S32:  -0.2421 S33:   0.1028                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 335:399)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  72.5167  76.5272 125.9979              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9313 T22:   0.6875                                     
REMARK   3      T33:   0.7593 T12:   0.0459                                     
REMARK   3      T13:   0.1649 T23:   0.0033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7281 L22:   3.0800                                     
REMARK   3      L33:   3.7595 L12:  -1.1051                                     
REMARK   3      L13:  -0.2420 L23:  -0.3897                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3028 S12:  -0.1513 S13:  -0.7217                       
REMARK   3      S21:  -0.0598 S22:   0.1876 S23:  -0.1357                       
REMARK   3      S31:   0.9781 S32:   0.0117 S33:   0.0806                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 400:428)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  75.2167  85.0353 132.2284              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7708 T22:   0.7279                                     
REMARK   3      T33:   0.5904 T12:   0.0284                                     
REMARK   3      T13:   0.0992 T23:   0.0305                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9366 L22:   4.4467                                     
REMARK   3      L33:   4.4813 L12:  -0.8754                                     
REMARK   3      L13:   0.9080 L23:  -0.9623                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2697 S12:  -0.0568 S13:  -0.2808                       
REMARK   3      S21:  -0.2122 S22:   0.1235 S23:   0.1660                       
REMARK   3      S31:   0.7441 S32:   0.2935 S33:   0.1406                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 429:453)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  81.5819  85.9104 136.5826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6476 T22:   0.8365                                     
REMARK   3      T33:   0.6813 T12:   0.0891                                     
REMARK   3      T13:   0.0886 T23:  -0.0817                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3123 L22:   7.0941                                     
REMARK   3      L33:   7.0916 L12:  -2.2105                                     
REMARK   3      L13:   1.1014 L23:  -3.7891                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2632 S12:  -0.3490 S13:  -0.4120                       
REMARK   3      S21:   0.5048 S22:   0.2713 S23:  -0.2205                       
REMARK   3      S31:   0.4160 S32:   0.3430 S33:  -0.0283                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 3:50)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  15.5018  69.1878 141.1737              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4448 T22:   1.9409                                     
REMARK   3      T33:   1.2864 T12:  -0.5568                                     
REMARK   3      T13:   0.2601 T23:  -0.0993                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9274 L22:   7.8361                                     
REMARK   3      L33:   8.6354 L12:   1.1777                                     
REMARK   3      L13:  -5.1305 L23:  -1.8193                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8274 S12:   0.5820 S13:  -0.6753                       
REMARK   3      S21:   0.1686 S22:   0.0503 S23:   0.8233                       
REMARK   3      S31:   1.5619 S32:  -1.5639 S33:   0.7689                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 51:176)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  43.9201  98.4268 105.0006              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0245 T22:   1.2264                                     
REMARK   3      T33:   0.7767 T12:  -0.1948                                     
REMARK   3      T13:  -0.0299 T23:   0.0199                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2244 L22:   1.3665                                     
REMARK   3      L33:   3.0298 L12:   0.9669                                     
REMARK   3      L13:  -1.1252 L23:  -1.0785                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1420 S12:   1.0218 S13:   0.6334                       
REMARK   3      S21:  -0.1998 S22:   0.3569 S23:   0.4273                       
REMARK   3      S31:   0.1329 S32:  -1.0973 S33:  -0.1964                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 177:353)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  60.0728 100.7889 101.2723              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8491 T22:   0.9948                                     
REMARK   3      T33:   0.6470 T12:  -0.1374                                     
REMARK   3      T13:   0.0458 T23:   0.0989                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7483 L22:   1.9882                                     
REMARK   3      L33:   4.7881 L12:   0.1039                                     
REMARK   3      L13:   1.6184 L23:  -0.6926                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2298 S12:   0.6173 S13:   0.3628                       
REMARK   3      S21:  -0.4280 S22:   0.2426 S23:  -0.0211                       
REMARK   3      S31:  -0.0778 S32:  -0.3928 S33:  -0.0267                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 354:440)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  32.8114  84.3298 118.3520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0346 T22:   1.3771                                     
REMARK   3      T33:   0.9818 T12:  -0.2351                                     
REMARK   3      T13:  -0.0185 T23:   0.0178                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7731 L22:   3.6389                                     
REMARK   3      L33:   5.0897 L12:   2.2622                                     
REMARK   3      L13:  -1.0531 L23:  -1.0403                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3468 S12:   0.7012 S13:  -0.3378                       
REMARK   3      S21:  -0.0091 S22:   0.2834 S23:  -0.0221                       
REMARK   3      S31:   0.7381 S32:  -0.1913 S33:   0.1493                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 441:465)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  19.9430  78.9416 156.9040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4154 T22:   1.6245                                     
REMARK   3      T33:   1.2851 T12:  -0.1587                                     
REMARK   3      T13:   0.3141 T23:  -0.2302                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.9995 L22:   7.5363                                     
REMARK   3      L33:   6.4548 L12:   2.3698                                     
REMARK   3      L13:   7.8733 L23:   0.9611                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5080 S12:  -0.7985 S13:   0.1389                       
REMARK   3      S21:   0.5400 S22:   0.0231 S23:   0.7757                       
REMARK   3      S31:   1.0909 S32:  -1.8710 S33:   0.5261                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 466:471)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  29.1534  72.4174 158.7455              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1642 T22:   1.2448                                     
REMARK   3      T33:   2.0543 T12:  -0.1086                                     
REMARK   3      T13:  -0.0128 T23:   0.0418                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6788 L22:   3.0475                                     
REMARK   3      L33:   6.3169 L12:   3.6727                                     
REMARK   3      L13:   5.3788 L23:   4.3671                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6519 S12:   0.2219 S13:  -4.2475                       
REMARK   3      S21:   2.2346 S22:   0.7815 S23:   0.9309                       
REMARK   3      S31:   2.2767 S32:  -0.9640 S33:  -1.4724                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 1:15)                               
REMARK   3    ORIGIN FOR THE GROUP (A): 119.6216  82.6083  83.3597              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4810 T22:   1.1990                                     
REMARK   3      T33:   1.2897 T12:   0.0000                                     
REMARK   3      T13:   0.2469 T23:  -0.0254                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3273 L22:   4.3005                                     
REMARK   3      L33:   9.2437 L12:  -2.9833                                     
REMARK   3      L13:   4.1906 L23:  -1.5853                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3219 S12:   0.5450 S13:  -0.8316                       
REMARK   3      S21:  -0.5718 S22:  -0.2925 S23:   0.0881                       
REMARK   3      S31:   1.8974 S32:   0.6646 S33:  -0.1772                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 16:22)                              
REMARK   3    ORIGIN FOR THE GROUP (A): 114.9261  84.9319  78.0284              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6808 T22:   1.6256                                     
REMARK   3      T33:   0.9979 T12:   0.0786                                     
REMARK   3      T13:   0.1719 T23:  -0.0573                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1749 L22:   6.4544                                     
REMARK   3      L33:   5.0134 L12:  -1.4160                                     
REMARK   3      L13:   6.3702 L23:  -0.5881                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3685 S12:   0.7756 S13:   0.7555                       
REMARK   3      S21:  -2.1661 S22:  -1.2198 S23:   0.8036                       
REMARK   3      S31:   1.5164 S32:   0.4338 S33:   1.1876                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 23:64)                              
REMARK   3    ORIGIN FOR THE GROUP (A): 111.6571  92.9801  87.5214              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0470 T22:   1.2946                                     
REMARK   3      T33:   0.9944 T12:  -0.0382                                     
REMARK   3      T13:   0.2843 T23:   0.0733                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7887 L22:   5.3498                                     
REMARK   3      L33:   6.9373 L12:  -4.6639                                     
REMARK   3      L13:   1.7979 L23:   1.3683                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1081 S12:  -0.0298 S13:   0.2376                       
REMARK   3      S21:  -0.9421 S22:  -0.0364 S23:  -0.2591                       
REMARK   3      S31:   0.9062 S32:  -0.2241 S33:  -0.1992                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 65:119)                             
REMARK   3    ORIGIN FOR THE GROUP (A): 114.8838  89.7009  85.2655              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1551 T22:   1.5581                                     
REMARK   3      T33:   1.0912 T12:  -0.0284                                     
REMARK   3      T13:   0.3616 T23:   0.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2371 L22:   4.4350                                     
REMARK   3      L33:   4.5757 L12:  -0.8519                                     
REMARK   3      L13:  -0.0447 L23:   0.3716                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0950 S12:   0.6760 S13:   0.0241                       
REMARK   3      S21:  -0.6573 S22:  -0.2537 S23:  -0.3899                       
REMARK   3      S31:   0.8789 S32:  -0.2670 S33:   0.4120                       
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 120:170)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 148.8460  82.1842  79.1160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5999 T22:   2.4659                                     
REMARK   3      T33:   1.6639 T12:   0.4860                                     
REMARK   3      T13:   0.2609 T23:   0.0676                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1109 L22:   3.7074                                     
REMARK   3      L33:   2.7128 L12:  -0.7468                                     
REMARK   3      L13:   0.1345 L23:   0.7671                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3800 S12:   0.9644 S13:  -0.1139                       
REMARK   3      S21:  -0.5688 S22:  -0.2254 S23:  -1.0678                       
REMARK   3      S31:   0.5569 S32:   1.3611 S33:  -0.1465                       
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 171:219)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 149.8738  80.8543  78.7600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9299 T22:   2.6531                                     
REMARK   3      T33:   1.6231 T12:   0.7412                                     
REMARK   3      T13:   0.1857 T23:  -0.1282                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6719 L22:   4.0326                                     
REMARK   3      L33:   3.3616 L12:  -2.8284                                     
REMARK   3      L13:   1.9449 L23:   1.5253                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   2.0527 S12:   1.3617 S13:   0.9150                       
REMARK   3      S21:  -0.8356 S22:  -0.9037 S23:  -0.5067                       
REMARK   3      S31:   1.2086 S32:   1.9672 S33:  -1.0109                       
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 1:11)                               
REMARK   3    ORIGIN FOR THE GROUP (A): 126.1923 106.9955  95.3924              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1909 T22:   1.4071                                     
REMARK   3      T33:   1.9571 T12:  -0.1864                                     
REMARK   3      T13:   0.5391 T23:  -0.0597                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.6512 L22:   4.3837                                     
REMARK   3      L33:   4.9038 L12:  -0.7563                                     
REMARK   3      L13:   2.3858 L23:  -1.4155                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0205 S12:   0.7385 S13:   1.9767                       
REMARK   3      S21:  -0.3329 S22:   0.0074 S23:  -1.2464                       
REMARK   3      S31:  -0.7730 S32:   1.4421 S33:   0.0779                       
REMARK   3   TLS GROUP : 32                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 12:24)                              
REMARK   3    ORIGIN FOR THE GROUP (A): 133.0694 102.3153 105.9041              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0267 T22:   1.6695                                     
REMARK   3      T33:   1.9131 T12:  -0.0970                                     
REMARK   3      T13:  -0.1225 T23:  -0.0916                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3312 L22:   8.9159                                     
REMARK   3      L33:   7.1440 L12:  -8.0890                                     
REMARK   3      L13:   4.0666 L23:  -5.1886                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4559 S12:  -0.3803 S13:   2.5543                       
REMARK   3      S21:   0.5805 S22:   0.3315 S23:  -1.5835                       
REMARK   3      S31:   0.9584 S32:  -0.2062 S33:   0.2326                       
REMARK   3   TLS GROUP : 33                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 25:102)                             
REMARK   3    ORIGIN FOR THE GROUP (A): 122.0738  98.5214 101.7476              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9364 T22:   1.6365                                     
REMARK   3      T33:   1.3025 T12:  -0.0721                                     
REMARK   3      T13:   0.2309 T23:  -0.0590                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9291 L22:   3.4837                                     
REMARK   3      L33:   2.9453 L12:  -2.6223                                     
REMARK   3      L13:   2.2276 L23:  -0.6170                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3068 S12:  -0.1028 S13:   0.8002                       
REMARK   3      S21:   0.2632 S22:  -0.0399 S23:  -0.9106                       
REMARK   3      S31:   0.1995 S32:   0.5019 S33:   0.2738                       
REMARK   3   TLS GROUP : 34                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 103:118)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 149.7989  96.7763  93.8993              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0752 T22:   2.8445                                     
REMARK   3      T33:   2.2367 T12:   0.1470                                     
REMARK   3      T13:   0.1883 T23:   0.1269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1214 L22:   0.8427                                     
REMARK   3      L33:   1.8131 L12:   0.5931                                     
REMARK   3      L13:  -0.9371 L23:   0.0015                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0544 S12:   1.4747 S13:   0.5287                       
REMARK   3      S21:  -0.1968 S22:  -0.4105 S23:  -0.6032                       
REMARK   3      S31:   0.2593 S32:   1.3693 S33:  -0.0035                       
REMARK   3   TLS GROUP : 35                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 119:164)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 151.3908  97.1663  77.7093              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6985 T22:   2.2631                                     
REMARK   3      T33:   1.7633 T12:   0.0450                                     
REMARK   3      T13:   0.4174 T23:   0.3499                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1737 L22:   3.7875                                     
REMARK   3      L33:   8.7482 L12:   0.6161                                     
REMARK   3      L13:   0.1320 L23:   1.5364                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0700 S12:   0.5423 S13:  -0.1607                       
REMARK   3      S21:  -0.6513 S22:  -0.4752 S23:  -0.6831                       
REMARK   3      S31:  -0.7399 S32:   3.2119 S33:   0.3812                       
REMARK   3   TLS GROUP : 36                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 165:214)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 155.4517  97.8492  79.0581              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5783 T22:   2.7252                                     
REMARK   3      T33:   2.1513 T12:  -0.1365                                     
REMARK   3      T13:   0.3513 T23:   0.4634                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9218 L22:   1.7008                                     
REMARK   3      L33:   4.5697 L12:   1.2027                                     
REMARK   3      L13:  -3.0636 L23:   0.0054                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0286 S12:   0.8534 S13:   1.0433                       
REMARK   3      S21:  -0.9328 S22:   0.4887 S23:  -0.9872                       
REMARK   3      S31:   0.1143 S32:   0.8844 S33:  -0.5934                       
REMARK   3   TLS GROUP : 37                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 1:31)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  19.5709  89.9312  85.7094              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3865 T22:   1.4370                                     
REMARK   3      T33:   1.1243 T12:   0.1730                                     
REMARK   3      T13:   0.0862 T23:   0.0295                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6748 L22:   4.4155                                     
REMARK   3      L33:   7.4723 L12:  -3.7352                                     
REMARK   3      L13:  -5.1092 L23:   5.1017                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6804 S12:  -1.1828 S13:  -0.6091                       
REMARK   3      S21:   1.6251 S22:   0.4389 S23:   0.0574                       
REMARK   3      S31:   1.9632 S32:   0.5387 S33:   0.1609                       
REMARK   3   TLS GROUP : 38                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 32:64)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  17.7624 101.5832  79.8590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9040 T22:   1.0133                                     
REMARK   3      T33:   0.8806 T12:   0.0815                                     
REMARK   3      T13:   0.2259 T23:  -0.0698                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5348 L22:   4.5407                                     
REMARK   3      L33:   3.8754 L12:   2.9041                                     
REMARK   3      L13:   2.6693 L23:   0.4348                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1562 S12:  -0.2628 S13:   0.4176                       
REMARK   3      S21:   0.4104 S22:   0.0189 S23:   0.4458                       
REMARK   3      S31:  -0.2598 S32:  -0.1673 S33:  -0.2524                       
REMARK   3   TLS GROUP : 39                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 65:120)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3596  95.9802  83.2240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0042 T22:   1.1518                                     
REMARK   3      T33:   0.8592 T12:   0.1185                                     
REMARK   3      T13:   0.1773 T23:   0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8796 L22:   3.8094                                     
REMARK   3      L33:   5.3267 L12:   0.5736                                     
REMARK   3      L13:  -3.6512 L23:   0.0595                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1663 S12:  -1.0935 S13:   0.0603                       
REMARK   3      S21:   0.9866 S22:   0.1404 S23:   0.3047                       
REMARK   3      S31:   0.0005 S32:  -0.0943 S33:   0.0980                       
REMARK   3   TLS GROUP : 40                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 121:151)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -16.8174  83.4341  95.1219              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1854 T22:   1.4719                                     
REMARK   3      T33:   1.8612 T12:   0.2010                                     
REMARK   3      T13:   0.4595 T23:   0.5050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3296 L22:   4.1506                                     
REMARK   3      L33:   3.5683 L12:   3.3018                                     
REMARK   3      L13:   2.6202 L23:   1.2848                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2350 S12:  -1.4249 S13:  -2.4458                       
REMARK   3      S21:   0.6222 S22:   0.2507 S23:   0.2748                       
REMARK   3      S31:   0.4500 S32:  -0.4905 S33:   0.0800                       
REMARK   3   TLS GROUP : 41                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 152:179)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.1913  82.2904  90.6956              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8866 T22:   1.5599                                     
REMARK   3      T33:   2.1106 T12:   0.3088                                     
REMARK   3      T13:   0.3613 T23:   0.3073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7421 L22:   7.7387                                     
REMARK   3      L33:   4.9437 L12:   6.8160                                     
REMARK   3      L13:   2.6021 L23:   2.4972                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4259 S12:  -0.2892 S13:  -1.1848                       
REMARK   3      S21:   0.9944 S22:   0.3611 S23:   0.6966                       
REMARK   3      S31:   0.9022 S32:   0.8620 S33:  -0.0219                       
REMARK   3   TLS GROUP : 42                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 180:219)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -15.3559  77.1154  94.6312              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3039 T22:   1.2789                                     
REMARK   3      T33:   2.3218 T12:   0.1109                                     
REMARK   3      T13:   0.4060 T23:   0.5248                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9681 L22:   2.0992                                     
REMARK   3      L33:   9.2851 L12:   3.7846                                     
REMARK   3      L13:   3.3945 L23:   2.7654                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2624 S12:  -0.5238 S13:  -1.7049                       
REMARK   3      S21:   0.4220 S22:  -0.2406 S23:   0.0522                       
REMARK   3      S31:   1.8217 S32:  -0.3087 S33:  -0.0537                       
REMARK   3   TLS GROUP : 43                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 1:27)                               
REMARK   3    ORIGIN FOR THE GROUP (A):   1.4903  99.4013  63.4689              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8572 T22:   1.4056                                     
REMARK   3      T33:   1.2726 T12:   0.1555                                     
REMARK   3      T13:   0.1278 T23:  -0.1269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2953 L22:   8.6842                                     
REMARK   3      L33:   1.3904 L12:   4.8016                                     
REMARK   3      L13:   0.6357 L23:   1.1004                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2117 S12:   0.8153 S13:   0.7968                       
REMARK   3      S21:   0.4115 S22:  -0.0246 S23:   1.6214                       
REMARK   3      S31:   0.0965 S32:  -0.7181 S33:  -0.0450                       
REMARK   3   TLS GROUP : 44                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 28:71)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  11.5019  93.5135  63.3695              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7110 T22:   1.1669                                     
REMARK   3      T33:   0.9371 T12:  -0.0266                                     
REMARK   3      T13:   0.1047 T23:  -0.0788                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7986 L22:   5.4234                                     
REMARK   3      L33:   3.0033 L12:  -1.1287                                     
REMARK   3      L13:   1.1559 L23:   0.9530                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1591 S12:   0.6977 S13:  -0.4182                       
REMARK   3      S21:  -0.2553 S22:  -0.0243 S23:   0.5576                       
REMARK   3      S31:   0.1995 S32:  -0.6454 S33:   0.1916                       
REMARK   3   TLS GROUP : 45                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 72:106)                             
REMARK   3    ORIGIN FOR THE GROUP (A):   5.6225  94.5579  66.7339              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7504 T22:   1.2854                                     
REMARK   3      T33:   1.0469 T12:  -0.0233                                     
REMARK   3      T13:   0.1522 T23:  -0.0802                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7801 L22:   5.8406                                     
REMARK   3      L33:   4.8367 L12:   1.2430                                     
REMARK   3      L13:  -0.6626 L23:   2.8982                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2289 S12:  -0.0511 S13:  -0.1986                       
REMARK   3      S21:   0.2906 S22:  -0.5998 S23:   0.9273                       
REMARK   3      S31:   0.4305 S32:  -1.1078 S33:   0.4059                       
REMARK   3   TLS GROUP : 46                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 107:145)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -19.7673  88.6789  84.8444              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8125 T22:   1.2919                                     
REMARK   3      T33:   1.6264 T12:   0.0914                                     
REMARK   3      T13:   0.2732 T23:   0.0695                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8871 L22:   1.9647                                     
REMARK   3      L33:   1.8592 L12:   0.0336                                     
REMARK   3      L13:   2.5956 L23:   0.7365                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6260 S12:  -0.0668 S13:  -1.2052                       
REMARK   3      S21:   0.2425 S22:   0.2104 S23:   0.3023                       
REMARK   3      S31:   0.0390 S32:   0.0513 S33:   0.2815                       
REMARK   3   TLS GROUP : 47                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 146:182)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -17.4696  93.8324  85.0241              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6808 T22:   1.3645                                     
REMARK   3      T33:   1.4431 T12:  -0.0128                                     
REMARK   3      T13:   0.1188 T23:   0.3663                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0794 L22:   3.5135                                     
REMARK   3      L33:   6.0252 L12:   0.4616                                     
REMARK   3      L13:   1.8749 L23:   1.6579                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1667 S12:  -0.6780 S13:  -0.8844                       
REMARK   3      S21:  -0.5048 S22:   0.3330 S23:  -0.0387                       
REMARK   3      S31:  -0.7688 S32:   0.3984 S33:  -0.0666                       
REMARK   3   TLS GROUP : 48                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 183:214)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -28.6454  94.6358  89.9801              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0060 T22:   1.3559                                     
REMARK   3      T33:   1.6196 T12:   0.1775                                     
REMARK   3      T13:   0.1523 T23:  -0.0084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2386 L22:   1.5031                                     
REMARK   3      L33:   8.5981 L12:   0.8332                                     
REMARK   3      L13:  -0.8143 L23:   1.2189                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2315 S12:  -0.1946 S13:  -0.4216                       
REMARK   3      S21:   0.1898 S22:  -0.2008 S23:   0.5413                       
REMARK   3      S31:   0.0504 S32:  -1.2569 S33:   0.4292                       
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 4Z7N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000208765.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332                             
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   : 139660                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.599                              
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     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.5100                             
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   (%): 62.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27                     
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      128.44150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.18650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      128.44150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.18650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L, G                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F, J                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU B   467                                                      
REMARK 465     GLY B   468                                                      
REMARK 465     SER B   469                                                      
REMARK 465     GLN B   470                                                      
REMARK 465     CYS B   471                                                      
REMARK 465     VAL C   454                                                      
REMARK 465     LYS C   455                                                      
REMARK 465     GLY E   135                                                      
REMARK 465     ASP E   136                                                      
REMARK 465     THR E   137                                                      
REMARK 465     GLY 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 A   61   CD                                                  
REMARK 480     MET B  118   CE                                                  
REMARK 480     LYS D  350   CD   CE   NZ                                        
REMARK 480     CYS F  194   SG                                                  
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   H    SER A    29     OE2  GLU A   136              1.55            
REMARK 500   HG   SER A   173     O    HOH A   626              1.57            
REMARK 500   O    GLY H   110     HG   SER L    43              1.59            
REMARK 500   HH   TYR C   448     O    HOH C   611              1.60            
REMARK 500   O    HOH D  2115     O    HOH D  2136              1.84            
REMARK 500   O    HOH A   663     O    HOH A   910              1.84            
REMARK 500   O    HOH A   866     O    HOH A   886              1.84            
REMARK 500   O    HOH A   749     O    HOH A   841              1.84            
REMARK 500   O    HOH A   663     O    HOH A   749              1.86            
REMARK 500   O    HOH A   770     O    HOH A   839              1.90            
REMARK 500   OD1  ASP C   245     OE1  GLU C   252              1.90            
REMARK 500   O    HOH A   893     O    HOH B  2213              1.91            
REMARK 500   O    HOH A   903     O    HOH B  2244              1.93            
REMARK 500   O    HOH A   886     O    HOH A   917              1.94            
REMARK 500   O    HOH A   733     O    HOH A   755              1.95            
REMARK 500   O    HOH B  2149     O    HOH B  2208              1.97            
REMARK 500   O    HOH A   735     O    HOH A   771              1.97            
REMARK 500   O    HOH A   877     O    HOH B  2220              1.99            
REMARK 500   O    HOH A   803     O    HOH B  2159              1.99            
REMARK 500   O    HOH D  2133     O    HOH D  2144              1.99            
REMARK 500   ND2  ASN D   320     O5   NAG D  2005              2.00            
REMARK 500   O    HOH D  2105     O    HOH D  2134              2.00            
REMARK 500   O    HOH A   805     O    HOH A   902              2.00            
REMARK 500   O    HOH C   712     O    HOH D  2126              2.00            
REMARK 500   O    HOH C   683     O    HOH C   721              2.00            
REMARK 500   O    HOH B  2135     O    HOH B  2148              2.00            
REMARK 500   O    HOH A   866     O    HOH A   917              2.00            
REMARK 500   O    HOH A   803     O    HOH B  2239              2.01            
REMARK 500   OD1  ASP A   245     OE1  GLU A   252              2.01            
REMARK 500   OE2  GLU C   243     OD1  ASP C   245              2.01            
REMARK 500   OD2  ASP A   369     O    HOH A   601              2.02            
REMARK 500   O    HOH A   659     O    HOH A   839              2.02            
REMARK 500   O    HOH A   841     O    HOH A   910              2.03            
REMARK 500   O    HOH A   659     O    HOH A   770              2.03            
REMARK 500   OE2  GLU A   243     OD1  ASP A   245              2.04            
REMARK 500   O    HOH B  2173     O    HOH B  2204              2.05            
REMARK 500   O    HOH C   648     O    HOH C   709              2.06            
REMARK 500   O    HOH C   662     O    HOH C   697              2.06            
REMARK 500   O    HOH B  2205     O    HOH B  2223              2.06            
REMARK 500   O    HOH C   650     O    HOH C   719              2.06            
REMARK 500   O    HOH A   884     O    HOH A   918              2.06            
REMARK 500   O    HOH C   688     O    HOH C   722              2.07            
REMARK 500   O    HOH A   909     O    HOH B  2159              2.07            
REMARK 500   O    HOH A   603     O    HOH A   861              2.07            
REMARK 500   O    HOH A   615     O    HOH A   812              2.07            
REMARK 500   O    HOH A   909     O    HOH B  2239              2.08            
REMARK 500   O    HOH A   663     O    HOH A   841              2.08            
REMARK 500   O    HOH B  2176     O    HOH B  2224              2.08            
REMARK 500   ND2  ASN B    99     O5   NAG B  2004              2.08            
REMARK 500   O4   NAG B  2010     C2   NAG B  2011              2.09            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     103 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   605     O    HOH C   632     1554     2.13            
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 101     -136.92     56.66                                   
REMARK 500    ASP A 102       35.44    -97.86                                   
REMARK 500    LYS A 118     -119.71     62.91                                   
REMARK 500    GLU A 123      136.09     83.81                                   
REMARK 500    ALA A 198      143.24   -172.85                                   
REMARK 500    LEU A 212      -49.67     70.51                                   
REMARK 500    SER A 222     -166.06    -76.97                                   
REMARK 500    ALA A 310       78.07   -118.36                                   
REMARK 500    PRO A 337       95.00    -67.47                                   
REMARK 500    THR A 350      -33.96   -131.55                                   
REMARK 500    ARG A 422      131.82   -172.22                                   
REMARK 500    ALA B  61       81.79   -167.17                                   
REMARK 500    ASP B  76      164.84     63.83                                   
REMARK 500    SER B  77       50.29    -95.29                                   
REMARK 500    VAL B 157      -89.06   -137.42                                   
REMARK 500    PRO B 160       73.70    -69.05                                   
REMARK 500    THR B 182     -165.30   -107.49                                   
REMARK 500    SER B 213     -155.54   -117.16                                   
REMARK 500    LEU B 258       -1.37     79.54                                   
REMARK 500    LEU B 333       61.17   -102.35                                   
REMARK 500    SER B 334     -153.96    -94.13                                   
REMARK 500    SER B 337     -166.70   -172.58                                   
REMARK 500    ASN B 339      128.00   -176.87                                   
REMARK 500    LEU B 341       -1.46     65.93                                   
REMARK 500    LEU B 375     -127.48     58.03                                   
REMARK 500    SER C 101     -137.17     56.52                                   
REMARK 500    ASP C 102       30.01    -96.92                                   
REMARK 500    LYS C 118     -111.02     59.24                                   
REMARK 500    GLU C 123      132.80     77.37                                   
REMARK 500    TYR C 143      110.25   -164.97                                   
REMARK 500    ALA C 198      133.91   -175.01                                   
REMARK 500    LEU C 212      -42.81     72.41                                   
REMARK 500    SER C 220      115.91   -160.25                                   
REMARK 500    TRP C 235       96.50    -65.57                                   
REMARK 500    VAL C 325      -32.00   -135.25                                   
REMARK 500    TYR C 353       15.45     59.92                                   
REMARK 500    ARG C 422      134.94   -170.06                                   
REMARK 500    ALA C 439       79.69   -154.25                                   
REMARK 500    THR D   7       46.21    -83.25                                   
REMARK 500    PHE D  56       81.49   -153.36                                   
REMARK 500    LEU D  64      -75.78    -99.57                                   
REMARK 500    ASP D  66       76.50   -155.67                                   
REMARK 500    VAL D 157      -81.35   -140.33                                   
REMARK 500    PRO D 160       75.00    -68.28                                   
REMARK 500    CYS D 177       45.52    -90.19                                   
REMARK 500    LYS D 181       39.63    -87.56                                   
REMARK 500    VAL D 193      -74.30    -89.99                                   
REMARK 500    SER D 213     -153.31   -126.14                                   
REMARK 500    ASP D 241       74.82   -115.20                                   
REMARK 500    ALA D 242      144.80   -171.15                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      74 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU B  341     GLN B  342                  138.50                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 243   OE1                                                    
REMARK 620 2 GLU A 243   OE2  56.3                                              
REMARK 620 3 ASP A 245   OD1 109.2  52.9                                        
REMARK 620 4 ASP A 247   O    73.4  67.1  82.4                                  
REMARK 620 5 THR A 250   O    70.0 126.2 178.2  95.9                            
REMARK 620 6 THR A 250   OG1 141.9 135.3  94.2  80.7  85.7                      
REMARK 620 7 GLU A 252   OE1  94.3  62.5  51.3 125.5 130.1 123.7                
REMARK 620 8 GLU A 252   OE2 121.2 117.8  90.0 165.3  91.7  87.3  55.6          
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  71.2                                              
REMARK 620 3 ASP A 301   OD1  76.3  79.8                                        
REMARK 620 4 ARG A 303   O    82.0 152.4  87.9                                  
REMARK 620 5 ASP A 305   OD1 138.9 119.4 142.1  85.1                            
REMARK 620 6 ASP A 305   OD2  96.0  78.2 158.0 111.7  53.6                      
REMARK 620 7 HOH A 617   O   147.0  84.9  77.5 116.6  72.7 101.0                
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  90.9                                              
REMARK 620 3 ASP A 369   OD1  72.1  75.1                                        
REMARK 620 4 TYR A 371   O    64.4 152.9  86.1                                  
REMARK 620 5 ASP A 373   OD1 147.1 106.5 138.7 100.5                            
REMARK 620 6 ASP A 373   OD2  95.5 100.2 166.5  93.5  54.6                      
REMARK 620 7 HOH A 601   O   128.2  86.5  57.2  99.8  81.5 135.8                
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  63.9                                              
REMARK 620 3 ASN A 430   OD1  76.3  74.1                                        
REMARK 620 4 TYR A 432   O    73.4 136.6  89.7                                  
REMARK 620 5 ASP A 434   OD1 143.7 122.3 139.5  96.3                            
REMARK 620 6 ASP A 434   OD2  93.5  81.6 155.7 108.8  56.2                      
REMARK 620 7 HOH A 607   O   132.4  77.4  66.8 132.8  80.3 107.8                
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   90.9                                              
REMARK 620 3 GLU B 220   OE2  86.7 174.8                                        
REMARK 620 4 ASP G 410   OD1 100.3  94.3  81.5                                  
REMARK 620 5 HOH B2146   O   166.2 102.4  80.3  82.6                            
REMARK 620 6 HOH B2114   O    82.0  74.1 110.2 168.3  98.0                      
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 126   OD1  80.3                                              
REMARK 620 3 ASP B 127   OD2 114.5  78.4                                        
REMARK 620 4 ASP B 251   OD2  84.2 164.3 106.2                                  
REMARK 620 5 HOH G 501   O    79.9 100.5 164.8  79.1                            
REMARK 620 6 HOH B2168   O   159.0 103.1  86.4  92.3  79.0                      
REMARK 620 N                    1     2     3     4     5                       
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 100.8                                              
REMARK 620 3 ASP B 217   O   164.9  84.8                                        
REMARK 620 4 ASP B 217   OD1  96.0  85.6  70.3                                  
REMARK 620 5 PRO B 219   O    79.8 173.0  96.4 101.3                            
REMARK 620 6 GLU B 220   OE1  93.9  84.7 100.5 167.2  88.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 243   OE1                                                    
REMARK 620 2 GLU C 243   OE2  56.3                                              
REMARK 620 3 ASP C 245   OD1 107.1  51.4                                        
REMARK 620 4 ASP C 247   O    74.4  63.7  82.4                                  
REMARK 620 5 THR C 250   O    70.5 124.3 171.2  88.8                            
REMARK 620 6 THR C 250   OG1 145.0 127.2  90.3  78.2  87.7                      
REMARK 620 7 GLU C 252   OE1  95.6  65.8  47.9 124.6 139.8 118.0                
REMARK 620 8 GLU C 252   OE2 120.5 121.5  90.7 164.9  97.8  88.5  56.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 297   OD1                                                    
REMARK 620 2 ASN C 299   OD1  69.3                                              
REMARK 620 3 ASP C 301   OD1  65.8  61.3                                        
REMARK 620 4 ARG C 303   O    77.2 145.3  96.9                                  
REMARK 620 5 ASP C 305   OD1 145.1 103.6 142.5 109.1                            
REMARK 620 6 ASP C 305   OD2  89.8  88.6 146.0 100.4  55.4                      
REMARK 620 7 HOH C 613   O   148.6  88.6  84.3 117.6  60.0 112.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 505  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 365   OD1                                                    
REMARK 620 2 ASP C 367   OD1  81.0                                              
REMARK 620 3 ASP C 369   OD1  67.0  65.7                                        
REMARK 620 4 TYR C 371   O    69.2 147.2  89.4                                  
REMARK 620 5 ASP C 373   OD1 153.4 114.5 138.2  98.3                            
REMARK 620 6 ASP C 373   OD2 101.7 102.6 164.2  96.9  55.2                      
REMARK 620 7 HOH C 614   O   133.0  95.5  68.9  94.9  69.5 124.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 506  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 426   OD1                                                    
REMARK 620 2 ASP C 428   OD1  56.6                                              
REMARK 620 3 ASN C 430   OD1  81.6  74.4                                        
REMARK 620 4 TYR C 432   O    82.6 138.7  95.5                                  
REMARK 620 5 ASP C 434   OD1 147.2 118.0 130.2  99.2                            
REMARK 620 6 ASP C 434   OD2  93.2  76.5 148.1 115.1  56.2                      
REMARK 620 7 HOH C 602   O   126.2  76.4  60.2 133.4  75.7 100.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D2001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER D 121   OG                                                     
REMARK 620 2 GLU D 220   OE2 129.3                                              
REMARK 620 3 ASP J 410   OD1 111.8 117.0                                        
REMARK 620 4 HOH D2105   O   136.4  61.9  85.8                                  
REMARK 620 5 HOH D2134   O    82.6  83.9 121.0  55.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D2002  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER D 123   O                                                      
REMARK 620 2 ASP D 126   OD1 123.2                                              
REMARK 620 3 ASP D 127   OD1 127.6  53.7                                        
REMARK 620 4 MET D 335   O   151.0  85.7  70.0                                  
REMARK 620 5 HOH D2115   O    92.3 141.2 118.7  59.2                            
REMARK 620 6 HOH D2136   O    90.0 109.6 142.5  75.8  49.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D2003  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 158   OD2                                                    
REMARK 620 2 ASN D 215   OD1 103.1                                              
REMARK 620 3 ASP D 217   O   159.0  76.7                                        
REMARK 620 4 ASP D 217   OD1  86.2  78.4  73.1                                  
REMARK 620 5 PRO D 219   O    76.3 173.5 101.5  95.0                            
REMARK 620 6 GLU D 220   OE1  87.0  90.9 114.0 165.6  95.6                      
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 SO4 A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN D 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN D 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN D 2003                 
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 2004        
REMARK 800  bound 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  2005 through MAN D 2008 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  2009 through NAG D 2010 bound to ASN D 371                          
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4Z7O   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Z7Q   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Z7S   RELATED DB: PDB                                   
DBREF  4Z7N A    1   455  UNP    P08514   ITA2B_HUMAN     32    486             
DBREF  4Z7N B    3   471  UNP    P05106   ITB3_HUMAN      29    497             
DBREF  4Z7N C    1   455  UNP    P08514   ITA2B_HUMAN     32    486             
DBREF  4Z7N D    3   471  UNP    P05106   ITB3_HUMAN      29    497             
DBREF  4Z7N E    1   219  PDB    4Z7N     4Z7N             1    219             
DBREF  4Z7N F    1   214  PDB    4Z7N     4Z7N             1    214             
DBREF  4Z7N H    1   219  PDB    4Z7N     4Z7N             1    219             
DBREF  4Z7N L    1   214  PDB    4Z7N     4Z7N             1    214             
DBREF  4Z7N G  408   411  PDB    4Z7N     4Z7N           408    411             
DBREF  4Z7N J  408   411  PDB    4Z7N     4Z7N           408    411             
SEQRES   1 A  455  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 A  455  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 A  455  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 A  455  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 A  455  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 A  455  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 A  455  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 A  455  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 A  455  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 A  455  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 A  455  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 A  455  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 A  455  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 A  455  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 A  455  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 A  455  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 A  455  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 A  455  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 A  455  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 A  455  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 A  455  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 A  455  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 A  455  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 A  455  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 A  455  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 A  455  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 A  455  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 A  455  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 A  455  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 A  455  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 A  455  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 A  455  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 A  455  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 A  455  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 A  455  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES   1 B  469  ASN ILE CYS THR THR ARG GLY VAL SER SER CYS GLN GLN          
SEQRES   2 B  469  CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS SER ASP          
SEQRES   3 B  469  GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP LEU LYS          
SEQRES   4 B  469  GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU SER ILE          
SEQRES   5 B  469  GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU ASP ARG          
SEQRES   6 B  469  PRO LEU SER ASP LYS GLY SER GLY ASP SER SER GLN VAL          
SEQRES   7 B  469  THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG LEU ARG          
SEQRES   8 B  469  PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL ARG GLN          
SEQRES   9 B  469  VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU MET ASP          
SEQRES  10 B  469  LEU SER TYR SER MET LYS ASP ASP LEU TRP SER ILE GLN          
SEQRES  11 B  469  ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG LYS LEU          
SEQRES  12 B  469  THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE VAL ASP          
SEQRES  13 B  469  LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO PRO GLU          
SEQRES  14 B  469  ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR THR CYS          
SEQRES  15 B  469  LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR LEU THR          
SEQRES  16 B  469  ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS LYS GLN          
SEQRES  17 B  469  SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY GLY PHE          
SEQRES  18 B  469  ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU LYS ILE          
SEQRES  19 B  469  GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL PHE THR          
SEQRES  20 B  469  THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY ARG LEU          
SEQRES  21 B  469  ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS HIS VAL          
SEQRES  22 B  469  GLY SER ASP ASN HIS TYR SER ALA SER THR THR MET ASP          
SEQRES  23 B  469  TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU SER GLN          
SEQRES  24 B  469  LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU ASN VAL          
SEQRES  25 B  469  VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE PRO GLY          
SEQRES  26 B  469  THR THR VAL GLY VAL LEU SER MET ASP SER SER ASN VAL          
SEQRES  27 B  469  LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE ARG SER          
SEQRES  28 B  469  LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU GLU LEU          
SEQRES  29 B  469  SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN GLU VAL          
SEQRES  30 B  469  ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS ILE GLY          
SEQRES  31 B  469  ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL ARG GLY          
SEQRES  32 B  469  CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE LYS PRO          
SEQRES  33 B  469  VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL THR PHE          
SEQRES  34 B  469  ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU PRO ASN          
SEQRES  35 B  469  SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE GLU CYS          
SEQRES  36 B  469  GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY SER GLN          
SEQRES  37 B  469  CYS                                                          
SEQRES   1 C  455  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 C  455  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 C  455  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 C  455  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 C  455  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 C  455  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 C  455  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 C  455  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 C  455  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 C  455  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 C  455  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 C  455  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 C  455  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 C  455  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 C  455  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 C  455  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 C  455  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 C  455  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 C  455  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 C  455  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 C  455  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 C  455  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 C  455  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 C  455  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 C  455  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 C  455  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 C  455  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 C  455  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 C  455  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 C  455  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 C  455  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 C  455  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 C  455  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 C  455  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 C  455  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES   1 D  469  ASN ILE CYS THR THR ARG GLY VAL SER SER CYS GLN GLN          
SEQRES   2 D  469  CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS SER ASP          
SEQRES   3 D  469  GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP LEU LYS          
SEQRES   4 D  469  GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU SER ILE          
SEQRES   5 D  469  GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU ASP ARG          
SEQRES   6 D  469  PRO LEU SER ASP LYS GLY SER GLY ASP SER SER GLN VAL          
SEQRES   7 D  469  THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG LEU ARG          
SEQRES   8 D  469  PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL ARG GLN          
SEQRES   9 D  469  VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU MET ASP          
SEQRES  10 D  469  LEU SER TYR SER MET LYS ASP ASP LEU TRP SER ILE GLN          
SEQRES  11 D  469  ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG LYS LEU          
SEQRES  12 D  469  THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE VAL ASP          
SEQRES  13 D  469  LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO PRO GLU          
SEQRES  14 D  469  ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR THR CYS          
SEQRES  15 D  469  LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR LEU THR          
SEQRES  16 D  469  ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS LYS GLN          
SEQRES  17 D  469  SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY GLY PHE          
SEQRES  18 D  469  ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU LYS ILE          
SEQRES  19 D  469  GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL PHE THR          
SEQRES  20 D  469  THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY ARG LEU          
SEQRES  21 D  469  ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS HIS VAL          
SEQRES  22 D  469  GLY SER ASP ASN HIS TYR SER ALA SER THR THR MET ASP          
SEQRES  23 D  469  TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU SER GLN          
SEQRES  24 D  469  LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU ASN VAL          
SEQRES  25 D  469  VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE PRO GLY          
SEQRES  26 D  469  THR THR VAL GLY VAL LEU SER MET ASP SER SER ASN VAL          
SEQRES  27 D  469  LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE ARG SER          
SEQRES  28 D  469  LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU GLU LEU          
SEQRES  29 D  469  SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN GLU VAL          
SEQRES  30 D  469  ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS ILE GLY          
SEQRES  31 D  469  ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL ARG GLY          
SEQRES  32 D  469  CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE LYS PRO          
SEQRES  33 D  469  VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL THR PHE          
SEQRES  34 D  469  ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU PRO ASN          
SEQRES  35 D  469  SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE GLU CYS          
SEQRES  36 D  469  GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY SER GLN          
SEQRES  37 D  469  CYS                                                          
SEQRES   1 E  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    4  ALA GLY ASP VAL                                              
SEQRES   1 J    4  ALA GLY ASP VAL                                              
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    SO4  A 508       5                                                       
HET    GOL  A 509      14                                                       
HET     MN  B2001       1                                                       
HET     MN  B2002       1                                                       
HET     MN  B2003       1                                                       
HET    NAG  B2004      27                                                       
HET    NAG  B2005      26                                                       
HET    NAG  B2006      26                                                       
HET    BMA  B2007      19                                                       
HET    MAN  B2008      21                                                       
HET    MAN  B2009      21                                                       
HET    NAG  B2010      26                                                       
HET    NAG  B2011      27                                                       
HET    SO4  C 501       5                                                       
HET     CL  C 502       1                                                       
HET     CA  C 503       1                                                       
HET     CA  C 504       1                                                       
HET     CA  C 505       1                                                       
HET     CA  C 506       1                                                       
HET    SO4  C 507       5                                                       
HET    SO4  C 508       5                                                       
HET     MN  D2001       1                                                       
HET     MN  D2002       1                                                       
HET     MN  D2003       1                                                       
HET    NAG  D2004      27                                                       
HET    NAG  D2005      26                                                       
HET    NAG  D2006      26                                                       
HET    BMA  D2007      20                                                       
HET    MAN  D2008      21                                                       
HET    NAG  D2009      26                                                       
HET    NAG  D2010      27                                                       
HET    SO4  L 301       5                                                       
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  11   CA    8(CA 2+)                                                     
FORMUL  15  SO4    8(O4 S 2-)                                                   
FORMUL  19  GOL    C3 H8 O3                                                     
FORMUL  20   MN    6(MN 2+)                                                     
FORMUL  23  NAG    10(C8 H15 N O6)                                              
FORMUL  24  BMA    2(C6 H12 O6)                                                 
FORMUL  24  MAN    3(C6 H12 O6)                                                 
FORMUL  27   CL    CL 1-                                                        
FORMUL  41  HOH   *732(H2 O)                                                    
HELIX    1 AA1 LEU A  151  ASN A  158  1                                   8    
HELIX    2 AA2 GLY A  187  LEU A  192  1                                   6    
HELIX    3 AA3 VAL A  200  SER A  206  1                                   7    
HELIX    4 AA4 ASN A  227  PHE A  231  5                                   5    
HELIX    5 AA5 THR A  259  LEU A  264  1                                   6    
HELIX    6 AA6 TYR A  440  ALA A  442  5                                   3    
HELIX    7 AA7 ILE B    4  ARG B    8  1                                   5    
HELIX    8 AA8 SER B   12  SER B   20  1                                   9    
HELIX    9 AA9 LEU B   40  ASP B   47  1                                   8    
HELIX   10 AB1 ALA B   50  GLU B   52  5                                   3    
HELIX   11 AB2 SER B  121  ILE B  131  5                                  11    
HELIX   12 AB3 ASN B  133  THR B  146  1                                  14    
HELIX   13 AB4 PRO B  169  ASN B  175  1                                   7    
HELIX   14 AB5 VAL B  200  LYS B  209  1                                  10    
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 LEU B  258  GLY B  264  5                                   7    
HELIX   18 AB9 SER B  291  LYS B  302  1                                  12    
HELIX   19 AC1 VAL B  314  ILE B  325  1                                  12    
HELIX   20 AC2 GLN B  342  ARG B  352  1                                  11    
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  SER C  206  1                                   7    
HELIX   25 AC7 ASN C  227  PHE C  231  5                                   5    
HELIX   26 AC8 THR C  259  LEU C  264  1                                   6    
HELIX   27 AC9 SER D   12  ALA D   18  1                                   7    
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  SER D  123  5                                   3    
HELIX   32 AD5 MET D  124  ILE D  131  1                                   8    
HELIX   33 AD6 ASN D  133  THR D  146  1                                  14    
HELIX   34 AD7 PRO D  169  ASN D  175  1                                   7    
HELIX   35 AD8 GLN D  199  LYS D  209  1                                  11    
HELIX   36 AD9 GLY D  221  CYS D  232  1                                  12    
HELIX   37 AE1 CYS D  232  GLY D  237  1                                   6    
HELIX   38 AE2 LEU D  258  GLY D  264  5                                   7    
HELIX   39 AE3 TYR D  281  THR D  286  5                                   6    
HELIX   40 AE4 SER D  291  ASN D  303  1                                  13    
HELIX   41 AE5 VAL D  314  ILE D  325  1                                  12    
HELIX   42 AE6 ASN D  339  ARG D  352  1                                  14    
HELIX   43 AE7 CYS D  435  ALA D  441  5                                   7    
HELIX   44 AE8 PRO E   62  GLN E   65  5                                   4    
HELIX   45 AE9 THR E   87  THR E   91  5                                   5    
HELIX   46 AF1 SER E  162  SER E  164  5                                   3    
HELIX   47 AF2 ASP F   79  PHE F   83  5                                   5    
HELIX   48 AF3 SER F  121  THR F  126  1                                   6    
HELIX   49 AF4 LYS F  183  GLU F  187  1                                   5    
HELIX   50 AF5 ASN H   28  THR H   32  5                                   5    
HELIX   51 AF6 PRO H   62  GLN H   65  5                                   4    
HELIX   52 AF7 SER H  192  TRP H  194  5                                   3    
HELIX   53 AF8 ASP L   79  PHE L   83  5                                   5    
HELIX   54 AF9 SER L  121  GLY L  128  1                                   8    
HELIX   55 AG1 LYS L  183  GLU L  187  1                                   5    
SHEET    1 AA1 4 THR A   9  ALA A  12  0                                        
SHEET    2 AA1 4 GLN A 444  TYR A 448 -1  O  VAL A 447   N  THR A   9           
SHEET    3 AA1 4 ASP A 434  ALA A 439 -1  N  LEU A 435   O  TYR A 448           
SHEET    4 AA1 4 SER A 420  VAL A 425 -1  N  VAL A 425   O  ASP A 434           
SHEET    1 AA2 4 LEU A  23  LYS A  27  0                                        
SHEET    2 AA2 4 VAL A  33  ALA A  39 -1  O  ALA A  34   N  HIS A  26           
SHEET    3 AA2 4 GLY A  52  PRO A  57 -1  O  GLY A  52   N  ALA A  39           
SHEET    4 AA2 4 SER A  67  LEU A  68 -1  O  LEU A  68   N  VAL A  53           
SHEET    1 AA3 4 GLU A  75  VAL A  79  0                                        
SHEET    2 AA3 4 GLN A  82  PHE A  87 -1  O  LEU A  84   N  ARG A  77           
SHEET    3 AA3 4 HIS A 112  GLU A 117 -1  O  HIS A 112   N  PHE A  87           
SHEET    4 AA3 4 GLU A 120  GLU A 121 -1  O  GLU A 120   N  GLU A 117           
SHEET    1 AA4 4 GLU A  75  VAL A  79  0                                        
SHEET    2 AA4 4 GLN A  82  PHE A  87 -1  O  LEU A  84   N  ARG A  77           
SHEET    3 AA4 4 HIS A 112  GLU A 117 -1  O  HIS A 112   N  PHE A  87           
SHEET    4 AA4 4 THR A 125  PRO A 126 -1  O  THR A 125   N  TRP A 113           
SHEET    1 AA5 4 VAL A  97  TRP A 100  0                                        
SHEET    2 AA5 4 VAL A 103  ALA A 108 -1  O  VAL A 105   N  VAL A  98           
SHEET    3 AA5 4 SER A 129  GLN A 134 -1  O  PHE A 131   N  ALA A 106           
SHEET    4 AA5 4 ARG A 139  TYR A 143 -1  O  ALA A 141   N  LEU A 132           
SHEET    1 AA6 4 SER A 173  VAL A 175  0                                        
SHEET    2 AA6 4 GLU A 180  ALA A 185 -1  O  VAL A 182   N  VAL A 174           
SHEET    3 AA6 4 LEU A 194  PRO A 199 -1  O  ALA A 196   N  LEU A 183           
SHEET    4 AA6 4 SER A 220  LEU A 221 -1  O  SER A 220   N  GLN A 197           
SHEET    1 AA7 4 VAL A 239  GLY A 242  0                                        
SHEET    2 AA7 4 GLU A 252  ALA A 257 -1  O  VAL A 254   N  ALA A 240           
SHEET    3 AA7 4 ALA A 266  LEU A 270 -1  O  LEU A 270   N  TYR A 253           
SHEET    4 AA7 4 ARG A 276  ARG A 281 -1  O  LEU A 280   N  VAL A 267           
SHEET    1 AA8 4 VAL A 293  THR A 296  0                                        
SHEET    2 AA8 4 ASP A 305  ALA A 310 -1  O  LEU A 307   N  ALA A 294           
SHEET    3 AA8 4 ARG A 327  PHE A 331 -1  O  PHE A 331   N  LEU A 306           
SHEET    4 AA8 4 LEU A 345  THR A 348 -1  O  LEU A 347   N  VAL A 328           
SHEET    1 AA9 2 MET A 314  ARG A 317  0                                        
SHEET    2 AA9 2 LYS A 321  GLU A 324 -1  O  LYS A 321   N  ARG A 317           
SHEET    1 AB1 4 ILE A 360  GLY A 364  0                                        
SHEET    2 AB1 4 ASP A 373  ALA A 377 -1  O  ASP A 373   N  GLY A 364           
SHEET    3 AB1 4 GLN A 388  PHE A 392 -1  O  LEU A 390   N  VAL A 376           
SHEET    4 AB1 4 GLN A 405  ASP A 408 -1  O  GLN A 405   N  VAL A 391           
SHEET    1 AB2 2 GLY A 394  GLN A 395  0                                        
SHEET    2 AB2 2 GLY A 398  LEU A 399 -1  O  GLY A 398   N  GLN A 395           
SHEET    1 AB3 3 CYS B  38  ASP B  39  0                                        
SHEET    2 AB3 3 ALA B  24  CYS B  26 -1  N  ALA B  24   O  ASP B  39           
SHEET    3 AB3 3 ILE B  54  GLU B  55 -1  O  GLU B  55   N  TRP B  25           
SHEET    1 AB4 6 ALA B  61  GLU B  65  0                                        
SHEET    2 AB4 6 ARG B  87  LEU B  92 -1  O  ALA B  89   N  ARG B  62           
SHEET    3 AB4 6 LEU B 425  PHE B 431  1  O  GLN B 428   N  LEU B  90           
SHEET    4 AB4 6 GLU B 411  PRO B 418 -1  N  ILE B 416   O  LEU B 425           
SHEET    5 AB4 6 LYS B 354  ARG B 360 -1  N  GLU B 358   O  LYS B 417           
SHEET    6 AB4 6 SER B 385  MET B 387 -1  O  CYS B 386   N  VAL B 355           
SHEET    1 AB5 5 VAL B  83  SER B  84  0                                        
SHEET    2 AB5 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3 AB5 5 THR B 394  LYS B 402 -1  O  ILE B 399   N  PHE B 100           
SHEET    4 AB5 5 SER B 367  CYS B 374 -1  N  SER B 367   O  LYS B 402           
SHEET    5 AB5 5 GLU B 378  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1 AB6 6 TYR B 190  THR B 197  0                                        
SHEET    2 AB6 6 LEU B 149  PHE B 156 -1  N  ILE B 151   O  THR B 197           
SHEET    3 AB6 6 VAL B 112  ASP B 119  1  N  TYR B 116   O  GLY B 154           
SHEET    4 AB6 6 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    5 AB6 6 ILE B 304  VAL B 310  1  O  ILE B 307   N  PHE B 248           
SHEET    6 AB6 6 THR B 329  VAL B 332  1  O  THR B 329   N  PHE B 308           
SHEET    1 AB7 3 GLU B 442  PRO B 443  0                                        
SHEET    2 AB7 3 GLY B 453  GLU B 456 -1  O  PHE B 455   N  GLU B 442           
SHEET    3 AB7 3 VAL B 459  CYS B 462 -1  O  ARG B 461   N  THR B 454           
SHEET    1 AB8 4 THR C   9  ALA C  12  0                                        
SHEET    2 AB8 4 GLN C 444  TYR C 448 -1  O  VAL C 445   N  TYR C  11           
SHEET    3 AB8 4 ASP C 434  ALA C 439 -1  N  LEU C 435   O  TYR C 448           
SHEET    4 AB8 4 LEU C 421  VAL C 425 -1  N  VAL C 425   O  ASP C 434           
SHEET    1 AB9 4 LEU C  23  LYS C  27  0                                        
SHEET    2 AB9 4 VAL C  33  ALA C  39 -1  O  VAL C  36   N  ASP C  24           
SHEET    3 AB9 4 GLY C  52  PRO C  57 -1  O  GLY C  52   N  ALA C  39           
SHEET    4 AB9 4 SER C  67  LEU C  68 -1  O  LEU C  68   N  VAL C  53           
SHEET    1 AC1 4 THR C  76  VAL C  79  0                                        
SHEET    2 AC1 4 GLN C  82  PHE C  87 -1  O  LEU C  84   N  ARG C  77           
SHEET    3 AC1 4 HIS C 112  GLU C 117 -1  O  LEU C 116   N  THR C  83           
SHEET    4 AC1 4 GLU C 120  GLU C 121 -1  O  GLU C 120   N  GLU C 117           
SHEET    1 AC2 4 THR C  76  VAL C  79  0                                        
SHEET    2 AC2 4 GLN C  82  PHE C  87 -1  O  LEU C  84   N  ARG C  77           
SHEET    3 AC2 4 HIS C 112  GLU C 117 -1  O  LEU C 116   N  THR C  83           
SHEET    4 AC2 4 THR C 125  PRO C 126 -1  O  THR C 125   N  TRP C 113           
SHEET    1 AC3 4 VAL C  97  TRP C 100  0                                        
SHEET    2 AC3 4 VAL C 103  ALA C 108 -1  O  VAL C 105   N  VAL C  98           
SHEET    3 AC3 4 SER C 129  ALA C 133 -1  O  SER C 129   N  ALA C 108           
SHEET    4 AC3 4 ARG C 140  TYR C 143 -1  O  ALA C 141   N  LEU C 132           
SHEET    1 AC4 4 SER C 172  VAL C 175  0                                        
SHEET    2 AC4 4 GLU C 180  ALA C 185 -1  O  GLY C 184   N  SER C 172           
SHEET    3 AC4 4 LEU C 194  PRO C 199 -1  O  LEU C 194   N  ALA C 185           
SHEET    4 AC4 4 SER C 220  LEU C 221 -1  O  SER C 220   N  GLN C 197           
SHEET    1 AC5 4 VAL C 239  GLY C 242  0                                        
SHEET    2 AC5 4 GLU C 252  ALA C 257 -1  O  VAL C 254   N  ALA C 240           
SHEET    3 AC5 4 ALA C 266  LEU C 270 -1  O  LEU C 270   N  TYR C 253           
SHEET    4 AC5 4 HIS C 278  ARG C 281 -1  O  LEU C 280   N  VAL C 267           
SHEET    1 AC6 4 VAL C 293  THR C 296  0                                        
SHEET    2 AC6 4 ASP C 305  ALA C 310 -1  O  LEU C 307   N  ALA C 294           
SHEET    3 AC6 4 ARG C 327  PHE C 331 -1  O  ARG C 327   N  ALA C 310           
SHEET    4 AC6 4 LEU C 345  THR C 348 -1  O  LEU C 347   N  VAL C 328           
SHEET    1 AC7 2 MET C 314  ARG C 317  0                                        
SHEET    2 AC7 2 LYS C 321  GLU C 324 -1  O  LYS C 321   N  ARG C 317           
SHEET    1 AC8 4 ILE C 360  GLY C 364  0                                        
SHEET    2 AC8 4 ASP C 373  ALA C 378 -1  O  ASP C 373   N  GLY C 364           
SHEET    3 AC8 4 GLN C 388  PHE C 392 -1  O  LEU C 390   N  VAL C 376           
SHEET    4 AC8 4 GLN C 405  ASP C 408 -1  O  LEU C 407   N  VAL C 389           
SHEET    1 AC9 2 GLY C 394  GLN C 395  0                                        
SHEET    2 AC9 2 GLY C 398  LEU C 399 -1  O  GLY C 398   N  GLN C 395           
SHEET    1 AD1 3 CYS D  38  ASP D  39  0                                        
SHEET    2 AD1 3 ALA D  24  CYS D  26 -1  N  ALA D  24   O  ASP D  39           
SHEET    3 AD1 3 ILE D  54  GLU D  55 -1  O  GLU D  55   N  TRP D  25           
SHEET    1 AD2 6 ALA D  61  GLU D  65  0                                        
SHEET    2 AD2 6 ARG D  87  LEU D  92 -1  O  ALA D  89   N  ARG D  62           
SHEET    3 AD2 6 LEU D 425  PHE D 431  1  O  GLN D 428   N  LEU D  90           
SHEET    4 AD2 6 GLU D 411  PRO D 418 -1  N  PHE D 414   O  VAL D 427           
SHEET    5 AD2 6 VAL D 355  ARG D 360 -1  N  ARG D 360   O  THR D 415           
SHEET    6 AD2 6 SER D 385  CYS D 386 -1  O  CYS D 386   N  VAL D 355           
SHEET    1 AD3 5 VAL D  83  SER D  84  0                                        
SHEET    2 AD3 5 SER D  97  ARG D 105 -1  O  GLN D 103   N  SER D  84           
SHEET    3 AD3 5 THR D 394  LYS D 402 -1  O  ILE D 399   N  PHE D 100           
SHEET    4 AD3 5 SER D 367  THR D 373 -1  N  ASN D 371   O  SER D 398           
SHEET    5 AD3 5 VAL D 379  PRO D 381 -1  O  ILE D 380   N  ALA D 372           
SHEET    1 AD4 6 TYR D 190  THR D 197  0                                        
SHEET    2 AD4 6 LEU D 149  PHE D 156 -1  N  ILE D 151   O  THR D 197           
SHEET    3 AD4 6 VAL D 112  ASP D 119  1  N  TYR D 116   O  GLY D 152           
SHEET    4 AD4 6 SER D 243  THR D 250  1  O  VAL D 247   N  LEU D 117           
SHEET    5 AD4 6 ASN D 305  THR D 311  1  O  ALA D 309   N  PHE D 248           
SHEET    6 AD4 6 THR D 329  LEU D 333  1  O  LEU D 333   N  VAL D 310           
SHEET    1 AD5 2 GLY D 453  GLU D 456  0                                        
SHEET    2 AD5 2 VAL D 459  CYS D 462 -1  O  ARG D 461   N  THR D 454           
SHEET    1 AD6 4 GLN E   3  GLN E   6  0                                        
SHEET    2 AD6 4 SER E  17  SER E  25 -1  O  THR E  23   N  GLN E   5           
SHEET    3 AD6 4 THR E  78  SER E  84 -1  O  LEU E  81   N  LEU E  20           
SHEET    4 AD6 4 THR E  69  ASP E  73 -1  N  THR E  69   O  GLN E  82           
SHEET    1 AD7 6 GLU E  10  VAL E  12  0                                        
SHEET    2 AD7 6 THR E 113  VAL E 117  1  O  THR E 116   N  GLU E  10           
SHEET    3 AD7 6 ALA E  92  ARG E  98 -1  N  ALA E  92   O  VAL E 115           
SHEET    4 AD7 6 VAL E  34  ARG E  40 -1  N  HIS E  35   O  VAL E  97           
SHEET    5 AD7 6 GLY E  44  ILE E  51 -1  O  GLU E  46   N  LYS E  38           
SHEET    6 AD7 6 THR E  58  TYR E  60 -1  O  LYS E  59   N  ARG E  50           
SHEET    1 AD8 4 GLU E  10  VAL E  12  0                                        
SHEET    2 AD8 4 THR E 113  VAL E 117  1  O  THR E 116   N  GLU E  10           
SHEET    3 AD8 4 ALA E  92  ARG E  98 -1  N  ALA E  92   O  VAL E 115           
SHEET    4 AD8 4 TYR E 108  TRP E 109 -1  O  TYR E 108   N  ARG E  98           
SHEET    1 AD9 4 SER E 126  LEU E 130  0                                        
SHEET    2 AD9 4 SER E 141  TYR E 151 -1  O  LYS E 149   N  SER E 126           
SHEET    3 AD9 4 LEU E 180  THR E 190 -1  O  LEU E 183   N  VAL E 148           
SHEET    4 AD9 4 VAL E 169  THR E 171 -1  N  HIS E 170   O  SER E 186           
SHEET    1 AE1 4 SER E 126  LEU E 130  0                                        
SHEET    2 AE1 4 SER E 141  TYR E 151 -1  O  LYS E 149   N  SER E 126           
SHEET    3 AE1 4 LEU E 180  THR E 190 -1  O  LEU E 183   N  VAL E 148           
SHEET    4 AE1 4 VAL E 175  GLN E 177 -1  N  GLN E 177   O  LEU E 180           
SHEET    1 AE2 3 THR E 159  TRP E 160  0                                        
SHEET    2 AE2 3 THR E 200  HIS E 205 -1  O  ASN E 202   N  THR E 159           
SHEET    3 AE2 3 THR E 210  LYS E 215 -1  O  VAL E 212   N  VAL E 203           
SHEET    1 AE3 4 MET F   4  SER F   7  0                                        
SHEET    2 AE3 4 VAL F  19  ALA F  25 -1  O  HIS F  24   N  THR F   5           
SHEET    3 AE3 4 ASP F  70  ILE F  75 -1  O  LEU F  73   N  ILE F  21           
SHEET    4 AE3 4 PHE F  62  SER F  67 -1  N  SER F  65   O  SER F  72           
SHEET    1 AE4 6 SER F  10  VAL F  13  0                                        
SHEET    2 AE4 6 THR F 102  ILE F 106  1  O  GLU F 105   N  MET F  11           
SHEET    3 AE4 6 ASP F  85  GLN F  90 -1  N  TYR F  86   O  THR F 102           
SHEET    4 AE4 6 ILE F  33  GLN F  38 -1  N  GLY F  34   O  VAL F  89           
SHEET    5 AE4 6 PHE F  44  TYR F  49 -1  O  LEU F  47   N  TRP F  35           
SHEET    6 AE4 6 ASN F  53  LEU F  54 -1  O  ASN F  53   N  TYR F  49           
SHEET    1 AE5 4 SER F  10  VAL F  13  0                                        
SHEET    2 AE5 4 THR F 102  ILE F 106  1  O  GLU F 105   N  MET F  11           
SHEET    3 AE5 4 ASP F  85  GLN F  90 -1  N  TYR F  86   O  THR F 102           
SHEET    4 AE5 4 THR F  97  PHE F  98 -1  O  THR F  97   N  GLN F  90           
SHEET    1 AE6 4 THR F 114  PHE F 118  0                                        
SHEET    2 AE6 4 GLY F 129  PHE F 139 -1  O  VAL F 133   N  PHE F 118           
SHEET    3 AE6 4 TYR F 173  THR F 182 -1  O  LEU F 181   N  ALA F 130           
SHEET    4 AE6 4 VAL F 159  TRP F 163 -1  N  SER F 162   O  SER F 176           
SHEET    1 AE7 4 SER F 153  ARG F 155  0                                        
SHEET    2 AE7 4 ASN F 145  ILE F 150 -1  N  ILE F 150   O  SER F 153           
SHEET    3 AE7 4 SER F 191  THR F 197 -1  O  THR F 197   N  ASN F 145           
SHEET    4 AE7 4 SER F 208  ASN F 210 -1  O  PHE F 209   N  TYR F 192           
SHEET    1 AE8 4 GLN H   3  GLN H   6  0                                        
SHEET    2 AE8 4 VAL H  18  SER H  25 -1  O  THR H  23   N  GLN H   5           
SHEET    3 AE8 4 THR H  78  LEU H  83 -1  O  LEU H  81   N  LEU H  20           
SHEET    4 AE8 4 ALA H  68  ASP H  73 -1  N  THR H  71   O  TYR H  80           
SHEET    1 AE9 6 GLU H  10  VAL H  12  0                                        
SHEET    2 AE9 6 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3 AE9 6 VAL H  93  ARG H  98 -1  N  TYR H  94   O  THR H 113           
SHEET    4 AE9 6 VAL H  34  ARG H  40 -1  N  HIS H  35   O  VAL H  97           
SHEET    5 AE9 6 GLY H  44  ILE H  51 -1  O  GLU H  46   N  LYS H  38           
SHEET    6 AE9 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  ARG H  50           
SHEET    1 AF1 4 GLU H  10  VAL H  12  0                                        
SHEET    2 AF1 4 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3 AF1 4 VAL H  93  ARG H  98 -1  N  TYR H  94   O  THR H 113           
SHEET    4 AF1 4 TYR H 108  TRP H 109 -1  O  TYR H 108   N  ARG H  98           
SHEET    1 AF2 4 SER H 126  LEU H 130  0                                        
SHEET    2 AF2 4 SER H 141  TYR H 151 -1  O  LYS H 149   N  SER H 126           
SHEET    3 AF2 4 LEU H 180  THR H 190 -1  O  LEU H 183   N  VAL H 148           
SHEET    4 AF2 4 VAL H 169  THR H 171 -1  N  HIS H 170   O  SER H 186           
SHEET    1 AF3 4 SER H 126  LEU H 130  0                                        
SHEET    2 AF3 4 SER H 141  TYR H 151 -1  O  LYS H 149   N  SER H 126           
SHEET    3 AF3 4 LEU H 180  THR H 190 -1  O  LEU H 183   N  VAL H 148           
SHEET    4 AF3 4 VAL H 175  GLN H 177 -1  N  GLN H 177   O  LEU H 180           
SHEET    1 AF4 3 THR H 157  TRP H 160  0                                        
SHEET    2 AF4 3 THR H 200  HIS H 205 -1  O  ASN H 202   N  THR H 159           
SHEET    3 AF4 3 THR H 210  LYS H 215 -1  O  THR H 210   N  HIS H 205           
SHEET    1 AF5 4 MET L   4  SER L   7  0                                        
SHEET    2 AF5 4 VAL L  19  ALA L  25 -1  O  HIS L  24   N  THR L   5           
SHEET    3 AF5 4 ASP L  70  ILE L  75 -1  O  LEU L  73   N  ILE L  21           
SHEET    4 AF5 4 PHE L  62  SER L  67 -1  N  SER L  63   O  THR L  74           
SHEET    1 AF6 6 SER L  10  VAL L  13  0                                        
SHEET    2 AF6 6 THR L 102  ILE L 106  1  O  GLU L 105   N  VAL L  13           
SHEET    3 AF6 6 ASP L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4 AF6 6 ILE L  33  GLN L  38 -1  N  GLY L  34   O  VAL L  89           
SHEET    5 AF6 6 PHE L  44  TYR L  49 -1  O  LEU L  47   N  TRP L  35           
SHEET    6 AF6 6 ASN L  53  LEU L  54 -1  O  ASN L  53   N  TYR L  49           
SHEET    1 AF7 4 SER L  10  VAL L  13  0                                        
SHEET    2 AF7 4 THR L 102  ILE L 106  1  O  GLU L 105   N  VAL L  13           
SHEET    3 AF7 4 ASP L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4 AF7 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1 AF8 4 THR L 114  PHE L 118  0                                        
SHEET    2 AF8 4 GLY L 129  PHE L 139 -1  O  PHE L 135   N  SER L 116           
SHEET    3 AF8 4 TYR L 173  THR L 182 -1  O  LEU L 181   N  ALA L 130           
SHEET    4 AF8 4 VAL L 159  TRP L 163 -1  N  LEU L 160   O  THR L 178           
SHEET    1 AF9 4 SER L 153  ARG L 155  0                                        
SHEET    2 AF9 4 ASN L 145  ILE L 150 -1  N  ILE L 150   O  SER L 153           
SHEET    3 AF9 4 SER L 191  THR L 197 -1  O  GLU L 195   N  LYS L 147           
SHEET    4 AF9 4 ILE L 205  ASN L 210 -1  O  ILE L 205   N  ALA L 196           
SSBOND   1 CYS A   56    CYS A   65                          1555   1555  2.03  
SSBOND   2 CYS A  107    CYS A  130                          1555   1555  2.03  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.02  
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  2.03  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.03  
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  2.02  
SSBOND  15 CYS C  107    CYS C  130                          1555   1555  2.03  
SSBOND  16 CYS C  146    CYS C  167                          1555   1555  2.02  
SSBOND  17 CYS D    5    CYS D   23                          1555   1555  2.03  
SSBOND  18 CYS D   13    CYS D  435                          1555   1555  2.03  
SSBOND  19 CYS D   16    CYS D   38                          1555   1555  2.03  
SSBOND  20 CYS D   26    CYS D   49                          1555   1555  2.03  
SSBOND  21 CYS D  177    CYS D  184                          1555   1555  2.04  
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  2.04  
SSBOND  28 CYS E   22    CYS E   96                          1555   1555  2.03  
SSBOND  29 CYS E  134    CYS F  214                          1555   1555  2.04  
SSBOND  30 CYS E  146    CYS E  201                          1555   1555  2.03  
SSBOND  31 CYS F   23    CYS F   88                          1555   1555  2.03  
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  2.35  
LINK         OE2 GLU A 243                CA    CA A 501     1555   1555  2.30  
LINK         OD1 ASP A 245                CA    CA A 501     1555   1555  2.29  
LINK         O   ASP A 247                CA    CA A 501     1555   1555  2.38  
LINK         O   THR A 250                CA    CA A 501     1555   1555  2.29  
LINK         OG1 THR A 250                CA    CA A 501     1555   1555  2.31  
LINK         OE1 GLU A 252                CA    CA A 501     1555   1555  2.36  
LINK         OE2 GLU A 252                CA    CA A 501     1555   1555  2.34  
LINK         OD1 ASP A 297                CA    CA A 502     1555   1555  2.31  
LINK         OD1 ASN A 299                CA    CA A 502     1555   1555  2.28  
LINK         OD1 ASP A 301                CA    CA A 502     1555   1555  2.53  
LINK         O   ARG A 303                CA    CA A 502     1555   1555  2.15  
LINK         OD1 ASP A 305                CA    CA A 502     1555   1555  2.37  
LINK         OD2 ASP A 305                CA    CA A 502     1555   1555  2.46  
LINK         OD1 ASP A 365                CA    CA A 503     1555   1555  2.27  
LINK         OD1 ASP A 367                CA    CA A 503     1555   1555  2.33  
LINK         OD1 ASP A 369                CA    CA A 503     1555   1555  2.38  
LINK         O   TYR A 371                CA    CA A 503     1555   1555  2.26  
LINK         OD1 ASP A 373                CA    CA A 503     1555   1555  2.39  
LINK         OD2 ASP A 373                CA    CA A 503     1555   1555  2.37  
LINK         OD1 ASP A 426                CA    CA A 504     1555   1555  2.24  
LINK         OD1 ASP A 428                CA    CA A 504     1555   1555  2.34  
LINK         OD1 ASN A 430                CA    CA A 504     1555   1555  2.33  
LINK         O   TYR A 432                CA    CA A 504     1555   1555  2.29  
LINK         OD1 ASP A 434                CA    CA A 504     1555   1555  2.29  
LINK         OD2 ASP A 434                CA    CA A 504     1555   1555  2.37  
LINK         ND2 ASN B  99                 C1  NAG B2004     1555   1555  1.41  
LINK         OG  SER B 121                MN    MN B2001     1555   1555  2.16  
LINK         O   SER B 123                MN    MN B2002     1555   1555  2.16  
LINK         OG  SER B 123                MN    MN B2001     1555   1555  2.17  
LINK         OD1 ASP B 126                MN    MN B2002     1555   1555  2.14  
LINK         OD2 ASP B 127                MN    MN B2002     1555   1555  2.13  
LINK         OD2 ASP B 158                MN    MN B2003     1555   1555  2.15  
LINK         OD1 ASN B 215                MN    MN B2003     1555   1555  2.16  
LINK         O   ASP B 217                MN    MN B2003     1555   1555  2.22  
LINK         OD1 ASP B 217                MN    MN B2003     1555   1555  2.14  
LINK         O   PRO B 219                MN    MN B2003     1555   1555  1.88  
LINK         OE1 GLU B 220                MN    MN B2003     1555   1555  2.18  
LINK         OE2 GLU B 220                MN    MN B2001     1555   1555  2.17  
LINK         OD2 ASP B 251                MN    MN B2002     1555   1555  2.15  
LINK         ND2 ASN B 320                 C1  NAG B2005     1555   1555  1.39  
LINK         ND2 ASN B 371                 C1  NAG B2010     1555   1555  1.39  
LINK         OE1 GLU C 243                CA    CA C 503     1555   1555  2.34  
LINK         OE2 GLU C 243                CA    CA C 503     1555   1555  2.31  
LINK         OD1 ASP C 245                CA    CA C 503     1555   1555  2.33  
LINK         O   ASP C 247                CA    CA C 503     1555   1555  2.36  
LINK         O   THR C 250                CA    CA C 503     1555   1555  2.33  
LINK         OG1 THR C 250                CA    CA C 503     1555   1555  2.31  
LINK         OE1 GLU C 252                CA    CA C 503     1555   1555  2.36  
LINK         OE2 GLU C 252                CA    CA C 503     1555   1555  2.30  
LINK         OD1 ASP C 297                CA    CA C 504     1555   1555  2.32  
LINK         OD1 ASN C 299                CA    CA C 504     1555   1555  2.34  
LINK         OD1 ASP C 301                CA    CA C 504     1555   1555  2.35  
LINK         O   ARG C 303                CA    CA C 504     1555   1555  2.13  
LINK         OD1 ASP C 305                CA    CA C 504     1555   1555  2.38  
LINK         OD2 ASP C 305                CA    CA C 504     1555   1555  2.33  
LINK         OD1 ASP C 365                CA    CA C 505     1555   1555  2.35  
LINK         OD1 ASP C 367                CA    CA C 505     1555   1555  2.34  
LINK         OD1 ASP C 369                CA    CA C 505     1555   1555  2.38  
LINK         O   TYR C 371                CA    CA C 505     1555   1555  2.24  
LINK         OD1 ASP C 373                CA    CA C 505     1555   1555  2.40  
LINK         OD2 ASP C 373                CA    CA C 505     1555   1555  2.34  
LINK         OD1 ASP C 426                CA    CA C 506     1555   1555  2.28  
LINK         OD1 ASP C 428                CA    CA C 506     1555   1555  2.33  
LINK         OD1 ASN C 430                CA    CA C 506     1555   1555  2.32  
LINK         O   TYR C 432                CA    CA C 506     1555   1555  2.23  
LINK         OD1 ASP C 434                CA    CA C 506     1555   1555  2.28  
LINK         OD2 ASP C 434                CA    CA C 506     1555   1555  2.37  
LINK         ND2 ASN D  99                 C1  NAG D2004     1555   1555  1.48  
LINK         OG  SER D 121                MN    MN D2001     1555   1555  2.14  
LINK         O   SER D 123                MN    MN D2002     1555   1555  2.19  
LINK         OD1 ASP D 126                MN    MN D2002     1555   1555  2.16  
LINK         OD1 ASP D 127                MN    MN D2002     1555   1555  2.14  
LINK         OD2 ASP D 158                MN    MN D2003     1555   1555  2.16  
LINK         OD1 ASN D 215                MN    MN D2003     1555   1555  2.16  
LINK         O   ASP D 217                MN    MN D2003     1555   1555  2.18  
LINK         OD1 ASP D 217                MN    MN D2003     1555   1555  2.14  
LINK         O   PRO D 219                MN    MN D2003     1555   1555  2.09  
LINK         OE1 GLU D 220                MN    MN D2003     1555   1555  2.16  
LINK         OE2 GLU D 220                MN    MN D2001     1555   1555  2.17  
LINK         ND2 ASN D 320                 C1  NAG D2005     1555   1555  1.45  
LINK         O   MET D 335                MN    MN D2002     1555   1555  2.77  
LINK         ND2 ASN D 371                 C1  NAG D2009     1555   1555  1.41  
LINK         OD1 ASP G 410                MN    MN B2001     1555   1555  2.11  
LINK         OD1 ASP J 410                MN    MN D2001     1555   1555  2.13  
LINK        CA    CA A 502                 O   HOH A 617     1555   1555  2.36  
LINK        CA    CA A 503                 O   HOH A 601     1555   1555  2.32  
LINK        CA    CA A 504                 O   HOH A 607     1555   1555  2.35  
LINK        MN    MN B2001                 O   HOH B2146     1555   1555  2.16  
LINK        MN    MN B2001                 O   HOH B2114     1555   1555  2.15  
LINK        MN    MN B2002                 O   HOH G 501     1555   1555  2.18  
LINK        MN    MN B2002                 O   HOH B2168     1555   1555  2.19  
LINK         O4  NAG B2005                 C1  NAG B2006     1555   1555  1.38  
LINK         O4  NAG B2006                 C1  BMA B2007     1555   1555  1.38  
LINK         O3  BMA B2007                 C1  MAN B2008     1555   1555  1.41  
LINK         O6  BMA B2007                 C1  MAN B2009     1555   1555  1.34  
LINK         O4  NAG B2010                 C1  NAG B2011     1555   1555  1.40  
LINK        CA    CA C 504                 O   HOH C 613     1555   1555  2.35  
LINK        CA    CA C 505                 O   HOH C 614     1555   1555  2.37  
LINK        CA    CA C 506                 O   HOH C 602     1555   1555  2.36  
LINK        MN    MN D2001                 O   HOH D2105     1555   1555  2.15  
LINK        MN    MN D2001                 O   HOH D2134     1555   1555  2.17  
LINK        MN    MN D2002                 O   HOH D2115     1555   1555  2.19  
LINK        MN    MN D2002                 O   HOH D2136     1555   1555  2.18  
LINK         O4  NAG D2005                 C1  NAG D2006     1555   1555  1.41  
LINK         O4  NAG D2006                 C1  BMA D2007     1555   1555  1.42  
LINK         O3  BMA D2007                 C1  MAN D2008     1555   1555  1.51  
LINK         O4  NAG D2009                 C1  NAG D2010     1555   1555  1.39  
CISPEP   1 SER B   84    PRO B   85          0        -1.09                     
CISPEP   2 SER B  162    PRO B  163          0         3.32                     
CISPEP   3 SER B  168    PRO B  169          0        -3.02                     
CISPEP   4 SER D   84    PRO D   85          0        -0.99                     
CISPEP   5 SER D  162    PRO D  163          0         2.20                     
CISPEP   6 SER D  168    PRO D  169          0        -3.62                     
CISPEP   7 PHE E  152    PRO E  153          0        -3.79                     
CISPEP   8 GLU E  154    PRO E  155          0        -5.11                     
CISPEP   9 TRP E  194    PRO E  195          0        -0.70                     
CISPEP  10 SER F    7    PRO F    8          0        -1.63                     
CISPEP  11 LEU F   94    PRO F   95          0         0.31                     
CISPEP  12 TYR F  140    PRO F  141          0         1.14                     
CISPEP  13 PHE H  152    PRO H  153          0        -4.46                     
CISPEP  14 GLU H  154    PRO H  155          0        -4.91                     
CISPEP  15 TRP H  194    PRO H  195          0        -0.43                     
CISPEP  16 SER L    7    PRO L    8          0        -1.79                     
CISPEP  17 LEU L   94    PRO L   95          0         0.64                     
CISPEP  18 TYR L  140    PRO L  141          0         0.41                     
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 617                                          
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 601                                          
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 607                                          
SITE     1 AC5  4 ILE A 154  TYR A 155  ASN A 158  SER A 161                    
SITE     1 AC6  4 PHE A  10  PRO A 410  GLN A 444  PRO C 383                    
SITE     1 AC7  5 ARG A 400  SER A 401  ARG A 402  HOH A 738                    
SITE     2 AC7  5 HOH A 745                                                     
SITE     1 AC8  5 ARG A 386  PRO A 412  THR A 413  ARG C 386                    
SITE     2 AC8  5 PRO C 412                                                     
SITE     1 AC9  3 ASN A 227  ARG A 276  ARG A 279                               
SITE     1 AD1  6 SER B 121  SER B 123  GLU B 220  HOH B2114                    
SITE     2 AD1  6 HOH B2146  ASP G 410                                          
SITE     1 AD2  6 SER B 123  ASP B 126  ASP B 127  ASP B 251                    
SITE     2 AD2  6 HOH B2168  HOH G 501                                          
SITE     1 AD3  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 AD3  5 GLU B 220                                                     
SITE     1 AD4  2 ALA C  89  ARG C  90                                          
SITE     1 AD5  1 HOH A 780                                                     
SITE     1 AD6  6 GLU C 243  ASP C 245  ASP C 247  THR C 250                    
SITE     2 AD6  6 THR C 251  GLU C 252                                          
SITE     1 AD7  6 ASP C 297  ASN C 299  ASP C 301  ARG C 303                    
SITE     2 AD7  6 ASP C 305  HOH C 613                                          
SITE     1 AD8  6 ASP C 365  ASP C 367  ASP C 369  TYR C 371                    
SITE     2 AD8  6 ASP C 373  HOH C 614                                          
SITE     1 AD9  6 ASP C 426  ASP C 428  ASN C 430  TYR C 432                    
SITE     2 AD9  6 ASP C 434  HOH C 602                                          
SITE     1 AE1  4 VAL A 454  ARG C 400  SER C 401  ARG C 402                    
SITE     1 AE2  3 ASN C 227  ARG C 276  ARG C 279                               
SITE     1 AE3  6 SER D 121  ASN D 215  GLU D 220  HOH D2105                    
SITE     2 AE3  6 HOH D2134  ASP J 410                                          
SITE     1 AE4  7 SER D 123  MET D 124  ASP D 126  ASP D 127                    
SITE     2 AE4  7 MET D 335  HOH D2115  HOH D2136                               
SITE     1 AE5  5 ASP D 158  ASN D 215  ASP D 217  PRO D 219                    
SITE     2 AE5  5 GLU D 220                                                     
SITE     1 AE6  3 SER L  30  SER L  67  GLY L  68                               
SITE     1 AE7  3 LYS B  98  ASN B  99  HOH B2127                               
SITE     1 AE8  5 ARG A 281  MET A 285  ASN B 320  HOH B2132                    
SITE     2 AE8  5 HOH B2159                                                     
SITE     1 AE9  3 ASN B 371  SER B 398  ILE B 399                               
SITE     1 AF1  3 LYS D  98  ASN D  99  SER D 101                               
SITE     1 AF2  2 ARG C 281  ASN D 320                                          
SITE     1 AF3  5 ASN D 371  PRO D 381  SER D 398  ILE D 399                    
SITE     2 AF3  5 GLU D 400                                                     
CRYST1  256.883  144.373  104.639  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      0.003893  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006927  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009557        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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