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Entry: 5I5K
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HEADER    IMMUNE SYSTEM                           15-FEB-16   5I5K              
TITLE     STRUCTURE OF COMPLEMENT C5 IN COMPLEX WITH ECULIZUMAB                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COMPLEMENT C5;                                             
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 SYNONYM: C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING     
COMPND   5 PROTEIN 4;                                                           
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ECULIZUMAB HEAVY CHAIN (VARIABLE DOMAIN);                  
COMPND   8 CHAIN: H, X;                                                         
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: ECULIZUMAB LIGHT CHAIN (VARIABLE DOMAIN);                  
COMPND  12 CHAIN: L, Y;                                                         
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  10 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  12 MOL_ID: 3;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  17 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    COMPLEMENT, FAB, IMMUNE SYSTEM                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.SCHATZ-JAKOBSEN,G.R.ANDERSEN                                      
REVDAT   3   29-JUN-16 5I5K    1       JRNL                                     
REVDAT   2   08-JUN-16 5I5K    1       JRNL                                     
REVDAT   1   16-MAR-16 5I5K    0                                                
JRNL        AUTH   J.A.SCHATZ-JAKOBSEN,Y.ZHANG,K.JOHNSON,A.NEILL,D.SHERIDAN,    
JRNL        AUTH 2 G.R.ANDERSEN                                                 
JRNL        TITL   STRUCTURAL BASIS FOR ECULIZUMAB-MEDIATED INHIBITION OF THE   
JRNL        TITL 2 COMPLEMENT TERMINAL PATHWAY.                                 
JRNL        REF    J IMMUNOL.                    V. 197   337 2016              
JRNL        REFN                   ESSN 1550-6606                               
JRNL        PMID   27194791                                                     
JRNL        DOI    10.4049/JIMMUNOL.1600280                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2152: ???)                              
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) : 4.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.80                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 76073                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.450                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1865                            
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 49.7983 -  9.8520    0.99     5765   144  0.1616 0.1874        
REMARK   3     2  9.8520 -  7.8297    1.00     5719   143  0.1537 0.1722        
REMARK   3     3  7.8297 -  6.8428    1.00     5746   145  0.1829 0.2501        
REMARK   3     4  6.8428 -  6.2184    1.00     5701   144  0.2053 0.2355        
REMARK   3     5  6.2184 -  5.7734    1.00     5715   143  0.2157 0.2748        
REMARK   3     6  5.7734 -  5.4335    1.00     5722   144  0.2223 0.2836        
REMARK   3     7  5.4335 -  5.1617    1.00     5714   144  0.2228 0.2628        
REMARK   3     8  5.1617 -  4.9372    1.00     5653   142  0.2312 0.2864        
REMARK   3     9  4.9372 -  4.7473    0.99     5696   143  0.2654 0.3225        
REMARK   3    10  4.7473 -  4.5836    1.00     5714   144  0.2725 0.3432        
REMARK   3    11  4.5836 -  4.4404    1.00     5704   143  0.2887 0.3500        
REMARK   3    12  4.4404 -  4.3135    1.00     5672   143  0.3073 0.3292        
REMARK   3    13  4.3135 -  4.2000    1.00     5687   143  0.3201 0.3358        
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)     : 0.610            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.760           
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      :  0.003          33282                                  
REMARK   3   ANGLE     :  0.641          45218                                  
REMARK   3   CHIRALITY :  0.045           5150                                  
REMARK   3   PLANARITY :  0.004           5738                                  
REMARK   3   DIHEDRAL  : 10.374          20052                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 34                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: RESID 19:120 AND CHAIN A                               
REMARK   3    ORIGIN FOR THE GROUP (A):  46.4197  82.7118  34.6804              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5383 T22:   5.2491                                     
REMARK   3      T33:   2.2178 T12:  -0.2139                                     
REMARK   3      T13:   0.0386 T23:  -0.4274                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8802 L22:   2.4430                                     
REMARK   3      L33:   1.1086 L12:   1.0083                                     
REMARK   3      L13:  -1.2744 L23:  -0.9290                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1120 S12:   2.0171 S13:  -0.7777                       
REMARK   3      S21:  -0.9858 S22:   1.0143 S23:  -0.9780                       
REMARK   3      S31:   1.3372 S32:   2.6633 S33:   0.0893                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: RESID 121:224 AND CHAIN A                              
REMARK   3    ORIGIN FOR THE GROUP (A):   9.9291  72.8424  42.0811              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6432 T22:   3.2998                                     
REMARK   3      T33:   1.8183 T12:  -0.2576                                     
REMARK   3      T13:   0.0376 T23:  -0.2953                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9192 L22:   3.0488                                     
REMARK   3      L33:   3.6850 L12:   1.0883                                     
REMARK   3      L13:   0.8555 L23:   2.8418                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5949 S12:   3.7888 S13:   0.0234                       
REMARK   3      S21:   0.2292 S22:   0.8936 S23:  -0.0874                       
REMARK   3      S31:  -0.4666 S32:   1.0674 S33:   0.0022                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: RESID 225:349 AND CHAIN A                              
REMARK   3    ORIGIN FOR THE GROUP (A): -14.9936  93.1880  23.7668              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.6630 T22:   3.4625                                     
REMARK   3      T33:   2.2688 T12:  -0.8105                                     
REMARK   3      T13:  -0.7104 T23:   1.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2027 L22:   1.6125                                     
REMARK   3      L33:   2.4515 L12:  -0.7604                                     
REMARK   3      L13:  -1.8485 L23:   1.7578                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0152 S12:   1.5954 S13:   0.9981                       
REMARK   3      S21:  -1.6176 S22:   0.1703 S23:   0.0833                       
REMARK   3      S31:   0.4953 S32:  -0.3277 S33:   0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: RESID 350:460 AND CHAIN A                              
REMARK   3    ORIGIN FOR THE GROUP (A):  19.5281 103.4406   9.8054              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.9705 T22:   5.9518                                     
REMARK   3      T33:   2.7214 T12:  -1.5073                                     
REMARK   3      T13:  -0.5301 T23:   1.3957                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2971 L22:   1.4510                                     
REMARK   3      L33:   0.1456 L12:  -0.7745                                     
REMARK   3      L13:  -0.2727 L23:   0.7558                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7298 S12:   1.0711 S13:   1.0470                       
REMARK   3      S21:  -1.5476 S22:   0.8208 S23:   0.3868                       
REMARK   3      S31:  -1.1697 S32:   0.0823 S33:   0.0004                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: RESID 461:566 AND CHAIN A                              
REMARK   3    ORIGIN FOR THE GROUP (A):  38.2146  88.0799  12.6360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.8808 T22:   7.1216                                     
REMARK   3      T33:   2.0880 T12:  -1.7317                                     
REMARK   3      T13:   0.2315 T23:   0.5433                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3752 L22:   3.1961                                     
REMARK   3      L33:   1.3745 L12:  -0.0012                                     
REMARK   3      L13:  -1.7635 L23:  -0.5566                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.5854 S12:   1.9956 S13:   1.8647                       
REMARK   3      S21:  -1.9620 S22:   0.8232 S23:   0.6276                       
REMARK   3      S31:  -0.8106 S32:   1.7126 S33:  -0.3309                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (RESID 567:606 OR RESID 760:821) AND CHAIN A           
REMARK   3    ORIGIN FOR THE GROUP (A):   4.1608  63.0752  24.5316              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8436 T22:   3.5923                                     
REMARK   3      T33:   1.7118 T12:  -0.1708                                     
REMARK   3      T13:   0.2632 T23:  -0.6163                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4869 L22:   2.3897                                     
REMARK   3      L33:   1.1247 L12:   2.0046                                     
REMARK   3      L13:   0.4626 L23:   1.6406                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8917 S12:   0.8513 S13:  -0.1413                       
REMARK   3      S21:  -0.5359 S22:   1.2697 S23:  -0.4426                       
REMARK   3      S31:   0.3322 S32:   0.9536 S33:   0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: RESID 822:930 AND CHAIN A                              
REMARK   3    ORIGIN FOR THE GROUP (A): -30.2270  53.9299  25.4987              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1256 T22:   2.7797                                     
REMARK   3      T33:   1.8026 T12:  -0.1146                                     
REMARK   3      T13:  -0.2656 T23:  -0.0312                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6095 L22:   2.0032                                     
REMARK   3      L33:   4.6689 L12:  -0.1065                                     
REMARK   3      L13:  -1.1084 L23:   1.0251                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4402 S12:  -0.3016 S13:  -1.2742                       
REMARK   3      S21:  -0.2690 S22:  -0.2035 S23:  -0.0256                       
REMARK   3      S31:   0.5947 S32:   1.6796 S33:  -0.0005                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: RESID 607:673 AND CHAIN A                              
REMARK   3    ORIGIN FOR THE GROUP (A):  24.9677  88.7406  27.1753              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.6337 T22:   4.5561                                     
REMARK   3      T33:   2.0823 T12:  -0.8450                                     
REMARK   3      T13:   0.0027 T23:   0.5578                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4337 L22:   1.8276                                     
REMARK   3      L33:  -0.0092 L12:  -1.7263                                     
REMARK   3      L13:   0.1251 L23:  -0.0896                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6118 S12:   3.8275 S13:   1.4183                       
REMARK   3      S21:   0.0161 S22:   0.9499 S23:  -0.0468                       
REMARK   3      S31:  -0.3557 S32:   1.0877 S33:   0.0022                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (RESID 931:983 OR RESID 1305:1367) AND CHAIN A         
REMARK   3    ORIGIN FOR THE GROUP (A): -19.0658  41.4981  65.9448              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.4578 T22:   1.4266                                     
REMARK   3      T33:   2.1414 T12:  -0.0708                                     
REMARK   3      T13:  -0.0156 T23:  -0.0331                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2044 L22:  -0.0591                                     
REMARK   3      L33:   3.0107 L12:  -0.3177                                     
REMARK   3      L13:  -0.2361 L23:   0.3404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4439 S12:   0.8677 S13:  -1.1201                       
REMARK   3      S21:   0.0982 S22:  -0.1239 S23:  -0.1835                       
REMARK   3      S31:   0.6679 S32:  -0.0993 S33:   0.0002                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: RESID 984:1304 AND CHAIN A                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.6947  67.6646  73.1274              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5394 T22:   1.3459                                     
REMARK   3      T33:   1.3045 T12:  -0.1476                                     
REMARK   3      T13:  -0.1293 T23:  -0.0202                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4033 L22:   5.7902                                     
REMARK   3      L33:   3.7375 L12:  -1.7200                                     
REMARK   3      L13:  -1.3973 L23:   0.0906                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0364 S12:   0.1247 S13:  -0.0092                       
REMARK   3      S21:   0.2697 S22:   0.0480 S23:   0.2402                       
REMARK   3      S31:  -0.0462 S32:   0.5210 S33:   0.0001                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: RESID 1368:1520 AND CHAIN A                            
REMARK   3    ORIGIN FOR THE GROUP (A): -33.3664  72.6395  54.7223              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7228 T22:   1.6916                                     
REMARK   3      T33:   1.5093 T12:  -0.2001                                     
REMARK   3      T13:  -0.0756 T23:   0.1481                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2500 L22:   5.5982                                     
REMARK   3      L33:   3.5009 L12:   0.7400                                     
REMARK   3      L13:   0.6078 L23:   2.5039                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3429 S12:   0.6933 S13:   0.3956                       
REMARK   3      S21:   0.1995 S22:  -0.2925 S23:   0.2654                       
REMARK   3      S31:   0.4192 S32:   0.0907 S33:  -0.0000                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: RESID 676:759 AND CHAIN A                              
REMARK   3    ORIGIN FOR THE GROUP (A): -26.3838  98.1266  46.7868              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1666 T22:   2.7812                                     
REMARK   3      T33:   2.3987 T12:   0.1862                                     
REMARK   3      T13:   0.1787 T23:   0.6589                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5171 L22:   2.2466                                     
REMARK   3      L33:   1.1724 L12:  -2.3915                                     
REMARK   3      L13:  -0.2730 L23:   0.9955                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.2224 S12:   2.7347 S13:   1.3379                       
REMARK   3      S21:  -0.9417 S22:  -0.7685 S23:   0.0213                       
REMARK   3      S31:  -0.3506 S32:   0.6105 S33:   0.0007                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: RESID 1525:1700 AND CHAIN A                            
REMARK   3    ORIGIN FOR THE GROUP (A): -56.2163  38.6856  53.3085              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   4.1503 T22:   3.6008                                     
REMARK   3      T33:   3.8026 T12:  -0.6353                                     
REMARK   3      T13:   0.0239 T23:   0.2777                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7035 L22:   0.1194                                     
REMARK   3      L33:   1.5624 L12:  -0.5497                                     
REMARK   3      L13:  -1.7671 L23:   0.5370                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.4306 S12:  -0.9894 S13:  -1.0444                       
REMARK   3      S21:   2.4971 S22:   0.5937 S23:   0.9587                       
REMARK   3      S31:  -0.6265 S32:  -1.6659 S33:  -0.0020                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN H AND RESID 1:120                                
REMARK   3    ORIGIN FOR THE GROUP (A):  69.3023 104.3467 133.8584              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6361 T22:   2.1279                                     
REMARK   3      T33:   2.1087 T12:  -0.0296                                     
REMARK   3      T13:  -0.3396 T23:  -0.1080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1274 L22:   2.7482                                     
REMARK   3      L33:   3.5180 L12:  -1.2634                                     
REMARK   3      L13:   2.2563 L23:  -0.2146                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1014 S12:  -0.2064 S13:   0.1311                       
REMARK   3      S21:  -1.0776 S22:  -0.2610 S23:   0.1102                       
REMARK   3      S31:  -0.3794 S32:   0.2102 S33:  -0.0004                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN H AND RESID 121:230                              
REMARK   3    ORIGIN FOR THE GROUP (A):  90.7756 107.6213 163.8024              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.7413 T22:   4.9418                                     
REMARK   3      T33:   3.3293 T12:   0.5159                                     
REMARK   3      T13:  -1.0062 T23:  -0.7861                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0223 L22:   0.0888                                     
REMARK   3      L33:   0.2969 L12:   0.0396                                     
REMARK   3      L13:  -0.1299 L23:  -0.3275                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1575 S12:  -4.4148 S13:   1.8865                       
REMARK   3      S21:   0.9867 S22:   0.3883 S23:  -0.6587                       
REMARK   3      S31:  -2.0733 S32:  -1.1776 S33:   0.0033                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN L AND RESID 1:105                                
REMARK   3    ORIGIN FOR THE GROUP (A):  83.4290  87.9934 131.1116              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7485 T22:   2.4717                                     
REMARK   3      T33:   2.8597 T12:   0.3197                                     
REMARK   3      T13:  -0.1208 T23:   0.0358                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7254 L22:   0.5326                                     
REMARK   3      L33:   1.6232 L12:  -0.5560                                     
REMARK   3      L13:   1.1426 L23:  -0.7457                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5733 S12:  -1.5528 S13:  -0.2362                       
REMARK   3      S21:  -0.4150 S22:   0.4851 S23:  -0.9527                       
REMARK   3      S31:   1.3988 S32:   1.7416 S33:   0.0002                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN L AND RESID 106:230                              
REMARK   3    ORIGIN FOR THE GROUP (A):  90.0092  92.1838 167.0681              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.1644 T22:   5.0468                                     
REMARK   3      T33:   2.6470 T12:   0.2456                                     
REMARK   3      T13:  -0.2267 T23:  -0.1462                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0647 L22:   1.2183                                     
REMARK   3      L33:   2.2809 L12:   0.1522                                     
REMARK   3      L13:   0.2433 L23:   1.7108                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6429 S12:  -1.5625 S13:   1.0063                       
REMARK   3      S21:   2.7381 S22:  -1.0630 S23:   0.5356                       
REMARK   3      S31:   2.7427 S32:  -2.5781 S33:  -0.0639                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: RESID 19:120 AND CHAIN B                               
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5196  35.2822  75.5519              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.3748 T22:   1.4977                                     
REMARK   3      T33:   1.6784 T12:  -0.1206                                     
REMARK   3      T13:   0.0028 T23:  -0.3091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3726 L22:   1.6911                                     
REMARK   3      L33:   2.7005 L12:   0.6547                                     
REMARK   3      L13:  -1.8323 L23:  -1.2509                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2672 S12:   0.6053 S13:  -0.2937                       
REMARK   3      S21:  -1.2958 S22:  -0.5180 S23:   0.4568                       
REMARK   3      S31:   0.8866 S32:   0.7961 S33:   0.0003                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: RESID 121:224 AND CHAIN B                              
REMARK   3    ORIGIN FOR THE GROUP (A):  32.2300  71.6584  83.1756              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6535 T22:   1.2054                                     
REMARK   3      T33:   1.9069 T12:  -0.2213                                     
REMARK   3      T13:   0.1710 T23:  -0.0546                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7651 L22:   2.9564                                     
REMARK   3      L33:   1.9839 L12:  -0.5058                                     
REMARK   3      L13:   0.1379 L23:  -0.2464                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1060 S12:   0.4396 S13:  -0.0292                       
REMARK   3      S21:  -0.7254 S22:  -0.2992 S23:  -0.1209                       
REMARK   3      S31:  -0.0994 S32:  -0.3508 S33:  -0.0000                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: RESID 225:349 AND CHAIN B                              
REMARK   3    ORIGIN FOR THE GROUP (A):  28.0572  81.4136 118.3565              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5917 T22:   1.5892                                     
REMARK   3      T33:   1.6928 T12:   0.1967                                     
REMARK   3      T13:  -0.1225 T23:  -0.0791                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7966 L22:   2.2650                                     
REMARK   3      L33:   3.6283 L12:   1.6931                                     
REMARK   3      L13:  -3.4279 L23:  -0.5695                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4123 S12:   0.2514 S13:  -0.2299                       
REMARK   3      S21:   0.1952 S22:   0.3089 S23:  -0.3747                       
REMARK   3      S31:   0.2537 S32:   0.1405 S33:   0.0000                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: RESID 350:460 AND CHAIN B                              
REMARK   3    ORIGIN FOR THE GROUP (A):  22.1558  42.8727 116.6889              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7279 T22:   1.3018                                     
REMARK   3      T33:   1.6859 T12:   0.0298                                     
REMARK   3      T13:   0.0915 T23:   0.0741                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5223 L22:   3.9092                                     
REMARK   3      L33:   4.7302 L12:  -0.3816                                     
REMARK   3      L13:   0.0395 L23:   1.7320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0686 S12:  -0.1356 S13:  -0.1866                       
REMARK   3      S21:  -0.1379 S22:   0.1115 S23:  -0.2669                       
REMARK   3      S31:  -0.3798 S32:   0.1048 S33:   0.0002                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: RESID 461:566 AND CHAIN B                              
REMARK   3    ORIGIN FOR THE GROUP (A):  30.6459  30.6272  97.5595              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8098 T22:   0.9951                                     
REMARK   3      T33:   1.9474 T12:   0.1012                                     
REMARK   3      T13:   0.0396 T23:  -0.0553                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4493 L22:   4.7864                                     
REMARK   3      L33:   2.7586 L12:   0.2487                                     
REMARK   3      L13:  -0.4158 L23:  -1.7233                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3380 S12:  -0.6589 S13:  -0.0882                       
REMARK   3      S21:  -0.3345 S22:  -0.4469 S23:  -0.9906                       
REMARK   3      S31:   0.8145 S32:   0.9286 S33:  -0.0003                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: (RESID 567:606 OR RESID 760:821) AND CHAIN B           
REMARK   3    ORIGIN FOR THE GROUP (A):  50.3287  69.5970  93.3101              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5616 T22:   1.4840                                     
REMARK   3      T33:   2.1153 T12:   0.1749                                     
REMARK   3      T13:  -0.0462 T23:   0.0083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6963 L22:   2.6439                                     
REMARK   3      L33:   0.7289 L12:   1.3473                                     
REMARK   3      L13:   1.7393 L23:   0.4941                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3224 S12:  -0.3549 S13:  -0.6603                       
REMARK   3      S21:   0.8670 S22:  -0.0698 S23:  -0.4129                       
REMARK   3      S31:   0.2315 S32:  -0.0442 S33:   0.0001                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: RESID 822:930 AND CHAIN B                              
REMARK   3    ORIGIN FOR THE GROUP (A):  62.1517 101.1343 106.0784              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6376 T22:   1.7122                                     
REMARK   3      T33:   2.0608 T12:  -0.1985                                     
REMARK   3      T13:   0.0429 T23:  -0.1034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2873 L22:   6.2915                                     
REMARK   3      L33:   2.0855 L12:  -1.8376                                     
REMARK   3      L13:   2.2044 L23:  -1.4046                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0300 S12:  -0.8259 S13:   0.1524                       
REMARK   3      S21:  -0.5558 S22:   0.7422 S23:  -0.8684                       
REMARK   3      S31:   0.4030 S32:  -0.0977 S33:  -0.0005                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: RESID 607:673 AND CHAIN B                              
REMARK   3    ORIGIN FOR THE GROUP (A):  24.2842  49.3802  94.1844              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9287 T22:   1.6149                                     
REMARK   3      T33:   1.8932 T12:   0.0857                                     
REMARK   3      T13:   0.1599 T23:  -0.0178                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2845 L22:   1.4546                                     
REMARK   3      L33:   1.6089 L12:   1.2708                                     
REMARK   3      L13:  -1.3736 L23:  -0.7408                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2134 S12:  -0.0472 S13:  -0.3157                       
REMARK   3      S21:  -0.5891 S22:  -0.4822 S23:  -0.9002                       
REMARK   3      S31:  -0.7760 S32:  -0.3658 S33:  -0.0010                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: (RESID 931:983 OR RESID 1305:1367) AND CHAIN B         
REMARK   3    ORIGIN FOR THE GROUP (A):  52.1106 111.7601  64.8671              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8490 T22:   2.0169                                     
REMARK   3      T33:   2.1506 T12:  -0.2547                                     
REMARK   3      T13:   0.3956 T23:   0.0800                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1354 L22:   2.9790                                     
REMARK   3      L33:   3.1052 L12:  -0.2358                                     
REMARK   3      L13:   1.0976 L23:   0.5388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4329 S12:   0.6568 S13:   0.0240                       
REMARK   3      S21:   0.4102 S22:   0.1953 S23:   0.1054                       
REMARK   3      S31:   0.1730 S32:   0.0831 S33:   0.0001                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: RESID 984:1304 AND CHAIN B                             
REMARK   3    ORIGIN FOR THE GROUP (A):  24.3640 103.2839  67.0735              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5923 T22:   1.4598                                     
REMARK   3      T33:   1.5785 T12:  -0.1301                                     
REMARK   3      T13:  -0.0911 T23:   0.2282                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9450 L22:   3.5846                                     
REMARK   3      L33:   3.8911 L12:  -1.4879                                     
REMARK   3      L13:  -0.1944 L23:  -0.1055                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0638 S12:   0.6733 S13:   0.5203                       
REMARK   3      S21:  -0.1648 S22:   0.1572 S23:   0.0552                       
REMARK   3      S31:   0.1078 S32:  -0.2542 S33:   0.0001                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: RESID 1368:1520 AND CHAIN B                            
REMARK   3    ORIGIN FOR THE GROUP (A):  32.3065 115.3965  94.6979              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7612 T22:   1.3280                                     
REMARK   3      T33:   2.0216 T12:  -0.0883                                     
REMARK   3      T13:   0.0565 T23:  -0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4306 L22:   1.3470                                     
REMARK   3      L33:   2.8279 L12:   1.0074                                     
REMARK   3      L13:   1.2606 L23:   0.8178                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2108 S12:  -0.3134 S13:   0.4906                       
REMARK   3      S21:   0.3363 S22:   0.0428 S23:   0.1954                       
REMARK   3      S31:  -0.2165 S32:  -0.2000 S33:   0.0001                       
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    SELECTION: RESID 676:759 AND CHAIN B                              
REMARK   3    ORIGIN FOR THE GROUP (A):  12.9786 102.2486 109.2576              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.6068 T22:   2.1089                                     
REMARK   3      T33:   2.4160 T12:   0.0192                                     
REMARK   3      T13:   0.1621 T23:   0.2365                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9780 L22:   0.8777                                     
REMARK   3      L33:   0.8999 L12:  -0.8665                                     
REMARK   3      L13:  -0.4399 L23:   0.0946                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8356 S12:  -0.7262 S13:   0.1912                       
REMARK   3      S21:   0.9949 S22:  -0.1074 S23:  -0.0845                       
REMARK   3      S31:   0.4055 S32:  -0.6575 S33:  -0.0001                       
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    SELECTION: RESID 1525:1700 AND CHAIN B                            
REMARK   3    ORIGIN FOR THE GROUP (A):  65.0070 140.4843  93.6650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8211 T22:   1.2477                                     
REMARK   3      T33:   2.2569 T12:  -0.0733                                     
REMARK   3      T13:   0.3394 T23:  -0.1753                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0378 L22:   5.2699                                     
REMARK   3      L33:   4.0507 L12:   0.0929                                     
REMARK   3      L13:   0.0044 L23:  -1.9443                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1552 S12:   0.5369 S13:   0.3348                       
REMARK   3      S21:  -0.8123 S22:   0.5769 S23:  -0.9104                       
REMARK   3      S31:  -0.5486 S32:   0.5409 S33:  -0.0002                       
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    SELECTION: CHAIN X AND RESID 1:120                                
REMARK   3    ORIGIN FOR THE GROUP (A): -46.8944  57.8315   2.0379              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.6896 T22:   3.1210                                     
REMARK   3      T33:   1.9217 T12:  -0.5189                                     
REMARK   3      T13:  -0.0893 T23:   0.4109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2584 L22:   1.6471                                     
REMARK   3      L33:   2.7964 L12:   1.8836                                     
REMARK   3      L13:   0.5392 L23:  -0.2014                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4390 S12:  -1.0334 S13:   0.7386                       
REMARK   3      S21:   0.4756 S22:   0.8483 S23:   1.4114                       
REMARK   3      S31:   1.4762 S32:  -1.4162 S33:   0.0003                       
REMARK   3   TLS GROUP : 32                                                     
REMARK   3    SELECTION: CHAIN X AND RESID 121:230                              
REMARK   3    ORIGIN FOR THE GROUP (A): -62.7009  50.8366 -31.0962              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.9613 T22:   5.5200                                     
REMARK   3      T33:   1.8971 T12:  -0.9709                                     
REMARK   3      T13:  -0.8148 T23:   0.0908                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8772 L22:   4.6151                                     
REMARK   3      L33:   0.0148 L12:  -1.1434                                     
REMARK   3      L13:  -0.0579 L23:  -0.2525                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1500 S12:   1.6550 S13:   0.0522                       
REMARK   3      S21:  -2.2380 S22:   0.3429 S23:  -0.2820                       
REMARK   3      S31:   0.9325 S32:  -4.3007 S33:   0.3820                       
REMARK   3   TLS GROUP : 33                                                     
REMARK   3    SELECTION: CHAIN Y AND RESID 1:105                                
REMARK   3    ORIGIN FOR THE GROUP (A): -30.9310  48.0456  -9.3747              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.9106 T22:   2.1079                                     
REMARK   3      T33:   1.7580 T12:  -0.1295                                     
REMARK   3      T13:   0.0760 T23:   0.0573                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6457 L22:   1.7758                                     
REMARK   3      L33:   2.4139 L12:  -1.1444                                     
REMARK   3      L13:  -1.4287 L23:  -1.0722                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5206 S12:   0.7581 S13:  -0.5100                       
REMARK   3      S21:  -2.3791 S22:   0.4469 S23:  -0.0020                       
REMARK   3      S31:   1.7570 S32:   1.5590 S33:   0.0009                       
REMARK   3   TLS GROUP : 34                                                     
REMARK   3    SELECTION: CHAIN Y AND RESID 106:230                              
REMARK   3    ORIGIN FOR THE GROUP (A): -50.5206  57.4187 -38.0880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.2691 T22:   4.8286                                     
REMARK   3      T33:   1.3746 T12:  -0.3531                                     
REMARK   3      T13:  -0.5633 T23:   0.1076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6246 L22:   0.7338                                     
REMARK   3      L33:   0.4597 L12:   0.3699                                     
REMARK   3      L13:  -0.1393 L23:  -0.4489                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2354 S12:   1.9905 S13:   2.2658                       
REMARK   3      S21:  -0.0333 S22:   0.2482 S23:   0.7850                       
REMARK   3      S31:   1.8827 S32:  -3.0883 S33:   0.0618                       
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 5I5K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-FEB-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000218321.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 76073                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.16600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.2800                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.01                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.290                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4KMT, 3PVM                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M IMIDAZOLE PH 6.2 4% V/V            
REMARK 280  TACSIMATE PH 7 8% PEG 3350, VAPOR DIFFUSION, SITTING DROP,          
REMARK 280  TEMPERATURE 277.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       98.85200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      134.66050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       98.85200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000      134.66050            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H, L                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, X, Y                               
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     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     ILE B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     CYS B     8                                                      
REMARK 465     PHE B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     ILE B    11                                                      
REMARK 465     PHE B    12                                                      
REMARK 465     LEU B    13                                                      
REMARK 465     GLY B    14                                                      
REMARK 465     LYS B    15                                                      
REMARK 465     THR B    16                                                      
REMARK 465     TRP B    17                                                      
REMARK 465     GLY B    18                                                      
REMARK 465     GLN B    19                                                      
REMARK 465     GLU B   671                                                      
REMARK 465     ILE B   672                                                      
REMARK 465     LEU B   673                                                      
REMARK 465     ARG B   674                                                      
REMARK 465     PRO B   675                                                      
REMARK 465     ARG B   676                                                      
REMARK 465     ARG B   677                                                      
REMARK 465     THR B   678                                                      
REMARK 465     ALA B  1388                                                      
REMARK 465     SER B  1389                                                      
REMARK 465     HIS B  1390                                                      
REMARK 465     TYR B  1391                                                      
REMARK 465     ARG B  1392                                                      
REMARK 465     GLY B  1393                                                      
REMARK 465     TYR B  1394                                                      
REMARK 465     GLY B  1395                                                      
REMARK 465     ASN B  1396                                                      
REMARK 465     GLN B  1517                                                      
REMARK 465     LYS B  1518                                                      
REMARK 465     VAL B  1519                                                      
REMARK 465     CYS B  1520                                                      
REMARK 465     GLU B  1521                                                      
REMARK 465     GLY B  1522                                                      
REMARK 465     PRO H   222                                                      
REMARK 465     LYS H   223                                                      
REMARK 465     SER H   224                                                      
REMARK 465     CYS H   225                                                      
REMARK 465     ASP H   226                                                      
REMARK 465     LYS H   227                                                      
REMARK 465     THR H   228                                                      
REMARK 465     HIS H   229                                                      
REMARK 465     THR H   230                                                      
REMARK 465     CYS L   214                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     ILE A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     CYS A     8                                                      
REMARK 465     PHE A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     ILE A    11                                                      
REMARK 465     PHE A    12                                                      
REMARK 465     LEU A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     LYS A    15                                                      
REMARK 465     THR A    16                                                      
REMARK 465     TRP A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     GLN A    19                                                      
REMARK 465     GLU A   671                                                      
REMARK 465     ILE A   672                                                      
REMARK 465     LEU A   673                                                      
REMARK 465     ARG A   674                                                      
REMARK 465     PRO A   675                                                      
REMARK 465     ARG A   676                                                      
REMARK 465     ARG A   677                                                      
REMARK 465     THR A   678                                                      
REMARK 465     ALA A  1388                                                      
REMARK 465     SER A  1389                                                      
REMARK 465     HIS A  1390                                                      
REMARK 465     TYR A  1391                                                      
REMARK 465     ARG A  1392                                                      
REMARK 465     GLY A  1393                                                      
REMARK 465     TYR A  1394                                                      
REMARK 465     GLY A  1395                                                      
REMARK 465     ASN A  1396                                                      
REMARK 465     GLN A  1517                                                      
REMARK 465     LYS A  1518                                                      
REMARK 465     VAL A  1519                                                      
REMARK 465     CYS A  1520                                                      
REMARK 465     GLU A  1521                                                      
REMARK 465     GLY A  1522                                                      
REMARK 465     ALA A  1523                                                      
REMARK 465     ALA A  1524                                                      
REMARK 465     PRO X   222                                                      
REMARK 465     LYS X   223                                                      
REMARK 465     SER X   224                                                      
REMARK 465     CYS X   225                                                      
REMARK 465     ASP X   226                                                      
REMARK 465     LYS X   227                                                      
REMARK 465     THR X   228                                                      
REMARK 465     HIS X   229                                                      
REMARK 465     THR X   230                                                      
REMARK 465     CYS Y   214                                                      
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   NZ   LYS A   364     OD2  ASP A   557              1.85            
REMARK 500   NH1  ARG B   717     O    ASP B  1447              1.99            
REMARK 500   OD2  ASP A   150     NZ   LYS A   508              2.00            
REMARK 500   NZ   LYS B  1229     O    SER B  1238              2.05            
REMARK 500   NH1  ARG A   717     O    ASP A  1447              2.06            
REMARK 500   NZ   LYS A  1229     O    SER A  1238              2.06            
REMARK 500   OD1  ASP A   131     OH   TYR A   135              2.08            
REMARK 500   OD2  ASP L   170     OG1  THR L   172              2.08            
REMARK 500   OD2  ASP Y   170     OG1  THR Y   172              2.09            
REMARK 500   OD1  ASP B   131     OH   TYR B   135              2.12            
REMARK 500   NZ   LYS B  1128     OG   SER B  1417              2.13            
REMARK 500   OD2  ASP B   150     NZ   LYS B   508              2.14            
REMARK 500   NZ   LYS B   506     O    ASN B   533              2.15            
REMARK 500   OG   SER B    58     O    ASP B    61              2.18            
REMARK 500   O    SER B  1427     OH   TYR B  1509              2.18            
REMARK 500   O    SER B  1286     OG1  THR B  1290              2.18            
REMARK 500   O    PRO B  1160     ND2  ASN A  1098              2.18            
REMARK 500   OG1  THR B   594     O    MET B   596              2.18            
REMARK 500   O    PRO B   360     OH   TYR B   369              2.19            
REMARK 500   O    LEU A  1175     OG1  THR A  1179              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER B 576   C     PRO B 577   N       0.178                       
REMARK 500    SER A 576   C     PRO A 577   N       0.195                       
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    GLU B  48     -133.91     61.50                                   
REMARK 500    ASN B 123      -75.51   -121.55                                   
REMARK 500    ALA B 155       71.59     51.43                                   
REMARK 500    VAL B 171      -64.98    -97.63                                   
REMARK 500    GLU B 207      -79.75   -103.05                                   
REMARK 500    TYR B 254      -78.85    -99.08                                   
REMARK 500    TYR B 256     -114.94     55.52                                   
REMARK 500    THR B 261      -72.64    -81.67                                   
REMARK 500    VAL B 307      -61.99   -106.91                                   
REMARK 500    LEU B 349      -70.03    -57.88                                   
REMARK 500    LEU B 476       70.08     62.66                                   
REMARK 500    SER B 490       50.61   -148.91                                   
REMARK 500    ASP B 520      -72.29    -94.97                                   
REMARK 500    SER B 522      -73.39    -89.26                                   
REMARK 500    SER B 537      162.33    177.25                                   
REMARK 500    GLN B 550      -64.65    -95.02                                   
REMARK 500    LYS B 745      -64.90   -142.89                                   
REMARK 500    LEU B 757      -20.22     74.53                                   
REMARK 500    SER B 761      172.71    175.57                                   
REMARK 500    GLU B 764      162.81    177.70                                   
REMARK 500    ARG B 782      -15.81     69.02                                   
REMARK 500    SER B 868       -4.05     68.35                                   
REMARK 500    GLU B 869      -57.31   -128.51                                   
REMARK 500    SER B 870       63.55     62.58                                   
REMARK 500    LYS B 882     -142.84     58.85                                   
REMARK 500    CYS B 883      161.21    176.77                                   
REMARK 500    LEU B 901      131.52   -175.22                                   
REMARK 500    LEU B 903      -63.69   -122.44                                   
REMARK 500    PRO B1181       74.59    -66.91                                   
REMARK 500    GLN B1183      -66.86   -121.60                                   
REMARK 500    ILE B1224      -60.11   -109.33                                   
REMARK 500    LEU B1232      -76.31   -126.53                                   
REMARK 500    LYS B1235       -8.74    -59.42                                   
REMARK 500    LEU B1303      -71.60    -92.37                                   
REMARK 500    LYS B1318      -71.22    -55.22                                   
REMARK 500    CYS B1525      -64.51   -131.57                                   
REMARK 500    CYS B1532      -63.79    -94.96                                   
REMARK 500    LEU B1539     -140.51     56.18                                   
REMARK 500    THR B1566      -62.63   -109.19                                   
REMARK 500    VAL B1573       -8.84     68.22                                   
REMARK 500    LEU B1582      -66.63   -120.29                                   
REMARK 500    ASN B1630      -22.69     75.75                                   
REMARK 500    ASP B1651      -15.10     58.75                                   
REMARK 500    MET H  48      -63.76   -103.21                                   
REMARK 500    ASP H 110      -75.63    -94.79                                   
REMARK 500    SER H 124     -118.60     56.44                                   
REMARK 500    PHE H 155      137.73   -177.61                                   
REMARK 500    GLN H 201      165.29    171.60                                   
REMARK 500    TYR L  30     -117.05     59.25                                   
REMARK 500    ALA L  51       -4.69     71.71                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     114 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 LYS B  489     SER B  490                  123.23                    
REMARK 500 ASP B  494     LYS B  495                  140.36                    
REMARK 500 TYR H  108     PHE H  109                  145.42                    
REMARK 500 LYS A  489     SER A  490                  124.99                    
REMARK 500 ASP A  494     LYS A  495                  141.36                    
REMARK 500 TYR X  108     PHE X  109                  147.81                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  2001 through BMA A 2003 bound to ASN A 911                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  2001 through BMA B 2003 bound to ASN B 911                          
DBREF  5I5K B    1  1676  UNP    P01031   CO5_HUMAN        1   1676             
DBREF  5I5K H    1   230  PDB    5I5K     5I5K             1    230             
DBREF  5I5K L    1   214  PDB    5I5K     5I5K             1    214             
DBREF  5I5K A    1  1676  UNP    P01031   CO5_HUMAN        1   1676             
DBREF  5I5K X    1   230  PDB    5I5K     5I5K             1    230             
DBREF  5I5K Y    1   214  PDB    5I5K     5I5K             1    214             
SEQRES   1 B 1676  MET GLY LEU LEU GLY ILE LEU CYS PHE LEU ILE PHE LEU          
SEQRES   2 B 1676  GLY LYS THR TRP GLY GLN GLU GLN THR TYR VAL ILE SER          
SEQRES   3 B 1676  ALA PRO LYS ILE PHE ARG VAL GLY ALA SER GLU ASN ILE          
SEQRES   4 B 1676  VAL ILE GLN VAL TYR GLY TYR THR GLU ALA PHE ASP ALA          
SEQRES   5 B 1676  THR ILE SER ILE LYS SER TYR PRO ASP LYS LYS PHE SER          
SEQRES   6 B 1676  TYR SER SER GLY HIS VAL HIS LEU SER SER GLU ASN LYS          
SEQRES   7 B 1676  PHE GLN ASN SER ALA ILE LEU THR ILE GLN PRO LYS GLN          
SEQRES   8 B 1676  LEU PRO GLY GLY GLN ASN PRO VAL SER TYR VAL TYR LEU          
SEQRES   9 B 1676  GLU VAL VAL SER LYS HIS PHE SER LYS SER LYS ARG MET          
SEQRES  10 B 1676  PRO ILE THR TYR ASP ASN GLY PHE LEU PHE ILE HIS THR          
SEQRES  11 B 1676  ASP LYS PRO VAL TYR THR PRO ASP GLN SER VAL LYS VAL          
SEQRES  12 B 1676  ARG VAL TYR SER LEU ASN ASP ASP LEU LYS PRO ALA LYS          
SEQRES  13 B 1676  ARG GLU THR VAL LEU THR PHE ILE ASP PRO GLU GLY SER          
SEQRES  14 B 1676  GLU VAL ASP MET VAL GLU GLU ILE ASP HIS ILE GLY ILE          
SEQRES  15 B 1676  ILE SER PHE PRO ASP PHE LYS ILE PRO SER ASN PRO ARG          
SEQRES  16 B 1676  TYR GLY MET TRP THR ILE LYS ALA LYS TYR LYS GLU ASP          
SEQRES  17 B 1676  PHE SER THR THR GLY THR ALA TYR PHE GLU VAL LYS GLU          
SEQRES  18 B 1676  TYR VAL LEU PRO HIS PHE SER VAL SER ILE GLU PRO GLU          
SEQRES  19 B 1676  TYR ASN PHE ILE GLY TYR LYS ASN PHE LYS ASN PHE GLU          
SEQRES  20 B 1676  ILE THR ILE LYS ALA ARG TYR PHE TYR ASN LYS VAL VAL          
SEQRES  21 B 1676  THR GLU ALA ASP VAL TYR ILE THR PHE GLY ILE ARG GLU          
SEQRES  22 B 1676  ASP LEU LYS ASP ASP GLN LYS GLU MET MET GLN THR ALA          
SEQRES  23 B 1676  MET GLN ASN THR MET LEU ILE ASN GLY ILE ALA GLN VAL          
SEQRES  24 B 1676  THR PHE ASP SER GLU THR ALA VAL LYS GLU LEU SER TYR          
SEQRES  25 B 1676  TYR SER LEU GLU ASP LEU ASN ASN LYS TYR LEU TYR ILE          
SEQRES  26 B 1676  ALA VAL THR VAL ILE GLU SER THR GLY GLY PHE SER GLU          
SEQRES  27 B 1676  GLU ALA GLU ILE PRO GLY ILE LYS TYR VAL LEU SER PRO          
SEQRES  28 B 1676  TYR LYS LEU ASN LEU VAL ALA THR PRO LEU PHE LEU LYS          
SEQRES  29 B 1676  PRO GLY ILE PRO TYR PRO ILE LYS VAL GLN VAL LYS ASP          
SEQRES  30 B 1676  SER LEU ASP GLN LEU VAL GLY GLY VAL PRO VAL THR LEU          
SEQRES  31 B 1676  ASN ALA GLN THR ILE ASP VAL ASN GLN GLU THR SER ASP          
SEQRES  32 B 1676  LEU ASP PRO SER LYS SER VAL THR ARG VAL ASP ASP GLY          
SEQRES  33 B 1676  VAL ALA SER PHE VAL LEU ASN LEU PRO SER GLY VAL THR          
SEQRES  34 B 1676  VAL LEU GLU PHE ASN VAL LYS THR ASP ALA PRO ASP LEU          
SEQRES  35 B 1676  PRO GLU GLU ASN GLN ALA ARG GLU GLY TYR ARG ALA ILE          
SEQRES  36 B 1676  ALA TYR SER SER LEU SER GLN SER TYR LEU TYR ILE ASP          
SEQRES  37 B 1676  TRP THR ASP ASN HIS LYS ALA LEU LEU VAL GLY GLU HIS          
SEQRES  38 B 1676  LEU ASN ILE ILE VAL THR PRO LYS SER PRO TYR ILE ASP          
SEQRES  39 B 1676  LYS ILE THR HIS TYR ASN TYR LEU ILE LEU SER LYS GLY          
SEQRES  40 B 1676  LYS ILE ILE HIS PHE GLY THR ARG GLU LYS PHE SER ASP          
SEQRES  41 B 1676  ALA SER TYR GLN SER ILE ASN ILE PRO VAL THR GLN ASN          
SEQRES  42 B 1676  MET VAL PRO SER SER ARG LEU LEU VAL TYR TYR ILE VAL          
SEQRES  43 B 1676  THR GLY GLU GLN THR ALA GLU LEU VAL SER ASP SER VAL          
SEQRES  44 B 1676  TRP LEU ASN ILE GLU GLU LYS CYS GLY ASN GLN LEU GLN          
SEQRES  45 B 1676  VAL HIS LEU SER PRO ASP ALA ASP ALA TYR SER PRO GLY          
SEQRES  46 B 1676  GLN THR VAL SER LEU ASN MET ALA THR GLY MET ASP SER          
SEQRES  47 B 1676  TRP VAL ALA LEU ALA ALA VAL ASP SER ALA VAL TYR GLY          
SEQRES  48 B 1676  VAL GLN ARG GLY ALA LYS LYS PRO LEU GLU ARG VAL PHE          
SEQRES  49 B 1676  GLN PHE LEU GLU LYS SER ASP LEU GLY CYS GLY ALA GLY          
SEQRES  50 B 1676  GLY GLY LEU ASN ASN ALA ASN VAL PHE HIS LEU ALA GLY          
SEQRES  51 B 1676  LEU THR PHE LEU THR ASN ALA ASN ALA ASP ASP SER GLN          
SEQRES  52 B 1676  GLU ASN ASP GLU PRO CYS LYS GLU ILE LEU ARG PRO ARG          
SEQRES  53 B 1676  ARG THR LEU GLN LYS LYS ILE GLU GLU ILE ALA ALA LYS          
SEQRES  54 B 1676  TYR LYS HIS SER VAL VAL LYS LYS CYS CYS TYR ASP GLY          
SEQRES  55 B 1676  ALA CYS VAL ASN ASN ASP GLU THR CYS GLU GLN ARG ALA          
SEQRES  56 B 1676  ALA ARG ILE SER LEU GLY PRO ARG CYS ILE LYS ALA PHE          
SEQRES  57 B 1676  THR GLU CYS CYS VAL VAL ALA SER GLN LEU ARG ALA ASN          
SEQRES  58 B 1676  ILE SER HIS LYS ASP MET GLN LEU GLY ARG LEU HIS MET          
SEQRES  59 B 1676  LYS THR LEU LEU PRO VAL SER LYS PRO GLU ILE ARG SER          
SEQRES  60 B 1676  TYR PHE PRO GLU SER TRP LEU TRP GLU VAL HIS LEU VAL          
SEQRES  61 B 1676  PRO ARG ARG LYS GLN LEU GLN PHE ALA LEU PRO ASP SER          
SEQRES  62 B 1676  LEU THR THR TRP GLU ILE GLN GLY VAL GLY ILE SER ASN          
SEQRES  63 B 1676  THR GLY ILE CYS VAL ALA ASP THR VAL LYS ALA LYS VAL          
SEQRES  64 B 1676  PHE LYS ASP VAL PHE LEU GLU MET ASN ILE PRO TYR SER          
SEQRES  65 B 1676  VAL VAL ARG GLY GLU GLN ILE GLN LEU LYS GLY THR VAL          
SEQRES  66 B 1676  TYR ASN TYR ARG THR SER GLY MET GLN PHE CYS VAL LYS          
SEQRES  67 B 1676  MET SER ALA VAL GLU GLY ILE CYS THR SER GLU SER PRO          
SEQRES  68 B 1676  VAL ILE ASP HIS GLN GLY THR LYS SER SER LYS CYS VAL          
SEQRES  69 B 1676  ARG GLN LYS VAL GLU GLY SER SER SER HIS LEU VAL THR          
SEQRES  70 B 1676  PHE THR VAL LEU PRO LEU GLU ILE GLY LEU HIS ASN ILE          
SEQRES  71 B 1676  ASN PHE SER LEU GLU THR TRP PHE GLY LYS GLU ILE LEU          
SEQRES  72 B 1676  VAL LYS THR LEU ARG VAL VAL PRO GLU GLY VAL LYS ARG          
SEQRES  73 B 1676  GLU SER TYR SER GLY VAL THR LEU ASP PRO ARG GLY ILE          
SEQRES  74 B 1676  TYR GLY THR ILE SER ARG ARG LYS GLU PHE PRO TYR ARG          
SEQRES  75 B 1676  ILE PRO LEU ASP LEU VAL PRO LYS THR GLU ILE LYS ARG          
SEQRES  76 B 1676  ILE LEU SER VAL LYS GLY LEU LEU VAL GLY GLU ILE LEU          
SEQRES  77 B 1676  SER ALA VAL LEU SER GLN GLU GLY ILE ASN ILE LEU THR          
SEQRES  78 B 1676  HIS LEU PRO LYS GLY SER ALA GLU ALA GLU LEU MET SER          
SEQRES  79 B 1676  VAL VAL PRO VAL PHE TYR VAL PHE HIS TYR LEU GLU THR          
SEQRES  80 B 1676  GLY ASN HIS TRP ASN ILE PHE HIS SER ASP PRO LEU ILE          
SEQRES  81 B 1676  GLU LYS GLN LYS LEU LYS LYS LYS LEU LYS GLU GLY MET          
SEQRES  82 B 1676  LEU SER ILE MET SER TYR ARG ASN ALA ASP TYR SER TYR          
SEQRES  83 B 1676  SER VAL TRP LYS GLY GLY SER ALA SER THR TRP LEU THR          
SEQRES  84 B 1676  ALA PHE ALA LEU ARG VAL LEU GLY GLN VAL ASN LYS TYR          
SEQRES  85 B 1676  VAL GLU GLN ASN GLN ASN SER ILE CYS ASN SER LEU LEU          
SEQRES  86 B 1676  TRP LEU VAL GLU ASN TYR GLN LEU ASP ASN GLY SER PHE          
SEQRES  87 B 1676  LYS GLU ASN SER GLN TYR GLN PRO ILE LYS LEU GLN GLY          
SEQRES  88 B 1676  THR LEU PRO VAL GLU ALA ARG GLU ASN SER LEU TYR LEU          
SEQRES  89 B 1676  THR ALA PHE THR VAL ILE GLY ILE ARG LYS ALA PHE ASP          
SEQRES  90 B 1676  ILE CYS PRO LEU VAL LYS ILE ASP THR ALA LEU ILE LYS          
SEQRES  91 B 1676  ALA ASP ASN PHE LEU LEU GLU ASN THR LEU PRO ALA GLN          
SEQRES  92 B 1676  SER THR PHE THR LEU ALA ILE SER ALA TYR ALA LEU SER          
SEQRES  93 B 1676  LEU GLY ASP LYS THR HIS PRO GLN PHE ARG SER ILE VAL          
SEQRES  94 B 1676  SER ALA LEU LYS ARG GLU ALA LEU VAL LYS GLY ASN PRO          
SEQRES  95 B 1676  PRO ILE TYR ARG PHE TRP LYS ASP ASN LEU GLN HIS LYS          
SEQRES  96 B 1676  ASP SER SER VAL PRO ASN THR GLY THR ALA ARG MET VAL          
SEQRES  97 B 1676  GLU THR THR ALA TYR ALA LEU LEU THR SER LEU ASN LEU          
SEQRES  98 B 1676  LYS ASP ILE ASN TYR VAL ASN PRO VAL ILE LYS TRP LEU          
SEQRES  99 B 1676  SER GLU GLU GLN ARG TYR GLY GLY GLY PHE TYR SER THR          
SEQRES 100 B 1676  GLN ASP THR ILE ASN ALA ILE GLU GLY LEU THR GLU TYR          
SEQRES 101 B 1676  SER LEU LEU VAL LYS GLN LEU ARG LEU SER MET ASP ILE          
SEQRES 102 B 1676  ASP VAL SER TYR LYS HIS LYS GLY ALA LEU HIS ASN TYR          
SEQRES 103 B 1676  LYS MET THR ASP LYS ASN PHE LEU GLY ARG PRO VAL GLU          
SEQRES 104 B 1676  VAL LEU LEU ASN ASP ASP LEU ILE VAL SER THR GLY PHE          
SEQRES 105 B 1676  GLY SER GLY LEU ALA THR VAL HIS VAL THR THR VAL VAL          
SEQRES 106 B 1676  HIS LYS THR SER THR SER GLU GLU VAL CYS SER PHE TYR          
SEQRES 107 B 1676  LEU LYS ILE ASP THR GLN ASP ILE GLU ALA SER HIS TYR          
SEQRES 108 B 1676  ARG GLY TYR GLY ASN SER ASP TYR LYS ARG ILE VAL ALA          
SEQRES 109 B 1676  CYS ALA SER TYR LYS PRO SER ARG GLU GLU SER SER SER          
SEQRES 110 B 1676  GLY SER SER HIS ALA VAL MET ASP ILE SER LEU PRO THR          
SEQRES 111 B 1676  GLY ILE SER ALA ASN GLU GLU ASP LEU LYS ALA LEU VAL          
SEQRES 112 B 1676  GLU GLY VAL ASP GLN LEU PHE THR ASP TYR GLN ILE LYS          
SEQRES 113 B 1676  ASP GLY HIS VAL ILE LEU GLN LEU ASN SER ILE PRO SER          
SEQRES 114 B 1676  SER ASP PHE LEU CYS VAL ARG PHE ARG ILE PHE GLU LEU          
SEQRES 115 B 1676  PHE GLU VAL GLY PHE LEU SER PRO ALA THR PHE THR VAL          
SEQRES 116 B 1676  TYR GLU TYR HIS ARG PRO ASP LYS GLN CYS THR MET PHE          
SEQRES 117 B 1676  TYR SER THR SER ASN ILE LYS ILE GLN LYS VAL CYS GLU          
SEQRES 118 B 1676  GLY ALA ALA CYS LYS CYS VAL GLU ALA ASP CYS GLY GLN          
SEQRES 119 B 1676  MET GLN GLU GLU LEU ASP LEU THR ILE SER ALA GLU THR          
SEQRES 120 B 1676  ARG LYS GLN THR ALA CYS LYS PRO GLU ILE ALA TYR ALA          
SEQRES 121 B 1676  TYR LYS VAL SER ILE THR SER ILE THR VAL GLU ASN VAL          
SEQRES 122 B 1676  PHE VAL LYS TYR LYS ALA THR LEU LEU ASP ILE TYR LYS          
SEQRES 123 B 1676  THR GLY GLU ALA VAL ALA GLU LYS ASP SER GLU ILE THR          
SEQRES 124 B 1676  PHE ILE LYS LYS VAL THR CYS THR ASN ALA GLU LEU VAL          
SEQRES 125 B 1676  LYS GLY ARG GLN TYR LEU ILE MET GLY LYS GLU ALA LEU          
SEQRES 126 B 1676  GLN ILE LYS TYR ASN PHE SER PHE ARG TYR ILE TYR PRO          
SEQRES 127 B 1676  LEU ASP SER LEU THR TRP ILE GLU TYR TRP PRO ARG ASP          
SEQRES 128 B 1676  THR THR CYS SER SER CYS GLN ALA PHE LEU ALA ASN LEU          
SEQRES 129 B 1676  ASP GLU PHE ALA GLU ASP ILE PHE LEU ASN GLY CYS              
SEQRES   1 H  230  GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 H  230  PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY          
SEQRES   3 H  230  TYR ILE PHE SER ASN TYR TRP ILE GLN TRP VAL ARG GLN          
SEQRES   4 H  230  ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLU ILE LEU          
SEQRES   5 H  230  PRO GLY SER GLY SER THR GLU TYR THR GLU ASN PHE LYS          
SEQRES   6 H  230  ASP ARG VAL THR MET THR ARG ASP THR SER THR SER THR          
SEQRES   7 H  230  VAL TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR          
SEQRES   8 H  230  ALA VAL TYR TYR CYS ALA ARG TYR PHE PHE GLY SER SER          
SEQRES   9 H  230  PRO ASN TRP TYR PHE ASP VAL TRP GLY GLN GLY THR LEU          
SEQRES  10 H  230  VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL          
SEQRES  11 H  230  PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY          
SEQRES  12 H  230  THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO          
SEQRES  13 H  230  GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR          
SEQRES  14 H  230  SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER          
SEQRES  15 H  230  GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER          
SEQRES  16 H  230  SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN          
SEQRES  17 H  230  HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU          
SEQRES  18 H  230  PRO LYS SER CYS ASP LYS THR HIS THR                          
SEQRES   1 L  214  ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA          
SEQRES   2 L  214  SER VAL GLY ASP ARG VAL THR ILE THR CYS GLY ALA SER          
SEQRES   3 L  214  GLU ASN ILE TYR GLY ALA LEU ASN TRP TYR GLN GLN LYS          
SEQRES   4 L  214  PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR GLY ALA THR          
SEQRES   5 L  214  ASN LEU ALA ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU          
SEQRES   7 L  214  GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN ASN VAL          
SEQRES   8 L  214  LEU ASN THR PRO LEU THR PHE GLY GLN GLY THR LYS VAL          
SEQRES   9 L  214  GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 L  214  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 L  214  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 L  214  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 L  214  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 L  214  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 L  214  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 L  214  PHE ASN ARG GLY GLU CYS                                      
SEQRES   1 A 1676  MET GLY LEU LEU GLY ILE LEU CYS PHE LEU ILE PHE LEU          
SEQRES   2 A 1676  GLY LYS THR TRP GLY GLN GLU GLN THR TYR VAL ILE SER          
SEQRES   3 A 1676  ALA PRO LYS ILE PHE ARG VAL GLY ALA SER GLU ASN ILE          
SEQRES   4 A 1676  VAL ILE GLN VAL TYR GLY TYR THR GLU ALA PHE ASP ALA          
SEQRES   5 A 1676  THR ILE SER ILE LYS SER TYR PRO ASP LYS LYS PHE SER          
SEQRES   6 A 1676  TYR SER SER GLY HIS VAL HIS LEU SER SER GLU ASN LYS          
SEQRES   7 A 1676  PHE GLN ASN SER ALA ILE LEU THR ILE GLN PRO LYS GLN          
SEQRES   8 A 1676  LEU PRO GLY GLY GLN ASN PRO VAL SER TYR VAL TYR LEU          
SEQRES   9 A 1676  GLU VAL VAL SER LYS HIS PHE SER LYS SER LYS ARG MET          
SEQRES  10 A 1676  PRO ILE THR TYR ASP ASN GLY PHE LEU PHE ILE HIS THR          
SEQRES  11 A 1676  ASP LYS PRO VAL TYR THR PRO ASP GLN SER VAL LYS VAL          
SEQRES  12 A 1676  ARG VAL TYR SER LEU ASN ASP ASP LEU LYS PRO ALA LYS          
SEQRES  13 A 1676  ARG GLU THR VAL LEU THR PHE ILE ASP PRO GLU GLY SER          
SEQRES  14 A 1676  GLU VAL ASP MET VAL GLU GLU ILE ASP HIS ILE GLY ILE          
SEQRES  15 A 1676  ILE SER PHE PRO ASP PHE LYS ILE PRO SER ASN PRO ARG          
SEQRES  16 A 1676  TYR GLY MET TRP THR ILE LYS ALA LYS TYR LYS GLU ASP          
SEQRES  17 A 1676  PHE SER THR THR GLY THR ALA TYR PHE GLU VAL LYS GLU          
SEQRES  18 A 1676  TYR VAL LEU PRO HIS PHE SER VAL SER ILE GLU PRO GLU          
SEQRES  19 A 1676  TYR ASN PHE ILE GLY TYR LYS ASN PHE LYS ASN PHE GLU          
SEQRES  20 A 1676  ILE THR ILE LYS ALA ARG TYR PHE TYR ASN LYS VAL VAL          
SEQRES  21 A 1676  THR GLU ALA ASP VAL TYR ILE THR PHE GLY ILE ARG GLU          
SEQRES  22 A 1676  ASP LEU LYS ASP ASP GLN LYS GLU MET MET GLN THR ALA          
SEQRES  23 A 1676  MET GLN ASN THR MET LEU ILE ASN GLY ILE ALA GLN VAL          
SEQRES  24 A 1676  THR PHE ASP SER GLU THR ALA VAL LYS GLU LEU SER TYR          
SEQRES  25 A 1676  TYR SER LEU GLU ASP LEU ASN ASN LYS TYR LEU TYR ILE          
SEQRES  26 A 1676  ALA VAL THR VAL ILE GLU SER THR GLY GLY PHE SER GLU          
SEQRES  27 A 1676  GLU ALA GLU ILE PRO GLY ILE LYS TYR VAL LEU SER PRO          
SEQRES  28 A 1676  TYR LYS LEU ASN LEU VAL ALA THR PRO LEU PHE LEU LYS          
SEQRES  29 A 1676  PRO GLY ILE PRO TYR PRO ILE LYS VAL GLN VAL LYS ASP          
SEQRES  30 A 1676  SER LEU ASP GLN LEU VAL GLY GLY VAL PRO VAL THR LEU          
SEQRES  31 A 1676  ASN ALA GLN THR ILE ASP VAL ASN GLN GLU THR SER ASP          
SEQRES  32 A 1676  LEU ASP PRO SER LYS SER VAL THR ARG VAL ASP ASP GLY          
SEQRES  33 A 1676  VAL ALA SER PHE VAL LEU ASN LEU PRO SER GLY VAL THR          
SEQRES  34 A 1676  VAL LEU GLU PHE ASN VAL LYS THR ASP ALA PRO ASP LEU          
SEQRES  35 A 1676  PRO GLU GLU ASN GLN ALA ARG GLU GLY TYR ARG ALA ILE          
SEQRES  36 A 1676  ALA TYR SER SER LEU SER GLN SER TYR LEU TYR ILE ASP          
SEQRES  37 A 1676  TRP THR ASP ASN HIS LYS ALA LEU LEU VAL GLY GLU HIS          
SEQRES  38 A 1676  LEU ASN ILE ILE VAL THR PRO LYS SER PRO TYR ILE ASP          
SEQRES  39 A 1676  LYS ILE THR HIS TYR ASN TYR LEU ILE LEU SER LYS GLY          
SEQRES  40 A 1676  LYS ILE ILE HIS PHE GLY THR ARG GLU LYS PHE SER ASP          
SEQRES  41 A 1676  ALA SER TYR GLN SER ILE ASN ILE PRO VAL THR GLN ASN          
SEQRES  42 A 1676  MET VAL PRO SER SER ARG LEU LEU VAL TYR TYR ILE VAL          
SEQRES  43 A 1676  THR GLY GLU GLN THR ALA GLU LEU VAL SER ASP SER VAL          
SEQRES  44 A 1676  TRP LEU ASN ILE GLU GLU LYS CYS GLY ASN GLN LEU GLN          
SEQRES  45 A 1676  VAL HIS LEU SER PRO ASP ALA ASP ALA TYR SER PRO GLY          
SEQRES  46 A 1676  GLN THR VAL SER LEU ASN MET ALA THR GLY MET ASP SER          
SEQRES  47 A 1676  TRP VAL ALA LEU ALA ALA VAL ASP SER ALA VAL TYR GLY          
SEQRES  48 A 1676  VAL GLN ARG GLY ALA LYS LYS PRO LEU GLU ARG VAL PHE          
SEQRES  49 A 1676  GLN PHE LEU GLU LYS SER ASP LEU GLY CYS GLY ALA GLY          
SEQRES  50 A 1676  GLY GLY LEU ASN ASN ALA ASN VAL PHE HIS LEU ALA GLY          
SEQRES  51 A 1676  LEU THR PHE LEU THR ASN ALA ASN ALA ASP ASP SER GLN          
SEQRES  52 A 1676  GLU ASN ASP GLU PRO CYS LYS GLU ILE LEU ARG PRO ARG          
SEQRES  53 A 1676  ARG THR LEU GLN LYS LYS ILE GLU GLU ILE ALA ALA LYS          
SEQRES  54 A 1676  TYR LYS HIS SER VAL VAL LYS LYS CYS CYS TYR ASP GLY          
SEQRES  55 A 1676  ALA CYS VAL ASN ASN ASP GLU THR CYS GLU GLN ARG ALA          
SEQRES  56 A 1676  ALA ARG ILE SER LEU GLY PRO ARG CYS ILE LYS ALA PHE          
SEQRES  57 A 1676  THR GLU CYS CYS VAL VAL ALA SER GLN LEU ARG ALA ASN          
SEQRES  58 A 1676  ILE SER HIS LYS ASP MET GLN LEU GLY ARG LEU HIS MET          
SEQRES  59 A 1676  LYS THR LEU LEU PRO VAL SER LYS PRO GLU ILE ARG SER          
SEQRES  60 A 1676  TYR PHE PRO GLU SER TRP LEU TRP GLU VAL HIS LEU VAL          
SEQRES  61 A 1676  PRO ARG ARG LYS GLN LEU GLN PHE ALA LEU PRO ASP SER          
SEQRES  62 A 1676  LEU THR THR TRP GLU ILE GLN GLY VAL GLY ILE SER ASN          
SEQRES  63 A 1676  THR GLY ILE CYS VAL ALA ASP THR VAL LYS ALA LYS VAL          
SEQRES  64 A 1676  PHE LYS ASP VAL PHE LEU GLU MET ASN ILE PRO TYR SER          
SEQRES  65 A 1676  VAL VAL ARG GLY GLU GLN ILE GLN LEU LYS GLY THR VAL          
SEQRES  66 A 1676  TYR ASN TYR ARG THR SER GLY MET GLN PHE CYS VAL LYS          
SEQRES  67 A 1676  MET SER ALA VAL GLU GLY ILE CYS THR SER GLU SER PRO          
SEQRES  68 A 1676  VAL ILE ASP HIS GLN GLY THR LYS SER SER LYS CYS VAL          
SEQRES  69 A 1676  ARG GLN LYS VAL GLU GLY SER SER SER HIS LEU VAL THR          
SEQRES  70 A 1676  PHE THR VAL LEU PRO LEU GLU ILE GLY LEU HIS ASN ILE          
SEQRES  71 A 1676  ASN PHE SER LEU GLU THR TRP PHE GLY LYS GLU ILE LEU          
SEQRES  72 A 1676  VAL LYS THR LEU ARG VAL VAL PRO GLU GLY VAL LYS ARG          
SEQRES  73 A 1676  GLU SER TYR SER GLY VAL THR LEU ASP PRO ARG GLY ILE          
SEQRES  74 A 1676  TYR GLY THR ILE SER ARG ARG LYS GLU PHE PRO TYR ARG          
SEQRES  75 A 1676  ILE PRO LEU ASP LEU VAL PRO LYS THR GLU ILE LYS ARG          
SEQRES  76 A 1676  ILE LEU SER VAL LYS GLY LEU LEU VAL GLY GLU ILE LEU          
SEQRES  77 A 1676  SER ALA VAL LEU SER GLN GLU GLY ILE ASN ILE LEU THR          
SEQRES  78 A 1676  HIS LEU PRO LYS GLY SER ALA GLU ALA GLU LEU MET SER          
SEQRES  79 A 1676  VAL VAL PRO VAL PHE TYR VAL PHE HIS TYR LEU GLU THR          
SEQRES  80 A 1676  GLY ASN HIS TRP ASN ILE PHE HIS SER ASP PRO LEU ILE          
SEQRES  81 A 1676  GLU LYS GLN LYS LEU LYS LYS LYS LEU LYS GLU GLY MET          
SEQRES  82 A 1676  LEU SER ILE MET SER TYR ARG ASN ALA ASP TYR SER TYR          
SEQRES  83 A 1676  SER VAL TRP LYS GLY GLY SER ALA SER THR TRP LEU THR          
SEQRES  84 A 1676  ALA PHE ALA LEU ARG VAL LEU GLY GLN VAL ASN LYS TYR          
SEQRES  85 A 1676  VAL GLU GLN ASN GLN ASN SER ILE CYS ASN SER LEU LEU          
SEQRES  86 A 1676  TRP LEU VAL GLU ASN TYR GLN LEU ASP ASN GLY SER PHE          
SEQRES  87 A 1676  LYS GLU ASN SER GLN TYR GLN PRO ILE LYS LEU GLN GLY          
SEQRES  88 A 1676  THR LEU PRO VAL GLU ALA ARG GLU ASN SER LEU TYR LEU          
SEQRES  89 A 1676  THR ALA PHE THR VAL ILE GLY ILE ARG LYS ALA PHE ASP          
SEQRES  90 A 1676  ILE CYS PRO LEU VAL LYS ILE ASP THR ALA LEU ILE LYS          
SEQRES  91 A 1676  ALA ASP ASN PHE LEU LEU GLU ASN THR LEU PRO ALA GLN          
SEQRES  92 A 1676  SER THR PHE THR LEU ALA ILE SER ALA TYR ALA LEU SER          
SEQRES  93 A 1676  LEU GLY ASP LYS THR HIS PRO GLN PHE ARG SER ILE VAL          
SEQRES  94 A 1676  SER ALA LEU LYS ARG GLU ALA LEU VAL LYS GLY ASN PRO          
SEQRES  95 A 1676  PRO ILE TYR ARG PHE TRP LYS ASP ASN LEU GLN HIS LYS          
SEQRES  96 A 1676  ASP SER SER VAL PRO ASN THR GLY THR ALA ARG MET VAL          
SEQRES  97 A 1676  GLU THR THR ALA TYR ALA LEU LEU THR SER LEU ASN LEU          
SEQRES  98 A 1676  LYS ASP ILE ASN TYR VAL ASN PRO VAL ILE LYS TRP LEU          
SEQRES  99 A 1676  SER GLU GLU GLN ARG TYR GLY GLY GLY PHE TYR SER THR          
SEQRES 100 A 1676  GLN ASP THR ILE ASN ALA ILE GLU GLY LEU THR GLU TYR          
SEQRES 101 A 1676  SER LEU LEU VAL LYS GLN LEU ARG LEU SER MET ASP ILE          
SEQRES 102 A 1676  ASP VAL SER TYR LYS HIS LYS GLY ALA LEU HIS ASN TYR          
SEQRES 103 A 1676  LYS MET THR ASP LYS ASN PHE LEU GLY ARG PRO VAL GLU          
SEQRES 104 A 1676  VAL LEU LEU ASN ASP ASP LEU ILE VAL SER THR GLY PHE          
SEQRES 105 A 1676  GLY SER GLY LEU ALA THR VAL HIS VAL THR THR VAL VAL          
SEQRES 106 A 1676  HIS LYS THR SER THR SER GLU GLU VAL CYS SER PHE TYR          
SEQRES 107 A 1676  LEU LYS ILE ASP THR GLN ASP ILE GLU ALA SER HIS TYR          
SEQRES 108 A 1676  ARG GLY TYR GLY ASN SER ASP TYR LYS ARG ILE VAL ALA          
SEQRES 109 A 1676  CYS ALA SER TYR LYS PRO SER ARG GLU GLU SER SER SER          
SEQRES 110 A 1676  GLY SER SER HIS ALA VAL MET ASP ILE SER LEU PRO THR          
SEQRES 111 A 1676  GLY ILE SER ALA ASN GLU GLU ASP LEU LYS ALA LEU VAL          
SEQRES 112 A 1676  GLU GLY VAL ASP GLN LEU PHE THR ASP TYR GLN ILE LYS          
SEQRES 113 A 1676  ASP GLY HIS VAL ILE LEU GLN LEU ASN SER ILE PRO SER          
SEQRES 114 A 1676  SER ASP PHE LEU CYS VAL ARG PHE ARG ILE PHE GLU LEU          
SEQRES 115 A 1676  PHE GLU VAL GLY PHE LEU SER PRO ALA THR PHE THR VAL          
SEQRES 116 A 1676  TYR GLU TYR HIS ARG PRO ASP LYS GLN CYS THR MET PHE          
SEQRES 117 A 1676  TYR SER THR SER ASN ILE LYS ILE GLN LYS VAL CYS GLU          
SEQRES 118 A 1676  GLY ALA ALA CYS LYS CYS VAL GLU ALA ASP CYS GLY GLN          
SEQRES 119 A 1676  MET GLN GLU GLU LEU ASP LEU THR ILE SER ALA GLU THR          
SEQRES 120 A 1676  ARG LYS GLN THR ALA CYS LYS PRO GLU ILE ALA TYR ALA          
SEQRES 121 A 1676  TYR LYS VAL SER ILE THR SER ILE THR VAL GLU ASN VAL          
SEQRES 122 A 1676  PHE VAL LYS TYR LYS ALA THR LEU LEU ASP ILE TYR LYS          
SEQRES 123 A 1676  THR GLY GLU ALA VAL ALA GLU LYS ASP SER GLU ILE THR          
SEQRES 124 A 1676  PHE ILE LYS LYS VAL THR CYS THR ASN ALA GLU LEU VAL          
SEQRES 125 A 1676  LYS GLY ARG GLN TYR LEU ILE MET GLY LYS GLU ALA LEU          
SEQRES 126 A 1676  GLN ILE LYS TYR ASN PHE SER PHE ARG TYR ILE TYR PRO          
SEQRES 127 A 1676  LEU ASP SER LEU THR TRP ILE GLU TYR TRP PRO ARG ASP          
SEQRES 128 A 1676  THR THR CYS SER SER CYS GLN ALA PHE LEU ALA ASN LEU          
SEQRES 129 A 1676  ASP GLU PHE ALA GLU ASP ILE PHE LEU ASN GLY CYS              
SEQRES   1 X  230  GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 X  230  PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY          
SEQRES   3 X  230  TYR ILE PHE SER ASN TYR TRP ILE GLN TRP VAL ARG GLN          
SEQRES   4 X  230  ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLU ILE LEU          
SEQRES   5 X  230  PRO GLY SER GLY SER THR GLU TYR THR GLU ASN PHE LYS          
SEQRES   6 X  230  ASP ARG VAL THR MET THR ARG ASP THR SER THR SER THR          
SEQRES   7 X  230  VAL TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR          
SEQRES   8 X  230  ALA VAL TYR TYR CYS ALA ARG TYR PHE PHE GLY SER SER          
SEQRES   9 X  230  PRO ASN TRP TYR PHE ASP VAL TRP GLY GLN GLY THR LEU          
SEQRES  10 X  230  VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL          
SEQRES  11 X  230  PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY          
SEQRES  12 X  230  THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO          
SEQRES  13 X  230  GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR          
SEQRES  14 X  230  SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER          
SEQRES  15 X  230  GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER          
SEQRES  16 X  230  SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN          
SEQRES  17 X  230  HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU          
SEQRES  18 X  230  PRO LYS SER CYS ASP LYS THR HIS THR                          
SEQRES   1 Y  214  ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA          
SEQRES   2 Y  214  SER VAL GLY ASP ARG VAL THR ILE THR CYS GLY ALA SER          
SEQRES   3 Y  214  GLU ASN ILE TYR GLY ALA LEU ASN TRP TYR GLN GLN LYS          
SEQRES   4 Y  214  PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR GLY ALA THR          
SEQRES   5 Y  214  ASN LEU ALA ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 Y  214  GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU          
SEQRES   7 Y  214  GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN ASN VAL          
SEQRES   8 Y  214  LEU ASN THR PRO LEU THR PHE GLY GLN GLY THR LYS VAL          
SEQRES   9 Y  214  GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 Y  214  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 Y  214  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 Y  214  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 Y  214  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 Y  214  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 Y  214  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 Y  214  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 Y  214  PHE ASN ARG GLY GLU CYS                                      
HET    NAG  B2001      14                                                       
HET    NAG  B2002      14                                                       
HET    BMA  B2003      11                                                       
HET    NAG  A2001      14                                                       
HET    NAG  A2002      14                                                       
HET    BMA  A2003      11                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
FORMUL   7  NAG    4(C8 H15 N O6)                                               
FORMUL   7  BMA    2(C6 H12 O6)                                                 
HELIX    1 AA1 GLN B   88  LEU B   92  5                                   5    
HELIX    2 AA2 ASP B  302  LYS B  308  1                                   7    
HELIX    3 AA3 SER B  314  ASN B  319  5                                   6    
HELIX    4 AA4 THR B  531  VAL B  535  5                                   5    
HELIX    5 AA5 ALA B  608  GLY B  611  5                                   4    
HELIX    6 AA6 LYS B  618  GLU B  628  1                                  11    
HELIX    7 AA7 LYS B  629  ASP B  631  5                                   3    
HELIX    8 AA8 ASN B  641  ALA B  649  1                                   9    
HELIX    9 AA9 GLN B  680  LYS B  691  1                                  12    
HELIX   10 AB1 HIS B  692  CYS B  704  1                                  13    
HELIX   11 AB2 THR B  710  ALA B  716  1                                   7    
HELIX   12 AB3 GLY B  721  ARG B  739  1                                  19    
HELIX   13 AB4 LYS B  745  LYS B  755  1                                  11    
HELIX   14 AB5 VAL B  984  SER B  993  1                                  10    
HELIX   15 AB6 SER B 1007  SER B 1014  1                                   8    
HELIX   16 AB7 VAL B 1015  GLY B 1028  1                                  14    
HELIX   17 AB8 HIS B 1030  PHE B 1034  5                                   5    
HELIX   18 AB9 ASP B 1037  SER B 1055  1                                  19    
HELIX   19 AC1 ILE B 1056  ARG B 1060  5                                   5    
HELIX   20 AC2 SER B 1075  ASN B 1090  1                                  16    
HELIX   21 AC3 ASN B 1096  TYR B 1111  1                                  16    
HELIX   22 AC4 THR B 1132  PHE B 1156  1                                  25    
HELIX   23 AC5 ASP B 1157  CYS B 1159  5                                   3    
HELIX   24 AC6 LEU B 1161  LEU B 1180  1                                  20    
HELIX   25 AC7 SER B 1184  LEU B 1197  1                                  14    
HELIX   26 AC8 HIS B 1202  GLU B 1215  1                                  14    
HELIX   27 AC9 THR B 1244  LYS B 1262  1                                  19    
HELIX   28 AD1 VAL B 1267  GLN B 1278  1                                  12    
HELIX   29 AD2 SER B 1286  VAL B 1304  1                                  19    
HELIX   30 AD3 ASN B 1435  GLU B 1444  1                                  10    
HELIX   31 AD4 SER B 1544  CYS B 1553  1                                  10    
HELIX   32 AD5 SER B 1656  LEU B 1673  1                                  18    
HELIX   33 AD6 ILE H   28  TYR H   32  5                                   5    
HELIX   34 AD7 PRO H  194  THR H  200  1                                   7    
HELIX   35 AD8 GLN L   79  PHE L   83  5                                   5    
HELIX   36 AD9 GLN A   88  LEU A   92  5                                   5    
HELIX   37 AE1 ASP A  302  LYS A  308  1                                   7    
HELIX   38 AE2 SER A  314  ASN A  319  5                                   6    
HELIX   39 AE3 THR A  531  VAL A  535  5                                   5    
HELIX   40 AE4 ALA A  608  GLY A  611  5                                   4    
HELIX   41 AE5 LYS A  618  GLU A  628  1                                  11    
HELIX   42 AE6 LYS A  629  ASP A  631  5                                   3    
HELIX   43 AE7 ASN A  641  ALA A  649  1                                   9    
HELIX   44 AE8 GLN A  680  LYS A  691  1                                  12    
HELIX   45 AE9 HIS A  692  CYS A  704  1                                  13    
HELIX   46 AF1 THR A  710  ALA A  716  1                                   7    
HELIX   47 AF2 GLY A  721  ARG A  739  1                                  19    
HELIX   48 AF3 LYS A  745  LYS A  755  1                                  11    
HELIX   49 AF4 VAL A  984  SER A  993  1                                  10    
HELIX   50 AF5 SER A 1007  SER A 1014  1                                   8    
HELIX   51 AF6 VAL A 1015  ASN A 1029  1                                  15    
HELIX   52 AF7 HIS A 1030  PHE A 1034  5                                   5    
HELIX   53 AF8 ASP A 1037  SER A 1055  1                                  19    
HELIX   54 AF9 ILE A 1056  ARG A 1060  5                                   5    
HELIX   55 AG1 SER A 1075  ASN A 1090  1                                  16    
HELIX   56 AG2 ASN A 1096  TYR A 1111  1                                  16    
HELIX   57 AG3 THR A 1132  PHE A 1156  1                                  25    
HELIX   58 AG4 ASP A 1157  CYS A 1159  5                                   3    
HELIX   59 AG5 LEU A 1161  LEU A 1180  1                                  20    
HELIX   60 AG6 SER A 1184  LEU A 1197  1                                  14    
HELIX   61 AG7 HIS A 1202  GLU A 1215  1                                  14    
HELIX   62 AG8 THR A 1244  LYS A 1262  1                                  19    
HELIX   63 AG9 VAL A 1267  GLN A 1278  1                                  12    
HELIX   64 AH1 SER A 1286  VAL A 1304  1                                  19    
HELIX   65 AH2 ASN A 1435  GLU A 1444  1                                  10    
HELIX   66 AH3 SER A 1544  CYS A 1553  1                                  10    
HELIX   67 AH4 SER A 1656  PHE A 1672  1                                  17    
HELIX   68 AH5 ILE X   28  TYR X   32  5                                   5    
HELIX   69 AH6 ARG X   87  THR X   91  5                                   5    
HELIX   70 AH7 PRO X  194  THR X  200  1                                   7    
HELIX   71 AH8 GLN Y   79  PHE Y   83  5                                   5    
SHEET    1 AA1 4 GLN B  80  THR B  86  0                                        
SHEET    2 AA1 4 SER B  36  TYR B  44 -1  N  ILE B  39   O  ALA B  83           
SHEET    3 AA1 4 THR B  22  PRO B  28 -1  N  SER B  26   O  VAL B  40           
SHEET    4 AA1 4 LEU B 651  THR B 655 -1  O  THR B 652   N  ALA B  27           
SHEET    1 AA2 5 PHE B  31  ARG B  32  0                                        
SHEET    2 AA2 5 SER B 112  THR B 120  1  O  THR B 120   N  PHE B  31           
SHEET    3 AA2 5 TYR B 101  SER B 108 -1  N  VAL B 106   O  LYS B 113           
SHEET    4 AA2 5 PHE B  50  SER B  58 -1  N  THR B  53   O  VAL B 107           
SHEET    5 AA2 5 SER B  65  LEU B  73 -1  O  VAL B  71   N  ALA B  52           
SHEET    1 AA3 3 PHE B 125  THR B 130  0                                        
SHEET    2 AA3 3 VAL B 143  LEU B 148 -1  O  TYR B 146   N  PHE B 127           
SHEET    3 AA3 3 ILE B 182  SER B 184 -1  O  ILE B 183   N  VAL B 145           
SHEET    1 AA4 5 VAL B 134  TYR B 135  0                                        
SHEET    2 AA4 5 THR B 212  VAL B 219  1  O  GLU B 218   N  TYR B 135           
SHEET    3 AA4 5 GLY B 197  TYR B 205 -1  N  ILE B 201   O  ALA B 215           
SHEET    4 AA4 5 THR B 159  ILE B 164 -1  N  VAL B 160   O  LYS B 204           
SHEET    5 AA4 5 GLU B 170  GLU B 176 -1  O  VAL B 174   N  LEU B 161           
SHEET    1 AA5 2 SER B 140  VAL B 141  0                                        
SHEET    2 AA5 2 PHE B 188  LYS B 189 -1  O  PHE B 188   N  VAL B 141           
SHEET    1 AA6 3 SER B 228  GLU B 232  0                                        
SHEET    2 AA6 3 PHE B 246  ARG B 253 -1  O  THR B 249   N  GLU B 232           
SHEET    3 AA6 3 ALA B 297  PHE B 301 -1  O  VAL B 299   N  ILE B 248           
SHEET    1 AA7 5 PHE B 237  ILE B 238  0                                        
SHEET    2 AA7 5 LYS B 346  TYR B 347  1  O  LYS B 346   N  ILE B 238           
SHEET    3 AA7 5 LYS B 321  GLU B 331 -1  N  LYS B 321   O  TYR B 347           
SHEET    4 AA7 5 GLU B 262  ARG B 272 -1  N  ASP B 264   O  ILE B 330           
SHEET    5 AA7 5 THR B 290  ILE B 293 -1  O  THR B 290   N  VAL B 265           
SHEET    1 AA8 4 GLU B 281  MET B 282  0                                        
SHEET    2 AA8 4 GLU B 262  ARG B 272 -1  N  ILE B 271   O  GLU B 281           
SHEET    3 AA8 4 LYS B 321  GLU B 331 -1  O  ILE B 330   N  ASP B 264           
SHEET    4 AA8 4 SER B 337  ILE B 342 -1  O  ALA B 340   N  VAL B 327           
SHEET    1 AA9 3 LYS B 353  LEU B 356  0                                        
SHEET    2 AA9 3 TYR B 369  LYS B 376 -1  O  LYS B 376   N  LYS B 353           
SHEET    3 AA9 3 VAL B 417  LEU B 422 -1  O  LEU B 422   N  TYR B 369           
SHEET    1 AB1 5 PHE B 362  LEU B 363  0                                        
SHEET    2 AB1 5 ARG B 449  ALA B 456  1  O  ILE B 455   N  LEU B 363           
SHEET    3 AB1 5 VAL B 430  THR B 437 -1  N  VAL B 435   O  GLU B 450           
SHEET    4 AB1 5 PRO B 387  ILE B 395 -1  N  THR B 389   O  LYS B 436           
SHEET    5 AB1 5 THR B 401  ASP B 403 -1  O  SER B 402   N  THR B 394           
SHEET    1 AB2 5 PHE B 362  LEU B 363  0                                        
SHEET    2 AB2 5 ARG B 449  ALA B 456  1  O  ILE B 455   N  LEU B 363           
SHEET    3 AB2 5 VAL B 430  THR B 437 -1  N  VAL B 435   O  GLU B 450           
SHEET    4 AB2 5 PRO B 387  ILE B 395 -1  N  THR B 389   O  LYS B 436           
SHEET    5 AB2 5 SER B 407  VAL B 410 -1  O  SER B 407   N  LEU B 390           
SHEET    1 AB3 3 TYR B 466  TRP B 469  0                                        
SHEET    2 AB3 3 HIS B 481  THR B 487 -1  O  THR B 487   N  TYR B 466           
SHEET    3 AB3 3 GLN B 524  PRO B 529 -1  O  ILE B 526   N  ILE B 484           
SHEET    1 AB4 4 LYS B 508  GLU B 516  0                                        
SHEET    2 AB4 4 HIS B 498  SER B 505 -1  N  TYR B 499   O  ARG B 515           
SHEET    3 AB4 4 SER B 537  THR B 547 -1  O  LEU B 541   N  LEU B 502           
SHEET    4 AB4 4 ALA B 552  ASN B 562 -1  O  ASP B 557   N  VAL B 542           
SHEET    1 AB5 5 GLN B 572  LEU B 575  0                                        
SHEET    2 AB5 5 THR B 587  ASP B 606 -1  O  ASN B 591   N  HIS B 574           
SHEET    3 AB5 5 THR B 795  ILE B 804 -1  O  VAL B 802   N  ALA B 601           
SHEET    4 AB5 5 ILE B 809  VAL B 819 -1  O  VAL B 815   N  ILE B 799           
SHEET    5 AB5 5 ALA B 581  TYR B 582  1  N  TYR B 582   O  LYS B 818           
SHEET    1 AB6 3 GLN B 572  LEU B 575  0                                        
SHEET    2 AB6 3 THR B 587  ASP B 606 -1  O  ASN B 591   N  HIS B 574           
SHEET    3 AB6 3 VAL B 777  ALA B 789 -1  O  PHE B 788   N  VAL B 588           
SHEET    1 AB7 4 VAL B 823  LEU B 825  0                                        
SHEET    2 AB7 4 GLN B 838  ASN B 847 -1  O  TYR B 846   N  PHE B 824           
SHEET    3 AB7 4 SER B 893  PRO B 902 -1  O  HIS B 894   N  VAL B 845           
SHEET    4 AB7 4 ILE B 865  CYS B 866 -1  N  CYS B 866   O  LEU B 901           
SHEET    1 AB8 3 VAL B 823  LEU B 825  0                                        
SHEET    2 AB8 3 GLN B 838  ASN B 847 -1  O  TYR B 846   N  PHE B 824           
SHEET    3 AB8 3 VAL B1485  GLY B1486 -1  O  GLY B1486   N  GLN B 838           
SHEET    1 AB9 2 VAL B 833  VAL B 834  0                                        
SHEET    2 AB9 2 VAL B 929  VAL B 930  1  O  VAL B 930   N  VAL B 833           
SHEET    1 AC1 4 GLN B 886  VAL B 888  0                                        
SHEET    2 AC1 4 MET B 853  MET B 859 -1  N  PHE B 855   O  GLN B 886           
SHEET    3 AC1 4 ILE B 910  THR B 916 -1  O  GLU B 915   N  CYS B 856           
SHEET    4 AC1 4 GLY B 919  LYS B 925 -1  O  GLU B 921   N  LEU B 914           
SHEET    1 AC2 4 VAL B 934  LEU B 944  0                                        
SHEET    2 AC2 4 ALA B1357  LYS B1367 -1  O  VAL B1361   N  SER B 940           
SHEET    3 AC2 4 LYS B 974  LYS B 980 -1  N  ILE B 976   O  THR B1362           
SHEET    4 AC2 4 VAL B1338  GLU B1339 -1  O  VAL B1338   N  LEU B 977           
SHEET    1 AC3 4 ARG B 956  PHE B 959  0                                        
SHEET    2 AC3 4 LEU B1346  THR B1350 -1  O  VAL B1348   N  LYS B 957           
SHEET    3 AC3 4 SER B1310  TYR B1317 -1  N  ASP B1314   O  SER B1349           
SHEET    4 AC3 4 LYS B1327  THR B1329 -1  O  MET B1328   N  MET B1311           
SHEET    1 AC4 2 LEU B1217  LYS B1219  0                                        
SHEET    2 AC4 2 TYR B1225  PHE B1227 -1  O  TYR B1225   N  LYS B1219           
SHEET    1 AC5 4 PHE B1377  ASP B1385  0                                        
SHEET    2 AC5 4 LYS B1400  TYR B1408 -1  O  VAL B1403   N  ASP B1382           
SHEET    3 AC5 4 LEU B1473  GLU B1481 -1  O  ILE B1479   N  LYS B1400           
SHEET    4 AC5 4 ILE B1432  ALA B1434 -1  N  SER B1433   O  PHE B1480           
SHEET    1 AC6 5 ASP B1452  ILE B1455  0                                        
SHEET    2 AC6 5 HIS B1459  LEU B1464 -1  O  ILE B1461   N  GLN B1454           
SHEET    3 AC6 5 ALA B1422  SER B1427 -1  N  ILE B1426   O  VAL B1460           
SHEET    4 AC6 5 ALA B1491  GLU B1497 -1  O  THR B1492   N  SER B1427           
SHEET    5 AC6 5 GLN B1504  TYR B1509 -1  O  TYR B1509   N  ALA B1491           
SHEET    1 AC7 5 GLU B1597  LYS B1603  0                                        
SHEET    2 AC7 5 PHE B1574  LYS B1586 -1  N  ALA B1579   O  ILE B1598           
SHEET    3 AC7 5 TYR B1559  GLU B1571 -1  N  THR B1569   O  LYS B1576           
SHEET    4 AC7 5 GLN B1616  GLY B1621 -1  O  TYR B1617   N  VAL B1563           
SHEET    5 AC7 5 TRP B1644  TYR B1647 -1  O  GLU B1646   N  LEU B1618           
SHEET    1 AC8 2 LEU B1625  LYS B1628  0                                        
SHEET    2 AC8 2 PHE B1633  ILE B1636 -1  O  ILE B1636   N  LEU B1625           
SHEET    1 AC9 4 GLN H   3  GLN H   6  0                                        
SHEET    2 AC9 4 VAL H  18  SER H  25 -1  O  SER H  25   N  GLN H   3           
SHEET    3 AC9 4 THR H  78  LEU H  83 -1  O  VAL H  79   N  CYS H  22           
SHEET    4 AC9 4 VAL H  68  ASP H  73 -1  N  ASP H  73   O  THR H  78           
SHEET    1 AD1 6 GLU H  10  LYS H  12  0                                        
SHEET    2 AD1 6 THR H 116  VAL H 120  1  O  THR H 119   N  GLU H  10           
SHEET    3 AD1 6 VAL H  93  PHE H 101 -1  N  TYR H  94   O  THR H 116           
SHEET    4 AD1 6 ILE H  34  GLN H  39 -1  N  GLN H  39   O  VAL H  93           
SHEET    5 AD1 6 LEU H  45  ILE H  51 -1  O  GLU H  46   N  ARG H  38           
SHEET    6 AD1 6 THR H  58  TYR H  60 -1  O  GLU H  59   N  GLU H  50           
SHEET    1 AD2 4 GLU H  10  LYS H  12  0                                        
SHEET    2 AD2 4 THR H 116  VAL H 120  1  O  THR H 119   N  GLU H  10           
SHEET    3 AD2 4 VAL H  93  PHE H 101 -1  N  TYR H  94   O  THR H 116           
SHEET    4 AD2 4 TRP H 107  TRP H 112 -1  O  ASP H 110   N  ARG H  98           
SHEET    1 AD3 4 SER H 129  LEU H 133  0                                        
SHEET    2 AD3 4 ALA H 145  LYS H 152 -1  O  LYS H 152   N  SER H 129           
SHEET    3 AD3 4 SER H 186  VAL H 193 -1  O  LEU H 187   N  VAL H 151           
SHEET    4 AD3 4 VAL H 172  THR H 174 -1  N  HIS H 173   O  VAL H 190           
SHEET    1 AD4 3 THR H 160  TRP H 163  0                                        
SHEET    2 AD4 3 TYR H 203  HIS H 209 -1  O  ASN H 206   N  SER H 162           
SHEET    3 AD4 3 THR H 214  VAL H 220 -1  O  THR H 214   N  HIS H 209           
SHEET    1 AD5 4 MET L   4  SER L   7  0                                        
SHEET    2 AD5 4 VAL L  19  ALA L  25 -1  O  THR L  22   N  SER L   7           
SHEET    3 AD5 4 ASP L  70  ILE L  75 -1  O  PHE L  71   N  CYS L  23           
SHEET    4 AD5 4 PHE L  62  SER L  65 -1  N  SER L  65   O  THR L  72           
SHEET    1 AD6 2 SER L  10  SER L  12  0                                        
SHEET    2 AD6 2 LYS L 103  GLU L 105  1  O  GLU L 105   N  LEU L  11           
SHEET    1 AD7 5 ASN L  53  LEU L  54  0                                        
SHEET    2 AD7 5 LYS L  45  TYR L  49 -1  N  TYR L  49   O  ASN L  53           
SHEET    3 AD7 5 LEU L  33  GLN L  38 -1  N  TRP L  35   O  ILE L  48           
SHEET    4 AD7 5 THR L  85  ASN L  90 -1  O  THR L  85   N  GLN L  38           
SHEET    5 AD7 5 THR L  97  PHE L  98 -1  O  THR L  97   N  ASN L  90           
SHEET    1 AD8 4 SER L 114  PHE L 118  0                                        
SHEET    2 AD8 4 THR L 129  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3 AD8 4 THR L 172  SER L 182 -1  O  LEU L 175   N  LEU L 136           
SHEET    4 AD8 4 SER L 159  ASP L 167 -1  N  GLN L 160   O  THR L 178           
SHEET    1 AD9 3 LYS L 145  VAL L 150  0                                        
SHEET    2 AD9 3 TYR L 192  THR L 197 -1  O  GLU L 195   N  GLN L 147           
SHEET    3 AD9 3 VAL L 205  PHE L 209 -1  O  PHE L 209   N  TYR L 192           
SHEET    1 AE1 4 GLN A  80  THR A  86  0                                        
SHEET    2 AE1 4 SER A  36  TYR A  44 -1  N  ILE A  39   O  ALA A  83           
SHEET    3 AE1 4 THR A  22  PRO A  28 -1  N  SER A  26   O  VAL A  40           
SHEET    4 AE1 4 LEU A 651  LEU A 654 -1  O  THR A 652   N  ALA A  27           
SHEET    1 AE2 5 PHE A  31  ARG A  32  0                                        
SHEET    2 AE2 5 SER A 112  THR A 120  1  O  THR A 120   N  PHE A  31           
SHEET    3 AE2 5 TYR A 101  SER A 108 -1  N  VAL A 106   O  LYS A 113           
SHEET    4 AE2 5 PHE A  50  SER A  58 -1  N  THR A  53   O  VAL A 107           
SHEET    5 AE2 5 SER A  65  LEU A  73 -1  O  VAL A  71   N  ALA A  52           
SHEET    1 AE3 3 PHE A 125  THR A 130  0                                        
SHEET    2 AE3 3 VAL A 143  LEU A 148 -1  O  TYR A 146   N  PHE A 127           
SHEET    3 AE3 3 ILE A 182  SER A 184 -1  O  ILE A 183   N  VAL A 145           
SHEET    1 AE4 5 VAL A 134  TYR A 135  0                                        
SHEET    2 AE4 5 THR A 212  VAL A 219  1  O  GLU A 218   N  TYR A 135           
SHEET    3 AE4 5 GLY A 197  TYR A 205 -1  N  ILE A 201   O  ALA A 215           
SHEET    4 AE4 5 THR A 159  ILE A 164 -1  N  VAL A 160   O  LYS A 204           
SHEET    5 AE4 5 GLU A 170  GLU A 176 -1  O  VAL A 174   N  LEU A 161           
SHEET    1 AE5 2 SER A 140  VAL A 141  0                                        
SHEET    2 AE5 2 PHE A 188  LYS A 189 -1  O  PHE A 188   N  VAL A 141           
SHEET    1 AE6 3 SER A 228  GLU A 232  0                                        
SHEET    2 AE6 3 PHE A 246  ARG A 253 -1  O  ARG A 253   N  SER A 228           
SHEET    3 AE6 3 ALA A 297  PHE A 301 -1  O  VAL A 299   N  ILE A 248           
SHEET    1 AE7 5 PHE A 237  ILE A 238  0                                        
SHEET    2 AE7 5 LYS A 346  TYR A 347  1  O  LYS A 346   N  ILE A 238           
SHEET    3 AE7 5 LYS A 321  GLU A 331 -1  N  LYS A 321   O  TYR A 347           
SHEET    4 AE7 5 GLU A 262  ARG A 272 -1  N  THR A 268   O  ALA A 326           
SHEET    5 AE7 5 THR A 290  ILE A 293 -1  O  THR A 290   N  VAL A 265           
SHEET    1 AE8 4 GLU A 281  MET A 282  0                                        
SHEET    2 AE8 4 GLU A 262  ARG A 272 -1  N  ILE A 271   O  GLU A 281           
SHEET    3 AE8 4 LYS A 321  GLU A 331 -1  O  ALA A 326   N  THR A 268           
SHEET    4 AE8 4 SER A 337  ILE A 342 -1  O  ALA A 340   N  VAL A 327           
SHEET    1 AE9 3 TYR A 352  LEU A 356  0                                        
SHEET    2 AE9 3 TYR A 369  ASP A 377 -1  O  LYS A 376   N  LYS A 353           
SHEET    3 AE9 3 VAL A 417  LEU A 422 -1  O  LEU A 422   N  TYR A 369           
SHEET    1 AF1 5 PHE A 362  LEU A 363  0                                        
SHEET    2 AF1 5 ARG A 449  ALA A 456  1  O  ILE A 455   N  LEU A 363           
SHEET    3 AF1 5 VAL A 430  THR A 437 -1  N  VAL A 435   O  GLU A 450           
SHEET    4 AF1 5 PRO A 387  ILE A 395 -1  N  THR A 389   O  LYS A 436           
SHEET    5 AF1 5 THR A 401  VAL A 410 -1  O  SER A 407   N  LEU A 390           
SHEET    1 AF2 3 TYR A 466  TRP A 469  0                                        
SHEET    2 AF2 3 HIS A 481  THR A 487 -1  O  ILE A 485   N  ASP A 468           
SHEET    3 AF2 3 GLN A 524  PRO A 529 -1  O  ILE A 528   N  LEU A 482           
SHEET    1 AF3 4 LYS A 508  GLU A 516  0                                        
SHEET    2 AF3 4 HIS A 498  SER A 505 -1  N  TYR A 499   O  ARG A 515           
SHEET    3 AF3 4 SER A 538  THR A 547 -1  O  LEU A 541   N  LEU A 502           
SHEET    4 AF3 4 ALA A 552  LEU A 561 -1  O  ASP A 557   N  VAL A 542           
SHEET    1 AF4 3 GLN A 572  LEU A 575  0                                        
SHEET    2 AF4 3 THR A 587  ALA A 593 -1  O  ASN A 591   N  HIS A 574           
SHEET    3 AF4 3 ARG A 783  ALA A 789 -1  O  LYS A 784   N  MET A 592           
SHEET    1 AF5 5 ALA A 581  TYR A 582  0                                        
SHEET    2 AF5 5 VAL A 815  VAL A 819  1  O  LYS A 818   N  TYR A 582           
SHEET    3 AF5 5 THR A 795  ILE A 804 -1  N  TRP A 797   O  ALA A 817           
SHEET    4 AF5 5 SER A 598  ASP A 606 -1  N  ALA A 601   O  VAL A 802           
SHEET    5 AF5 5 VAL A 777  VAL A 780 -1  O  VAL A 780   N  SER A 598           
SHEET    1 AF6 4 ALA A 581  TYR A 582  0                                        
SHEET    2 AF6 4 VAL A 815  VAL A 819  1  O  LYS A 818   N  TYR A 582           
SHEET    3 AF6 4 THR A 795  ILE A 804 -1  N  TRP A 797   O  ALA A 817           
SHEET    4 AF6 4 ILE A 809  VAL A 811 -1  O  CYS A 810   N  GLY A 803           
SHEET    1 AF7 3 VAL A 823  GLU A 826  0                                        
SHEET    2 AF7 3 GLN A 838  ASN A 847 -1  O  THR A 844   N  GLU A 826           
SHEET    3 AF7 3 SER A 893  VAL A 900 -1  O  HIS A 894   N  VAL A 845           
SHEET    1 AF8 3 VAL A 823  GLU A 826  0                                        
SHEET    2 AF8 3 GLN A 838  ASN A 847 -1  O  THR A 844   N  GLU A 826           
SHEET    3 AF8 3 VAL A1485  GLY A1486 -1  O  GLY A1486   N  GLN A 838           
SHEET    1 AF9 2 VAL A 833  VAL A 834  0                                        
SHEET    2 AF9 2 VAL A 929  VAL A 930  1  O  VAL A 930   N  VAL A 833           
SHEET    1 AG1 4 GLN A 886  VAL A 888  0                                        
SHEET    2 AG1 4 MET A 853  MET A 859 -1  N  PHE A 855   O  GLN A 886           
SHEET    3 AG1 4 ILE A 910  THR A 916 -1  O  GLU A 915   N  CYS A 856           
SHEET    4 AG1 4 GLY A 919  LYS A 925 -1  O  GLU A 921   N  LEU A 914           
SHEET    1 AG2 4 VAL A 934  LEU A 944  0                                        
SHEET    2 AG2 4 ALA A1357  LYS A1367 -1  O  VAL A1361   N  SER A 940           
SHEET    3 AG2 4 LYS A 974  LYS A 980 -1  N  ILE A 976   O  THR A1362           
SHEET    4 AG2 4 VAL A1338  GLU A1339 -1  O  VAL A1338   N  LEU A 977           
SHEET    1 AG3 4 ARG A 956  PHE A 959  0                                        
SHEET    2 AG3 4 LEU A1346  THR A1350 -1  O  VAL A1348   N  LYS A 957           
SHEET    3 AG3 4 SER A1310  TYR A1317 -1  N  ASP A1314   O  SER A1349           
SHEET    4 AG3 4 LYS A1327  THR A1329 -1  O  MET A1328   N  MET A1311           
SHEET    1 AG4 2 LEU A1217  LYS A1219  0                                        
SHEET    2 AG4 2 TYR A1225  PHE A1227 -1  O  PHE A1227   N  LEU A1217           
SHEET    1 AG5 4 PHE A1377  ASP A1385  0                                        
SHEET    2 AG5 4 LYS A1400  TYR A1408 -1  O  VAL A1403   N  ASP A1382           
SHEET    3 AG5 4 LEU A1473  GLU A1481 -1  O  ILE A1479   N  LYS A1400           
SHEET    4 AG5 4 ILE A1432  ALA A1434 -1  N  SER A1433   O  PHE A1480           
SHEET    1 AG6 5 ASP A1452  LYS A1456  0                                        
SHEET    2 AG6 5 HIS A1459  LEU A1464 -1  O  ILE A1461   N  GLN A1454           
SHEET    3 AG6 5 ALA A1422  SER A1427 -1  N  ILE A1426   O  VAL A1460           
SHEET    4 AG6 5 ALA A1491  GLU A1497 -1  O  THR A1492   N  SER A1427           
SHEET    5 AG6 5 GLN A1504  TYR A1509 -1  O  TYR A1509   N  ALA A1491           
SHEET    1 AG7 5 GLU A1597  LYS A1603  0                                        
SHEET    2 AG7 5 PHE A1574  LYS A1586 -1  N  ALA A1579   O  ILE A1598           
SHEET    3 AG7 5 TYR A1559  GLU A1571 -1  N  GLU A1571   O  PHE A1574           
SHEET    4 AG7 5 GLN A1616  GLY A1621 -1  O  TYR A1617   N  VAL A1563           
SHEET    5 AG7 5 TRP A1644  TYR A1647 -1  O  GLU A1646   N  LEU A1618           
SHEET    1 AG8 2 LEU A1625  LYS A1628  0                                        
SHEET    2 AG8 2 PHE A1633  ILE A1636 -1  O  ILE A1636   N  LEU A1625           
SHEET    1 AG9 4 GLN X   3  GLN X   6  0                                        
SHEET    2 AG9 4 VAL X  18  SER X  25 -1  O  SER X  25   N  GLN X   3           
SHEET    3 AG9 4 THR X  78  LEU X  83 -1  O  VAL X  79   N  CYS X  22           
SHEET    4 AG9 4 VAL X  68  ASP X  73 -1  N  ASP X  73   O  THR X  78           
SHEET    1 AH1 6 GLU X  10  LYS X  12  0                                        
SHEET    2 AH1 6 THR X 116  VAL X 120  1  O  THR X 119   N  GLU X  10           
SHEET    3 AH1 6 VAL X  93  PHE X 101 -1  N  TYR X  94   O  THR X 116           
SHEET    4 AH1 6 ILE X  34  GLN X  39 -1  N  GLN X  35   O  ALA X  97           
SHEET    5 AH1 6 LEU X  45  ILE X  51 -1  O  GLU X  46   N  ARG X  38           
SHEET    6 AH1 6 THR X  58  TYR X  60 -1  O  GLU X  59   N  GLU X  50           
SHEET    1 AH2 4 GLU X  10  LYS X  12  0                                        
SHEET    2 AH2 4 THR X 116  VAL X 120  1  O  THR X 119   N  GLU X  10           
SHEET    3 AH2 4 VAL X  93  PHE X 101 -1  N  TYR X  94   O  THR X 116           
SHEET    4 AH2 4 TRP X 107  TRP X 112 -1  O  ASP X 110   N  ARG X  98           
SHEET    1 AH3 4 SER X 129  LEU X 133  0                                        
SHEET    2 AH3 4 ALA X 145  LYS X 152 -1  O  LYS X 152   N  SER X 129           
SHEET    3 AH3 4 SER X 186  VAL X 193 -1  O  VAL X 193   N  ALA X 145           
SHEET    4 AH3 4 VAL X 172  PHE X 175 -1  N  PHE X 175   O  SER X 188           
SHEET    1 AH4 3 THR X 160  TRP X 163  0                                        
SHEET    2 AH4 3 TYR X 203  HIS X 209 -1  O  ASN X 208   N  THR X 160           
SHEET    3 AH4 3 THR X 214  VAL X 220 -1  O  THR X 214   N  HIS X 209           
SHEET    1 AH5 4 MET Y   4  SER Y   7  0                                        
SHEET    2 AH5 4 VAL Y  19  ALA Y  25 -1  O  THR Y  22   N  SER Y   7           
SHEET    3 AH5 4 ASP Y  70  ILE Y  75 -1  O  PHE Y  71   N  CYS Y  23           
SHEET    4 AH5 4 PHE Y  62  SER Y  65 -1  N  SER Y  65   O  THR Y  72           
SHEET    1 AH6 2 SER Y  10  SER Y  12  0                                        
SHEET    2 AH6 2 LYS Y 103  GLU Y 105  1  O  GLU Y 105   N  LEU Y  11           
SHEET    1 AH7 5 ASN Y  53  LEU Y  54  0                                        
SHEET    2 AH7 5 LYS Y  45  TYR Y  49 -1  N  TYR Y  49   O  ASN Y  53           
SHEET    3 AH7 5 LEU Y  33  GLN Y  38 -1  N  TRP Y  35   O  ILE Y  48           
SHEET    4 AH7 5 THR Y  85  ASN Y  90 -1  O  THR Y  85   N  GLN Y  38           
SHEET    5 AH7 5 THR Y  97  PHE Y  98 -1  O  THR Y  97   N  ASN Y  90           
SHEET    1 AH8 4 SER Y 114  PHE Y 118  0                                        
SHEET    2 AH8 4 THR Y 129  PHE Y 139 -1  O  LEU Y 135   N  PHE Y 116           
SHEET    3 AH8 4 THR Y 172  SER Y 182 -1  O  LEU Y 175   N  LEU Y 136           
SHEET    4 AH8 4 SER Y 159  ASP Y 167 -1  N  GLN Y 160   O  THR Y 178           
SHEET    1 AH9 3 LYS Y 145  VAL Y 150  0                                        
SHEET    2 AH9 3 TYR Y 192  HIS Y 198 -1  O  GLU Y 195   N  GLN Y 147           
SHEET    3 AH9 3 LEU Y 201  PHE Y 209 -1  O  PHE Y 209   N  TYR Y 192           
SSBOND   1 CYS B  567    CYS B  810                          1555   1555  2.03  
SSBOND   2 CYS B  634    CYS B  669                          1555   1555  2.03  
SSBOND   3 CYS B  698    CYS B  724                          1555   1555  2.03  
SSBOND   4 CYS B  699    CYS B  731                          1555   1555  2.03  
SSBOND   5 CYS B  711    CYS B  732                          1555   1555  2.03  
SSBOND   6 CYS B  856    CYS B  883                          1555   1555  2.03  
SSBOND   7 CYS B  866    CYS B 1527                          1555   1555  2.03  
SSBOND   8 CYS B 1101    CYS B 1159                          1555   1555  2.03  
SSBOND   9 CYS B 1375    CYS B 1505                          1555   1555  2.03  
SSBOND  10 CYS B 1405    CYS B 1474                          1555   1555  2.03  
SSBOND  11 CYS B 1532    CYS B 1606                          1555   1555  2.03  
SSBOND  12 CYS B 1553    CYS B 1676                          1555   1555  2.03  
SSBOND  13 CYS B 1654    CYS B 1657                          1555   1555  2.03  
SSBOND  14 CYS H   22    CYS H   96                          1555   1555  2.03  
SSBOND  15 CYS H  149    CYS H  205                          1555   1555  2.04  
SSBOND  16 CYS L   23    CYS L   88                          1555   1555  2.04  
SSBOND  17 CYS L  134    CYS L  194                          1555   1555  2.04  
SSBOND  18 CYS A  567    CYS A  810                          1555   1555  2.02  
SSBOND  19 CYS A  634    CYS A  669                          1555   1555  2.03  
SSBOND  20 CYS A  698    CYS A  724                          1555   1555  2.03  
SSBOND  21 CYS A  699    CYS A  731                          1555   1555  2.03  
SSBOND  22 CYS A  711    CYS A  732                          1555   1555  2.03  
SSBOND  23 CYS A  856    CYS A  883                          1555   1555  2.03  
SSBOND  24 CYS A  866    CYS A 1527                          1555   1555  2.02  
SSBOND  25 CYS A 1101    CYS A 1159                          1555   1555  2.03  
SSBOND  26 CYS A 1375    CYS A 1505                          1555   1555  2.04  
SSBOND  27 CYS A 1405    CYS A 1474                          1555   1555  2.03  
SSBOND  28 CYS A 1532    CYS A 1606                          1555   1555  2.03  
SSBOND  29 CYS A 1553    CYS A 1676                          1555   1555  2.03  
SSBOND  30 CYS A 1654    CYS A 1657                          1555   1555  2.03  
SSBOND  31 CYS X   22    CYS X   96                          1555   1555  2.04  
SSBOND  32 CYS X  149    CYS X  205                          1555   1555  2.03  
SSBOND  33 CYS Y   23    CYS Y   88                          1555   1555  2.04  
SSBOND  34 CYS Y  134    CYS Y  194                          1555   1555  2.03  
LINK         ND2 ASN B 911                 C1  NAG B2001     1555   1555  1.44  
LINK         ND2 ASN A 911                 C1  NAG A2001     1555   1555  1.45  
LINK         O4  NAG B2001                 C1  NAG B2002     1555   1555  1.45  
LINK         O4  NAG B2002                 C1  BMA B2003     1555   1555  1.45  
LINK         O4  NAG A2001                 C1  NAG A2002     1555   1555  1.45  
LINK         O4  NAG A2002                 C1  BMA A2003     1555   1555  1.45  
CISPEP   1 ASN B 1221    PRO B 1222          0        -2.07                     
CISPEP   2 PHE H  155    PRO H  156          0        -5.83                     
CISPEP   3 GLU H  157    PRO H  158          0        -1.76                     
CISPEP   4 SER L    7    PRO L    8          0        -3.18                     
CISPEP   5 TYR L  140    PRO L  141          0         0.68                     
CISPEP   6 ASN A 1221    PRO A 1222          0        -1.45                     
CISPEP   7 PHE X  155    PRO X  156          0        -5.17                     
CISPEP   8 GLU X  157    PRO X  158          0        -2.59                     
CISPEP   9 SER Y    7    PRO Y    8          0        -1.55                     
CISPEP  10 TYR Y  140    PRO Y  141          0         1.52                     
SITE     1 AC1  3 SER A 860  ASN A 909  ASN A 911                               
SITE     1 AC2  3 SER B 860  ASN B 909  ASN B 911                               
CRYST1  197.704  269.321  202.824  90.00  98.58  90.00 C 1 2 1       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      0.005058  0.000000  0.000763        0.00000                         
SCALE2      0.000000  0.003713  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004986        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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